ID AAT_METJA Reviewed; 375 AA. AC Q60317; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Probable aspartate aminotransferase; DE Short=AspAT; DE EC=2.6.1.1; DE AltName: Full=Transaminase A; GN OrderedLocusNames=MJ0001; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: L-aspartate + 2-oxoglutarate = oxaloacetate + CC L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97984.1; -; Genomic_DNA. DR PIR; A64300; A64300. DR ProteinModelPortal; Q60317; -. DR STRING; 243232.MJ_0001; -. DR EnsemblBacteria; AAB97984; AAB97984; MJ_0001. DR KEGG; mja:MJ_0001; -. DR eggNOG; arCOG01130; Archaea. DR eggNOG; COG0436; LUCA. DR InParanoid; Q60317; -. DR KO; K00812; -. DR OMA; TDNCILI; -. DR PhylomeDB; Q60317; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004069; F:L-aspartate:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 375 Probable aspartate aminotransferase. FT /FTId=PRO_0000123858. FT BINDING 31 31 Aspartate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 165 165 Aspartate. {ECO:0000250}. FT BINDING 353 353 Aspartate. {ECO:0000250}. FT MOD_RES 223 223 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 375 AA; 42396 MW; 31349B11FC9B83A9 CRC64; MISSRCKNIK PSAIREIFNL ATSDCINLGI GEPDFDTPKH IIEAAKRALD EGKTHYSPNN GIPELREEIS NKLKDDYNLD VDKDNIIVTC GASEALMLSI MTLIDRGDEV LIPNPSFVSY FSLTEFAEGK IKNIDLDENF NIDLEKVKES ITKKTKLIIF NSPSNPTGKV YDKETIKGLA EIAEDYNLII VSDEVYDKII YDKKHYSPMQ FTDRCILING FSKTYAMTGW RIGYLAVSDE LNKELDLINN MIKIHQYSFA CATTFAQYGA LAALRGSQKC VEDMVREFKM RRDLIYNGLK DIFKVNKPDG AFYIFPDVSE YGDGVEVAKK LIENKVLCVP GVAFGENGAN YIRFSYATKY EDIEKALGII KEIFE // ID ACDB1_METJA Reviewed; 748 AA. AC Q57616; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 1; DE Short=ACDS complex subunit beta 1; DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138}; DE AltName: Full=ACDS complex acyltransferase 1; GN Name=cdhC1; OrderedLocusNames=MJ0152; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha- CC epsilon complex generates CO from CO(2), while the beta subunit CC (this protein) combines the CO with CoA and a methyl group to form CC acetyl-CoA. The methyl group, which is incorporated into acetyl- CC CoA, is transferred to the beta subunit by a corrinoid iron-sulfur CC protein (the gamma-delta complex). {ECO:0000255|HAMAP- CC Rule:MF_01138}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + a [Co(I) corrinoid Fe-S protein] CC = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]. CC {ECO:0000255|HAMAP-Rule:MF_01138}. CC -!- COFACTOR: CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; CC Evidence={ECO:0000250}; CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000250}; CC -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, CC beta, gamma and delta chains with a probable stoichiometry of CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98134.1; -; Genomic_DNA. DR PIR; A64319; A64319. DR ProteinModelPortal; Q57616; -. DR STRING; 243232.MJ_0152; -. DR EnsemblBacteria; AAB98134; AAB98134; MJ_0152. DR KEGG; mja:MJ_0152; -. DR eggNOG; arCOG02428; Archaea. DR eggNOG; arCOG04360; Archaea. DR eggNOG; ENOG4102TE3; Archaea. DR eggNOG; COG1152; LUCA. DR eggNOG; COG1614; LUCA. DR InParanoid; Q57616; -. DR KO; K00192; -. DR KO; K00193; -. DR OMA; PTGPNQP; -. DR PhylomeDB; Q57616; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro. DR GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2030; -; 1. DR HAMAP; MF_01138; CdhC; 1. DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu. DR InterPro; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR Pfam; PF03598; CdhC; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR00316; cdhC; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Nickel; Reference proteome; Transferase. FT CHAIN 1 748 Acetyl-CoA decarbonylase/synthase complex FT subunit beta 1. FT /FTId=PRO_0000155101. FT COMPBIAS 692 714 Glu-rich. FT METAL 480 480 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 483 483 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 569 569 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 571 571 Nickel-iron-sulfur. {ECO:0000255}. SQ SEQUENCE 748 AA; 82957 MW; 3BD5E42A4ABA3E8E CRC64; MKIRLYGETM VVGNIIEGGK TVLNLTKEIL EKEDENLKVS YPGTNYNLPI IYGLLGKKIE TVKDLKELIN SLEIKDEETL ENALDAGVVT LICAEAIEAL KYAKSEKPYK EPYVGFIPDE ILRGLGVPLV EGKIPAILVV IGKVGDKEKL KKLIDDIKKR NILALLVGDI VKEMDEADIE YGLDKLLVPV GNEITSAIHA ANLAIRAPLI FGGIEPGKTE EIIDYLKNRV PAVVVALGEL DNITLAAGAG CIKAGVPVIT NNEVPVIKGA LESSDIDNIV ENALKMKGVK VKVVEFDIPV SVGPMNEGER VRGPDMYVEL AGPKSYGFEL VKVVNKAEDK VEIIGKDIDE MEEGSRNPFA IIVEVSGSNL EEDLEGVLER RIHEFLNYIE GVMHLNQRDQ VWIRINKNSF NKGLRLKHIG EVVKQLFKEH FPIVEKCNVI IITDPDKVKE ELEKAKEIYK KRDEKTKSIR EEDVDVFYGC VMCQSFAPTH VCIITPDRPS LCGSINYLDA RAAAKIDPNG PIFEIPKGEC LDEKLGIYTG VNEVVRERSQ GSVEEMALHS ALTNPCTSCG CFEAIVFYIP EVDGFGVAHR NFRGETPFGL PFSTLAGQCS GGKQVPGFVG ISISYMKSPK FLQGDGGWER VVWLPKELKE RVKDAIPEEL YDKIATEEDV KTTDELIKFL KEKGHPIVKK TEEEVVEEVE EEKEEVKATE EEKEGIEVGE LITKLAKEGG IQIIMKNVKI VINLNVKR // ID ACDG_METJA Reviewed; 488 AA. AC Q57576; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit gamma {ECO:0000255|HAMAP-Rule:MF_01136}; DE Short=ACDS complex subunit gamma {ECO:0000255|HAMAP-Rule:MF_01136}; DE EC=2.1.1.245 {ECO:0000255|HAMAP-Rule:MF_01136}; DE AltName: Full=5-methyltetrahydrosarcinapterin:corrinoid/iron-sulfur protein Co-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01136}; DE AltName: Full=ACDS complex methyltransferase {ECO:0000255|HAMAP-Rule:MF_01136}; DE AltName: Full=Corrinoid/iron-sulfur component large subunit {ECO:0000255|HAMAP-Rule:MF_01136}; GN Name=cdhE {ECO:0000255|HAMAP-Rule:MF_01136}; OrderedLocusNames=MJ0112; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01136}. CC -!- CATALYTIC ACTIVITY: A [methyl-Co(III) corrinoid Fe-S protein] + CC tetrahydrosarcinapterin = a [Co(I) corrinoid Fe-S protein] + 5- CC methyltetrahydrosarcinapterin. {ECO:0000255|HAMAP-Rule:MF_01136}. CC -!- COFACTOR: CC Name=corrinoid; Xref=ChEBI:CHEBI:33913; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01136}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_01136}; CC -!- SUBUNIT: Heterodimer of delta and gamma chains. The ACDS complex CC is made up of alpha, epsilon, beta, gamma and delta chains with a CC probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)- CC (gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01136}. CC -!- SIMILARITY: Contains 1 4Fe-4S domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98093.1; -; Genomic_DNA. DR PIR; H64313; H64313. DR ProteinModelPortal; Q57576; -. DR STRING; 243232.MJ_0112; -. DR EnsemblBacteria; AAB98093; AAB98093; MJ_0112. DR KEGG; mja:MJ_0112; -. DR eggNOG; arCOG01979; Archaea. DR eggNOG; COG1456; LUCA. DR InParanoid; Q57576; -. DR KO; K00197; -. DR OMA; ELTYYNP; -. DR PhylomeDB; Q57576; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046356; P:acetyl-CoA catabolic process; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR HAMAP; MF_01136; CdhE; 1. DR InterPro; IPR007202; 4Fe-4S_dom. DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl. DR InterPro; IPR016218; AcylCoA_decarb/synth_gsu. DR InterPro; IPR023427; AcylCoA_decarb/synth_gsu_arc. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF03599; CdhD; 1. DR Pfam; PF04060; FeS; 1. DR PIRSF; PIRSF000376; AcCoA_decarb_gamma; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR PROSITE; PS51656; 4FE4S; 1. PE 3: Inferred from homology; KW 4Fe-4S; Cobalt; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 488 Acetyl-CoA decarbonylase/synthase complex FT subunit gamma. FT /FTId=PRO_0000155120. FT DOMAIN 1 61 4Fe-4S. FT METAL 19 19 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01136}. FT METAL 22 22 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01136}. FT METAL 27 27 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01136}. FT METAL 44 44 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01136}. SQ SEQUENCE 488 AA; 55027 MW; AE09B3CECD238B5A CRC64; MPKKISAMDI YKLLPKTNCK KCGYPSCMAF ATKLLEKEAT IDQCPILNTP KFEKNKKKII ELISPPVKEV WFGNEEKKAV MGGDEVMYRY QLSFFNPTPI GVDISDELSE EEIKNRAKEI ENFVFERTGE KLKLDFIVIR NASGDVEKFK KAIEIVEKET KMPICIASLN PEVIKEALKV VKSKPMVYAA TKETLNDFIK VIKEVKKDVV LVLSSNNVKD LKNMAAKCLA NGIEDLVLEP HTYPENIAET LDLNVMIRRS AIEKEDKYLG FPILNLPINA YYYALKNECP ISGFFEDKEV VAKMFEATIA NTLMNRYADA LIMHGMDIWE LMPVLTLRQC IYTDPRKPQA VEPGLYPIGN PDENSPVILT TNFSLTFYTV TGDFEKDNVT CWLLVMDTGG KAVDVSVAGG QYNGENAKKL IEETGIADKV SHRIIILPAL AASTRGDIED KTGWTCVVGT RDSSQVGDFL RNNWDKILKE WKEKNQTA // ID ACDD_METJA Reviewed; 405 AA. AC Q57577; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit delta {ECO:0000255|HAMAP-Rule:MF_01135}; DE Short=ACDS complex subunit delta {ECO:0000255|HAMAP-Rule:MF_01135}; DE AltName: Full=Corrinoid/iron-sulfur component small subunit {ECO:0000255|HAMAP-Rule:MF_01135}; GN Name=cdhD {ECO:0000255|HAMAP-Rule:MF_01135}; OrderedLocusNames=MJ0113; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). Probably CC maintains the overall quaternary structure of the ACDS complex. CC {ECO:0000255|HAMAP-Rule:MF_01135}. CC -!- SUBUNIT: Heterodimer of delta and gamma chains. The ACDS complex CC is made up of alpha, epsilon, beta, gamma and delta chains with a CC probable stoichiometry of (alpha(2)epsilon(2))(4)-beta(8)- CC (gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01135}. CC -!- SIMILARITY: Belongs to the CdhD family. {ECO:0000255|HAMAP- CC Rule:MF_01135}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98094.1; -; Genomic_DNA. DR PIR; A64314; A64314. DR ProteinModelPortal; Q57577; -. DR STRING; 243232.MJ_0113; -. DR EnsemblBacteria; AAB98094; AAB98094; MJ_0113. DR KEGG; mja:MJ_0113; -. DR eggNOG; arCOG01980; Archaea. DR eggNOG; COG2069; LUCA. DR InParanoid; Q57577; -. DR KO; K00194; -. DR OMA; IEINEFR; -. DR PhylomeDB; Q57577; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:InterPro. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 1. DR HAMAP; MF_01135; CdhD; 1. DR InterPro; IPR016041; Ac-CoA_synth_d_su_TIM-brl. DR InterPro; IPR004486; CO_DH/Ac-CoA_synth_dsu. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF03599; CdhD; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR00381; cdhD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 405 Acetyl-CoA decarbonylase/synthase complex FT subunit delta. FT /FTId=PRO_0000155112. SQ SEQUENCE 405 AA; 45344 MW; AAD33B438559E911 CRC64; MIYNDRLGEV MDLNTLIKII EKVGRIEIED IKITADELII NIPSAPPIVI PQTPSIKEKL AEEGIIEIKD VPELDWEPPV EKYPGYIREV QFGKPKSEGG RGKVVKIGGQ RALYRFEEPQ PNPPVVTFDI FDIPMPGLPK PIRQFFQDVM EDPCEWAKKC VKEFGADMIT IHHISTDPKI KDKSPKEAAK LMEDLLQAVD VPFVIGGSGN PQKDPLVLEA CAEVAEGDRC LLASANLELD YKKIVDAAMK YDHNVLAWSI MDPNMARDLN RKLVEAGLDP NRIVMDPTTC ALGYGIEFSI NAMVRLRLNG LKGDELVNMP MSSGTTNAIG AREAWMNNPE WGPREYRLPL WEITTGITMM MCGVDLFMML NPISVKTLKE IGKTLTTKPG EVKLNTNNYE WIVSP // ID ADHS_METJA Reviewed; 273 AA. AC Q57843; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate synthase {ECO:0000255|HAMAP-Rule:MF_00960}; DE Short=ADH synthase {ECO:0000255|HAMAP-Rule:MF_00960}; DE Short=ADHS {ECO:0000255|HAMAP-Rule:MF_00960}; DE Short=ADTH synthase {ECO:0000255|HAMAP-Rule:MF_00960}; DE EC=2.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00960}; DE AltName: Full=Transaldolase-like ADHS; GN Name=aroA' {ECO:0000255|HAMAP-Rule:MF_00960}; GN OrderedLocusNames=MJ0400; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS AN ADH SYNTHASE. RX PubMed=15182204; DOI=10.1021/bi0495127; RA White R.H.; RT "L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are RT the precursors to the aromatic amino acids in Methanocaldococcus RT jannaschii."; RL Biochemistry 43:7618-7627(2004). RN [3] RP FUNCTION AS A FBP ALDOLASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND ENZYME REGULATION. RX PubMed=18318840; DOI=10.1111/j.1574-6968.2008.01079.x; RA Samland A.K., Wang M., Sprenger G.A.; RT "MJ0400 from Methanocaldococcus jannaschii exhibits fructose-1,6- RT bisphosphate aldolase activity."; RL FEMS Microbiol. Lett. 281:36-41(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS, REACTION MECHANISM, SUBUNIT, AND ACTIVE SITE. RX PubMed=17713928; DOI=10.1021/bi700934v; RA Morar M., White R.H., Ealick S.E.; RT "Structure of 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid RT synthase, a catalyst in the archaeal pathway for the biosynthesis of RT aromatic amino acids."; RL Biochemistry 46:10562-10571(2007). CC -!- FUNCTION: Catalyzes a transaldol reaction between 6-deoxy-5- CC ketofructose 1-phosphate (DKFP) and L-aspartate semialdehyde (ASA) CC with an elimination of hydroxypyruvaldehyde phosphate to yield 2- CC amino-3,7-dideoxy-D-threo-hept-6-ulosonate (ADH). Plays a key role CC in an alternative pathway of the biosynthesis of 3-dehydroquinate CC (DHQ), which is involved in the canonical pathway for the CC biosynthesis of aromatic amino acids. Can also catalyze the CC cleavage of fructose-1,6-bisphosphate (FBP) to glyceraldehyde-3- CC phosphate (GAP) and dihydroxyacetone phosphate (DHAP). CC {ECO:0000255|HAMAP-Rule:MF_00960, ECO:0000269|PubMed:15182204, CC ECO:0000269|PubMed:18318840}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + 1-deoxy-D-threo- CC hexo-2,5-diulose 6-phosphate = 2-amino-2,3,7-trideoxy-D-lyxo-hept- CC 6-ulosonate + 2,3-dioxopropylaldehyde phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00960, ECO:0000269|PubMed:18318840}. CC -!- ENZYME REGULATION: Inhibited by NaBH4 in the presence of FBP. CC {ECO:0000269|PubMed:18318840}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=430 uM for fructose-1,6-bisphosphate (at pH 7 and 50 degrees CC Celsius) {ECO:0000269|PubMed:18318840}; CC Vmax=33 nmol/min/mg enzyme for the FBP aldolase activity (at pH CC 7 and 50 degrees Celsius) {ECO:0000269|PubMed:18318840}; CC Temperature dependence: CC Optimum temperature is not reached at 100 degrees Celsius. CC {ECO:0000269|PubMed:18318840}; CC -!- SUBUNIT: Homodecamer. {ECO:0000255|HAMAP-Rule:MF_00960, CC ECO:0000269|PubMed:17713928}. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. ADHS CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00960}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98389.1; -; Genomic_DNA. DR PIR; H64349; H64349. DR PDB; 2QJG; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273. DR PDB; 2QJH; X-ray; 2.60 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273. DR PDB; 2QJI; X-ray; 2.80 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N/O/P/Q/R/S/T=1-273. DR PDBsum; 2QJG; -. DR PDBsum; 2QJH; -. DR PDBsum; 2QJI; -. DR ProteinModelPortal; Q57843; -. DR SMR; Q57843; 1-272. DR STRING; 243232.MJ_0400; -. DR EnsemblBacteria; AAB98389; AAB98389; MJ_0400. DR KEGG; mja:MJ_0400; -. DR eggNOG; arCOG04044; Archaea. DR eggNOG; COG1830; LUCA. DR InParanoid; Q57843; -. DR KO; K16306; -. DR OMA; IVRHGHR; -. DR PhylomeDB; Q57843; -. DR BioCyc; MetaCyc:MONOMER-14592; -. DR BRENDA; 2.2.1.10; 3260. DR SABIO-RK; Q57843; -. DR EvolutionaryTrace; Q57843; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro. DR GO; GO:0016744; F:transferase activity, transferring aldehyde or ketonic groups; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00960; ADH_synthase; 1. DR InterPro; IPR010210; ADH_synthase. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF038992; Aldolase_Ia; 1. DR SMART; SM01133; DeoC; 1. DR TIGRFAMs; TIGR01949; AroFGH_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; KW Reference proteome; Schiff base; Transferase. FT CHAIN 1 273 2-amino-3,7-dideoxy-D-threo-hept-6- FT ulosonate synthase. FT /FTId=PRO_0000138957. FT REGION 33 37 DKFP binding. FT {ECO:0000305|PubMed:17713928}. FT REGION 153 155 DKFP binding. FT {ECO:0000305|PubMed:17713928}. FT REGION 209 210 DKFP binding. FT {ECO:0000305|PubMed:17713928}. FT REGION 237 238 DKFP binding. FT {ECO:0000305|PubMed:17713928}. FT ACT_SITE 33 33 Proton acceptor. FT {ECO:0000305|PubMed:17713928}. FT ACT_SITE 153 153 Proton donor. FT {ECO:0000305|PubMed:17713928}. FT ACT_SITE 184 184 Schiff-base intermediate with substrate. FT {ECO:0000305|PubMed:17713928}. FT TURN 3 6 {ECO:0000244|PDB:2QJG}. FT HELIX 10 16 {ECO:0000244|PDB:2QJG}. FT TURN 17 19 {ECO:0000244|PDB:2QJG}. FT TURN 22 24 {ECO:0000244|PDB:2QJG}. FT STRAND 27 31 {ECO:0000244|PDB:2QJG}. FT HELIX 34 38 {ECO:0000244|PDB:2QJG}. FT STRAND 44 46 {ECO:0000244|PDB:2QJG}. FT HELIX 47 57 {ECO:0000244|PDB:2QJG}. FT STRAND 60 64 {ECO:0000244|PDB:2QJG}. FT HELIX 66 70 {ECO:0000244|PDB:2QJG}. FT STRAND 75 77 {ECO:0000244|PDB:2QJG}. FT STRAND 81 85 {ECO:0000244|PDB:2QJG}. FT STRAND 93 95 {ECO:0000244|PDB:2QJG}. FT HELIX 105 110 {ECO:0000244|PDB:2QJG}. FT STRAND 114 122 {ECO:0000244|PDB:2QJG}. FT HELIX 127 144 {ECO:0000244|PDB:2QJG}. FT STRAND 148 154 {ECO:0000244|PDB:2QJG}. FT HELIX 165 177 {ECO:0000244|PDB:2QJG}. FT STRAND 181 185 {ECO:0000244|PDB:2QJG}. FT HELIX 191 200 {ECO:0000244|PDB:2QJG}. FT STRAND 205 208 {ECO:0000244|PDB:2QJG}. FT HELIX 216 229 {ECO:0000244|PDB:2QJG}. FT STRAND 232 235 {ECO:0000244|PDB:2QJG}. FT HELIX 238 241 {ECO:0000244|PDB:2QJG}. FT STRAND 243 245 {ECO:0000244|PDB:2QJG}. FT HELIX 246 259 {ECO:0000244|PDB:2QJG}. FT HELIX 263 267 {ECO:0000244|PDB:2QJG}. SQ SEQUENCE 273 AA; 29675 MW; 06DDA2E51E8275E6 CRC64; MELFKDIKNL GKLVRLERIF NRESEKTVIV PMDHGVSNGP IKGLIDIRKT VNDVAEGGAN AVLLHKGIVR HGHRGYGKDV GLIIHLSGGT AISPNPLKKV IVTTVEEAIR MGADAVSIHV NVGSDEDWEA YRDLGMIAET CEYWGMPLIA MMYPRGKHIQ NERDPELVAH AARLGAELGA DIVKTSYTGD IDSFRDVVKG CPAPVVVAGG PKTNTDEEFL QMIKDAMEAG AAGVAVGRNI FQHDDVVGIT RAVCKIVHEN ADVEEALKEI RKK // ID ACD_METJA Reviewed; 704 AA. AC Q58010; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Acetate--CoA ligase [ADP-forming] {ECO:0000305}; DE EC=6.2.1.13 {ECO:0000269|PubMed:11790732}; DE AltName: Full=ADP-forming acetyl coenzyme A synthetase {ECO:0000305}; DE Short=ACS {ECO:0000305}; GN OrderedLocusNames=MJ0590 {ECO:0000312|EMBL:AAB98580.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RX PubMed=11790732; DOI=10.1128/JB.184.3.636-644.2002; RA Musfeldt M., Schoenheit P.; RT "Novel type of ADP-forming acetyl coenzyme A synthetase in RT hyperthermophilic archaea: heterologous expression and RT characterization of isoenzymes from the sulfate reducer Archaeoglobus RT fulgidus and the methanogen Methanococcus jannaschii."; RL J. Bacteriol. 184:636-644(2002). CC -!- FUNCTION: Catalyzes the formation of acetate and ATP from acetyl- CC CoA by using ADP and phosphate. Can also use butyryl-CoA, but not CC phenylacetyl-CoA. Can not catalyze the reverse reaction. CC {ECO:0000269|PubMed:11790732}. CC -!- CATALYTIC ACTIVITY: ATP + acetate + CoA = ADP + phosphate + CC acetyl-CoA. {ECO:0000269|PubMed:11790732}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=37 uM for acetyl-CoA {ECO:0000269|PubMed:11790732}; CC KM=15 uM for ADP {ECO:0000269|PubMed:11790732}; CC KM=470 uM for phosphate {ECO:0000269|PubMed:11790732}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11790732}. CC -!- SIMILARITY: In the N-terminal section; belongs to the acetate CoA CC ligase alpha subunit family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the acetate CoA CC ligase beta subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98580.1; -; Genomic_DNA. DR PIR; F64373; F64373. DR ProteinModelPortal; Q58010; -. DR STRING; 243232.MJ_0590; -. DR EnsemblBacteria; AAB98580; AAB98580; MJ_0590. DR KEGG; mja:MJ_0590; -. DR eggNOG; arCOG01340; Archaea. DR eggNOG; COG1042; LUCA. DR InParanoid; Q58010; -. DR KO; K09181; -. DR OMA; RTIGPNC; -. DR PhylomeDB; Q58010; -. DR BRENDA; 6.2.1.B11; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0043758; F:acetate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central. DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.261; -; 2. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR014089; AcCoA-synth-alpha. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR032875; Succ_CoA_lig_flav_dom. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR Pfam; PF13380; CoA_binding_2; 1. DR Pfam; PF13607; Succ_CoA_lig; 1. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52210; SSF52210; 2. DR TIGRFAMs; TIGR02717; AcCoA-syn-alpha; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 704 Acetate--CoA ligase [ADP-forming]. FT /FTId=PRO_0000106948. SQ SEQUENCE 704 AA; 78172 MW; A60E5F19DA1B2C58 CRC64; MWGRDYELKY ISYPKSVAII GASKTEGKVG YAIMKNLKDF NGKIYPINPK YDEIFGIKCY KSVLDVEDDI DLAVIVVPNI VVPKVLEECG KKGVKGAVII TAGFSEVGNY ELENKIKEIA KRYNIRIIGP NCLGIMNTHI NLNATFAKVF PPKGGVSIIS QSGAVLNAIL DIAPLLNIGF SKVVSIGNKA DIQESDLLEY FLDDEDTKIV VLYIEGLKDK RFLKVAKKLS KKKPIIALKS GRTEVGKKAA KSHTGSLAGE DVIYEAAFKE AGIIRAYTFE ELVDLIHLFS TQPTISSNEI GIITNAGGFG VLAADSCVDY NMKLSNFEKS TIEKLKNILP PTANISNPLD IIGDATPERY KKVIEVLAED SNVKGLLVIL TPQEMTKPLE VAKSIIEVKN SHKEFKNKPL ITSFVGGVSV KGAKSYLRKN GIPAYITPEN GVKALSHLYK YSLMKVKEDY DEYLENIKEE FIKITEENKE IIKELLSNPN EYTAKKLLSI YGLPVPKGYL AKNEDEALEY CKKLGKCVMK IVSPQIIHKT EAGGVIINPK NPKEAFKKLI ENAKEYAKRM GIDNLIIEGV LVEEFIEKDM MEIIIGAKRD DIFGSVVMVG LGGVFVEVLK DVSFGISPIT RDFAHEMLRE LKSYKVLEGV RGRPKRDINF IVDTLIKIGV FMDIHKEIKE LDLNPVFVFN EKEGGCIGDA RIIK // ID ACDA_METJA Reviewed; 774 AA. AC Q57617; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 108. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit alpha; DE Short=ACDS complex subunit alpha; DE EC=1.2.99.2; DE AltName: Full=ACDS complex carbon monoxide dehydrogenase; DE Short=ACDS CODH; GN Name=cdhA; OrderedLocusNames=MJ0153; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CO + H(2)O + A = CO(2) + AH(2). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 7 [4Fe-4S] clusters per heterotetramer. {ECO:0000305}; CC -!- COFACTOR: CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; CC Evidence={ECO:0000305}; CC Note=Binds 2 [Ni-Fe-S] clusters per heterotetramer. {ECO:0000305}; CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon chains. The CC ACDS complex is made up of alpha, epsilon, beta, gamma and delta CC chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)- CC beta(8)-(gamma(1)delta(1))(8) (Potential). {ECO:0000305}. CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; CC cluster C is a mixed Ni-Fe-S cluster which appears to be the CC active site of CO oxidation. Cluster D is also an all-cysteinyl- CC liganded 4Fe4S cluster that bridges the two subunits of the CODH CC dimer. May contain two additional 4Fe-4S clusters, dubbed E and F, CC that might reroute electron transfer along different paths. CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide CC dehydrogenase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98135.1; -; Genomic_DNA. DR PIR; B64319; B64319. DR ProteinModelPortal; Q57617; -. DR STRING; 243232.MJ_0153; -. DR EnsemblBacteria; AAB98135; AAB98135; MJ_0153. DR KEGG; mja:MJ_0153; -. DR eggNOG; arCOG02428; Archaea. DR eggNOG; COG1152; LUCA. DR InParanoid; Q57617; -. DR KO; K00192; -. DR OMA; ICCTAID; -. DR PhylomeDB; Q57617; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2030; -; 2. DR HAMAP; MF_01137; CdhA; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR004460; CO_DH/Ac-CoA_synth_asu. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF03063; Prismane; 2. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR00314; cdhA; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 774 Acetyl-CoA decarbonylase/synthase complex FT subunit alpha. FT /FTId=PRO_0000155077. FT DOMAIN 398 427 4Fe-4S ferredoxin-type 1. FT DOMAIN 436 466 4Fe-4S ferredoxin-type 2. FT METAL 73 73 Iron-sulfur 1 (4Fe-4S); shared with FT dimeric partner. {ECO:0000250}. FT METAL 76 76 Iron-sulfur 1 (4Fe-4S); shared with FT dimeric partner. {ECO:0000250}. FT METAL 77 77 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 79 79 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 84 84 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 94 94 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 251 251 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 279 279 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 318 318 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 408 408 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 411 411 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 414 414 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 418 418 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 446 446 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 449 449 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 452 452 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 456 456 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 514 514 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 543 543 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 578 578 Nickel-iron-sulfur. {ECO:0000250}. SQ SEQUENCE 774 AA; 85900 MW; F7CFD66F15CB1C7E CRC64; MVMGNNVEMD IKKLLTPLVK MKNANISMSI KFGEEEEEEW EPMGPTPMPK IPTLRHWDFK LLERYPPFYM PICDLCCLCT FGKCDLSRGK KGACGLNIKA QQARIVLIAC CIGAACHAGH SRHLVHHLIE TLGRDYPIDL GNEIEVEAPI ARTVTGIKPK TLGDLEKILD YCEEQITHLL SAAHTGQEGD YLDFESKALH AGMIDDLARE AGDLAQIVAY NMPKGDEDAP LIELGFGCID KSKPVILCIG HNVVPGSYIL EYLEENSMED EVEVCGICCT AIDITRVSDK PKVVGPLSRQ LMFVRSGVAD VVIVDEQCIR TDILEEVLKT GAVLIATNEK MCLGLEDVSH MDEDEIIGYL LRNRAALLLD EKKVGKVAVE VAKIVAKERK DRKTLPDLNE VVELAKQCTE CGWCNRNCPN AFKVKEAMAL AKQGNFKGFI DLYKRCYGCG RCEAICPRNL PIVSMTTKVG EAYYKDLKFK MRAGRGPIKD VEIRSVGAPI VFGDIPGVVA LVGCSNHPNG EEEVAMIAKE FLERKYIVVA TGCAAMAIGM WKDKDGKTLY EKYPGEFRAG GLVNCGSCLS NCHITGAAIK IANIFAKVPL RGNYAEVADY ILNKVGAVGV AWGAMSQKAA AIATGVNRWG IPVILGPHGA KYRRLYLSNG EKFKVKDKKT GEILEIEPAP EHLIVTAENV KECICMIPKL CMRPNDTPKG RANKIYHYVD VYEKYFGRMP PDLEKFVRTE KDIPFMMKDK IMAYLEEKGW KPLEKYPQDP TILY // ID ACDB2_METJA Reviewed; 469 AA. AC Q57620; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit beta 2; DE Short=ACDS complex subunit beta 2; DE EC=2.3.1.169 {ECO:0000255|HAMAP-Rule:MF_01138}; DE AltName: Full=ACDS complex acyltransferase 2; GN Name=cdhC2; OrderedLocusNames=MJ0156; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). The alpha- CC epsilon complex generates CO from CO(2), while the beta subunit CC (this protein) combines the CO with CoA and a methyl group to form CC acetyl-CoA. The methyl group, which is incorporated into acetyl- CC CoA, is transferred to the beta subunit by a corrinoid iron-sulfur CC protein (the gamma-delta complex). {ECO:0000255|HAMAP- CC Rule:MF_01138}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + a [Co(I) corrinoid Fe-S protein] CC = CO + CoA + a [methyl-Co(III) corrinoid Fe-S protein]. CC {ECO:0000255|HAMAP-Rule:MF_01138}. CC -!- COFACTOR: CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; CC Evidence={ECO:0000250}; CC Note=Binds 1 [Ni-Fe-S] cluster. {ECO:0000250}; CC -!- SUBUNIT: Monomer. The ACDS complex is made up of alpha, epsilon, CC beta, gamma and delta chains with a probable stoichiometry of CC (alpha(2)epsilon(2))(4)-beta(8)-(gamma(1)delta(1))(8) (Potential). CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CdhC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98138.1; -; Genomic_DNA. DR PIR; E64319; E64319. DR ProteinModelPortal; Q57620; -. DR STRING; 243232.MJ_0156; -. DR EnsemblBacteria; AAB98138; AAB98138; MJ_0156. DR KEGG; mja:MJ_0156; -. DR eggNOG; arCOG04360; Archaea. DR eggNOG; COG1614; LUCA. DR InParanoid; Q57620; -. DR KO; K00193; -. DR OMA; NVCVITP; -. DR PhylomeDB; Q57620; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016407; F:acetyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro. DR GO; GO:0043884; F:CO-methylating acetyl-CoA synthase activity; IEA:UniProtKB-EC. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006084; P:acetyl-CoA metabolic process; IEA:InterPro. DR HAMAP; MF_01138; CdhC; 1. DR InterPro; IPR004461; CO_DH/Ac-CoA_synth_bsu. DR InterPro; IPR023432; CO_DH/Ac-CoA_synth_bsu_arc. DR InterPro; IPR011254; Prismane-like. DR Pfam; PF03598; CdhC; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR00316; cdhC; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Nickel; Reference proteome; Transferase. FT CHAIN 1 469 Acetyl-CoA decarbonylase/synthase complex FT subunit beta 2. FT /FTId=PRO_0000155102. FT COMPBIAS 401 420 Glu-rich. FT METAL 187 187 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 190 190 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 276 276 Nickel-iron-sulfur. {ECO:0000255}. FT METAL 278 278 Nickel-iron-sulfur. {ECO:0000255}. SQ SEQUENCE 469 AA; 52642 MW; BDC866AD7C28661C CRC64; MFDDIPVSVG PMNEGERVRG PDMYVELAGP KSYGFELVKV VNKAEDKVEI IGKDIDEMEE GSRNPFAIIV EVSGSNLEED LEGVLERRIH EFLNYIEGVM HLNQRDQVWI RINKDSFNKG LRLKHIGKVV QRLFKAEFPF IEKCDVTIIT DPEKVKEELE KAREIYNKRD EKTKALHEED VDVFYGCVMC QSFAPTHVCV ITPDRPALCG GINYLDARAA AKIDPNGPIF EIPKGECLDE KLGIYSGVNE VVRERSQGTV EEVTLHSALE KPCTSCGCFE AIVFYIPEVD GFGIAHRGYK GETPMGIPFS TLAGQCSGGK QVPGFVGISI SYMKSPKFLQ GDGGWERVVW LPKELKERVK DAIPEELYDK IATEEDVKTT DELIKFLKEK GHPCAERIGA EVEEEAIEEE EVEEEMEEVE GIEVPTMTLP GTFAGLPPGI KIVLYNAVIK AEKIIITKEE PEKKKKKKK // ID ACDE_METJA Reviewed; 146 AA. AC P81332; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Acetyl-CoA decarbonylase/synthase complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134}; DE Short=ACDS complex subunit epsilon {ECO:0000255|HAMAP-Rule:MF_01134}; GN Name=cdhB {ECO:0000255|HAMAP-Rule:MF_01134}; OrderedLocusNames=MJ0154; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible cleavage CC of acetyl-CoA, allowing autotrophic growth from CO(2). Probably CC has a structural role in stabilizing the alpha-epsilon CC subcomponent of the ACDS complex by forming a structural link CC between the two alpha subunits. {ECO:0000255|HAMAP-Rule:MF_01134}. CC -!- SUBUNIT: Heterotetramer of two alpha and two epsilon chains. The CC ACDS complex is made up of alpha, epsilon, beta, gamma and delta CC chains with a probable stoichiometry of (alpha(2)epsilon(2))(4)- CC beta(8)-(gamma(1)delta(1))(8). {ECO:0000255|HAMAP-Rule:MF_01134}. CC -!- SIMILARITY: Belongs to the CdhB family. {ECO:0000255|HAMAP- CC Rule:MF_01134}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98136.1; -; Genomic_DNA. DR ProteinModelPortal; P81332; -. DR STRING; 243232.MJ_0154; -. DR EnsemblBacteria; AAB98136; AAB98136; MJ_0154. DR KEGG; mja:MJ_0154; -. DR eggNOG; arCOG04408; Archaea. DR eggNOG; COG1880; LUCA. DR InParanoid; P81332; -. DR KO; K00195; -. DR OMA; ITYYYLA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0019385; P:methanogenesis, from acetate; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR HAMAP; MF_01134; CdhB; 1. DR InterPro; IPR003704; CO_DH_CoA_synth. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR Pfam; PF02552; CO_dh; 1. DR PIRSF; PIRSF006035; CO_dh_b_ACDS_e; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR TIGRFAMs; TIGR00315; cdhB; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Acetyl-CoA decarbonylase/synthase complex FT subunit epsilon. FT /FTId=PRO_0000155090. SQ SEQUENCE 146 AA; 16858 MW; EFF8B65DDF4518D6 CRC64; MDERFIAYIP TAGSNVAHAE ITSPTLVKMM IRRAKKPILI LGENLEENEK ELISKLIEKF NLKTIKTPEE MNLMAIMKYL ASSDYDLALF TGITYYYLAQ AATHLKQFSN VVTISIDKYY QPNTLYSFPN LSKEEYLDYL RKLLEG // ID ADEC_METJA Reviewed; 556 AA. AC Q58854; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Adenine deaminase {ECO:0000255|HAMAP-Rule:MF_01518}; DE Short=Adenase {ECO:0000255|HAMAP-Rule:MF_01518}; DE Short=Adenine aminase {ECO:0000255|HAMAP-Rule:MF_01518}; DE EC=3.5.4.2 {ECO:0000255|HAMAP-Rule:MF_01518}; GN Name=ade {ECO:0000255|HAMAP-Rule:MF_01518}; OrderedLocusNames=MJ1459; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Adenine + H(2)O = hypoxanthine + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01518}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01518}; CC -!- SIMILARITY: Belongs to the adenine deaminase family. CC {ECO:0000255|HAMAP-Rule:MF_01518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99467.1; -; Genomic_DNA. DR PIR; B64482; B64482. DR ProteinModelPortal; Q58854; -. DR STRING; 243232.MJ_1459; -. DR EnsemblBacteria; AAB99467; AAB99467; MJ_1459. DR KEGG; mja:MJ_1459; -. DR eggNOG; arCOG00693; Archaea. DR eggNOG; COG1001; LUCA. DR InParanoid; Q58854; -. DR KO; K01486; -. DR OMA; CTDDKHL; -. DR PhylomeDB; Q58854; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000034; F:adenine deaminase activity; IBA:GO_Central. DR GO; GO:0006146; P:adenine catabolic process; IBA:GO_Central. DR GO; GO:0046101; P:hypoxanthine biosynthetic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 2. DR HAMAP; MF_01518; Adenine_deamin; 1. DR InterPro; IPR006679; Adenine_deam. DR InterPro; IPR026912; Adenine_deam_C. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF13382; Adenine_deam_C; 1. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR01178; ade; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Reference proteome. FT CHAIN 1 556 Adenine deaminase. FT /FTId=PRO_0000142440. SQ SEQUENCE 556 AA; 62623 MW; 06BD5E31E7EF5EFD CRC64; MIVFKNTKII DVYTGEVVKG NVAVERDKIS FVDLNDEIDK IIEKIKEDVK VIDLKGKYLS PTFIDGHIHI ESSHLIPSEF EKFVLKSGVS KVVIDPHEIA NIAGKEGILF MLNDAKILDV YVMLPSCVPA TNLETSGAEI TAENIEELIL LDNVLGLGEV MNYPAVINED EEMLKKIEVA KKYNKLIDGH CPKLKGWELN KYISHGIMSD HESVDEDEAL EKLRLGLKLM IREGTASKNI YLLNICKKIK DFRNIMLVSD DVCIKDLDGY MLNILRKATN YVSPIEAIQM VTINPANYFG FDVGIKAGNE ASFVIFEDLD NFKVYNIVIK GRFLDDVLNE LNKNKKRKIP EKLMNTLKYQ YKNEGDFLIK GIDYKERDGF IRVIKPLKDS LITEELIFST EEIKILLNEN AINKIFVIER HKNTGNIGKG LIYNFLEEGA LASSYAHDSH NVIAIGNNEK DLALAVNKLK DIGGGFIAAK DGEVVEYLPL PVGGIMGDDG KYIAEKINAL YKKIEGWSSF ENPFLSMSFF SLPVIPELKI TDKGLVKDMQ LVDLFI // ID AKSF_METJA Reviewed; 347 AA. AC Q58991; B1PL93; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 24-MAR-2009, sequence version 3. DT 11-MAY-2016, entry version 108. DE RecName: Full=Homoisocitrate dehydrogenase; DE Short=HICDH; DE EC=1.1.1.87; DE AltName: Full=Isohomocitrate dehydrogenase; DE Short=IHDH; DE AltName: Full=NAD-dependent threo-isohomocitrate dehydrogenase; GN Name=aksF; Synonyms=icd; OrderedLocusNames=MJ1596; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND RP SUBSTRATE SPECIFICITY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18765671; DOI=10.1074/jbc.M802159200; RA Drevland R.M., Jia Y., Palmer D.R.J., Graham D.E.; RT "Methanogen homoaconitase catalyzes both hydrolyase reactions in RT coenzyme B biosynthesis."; RL J. Biol. Chem. 283:28888-28896(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [3] RP CHARACTERIZATION, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10940051; DOI=10.1128/JB.182.17.5013-5016.2000; RA Howell D.M., Graupner M., Xu H., White R.H.; RT "Identification of enzymes homologous to isocitrate dehydrogenase that RT are involved in coenzyme B and leucine biosynthesis in RT methanoarchaea."; RL J. Bacteriol. 182:5013-5016(2000). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidation and CC decarboxylation of (2R,3S)-homoisocitrate ((1R,2S)-1- CC hydroxybutane-1,2,4-tricarboxylate), (2R,3S)-homo(2)-isocitrate CC and (2R,3S)-homo(3)-isocitrate, into 2-oxoadipate, 2-oxopimelate, CC and 2-oxosuberate, respectively. This last compound is a precursor CC to coenzyme B and biotin in methanoarchaea. Is also able to CC produce 2-oxoazelate from (2R,3S)-homo(4)-isocitrate. Is not able CC to use NADP as an oxidant. {ECO:0000269|PubMed:18765671}. CC -!- CATALYTIC ACTIVITY: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate + CC NAD(+) = 2-oxoadipate + CO(2) + NADH. CC {ECO:0000269|PubMed:18765671}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.037 mM for (2R,3S)-homoisocitrate CC {ECO:0000269|PubMed:10940051}; CC KM=0.016 mM for (2R,3S)-homo(2)-isocitrate CC {ECO:0000269|PubMed:10940051}; CC KM=0.021 mM for (2R,3S)-homo(3)-isocitrate CC {ECO:0000269|PubMed:10940051}; CC Vmax=2.6 umol/min/mg enzyme with (2R,3S)-homoisocitrate as CC substrate {ECO:0000269|PubMed:10940051}; CC Vmax=8.7 umol/min/mg enzyme with (2R,3S)-homo(2)-isocitrate as CC substrate {ECO:0000269|PubMed:10940051}; CC Vmax=7.1 umol/min/mg enzyme with (2R,3S)-homo(3)-isocitrate as CC substrate {ECO:0000269|PubMed:10940051}; CC Temperature dependence: CC Stable at 100 degrees Celsius for 10 min. CC {ECO:0000269|PubMed:10940051}; CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU447775; ACA28837.1; -; Genomic_DNA. DR EMBL; L77117; AAB99614.1; -; Genomic_DNA. DR ProteinModelPortal; Q58991; -. DR STRING; 243232.MJ_1596; -. DR EnsemblBacteria; AAB99614; AAB99614; MJ_1596. DR KEGG; mja:MJ_1596; -. DR eggNOG; arCOG01163; Archaea. DR eggNOG; COG0473; LUCA. DR InParanoid; Q58991; -. DR KO; K10978; -. DR OMA; PINNFGI; -. DR PhylomeDB; Q58991; -. DR BioCyc; MetaCyc:MONOMER-2004; -. DR BRENDA; 4.2.1.114; 3260. DR UniPathway; UPA00919; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:InterPro. DR GO; GO:0047046; F:homoisocitrate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0019298; P:coenzyme B biosynthetic process; IDA:MENGO. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR011828; LEU3_arc. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR02088; LEU3_arch; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Manganese; Metal-binding; NAD; KW Oxidoreductase; Phosphoprotein; Reference proteome. FT CHAIN 1 347 Homoisocitrate dehydrogenase. FT /FTId=PRO_0000083574. FT METAL 213 213 Magnesium or manganese. {ECO:0000250}. FT METAL 237 237 Magnesium or manganese. {ECO:0000250}. FT METAL 241 241 Magnesium or manganese. {ECO:0000250}. FT BINDING 81 81 Substrate. {ECO:0000250}. FT BINDING 87 87 Substrate. {ECO:0000250}. FT BINDING 97 97 Substrate. {ECO:0000250}. FT BINDING 128 128 Substrate. {ECO:0000250}. FT BINDING 213 213 Substrate. {ECO:0000250}. FT SITE 135 135 Critical for catalysis. {ECO:0000250}. FT SITE 181 181 Critical for catalysis. {ECO:0000250}. FT MOD_RES 81 81 Phosphoserine. {ECO:0000250}. FT CONFLICT 77 77 K -> Q (in Ref. 2; AAB99614). FT {ECO:0000305}. SQ SEQUENCE 347 AA; 38536 MW; 20D7BF9FDA451116 CRC64; MMKVCVIEGD GIGKEVIPEA IKILNELGEF EIIKGEAGLE CLKKYGNALP EDTIEKAKEA DIILFGAITS PKPGEVKNYK SPIITLRKMF HLYANVRPIN NFGIGQLIGK IADYEFLNAK NIDIVIIREN TEDLYVGRER LENDTAIAER VITRKGSERI IRFAFEYAIK NNRKKVSCIH KANVLRITDG LFLEVFNEIK KHYNIEADDY LVDSTAMNLI KHPEKFDVIV TTNMFGDILS DEASALIGGL GLAPSANIGD DKALFEPVHG SAPDIAGKGI ANPMASILSI AMLFDYIGEK EKGDLIREAV KYCLINKKVT PDLGGDLKTK DVGDEILNYI RKKLKGY // ID ADPP_METJA Reviewed; 169 AA. AC Q58549; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=ADP-ribose pyrophosphatase; DE EC=3.6.1.13; DE AltName: Full=ADP-ribose diphosphatase; DE AltName: Full=ADP-ribose phosphohydrolase; DE AltName: Full=Adenosine diphosphoribose pyrophosphatase; DE Short=ADPR-PPase; GN Name=nudF; OrderedLocusNames=MJ1149; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=9694840; DOI=10.1074/jbc.273.33.20924; RA Sheikh S., O'Handley S.F., Dunn C.A., Bessman M.J.; RT "Identification and characterization of the Nudix hydrolase from the RT Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose RT pyrophosphatase."; RL J. Biol. Chem. 273:20924-20928(1998). CC -!- CATALYTIC ACTIVITY: ADP-D-ribose + H(2)O = AMP + D-ribose 5- CC phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 4.85.; CC Temperature dependence: CC Thermostable.; CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. NudF subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 nudix hydrolase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00794}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99149.1; -; Genomic_DNA. DR PIR; D64443; D64443. DR ProteinModelPortal; Q58549; -. DR STRING; 243232.MJ_1149; -. DR EnsemblBacteria; AAB99149; AAB99149; MJ_1149. DR KEGG; mja:MJ_1149; -. DR eggNOG; arCOG01075; Archaea. DR eggNOG; COG1051; LUCA. DR InParanoid; Q58549; -. DR KO; K03574; -. DR OMA; YNNGIVL; -. DR PhylomeDB; Q58549; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047631; F:ADP-ribose diphosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.90.79.10; -; 1. DR InterPro; IPR020476; Nudix_hydrolase. DR InterPro; IPR020084; NUDIX_hydrolase_CS. DR InterPro; IPR000086; NUDIX_hydrolase_dom. DR InterPro; IPR015797; NUDIX_hydrolase_dom-like. DR Pfam; PF00293; NUDIX; 1. DR PRINTS; PR00502; NUDIXFAMILY. DR SUPFAM; SSF55811; SSF55811; 1. DR PROSITE; PS51462; NUDIX; 1. DR PROSITE; PS00893; NUDIX_BOX; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 169 ADP-ribose pyrophosphatase. FT /FTId=PRO_0000057047. FT REGION 12 13 Substrate binding. {ECO:0000250}. FT REGION 35 36 Substrate binding; shared with dimeric FT partner. {ECO:0000250}. FT REGION 109 111 Substrate binding; shared with dimeric FT partner. {ECO:0000250}. FT MOTIF 74 95 Nudix box. FT ACT_SITE 140 140 Proton acceptor. {ECO:0000255}. FT METAL 73 73 Magnesium 1; via carbonyl oxygen. FT {ECO:0000250}. FT METAL 89 89 Magnesium 2. {ECO:0000250}. FT METAL 89 89 Magnesium 3. {ECO:0000250}. FT METAL 93 93 Magnesium 1. {ECO:0000250}. FT METAL 93 93 Magnesium 3. {ECO:0000250}. FT METAL 142 142 Magnesium 3. {ECO:0000250}. SQ SEQUENCE 169 AA; 19144 MW; 1966F84445658B00 CRC64; MAKKCFCISG KIFALNLFGK RYSKKIIKKR DLKKYRLYLH PAVAVDGIIE KDNKILLIKR KNNPFKGCFA LPGGFVECGE TVEEAVVREI KEETGLIPKV KSLLGVYSSP DRDPRGHVIS IVFILDVIGG ELKAGDDAKE AEFFDLNNLP KLAFDHEKII KDYMRWKNG // ID AMTAB_METJA Reviewed; 427 AA. AC Q58277; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Probable threonylcarbamoyladenosine tRNA methylthiotransferase; DE EC=2.8.4.5; DE AltName: Full=tRNA-t(6)A37 methylthiotransferase; GN OrderedLocusNames=MJ0867; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the methylthiolation of N6- CC threonylcarbamoyladenosine (t(6)A), leading to the formation of 2- CC methylthio-N6-threonylcarbamoyladenosine (ms(2)t(6)A) at position CC 37 in tRNAs that read codons beginning with adenine. CC {ECO:0000250|UniProtKB:Q5VV42}. CC -!- CATALYTIC ACTIVITY: N(6)-L-threonylcarbamoyladenine(37) in tRNA + CC sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine + reduced CC electron acceptor = 2-methylthio-N(6)-L- CC threonylcarbamoyladenine(37) in tRNA + S-adenosyl-L-homocysteine + CC (sulfur carrier) + L-methionine + 5'-deoxyadenosine + electron CC acceptor. {ECO:0000250|UniProtKB:Q5VV42}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00780}; CC Note=Binds 2 [4Fe-4S] clusters. One cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|PROSITE-ProRule:PRU00780}; CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CDKAL1 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MTTase N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00780}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98872.1; -; Genomic_DNA. DR PIR; C64408; C64408. DR ProteinModelPortal; Q58277; -. DR STRING; 243232.MJ_0867; -. DR EnsemblBacteria; AAB98872; AAB98872; MJ_0867. DR KEGG; mja:MJ_0867; -. DR eggNOG; arCOG01358; Archaea. DR eggNOG; COG0621; LUCA. DR InParanoid; Q58277; -. DR OMA; VRVGMMN; -. DR PhylomeDB; Q58277; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035598; F:N6-threonylcarbomyladenosine methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0061712; F:tRNA (N(6)-L-threonylcarbamoyladenosine(37)-C(2))-methylthiotransferase; IEA:UniProtKB-EC. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GOC. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR005839; Methylthiotransferase. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR013848; Methylthiotransferase_N. DR InterPro; IPR006466; MiaB-like_B. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF01938; TRAM; 1. DR Pfam; PF00919; UPF0004; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01578; MiaB-like-B; 1. DR TIGRFAMs; TIGR00089; TIGR00089; 1. DR PROSITE; PS51449; MTTASE_N; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 427 Probable threonylcarbamoyladenosine tRNA FT methylthiotransferase. FT /FTId=PRO_0000141760. FT DOMAIN 12 118 MTTase N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00780}. FT DOMAIN 373 427 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. FT METAL 21 21 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 57 57 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 86 86 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 155 155 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 159 159 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 162 162 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. SQ SEQUENCE 427 AA; 49090 MW; CF9834E3B849F0FF CRC64; MWLYYLQVVM DMRVYVEGYG CVLNTADTEI IKNSLKKHGF EVVNNLEEAD IAIINTCVVR LETENRMIYR INELKNLGKE VVVAGCLPKA LKNKVKGFLH IYPREAHKAG EILKNYVEKH YRMPYIEEDI NKTLYKKLDY LKPSLITPLP ICEGCIGNCS YCIVKIARGG LISYPREKIV NKAKELINKG AKCLLITAQD TACYGFDIGD NLANLLNELT QIKGEFIMRV GMMHAKNAEL ILDELIEVYQ NEKVGKFLHL PLQSGDDEIL KRMKRGYTVD EFKDIVNEFR RKIKNLCFTT DIIVGFPGET EEQFQNTLEV LRELKPDYIH GAKYSQRKGT EAAKMKQIDT KIRKRRSEIL DKLRRELSYL NNKKYIGKAM KVLVLDEGKG YTDNFKVVKF EGGEVGEFRK VKITDAKTFG LKGELIL // ID ALBA_METJA Reviewed; 87 AA. AC Q57665; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=DNA/RNA-binding protein Alba {ECO:0000255|HAMAP-Rule:MF_01122}; GN Name=albA {ECO:0000255|HAMAP-Rule:MF_01122}; OrderedLocusNames=MJ0212; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds double-stranded DNA tightly but without sequence CC specificity. It is distributed uniformly and abundantly on the CC chromosome, suggesting a role in chromatin architecture. However, CC it does not significantly compact DNA. Binds rRNA and mRNA in CC vivo. May play a role in maintaining the structural and functional CC stability of RNA, and, perhaps, ribosomes. {ECO:0000255|HAMAP- CC Rule:MF_01122}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01122}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01122}. CC Chromosome {ECO:0000255|HAMAP-Rule:MF_01122}. CC -!- PTM: Acetylated. Deacetylation by the SIR2-homolog deacetylase may CC regulate its activity. {ECO:0000255|HAMAP-Rule:MF_01122}. CC -!- SIMILARITY: Belongs to the histone-like Alba family. CC {ECO:0000255|HAMAP-Rule:MF_01122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98197.1; -; Genomic_DNA. DR PIR; E64326; E64326. DR PDB; 1NH9; X-ray; 2.00 A; A=1-87. DR PDBsum; 1NH9; -. DR ProteinModelPortal; Q57665; -. DR SMR; Q57665; 1-87. DR STRING; 243232.MJ_0212; -. DR EnsemblBacteria; AAB98197; AAB98197; MJ_0212. DR KEGG; mja:MJ_0212; -. DR eggNOG; arCOG01753; Archaea. DR eggNOG; COG1581; LUCA. DR InParanoid; Q57665; -. DR KO; K03622; -. DR OMA; YVIATVM; -. DR PhylomeDB; Q57665; -. DR EvolutionaryTrace; Q57665; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003690; F:double-stranded DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.110.20; -; 1. DR HAMAP; MF_01122; AlbA; 1. DR InterPro; IPR013795; DNA/RNA-bd_Alba. DR InterPro; IPR002775; DNA/RNA-bd_Alba-like. DR Pfam; PF01918; Alba; 1. DR PIRSF; PIRSF028732; Alba; 1. DR SUPFAM; SSF82704; SSF82704; 1. DR TIGRFAMs; TIGR00285; TIGR00285; 1. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Chromosome; Complete proteome; Cytoplasm; KW DNA-binding; Reference proteome; RNA-binding. FT CHAIN 1 87 DNA/RNA-binding protein Alba. FT /FTId=PRO_0000151698. FT MOD_RES 10 10 N6-acetyllysine. {ECO:0000255|HAMAP- FT Rule:MF_01122}. FT STRAND 3 7 {ECO:0000244|PDB:1NH9}. FT HELIX 12 25 {ECO:0000244|PDB:1NH9}. FT STRAND 27 34 {ECO:0000244|PDB:1NH9}. FT HELIX 35 37 {ECO:0000244|PDB:1NH9}. FT HELIX 38 51 {ECO:0000244|PDB:1NH9}. FT STRAND 57 66 {ECO:0000244|PDB:1NH9}. FT STRAND 78 86 {ECO:0000244|PDB:1NH9}. SQ SEQUENCE 87 AA; 9675 MW; 50B16E3E9D2DB157 CRC64; MDNVVLIGKK PVMNYVVAVL TQLTSNDEVI IKARGKAINK AVDVAEMIRN RFIKDIKIKK IEIGTDKVKN PDGREVNVST IEIVLAK // ID AGLUS_METJA Reviewed; 510 AA. AC Q58746; Q4U2V1; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Archaeal glutamate synthase [NADPH]; DE EC=1.4.1.13; DE AltName: Full=Archaeal NADPH-GOGAT; GN OrderedLocusNames=MJ1351; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RA Dincturk H.B.; RT "Putative FMN-binding domain of glutamate synthase."; RL Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 L-glutamate + NADP(+) = L-glutamine + 2- CC oxoglutarate + NADPH. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the glutamate synthase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; DQ018115; AAY33887.1; -; Genomic_DNA. DR EMBL; L77117; AAB99362.1; -; Genomic_DNA. DR PIR; F64468; F64468. DR ProteinModelPortal; Q58746; -. DR STRING; 243232.MJ_1351; -. DR EnsemblBacteria; AAB99362; AAB99362; MJ_1351. DR KEGG; mja:MJ_1351; -. DR eggNOG; arCOG00619; Archaea. DR eggNOG; COG0069; LUCA. DR InParanoid; Q58746; -. DR OMA; DACQVTN; -. DR PhylomeDB; Q58746; -. DR BRENDA; 1.4.1.13; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004355; F:glutamate synthase (NADPH) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006537; P:glutamate biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR024188; GltB. DR InterPro; IPR002932; Glu_synthdom. DR Pfam; PF01645; Glu_synthase; 1. DR PIRSF; PIRSF006429; GOGAT_lg_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; Complete proteome; Flavoprotein; FMN; KW Glutamate biosynthesis; Iron; Iron-sulfur; Metal-binding; NADP; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 510 Archaeal glutamate synthase [NADPH]. FT /FTId=PRO_0000170804. FT DOMAIN 10 37 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 38 68 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 25 25 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 29 29 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 48 48 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 51 51 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 58 58 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 510 AA; 55454 MW; 4EE38CB9351D1CFA CRC64; MIPSYVPPKY KVEVDPNRCM LCERCTIECS WGVYRREGDR IISYSNRCGA CHRCVVMCPR DAITIKENAI SWRSHPLWDV DARVDIYNQA KTGCILLSGM GNAKEHPIYF DKIVLDACQV TNPSIDPLRE PMELRTYIGK KPKQLEFEFV EEEIDGKKIK KAKLKTKIAP NLKLDTPIMI AHMSYGALSL NAHLSFAKAV KECGTFMGTG EGGLPKALYP YADHIITQVA SGRFGVNEEY LMKGSAIEIK IGQGAKPGIG GHLPGEKVTA EISATRMIPE GSDAISPAPH HDIYSIEDLA QLVRSLKEAT RWKKPVFVKI AAVHNAPAIA VGIATSDADA VVIDGYKGGT GAAPKVFRDH VGIPIEMAIA AVDQRLREEG LRNEISIIAS GGIRCSADVF KAIALGADAV YIGTAAMVAL GCRVCGRCYT GLCAWGIATQ RPELVKRLDP EVGARRVANL IKAWTHEIKE LLGAAGINSI ESLRGNRDRL RGVGLNEKEL EVLGIKAAGE // ID AKSA_METJA Reviewed; 406 AA. AC Q57926; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 3. DT 11-NOV-2015, entry version 87. DE RecName: Full=Probable homocitrate synthase AksA; DE EC=2.3.3.14; DE AltName: Full=(R)-homo(2)citrate synthase; DE EC=2.3.3.-; DE AltName: Full=(R)-homo(3)citrate synthase; DE EC=2.3.3.-; GN Name=aksA; OrderedLocusNames=MJ0503; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-5, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=9665716; DOI=10.1021/bi980662p; RA Howell D.M., Harich K., Xu H., White R.H.; RT "Alpha-keto acid chain elongation reactions involved in the RT biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) RT in methanogenic Archaea."; RL Biochemistry 37:10108-10117(1998). CC -!- FUNCTION: Catalyzes the condensation of alpha-ketoglutarate and CC acetyl-CoA to form trans-homoaconitate. Can also catalyze the CC condensation of alpha-ketoadipate with acetyl-CoA to form (R)- CC homo(2)citrate, and the condensation of alpha-ketopimelate with CC acetyl-CoA to form (R)-homo(3)citrate. CC {ECO:0000269|PubMed:9665716}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + 2-oxoglutarate = (R)-2- CC hydroxybutane-1,2,4-tricarboxylate + CoA. CC {ECO:0000269|PubMed:9665716}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + 2-oxoadipate = (R)-2- CC hydroxy-1,2,5-pentanetricarboxylate + CoA. CC {ECO:0000269|PubMed:9665716}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + H(2)O + 2-oxopimelate = (R)-2- CC hydroxy-1,2,6-hexanetricarboxylate + CoA. CC {ECO:0000269|PubMed:9665716}. CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis. CC {ECO:0000269|PubMed:9665716}. CC -!- MISCELLANEOUS: Has been shown to catalyze the formation of trans- CC homoaconitate (PubMed:9665716). However, probably catalyzes the CC formation of (R)-homocitrate. {ECO:0000305|PubMed:9665716}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98494.1; -; Genomic_DNA. DR PIR; G64362; G64362. DR ProteinModelPortal; Q57926; -. DR STRING; 243232.MJ_0503; -. DR EnsemblBacteria; AAB98494; AAB98494; MJ_0503. DR KEGG; mja:MJ_0503; -. DR eggNOG; arCOG02092; Archaea. DR eggNOG; COG0119; LUCA. DR InParanoid; Q57926; -. DR KO; K10977; -. DR UniPathway; UPA00919; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004410; F:homocitrate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0019298; P:coenzyme B biosynthetic process; IDA:MENGO. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011830; LEU1_arch. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR TIGRFAMs; TIGR02090; LEU1_arch; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Transferase. FT CHAIN 1 406 Probable homocitrate synthase AksA. FT /FTId=PRO_0000140410. SQ SEQUENCE 406 AA; 45365 MW; F50D71024B188157 CRC64; MTKVLVMFMD FLFENSWKAV CPYNPKLDLK DIYIYDTTLR DGEQTPGVCF TKEQKLEIAR KLDELGLKQI EAGFPIVSER EADIVKTIAN EGLNADILAL CRALKKDIDK AIECDVDGII TFIATSPLHL KYKFNNKSLD EILEMGVEAV EYAKEHGLFV AFSAEDATRT PIEDLIKVHK AAEEAGADRV HIADTTGCAT PQSMEFICKT LKENLKKAHI GVHCHNDFGF AVINSIYGLI GGAKAVSTTV NGIGERAGNA ALEELIMALT VLYDVDLGLN LEVLPELCRM VEEYSGIKMP KNKPIVGELV FAHESGIHVD AVIENPLTYE PFLPEKIGLK RNILLGKHSG CRAVAYKLKL MGIDYDREML CEIVKKVKEI REEGKFITDE VFKEIVEEVL RKRNKN // ID ARCH_METJA Reviewed; 139 AA. AC Q60334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Protein archease {ECO:0000255|HAMAP-Rule:MF_01222}; GN OrderedLocusNames=MJ0024; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Activates the tRNA-splicing ligase complex by CC facilitating the enzymatic turnover of catalytic subunit RtcB. CC Acts by promoting the guanylylation of RtcB, a key intermediate CC step in tRNA ligation. Can also alter the NTP specificity of RtcB CC such that ATP, dGTP or ITP is used efficiently (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the archease family. {ECO:0000255|HAMAP- CC Rule:MF_01222}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98005.1; -; Genomic_DNA. DR PIR; H64302; H64302. DR ProteinModelPortal; Q60334; -. DR STRING; 243232.MJ_0024; -. DR EnsemblBacteria; AAB98005; AAB98005; MJ_0024. DR KEGG; mja:MJ_0024; -. DR eggNOG; arCOG04055; Archaea. DR eggNOG; COG1371; LUCA. DR InParanoid; Q60334; -. DR OMA; YSAMQIH; -. DR PhylomeDB; Q60334; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005509; F:calcium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006388; P:tRNA splicing, via endonucleolytic cleavage and ligation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.55.10.10; -; 1. DR HAMAP; MF_01222; Archease_arch; 1. DR InterPro; IPR002804; Archease. DR InterPro; IPR022952; Archease_arc. DR InterPro; IPR023572; Archease_dom. DR PANTHER; PTHR12682; PTHR12682; 1. DR Pfam; PF01951; Archease; 1. DR ProDom; PD012969; PD012969; 1. DR SUPFAM; SSF69819; SSF69819; 1. PE 3: Inferred from homology; KW Calcium; Complete proteome; Metal-binding; Reference proteome; KW tRNA processing. FT CHAIN 1 139 Protein archease. FT /FTId=PRO_0000068843. FT METAL 10 10 Calcium. {ECO:0000250}. FT METAL 138 138 Calcium. {ECO:0000250}. FT METAL 139 139 Calcium; via carboxylate. {ECO:0000250}. SQ SEQUENCE 139 AA; 16411 MW; 9FD640383110CEA6 CRC64; MFNYFETTAD LGVEAKGKSL EEAFKEGAKG LYNIMVDIDK VDKKEKIEFE ITGEDLEELL YNFLNELLFY TDVENLVFND FDVKIEKNDN GYRLKCTAYG EKINKEKHNI KEEVKAVTYH KMEIKQEEDG WKIRYIVDL // ID AK_METJA Reviewed; 473 AA. AC Q57991; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 106. DE RecName: Full=Probable aspartokinase; DE EC=2.7.2.4; DE AltName: Full=Aspartate kinase; GN OrderedLocusNames=MJ0571; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L- CC aspartate. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 1/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 1/5. CC -!- SIMILARITY: Belongs to the aspartokinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ACT domains. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98565.1; -; Genomic_DNA. DR PIR; C64371; C64371. DR PDB; 2HMF; X-ray; 2.70 A; A/B/C/D=2-470. DR PDB; 3C1M; X-ray; 2.30 A; A/B/C/D=1-473. DR PDB; 3C1N; X-ray; 2.72 A; A/B/C/D=1-473. DR PDB; 3C20; X-ray; 2.70 A; A/B=1-473. DR PDBsum; 2HMF; -. DR PDBsum; 3C1M; -. DR PDBsum; 3C1N; -. DR PDBsum; 3C20; -. DR ProteinModelPortal; Q57991; -. DR SMR; Q57991; 2-470. DR STRING; 243232.MJ_0571; -. DR EnsemblBacteria; AAB98565; AAB98565; MJ_0571. DR KEGG; mja:MJ_0571; -. DR eggNOG; arCOG00861; Archaea. DR eggNOG; COG0527; LUCA. DR InParanoid; Q57991; -. DR KO; K00928; -. DR OMA; GANIKMI; -. DR PhylomeDB; Q57991; -. DR BRENDA; 2.7.2.4; 3260. DR UniPathway; UPA00034; UER00015. DR UniPathway; UPA00050; UER00461. DR UniPathway; UPA00051; UER00462. DR EvolutionaryTrace; Q57991; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004072; F:aspartate kinase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1160.10; -; 2. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR005260; Asp_kin_monofn. DR InterPro; IPR001341; Asp_kinase_dom. DR InterPro; IPR018042; Aspartate_kinase_CS. DR InterPro; IPR027795; GATS-like_ACT_dom. DR Pfam; PF00696; AA_kinase; 1. DR Pfam; PF01842; ACT; 1. DR Pfam; PF13840; ACT_7; 1. DR PIRSF; PIRSF000726; Asp_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00656; asp_kin_monofn; 1. DR TIGRFAMs; TIGR00657; asp_kinases; 1. DR PROSITE; PS51671; ACT; 2. DR PROSITE; PS00324; ASPARTOKINASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Kinase; Nucleotide-binding; Reference proteome; Repeat; KW Threonine biosynthesis; Transferase. FT CHAIN 1 473 Probable aspartokinase. FT /FTId=PRO_0000066688. FT DOMAIN 323 392 ACT 1. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT DOMAIN 409 473 ACT 2. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT STRAND 3 7 {ECO:0000244|PDB:3C1M}. FT TURN 9 12 {ECO:0000244|PDB:3C1M}. FT HELIX 15 29 {ECO:0000244|PDB:3C1M}. FT STRAND 35 39 {ECO:0000244|PDB:3C1M}. FT HELIX 45 58 {ECO:0000244|PDB:3C1M}. FT HELIX 62 83 {ECO:0000244|PDB:3C1M}. FT HELIX 87 114 {ECO:0000244|PDB:3C1M}. FT HELIX 119 143 {ECO:0000244|PDB:3C1M}. FT STRAND 148 151 {ECO:0000244|PDB:3C1M}. FT HELIX 153 156 {ECO:0000244|PDB:3C1M}. FT STRAND 158 160 {ECO:0000244|PDB:3C1M}. FT STRAND 169 172 {ECO:0000244|PDB:3C1M}. FT HELIX 174 183 {ECO:0000244|PDB:3C1M}. FT STRAND 187 197 {ECO:0000244|PDB:3C1M}. FT STRAND 202 204 {ECO:0000244|PDB:3C1M}. FT TURN 207 209 {ECO:0000244|PDB:3C1M}. FT HELIX 210 220 {ECO:0000244|PDB:3C1M}. FT STRAND 224 234 {ECO:0000244|PDB:3C1M}. FT STRAND 236 238 {ECO:0000244|PDB:3C1M}. FT TURN 240 242 {ECO:0000244|PDB:3C1M}. FT STRAND 250 253 {ECO:0000244|PDB:3C1M}. FT HELIX 254 262 {ECO:0000244|PDB:3C1M}. FT STRAND 265 267 {ECO:0000244|PDB:3C20}. FT HELIX 270 272 {ECO:0000244|PDB:3C1M}. FT HELIX 273 279 {ECO:0000244|PDB:3C1M}. FT STRAND 283 287 {ECO:0000244|PDB:3C1M}. FT STRAND 296 300 {ECO:0000244|PDB:3C1M}. FT STRAND 306 308 {ECO:0000244|PDB:2HMF}. FT STRAND 311 325 {ECO:0000244|PDB:3C1M}. FT STRAND 327 329 {ECO:0000244|PDB:3C1M}. FT HELIX 331 344 {ECO:0000244|PDB:3C1M}. FT STRAND 349 354 {ECO:0000244|PDB:3C1M}. FT STRAND 361 366 {ECO:0000244|PDB:3C1M}. FT HELIX 367 369 {ECO:0000244|PDB:3C1M}. FT HELIX 370 381 {ECO:0000244|PDB:3C1M}. FT STRAND 390 392 {ECO:0000244|PDB:3C20}. FT STRAND 395 410 {ECO:0000244|PDB:3C1M}. FT TURN 412 416 {ECO:0000244|PDB:3C1M}. FT HELIX 420 431 {ECO:0000244|PDB:3C1M}. FT STRAND 437 442 {ECO:0000244|PDB:3C1M}. FT STRAND 444 452 {ECO:0000244|PDB:3C1M}. FT HELIX 453 455 {ECO:0000244|PDB:3C1M}. FT HELIX 456 467 {ECO:0000244|PDB:3C1M}. SQ SEQUENCE 473 AA; 51392 MW; 811C6E0F4B66BC5F CRC64; MTTVMKFGGT SVGSGERIRH VAKIVTKRKK EDDDVVVVVS AMSEVTNALV EISQQALDVR DIAKVGDFIK FIREKHYKAI EEAIKSEEIK EEVKKIIDSR IEELEKVLIG VAYLGELTPK SRDYILSFGE RLSSPILSGA IRDLGEKSIA LEGGEAGIIT DNNFGSARVK RLEVKERLLP LLKEGIIPVV TGFIGTTEEG YITTLGRGGS DYSAALIGYG LDADIIEIWT DVSGVYTTDP RLVPTARRIP KLSYIEAMEL AYFGAKVLHP RTIEPAMEKG IPILVKNTFE PESEGTLITN DMEMSDSIVK AISTIKNVAL INIFGAGMVG VSGTAARIFK ALGEEEVNVI LISQGSSETN ISLVVSEEDV DKALKALKRE FGDFGKKSFL NNNLIRDVSV DKDVCVISVV GAGMRGAKGI AGKIFTAVSE SGANIKMIAQ GSSEVNISFV IDEKDLLNCV RKLHEKFIEK TNS // ID AMPPA_METJA Reviewed; 503 AA. AC Q58081; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=AMP phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; DE Short=AMPpase {ECO:0000255|HAMAP-Rule:MF_02132}; DE EC=2.4.2.57 {ECO:0000255|HAMAP-Rule:MF_02132}; DE AltName: Full=Nucleoside monophosphate phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; DE Short=NMP phosphorylase {ECO:0000255|HAMAP-Rule:MF_02132}; GN OrderedLocusNames=MJ0667; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of AMP and phosphate to adenine CC and ribose 1,5-bisphosphate (R15P). Exhibits phosphorylase CC activity toward CMP and UMP in addition to AMP. Functions in an CC archaeal AMP degradation pathway, together with R15P isomerase and CC RubisCO. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: AMP + phosphate = adenine + alpha-D-ribose CC 1,5-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: CMP + phosphate = cytosine + alpha-D-ribose CC 1,5-bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- CATALYTIC ACTIVITY: UMP + phosphate = uracil + alpha-D-ribose 1,5- CC bisphosphate. {ECO:0000255|HAMAP-Rule:MF_02132}. CC -!- SIMILARITY: Belongs to the thymidine/pyrimidine-nucleoside CC phosphorylase family. Type 2 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_02132}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98662.1; -; Genomic_DNA. DR PIR; C64383; C64383. DR ProteinModelPortal; Q58081; -. DR STRING; 243232.MJ_0667; -. DR EnsemblBacteria; AAB98662; AAB98662; MJ_0667. DR KEGG; mja:MJ_0667; -. DR eggNOG; arCOG02013; Archaea. DR eggNOG; COG0213; LUCA. DR InParanoid; Q58081; -. DR KO; K18931; -. DR OMA; YVEVAIT; -. DR PhylomeDB; Q58081; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016208; F:AMP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004645; F:phosphorylase activity; IEA:InterPro. DR GO; GO:0009032; F:thymidine phosphorylase activity; IEA:InterPro. DR GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0046125; P:pyrimidine deoxyribonucleoside metabolic process; IEA:InterPro. DR GO; GO:0006206; P:pyrimidine nucleobase metabolic process; IEA:InterPro. DR Gene3D; 3.40.1030.10; -; 1. DR Gene3D; 3.90.1170.30; -; 1. DR HAMAP; MF_02132; AMP_phosphorylase; 1. DR InterPro; IPR017713; AMP_phosphorylase. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR InterPro; IPR013102; PYNP_C. DR InterPro; IPR017872; Pyrmidine_PPase_CS. DR InterPro; IPR013466; Thymidine/AMP_Pase. DR InterPro; IPR000053; Thymidine/pyrmidine_PPase. DR PANTHER; PTHR10515; PTHR10515; 1. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR Pfam; PF07831; PYNP_C; 1. DR PIRSF; PIRSF000478; TP_PyNP; 1. DR SMART; SM00941; PYNP_C; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR SUPFAM; SSF54680; SSF54680; 1. DR TIGRFAMs; TIGR03327; AMP_phos; 1. DR TIGRFAMs; TIGR02645; ARCH_P_rylase; 1. DR PROSITE; PS00647; THYMID_PHOSPHORYLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 503 AMP phosphorylase. FT /FTId=PRO_0000059088. FT NP_BIND 194 199 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. FT ACT_SITE 256 256 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02132}. FT BINDING 168 168 AMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 203 203 AMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 264 264 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. FT BINDING 288 288 AMP. {ECO:0000255|HAMAP-Rule:MF_02132}. SQ SEQUENCE 503 AA; 54722 MW; EFBB97D4A9ADEE18 CRC64; MLFLKVRVLD IDLENLVLIN SEDLKSSQYF PQDRVVVEFK GKEVIGILHS STTLINRGEI GLPQKVVKEL GVKEGDIVTI KHAEKPKSLP YIRKKMDGNK LKKEEIFEII DEMVDGKLTN IEISAFVTSL YINGMDMDEI EAMTIRMAET GEMVNWEGHI FDVHSIGGVP GNKYALLVVP IVASAGLKIP KTSSRAITSA AGTADVVEVL TRVDLTIEEI KRVVKETNGC MVWGGALDLA PADDITINVE RPLGIDPEPL LLSSVMAKKL AMGVNKLLID IPTGYGAKVK SIKEASSLAR KFIELSDRLR IVTECAITYG GQPIGRAIGP ALEAKEALLA LEDYTQAPTS LVEKSISLAG ILLEMGGVAP TGEGKELAED LLARGKAHDK FMEIIVAQGG KEVSSDEIEV GKYKADIHSP IDGYVTRISN AGITKIAKEA GAPNDKKAGI YLNVKVGNKV EKGDVLYTIY SDSEERLKSA IKLARILYPI KVEGMLLQKI SRF // ID AMYA_METJA Reviewed; 467 AA. AC Q59006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative alpha-amylase; DE EC=3.2.1.1; GN OrderedLocusNames=MJ1611; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-alpha-D-glucosidic CC linkages in polysaccharides containing three or more (1->4)-alpha- CC linked D-glucose units. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 57 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99631.1; -; Genomic_DNA. DR PIR; B64501; B64501. DR ProteinModelPortal; Q59006; -. DR STRING; 243232.MJ_1611; -. DR CAZy; GH57; Glycoside Hydrolase Family 57. DR EnsemblBacteria; AAB99631; AAB99631; MJ_1611. DR KEGG; mja:MJ_1611; -. DR eggNOG; arCOG03278; Archaea. DR eggNOG; COG1449; LUCA. DR InParanoid; Q59006; -. DR KO; K07405; -. DR OMA; SDHFYYM; -. DR PhylomeDB; Q59006; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.110.10; -; 1. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR027291; Glyco_hydro_38/57_N. DR InterPro; IPR004300; Glyco_hydro_57_N. DR Pfam; PF03065; Glyco_hydro_57; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Glycosidase; Hydrolase; KW Reference proteome. FT CHAIN 1 467 Putative alpha-amylase. FT /FTId=PRO_0000184575. FT ACT_SITE 145 145 Nucleophile. {ECO:0000250}. SQ SEQUENCE 467 AA; 55558 MW; 40A6B1CDDD4D967E CRC64; MLITFNFEVH QPHRLNKEIN QNGNTLWEKY VDTKLNKEVF NKVANKCYIP TNELILELID EYDFKVNYSI TGVFVEQALE FNDYVLDLFK DLVKTGNVEL IAETYHHSLT SLFETEDEFI EDIEMHRKMY KEIFGFKAKV FRNTELIYNN RIAKIAKDLG FKAIFTEGIE KILGWRSPNY LYQSPDGMKI LLRNYRLSDD IGFRFSARDW DQYPLTADKY AIWLASTPGE VINIYMDYET FGEHHWKETG IFEFLRYLPI EIAKHEHLEV VNVSEVVDRL EPRGEIYVHE FATISWADTE RDVSAWLGNK MQRISFEKLK DIGKFIKENS NKLKKLNKFD EIYKMYKVLQ TSDNLYYQSI KGLSDMSVHN YFSHFDTPFD AYASYLNILY DFEYYIKELL AKSEFDKNNR RKDGQKQYEK DDEVKKESLI NTNIIVAKDD KTESIYIEDE EGKKNKRYER DEGFIIA // ID APBC_METJA Reviewed; 290 AA. AC Q57731; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Iron-sulfur cluster carrier protein {ECO:0000255|HAMAP-Rule:MF_02040, ECO:0000303|PubMed:19114487}; GN OrderedLocusNames=MJ0283; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=19114487; DOI=10.1128/JB.01469-08; RA Boyd J.M., Drevland R.M., Downs D.M., Graham D.E.; RT "Archaeal ApbC/Nbp35 homologs function as iron-sulfur cluster carrier RT proteins."; RL J. Bacteriol. 191:1490-1497(2009). CC -!- FUNCTION: Binds and transfers iron-sulfur (Fe-S) clusters to CC target apoproteins. Can hydrolyze ATP. {ECO:0000255|HAMAP- CC Rule:MF_02040, ECO:0000269|PubMed:19114487}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02040}. CC -!- SIMILARITY: Belongs to the Mrp/NBP35 ATP-binding proteins family. CC {ECO:0000255|HAMAP-Rule:MF_02040}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98271.1; -; Genomic_DNA. DR PIR; D64335; D64335. DR ProteinModelPortal; Q57731; -. DR STRING; 243232.MJ_0283; -. DR EnsemblBacteria; AAB98271; AAB98271; MJ_0283. DR KEGG; mja:MJ_0283; -. DR eggNOG; arCOG00585; Archaea. DR eggNOG; COG0489; LUCA. DR InParanoid; Q57731; -. DR OMA; FEMIPPM; -. DR PhylomeDB; Q57731; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_02040; Mrp_NBP35; 1. DR InterPro; IPR019591; Mrp/NBP35_ATP-bd. DR InterPro; IPR000808; Mrp_CS. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23264; PTHR23264; 1. DR Pfam; PF10609; ParA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01215; MRP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Iron; Iron-sulfur; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 290 Iron-sulfur cluster carrier protein. FT /FTId=PRO_0000184953. FT NP_BIND 47 54 ATP. {ECO:0000255|HAMAP-Rule:MF_02040}. SQ SEQUENCE 290 AA; 31243 MW; D5C0E3A15DB728EF CRC64; MAECDGKCDT CPSKNTCPDT KKLLAQQDAK IRENMSKIKH KIVILSGKGG VGKSTVTVNL AAALNLMGKK VGVLDADIHG PNIPKMLGVE NTQPMAGPAG IFPIVTKDGI KTMSIGYLLP DDKTPVIWRG PKVSGAIRQF LSDVVWGELD YLLIDTPPGT GDEQLTIMQS IPDIDGAIIV TTPEEVSVLD VKKSIMMAKM LNIPIIGIIE NMSGFVCPYC NKVVDIFGRG GGEKAAKELG VEFLGRIPLD IKAREASDKG IPMVLLDCKA SEEFKKIVKR IVEKVEGKKE // ID AMZA_METJA Reviewed; 179 AA. AC Q57729; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Archaemetzincin {ECO:0000255|HAMAP-Rule:MF_01842}; DE EC=3.4.-.- {ECO:0000255|HAMAP-Rule:MF_01842}; GN Name=amzA {ECO:0000255|HAMAP-Rule:MF_01842}; OrderedLocusNames=MJ0281; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probable zinc metalloprotease whose natural substrate is CC unknown. {ECO:0000255|HAMAP-Rule:MF_01842}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01842}; CC Note=Binds 2 Zn(2+) ions per subunit. One is catalytic, whereas CC the other seems to have a structural role. {ECO:0000255|HAMAP- CC Rule:MF_01842}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01842}. CC -!- SIMILARITY: Belongs to the peptidase M54 family. CC {ECO:0000255|HAMAP-Rule:MF_01842}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98269.1; -; Genomic_DNA. DR PIR; B64335; B64335. DR ProteinModelPortal; Q57729; -. DR STRING; 243232.MJ_0281; -. DR MEROPS; M54.001; -. DR EnsemblBacteria; AAB98269; AAB98269; MJ_0281. DR KEGG; mja:MJ_0281; -. DR eggNOG; arCOG00458; Archaea. DR eggNOG; COG1913; LUCA. DR InParanoid; Q57729; -. DR KO; K06974; -. DR OMA; CNAIMRR; -. DR PhylomeDB; Q57729; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.390.10; -; 1. DR HAMAP; MF_01842; Archaemetzincin; 1. DR InterPro; IPR024079; MetalloPept_cat_dom. DR InterPro; IPR012962; Pept_M54_archaemetzincn. DR InterPro; IPR012091; Pept_M54_archaemetzncn_arc/bac. DR Pfam; PF07998; Peptidase_M54; 1. DR PIRSF; PIRSF005785; Zn-prot_arch; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Metalloprotease; KW Protease; Reference proteome; Zinc. FT CHAIN 1 179 Archaemetzincin. FT /FTId=PRO_0000159626. FT ACT_SITE 129 129 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01842}. FT METAL 128 128 Zinc 1; via tele nitrogen; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01842}. FT METAL 132 132 Zinc 1; via tele nitrogen; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01842}. FT METAL 138 138 Zinc 1; via tele nitrogen; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01842}. FT METAL 139 139 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01842}. FT METAL 144 144 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01842}. FT METAL 163 163 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01842}. FT METAL 166 166 Zinc 2. {ECO:0000255|HAMAP- FT Rule:MF_01842}. SQ SEQUENCE 179 AA; 20514 MW; 895A7E935A757CE8 CRC64; MVMIMRICIQ PVGDVNDEIL KFLKKKFGEV FGMCEILPKI DIPIYAYNFS RGQFNSTLIL KSLPTVEDIV LGVTEVDIYA DNLNFVFGEA ELFGKRALIS LARLRPEFYG LPPNKDVLKI RALKEAIHEI GHVLGLIHCE NKRCVMSFSN SIIDVDLKDW RYCKKCLKKL QDRGIYISI // ID APGM2_METJA Reviewed; 428 AA. AC Q60326; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 2; DE Short=BPG-independent PGAM 2; DE Short=Phosphoglyceromutase 2; DE Short=aPGAM 2; DE EC=5.4.2.12; DE AltName: Full=aPGAM-Mj2; GN Name=apgM2; OrderedLocusNames=MJ0010; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CATALYTIC ACTIVITY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12062435; DOI=10.1016/S0014-5793(02)02619-4; RA Graham D.E., Xu H., White R.H.; RT "A divergent archaeal member of the alkaline phosphatase binuclear RT metalloenzyme superfamily has phosphoglycerate mutase activity."; RL FEBS Lett. 517:190-194(2002). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000269|PubMed:12062435}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. A-PGAM subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97991.1; -; Genomic_DNA. DR PIR; B64301; B64301. DR ProteinModelPortal; Q60326; -. DR STRING; 243232.MJ_0010; -. DR EnsemblBacteria; AAB97991; AAB97991; MJ_0010. DR KEGG; mja:MJ_0010; -. DR eggNOG; arCOG01696; Archaea. DR eggNOG; COG3635; LUCA. DR InParanoid; Q60326; -. DR KO; K15635; -. DR OMA; DEAAHTK; -. DR PhylomeDB; Q60326; -. DR BRENDA; 5.4.2.12; 3260. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.720.10; -; 4. DR HAMAP; MF_01402_A; ApgM_A; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR023665; ApgAM_prokaryotes. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR004456; Phosphoglycerate_mutase_apgM. DR Pfam; PF01676; Metalloenzyme; 1. DR Pfam; PF10143; PhosphMutase; 1. DR PIRSF; PIRSF006392; IPGAM_arch; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR TIGRFAMs; TIGR00306; apgM; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycolysis; Isomerase; Reference proteome. FT CHAIN 1 428 2,3-bisphosphoglycerate-independent FT phosphoglycerate mutase 2. FT /FTId=PRO_0000138135. SQ SEQUENCE 428 AA; 49350 MW; 7107678524B1C168 CRC64; MRAILILLDG LGDRASEILN NKTPLQFAKT PNLDRLAENG MCGLMTTYKE GIPLGTEVAH FLLWGYSLEE FPGRGVIEAL GEDIEIEKNA IYLRASLGFV KKDEKGFLVI DRRTKDISRE EIEKLVDSLP TCVDGYKFEL FYSFDVHFIL KIKERNGWIS DKISDSDPFY KNRYVMKVKA IRELCKSEVE YSKAKDTARA LNKYLLNVYK ILQNHKINRK RRKLEKMPAN FLLTKWASRY KRVESFKEKW GMNAVILAES SLFKGLAKFL GMDFIKIESF EEGIDLIPEL DYDFIHLHTK ETDEAAHTKN PLNKVKVIEK IDKLIGNLKL REDDLLIITA DHSTPSVGNL IHSGESVPIL FYGKNVRVDN VKEFNEISCS NGHLRIRGEE LMHLILNYTD RALLYGLRSG DRLRYYIPKD DEIDLLEG // ID ARCS_METJA Reviewed; 569 AA. AC Q58428; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Archaeosine synthase; DE EC=2.6.1.97; DE AltName: Full=Glutamine:preQ0-tRNA amidinotransferase; GN Name=arcS; OrderedLocusNames=MJ1022; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, RP SUBSTRATE SPECIFICITY, AND NOMENCLATURE. RX PubMed=20129918; DOI=10.1074/jbc.M110.102236; RA Phillips G., Chikwana V.M., Maxwell A., El-Yacoubi B., Swairjo M.A., RA Iwata-Reuyl D., de Crecy-Lagard V.; RT "Discovery and characterization of an amidinotransferase involved in RT the modification of archaeal tRNA."; RL J. Biol. Chem. 285:12706-12713(2010). RN [3] RP FUNCTION. RX PubMed=22032275; DOI=10.1021/cb200361w; RA Phillips G., Swairjo M.A., Gaston K.W., Bailly M., Limbach P.A., RA Iwata-Reuyl D., de Crecy-Lagard V.; RT "Diversity of archaeosine synthesis in crenarchaeota."; RL ACS Chem. Biol. 7:300-305(2012). CC -!- FUNCTION: Catalyzes the conversion of 7-cyano-7-deazaguanine CC (preQ0) to archaeosine. It can also use asparagine in place of CC glutamine. {ECO:0000269|PubMed:20129918, CC ECO:0000269|PubMed:22032275}. CC -!- CATALYTIC ACTIVITY: L-glutamine + 7-cyano-7-carbaguanine(15) in CC tRNA + H(2)O = L-glutamate + archaeine(15) in tRNA. CC {ECO:0000269|PubMed:20129918}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 40 degrees Celsius. It decreases CC significantly at temperatures above 45 degrees Celsius. CC {ECO:0000269|PubMed:20129918}; CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20129918}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99026.1; -; Genomic_DNA. DR PIR; E64427; E64427. DR ProteinModelPortal; Q58428; -. DR STRING; 243232.MJ_1022; -. DR EnsemblBacteria; AAB99026; AAB99026; MJ_1022. DR KEGG; mja:MJ_1022; -. DR eggNOG; arCOG00990; Archaea. DR eggNOG; COG1549; LUCA. DR InParanoid; Q58428; -. DR KO; K07557; -. DR OMA; MTSPIGV; -. DR PhylomeDB; Q58428; -. DR BioCyc; MetaCyc:MONOMER-16209; -. DR UniPathway; UPA00393; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002948; F:archaeosine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0002927; P:archaeosine-tRNA biosynthetic process; IDA:UniProtKB. DR GO; GO:0008616; P:queuosine biosynthetic process; IEA:InterPro. DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.20.20.105; -; 1. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR InterPro; IPR005122; Uracil-DNA_glycosylase-like. DR Pfam; PF01472; PUA; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR SUPFAM; SSF52141; SSF52141; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 569 Archaeosine synthase. FT /FTId=PRO_0000107146. FT DOMAIN 495 569 PUA. {ECO:0000255|PROSITE- FT ProRule:PRU00161}. SQ SEQUENCE 569 AA; 65582 MW; E29EC27908E366ED CRC64; MLEPIAYDIG RLCKEEDKEL TPKLIDIDVI GLSQEKIFYG IMTPFRCPNS KSIYELRKSY VKADGIKMPF DTFRELTSIF KKSFIGTVKY KGNVFKYQIL NFGKHVDLIE LEDADLYIIA DGRRLIERKE LQIIPKIREK ISPNSAIYSP AVFPWEIPLL AYIGVDYFDD SLAKLYASMG YKFTKNRAVK VDSFSFEELY NNNKKVYEEI LEEVRIAIKN GFLRNVVEET AVSHPYLWAN YRRYEPDLRN IPLSKENKII VTTNINIPEV KKYLERLDNY EPYSNIIVLL PCSSKKPYSI SQSHQKFIKA IKSAKVVVEE VILTSPYGLV PRALERLVNY DIPVTGEWSF EEIELINNCL KNFLKKVKEK FDDYIVIAHL PEHYLEILEL DDIVITSKGN PTSEEALKNL TDTLKKYKEL TKSKDINKKG QRIHNIQQLA EFQFGINFIP NEIFINHKGQ IFTKINNKNQ QIASINPKNG LLILTLSGGE LLWNSGGKDI NYIEVNYEIK KGSLFPPGFV DCNENISYND EVVLIKDDTF LGIGRALMSG FEMKKAKHGA LVNIRNVKS // ID ARGC_METJA Reviewed; 341 AA. AC Q58496; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 09-DEC-2015, entry version 109. DE RecName: Full=N-acetyl-gamma-glutamyl-phosphate reductase; DE Short=AGPR; DE EC=1.2.1.38; DE AltName: Full=N-acetyl-glutamate semialdehyde dehydrogenase; DE Short=NAGSA dehydrogenase; GN Name=argC; OrderedLocusNames=MJ1096; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: N-acetyl-L-glutamate 5-semialdehyde + NADP(+) CC + phosphate = N-acetyl-5-glutamyl phosphate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 3/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NAGSA dehydrogenase family. Type 1 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99099.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99099.1; ALT_INIT; Genomic_DNA. DR PIR; G64436; G64436. DR ProteinModelPortal; Q58496; -. DR STRING; 243232.MJ_1096; -. DR EnsemblBacteria; AAB99099; AAB99099; MJ_1096. DR KEGG; mja:MJ_1096; -. DR eggNOG; arCOG00495; Archaea. DR eggNOG; COG0002; LUCA. DR InParanoid; Q58496; -. DR KO; K00145; -. DR OMA; TFVPHLT; -. DR PhylomeDB; Q58496; -. DR UniPathway; UPA00068; UER00108. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0006526; P:arginine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00150; ArgC_type1; 1. DR InterPro; IPR023013; AGPR_AS. DR InterPro; IPR000706; AGPR_type-1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01850; argC; 1. DR PROSITE; PS01224; ARGC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 341 N-acetyl-gamma-glutamyl-phosphate FT reductase. FT /FTId=PRO_0000112486. FT ACT_SITE 149 149 {ECO:0000250}. SQ SEQUENCE 341 AA; 38172 MW; 72AE13AD35061D88 CRC64; MKEVAIIGAT GYTGAELLRL LANHEKVNVT YITSRKEAGK HVFKVHPHLK GIEKYKNLCF TGDIDKVDAY LVFTATPHGA SMDIVPDFIE RGMKVIDLSG DYRFEDLSLY EKYYKIKHKG LPDVKIAYGL PELHREEIKE AQLVANPGCF PTGAILAVAP LVKENIIEER IIFDSKTGVS GAGIKPTETT HFPNVNENIN PYKITTHRHT PEIEKELKKL GKAKVSFTPH LAPITRGILT TAHTFLAKDV DREEIIKIYE KFYGSEVFVR IFSEEIPKLT WVRGTNFCDI GGFEIDEHGR LVVISAIDNL VKGASGQAIQ NMNIMFGFDE KEGLFDVGLN P // ID ARGJ_METJA Reviewed; 402 AA. AC Q57645; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Glutamate N-acetyltransferase; DE EC=2.3.1.35; DE AltName: Full=Ornithine acetyltransferase; DE Short=OATase; DE AltName: Full=Ornithine transacetylase; DE Contains: DE RecName: Full=Glutamate N-acetyltransferase alpha chain; DE Contains: DE RecName: Full=Glutamate N-acetyltransferase beta chain; GN Name=argJ; OrderedLocusNames=MJ0186; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 185-192, FUNCTION AS AN OATASE, BIOPHYSICOCHEMICAL RP PROPERTIES, CATALYTIC ACTIVITY, ENZYME REGULATION, REACTION MECHANISM, RP AND SUBUNIT. RC STRAIN=NCIMB 8224 / CCM 2186 / VKM B-718; RX PubMed=10931207; DOI=10.1046/j.1432-1327.2000.01593.x; RA Marc F., Weigel P., Legrain C., Almeras Y., Santrot M., Glansdorff N., RA Sakanyan V.; RT "Characterization and kinetic mechanism of mono- and bifunctional RT ornithine acetyltransferases from thermophilic microorganisms."; RL Eur. J. Biochem. 267:5217-5226(2000). CC -!- FUNCTION: Catalyzes only the synthesis of N-acetylglutamate from CC glutamate and acetyl-CoA as the acetyl donor. CC {ECO:0000269|PubMed:10931207}. CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + L-glutamate = L- CC ornithine + N-acetyl-L-glutamate. {ECO:0000269|PubMed:10931207}. CC -!- ENZYME REGULATION: Competitively inhibited by L-ornithine. CC {ECO:0000269|PubMed:10931207}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=9.6 mM for N-acetyl-L-ornithine CC {ECO:0000269|PubMed:10931207}; CC KM=11.3 mM for L-glutamate {ECO:0000269|PubMed:10931207}; CC Vmax=175 mmol/min/mg enzyme {ECO:0000269|PubMed:10931207}; CC pH dependence: CC Optimum pH is 8. {ECO:0000269|PubMed:10931207}; CC Temperature dependence: CC Optimum temperature is above 95 degrees Celsius. CC {ECO:0000269|PubMed:10931207}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC ornithine and N-acetyl-L-glutamate from L-glutamate and N(2)- CC acetyl-L-ornithine (cyclic): step 1/1. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains. CC {ECO:0000269|PubMed:10931207}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- MISCELLANEOUS: Some bacteria possess a monofunctional ArgJ, i.e. CC capable of catalyzing only the fifth step of the arginine CC biosynthetic pathway. CC -!- SIMILARITY: Belongs to the ArgJ family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98166.1; -; Genomic_DNA. DR PIR; C64323; C64323. DR ProteinModelPortal; Q57645; -. DR STRING; 243232.MJ_0186; -. DR MEROPS; T05.001; -. DR DNASU; 1451033; -. DR EnsemblBacteria; AAB98166; AAB98166; MJ_0186. DR KEGG; mja:MJ_0186; -. DR eggNOG; arCOG04413; Archaea. DR eggNOG; COG1364; LUCA. DR InParanoid; Q57645; -. DR KO; K00620; -. DR OMA; WTCDLTH; -. DR PhylomeDB; Q57645; -. DR UniPathway; UPA00068; UER00111. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004042; F:acetyl-CoA:L-glutamate N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0004358; F:glutamate N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0006592; P:ornithine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.60.70.12; -; 1. DR HAMAP; MF_01106; ArgJ; 1. DR InterPro; IPR002813; Arg_biosynth_ArgJ. DR InterPro; IPR016117; ArgJ-like_dom. DR PANTHER; PTHR23100; PTHR23100; 1. DR Pfam; PF01960; ArgJ; 1. DR SUPFAM; SSF56266; SSF56266; 1. DR TIGRFAMs; TIGR00120; ArgJ; 1. PE 1: Evidence at protein level; KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; KW Autocatalytic cleavage; Complete proteome; Cytoplasm; KW Direct protein sequencing; Reference proteome; Transferase. FT CHAIN 1 184 Glutamate N-acetyltransferase alpha FT chain. {ECO:0000250}. FT /FTId=PRO_0000002273. FT CHAIN 185 402 Glutamate N-acetyltransferase beta chain. FT {ECO:0000250}. FT /FTId=PRO_0000002274. FT ACT_SITE 185 185 Nucleophile. {ECO:0000250}. FT BINDING 146 146 Substrate. {ECO:0000250}. FT BINDING 172 172 Substrate. {ECO:0000250}. FT BINDING 185 185 Substrate. {ECO:0000250}. FT BINDING 267 267 Substrate. {ECO:0000250}. FT BINDING 397 397 Substrate.]. {ECO:0000250}. FT BINDING 402 402 Substrate. {ECO:0000250}. FT SITE 108 108 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000250}. FT SITE 109 109 Involved in the stabilization of negative FT charge on the oxyanion by the formation FT of the oxyanion hole. {ECO:0000250}. FT SITE 184 185 Cleavage; by autolysis. {ECO:0000250}. SQ SEQUENCE 402 AA; 43757 MW; 2D915AB01CC7A8D6 CRC64; MRVIDGGVTA PKGFKANGYK EGKFGVAIII SEKDAVGAGT FTTNKVVAHP VVLSRELIKN RDKFRAIVAN SGNANCFTKD GMEDAKEMQR LVAELFNINE DEVLVASTGV IGRKMDMNII KDRINKVYNL IKEGNSSINA AKAIMTTDTK PKEIAVEFEV NGKTVRVGGI AKGAGMIAPN MLHATMLCFI TTDIEIDKES LTNILQKVVD KTFNNISVDG DTSTNDTVFV LANGLSGVNY EECGEEFENA LLYVCRELAK MIVKDGEGAT KFMEVVVKGA KTEEDAVKAS KAIVNSLLVK TAVFGGDPNW GRIVAAVGYS GADFNPEVVD VILSNYKDEV YLVKDGIPLA DEGTEELKKA EEIMKSDEIK IVVDLKMGEF ENVCYGCDLS YEYVRINAEY TT // ID APGM1_METJA Reviewed; 411 AA. AC Q59007; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=2,3-bisphosphoglycerate-independent phosphoglycerate mutase 1; DE Short=BPG-independent PGAM 1; DE Short=Phosphoglyceromutase 1; DE Short=aPGAM 1; DE EC=5.4.2.12; DE AltName: Full=aPGAM-Mj1; GN Name=apgM1; OrderedLocusNames=MJ1612; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12062435; DOI=10.1016/S0014-5793(02)02619-4; RA Graham D.E., Xu H., White R.H.; RT "A divergent archaeal member of the alkaline phosphatase binuclear RT metalloenzyme superfamily has phosphoglycerate mutase activity."; RL FEBS Lett. 517:190-194(2002). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12076796; DOI=10.1111/j.1574-6968.2002.tb11253.x; RA van der Oost J., Huynen M.A., Verhees C.H.; RT "Molecular characterization of phosphoglycerate mutase in archaea."; RL FEMS Microbiol. Lett. 212:111-120(2002). CC -!- FUNCTION: Catalyzes the interconversion of 2-phosphoglycerate and CC 3-phosphoglycerate. {ECO:0000269|PubMed:12062435, CC ECO:0000269|PubMed:12076796}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = 3-phospho-D-glycerate. CC {ECO:0000269|PubMed:12062435, ECO:0000269|PubMed:12076796}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000305|PubMed:12076796}; CC -!- ENZYME REGULATION: Inhibited to approximately 20% by EDTA. CC {ECO:0000269|PubMed:12076796}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.0. {ECO:0000269|PubMed:12076796}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 3/5. CC {ECO:0000269|PubMed:12076796}. CC -!- SUBUNIT: Homotetramer. {ECO:0000305|PubMed:12076796}. CC -!- SIMILARITY: Belongs to the BPG-independent phosphoglycerate mutase CC family. A-PGAM subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99632.1; -; Genomic_DNA. DR PIR; C64501; C64501. DR ProteinModelPortal; Q59007; -. DR STRING; 243232.MJ_1612; -. DR EnsemblBacteria; AAB99632; AAB99632; MJ_1612. DR KEGG; mja:MJ_1612; -. DR eggNOG; arCOG01696; Archaea. DR eggNOG; COG3635; LUCA. DR InParanoid; Q59007; -. DR KO; K15635; -. DR OMA; KKTDSYG; -. DR PhylomeDB; Q59007; -. DR BRENDA; 5.4.2.12; 3260. DR UniPathway; UPA00109; UER00186. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046537; F:2,3-bisphosphoglycerate-independent phosphoglycerate mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.720.10; -; 2. DR HAMAP; MF_01402_A; ApgM_A; 1. DR InterPro; IPR017849; Alkaline_Pase-like_a/b/a. DR InterPro; IPR017850; Alkaline_phosphatase_core. DR InterPro; IPR023665; ApgAM_prokaryotes. DR InterPro; IPR006124; Metalloenzyme. DR InterPro; IPR004456; Phosphoglycerate_mutase_apgM. DR Pfam; PF01676; Metalloenzyme; 1. DR Pfam; PF10143; PhosphMutase; 1. DR PIRSF; PIRSF006392; IPGAM_arch; 1. DR SUPFAM; SSF53649; SSF53649; 2. DR TIGRFAMs; TIGR00306; apgM; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycolysis; Isomerase; Magnesium; KW Reference proteome. FT CHAIN 1 411 2,3-bisphosphoglycerate-independent FT phosphoglycerate mutase 1. FT /FTId=PRO_0000138134. SQ SEQUENCE 411 AA; 45226 MW; 47A986FD09BA1099 CRC64; MKKGKCVIFI IDGLGDRPNE KGLTPLKEAK TPTMDKIAKE GICGLMNAID IGIRPGSDTA HLAILGYNPY EVYTGRGPLE AFGVGLDLKE GDIAFRCNFA TVDENFVVLD RRAGRISPEE AEELEKEIDG LEIDGVKVIF KSSKGYRGAL VLRGEGLSCR VSDGDPHEEG VKVSEIKPLD DSEEAKRTAE ILNKLLKIVY EKLNNHPINE ERRKKGLPPA NIILPRGAGV VPKIEKFSEK YNMKGACICG TGLIKGMAKM IGLDVIEVEG ATGTPKTNFM GKAKALVEAL KEYDFVLVNV KGADEASHDG NYELKKEVLE KIDEMLAYVF EHINKDEVYF VLTGDHSTPI EMKDHSADPI PIVIWGKSVR VDDVTEFNEF ACAKGALHWI KGEHVMKILL DLTGRNEKFG A // ID ARTA_METJA Reviewed; 184 AA. AC Q60336; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Archaeosortase A; DE EC=3.4.-.-; GN Name=artA; OrderedLocusNames=MJ0027; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative protease that cleaves the C-terminus of target CC proteins. May recognize the Pro-Gly-Phe motif (Potential). CC Required for proteolytic processing of cell surface glycoprotein CC Csg near the C-terminus (By similarity). {ECO:0000250, CC ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeosortase A family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98013.1; -; Genomic_DNA. DR PIR; C64303; C64303. DR ProteinModelPortal; Q60336; -. DR STRING; 243232.MJ_0027; -. DR PRIDE; Q60336; -. DR EnsemblBacteria; AAB98013; AAB98013; MJ_0027. DR KEGG; mja:MJ_0027; -. DR eggNOG; arCOG04471; Archaea. DR eggNOG; COG4083; LUCA. DR OMA; NIFRIVL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR026485; Archaeo_ArtE. DR InterPro; IPR026392; Exo/Archaeosortase_dom. DR InterPro; IPR019127; Exosortase_EpsH-related. DR Pfam; PF09721; Exosortase_EpsH; 1. DR TIGRFAMs; TIGR04124; archaeo_artE; 1. DR TIGRFAMs; TIGR04178; exo_archaeo; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Membrane; Protease; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 184 Archaeosortase A. FT /FTId=PRO_0000106660. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. SQ SEQUENCE 184 AA; 21259 MW; DA95536BB790C5B4 CRC64; MGSLLMERNF MVEDTFTNGK LSKKEKILFL IKFYIIFLVV FFILSYFGKY LIGIVTYLSY IFTKIIISDA RLADNFIYLP NNTVEVVEEC TGSFLIAGLL ALIIVYSKNI KEFIIGIFFV LLAFFVNIFR IVLICYLVNM HPESSYLYHE IAGYGVILTL VPVLVIGYLK IIEKYRHSSN KSHL // ID ASSY_METJA Reviewed; 395 AA. AC Q60174; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Argininosuccinate synthase {ECO:0000255|HAMAP-Rule:MF_00005}; DE EC=6.3.4.5 {ECO:0000255|HAMAP-Rule:MF_00005}; DE AltName: Full=Citrulline--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00005}; GN Name=argG {ECO:0000255|HAMAP-Rule:MF_00005}; OrderedLocusNames=MJ0429; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-citrulline + L-aspartate = AMP + CC diphosphate + N(omega)-(L-arginino)succinate. {ECO:0000255|HAMAP- CC Rule:MF_00005}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00005}. CC -!- SIMILARITY: Belongs to the argininosuccinate synthase family. Type CC 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00005}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98414.1; -; Genomic_DNA. DR PIR; E64353; E64353. DR ProteinModelPortal; Q60174; -. DR STRING; 243232.MJ_0429; -. DR PRIDE; Q60174; -. DR EnsemblBacteria; AAB98414; AAB98414; MJ_0429. DR KEGG; mja:MJ_0429; -. DR eggNOG; arCOG00112; Archaea. DR eggNOG; COG0137; LUCA. DR InParanoid; Q60174; -. DR KO; K01940; -. DR OMA; PAREWGM; -. DR PhylomeDB; Q60174; -. DR UniPathway; UPA00068; UER00113. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004055; F:argininosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000053; P:argininosuccinate metabolic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.90.1260.10; -; 1. DR HAMAP; MF_00005; Arg_succ_synth_type1; 1. DR InterPro; IPR001518; Arginosuc_synth. DR InterPro; IPR018223; Arginosuc_synth_CS. DR InterPro; IPR023434; Arginosuc_synth_type_1_subfam. DR InterPro; IPR024074; AS_cat/multimer_dom_body. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00764; Arginosuc_synth; 1. DR TIGRFAMs; TIGR00032; argG; 1. DR PROSITE; PS00564; ARGININOSUCCIN_SYN_1; 1. DR PROSITE; PS00565; ARGININOSUCCIN_SYN_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 395 Argininosuccinate synthase. FT /FTId=PRO_0000148676. FT NP_BIND 8 16 ATP. {ECO:0000255|HAMAP-Rule:MF_00005}. FT BINDING 86 86 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 116 116 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00005}. FT BINDING 118 118 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 122 122 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 122 122 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 123 123 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 126 126 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 173 173 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 182 182 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 257 257 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. FT BINDING 269 269 Citrulline. {ECO:0000255|HAMAP- FT Rule:MF_00005}. SQ SEQUENCE 395 AA; 44723 MW; 655D4A7AC06E7A7F CRC64; MERIAVLAYS GGLDTSCCLK LLEDKYGYKV VSVCVDVGQP EEEIKEVEEK AKKLGVLKHY TIDAKEEFVK DYIFRAIKAN AMYEGYPLST ALARPLIAHK VVEIAEEVGA EAVAHGCTGK GNDQFRFETT IRIKAPHLKI IAPIRDLNLT RAEEIEYAKE KGIPIPTESK KYSIDENLWG RSIEGSELEN PDFVPPEEIY AWTKNPVEDK EEEIVEIEFK EGVPVAINGE KLEPVELIKK ANEIAGKHGV GRIDIIEDRI IGLKSRENYE CPGAVLLLTA HKALEQLVLT RDELRFKEIV DSLYGELIYK GLWFDPLRED LDAFIDKTQE RVTGTVKVKL FGGTARVVGR DSPYALYSKE LVSFDEKEID QKELAGMVKY HGLQAMLYEM RKKRK // ID ARFB_METJA Reviewed; 225 AA. AC Q57580; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=2-amino-5-formylamino-6-ribosylaminopyrimidin-4(3H)-one 5'-monophosphate deformylase; DE Short=FAPy deformylase; DE EC=3.5.1.102; DE AltName: Full=Formamide hydrolase; GN Name=arfB; OrderedLocusNames=MJ0116; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, PATHWAY, GENE NAME, PH RP DEPENDENCE, AND SUBUNIT. RX PubMed=19309161; DOI=10.1021/bi802341p; RA Grochowski L.L., Xu H., White R.H.; RT "An iron(II) dependent formamide hydrolase catalyzes the second step RT in the archaeal biosynthetic pathway to riboflavin and 7,8-didemethyl- RT 8-hydroxy-5-deazariboflavin."; RL Biochemistry 48:4181-4188(2009). CC -!- FUNCTION: Catalyzes the hydrolysis of the formamide of 2-amino-5- CC formylamino-6-ribosylamino-4(3H)-pyrimidinone 5'-monophosphate CC (FAPy) to form 2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'- CC phosphate (APy). {ECO:0000269|PubMed:19309161}. CC -!- CATALYTIC ACTIVITY: 2-amino-5-formylamino-6-(5-phospho-D- CC ribosylamino)pyrimidin-4(3H)-one + H(2)O = 2,5-diamino-6-(5- CC phospho-D-ribosylamino)pyrimidin-4(3H)-one + formate. CC {ECO:0000269|PubMed:19309161}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:19309161}; CC Note=Requires one Fe(2+) ion for activity. CC {ECO:0000269|PubMed:19309161}; CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:19309161}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:19309161}; CC Note=Requires an additional second metal ion that could be Fe(2+) CC or Zn(2+). {ECO:0000269|PubMed:19309161}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7-8. Has approximately 80% maximal activity at pH CC 6.5 and 40% activity at pH 8.5. {ECO:0000269|PubMed:19309161}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC {ECO:0000269|PubMed:19309161}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis. CC {ECO:0000269|PubMed:19309161}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19309161}. CC -!- SIMILARITY: Belongs to the creatininase superfamily. FAPy CC deformylase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98097.1; -; Genomic_DNA. DR PIR; D64314; D64314. DR ProteinModelPortal; Q57580; -. DR STRING; 243232.MJ_0116; -. DR EnsemblBacteria; AAB98097; AAB98097; MJ_0116. DR KEGG; mja:MJ_0116; -. DR eggNOG; arCOG04536; Archaea. DR eggNOG; COG1402; LUCA. DR InParanoid; Q57580; -. DR KO; K14653; -. DR OMA; VKHGIHN; -. DR BioCyc; MetaCyc:MONOMER-15290; -. DR BRENDA; 3.5.1.102; 3260. DR UniPathway; UPA00071; -. DR UniPathway; UPA00275; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008198; F:ferrous iron binding; IDA:UniProtKB. DR GO; GO:0016811; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amides; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0052645; P:F420-0 metabolic process; IDA:UniProtKB. DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.10310; -; 1. DR HAMAP; MF_02116; FAPy_deform; 1. DR InterPro; IPR024087; Creatininase-like_dom. DR InterPro; IPR003785; Creatininase/forma_Hydrolase. DR InterPro; IPR024901; FAPy_deformylase. DR Pfam; PF02633; Creatininase; 1. DR SUPFAM; SSF102215; SSF102215; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Iron; Metal-binding; Reference proteome; KW Zinc. FT CHAIN 1 225 2-amino-5-formylamino-6- FT ribosylaminopyrimidin-4(3H)-one 5'- FT monophosphate deformylase. FT /FTId=PRO_0000106700. FT METAL 28 28 Iron 1. {ECO:0000250}. FT METAL 30 30 Iron 2; via tele nitrogen. {ECO:0000250}. FT METAL 39 39 Iron 1. {ECO:0000250}. FT METAL 39 39 Iron 2. {ECO:0000250}. FT METAL 107 107 Iron 1; via pros nitrogen. {ECO:0000250}. SQ SEQUENCE 225 AA; 25305 MW; 929EF2CEC84DE35C CRC64; MQLRLSSGNV LNEKVHKVGI IALGSFLENH GAVLPIDTDI KIASYIALKA SILTGAKFLG VVIPSTEYEY VKHGIHNKPE EVYSYMRFLI NEGKKIGVEK FLIVNCHGGN ILVESFLKDL EYEFDIKVEM INITFTHAST EEVSVGYIIG IAKADEETLK EHNNFEKYPE VGMVGLKEAR ENNKAIDKEA KVVKRFGVKL DKKLGEKILN NAIEKVVEKI KEMIR // ID ARGB_METJA Reviewed; 300 AA. AC Q60382; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Probable acetylglutamate kinase; DE EC=2.7.2.8; DE AltName: Full=N-acetyl-L-glutamate 5-phosphotransferase; DE AltName: Full=NAG kinase; DE Short=AGK; GN Name=argB; OrderedLocusNames=MJ0069; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + N-acetyl-L-glutamate = ADP + N-acetyl-L- CC glutamate 5-phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 2/4. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the acetylglutamate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98048.1; -; Genomic_DNA. DR PIR; E64308; E64308. DR ProteinModelPortal; Q60382; -. DR SMR; Q60382; 9-300. DR STRING; 243232.MJ_0069; -. DR EnsemblBacteria; AAB98048; AAB98048; MJ_0069. DR KEGG; mja:MJ_0069; -. DR eggNOG; arCOG00862; Archaea. DR eggNOG; COG0548; LUCA. DR InParanoid; Q60382; -. DR KO; K00930; -. DR OMA; PKTECCI; -. DR PhylomeDB; Q60382; -. DR UniPathway; UPA00068; UER00107. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003991; F:acetylglutamate kinase activity; IBA:GO_Central. DR GO; GO:0034618; F:arginine binding; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_00082_A; ArgB_A; 1. DR HAMAP; MF_00082_B; ArgB_B; 1. DR InterPro; IPR004662; AcgluKinase. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF000728; NAGK; 1. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR00761; argB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 300 Probable acetylglutamate kinase. FT /FTId=PRO_0000112694. FT REGION 68 69 Substrate binding. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT BINDING 194 194 Substrate. {ECO:0000250}. FT SITE 33 33 Transition state stabilizer. FT {ECO:0000250}. FT SITE 257 257 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 300 AA; 32725 MW; B54C58AAFA43F7DA CRC64; MGMDMIEMIE KAEILMEALP FIQKFYGKIF VIKYGGHAMI DEKAKNWTAQ DVVLLKYVGI NPVVVHGGGP EINKAMEKMG KKPEFVHGLR VTDEETLDIV EMVLAGKING DIVSKLSKFG GKAVGLSGKS GRIILAKKKL KKIKTEKGEE IEVDLGRVGE TVEVNTELLE ILINNGYIPV VSPIGLDEKG EAYNLNADTV AGDIAGALKA EKLILITDVD GIMDDINNPE TLHRKLTASE LKEMIEDGRI KGGMIPKAES ALYALEHGVK SVHIINGKIP HALLLEIFTE EGIGTMITRD // ID AROD_METJA Reviewed; 220 AA. AC Q58849; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=3-dehydroquinate dehydratase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=3-dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE EC=4.2.1.10 {ECO:0000255|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I DHQase {ECO:0000255|HAMAP-Rule:MF_00214}; DE AltName: Full=Type I dehydroquinase {ECO:0000255|HAMAP-Rule:MF_00214}; DE Short=DHQ1 {ECO:0000255|HAMAP-Rule:MF_00214}; GN Name=aroD {ECO:0000255|HAMAP-Rule:MF_00214}; OrderedLocusNames=MJ1454; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the third step of the chorismate pathway, CC which leads to the biosynthesis of aromatic amino acids. Catalyzes CC the cis-dehydration of 3-dehydroquinate (DHQ) and introduces the CC first double bond of the aromatic ring to yield 3- CC dehydroshikimate. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- CATALYTIC ACTIVITY: 3-dehydroquinate = 3-dehydroshikimate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 3/7. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00214}. CC -!- SIMILARITY: Belongs to the type-I 3-dehydroquinase family. CC {ECO:0000255|HAMAP-Rule:MF_00214}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99464.1; -; Genomic_DNA. DR PIR; E64481; E64481. DR ProteinModelPortal; Q58849; -. DR STRING; 243232.MJ_1454; -. DR EnsemblBacteria; AAB99464; AAB99464; MJ_1454. DR KEGG; mja:MJ_1454; -. DR eggNOG; arCOG02097; Archaea. DR eggNOG; COG0710; LUCA. DR InParanoid; Q58849; -. DR KO; K03785; -. DR OMA; CTFGAGE; -. DR PhylomeDB; Q58849; -. DR UniPathway; UPA00053; UER00086. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003855; F:3-dehydroquinate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00214; AroD; 1. DR InterPro; IPR018508; 3-dehydroquinate_DH_AS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001381; DHquinase_I. DR Pfam; PF01487; DHquinase_I; 1. DR TIGRFAMs; TIGR01093; aroD; 1. DR PROSITE; PS01028; DEHYDROQUINASE_I; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Schiff base. FT CHAIN 1 220 3-dehydroquinate dehydratase. FT /FTId=PRO_0000138829. FT REGION 29 31 3-dehydroquinate binding. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT ACT_SITE 116 116 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT ACT_SITE 142 142 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00214}. FT BINDING 56 56 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 180 180 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 200 200 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. FT BINDING 204 204 3-dehydroquinate. {ECO:0000255|HAMAP- FT Rule:MF_00214}. SQ SEQUENCE 220 AA; 25045 MW; D607C5D02FE39363 CRC64; MICLPVVEDS VEKAIKTAEK YLEIADIVEF RIDMLKEVSE EDIEKFAKYP CIITVRADWE GGYWKGNNEE RLNLIKKAIE CNAKFVDIEL REEKNKELVK FRDEIGSKTK IIISYHDFEK TPSKEKLVEI VEKALSIGDI AKFATMANSK EDVLNILEVI NKYPGKIIGI GMGEKGKLTR ILGVYFGSIL TFASYKGKSS APGQVDIDTL KEIWRLMDLK // ID AROE_METJA Reviewed; 282 AA. AC Q58484; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 117. DE RecName: Full=Shikimate dehydrogenase (NADP(+)) {ECO:0000255|HAMAP-Rule:MF_00222}; DE Short=SDH {ECO:0000255|HAMAP-Rule:MF_00222}; DE EC=1.1.1.25 {ECO:0000255|HAMAP-Rule:MF_00222}; GN Name=aroE {ECO:0000255|HAMAP-Rule:MF_00222}; OrderedLocusNames=MJ1084; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS) IN COMPLEX WITH NADP, AND RP SUBUNIT. RX PubMed=12906831; DOI=10.1016/S0969-2126(03)00159-X; RA Padyana A.K., Burley S.K.; RT "Crystal structure of shikimate 5-dehydrogenase (SDH) bound to NADP: RT insights into function and evolution."; RL Structure 11:1005-1013(2003). CC -!- FUNCTION: Involved in the biosynthesis of the chorismate, which CC leads to the biosynthesis of aromatic amino acids. Catalyzes the CC reversible NADPH linked reduction of 3-dehydroshikimate (DHSA) to CC yield shikimate (SA). {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- CATALYTIC ACTIVITY: Shikimate + NADP(+) = 3-dehydroshikimate + CC NADPH. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 4/7. {ECO:0000255|HAMAP-Rule:MF_00222}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00222, CC ECO:0000269|PubMed:12906831}. CC -!- SIMILARITY: Belongs to the shikimate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_00222}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99086.1; -; Genomic_DNA. DR PIR; C64435; C64435. DR PDB; 1NVT; X-ray; 2.35 A; A/B=1-282. DR PDBsum; 1NVT; -. DR ProteinModelPortal; Q58484; -. DR SMR; Q58484; 1-282. DR STRING; 243232.MJ_1084; -. DR EnsemblBacteria; AAB99086; AAB99086; MJ_1084. DR KEGG; mja:MJ_1084; -. DR eggNOG; arCOG01033; Archaea. DR eggNOG; COG0169; LUCA. DR InParanoid; Q58484; -. DR KO; K00014; -. DR OMA; SIYIDAT; -. DR PhylomeDB; Q58484; -. DR BRENDA; 1.1.1.25; 3260. DR UniPathway; UPA00053; UER00087. DR EvolutionaryTrace; Q58484; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0004764; F:shikimate 3-dehydrogenase (NADP+) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019632; P:shikimate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00222; Shikimate_DH_AroE; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR011342; Shikimate_DH. DR InterPro; IPR013708; Shikimate_DH-bd_N. DR InterPro; IPR022893; Shikimate_DH_fam. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF01488; Shikimate_DH; 1. DR Pfam; PF08501; Shikimate_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00507; aroE; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Aromatic amino acid biosynthesis; Complete proteome; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 282 Shikimate dehydrogenase (NADP(+)). FT /FTId=PRO_0000136060. FT NP_BIND 130 134 NADP. {ECO:0000255|HAMAP-Rule:MF_00222, FT ECO:0000269|PubMed:12906831}. FT NP_BIND 152 157 NADP. {ECO:0000255|HAMAP-Rule:MF_00222, FT ECO:0000269|PubMed:12906831}. FT REGION 19 21 Shikimate binding. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT ACT_SITE 70 70 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 66 66 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 91 91 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 106 106 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 196 196 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222, FT ECO:0000269|PubMed:12906831}. FT BINDING 200 200 NADP. {ECO:0000269|PubMed:12906831}. FT BINDING 224 224 NADP; via carbonyl oxygen. FT {ECO:0000269|PubMed:12906831}. FT BINDING 226 226 Shikimate. {ECO:0000255|HAMAP- FT Rule:MF_00222}. FT BINDING 247 247 NADP; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00222}. FT STRAND 7 15 {ECO:0000244|PDB:1NVT}. FT HELIX 21 31 {ECO:0000244|PDB:1NVT}. FT STRAND 36 42 {ECO:0000244|PDB:1NVT}. FT HELIX 45 50 {ECO:0000244|PDB:1NVT}. FT HELIX 51 58 {ECO:0000244|PDB:1NVT}. FT STRAND 62 65 {ECO:0000244|PDB:1NVT}. FT HELIX 72 76 {ECO:0000244|PDB:1NVT}. FT STRAND 78 80 {ECO:0000244|PDB:1NVT}. FT HELIX 82 87 {ECO:0000244|PDB:1NVT}. FT STRAND 92 96 {ECO:0000244|PDB:1NVT}. FT STRAND 99 103 {ECO:0000244|PDB:1NVT}. FT HELIX 106 118 {ECO:0000244|PDB:1NVT}. FT STRAND 125 129 {ECO:0000244|PDB:1NVT}. FT HELIX 133 142 {ECO:0000244|PDB:1NVT}. FT STRAND 144 151 {ECO:0000244|PDB:1NVT}. FT HELIX 155 169 {ECO:0000244|PDB:1NVT}. FT HELIX 173 176 {ECO:0000244|PDB:1NVT}. FT STRAND 177 180 {ECO:0000244|PDB:1NVT}. FT STRAND 191 194 {ECO:0000244|PDB:1NVT}. FT STRAND 217 223 {ECO:0000244|PDB:1NVT}. FT STRAND 227 230 {ECO:0000244|PDB:1NVT}. FT HELIX 232 238 {ECO:0000244|PDB:1NVT}. FT TURN 239 241 {ECO:0000244|PDB:1NVT}. FT STRAND 243 245 {ECO:0000244|PDB:1NVT}. FT HELIX 248 263 {ECO:0000244|PDB:1NVT}. FT HELIX 269 280 {ECO:0000244|PDB:1NVT}. SQ SEQUENCE 282 AA; 30877 MW; E7398E5D642F7BD1 CRC64; MINAKTKVIG LIGHPVEHSF SPIMHNAAFK DKGLNYVYVA FDVLPENLKY VIDGAKALGI VGFNVTIPHK IEIMKYLDEI DKDAQLIGAV NTIKIEDGKA IGYNTDGIGA RMALEEEIGR VKDKNIVIYG AGGAARAVAF ELAKDNNIII ANRTVEKAEA LAKEIAEKLN KKFGEEVKFS GLDVDLDGVD IIINATPIGM YPNIDVEPIV KAEKLREDMV VMDLIYNPLE TVLLKEAKKV NAKTINGLGM LIYQGAVAFK IWTGVEPNIE VMKNAIIDKI TK // ID ARGD_METJA Reviewed; 398 AA. AC Q58131; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 111. DE RecName: Full=Acetylornithine aminotransferase {ECO:0000255|HAMAP-Rule:MF_01107}; DE Short=ACOAT {ECO:0000255|HAMAP-Rule:MF_01107}; DE EC=2.6.1.11 {ECO:0000255|HAMAP-Rule:MF_01107}; GN Name=argD {ECO:0000255|HAMAP-Rule:MF_01107}; OrderedLocusNames=MJ0721; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: N(2)-acetyl-L-ornithine + 2-oxoglutarate = N- CC acetyl-L-glutamate 5-semialdehyde + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01107}; CC Note=Binds 1 pyridoxal phosphate per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01107}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; N(2)- CC acetyl-L-ornithine from L-glutamate: step 4/4. {ECO:0000255|HAMAP- CC Rule:MF_01107}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01107}. CC -!- MISCELLANEOUS: May also have succinyldiaminopimelate CC aminotransferase activity, thus carrying out the corresponding CC step in lysine biosynthesis. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. ArgD subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01107}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98717.1; -; Genomic_DNA. DR PIR; A64390; A64390. DR ProteinModelPortal; Q58131; -. DR STRING; 243232.MJ_0721; -. DR EnsemblBacteria; AAB98717; AAB98717; MJ_0721. DR KEGG; mja:MJ_0721; -. DR eggNOG; arCOG00914; Archaea. DR eggNOG; COG4992; LUCA. DR InParanoid; Q58131; -. DR KO; K00821; -. DR OMA; LQVSKRP; -. DR PhylomeDB; Q58131; -. DR UniPathway; UPA00068; UER00109. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0003992; F:N2-acetyl-L-ornithine:2-oxoglutarate 5-aminotransferase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_01107; ArgD_aminotrans_3; 1. DR InterPro; IPR004636; AcOrn/SuccOrn_fam. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00707; argD; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Arginine biosynthesis; KW Complete proteome; Cytoplasm; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 398 Acetylornithine aminotransferase. FT /FTId=PRO_0000112821. FT REGION 223 226 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 138 138 Pyridoxal phosphate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 141 141 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 280 280 N2-acetyl-L-ornithine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. FT BINDING 281 281 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01107}. FT MOD_RES 252 252 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01107}. SQ SEQUENCE 398 AA; 44065 MW; D9EF588A9B5C3EEF CRC64; MSQENWIDLE KKYHLQIYGR LPVVLVEGKG MEVYDIDGKK YLDFLAGIGV NNVGHCHPKV VEAIKKQAET LIHTSNIYYT IPQIKLAKKL VELSGLDRAF FCNSGAEANE GAIKFARKYV SKVLGREGGE IISMYNAFHG RTLTTLAATP KPKYQDGFYP LPPGFKYVPF NDIEALKEAI TDKTAAIMIE PVQGEGGIHV ADKDYLKAVR DLCDDKNIVL IFDEVQCGMG RTGRMFAFEH YGVEPDILTL AKALGGGVPI GAVVLKEEIA KALSYGDHGT TFGGNPLACS AALASVEVIE ELIKDDKVIE KGKYFIRKLE NLIEKYNFIK EVRGLGLMIG AELEFNGADI VKKMLEKGFL INCTSDTVLR FLPPLIVEKE HIDALINALD EVFTEIKK // ID ARLY_METJA Reviewed; 484 AA. AC Q58201; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006}; DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006}; DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006}; DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006}; GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=MJ0791; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2-(N(omega)-L-arginino)succinate = fumarate + CC L-arginine. {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 3/3. CC {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98785.1; -; Genomic_DNA. DR PIR; G64398; G64398. DR ProteinModelPortal; Q58201; -. DR STRING; 243232.MJ_0791; -. DR EnsemblBacteria; AAB98785; AAB98785; MJ_0791. DR KEGG; mja:MJ_0791; -. DR eggNOG; arCOG01748; Archaea. DR eggNOG; COG0165; LUCA. DR InParanoid; Q58201; -. DR KO; K01755; -. DR OMA; AHHLMAY; -. DR PhylomeDB; Q58201; -. DR UniPathway; UPA00068; UER00114. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR HAMAP; MF_00006; Arg_succ_lyase; 1. DR InterPro; IPR029419; Arg_succ_lyase_C. DR InterPro; IPR009049; Argininosuccinate_lyase. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR PANTHER; PTHR11444; PTHR11444; 1. DR PANTHER; PTHR11444:SF3; PTHR11444:SF3; 1. DR Pfam; PF14698; ASL_C2; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00838; argH; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Lyase; Reference proteome. FT CHAIN 1 484 Argininosuccinate lyase. FT /FTId=PRO_0000137862. SQ SEQUENCE 484 AA; 55164 MW; D99A3A370E981965 CRC64; MNILRRGRLG NSIKEDVAKY TTSLSFDKEI FEADILCDIA HVIMLYEQGI IKKEDAKKII EGLKEIYKKG MENLNLDPSL DDIHMVIESE LIKKLGEDVA GRMHTGRSRN DEVATDLRIA LREKVLIIAK SLIKMLKDIL ELAEKHKETL IVGYTHLQHA QPVTFAHHLL SYVSAIERDI LRLLDAYKRI NISPLGCGAM ATTGFKINRE RTKELLGFDA LIENSMDGVS ARDFILETMA DLAILGTNLS KICEELILFS TYEFGTIEIA NEFCSTSSIM PQKKNPDVAE IARAKLSKLN GNLVTALTIL KALPNTYNRD LQEISPHLWD SVYTTIDTIK MVHGMLKTIK INKERMEELA KANYSTATEL ADTLVRETGI PFRTAHGIVG EVVRRSIEEK KDMIEVIYEV LEKYNLKVDE EKIKKALDPY ENVKMRDVIG GPAPEEVEKR IKVFRERLDR YEKEVDEKLQ KINKVKEILL SYEI // ID AROC_METJA Reviewed; 378 AA. AC Q58575; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Chorismate synthase {ECO:0000255|HAMAP-Rule:MF_00300}; DE Short=CS {ECO:0000255|HAMAP-Rule:MF_00300}; DE EC=4.2.3.5 {ECO:0000255|HAMAP-Rule:MF_00300}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate phospholyase {ECO:0000255|HAMAP-Rule:MF_00300}; GN Name=aroC {ECO:0000255|HAMAP-Rule:MF_00300}; OrderedLocusNames=MJ1175; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the anti-1,4-elimination of the C-3 phosphate CC and the C-6 proR hydrogen from 5-enolpyruvylshikimate-3-phosphate CC (EPSP) to yield chorismate, which is the branch point compound CC that serves as the starting substrate for the three terminal CC pathways of aromatic amino acid biosynthesis. This reaction CC introduces a second double bond into the aromatic ring system. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- CATALYTIC ACTIVITY: 5-O-(1-carboxyvinyl)-3-phosphoshikimate = CC chorismate + phosphate. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- COFACTOR: CC Name=FMNH2; Xref=ChEBI:CHEBI:57618; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00300}; CC Note=Reduced FMN (FMNH(2)). {ECO:0000255|HAMAP-Rule:MF_00300}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 7/7. {ECO:0000255|HAMAP-Rule:MF_00300}. CC -!- SIMILARITY: Belongs to the chorismate synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00300}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99178.1; -; Genomic_DNA. DR PIR; F64446; F64446. DR ProteinModelPortal; Q58575; -. DR STRING; 243232.MJ_1175; -. DR EnsemblBacteria; AAB99178; AAB99178; MJ_1175. DR KEGG; mja:MJ_1175; -. DR eggNOG; arCOG04133; Archaea. DR eggNOG; COG0082; LUCA. DR InParanoid; Q58575; -. DR KO; K01736; -. DR OMA; MLSINAV; -. DR PhylomeDB; Q58575; -. DR UniPathway; UPA00053; UER00090. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004107; F:chorismate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.150.10; -; 1. DR HAMAP; MF_00300; Chorismate_synth; 1. DR InterPro; IPR000453; Chorismate_synth. DR InterPro; IPR020541; Chorismate_synthase_CS. DR PANTHER; PTHR21085; PTHR21085; 1. DR Pfam; PF01264; Chorismate_synt; 1. DR PIRSF; PIRSF001456; Chorismate_synth; 1. DR SUPFAM; SSF103263; SSF103263; 1. DR TIGRFAMs; TIGR00033; aroC; 1. DR PROSITE; PS00787; CHORISMATE_SYNTHASE_1; 1. DR PROSITE; PS00788; CHORISMATE_SYNTHASE_2; 1. DR PROSITE; PS00789; CHORISMATE_SYNTHASE_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; FMN; Lyase; NADP; KW Reference proteome. FT CHAIN 1 378 Chorismate synthase. FT /FTId=PRO_0000140690. FT NP_BIND 127 129 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 255 256 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT NP_BIND 315 319 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 50 50 NADP. {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 300 300 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00300}. FT BINDING 342 342 FMN. {ECO:0000255|HAMAP-Rule:MF_00300}. SQ SEQUENCE 378 AA; 41615 MW; DEA200AFC32B0CF5 CRC64; MVTLMNTYGD MFRVTVFGES HGKAVGAVVD GCPANLPLSE EDIQKELDRR RPGQSIFSTP RKEEDKVEIL SGIFEGKTTG APICSIVYNK NMRPKDYSKI KDTPRPGHAD LTYRLKYKNY DYRGGGRASG RVTIGHVIGG AIAKKLLSYT YNIKIIGYTI KIGKIEGDFS YYKNPEVFEN EKSLERLIEI IESNPLRCPS MNEKEMEEYV LKAMENKDSV GGVVEIVALN VPVGVGNPIF NKLNGELARA LMSINAVKGV EIGAGFKAAE MYGSEMNDEM YFDDDKNIRF KTNNCGGILG GISCGTPIVL RIAVKPTPSI GKKQKTINLK TLENVEIEIE GRHDPVIVPR IVPVAEAMVA ITLADLMIKG GFIHPCSL // ID AROK_METJA Reviewed; 282 AA. AC Q58835; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Shikimate kinase; DE Short=SK; DE EC=2.7.1.71; GN Name=aroK; OrderedLocusNames=MJ1440; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CATALYTIC ACTIVITY, PATHWAY, AND SUBCELLULAR LOCATION. RX PubMed=11114929; DOI=10.1128/JB.183.1.292-300.2001; RA Daugherty M., Vonstein V., Overbeek R., Osterman A.; RT "Archaeal shikimate kinase, a new member of the GHMP-kinase family."; RL J. Bacteriol. 183:292-300(2001). CC -!- CATALYTIC ACTIVITY: ATP + shikimate = ADP + shikimate 3-phosphate. CC {ECO:0000269|PubMed:11114929}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis; chorismate from D-erythrose 4-phosphate and CC phosphoenolpyruvate: step 5/7. {ECO:0000269|PubMed:11114929}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:11114929}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Archaeal shikimate CC kinase subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99451.1; -; Genomic_DNA. DR PIR; G64479; G64479. DR ProteinModelPortal; Q58835; -. DR STRING; 243232.MJ_1440; -. DR EnsemblBacteria; AAB99451; AAB99451; MJ_1440. DR KEGG; mja:MJ_1440; -. DR eggNOG; arCOG01025; Archaea. DR eggNOG; COG1685; LUCA. DR InParanoid; Q58835; -. DR KO; K00891; -. DR OMA; DATASYY; -. DR PhylomeDB; Q58835; -. DR SABIO-RK; Q58835; -. DR UniPathway; UPA00053; UER00088. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004765; F:shikimate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00370; Shik_kinase_arch; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR010189; SK_arc. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF005758; Shikimt_kin_arch; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR01920; Shik_kin_archae; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 282 Shikimate kinase. FT /FTId=PRO_0000141574. FT NP_BIND 86 96 ATP. {ECO:0000255}. SQ SEQUENCE 282 AA; 30598 MW; 20EDBD4B736AE011 CRC64; MEGKAYALAS GTIINAIATG KGSAFGLDLK VYAKVKLIDD GKNKIEGKVL DNPNIKPNLI VRCVKNTLDY FGLNYSAYVE TKTEIPIKSG LSSSSATSNA VVLATFDALG EKIDDELILN LGIKSSFDEK LTVTGAYDDA TASYYGGITI TDNIERKILK RDKMRDDLNV LILIPNLEKN VDVNRMKLIK DYVEIAFNEA INGNYFKALF LNGILYASAL NFPTNIAIDA LDAGAITAGL SGTGPSYIAM VEDENVEKVK EKLNRYGKVI LTKPNNDGAS IY // ID ARSA_METJA Reviewed; 349 AA. AC Q58542; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative arsenical pump-driving ATPase; DE EC=3.6.3.16; DE AltName: Full=Arsenical resistance ATPase; DE AltName: Full=Arsenite-translocating ATPase; DE AltName: Full=Arsenite-transporting ATPase; GN OrderedLocusNames=MJ1142; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Anion-transporting ATPase. Catalyzes the extrusion of CC arsenite (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + arsenite(In) = ADP + phosphate + CC arsenite(Out). CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-7584233, EBI-7584233; CC -!- SIMILARITY: Belongs to the arsA ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99142.1; -; Genomic_DNA. DR PIR; E64442; E64442. DR PDB; 3UG6; X-ray; 3.30 A; A/B/C/D=1-349. DR PDB; 3UG7; X-ray; 2.90 A; A/B/C/D=1-349. DR PDBsum; 3UG6; -. DR PDBsum; 3UG7; -. DR ProteinModelPortal; Q58542; -. DR IntAct; Q58542; 5. DR MINT; MINT-8378538; -. DR STRING; 243232.MJ_1142; -. DR EnsemblBacteria; AAB99142; AAB99142; MJ_1142. DR KEGG; mja:MJ_1142; -. DR eggNOG; arCOG02849; Archaea. DR eggNOG; COG0003; LUCA. DR InParanoid; Q58542; -. DR KO; K01551; -. DR OMA; YEIDTHN; -. DR PhylomeDB; Q58542; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015446; F:arsenite-transmembrane transporting ATPase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046685; P:response to arsenic-containing substance; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR025723; Anion-transp_ATPase-like_dom. DR InterPro; IPR016300; ATPase_ArsA/GET3. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR10803; PTHR10803; 1. DR Pfam; PF02374; ArsA_ATPase; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00345; GET3_arsA_TRC40; 1. PE 1: Evidence at protein level; KW 3D-structure; Arsenical resistance; ATP-binding; Complete proteome; KW Hydrolase; Nucleotide-binding; Reference proteome. FT CHAIN 1 349 Putative arsenical pump-driving ATPase. FT /FTId=PRO_0000152257. FT NP_BIND 33 40 ATP. {ECO:0000255}. FT HELIX 13 21 {ECO:0000244|PDB:3UG7}. FT STRAND 27 32 {ECO:0000244|PDB:3UG7}. FT STRAND 34 36 {ECO:0000244|PDB:3UG7}. FT HELIX 39 52 {ECO:0000244|PDB:3UG7}. FT STRAND 57 61 {ECO:0000244|PDB:3UG7}. FT HELIX 67 72 {ECO:0000244|PDB:3UG7}. FT STRAND 77 79 {ECO:0000244|PDB:3UG6}. FT STRAND 87 93 {ECO:0000244|PDB:3UG7}. FT HELIX 96 110 {ECO:0000244|PDB:3UG7}. FT HELIX 111 113 {ECO:0000244|PDB:3UG7}. FT HELIX 115 130 {ECO:0000244|PDB:3UG7}. FT HELIX 134 148 {ECO:0000244|PDB:3UG7}. FT STRAND 153 157 {ECO:0000244|PDB:3UG7}. FT HELIX 165 170 {ECO:0000244|PDB:3UG7}. FT HELIX 171 199 {ECO:0000244|PDB:3UG7}. FT HELIX 211 232 {ECO:0000244|PDB:3UG7}. FT TURN 235 237 {ECO:0000244|PDB:3UG7}. FT STRAND 238 244 {ECO:0000244|PDB:3UG7}. FT HELIX 248 263 {ECO:0000244|PDB:3UG7}. FT STRAND 268 276 {ECO:0000244|PDB:3UG7}. FT HELIX 284 303 {ECO:0000244|PDB:3UG7}. FT STRAND 307 313 {ECO:0000244|PDB:3UG7}. FT HELIX 322 332 {ECO:0000244|PDB:3UG7}. SQ SEQUENCE 349 AA; 39919 MW; 00041F603DFDD5A3 CRC64; MLSKIKDSIN SLRGITEKKL EKKDGTKYIM FGGKGGVGKT TMSAATGVYL AEKGLKVVIV STDPAHSLRD IFEQEFGHEP TKVKGYDNLY VVEIDPQKAM EEYKEKLKAQ IEENPFLGEM LEDQLEMAAL SPGTDESAAF DVFLKYMDSN EFDVVIFDTA PTGHTLRFLG MPEVMDKYMT KLIKLRKQMS GFMKMMKKLL PFGGKDEDID YDKMLEELEK MKERIVRARN ILSDPERTAF RLVVIPEEMS ILESERAMKA LQKYGIPIDA VIVNQLIPED VQCDFCRARR ELQLKRLEMI KEKFGDKVIA YVPLLRTEAK GIETLKQIAK ILYGEEEKEE QKIEQKVGQ // ID AROA_METJA Reviewed; 429 AA. AC Q57925; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 104. DE RecName: Full=3-phosphoshikimate 1-carboxyvinyltransferase {ECO:0000255|HAMAP-Rule:MF_00210}; DE EC=2.5.1.19 {ECO:0000255|HAMAP-Rule:MF_00210}; DE AltName: Full=5-enolpyruvylshikimate-3-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSP synthase {ECO:0000255|HAMAP-Rule:MF_00210}; DE Short=EPSPS {ECO:0000255|HAMAP-Rule:MF_00210}; GN Name=aroA {ECO:0000255|HAMAP-Rule:MF_00210}; OrderedLocusNames=MJ0502; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transfer of the enolpyruvyl moiety of CC phosphoenolpyruvate (PEP) to the 5-hydroxyl of shikimate-3- CC phosphate (S3P) to produce enolpyruvyl shikimate-3-phosphate and CC inorganic phosphate. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- CATALYTIC ACTIVITY: Phosphoenolpyruvate + 3-phosphoshikimate = CC phosphate + 5-O-(1-carboxyvinyl)-3-phosphoshikimate. CC {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- PATHWAY: Metabolic intermediate biosynthesis; chorismate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00210}. CC -!- SIMILARITY: Belongs to the EPSP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00210, ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98493.1; -; Genomic_DNA. DR ProteinModelPortal; Q57925; -. DR STRING; 243232.MJ_0502; -. DR EnsemblBacteria; AAB98493; AAB98493; MJ_0502. DR KEGG; mja:MJ_0502; -. DR eggNOG; arCOG04134; Archaea. DR eggNOG; COG0128; LUCA. DR InParanoid; Q57925; -. DR KO; K00800; -. DR OMA; CPDLAQT; -. DR PhylomeDB; Q57925; -. DR UniPathway; UPA00053; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003866; F:3-phosphoshikimate 1-carboxyvinyltransferase activity; IBA:GO_Central. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009423; P:chorismate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.65.10.10; -; 2. DR HAMAP; MF_00210; EPSP_synth; 1. DR InterPro; IPR001986; Enolpyruvate_Tfrase_dom. DR InterPro; IPR006264; EPSP_synthase. DR InterPro; IPR023193; EPSP_synthase_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR Pfam; PF00275; EPSP_synthase; 1. DR PIRSF; PIRSF000505; EPSPS; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR01356; aroA; 1. DR PROSITE; PS00104; EPSP_SYNTHASE_1; 1. DR PROSITE; PS00885; EPSP_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 429 3-phosphoshikimate 1- FT carboxyvinyltransferase. FT /FTId=PRO_0000088329. FT REGION 22 23 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT REGION 91 94 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT REGION 168 170 Shikimate-3-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT ACT_SITE 311 311 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT ACT_SITE 339 339 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 27 27 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 122 122 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 196 196 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 338 338 Shikimate-3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_00210}. FT BINDING 342 342 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. FT BINDING 384 384 Phosphoenolpyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00210}. SQ SEQUENCE 429 AA; 47009 MW; EE1D8C083B934D59 CRC64; MYLLIVKKTD RLEGIVKAPP SKSYTHRAVI GASLADGVSR IINPLWGADC LSSVHGCRML GANIELDKEK DEWIVKGGEL KTPDNIIDIG NSGTTLRILT SIASQIPKGY AILTGDDSIR KRPMQPLLDA LKQLNIEAFS SKLDGTAPII VKSGKIYGNV VKIRGDISSQ FITSLMMLLP FNKEDTEIIL TSPLKSKPYI DITLDILNKF GIKIDKTDNG FLVYGNQKYK PIDYIVEGDY SSASYLIAAG VLINSNITIE NLFANSKQGD KAIINIVKEM GADIKVKKDK VIIEGEYSLK GIDVDVKDIP DLVPTIAVLG CFAEGKTEIY NGEHVRLKEC DRLRACAVEL KKMGADIEEK PDGLIIRGVK KLKGAKLNTY HDHRLVMAFT IAGLKAEGET IIEGEEAVKI SFPNFVDVMK SLGANIEVK // ID ATGT_METJA Reviewed; 655 AA. AC Q57878; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 17-FEB-2016, entry version 97. DE RecName: Full=tRNA-guanine(15) transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634}; DE EC=2.4.2.48 {ECO:0000255|HAMAP-Rule:MF_01634}; DE AltName: Full=7-cyano-7-deazaguanine tRNA-ribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01634}; DE AltName: Full=Archaeal tRNA-guanine transglycosylase {ECO:0000255|HAMAP-Rule:MF_01634}; GN Name=tgtA {ECO:0000255|HAMAP-Rule:MF_01634}; OrderedLocusNames=MJ0436; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, RP SUBSTRATES, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10862614; DOI=10.1074/jbc.M002174200; RA Bai Y., Fox D.T., Lacy J.A., Van Lanen S.G., Iwata-Reuyl D.; RT "Hypermodification of tRNA in Thermophilic archaea. Cloning, RT overexpression, and characterization of tRNA-guanine transglycosylase RT from Methanococcus jannaschii."; RL J. Biol. Chem. 275:28731-28738(2000). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Exchanges the guanine residue with 7-cyano-7- CC deazaguanine (preQ0) at position 15 in the dihydrouridine loop (D- CC loop) of archaeal tRNAs. Can also utilize guanine as substrate. CC {ECO:0000269|PubMed:10862614}. CC -!- CATALYTIC ACTIVITY: Guanine(15) in tRNA + 7-cyano-7-carbaguanine = CC 7-cyano-7-carbaguanine(15) in tRNA + guanine. CC {ECO:0000269|PubMed:10862614}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01634}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01634}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.5. {ECO:0000269|PubMed:10862614}; CC Temperature dependence: CC Optimum temperature is 85 degrees Celsius. CC {ECO:0000269|PubMed:10862614}; CC -!- PATHWAY: tRNA modification; archaeosine-tRNA biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01634}. CC -!- SIMILARITY: Belongs to the archaeosine tRNA-ribosyltransferase CC family. {ECO:0000255|HAMAP-Rule:MF_01634}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98424.1; Type=Frameshift; Positions=57; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98424.1; ALT_FRAME; Genomic_DNA. DR PIR; D64354; D64354. DR ProteinModelPortal; Q57878; -. DR STRING; 243232.MJ_0436; -. DR PRIDE; Q57878; -. DR EnsemblBacteria; AAB98424; AAB98424; MJ_0436. DR KEGG; mja:MJ_0436; -. DR eggNOG; arCOG00989; Archaea. DR eggNOG; arCOG00991; Archaea. DR eggNOG; COG0343; LUCA. DR eggNOG; COG1370; LUCA. DR InParanoid; Q57878; -. DR KO; K18779; -. DR OMA; HPNPKKQ; -. DR PhylomeDB; Q57878; -. DR BioCyc; MetaCyc:MONOMER-16210; -. DR BRENDA; 2.4.2.48; 3260. DR UniPathway; UPA00393; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008479; F:queuine tRNA-ribosyltransferase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR GO; GO:0006400; P:tRNA modification; IEA:InterPro. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.20.20.105; -; 1. DR HAMAP; MF_01634; TgtA_arch; 1. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR029402; TGT_C2. DR InterPro; IPR004804; TgtA. DR InterPro; IPR002616; tRNA_ribo_trans-like. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR Pfam; PF01472; PUA; 1. DR Pfam; PF01702; TGT; 1. DR Pfam; PF14810; TGT_C2; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF51713; SSF51713; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00432; arcsn_tRNA_tgt; 1. DR TIGRFAMs; TIGR00449; tgt_general; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Metal-binding; KW Reference proteome; Transferase; tRNA processing; Zinc. FT CHAIN 1 655 tRNA-guanine(15) transglycosylase. FT /FTId=PRO_0000135572. FT DOMAIN 577 652 PUA. FT ACT_SITE 89 89 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01634}. FT METAL 281 281 Zinc. {ECO:0000255|HAMAP-Rule:MF_01634}. FT METAL 283 283 Zinc. {ECO:0000255|HAMAP-Rule:MF_01634}. FT METAL 286 286 Zinc. {ECO:0000255|HAMAP-Rule:MF_01634}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01634}. FT BINDING 195 195 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01634}. SQ SEQUENCE 655 AA; 76076 MW; 7BE489600334AF62 CRC64; MTFEIKHRDA MGRIGILNIN GKKIETPTIM PVIHPNPKKQ IVSMDLINKL ADVIITNSYI TYKTKHLREI AEEKGIHKLI GFDKVIVTDS GSFQLGVYGD VEVEPMEIIE FQERIGVDVG TILDIPTPPD VDRERAEKEL EETLKRAKAS IELKEERGFK LLLNGTVQGS TYLDLRQKSA KEMAKLGFDI YPIGAVVPLM EQYRYRDVAE IIINSKMYLP TNKPVHLFGC GHPMFFALAV ALGCDLFDSA AYALYAKDDR YLTERGTLHL EEIKDLKAFP CSCPVCSSYT PKELASLNKK ERERLLAEHN LYVTFEEINR IKQAIRDGSL WELVEERVRC HPKLLEAYRV VRKYIDYIEK FDPVTKKSAF FYTGIESMFR PEVLRHKKRL KRLRYEKVYI TTVSSSIEKP YHEHLNVVET DVDILIKDPV FGFIPYYIDT VYPLSQHEIP ELFDYEKEIN KRFVDEFIDW LKKKIGEDNI LDIMTYNYYI NYFSANKKIN ADALRIRKML QYQYGFDIID DELMNKIKVV RSKTTGRLRQ VLDENGEILF SVRSNDNLLI PSEKGAKLLW KKIPFPKYRV VVNKEAEEFA REGRNVFAKF VIDCDEELRP YEEVLVVNED DELLAYGTTI LNGIELREFN YGLAVKVRGG LKINK // ID ASD_METJA Reviewed; 206 AA. AC Q58227; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 94. DE RecName: Full=Putative archaetidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664}; DE EC=4.1.1.- {ECO:0000255|HAMAP-Rule:MF_00664}; DE Contains: DE RecName: Full=Archaetidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664}; DE Contains: DE RecName: Full=Archaetidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664}; GN Name=asd {ECO:0000255|HAMAP-Rule:MF_00664}; OrderedLocusNames=MJ0817; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the formation of archaetidylethanolamine CC (PtdEtn) from archaetidylserine (PtdSer). {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- CATALYTIC ACTIVITY: Archaetidyl-L-serine = Archaetidylethanolamine CC + CO(2). {ECO:0000255|HAMAP-Rule:MF_00664}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00664}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00664}; CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit CC and a small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00664}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00664}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The post-translation cleavage follows an CC unusual pathway, termed non-hydrolytic serinolysis, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom CC to form the C-terminus of the beta chain, while the remainder of CC the serine residue undergoes an oxidative deamination to produce CC ammonia and the pyruvoyl prosthetic group on the alpha chain. CC {ECO:0000255|HAMAP-Rule:MF_00664}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase CC family. PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98815.1; -; Genomic_DNA. DR PIR; A64402; A64402. DR ProteinModelPortal; Q58227; -. DR STRING; 243232.MJ_0817; -. DR EnsemblBacteria; AAB98815; AAB98815; MJ_0817. DR KEGG; mja:MJ_0817; -. DR eggNOG; arCOG04470; Archaea. DR eggNOG; COG0688; LUCA. DR InParanoid; Q58227; -. DR KO; K01613; -. DR OMA; WKDGRTR; -. DR PhylomeDB; Q58227; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00664; PS_decarb_PSD_A; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033175; PSD-A. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR TIGRFAMs; TIGR00164; PS_decarb_rel; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Decarboxylase; Lipid biosynthesis; KW Lipid metabolism; Lyase; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Pyruvate; Reference proteome; Zymogen. FT CHAIN 1 171 Archaetidylserine decarboxylase beta FT chain. {ECO:0000255|HAMAP-Rule:MF_00664}. FT /FTId=PRO_0000029825. FT CHAIN 172 206 Archaetidylserine decarboxylase alpha FT chain. {ECO:0000255|HAMAP-Rule:MF_00664}. FT /FTId=PRO_0000029826. FT ACT_SITE 172 172 Schiff-base intermediate with substrate; FT via pyruvic acid. {ECO:0000255|HAMAP- FT Rule:MF_00664}. FT SITE 171 172 Cleavage (non-hydrolytic); by FT autocatalysis. {ECO:0000255|HAMAP- FT Rule:MF_00664}. FT MOD_RES 172 172 Pyruvic acid (Ser); by autocatalysis. FT {ECO:0000255|HAMAP-Rule:MF_00664}. SQ SEQUENCE 206 AA; 23055 MW; 45A264987E23FCBF CRC64; MGKYKKFFAI AVCSLLLFTV YFYRDPDRVI TKGNNIILSP ADGTVEYIKF YENGNPEVFK DGNCYVLNVS RYFPNGCYVV GIFMSPLDVH VNRAPIGGRI VYIKHIDGSF YPAFLEGVEK INERNIVIIK NGSEYVGVVQ IAGFVARRCW LSIKEGECIN MGQKIGMIKL GSQTAVIIPA NYNITVKVGE RVYAGQTIIA VKRTDN // ID ASNH2_METJA Reviewed; 515 AA. AC Q58456; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 3. DT 17-FEB-2016, entry version 101. DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] 2; DE EC=6.3.5.4; GN OrderedLocusNames=MJ1056; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + L-glutamine + H(2)O = AMP CC + diphosphate + L-asparagine + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L- CC asparagine from L-aspartate (L-Gln route): step 1/1. CC -!- SIMILARITY: Belongs to the asparagine synthetase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99058.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99058.1; ALT_INIT; Genomic_DNA. DR PIR; G64431; G64431. DR ProteinModelPortal; Q58456; -. DR STRING; 243232.MJ_1056; -. DR MEROPS; C44.001; -. DR EnsemblBacteria; AAB99058; AAB99058; MJ_1056. DR KEGG; mja:MJ_1056; -. DR eggNOG; arCOG00071; Archaea. DR eggNOG; COG0367; LUCA. DR InParanoid; Q58456; -. DR KO; K01953; -. DR OMA; WNGALYN; -. DR PhylomeDB; Q58456; -. DR UniPathway; UPA00134; UER00195. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central. DR GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR006426; Asn_synth_AEB. DR InterPro; IPR001962; Asn_synthase. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00733; Asn_synthase; 1. DR Pfam; PF13537; GATase_7; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 515 Putative asparagine synthetase FT [glutamine-hydrolyzing] 2. FT /FTId=PRO_0000056938. FT DOMAIN 2 229 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT NP_BIND 378 379 ATP. {ECO:0000250}. FT REGION 52 56 Glutamine binding. {ECO:0000250}. FT REGION 92 94 Glutamine binding. {ECO:0000250}. FT ACT_SITE 2 2 For GATase activity. {ECO:0000250}. FT BINDING 114 114 Glutamine. {ECO:0000250}. FT BINDING 306 306 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. FT SITE 380 380 Important for beta-aspartyl-AMP FT intermediate formation. {ECO:0000250}. SQ SEQUENCE 515 AA; 60473 MW; EE9EFBD4E643EDEB CRC64; MCGINGIIRF GKEVIKEEIN KMNKAIKHRG PDDEGIFIYN FKNYSIGLGH VRLAILDLSE KGHQPMGYNV DEDKIIYRDD ELDRADIIIV YNGEIYNYLE LKEKFNLETE TGTDTEVILK LYNKLGFDCV KEFNGMWAFC IFDKKKGLIF CSRDRLGVKP FYYYWDGNEF IFSSELKGIL AVKEINKKEN INKDAVELYF ALGFIPSPYS IYKNTFKLEA RQNLIFDLDK REIRKYYYWE LPDYKPIYDK KKLIEEGKKL LYDAVKIRMR SDVPVGAFLS GGLDSSTVVG VMREFTDLSK LHTFSIGFEG KYDETPYIKI VVDYFKTQHH HYYFKERDFE ELIDKYSWIY DEPFGDYSGF PTYKVSEMAR KFVTVVLSGD GGDEVFGGYM THLNGYRMDF IRKLPKFLRV VGSKLPVKKD LNGIANLYLL KEAFRLSLIN PEEFYAESIK EDAIRPEIYK KWTIEKLRYC LNKGDNKLGE ALRIFDLLFN TLCDNFLVKV DRASMLTLWK LEVHF // ID ASPD_METJA Reviewed; 267 AA. AC Q58325; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=Probable L-aspartate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01265}; DE EC=1.4.1.21 {ECO:0000255|HAMAP-Rule:MF_01265}; GN Name=nadX {ECO:0000255|HAMAP-Rule:MF_01265}; OrderedLocusNames=MJ0915; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Specifically catalyzes the NAD or NADP-dependent CC dehydrogenation of L-aspartate to iminoaspartate. CC {ECO:0000255|HAMAP-Rule:MF_01265}. CC -!- CATALYTIC ACTIVITY: L-aspartate + H(2)O + NAD(P)(+) = oxaloacetate CC + NH(3) + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_01265}. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; CC iminoaspartate from L-aspartate (dehydrogenase route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01265}. CC -!- MISCELLANEOUS: The iminoaspartate product is unstable in aqueous CC solution and can decompose to oxaloacetate and ammonia. CC {ECO:0000255|HAMAP-Rule:MF_01265}. CC -!- SIMILARITY: Belongs to the L-aspartate dehydrogenase family. CC {ECO:0000255|HAMAP-Rule:MF_01265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98920.1; -; Genomic_DNA. DR PIR; C64414; C64414. DR ProteinModelPortal; Q58325; -. DR STRING; 243232.MJ_0915; -. DR EnsemblBacteria; AAB98920; AAB98920; MJ_0915. DR KEGG; mja:MJ_0915; -. DR eggNOG; arCOG00254; Archaea. DR eggNOG; COG1712; LUCA. DR InParanoid; Q58325; -. DR KO; K06989; -. DR OMA; MIMSVGA; -. DR PhylomeDB; Q58325; -. DR UniPathway; UPA00253; UER00456. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033735; F:aspartate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006742; P:NADP catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01265; NadX; 1. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR002811; Asp_DH. DR InterPro; IPR022487; Asp_DH_arc. DR InterPro; IPR020626; Asp_DH_prok. DR InterPro; IPR011182; L-Asp_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01958; DUF108; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF005227; Asp_dh_NAD_syn; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR03855; NAD_NadX; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; NADP; Oxidoreductase; KW Pyridine nucleotide biosynthesis; Reference proteome. FT CHAIN 1 267 Probable L-aspartate dehydrogenase. FT /FTId=PRO_0000144896. FT ACT_SITE 218 218 {ECO:0000255|HAMAP-Rule:MF_01265}. FT BINDING 124 124 NAD; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01265}. FT BINDING 190 190 NAD. {ECO:0000255|HAMAP-Rule:MF_01265}. SQ SEQUENCE 267 AA; 28755 MW; B2C427DFD3AE1A4F CRC64; MLKIGIVGCG AIGNFITKKV LDGTIKNAKI SAVYDRNFDK AKTLSERTGA KICSSIDDLV KEDLDLVVEA ASIKAVEEIA EKSLINNKDV LIMSVGALAD KKLFLKLRDL AKTVGRKIYL PSGAIGGLDA IKALRLGEIE EVVLKTTKPV AALEDALKNL GYKPEDIKNP VIVFEGDVFK AIKEFPANIN VSVTLSIAAE FPAKVVIVAD PNAKLNKHEL FVKSSIGTLR VCIENVPFEE NPRTSALAAY SAVRLIRDLA EPVKVGT // ID ASNH1_METJA Reviewed; 541 AA. AC Q58516; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Putative asparagine synthetase [glutamine-hydrolyzing] 1; DE EC=6.3.5.4; GN OrderedLocusNames=MJ1116; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + L-glutamine + H(2)O = AMP CC + diphosphate + L-asparagine + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-asparagine biosynthesis; L- CC asparagine from L-aspartate (L-Gln route): step 1/1. CC -!- SIMILARITY: Belongs to the asparagine synthetase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99117.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99117.1; ALT_INIT; Genomic_DNA. DR PIR; C64439; C64439. DR ProteinModelPortal; Q58516; -. DR STRING; 243232.MJ_1116; -. DR MEROPS; C44.001; -. DR DNASU; 1452012; -. DR EnsemblBacteria; AAB99117; AAB99117; MJ_1116. DR KEGG; mja:MJ_1116; -. DR eggNOG; arCOG00071; Archaea. DR eggNOG; COG0367; LUCA. DR InParanoid; Q58516; -. DR KO; K01953; -. DR OMA; IAHYLLC; -. DR PhylomeDB; Q58516; -. DR UniPathway; UPA00134; UER00195. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004066; F:asparagine synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0042803; F:protein homodimerization activity; IBA:GO_Central. DR GO; GO:0006529; P:asparagine biosynthetic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0070981; P:L-asparagine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.620; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR006426; Asn_synth_AEB. DR InterPro; IPR001962; Asn_synthase. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00733; Asn_synthase; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01536; asn_synth_AEB; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Asparagine biosynthesis; ATP-binding; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 541 Putative asparagine synthetase FT [glutamine-hydrolyzing] 1. FT /FTId=PRO_0000056937. FT DOMAIN 2 213 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT NP_BIND 363 364 ATP. {ECO:0000250}. FT REGION 68 72 Glutamine binding. {ECO:0000250}. FT REGION 92 94 Glutamine binding. {ECO:0000250}. FT ACT_SITE 2 2 For GATase activity. {ECO:0000250}. FT BINDING 116 116 Glutamine. {ECO:0000250}. FT BINDING 289 289 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000250}. SQ SEQUENCE 541 AA; 62655 MW; 9B3FA64E39A957BB CRC64; MCSISGIIVK DNQISAKYSI DMMKILKHRG RDNSGLLLDD EVIYFNDFED VEDLEEEMIG NLSLAHNRLA IVGRYGVQPI PNEDETIWLV CNGEIYNYIE LREYLKQNHE FRTDSDNEVI IHLYEEEKLE ELDGDYAFAI YDKSKNVVRL ARDMFGVKPL FYVDRDKYFA FASERKALWH LLINIDGCER DLDELNSKIK TLKPNSQLIY YLDDNRFEII EGFKKLELNY MKERSYEEAK EYLDRALKNS VLKRVRGLDK VGIICSGGVD SSLIAKLASL YCEVILYAVG TENSEDLIYA ERLAKDLNLK LRKKIISEEE YEEYVFKVAK AIDEVDLMKI GVGIPIYVAS EMANEDGLKV VLSGQGADEL FGGYARHERI YRERGEEELK KELLKDVYNL YKVNLERDDH CTMANGVELR VPFLDEEVVE IALSIPIEYK MSELSNRPYA ESNISLKSEP INGLKNTNLN IKCVRSVRKK ILRDVASQYL PDYIAYRPKK AAQYGSGGEK MIYKVAKKYG FSKKRINEFL DMLKRKIVSE F // ID BIOB_METJA Reviewed; 358 AA. AC Q58692; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=Biotin synthase {ECO:0000255|HAMAP-Rule:MF_01694}; DE EC=2.8.1.6 {ECO:0000255|HAMAP-Rule:MF_01694}; GN Name=bioB {ECO:0000255|HAMAP-Rule:MF_01694}; OrderedLocusNames=MJ1296; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of dethiobiotin (DTB) to biotin CC by the insertion of a sulfur atom into dethiobiotin via a radical- CC based mechanism. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- CATALYTIC ACTIVITY: Dethiobiotin + sulfur-(sulfur carrier) + 2 S- CC adenosyl-L-methionine + 2 reduced [2Fe-2S] ferredoxin = biotin + CC (sulfur carrier) + 2 L-methionine + 2 5'-deoxyadenosine + 2 CC oxidized [2Fe-2S] ferredoxin. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01694}; CC Note=Binds 1 [2Fe-2S] cluster. The cluster is coordinated with 3 CC cysteines and 1 arginine. {ECO:0000255|HAMAP-Rule:MF_01694}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01694}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Biotin CC synthase family. {ECO:0000255|HAMAP-Rule:MF_01694}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99303.1; -; Genomic_DNA. DR PIR; G64461; G64461. DR ProteinModelPortal; Q58692; -. DR STRING; 243232.MJ_1296; -. DR EnsemblBacteria; AAB99303; AAB99303; MJ_1296. DR KEGG; mja:MJ_1296; -. DR eggNOG; arCOG00658; Archaea. DR eggNOG; COG0502; LUCA. DR InParanoid; Q58692; -. DR KO; K01012; -. DR OMA; NCRFCAQ; -. DR PhylomeDB; Q58692; -. DR UniPathway; UPA00078; UER00162. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004076; F:biotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_01694; BioB; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR002684; Biotin_synth/BioAB. DR InterPro; IPR024177; Biotin_synthase. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF001619; Biotin_synth; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR00433; bioB; 1. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Biotin biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Metal-binding; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 358 Biotin synthase. FT /FTId=PRO_0000185564. FT METAL 65 65 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 69 69 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 72 72 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 142 142 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 174 174 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 233 233 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. FT METAL 309 309 Iron-sulfur 2 (2Fe-2S). FT {ECO:0000255|HAMAP-Rule:MF_01694}. SQ SEQUENCE 358 AA; 40722 MW; 7EB75DC2ED9996BF CRC64; MIFMEIETFL KKSLKNKIDF DDALYLYNNF SAIDLLYLAF KIKNRIKNNS KIKLCAIINA KSGKCKEDCI FCSQSIYSKC NIPIYPLKSK KEILEYAKKI IDECSKISSS IERGTLIGAE SPNLMDVGYP NRGFPLWVER FSIVTSGKKI NDDEFIEIVE AIELIKEETN LKVCCSLGLL DREKLKELKK LDVRIHNNLE ASKNYFKNIC STHSYEDKVK VIKEAKKLDL EVCSGGIFGL GESVEERIKM AFELKELGVD SVPINILHPI EGTKAYEKIK NGEIKPISVS DALKLIALYK IIMPYAEIRL AGGRIYNLRD FQSYALMVLD GLMVGNYLTT KGRCLEDDLK MIADFHSL // ID BIOD_METJA Reviewed; 214 AA. AC Q58695; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 11-NOV-2015, entry version 95. DE RecName: Full=ATP-dependent dethiobiotin synthetase BioD {ECO:0000255|HAMAP-Rule:MF_00336}; DE EC=6.3.3.3 {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=DTB synthetase {ECO:0000255|HAMAP-Rule:MF_00336}; DE Short=DTBS {ECO:0000255|HAMAP-Rule:MF_00336}; DE AltName: Full=Dethiobiotin synthase {ECO:0000255|HAMAP-Rule:MF_00336}; GN Name=bioD {ECO:0000255|HAMAP-Rule:MF_00336}; OrderedLocusNames=MJ1299; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes a mechanistically unusual reaction, the ATP- CC dependent insertion of CO2 between the N7 and N8 nitrogen atoms of CC 7,8-diaminopelargonic acid (DAPA) to form an ureido ring. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- CATALYTIC ACTIVITY: ATP + 7,8-diaminononanoate + CO(2) = ADP + CC phosphate + dethiobiotin. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00336}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; biotin from CC 7,8-diaminononanoate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SIMILARITY: Belongs to the dethiobiotin synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00336}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99306.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99306.1; ALT_INIT; Genomic_DNA. DR PIR; B64462; B64462. DR ProteinModelPortal; Q58695; -. DR STRING; 243232.MJ_1299; -. DR EnsemblBacteria; AAB99306; AAB99306; MJ_1299. DR KEGG; mja:MJ_1299; -. DR eggNOG; arCOG00100; Archaea. DR eggNOG; COG0132; LUCA. DR InParanoid; Q58695; -. DR KO; K01935; -. DR OMA; CINHAVL; -. DR PhylomeDB; Q58695; -. DR UniPathway; UPA00078; UER00161. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004141; F:dethiobiotin synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00336; BioD; 1. DR InterPro; IPR004472; DTB_synth_BioD. DR InterPro; IPR027417; P-loop_NTPase. DR PIRSF; PIRSF006755; DTB_synth; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00347; bioD; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 214 ATP-dependent dethiobiotin synthetase FT BioD. FT /FTId=PRO_0000188005. FT NP_BIND 109 112 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT NP_BIND 169 170 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. FT METAL 14 14 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 44 44 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT METAL 109 109 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 39 39 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00336}. FT BINDING 44 44 ATP. {ECO:0000255|HAMAP-Rule:MF_00336}. SQ SEQUENCE 214 AA; 23935 MW; 0E6AA4C9FA7D39C4 CRC64; MIFITGTDTG IGKTYVSSIL AENLKKMGIN VGYLKPVETG GREDTLTLKN ILNTDDDLDL MNPINLKLPL SPNIAFDVEN SPLTLDEIKE KIKNAYETLK EKYDFLIVEG AGGVCVPIKE DFLMSDLIKF LGLDAVVVSR PNLGTINHTL LTVEHLRNKG INVRGVIINC ITDLSEVLYY EKTFETIEKV GNIEIIGIVK SREDFEIDFE KILR // ID ATPL_METJA Reviewed; 220 AA. AC Q57674; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Probable ATPase proteolipid chain; GN OrderedLocusNames=MJ0221; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the V-ATPase proteolipid subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98207.1; -; Genomic_DNA. DR PIR; F64327; F64327. DR ProteinModelPortal; Q57674; -. DR STRING; 243232.MJ_0221; -. DR EnsemblBacteria; AAB98207; AAB98207; MJ_0221. DR KEGG; mja:MJ_0221; -. DR eggNOG; arCOG02455; Archaea. DR eggNOG; COG0636; LUCA. DR InParanoid; Q57674; -. DR KO; K02124; -. DR OMA; TCAIVFT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008289; F:lipid binding; IEA:UniProtKB-KW. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR HAMAP; MF_01396; ATP_synth_c_bact; 2. DR InterPro; IPR002379; ATPase_proteolipid_c-like_dom. DR InterPro; IPR000245; ATPase_proteolipid_csu. DR Pfam; PF00137; ATP-synt_C; 3. DR PRINTS; PR00122; VACATPASE. DR SUPFAM; SSF81333; SSF81333; 3. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrogen ion transport; KW Hydrolase; Ion transport; Lipid-binding; Membrane; Nucleotide-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 220 Probable ATPase proteolipid chain. FT /FTId=PRO_0000071731. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. SQ SEQUENCE 220 AA; 21332 MW; 72DA35D2448BEAE6 CRC64; MVDPLILGAV GAGLAVGIAG LGSGIGAGIT GASGAGVVAE DPNKFGTAIV FQALPQTQGL YGFLVAILIL FVFKTVSPWA MFAAGLAAGL AGLSAIGQGI AASAGLGAVA EDNSIFGKAM VFSVLPETQA IYGLLIAILL LVGVFKGNAG AETVAALGAG FAVGFAGLSG IGQGITAAGA IGATARDPDA MGKGLVLAVM PETFAIFGLL IAILIMLMIK // ID BIOF_METJA Reviewed; 372 AA. AC Q58694; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Putative 8-amino-7-oxononanoate synthase; DE Short=AONS; DE EC=2.3.1.47; DE AltName: Full=7-keto-8-amino-pelargonic acid synthase; DE Short=7-KAP synthase; DE AltName: Full=8-amino-7-ketopelargonate synthase; GN Name=bioF; OrderedLocusNames=MJ1298; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the decarboxylative condensation of pimeloyl- CC [acyl-carrier protein] and L-alanine to produce 8-amino-7- CC oxononanoate (AON), [acyl-carrier protein], and carbon dioxide. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Pimeloyl-[acyl-carrier protein] + L-alanine = CC 8-amino-7-oxononanoate + CO(2) + holo-[acyl-carrier protein]. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. BioF subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99305.1; -; Genomic_DNA. DR PIR; A64462; A64462. DR ProteinModelPortal; Q58694; -. DR STRING; 243232.MJ_1298; -. DR EnsemblBacteria; AAB99305; AAB99305; MJ_1298. DR KEGG; mja:MJ_1298; -. DR eggNOG; arCOG00113; Archaea. DR eggNOG; COG0156; LUCA. DR InParanoid; Q58694; -. DR KO; K00652; -. DR OMA; NNIFCVG; -. DR PhylomeDB; Q58694; -. DR UniPathway; UPA00078; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008710; F:8-amino-7-oxononanoate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR001917; Aminotrans_II_pyridoxalP_BS. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004723; AONS_Archaea/Proteobacteria. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00858; bioF; 1. DR PROSITE; PS00599; AA_TRANSFER_CLASS_2; 1. PE 3: Inferred from homology; KW Biotin biosynthesis; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 372 Putative 8-amino-7-oxononanoate synthase. FT /FTId=PRO_0000163820. FT REGION 94 95 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 192 195 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 223 226 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 20 20 Substrate. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000250}. FT BINDING 167 167 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 337 337 Substrate. {ECO:0000250}. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 372 AA; 41895 MW; 145B2FA8A5F8B9D5 CRC64; MFREKLRREI EIIKNNGLYR FLRKKDDGVL DFSSNDYLCL SKHPEVIEAV KEGLKYGAGS TGSRLTSGNI NHQRLEEKIA EFKETERTLV YSSGYATNVG VISALCKKGD LILSDKLNHA SIIDGCKLSK ADVLIYNHCD VEHLTNLIEE NWGKYNNLFI VTDGVFSMDG DIAPLRDLKK IADEFNAILI IDDAHGTGVL GDGRGTLKHF NLKPSDNIVQ IGTLSKAIGG LGGFVCGIEE VVEYLINTSR SFIFSTALPP HVVEGCIKAF EIIEKTDIVK KLQKNIKIAN KVFKKYEFIK EDNLTPIYPF IFKEKTMEIA EHLIKNNIFC VGIRYPTVPK GLERIRVSIN VGHEKEDFEL LCERIKEVYS SD // ID BIOW_METJA Reviewed; 237 AA. AC Q58693; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=6-carboxyhexanoate--CoA ligase {ECO:0000255|HAMAP-Rule:MF_00668}; DE EC=6.2.1.14 {ECO:0000255|HAMAP-Rule:MF_00668}; DE AltName: Full=Pimeloyl-CoA synthase {ECO:0000255|HAMAP-Rule:MF_00668}; GN Name=bioW {ECO:0000255|HAMAP-Rule:MF_00668}; OrderedLocusNames=MJ1297; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transformation of pimelate into pimeloyl- CC CoA with concomitant hydrolysis of ATP to AMP. {ECO:0000255|HAMAP- CC Rule:MF_00668}. CC -!- CATALYTIC ACTIVITY: ATP + 6-carboxyhexanoate + CoA = AMP + CC diphosphate + 6-carboxyhexanoyl-CoA. {ECO:0000255|HAMAP- CC Rule:MF_00668}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00668}; CC -!- PATHWAY: Metabolic intermediate metabolism; pimeloyl-CoA CC biosynthesis; pimeloyl-CoA from pimelate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00668}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00668}. CC -!- SIMILARITY: Belongs to the BioW family. {ECO:0000255|HAMAP- CC Rule:MF_00668}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99304.1; -; Genomic_DNA. DR PIR; H64461; H64461. DR ProteinModelPortal; Q58693; -. DR STRING; 243232.MJ_1297; -. DR DNASU; 1452199; -. DR EnsemblBacteria; AAB99304; AAB99304; MJ_1297. DR KEGG; mja:MJ_1297; -. DR eggNOG; arCOG05075; Archaea. DR eggNOG; COG1424; LUCA. DR InParanoid; Q58693; -. DR KO; K01906; -. DR OMA; LCWSDDP; -. DR PhylomeDB; Q58693; -. DR UniPathway; UPA00999; UER00351. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042410; F:6-carboxyhexanoate-CoA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009102; P:biotin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00668; BioW; 1. DR InterPro; IPR005499; BioW. DR Pfam; PF03744; BioW; 1. DR ProDom; PD017229; BioW; 1. DR TIGRFAMs; TIGR01204; bioW; 1. PE 3: Inferred from homology; KW ATP-binding; Biotin biosynthesis; Complete proteome; Ligase; KW Magnesium; Nucleotide-binding; Reference proteome. FT CHAIN 1 237 6-carboxyhexanoate--CoA ligase. FT /FTId=PRO_0000191025. SQ SEQUENCE 237 AA; 26884 MW; A6B385A9524CA29D CRC64; MVIVMYSIKM RASKNGKHIS GAERIVNKDE IEETVKELVR RALTHENGTP DFINIKIEEI KEEITYINHL PIKTIHCKDK EEARETAKKI LRNEGIPDSV IDYAYEIIDK GGMRGAAILN LKGERLEPDK ERGVRVKNID TTKELKEKIL KENLGTERTV DAIAIASKVI HLGVIAELCT SDNKSYTTGY VATKKGYFRI TNLKKEGESG GRVFFVKDDV DIEDLINKLE NKPFIIK // ID BPL_METJA Reviewed; 237 AA. AC Q59014; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative biotin ligase; DE EC=6.3.4.15; GN OrderedLocusNames=MJ1619; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + biotin + apo-[acetyl-CoA:carbon-dioxide CC ligase (ADP-forming)] = AMP + diphosphate + [acetyl-CoA:carbon- CC dioxide ligase (ADP-forming)]. CC -!- SIMILARITY: Belongs to the biotin--protein ligase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 BPL/LPL catalytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01067}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99640.1; -; Genomic_DNA. DR PIR; B64502; B64502. DR PDB; 2EJ9; X-ray; 2.00 A; A=1-237. DR PDBsum; 2EJ9; -. DR ProteinModelPortal; Q59014; -. DR SMR; Q59014; 1-237. DR STRING; 243232.MJ_1619; -. DR PRIDE; Q59014; -. DR EnsemblBacteria; AAB99640; AAB99640; MJ_1619. DR KEGG; mja:MJ_1619; -. DR eggNOG; arCOG01940; Archaea. DR eggNOG; COG0340; LUCA. DR InParanoid; Q59014; -. DR KO; K03524; -. DR OMA; NNDPPLE; -. DR PhylomeDB; Q59014; -. DR EvolutionaryTrace; Q59014; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004077; F:biotin-[acetyl-CoA-carboxylase] ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR InterPro; IPR004408; Biotin_CoA_COase_ligase. DR InterPro; IPR003142; BPL_C. DR InterPro; IPR004143; BPL_LPL_catalytic. DR PANTHER; PTHR12835; PTHR12835; 1. DR Pfam; PF02237; BPL_C; 1. DR Pfam; PF03099; BPL_LplA_LipB; 1. DR TIGRFAMs; TIGR00121; birA_ligase; 1. DR PROSITE; PS51733; BPL_LPL_CATALYTIC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Biotin; Complete proteome; Ligase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 237 Putative biotin ligase. FT /FTId=PRO_0000064982. FT DOMAIN 1 191 BPL/LPL catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01067}. FT STRAND 2 7 {ECO:0000244|PDB:2EJ9}. FT HELIX 12 21 {ECO:0000244|PDB:2EJ9}. FT STRAND 26 32 {ECO:0000244|PDB:2EJ9}. FT STRAND 34 36 {ECO:0000244|PDB:2EJ9}. FT HELIX 40 42 {ECO:0000244|PDB:2EJ9}. FT STRAND 51 59 {ECO:0000244|PDB:2EJ9}. FT HELIX 65 80 {ECO:0000244|PDB:2EJ9}. FT TURN 81 83 {ECO:0000244|PDB:2EJ9}. FT STRAND 88 91 {ECO:0000244|PDB:2EJ9}. FT TURN 92 94 {ECO:0000244|PDB:2EJ9}. FT STRAND 95 100 {ECO:0000244|PDB:2EJ9}. FT STRAND 103 114 {ECO:0000244|PDB:2EJ9}. FT STRAND 116 125 {ECO:0000244|PDB:2EJ9}. FT STRAND 127 129 {ECO:0000244|PDB:2EJ9}. FT HELIX 133 137 {ECO:0000244|PDB:2EJ9}. FT HELIX 142 146 {ECO:0000244|PDB:2EJ9}. FT HELIX 152 171 {ECO:0000244|PDB:2EJ9}. FT HELIX 177 187 {ECO:0000244|PDB:2EJ9}. FT STRAND 188 190 {ECO:0000244|PDB:2EJ9}. FT STRAND 194 199 {ECO:0000244|PDB:2EJ9}. FT STRAND 204 212 {ECO:0000244|PDB:2EJ9}. FT STRAND 214 221 {ECO:0000244|PDB:2EJ9}. FT STRAND 224 229 {ECO:0000244|PDB:2EJ9}. FT HELIX 230 232 {ECO:0000244|PDB:2EJ9}. FT STRAND 233 236 {ECO:0000244|PDB:2EJ9}. SQ SEQUENCE 237 AA; 27185 MW; 602506218437B1F6 CRC64; MEIIHLSEID STNDYAKELA KEGKRNFIVL ADKQNNGKGR WGRVWYSDEG GLYFSMVLDS KLYNPKVINL LVPICIIEVL KNYVDKELGL KFPNDIMVKV NDNYKKLGGI LTELTDDYMI IGIGINVNNQ IRNEIREIAI SLKEITGKEL DKVEILSNFL KTFESYLEKL KNKEIDDYEI LKKYKKYSIT IGKQVKILLS NNEIITGKVY DIDFDGIVLG TEKGIERIPS GICIHVR // ID BPSA_METJA Reviewed; 350 AA. AC Q58669; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=N(4)-bis(aminopropyl)spermidine synthase {ECO:0000255|HAMAP-Rule:MF_01947}; DE EC=2.5.1.128 {ECO:0000255|HAMAP-Rule:MF_01947}; DE AltName: Full=Branched-chain polyamine synthase A {ECO:0000255|HAMAP-Rule:MF_01947}; GN Name=bpsA {ECO:0000255|HAMAP-Rule:MF_01947}; OrderedLocusNames=MJ1273; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the biosynthesis of branched-chain CC polyamines, which support the growth of thermophiles under high- CC temperature conditions. Catalyzes the sequential condensation of CC spermidine with the aminopropyl groups of decarboxylated S- CC adenosylmethionines to produce N(4)-bis(aminopropyl)spermidine via CC N(4)-aminopropylspermidine. {ECO:0000255|HAMAP-Rule:MF_01947}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl 3-(methylthio)propylamine + CC spermidine = 2 S-methyl-5'-thioadenosine + N(4)- CC bis(aminopropyl)spermidine. {ECO:0000255|HAMAP-Rule:MF_01947}. CC -!- PATHWAY: Amine and polyamine biosynthesis. {ECO:0000255|HAMAP- CC Rule:MF_01947}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01947}. CC -!- SIMILARITY: Belongs to the branched-chain polyamine synthase CC family. {ECO:0000255|HAMAP-Rule:MF_01947}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99279.1; -; Genomic_DNA. DR PIR; H64458; H64458. DR ProteinModelPortal; Q58669; -. DR SMR; Q58669; 1-343. DR STRING; 243232.MJ_1273; -. DR EnsemblBacteria; AAB99279; AAB99279; MJ_1273. DR KEGG; mja:MJ_1273; -. DR eggNOG; arCOG00913; Archaea. DR eggNOG; COG1568; LUCA. DR InParanoid; Q58669; -. DR KO; K07057; -. DR OMA; KSYMFRI; -. DR PhylomeDB; Q58669; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:UniProtKB-HAMAP. DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01947; Aminopropyltransf_BpsA; 1. DR InterPro; IPR014435; BpsA. DR InterPro; IPR002723; BpsA_C. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01861; DUF43; 1. DR PIRSF; PIRSF005895; UCP005895_mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Polyamine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 350 N(4)-bis(aminopropyl)spermidine synthase. FT /FTId=PRO_0000107245. SQ SEQUENCE 350 AA; 40420 MW; 2F301BF8976C22BB CRC64; MERILEKVRA KSEIPVYDKS IENVLSAILT TNDFWKIVDL SEEPLPLVAD IIRILEEEGL VKISNGIEFT EKGNEFIKSY GIGAKDNSVC ECCEGRGVSL KNYQDLLERF KEIVKNRPMP KHEYDQGFVT PECTISRIAL MNSRGDLFNK DVLVLGDDDL TSIALMLSNL PKKIVVVDID DRLINFIKEV AEQLNYKNIE VITLDLRKPL PEKYSRAFDT FITDPPETVY AVKTFIGRGI SALKGERRAG YFGITRRESS LDKWREIQRT LINDFNVVIT DIIRNFNHYV NWGYEEETRA WKLAPVKKKP EDIWYKSYMF RIETLKDSRG FEEEVDVGDE LYNDAESSTT // ID BRIX_METJA Reviewed; 169 AA. AC Q58012; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Probable Brix domain-containing ribosomal biogenesis protein {ECO:0000255|HAMAP-Rule:MF_00699}; GN OrderedLocusNames=MJ0594; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably involved in the biogenesis of the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_00699}. CC -!- SIMILARITY: Contains 1 Brix domain. {ECO:0000255|HAMAP- CC Rule:MF_00699}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98595.1; -; Genomic_DNA. DR PIR; B64374; B64374. DR ProteinModelPortal; Q58012; -. DR STRING; 243232.MJ_0594; -. DR EnsemblBacteria; AAB98595; AAB98595; MJ_0594. DR KEGG; mja:MJ_0594; -. DR eggNOG; arCOG03247; Archaea. DR eggNOG; COG2136; LUCA. DR InParanoid; Q58012; -. DR KO; K14561; -. DR OMA; NKILSMN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042254; P:ribosome biogenesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.10480; -; 1. DR HAMAP; MF_00699; BriX; 1. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR007109; Brix. DR InterPro; IPR023548; Brix_dom_Rbsml_bgen_prot. DR SMART; SM00879; Brix; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR PROSITE; PS50833; BRIX; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribosome biogenesis. FT CHAIN 1 169 Probable Brix domain-containing ribosomal FT biogenesis protein. FT /FTId=PRO_0000120270. FT DOMAIN 1 169 Brix. {ECO:0000255|HAMAP-Rule:MF_00699}. SQ SEQUENCE 169 AA; 20053 MW; 9FF6090865C6E4B0 CRC64; MILTTSRKPS QRTRSFARDL ERTLNIPYVQ RGKLSLKEIF EIDKHVLLIG EFKANPGTLV VYDVENEKRL SSFISVKLQR EICGEKIYND DGIRIKISRE LKDNEEFQKY YEIYDEFLFQ HLNINEDSDI TLRLEKDPKY LFAIQFYKGR VKIGPLIRIK SIKLFDSLL // ID BSUHB_METJA Reviewed; 252 AA. AC Q57573; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=Fructose-1,6-bisphosphatase/inositol-1-monophosphatase; DE Short=FBPase/IMPase; DE EC=3.1.3.11 {ECO:0000269|PubMed:9647837}; DE EC=3.1.3.25 {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837}; DE AltName: Full=Inositol-1-phosphatase; DE Short=I-1-Pase; GN Name=suhB; OrderedLocusNames=MJ0109; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS IMPASE, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND ENZYME RP REGULATION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9647837; RA Chen L., Roberts M.F.; RT "Cloning and expression of the inositol monophosphatase gene from RT Methanococcus jannaschii and characterization of the enzyme."; RL Appl. Environ. Microbiol. 64:2609-2615(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS) IN COMPLEX WITH PHOSPHATE AND RP METAL IONS, FUNCTION AS BOTH FBPASE AND IMPASE, CATALYTIC ACTIVITY, RP SUBSTRATE SPECIFICITY, AND KINETIC PARAMETERS. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11062561; DOI=10.1038/80968; RA Stec B., Yang H., Johnson K.A., Chen L., Roberts M.F.; RT "MJ0109 is an enzyme that is both an inositol monophosphatase and the RT 'missing' archaeal fructose-1,6-bisphosphatase."; RL Nat. Struct. Biol. 7:1046-1050(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) IN COMPLEXES WITH MYO-INOSITOL RP PHOSPHATE; MYO-INOSITOL AND METAL IONS. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11170378; DOI=10.1021/bi0016422; RA Johnson K.A., Chen L., Yang H., Roberts M.F., Stec B.; RT "Crystal structure and catalytic mechanism of the MJ0109 gene product: RT a bifunctional enzyme with inositol monophosphatase and fructose 1,6- RT bisphosphatase activities."; RL Biochemistry 40:618-630(2001). CC -!- FUNCTION: Phosphatase with broad specificity; it can CC dephosphorylate fructose 1,6-bisphosphate, both D and L isomers of CC inositol-1-phosphate (I-1-P), 2'-AMP, pNPP, beta-glycerol CC phosphate, and alpha-D-glucose-1-phosphate. Cannot hydrolyze CC glucose-6-phosphate, fructose-6-phosphate, NAD(+) or 5'-AMP. May CC be involved in the biosynthesis of a unique osmolyte, di-myo- CC inositol 1,1-phosphate. {ECO:0000269|PubMed:11062561, CC ECO:0000269|PubMed:9647837}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate + H(2)O = D- CC fructose 6-phosphate + phosphate. {ECO:0000269|PubMed:11062561}. CC -!- CATALYTIC ACTIVITY: Myo-inositol phosphate + H(2)O = myo-inositol CC + phosphate. {ECO:0000269|PubMed:11062561, CC ECO:0000269|PubMed:9647837}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:9647837}; CC -!- ENZYME REGULATION: IMPase activity is inhibited by Ca(2+) and CC Zn(2+). In contrast to mammalian I-1-P phosphatases, is not CC inhibited by Li(+) up to 100 mM. {ECO:0000269|PubMed:9647837}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.091 mM for inositol-1-phosphate (at 85 degrees Celsius) CC {ECO:0000269|PubMed:11062561, ECO:0000269|PubMed:9647837}; CC KM=0.038 mM for D-fructose 1,6-bisphosphate (at 85 degrees CC Celsius) {ECO:0000269|PubMed:11062561, CC ECO:0000269|PubMed:9647837}; CC Vmax=9.3 umol/min/mg enzyme for IMPase activity (at 85 degrees CC Celsius) {ECO:0000269|PubMed:11062561, CC ECO:0000269|PubMed:9647837}; CC Note=kcat is 4.2 sec(-1) for IMPase activity (at 85 degrees CC Celsius) and 7.0 sec(-1) for FBPase activity (at 85 degrees CC Celsius).; CC Temperature dependence: CC Is thermostable. After incubation at 85 degrees Celsius for 30 CC minutes, more than 95% of I-1-Pase activity remains. CC {ECO:0000269|PubMed:9647837}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11062561, CC ECO:0000269|PubMed:9647837}. CC -!- SIMILARITY: Belongs to the inositol monophosphatase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98091.1; -; Genomic_DNA. DR PIR; E64313; E64313. DR PDB; 1DK4; X-ray; 2.60 A; A/B=1-252. DR PDB; 1G0H; X-ray; 2.30 A; A/B=1-252. DR PDB; 1G0I; X-ray; 2.40 A; A/B=1-252. DR PDBsum; 1DK4; -. DR PDBsum; 1G0H; -. DR PDBsum; 1G0I; -. DR ProteinModelPortal; Q57573; -. DR SMR; Q57573; 1-252. DR STRING; 243232.MJ_0109; -. DR EnsemblBacteria; AAB98091; AAB98091; MJ_0109. DR KEGG; mja:MJ_0109; -. DR eggNOG; arCOG01349; Archaea. DR eggNOG; COG0483; LUCA. DR InParanoid; Q57573; -. DR KO; K01092; -. DR OMA; SALELCY; -. DR PhylomeDB; Q57573; -. DR BioCyc; MetaCyc:MONOMER-5062; -. DR BRENDA; 3.1.3.25; 3260. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; Q57573; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0042132; F:fructose 1,6-bisphosphate 1-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0008934; F:inositol monophosphate 1-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052832; F:inositol monophosphate 3-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0052833; F:inositol monophosphate 4-phosphatase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR020550; Inositol_monophosphatase_CS. DR PANTHER; PTHR20854; PTHR20854; 1. DR Pfam; PF00459; Inositol_P; 1. DR PRINTS; PR00377; IMPHPHTASES. DR PROSITE; PS00629; IMP_1; 1. DR PROSITE; PS00630; IMP_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; KW Gluconeogenesis; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 252 Fructose-1,6-bisphosphatase/inositol-1- FT monophosphatase. FT /FTId=PRO_0000142580. FT REGION 84 86 Substrate binding. FT METAL 65 65 Magnesium 1. FT METAL 81 81 Magnesium 1. FT METAL 81 81 Magnesium 2. FT METAL 83 83 Magnesium 1; via carbonyl oxygen. FT METAL 84 84 Magnesium 2. FT METAL 201 201 Magnesium 2. FT BINDING 170 170 Substrate. FT BINDING 175 175 Substrate; via amide nitrogen. FT BINDING 194 194 Substrate. FT HELIX 3 18 {ECO:0000244|PDB:1G0H}. FT HELIX 19 21 {ECO:0000244|PDB:1G0H}. FT TURN 25 27 {ECO:0000244|PDB:1G0H}. FT STRAND 30 34 {ECO:0000244|PDB:1G0H}. FT TURN 35 37 {ECO:0000244|PDB:1G0H}. FT STRAND 38 41 {ECO:0000244|PDB:1G0H}. FT HELIX 42 55 {ECO:0000244|PDB:1G0H}. FT HELIX 56 58 {ECO:0000244|PDB:1G0H}. FT STRAND 60 64 {ECO:0000244|PDB:1G0H}. FT HELIX 65 67 {ECO:0000244|PDB:1G0H}. FT STRAND 68 70 {ECO:0000244|PDB:1G0H}. FT STRAND 75 84 {ECO:0000244|PDB:1G0H}. FT HELIX 86 90 {ECO:0000244|PDB:1G0H}. FT STRAND 97 115 {ECO:0000244|PDB:1G0H}. FT HELIX 116 118 {ECO:0000244|PDB:1G0H}. FT STRAND 120 125 {ECO:0000244|PDB:1G0H}. FT TURN 126 128 {ECO:0000244|PDB:1G0H}. FT STRAND 129 132 {ECO:0000244|PDB:1G0I}. FT HELIX 144 146 {ECO:0000244|PDB:1G0I}. FT STRAND 148 152 {ECO:0000244|PDB:1G0H}. FT STRAND 155 157 {ECO:0000244|PDB:1DK4}. FT HELIX 159 165 {ECO:0000244|PDB:1G0H}. FT STRAND 167 169 {ECO:0000244|PDB:1G0H}. FT HELIX 175 183 {ECO:0000244|PDB:1G0H}. FT STRAND 188 192 {ECO:0000244|PDB:1G0H}. FT HELIX 199 210 {ECO:0000244|PDB:1G0H}. FT TURN 211 213 {ECO:0000244|PDB:1G0H}. FT STRAND 215 217 {ECO:0000244|PDB:1G0H}. FT STRAND 219 223 {ECO:0000244|PDB:1G0H}. FT STRAND 237 241 {ECO:0000244|PDB:1G0H}. FT HELIX 242 249 {ECO:0000244|PDB:1G0H}. SQ SEQUENCE 252 AA; 28578 MW; 3ED5B4401075EE6E CRC64; MKWDEIGKNI AKEIEKEILP YFGRKDKSYV VGTSPSGDET EIFDKISEDI ALKYLKSLNV NIVSEELGVI DNSSEWTVVI DPIDGSFNFI NGIPFFAFCF GVFKNNEPYY GLTYEFLTKS FYEAYKGKGA YLNGRKIKVK DFNPNNIVIS YYPSKKIDLE KLRNKVKRVR IFGAFGLEMC YVAKGTLDAV FDVRPKVRAV DIASSYIICK EAGALITDEN GDELKFDLNA TDRLNIIVAN SKEMLDIILD LL // ID BIOA_METJA Reviewed; 461 AA. AC Q58696; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 22-SEP-2009, sequence version 2. DT 17-FEB-2016, entry version 105. DE RecName: Full=Adenosylmethionine-8-amino-7-oxononanoate aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE EC=2.6.1.62 {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diamino-pelargonic acid aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DAPA AT {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DAPA aminotransferase {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=7,8-diaminononanoate synthase {ECO:0000255|HAMAP-Rule:MF_00834}; DE Short=DANS {ECO:0000255|HAMAP-Rule:MF_00834}; DE AltName: Full=Diaminopelargonic acid synthase {ECO:0000255|HAMAP-Rule:MF_00834}; GN Name=bioA {ECO:0000255|HAMAP-Rule:MF_00834}; OrderedLocusNames=MJ1300; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transfer of the alpha-amino group from S- CC adenosyl-L-methionine (SAM) to 7-keto-8-aminopelargonic acid CC (KAPA) to form 7,8-diaminopelargonic acid (DAPA). It is the only CC animotransferase known to utilize SAM as an amino donor. CC {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 8-amino-7- CC oxononanoate = S-adenosyl-4-methylthio-2-oxobutanoate + 7,8- CC diaminononanoate. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00834}; CC -!- PATHWAY: Cofactor biosynthesis; biotin biosynthesis; 7,8- CC diaminononanoate from 8-amino-7-oxononanoate (SAM route): step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00834}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. BioA subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00834}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99307.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99307.1; ALT_INIT; Genomic_DNA. DR PIR; C64462; C64462. DR ProteinModelPortal; Q58696; -. DR STRING; 243232.MJ_1300; -. DR EnsemblBacteria; AAB99307; AAB99307; MJ_1300. DR KEGG; mja:MJ_1300; -. DR eggNOG; arCOG00917; Archaea. DR eggNOG; COG0161; LUCA. DR InParanoid; Q58696; -. DR KO; K00833; -. DR PhylomeDB; Q58696; -. DR UniPathway; UPA00078; UER00160. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00834; BioA; 1. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR005815; BioA. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00508; bioA; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Aminotransferase; Biotin biosynthesis; Complete proteome; Cytoplasm; KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 461 Adenosylmethionine-8-amino-7-oxononanoate FT aminotransferase. FT /FTId=PRO_0000120377. FT REGION 117 118 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT BINDING 150 150 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 263 263 Pyridoxal phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 296 296 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT BINDING 331 331 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT BINDING 426 426 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00834}. FT SITE 20 20 Participates in the substrate recognition FT with KAPA and in a stacking interaction FT with the adenine ring of SAM. FT {ECO:0000255|HAMAP-Rule:MF_00834}. FT MOD_RES 296 296 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_00834}. SQ SEQUENCE 461 AA; 52314 MW; 8CF29B3FCBC280FC CRC64; MNIDKNLLEK WDKEYIWHPY TQMKEYRESK NLIIERGEGN YLIDIYGNKY LDAVSSIWCN LFGHSRKEII EAIKNQADKI CHSTLLGCGN VPSILLAKKL VDITPKHLTK VFYSEDGAEA VEIAIKMAYQ YYVLRGDKGR TKFISVKEGY HGDTVGAMSV GGSELFHGVF KPLLFKGYHA NPPYCYRCKY HNFKDTDERN EKGCEMECLN EMISLIEKHA EEVFCVILEG GIMGSAGMIP YPDGYIEGVA KACKENDVIF ILDEVATGFG RTGKMFFCDN EELKKLEKPD ILCLGKGLTG GYLPLAATLT TDEIYNQFLG EFGESKQLYH GHTYTGNQLL CSAALATLEI FEKENVIENI QPKIKLFHKE LRKLKELEHV GDVRGRGFMV GIELVKDKET KEPYPYGYKA GYRVAEKLLE KGIYMRPIGN VIILVPPLSI TEKEIIYLCD ALYEAIKEAD L // ID CARB2_METJA Reviewed; 618 AA. AC Q58776; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=Carbamoyl-phosphate synthase large chain, C-terminal section; DE EC=6.3.5.5; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain; GN Name=carB2; OrderedLocusNames=MJ1381; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000250}. CC -!- DOMAIN: Corresponds to the C-terminal section. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC -!- CAUTION: CarB is split into two genes in M.jannaschii (MJ1378 and CC MJ1381). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99391.1; -; Genomic_DNA. DR PIR; D64472; D64472. DR ProteinModelPortal; Q58776; -. DR STRING; 243232.MJ_1381; -. DR EnsemblBacteria; AAB99391; AAB99391; MJ_1381. DR KEGG; mja:MJ_1381; -. DR eggNOG; arCOG01594; Archaea. DR eggNOG; COG0458; LUCA. DR InParanoid; Q58776; -. DR KO; K01955; -. DR OMA; CVQAVFA; -. DR PhylomeDB; Q58776; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.1380; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR011607; MGS-like_dom. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF02786; CPSase_L_D2; 1. DR Pfam; PF02787; CPSase_L_D3; 1. DR Pfam; PF02142; MGS; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SMART; SM00851; MGS; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52335; SSF52335; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 618 Carbamoyl-phosphate synthase large chain, FT C-terminal section. FT /FTId=PRO_0000145076. FT DOMAIN 208 399 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 234 291 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT REGION 81 477 Carbamoyl phosphate synthetic domain. FT REGION 478 618 Allosteric domain. FT METAL 358 358 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 370 370 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 370 370 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 372 372 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. SQ SEQUENCE 618 AA; 68453 MW; 8C3D4D9C192A954E CRC64; MDMEKLKEIL LKAKKLGFSD KQIANLLGMD EIEVRDLRKK LNIIPLYKMV DTCAAEFEAK TPYYYSAYET FVYKEQDESN PSDRKKVIII GSGPIRIGQG IEFDYSSVHA VLALKEMGIE AIIINNNPET VSTDYDTSDK LYFEPITFEE VLNIAEREKE KGELLGVIVQ FGGQTAINLA MKLKNAGVNI LGTTPENINA AEDREEFSKL LKKLNIPQAE GGTAYTKEEA LEIAKRIGYP VLVRPSYVLG GRAMQIVYSE DELIEYMEEA VKVSEEHPVL IDKFLEDAIE LDVDAVCDGE SVLIGAIMEH IEEAGVHSGD SATVIPPQTL PKEIIDTVID YTAKLARALN IVGLLNVQYA VKDGVVYVLE ANPRASRTVP YVSKSVGIPL AKLATKIMLG KKLEELIKDY DVEKVAEKVW IAKPKYVSIK EAVFPFQKLP GVDPVLGPEM KSTGEAIGID KDFGRAYYKA QLSANMELPI VGNVFISVRD RDKKHIVDVA KKLHELGFTI YATEGTAKVL RENGIPAILV KKISESPNDN ILKLMRDGKM HLIINTSSGK KAKSDGYYIR RAAVDLGIPY ITTIPGAKAA VKAIEAVKTG ELSVYSLDEL DARIKNRF // ID CAS2_METJA Reviewed; 114 AA. AC Q57831; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=CRISPR-associated endoribonuclease Cas2; DE EC=3.1.-.-; GN Name=cas2; OrderedLocusNames=MJ0386; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Functions as a ssRNA-specific CC endoribonuclease. Involved in the integration of spacer DNA into CC the CRISPR cassette (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas1 homodimer. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated endoribonuclease Cas2 CC protein family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98372.1; -; Genomic_DNA. DR PIR; B64348; B64348. DR ProteinModelPortal; Q57831; -. DR SMR; Q57831; 28-113. DR STRING; 243232.MJ_0386; -. DR EnsemblBacteria; AAB98372; AAB98372; MJ_0386. DR KEGG; mja:MJ_0386; -. DR eggNOG; arCOG04194; Archaea. DR eggNOG; COG1343; LUCA. DR InParanoid; Q57831; -. DR KO; K09951; -. DR OMA; MRVINTE; -. DR PhylomeDB; Q57831; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004521; F:endoribonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-HAMAP. DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.240; -; 1. DR HAMAP; MF_01471; Cas2; 1. DR InterPro; IPR021127; CRISPR_associated_Cas2. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR019199; Virulence_VapD/CRISPR_Cas2. DR Pfam; PF09827; CRISPR_Cas2; 1. DR TIGRFAMs; TIGR01573; cas2; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Endonuclease; Hydrolase; KW Magnesium; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 114 CRISPR-associated endoribonuclease Cas2. FT /FTId=PRO_0000106849. FT COMPBIAS 3 17 Lys-rich. FT METAL 35 35 Magnesium; catalytic. {ECO:0000255}. SQ SEQUENCE 114 AA; 13655 MW; 2F817459771C9306 CRC64; MLKKEWDYVN KILKKIKNIR NLLQDESMYV IIVYDVNVSR VNKIKSFLRK HLNWVQNSVF EGEVTKAEFE RIKDGILRII DEDEDSVIIY QFPLNFMPKR EILGLEKNPI DDII // ID CAS3_METJA Reviewed; 728 AA. AC Q57821; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 90. DE RecName: Full=Putative CRISPR-associated nuclease/helicase Cas3; DE EC=3.1.-.-; DE EC=3.6.4.-; GN Name=cas3; OrderedLocusNames=MJ0376; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate CC in CRISPR interference, the third stage of CRISPR immunity (By CC similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: In the N-terminal section; belongs to the CRISPR- CC associated nuclease Cas3-HD family. {ECO:0000305}. CC -!- SIMILARITY: In the central section; belongs to the CRISPR- CC associated helicase Cas3 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HD Cas3-type domain. {ECO:0000255|PROSITE- CC ProRule:PRU00974}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC -!- CAUTION: This protein is about 60 residues too short at the N- CC terminus compared to its close orthologs. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98365.1; -; Genomic_DNA. DR PIR; H64346; H64346. DR ProteinModelPortal; Q57821; -. DR STRING; 243232.MJ_0376; -. DR EnsemblBacteria; AAB98365; AAB98365; MJ_0376. DR KEGG; mja:MJ_0376; -. DR eggNOG; arCOG01445; Archaea. DR eggNOG; COG1203; LUCA. DR InParanoid; Q57821; -. DR KO; K07012; -. DR OMA; PTQVTSN; -. DR PhylomeDB; Q57821; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR01587; cas3_core; 1. DR PROSITE; PS51643; HD_CAS3; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Nucleotide-binding; Reference proteome. FT CHAIN 1 728 Putative CRISPR-associated FT nuclease/helicase Cas3. FT /FTId=PRO_0000106839. FT DOMAIN 1 163 HD Cas3-type. {ECO:0000255|PROSITE- FT ProRule:PRU00974}. FT DOMAIN 213 404 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 434 592 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT MOTIF 352 355 DEAH box. FT METAL 3 3 Magnesium. {ECO:0000255}. FT METAL 55 55 Magnesium. {ECO:0000255}. SQ SEQUENCE 728 AA; 86467 MW; 8BC3DBCA30226B40 CRC64; MHDIGKITEG FQNNIKKGKR SNKHPHPLYA LPIIKNIEFD YLFDIPIEVF AILSHHTQLY NNLYADYQQY KKGTFLIEEI KEFIKNSKEA YESLGFSKFF EFEDLKIEDI PKDAKPLELH RLRRKYWIEA NNYIKSLSFD DKIKIKSIFS FMFSILQLCD DFASLNFSEY AKDREGIFDD VLENPEIYVP TLNIDNPISF ILKDYEPYKF QKELYNSKNK FVMLFAPCGR GKTEGALLWA LNALKNFKRN KIILAMPTQV TSNAMYDRLV KIFGEENVGL FHGKSFIKLR DSKEIEDEDD LEEIRDENFK GNVFFKPITI TTIDHVIYSF VHGFSQADFA LGNIQNSVII FDEVHYYEKY TLEHLLTLFD ILRRMDIPHL LMSGTLPNFL MNNLEGYELV VDEEGLNYKP FKLKCSENHL IWKEDDEWKV NENIINEIIE NYKKGLSQAI ILNTVERARE FYKAVRDKVP AILYHSQFAY KDRVKKEDEI FTLEEMRKSQ NKPYVIVATQ VIEISLDMSV DVMYSELSPP DALGQRAGRL HRKGKDWREN GKEYKLKIFL PYKHLPYSKE LIEKTINHIK FYEKPLDYRD IKDFVDNVYK DYNLSIPSDL KLFFDEAILF GRHWTDISTI DEEGRFFKVR DDKFMKIEVV PQVYFDELGE NSLRAEYMAK IPAYLILNEM KNEEGLIHFY PYEKRVGRKT RRYLICSFKY TYEIGFDYKE EEEFEDIL // ID CAS7_METJA Reviewed; 320 AA. AC Q57826; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 78. DE RecName: Full=CRISPR-associated protein Cas7/Cst2/DevR; DE AltName: Full=CRISPR-associated protein Cas7/Csa2, subtype I-A/Apern; GN Name=cas7; OrderedLocusNames=MJ0381; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein CC Cas7/Cst2/DevR family. Subtype I-a/Apern subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98370.1; -; Genomic_DNA. DR PIR; E64347; E64347. DR ProteinModelPortal; Q57826; -. DR STRING; 243232.MJ_0381; -. DR EnsemblBacteria; AAB98370; AAB98370; MJ_0381. DR KEGG; mja:MJ_0381; -. DR eggNOG; arCOG03617; Archaea. DR eggNOG; COG1857; LUCA. DR InParanoid; Q57826; -. DR KO; K19075; -. DR OMA; CNDLHGF; -. DR PhylomeDB; Q57826; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR002764; Cas7/Cst2/DevR_sub_I-a/Apern. DR InterPro; IPR010154; CRISPR-assoc_Cas7/Cst2/DevR. DR Pfam; PF01905; DevR; 1. DR TIGRFAMs; TIGR01875; cas_MJ0381; 1. DR TIGRFAMs; TIGR02583; DevR_archaea; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 320 CRISPR-associated protein Cas7/Cst2/DevR. FT /FTId=PRO_0000106844. SQ SEQUENCE 320 AA; 35924 MW; 81CA8DE178F4B223 CRC64; MFLRISGRVR LNSHSLNAQG GGGTNYVEIT KAKVSIKNDD RWEILEVPAI SGNMVKHWHF VSFVDFFRET DYKDNLTERA LRYNGARFGQ ETKAKKADGS EVELKDESEI IKNFADADVH GFLAPKTGVR RVSLVKTSFI LPTEDFIKEV DERLVYAVKH NRVDIDEKGA IKSGEEQTAQ MLFNREYATG LYGFEIILDL GFVGVPQSSP SNPVIEDDER KARIVSALKA LIPMLSGYIG ANLARSFPVF KLEEMIAVVS EKPIPALVHG FYEDYVEVSK NVVENAKKLG FEIEDFGYNV DFGESVSSVE ELISKIIEKL // ID CBIF_METJA Reviewed; 259 AA. AC Q58973; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Cobalt-precorrin-4 C(11)-methyltransferase; DE EC=2.1.1.271; DE AltName: Full=Cobalt-precorrin-3 methylase; GN Name=cbiF; OrderedLocusNames=MJ1578; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the methylation of C-11 in cobalt-precorrin-4 CC to form cobalt-precorrin-5A. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cobalt-precorrin-4 = CC S-adenosyl-L-homocysteine + cobalt-precorrin-5A. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 4/10. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99599.1; -; Genomic_DNA. DR PIR; A64497; A64497. DR ProteinModelPortal; Q58973; -. DR SMR; Q58973; 5-235. DR STRING; 243232.MJ_1578; -. DR EnsemblBacteria; AAB99599; AAB99599; MJ_1578. DR KEGG; mja:MJ_1578; -. DR eggNOG; arCOG00645; Archaea. DR eggNOG; COG2875; LUCA. DR InParanoid; Q58973; -. DR KO; K05936; -. DR OMA; MAIHLGV; -. DR PhylomeDB; Q58973; -. DR UniPathway; UPA00148; UER00226. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro. DR GO; GO:0046026; F:precorrin-4 C11-methyltransferase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR006362; Cbl_synth_CobM/CibF. DR InterPro; IPR006366; CobA/CysG_C. DR InterPro; IPR003043; Uropor_MeTrfase_CS. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1. DR TIGRFAMs; TIGR01465; cobM_cbiF; 1. DR PROSITE; PS00839; SUMT_1; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 259 Cobalt-precorrin-4 C(11)- FT methyltransferase. FT /FTId=PRO_0000150399. SQ SEQUENCE 259 AA; 29004 MW; C5DB9E3C78143521 CRC64; MDNNRKVIIV GAGPGDPELI TIKGKKAIEE ADVIIYAGSL VNEKLLEYNK KNAEIYNSAN MNLEEIIDVM VKAVNQGKKV VRLHTGDPSI YGAIKEQIDE LSKYGIDVEI IPGVSSLFAA TASLKVELTL PEVSQTVIIT RPEGRTPMPE KEKLRDLAKH QSTMAIFLGV SMIDKVVKEL IEGGYREETP VAVVYHASWD DEKIVRGTLK DIAEKVKKEG IKKTALIIVG EVLNPKYYAY SKLYDKNFEH EYRKSHKKF // ID CBID_METJA Reviewed; 362 AA. AC Q60342; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Cobalt-precorrin-5B C(1)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00787}; DE EC=2.1.1.195 {ECO:0000255|HAMAP-Rule:MF_00787}; DE AltName: Full=Cobalt-precorrin-6A synthase {ECO:0000255|HAMAP-Rule:MF_00787}; GN Name=cbiD {ECO:0000255|HAMAP-Rule:MF_00787}; OrderedLocusNames=MJ0022; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the methylation of C-1 in cobalt-precorrin-5B CC to form cobalt-precorrin-6A. {ECO:0000255|HAMAP-Rule:MF_00787}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-5B + S-adenosyl-L-methionine CC = cobalt-precorrin-6A + S-adenosyl-L-homocysteine. CC {ECO:0000255|HAMAP-Rule:MF_00787}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 6/10. {ECO:0000255|HAMAP-Rule:MF_00787}. CC -!- SIMILARITY: Belongs to the CbiD family. {ECO:0000255|HAMAP- CC Rule:MF_00787}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98004.1; -; Genomic_DNA. DR PIR; F64302; F64302. DR ProteinModelPortal; Q60342; -. DR STRING; 243232.MJ_0022; -. DR EnsemblBacteria; AAB98004; AAB98004; MJ_0022. DR KEGG; mja:MJ_0022; -. DR eggNOG; arCOG04383; Archaea. DR eggNOG; COG1903; LUCA. DR InParanoid; Q60342; -. DR KO; K02188; -. DR OMA; MMVHSKS; -. DR PhylomeDB; Q60342; -. DR UniPathway; UPA00148; UER00227. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00787; CbiD; 1. DR InterPro; IPR002748; CbiD. DR Pfam; PF01888; CbiD; 1. DR PIRSF; PIRSF026782; CbiD; 1. DR SUPFAM; SSF111342; SSF111342; 1. DR TIGRFAMs; TIGR00312; cbiD; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 362 Cobalt-precorrin-5B C(1)- FT methyltransferase. FT /FTId=PRO_0000141692. SQ SEQUENCE 362 AA; 39951 MW; 6AA2947C871906B7 CRC64; MIYDFRKKSK FGYTTGSCAA AGAYSALYYL KFGKKLSYVE IENLNGDKLI IPIEKIEKCG NKAKAVVIKD AGGDIDITNG IEIITEVELK KGKKDVIIKG GEGVGIVTKN GLQVKKGEPA INPKPREMIR NNLLKLLNDD EVVEVTISIP KGKELAKKTL NPKLGIVGGL SILGTTGIVR PMSNEAYMNS LAPQIDVALA NGYKRLIFVP GNIGTKYAKQ LLNANDDEII EVSNFWGFML DKAKEKGVEE ILIFGHAGKI IKLAGGIYNT HSKVADCRNE ILAAYSSLFI DDKEAIKKIL YSNTTEEVIK ILEEKGVLND VFNFIAKRVV ERLSERWKGI KFSCIIINMK GEVLGSYIWN KK // ID CBIH_METJA Reviewed; 249 AA. AC Q58223; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Probable cobalt-factor III C(17)-methyltransferase; DE EC=2.1.1.-; DE AltName: Full=Cobalt-precorrin-3 methyltransferase; DE Short=Cobalt-precorrin-3 methylase; GN Name=cbiH; Synonyms=cobJ; OrderedLocusNames=MJ0813; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Methyltransferase that likely catalyzes the ring CC contraction and methylation of C-17 in cobalt-factor III to form CC cobalt-factor IV. May also convert cobalt-precorrin-3 to cobalt- CC precorrin-4 (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cobalt-factor III = CC S-adenosyl-L-homocysteine + cobalt-factor IV. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 3/10. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98812.1; -; Genomic_DNA. DR PIR; E64401; E64401. DR ProteinModelPortal; Q58223; -. DR STRING; 243232.MJ_0813; -. DR EnsemblBacteria; AAB98812; AAB98812; MJ_0813. DR KEGG; mja:MJ_0813; -. DR eggNOG; arCOG00647; Archaea. DR eggNOG; COG1010; LUCA. DR InParanoid; Q58223; -. DR KO; K05934; -. DR OMA; GAPLNHD; -. DR PhylomeDB; Q58223; -. DR UniPathway; UPA00148; UER00225. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008898; F:S-adenosylmethionine-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR006363; Cbl_synth_CobJ/CibH_dom. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01466; cobJ_cbiH; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 249 Probable cobalt-factor III C(17)- FT methyltransferase. FT /FTId=PRO_0000150403. SQ SEQUENCE 249 AA; 28131 MW; EE25D9F73D0C0911 CRC64; MLYVVGIGSG NERHFTKEAE EILNKVDLIV CYKNYKKFVE RLNKPIYTTG MTREIDRVDY ALKEAKDKDV ALVSSGDATI YGLASLAYEI NAVKGYNVDI KVVPGITACS LASAILGSPL NHDFVVISFS DLLTPLETIL KRFRCALEGD FVICIYNPLS KRRKEPFLKA MEILAEFAKD KDYIIGIVKN AGRNKEEVVI TNFKDLYKNL EKYLEFIDMN TILIIGNSST KIINGKMITP RGYLDKYKI // ID CBIX_METJA Reviewed; 143 AA. AC Q58380; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Sirohydrochlorin cobaltochelatase {ECO:0000255|HAMAP-Rule:MF_00785}; DE EC=4.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00785}; DE AltName: Full=CbiXS {ECO:0000255|HAMAP-Rule:MF_00785}; GN Name=cbiX {ECO:0000255|HAMAP-Rule:MF_00785}; OrderedLocusNames=MJ0970; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the insertion of Co(2+) into sirohydrochlorin CC as part of the anaerobic pathway to cobalamin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00785}. CC -!- CATALYTIC ACTIVITY: Cobalt-sirohydrochlorin + 2 H(+) = CC sirohydrochlorin + Co(2+). {ECO:0000255|HAMAP-Rule:MF_00785}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 1/10. {ECO:0000255|HAMAP-Rule:MF_00785}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP- CC Rule:MF_00785}. CC -!- SIMILARITY: Belongs to the CbiX family. CbiXS subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00785}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98975.1; -; Genomic_DNA. DR PIR; B64421; B64421. DR ProteinModelPortal; Q58380; -. DR STRING; 243232.MJ_0970; -. DR EnsemblBacteria; AAB98975; AAB98975; MJ_0970. DR KEGG; mja:MJ_0970; -. DR eggNOG; arCOG02246; Archaea. DR eggNOG; COG2138; LUCA. DR InParanoid; Q58380; -. DR KO; K03795; -. DR OMA; VRAGFME; -. DR PhylomeDB; Q58380; -. DR UniPathway; UPA00148; UER00223. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050897; F:cobalt ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016852; F:sirohydrochlorin cobaltochelatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019251; P:anaerobic cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00785; CbiX; 1. DR InterPro; IPR002762; Cbl_biosynth_CbiX. DR InterPro; IPR023652; SiroHydchlorin_Cochelatase. DR Pfam; PF01903; CbiX; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Cobalt; Complete proteome; Lyase; KW Metal-binding; Reference proteome. FT CHAIN 1 143 Sirohydrochlorin cobaltochelatase. FT /FTId=PRO_0000150356. FT REGION 70 75 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00785}. FT COMPBIAS 93 109 Poly-His. FT ACT_SITE 9 9 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00785}. FT METAL 9 9 Cobalt. {ECO:0000255|HAMAP- FT Rule:MF_00785}. FT METAL 75 75 Cobalt. {ECO:0000255|HAMAP- FT Rule:MF_00785}. FT BINDING 45 45 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00785}. SQ SEQUENCE 143 AA; 16519 MW; 3B2947A443F25098 CRC64; MEALVLVGHG SRLPYSKELL VKLAEKVKER NLFPIVEIGL MEFSEPTIPQ AVKKAIEQGA KRIIVVPVFL AHGIHTTRDI PRLLGLIEDN HEHHHEHSHH HHHHHHHEHE KLEIPEDVEI IYREPIGADD RIVDIIIDRA FGR // ID CCA_METJA Reviewed; 449 AA. AC Q58511; Q58512; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 95. DE RecName: Full=CCA-adding enzyme; DE EC=2.7.7.72; DE AltName: Full=CCA tRNA nucleotidyltransferase; DE AltName: Full=tRNA CCA-pyrophosphorylase; DE AltName: Full=tRNA adenylyl-/cytidylyl- transferase; DE AltName: Full=tRNA nucleotidyltransferase; DE AltName: Full=tRNA-NT; GN Name=cca; OrderedLocusNames=MJ1111; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP FUNCTION, KINETIC PARAMETERS, 3D-STRUCTURE MODELING, AND MUTAGENESIS RP OF ARG-164; LYS-167 AND LYS-171. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12866049; DOI=10.1002/prot.10374; RA Bujnicki J.M., Albert M.A., Nelson D.J., Thurlow D.L.; RT "Fold recognition, homology modeling, docking simulations, kinetics RT analysis and mutagenesis of ATP/CTP:tRNA nucleotidyltransferase from RT Methanococcus jannaschii."; RL Proteins 52:349-359(2003). CC -!- FUNCTION: Catalyzes the addition and repair of the essential 3'- CC terminal CCA sequence in tRNAs without using a nucleic acid CC template. Adds these three nucleotides in the order of C, C, and A CC to the tRNA nucleotide-73, using CTP and ATP as substrates and CC producing inorganic pyrophosphate. {ECO:0000269|PubMed:12866049}. CC -!- CATALYTIC ACTIVITY: A tRNA precursor + 2 CTP + ATP = a tRNA with a CC 3' CCA end + 3 diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=21 uM for ATP {ECO:0000269|PubMed:12866049}; CC KM=38 uM for CTP {ECO:0000269|PubMed:12866049}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- MISCELLANEOUS: A single active site specifically recognizes both CC ATP and CTP and is responsible for their addition. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the tRNA nucleotidyltransferase/poly(A) CC polymerase family. Archaeal CCA-adding enzyme subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99114.1; -; Genomic_DNA. DR ProteinModelPortal; Q58511; -. DR STRING; 243232.MJ_1111; -. DR EnsemblBacteria; AAB99114; AAB99114; MJ_1111. DR KEGG; mja:MJ_1111; -. DR eggNOG; arCOG04249; Archaea. DR eggNOG; COG1746; LUCA. DR InParanoid; Q58511; -. DR KO; K07558; -. DR OMA; DRTPFHN; -. DR PhylomeDB; Q58511; -. DR SABIO-RK; Q58511; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0052929; F:ATP:3'-cytidine-cytidine-tRNA adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052928; F:CTP:3'-cytidine-tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0052927; F:CTP:tRNA cytidylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016437; F:tRNA cytidylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042245; P:RNA repair; IEA:UniProtKB-KW. DR GO; GO:0001680; P:tRNA 3'-terminal CCA addition; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01264; CCA_arch; 1. DR InterPro; IPR008229; CCA-adding_arc. DR InterPro; IPR011068; NuclTrfase_I_C. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR InterPro; IPR015329; tRNA_NucTransf2. DR Pfam; PF01909; NTP_transf_2; 1. DR Pfam; PF09249; tRNA_NucTransf2; 1. DR PIRSF; PIRSF005335; CCA_arch; 1. DR SUPFAM; SSF55003; SSF55003; 1. DR TIGRFAMs; TIGR03671; cca_archaeal; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Magnesium; Metal-binding; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW RNA repair; RNA-binding; Transferase; tRNA processing. FT CHAIN 1 449 CCA-adding enzyme. FT /FTId=PRO_0000139069. FT METAL 69 69 Magnesium. {ECO:0000250}. FT METAL 71 71 Magnesium. {ECO:0000250}. FT METAL 124 124 Magnesium. {ECO:0000250}. FT BINDING 57 57 ATP or CTP. {ECO:0000250}. FT BINDING 60 60 ATP or CTP. {ECO:0000250}. FT BINDING 147 147 ATP or CTP. {ECO:0000250}. FT BINDING 167 167 ATP or CTP. {ECO:0000250}. FT BINDING 176 176 ATP or CTP. {ECO:0000250}. FT MUTAGEN 164 164 R->A: Loss of both AMP and CMP FT incorporation. FT {ECO:0000269|PubMed:12866049}. FT MUTAGEN 167 167 K->A: Loss of AMP incorporation and high FT decrease in CMP incorporation. FT {ECO:0000269|PubMed:12866049}. FT MUTAGEN 171 171 K->A: No decrease in both AMP and CMP FT incorporation. FT {ECO:0000269|PubMed:12866049}. SQ SEQUENCE 449 AA; 52784 MW; F9BFACC8157AE994 CRC64; MIVLTIEEIL KEVLNEIKPS KEDMEKLQLK ANEIIDKIWE IVRENSYPIL EVLLVGSSAR NTNLKDDYDI DIFVLFDKSV SEDELEEIGL KIGTEAIKRL NGSYNINYAS HPYVNGEVDG YEVDIVPCYK IDFGEKIISA VDRTPLHHKF LISRLNERLC DEVRLLKAFL KSLGLYGSDV KTKGFSGYLC ELLILHYGSF INLLKEAQNW RIGKKIILKD IFEIYKDVDI NKLKKFDEPF IVYDPVDLNR NVASPLSKDN FCRFIFYSRQ FLKNPSIEFF KDYAKKLEEI LENREHGYRL ILKIPRENVV DDIIYPQMEK LQKSINKVIV KNEFVILNSK CFADDNYCYL YWEFLVYELP KIALREGPPV FEKERAERFL KKYGKVFIRD CKLFAYTERE YSHIIDLFKD IVNGNLQNIS IPKYVNPRNG KIIELNSHGE HKQFNKECQ // ID CARA_METJA Reviewed; 354 AA. AC Q58425; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 112. DE RecName: Full=Carbamoyl-phosphate synthase small chain; DE EC=6.3.5.5; DE AltName: Full=Carbamoyl-phosphate synthetase glutamine chain; GN Name=carA; OrderedLocusNames=MJ1019; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CarA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99021.1; -; Genomic_DNA. DR ProteinModelPortal; Q58425; -. DR STRING; 243232.MJ_1019; -. DR MEROPS; C26.A33; -. DR EnsemblBacteria; AAB99021; AAB99021; MJ_1019. DR KEGG; mja:MJ_1019; -. DR eggNOG; arCOG00064; Archaea. DR eggNOG; COG0505; LUCA. DR InParanoid; Q58425; -. DR KO; K01956; -. DR OMA; VDTRYIT; -. DR PhylomeDB; Q58425; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005951; C:carbamoyl-phosphate synthase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR Gene3D; 3.50.30.20; -; 1. DR HAMAP; MF_01209; CPSase_S_chain; 1. DR InterPro; IPR006274; CarbamoylP_synth_ssu. DR InterPro; IPR002474; CarbamoylP_synth_ssu_N. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR Pfam; PF00988; CPSase_sm_chain; 1. DR Pfam; PF00117; GATase; 1. DR SMART; SM01097; CPSase_sm_chain; 1. DR SUPFAM; SSF52021; SSF52021; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01368; CPSaseIIsmall; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 354 Carbamoyl-phosphate synthase small chain. FT /FTId=PRO_0000112358. FT DOMAIN 171 354 Glutamine amidotransferase type-1. FT REGION 1 171 CPSase. FT ACT_SITE 246 246 Nucleophile. {ECO:0000250}. FT ACT_SITE 330 330 {ECO:0000250}. FT ACT_SITE 332 332 {ECO:0000250}. SQ SEQUENCE 354 AA; 39920 MW; 4D8F07776CA65F9F CRC64; MEAVLILEDG TILKGKGFGA EKEVFGELVF TTVMTGYVEV LTDPSYKGQI VMMTYPLEGN YGVKKDWFES DGIKAEGFVV REVTSKALDD FLKEYDIPGI QDIDTRFLTR KIRDKGVVKS CLKVAEEISD DEISELLERV KRYSDISDID LVPLVSTKEP KIHKTANPKA RCVLIDCGVK LNIIRSLVQR NCEVIQVPYN TKYDEILEYK PDFVLISNGP GDPARLKEVI KNIKNLIGVV PITGICLGNQ LLSLAFGGET YKMKFGHRGG NQPVKDLKTQ KVYITSQNHG FAVRKESLPD DVEVSFINLN DMTVEGIRHK DLPIFSVQFH PEARPGPHDT MFLFDEMIKL KDRK // ID CBIE_METJA Reviewed; 211 AA. AC Q58917; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Probable cobalt-precorrin-7 C(5)-methyltransferase; DE EC=2.1.1.289; DE AltName: Full=Cobalt-precorrin-6Y C(5)-methyltransferase; DE Short=Cobalt-precorrin-6 methyltransferase; DE Short=Cobalt-precorrin-6Y methylase; GN Name=cbiE; Synonyms=cobL; OrderedLocusNames=MJ1522; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the methylation of C-5 in cobalt-precorrin-7 CC to form cobalt-precorrin-8. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-7 + S-adenosyl-L-methionine = CC cobalt-precorrin-8 + S-adenosyl-L-homocysteine. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 8/10. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99541.1; -; Genomic_DNA. DR PIR; A64490; A64490. DR ProteinModelPortal; Q58917; -. DR STRING; 243232.MJ_1522; -. DR EnsemblBacteria; AAB99541; AAB99541; MJ_1522. DR KEGG; mja:MJ_1522; -. DR eggNOG; arCOG00650; Archaea. DR eggNOG; COG2241; LUCA. DR InParanoid; Q58917; -. DR KO; K03399; -. DR OMA; DFRIEFI; -. DR PhylomeDB; Q58917; -. DR UniPathway; UPA00148; UER00229. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR012818; Cbl_synth_CbiE. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR02467; CbiE; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 211 Probable cobalt-precorrin-7 C(5)- FT methyltransferase. FT /FTId=PRO_0000150410. SQ SEQUENCE 211 AA; 23806 MW; 279A1A2B14369510 CRC64; MIYIVGIGPG DREYLTLKAI KIVENADLVV GSKRALELFN IDEDKKITLT KNLIGELKEL IKNENIKNKK IAILSTGDPC FSGLLKTLLK IGAKKEDIEA ISGISSIQIA AAKLKISWED YYIITLHGKE ENRKKLLNLI KNHEKVIFLP NNLKEDAKFL INNGINPDTK IWVLENLTYE NEKISLKSLK EIANGDFSYL TVCVYEGDEE I // ID CBIT_METJA Reviewed; 183 AA. AC Q57836; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Probable cobalt-precorrin-6B C(15)-methyltransferase (decarboxylating) {ECO:0000255|HAMAP-Rule:MF_00786}; DE EC=2.1.1.196 {ECO:0000255|HAMAP-Rule:MF_00786}; GN Name=cbiT {ECO:0000255|HAMAP-Rule:MF_00786}; OrderedLocusNames=MJ0391; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=23688113; DOI=10.1186/1472-6807-13-10; RA Padmanabhan B., Yokoyama S., Bessho Y.; RT "Crystal structure of putative CbiT from Methanocaldococcus RT jannaschii: an intermediate enzyme activity in cobalamin (vitamin B12) RT biosynthesis."; RL BMC Struct. Biol. 13:10-10(2013). CC -!- FUNCTION: Catalyzes the methylation of C-15 in cobalt-precorrin-6B CC followed by the decarboxylation of C-12 to form cobalt-precorrin- CC 7. {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-6B + S-adenosyl-L-methionine CC = cobalt-precorrin-7 + S-adenosyl-L-homocysteine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 8/10. {ECO:0000255|HAMAP-Rule:MF_00786}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC Archaeal-type CbiT family. {ECO:0000255|HAMAP-Rule:MF_00786}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98376.1; -; Genomic_DNA. DR PIR; G64348; G64348. DR PDB; 2YXD; X-ray; 2.30 A; A/B=1-183. DR PDBsum; 2YXD; -. DR ProteinModelPortal; Q57836; -. DR SMR; Q57836; 4-183. DR STRING; 243232.MJ_0391; -. DR EnsemblBacteria; AAB98376; AAB98376; MJ_0391. DR KEGG; mja:MJ_0391; -. DR eggNOG; arCOG00977; Archaea. DR eggNOG; COG2242; LUCA. DR InParanoid; Q57836; -. DR KO; K02191; -. DR OMA; KFVYAID; -. DR PhylomeDB; Q57836; -. DR UniPathway; UPA00148; UER00229. DR EvolutionaryTrace; Q57836; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046140; P:corrin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00786; CbiT; 1. DR InterPro; IPR023475; CbiT. DR InterPro; IPR014008; Cbl_synth_MTase_CbiT. DR InterPro; IPR025714; Methyltranfer_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF13847; Methyltransf_31; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR02469; CbiT; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Complete proteome; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 183 Probable cobalt-precorrin-6B C(15)- FT methyltransferase (decarboxylating). FT /FTId=PRO_0000134938. FT REGION 43 47 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00786}. FT BINDING 19 19 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00786}. FT BINDING 64 64 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00786}. FT BINDING 92 92 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00786}. FT HELIX 21 31 {ECO:0000244|PDB:2YXD}. FT STRAND 38 43 {ECO:0000244|PDB:2YXD}. FT HELIX 48 54 {ECO:0000244|PDB:2YXD}. FT STRAND 57 64 {ECO:0000244|PDB:2YXD}. FT HELIX 67 79 {ECO:0000244|PDB:2YXD}. FT STRAND 84 90 {ECO:0000244|PDB:2YXD}. FT HELIX 92 95 {ECO:0000244|PDB:2YXD}. FT HELIX 96 98 {ECO:0000244|PDB:2YXD}. FT STRAND 102 106 {ECO:0000244|PDB:2YXD}. FT HELIX 112 121 {ECO:0000244|PDB:2YXD}. FT STRAND 126 132 {ECO:0000244|PDB:2YXD}. FT HELIX 134 146 {ECO:0000244|PDB:2YXD}. FT STRAND 150 164 {ECO:0000244|PDB:2YXD}. FT STRAND 167 172 {ECO:0000244|PDB:2YXD}. FT STRAND 176 182 {ECO:0000244|PDB:2YXD}. SQ SEQUENCE 183 AA; 20502 MW; CB47419BB8781340 CRC64; MKYMIPDEEF IRREGVPITK EEIRAVSIGK LNLNKDDVVV DVGCGSGGMT VEIAKRCKFV YAIDYLDGAI EVTKQNLAKF NIKNCQIIKG RAEDVLDKLE FNKAFIGGTK NIEKIIEILD KKKINHIVAN TIVLENAAKI INEFESRGYN VDAVNVFISY AKKIPSGHMF LAKNPITIIK AVR // ID CAS10_METJA Reviewed; 800 AA. AC Q59066; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=CRISPR-associated protein Cas10/Csm1; DE AltName: Full=CRISPR-associated protein Cas10/Csm1, subtype III-A/Mtube; GN Name=cas10; Synonyms=csm1; OrderedLocusNames=MJ1672; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Cas10/Csm1 family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GGDEF domain. {ECO:0000255|PROSITE- CC ProRule:PRU00095}. CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99690.1; -; Genomic_DNA. DR PIR; F64508; F64508. DR STRING; 243232.MJ_1672; -. DR EnsemblBacteria; AAB99690; AAB99690; MJ_1672. DR KEGG; mja:MJ_1672; -. DR eggNOG; arCOG02666; Archaea. DR eggNOG; COG1353; LUCA. DR InParanoid; Q59066; -. DR KO; K07016; -. DR OMA; GGHFYIL; -. DR PhylomeDB; Q59066; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR013408; CRISPR-assoc_prot_Csm1. DR InterPro; IPR000160; GGDEF_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR TIGRFAMs; TIGR02578; cas_TM1811_Csm1; 1. DR PROSITE; PS50887; GGDEF; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 800 CRISPR-associated protein Cas10/Csm1. FT /FTId=PRO_0000107470. FT DOMAIN 1 92 HD. FT DOMAIN 578 722 GGDEF. {ECO:0000255|PROSITE- FT ProRule:PRU00095}. SQ SEQUENCE 800 AA; 93633 MW; E4CD16D129C0FB0C CRC64; MGNCNEYTAL KIGALLHDIG KFIQRASDKP KSKGHDKFGY EFLKEKFKNG FLNHLDEKTK DKILEIVKEH HNQKIKDDLI GIVRLADWLS SGERREPKGD PENVEVLNTE EQKLLSIFET VCIGELTENL YKNGFKYSLK PLNVSDAIFT DKPYPNENYK ELFSKFEDEI KDFKGDVSFE ELYQLMQKYT WCIPSVTMWK KAGSLKGGLP DVSLFDHSKT TCAIACCLYQ MYVKENKKKN KYAKEYIDDK TLEKLFNNDN GWNKEIFSLI HGDLSGIQDF VFTITTKYAT KSLKGRSFYL DFLTEYFAKY ICKELNLPIT NILFYGGGHF YILSYKVDEN LINKLEKEIN EVLFNMFRTK IYITIAEVGV TPNDFKKSED KESKEKTWGF AKKWKEVSEK TVEKKLRRFE YKLEGLFEPY NRGSENRCVI CRNEFDKNEK GYAIRENESK SERICDYCAS FVALTDILKN FQMEKTIKFN KAYPIIHLTK NKDNLSLQRE EFSFLTVKAI EKLESKFRVL SDENYFLKEY KLPHDSGELI IPYKIWAIAF PIIENETEKR ILDFDGLAEK AFERTGTRKI GILKMDVDNL GEIFTTGLGN DATISRMSTL SSMLTLFFTG YIPHLIKNEE FEVNGKKYKF KDNIYLVYAG GDDTLIVGAW DAVWELAKRI RGDFKKFVCY NPYITLSAGI VFVNPKFEFK KAVNMAEEEL ENGKNYIIYE DEETEKKVDK NALTVFNCPM NWDLEVEYNE YCWTKLKSYL EGINKEMVEL ESLVKKFNED DLEKNLKKQL KRQIRKESYI // ID CAS4_METJA Reviewed; 170 AA. AC Q57822; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=CRISPR-associated exonuclease Cas4; DE EC=3.1.12.1 {ECO:0000250|UniProtKB:Q97TX9}; GN Name=cas4; OrderedLocusNames=MJ0377; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). This protein may be a 5' to 3' CC ssDNA exonuclease. {ECO:0000250|UniProtKB:Q97TX9}. CC -!- CATALYTIC ACTIVITY: Exonucleolytic cleavage in the 5'- to 3'- CC direction to yield nucleoside 3'-phosphates. CC {ECO:0000250|UniProtKB:Q97TX9}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q97TX9}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q97TX9}; CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000250|UniProtKB:Q97TX9}; CC Note=Mg(2+) or Mn(2+) required for ssDNA cleavage activity. Can CC also utilise Cu(2+). {ECO:0000250|UniProtKB:Q97TX9}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q97TX9}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. It may be important for CC protein stability, since mutation of the Cys that bind the CC cofactor leads to a colorless, insoluble protein. CC {ECO:0000250|UniProtKB:Q97TX9}; CC -!- SIMILARITY: Belongs to the CRISPR-associated exonuclease Cas4 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98366.1; -; Genomic_DNA. DR PIR; A64347; A64347. DR STRING; 243232.MJ_0377; -. DR EnsemblBacteria; AAB98366; AAB98366; MJ_0377. DR KEGG; mja:MJ_0377; -. DR eggNOG; arCOG00794; Archaea. DR eggNOG; COG1468; LUCA. DR InParanoid; Q57822; -. DR KO; K07464; -. DR OMA; ICKTKLW; -. DR PhylomeDB; Q57822; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; ISS:UniProtKB. DR GO; GO:0030145; F:manganese ion binding; ISS:UniProtKB. DR GO; GO:0045145; F:single-stranded DNA 5'-3' exodeoxyribonuclease activity; ISS:UniProtKB. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; ISS:UniProtKB. DR InterPro; IPR013343; CRISPR-assoc_prot_Cas4. DR InterPro; IPR022765; Dna2/Cas4_DUF83. DR Pfam; PF01930; Cas_Cas4; 1. DR TIGRFAMs; TIGR00372; cas4; 1. PE 3: Inferred from homology; KW 4Fe-4S; Antiviral defense; Complete proteome; Exonuclease; Hydrolase; KW Iron; Iron-sulfur; Manganese; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 170 CRISPR-associated exonuclease Cas4. FT /FTId=PRO_0000106840. FT METAL 22 22 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 49 49 Manganese; via tele nitrogen. FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 68 68 Manganese. FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 80 80 Manganese. FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 159 159 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 162 162 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:Q97TX9}. FT METAL 168 168 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:Q97TX9}. SQ SEQUENCE 170 AA; 20420 MW; 10CEBC592550AA4B CRC64; MENYLEEELI IGGIEINYLY VCKTKLWYFV RGITMEQESD FVDLGKFLHE KSYFGEEKEV QIGSIKIDFI KKRDVIEIHE VKRGKQMEKA HIMQVLYYIY YLNSLGIKSK AILHYPKLKE IKEIELKENN KEEIKRAIKE IEYIKSLKEP PEPIYQKICK NCAYYELCFI // ID CAS5_METJA Reviewed; 245 AA. AC Q57827; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=CRISPR-associated protein Cas5; GN Name=cas5; OrderedLocusNames=MJ0382; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas5 family. CC Subtype I-A/Apern subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98378.1; -; Genomic_DNA. DR PIR; F64347; F64347. DR ProteinModelPortal; Q57827; -. DR STRING; 243232.MJ_0382; -. DR EnsemblBacteria; AAB98378; AAB98378; MJ_0382. DR KEGG; mja:MJ_0382; -. DR eggNOG; arCOG02672; Archaea. DR eggNOG; COG1688; LUCA. DR OMA; LKAAMLI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR021124; CRISPR-assoc_prot_Cas5. DR InterPro; IPR013422; CRISPR-assoc_prot_Cas5_N. DR InterPro; IPR010153; CRISPR-assoc_prot_Cas5a-typ. DR Pfam; PF09704; Cas_Cas5d; 1. DR TIGRFAMs; TIGR01874; cas_cas5a; 1. DR TIGRFAMs; TIGR02593; CRISPR_cas5; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 245 CRISPR-associated protein Cas5. FT /FTId=PRO_0000106845. SQ SEQUENCE 245 AA; 28255 MW; 6169A4FFC51AE8BA CRC64; MIMEALVALL RFPFYSFGKQ SYQVRQSLLL PSPSALKGAL AKGIILLGGK KGKSLDEIAK KTVEELENKL IYVGAKPYKS SIIKTPILLK RLRNLEDQKN PEKSDAMRRE YVFAREILAI YVFRRKLSEE EKDLMLKAVY LIDQLGDTEC VGNVIKTEWV EVKEEKAPLK TYVKFKKVSK MSINGGIIEN MLETPNFGNK VKEEPYLLPL IEKRYRRSSY YVESDRIFDG NYKIIAFDEV IGLWI // ID CBIC_METJA Reviewed; 210 AA. AC Q58340; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Cobalt-precorrin-8 methylmutase; DE EC=5.4.99.60; DE AltName: Full=Cobalt-precorrin isomerase; GN Name=cbiC; Synonyms=cobH; OrderedLocusNames=MJ0930; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of cobalt-precorrin-8 to CC cobyrinate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-8 = cobyrinate. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 9/10. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CobH/CbiC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98932.1; -; Genomic_DNA. DR PIR; B64416; B64416. DR ProteinModelPortal; Q58340; -. DR STRING; 243232.MJ_0930; -. DR EnsemblBacteria; AAB98932; AAB98932; MJ_0930. DR KEGG; mja:MJ_0930; -. DR eggNOG; arCOG02247; Archaea. DR eggNOG; COG2082; LUCA. DR InParanoid; Q58340; -. DR KO; K06042; -. DR OMA; GLQFSEG; -. DR PhylomeDB; Q58340; -. DR UniPathway; UPA00148; UER00230. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016993; F:precorrin-8X methylmutase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.10230; -; 1. DR InterPro; IPR003722; Cbl_synth_CobH/CbiC. DR Pfam; PF02570; CbiC; 1. DR SUPFAM; SSF63965; SSF63965; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 210 Cobalt-precorrin-8 methylmutase. FT /FTId=PRO_0000135928. FT ACT_SITE 47 47 Proton donor/acceptor. {ECO:0000250}. FT BINDING 15 15 Substrate. {ECO:0000250}. FT BINDING 44 44 Substrate. {ECO:0000250}. SQ SEQUENCE 210 AA; 22974 MW; 2B5773E46E3105E6 CRC64; MGAISKDGLN IANKSREIVR NKIKEVLGDR INEFNEKEMG IIERVVHATA DPEYAKLLVF KNNPIEEGIK AIKEEKPIIV DVNMIKAGIR YNKVHCFINH PDVYEVAKKE GITRAVASMR LAKDLIDDGI VVIGNSPTAL FEVIRLVKEE NIKPKLIVGV PVGFVQASES KEALREVNVP SISTIGPKGG TPVAVAIING IIAYAKNEKA // ID CBIG_METJA Reviewed; 323 AA. AC Q58544; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Probable cobalt-precorrin-5A hydrolase; DE EC=3.7.1.12; GN Name=cbiG; OrderedLocusNames=MJ1144; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the hydrolysis of the ring A acetate delta- CC lactone of cobalt-precorrin-5A resulting in the loss of the C-20 CC carbon and its attached methyl group in the form of acetaldehyde. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-5A + H(2)O = cobalt- CC precorrin-5B + acetaldehyde + 2 H(+). CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 5/10. CC -!- SIMILARITY: Belongs to the CbiG family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99144.1; -; Genomic_DNA. DR PIR; G64442; G64442. DR ProteinModelPortal; Q58544; -. DR STRING; 243232.MJ_1144; -. DR EnsemblBacteria; AAB99144; AAB99144; MJ_1144. DR KEGG; mja:MJ_1144; -. DR eggNOG; arCOG00651; Archaea. DR eggNOG; COG2073; LUCA. DR InParanoid; Q58544; -. DR KO; K02189; -. DR OMA; WAVKKAL; -. DR PhylomeDB; Q58544; -. DR UniPathway; UPA00148; UER00561. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.420.180; -; 1. DR InterPro; IPR021744; CbiG_N. DR InterPro; IPR002750; CobE/GbiG_C. DR Pfam; PF01890; CbiG_C; 1. DR Pfam; PF11760; CbiG_N; 1. DR SUPFAM; SSF159664; SSF159664; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Hydrolase; KW Reference proteome. FT CHAIN 1 323 Probable cobalt-precorrin-5A hydrolase. FT /FTId=PRO_0000107187. SQ SEQUENCE 323 AA; 37500 MW; E6476F3F39DDBCE4 CRC64; MMIKIVYITK RGKKIAEEIK DVLDYYHYDN KVEPIKDFKI ERNEGGFIFI MATGIVLRKF LDEIKNDKFK DPFVIICNEN KELIPILSNH LGGGNYFSKL IANNINGRVI FTTATDVNGK VGIDELSKML FLETPKRKHI LDINKKILEE DVSLTLPKYW KLRNLNGYKI SYHDKYEVVV DDSIRLKPLK IAVGLGARKG IERYKVYWAV KKALFLRNIP VWRVDAFATI EDKKHERGIL ETVNKFKKPL IIFKREEINE IYEKIDLEKS EFVYKHLGVY GVSEPASILA VKKLTNKDFD SIKLILKKFK RNGVTVAIAT ENL // ID CARB1_METJA Reviewed; 482 AA. AC Q58773; DT 02-AUG-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 17-FEB-2016, entry version 118. DE RecName: Full=Carbamoyl-phosphate synthase large chain, N-terminal section; DE EC=6.3.5.5; DE AltName: Full=Carbamoyl-phosphate synthetase ammonia chain; GN Name=carB1; OrderedLocusNames=MJ1378; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 ATP + L-glutamine + HCO(3)(-) + H(2)O = 2 CC ADP + phosphate + L-glutamate + carbamoyl phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; CC carbamoyl phosphate from bicarbonate: step 1/1. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 1/3. CC -!- SUBUNIT: Composed of two chains; the small (or glutamine) chain CC promotes the hydrolysis of glutamine to ammonia, which is used by CC the large (or ammonia) chain to synthesize carbamoyl phosphate. CC -!- DOMAIN: Corresponds to the N-terminal section. CC -!- SIMILARITY: Belongs to the CarB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC -!- CAUTION: CarB is split into two genes in M.jannaschii (MJ1378 and CC MJ1381). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99385.1; -; Genomic_DNA. DR ProteinModelPortal; Q58773; -. DR SMR; Q58773; 2-474. DR STRING; 243232.MJ_1378; -. DR EnsemblBacteria; AAB99385; AAB99385; MJ_1378. DR KEGG; mja:MJ_1378; -. DR eggNOG; arCOG01594; Archaea. DR eggNOG; COG0458; LUCA. DR InParanoid; Q58773; -. DR KO; K01955; -. DR OMA; DPWFLDN; -. DR PhylomeDB; Q58773; -. DR UniPathway; UPA00068; UER00171. DR UniPathway; UPA00070; UER00115. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004087; F:carbamoyl-phosphate synthase (ammonia) activity; IBA:GO_Central. DR GO; GO:0004088; F:carbamoyl-phosphate synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006526; P:arginine biosynthetic process; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 1.10.1030.10; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005480; CarbamoylP_synth_lsu_oligo. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR005483; CbamoylP_synth_lsu_CPSase_dom. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF02786; CPSase_L_D2; 1. DR Pfam; PF02787; CPSase_L_D3; 1. DR PRINTS; PR00098; CPSASE. DR SMART; SM01096; CPSase_L_D3; 1. DR SUPFAM; SSF48108; SSF48108; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; ATP-binding; KW Complete proteome; Ligase; Magnesium; Manganese; Metal-binding; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 482 Carbamoyl-phosphate synthase large chain, FT N-terminal section. FT /FTId=PRO_0000145075. FT DOMAIN 130 324 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 156 213 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT REGION 1 398 Carboxyphosphate synthetic domain. FT METAL 281 281 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 295 295 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 295 295 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 297 297 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. SQ SEQUENCE 482 AA; 53609 MW; A8ABE2570B2E3D96 CRC64; MESIKKVMVF GSGPIVIGQA AEFDFSGSQA CKALKEEGIY TILVNSNPAT IQTDTDMADK VYLEPLHPTI VEKIIEKERP DAILPTMGGQ TGLNLALELH RRGILDKYGI KLLGSNIRTI EIAEDRELFA EAMAEINEPV TKCKAVNSVD EAVEFAEEIG YPVIVRPAFT LGGTGGGIAH NKEELIDITS KGLKYSIINQ VLIDESVLGW KEFELEVMRD RKDTCIIVCG MENIDPMGIH TGESIVVSPI QTLPDEFYQK LRNAAIKIIR HLGIEGGCNI QFAVNKEMTE YRVIEVNPRV SRSSALASKA TGYPIARIAA KIAIGKTLDE ILNDVTKETP ASFEPTLDYV VVKIPRWPFD KFKTVDKKLG TSMKSTGEVM AIGRSFEEAL QKAIRSLDIG RFGIIGDGKD KDYTDEEIEE ILKNPTDERI FVIAKALEKG WSVEKIVELT DIDEFFIKKI KNIVDMKKEL EKLKEEIKKL NA // ID CAS1_METJA Reviewed; 322 AA. AC Q57823; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=CRISPR-associated endonuclease Cas1 {ECO:0000255|HAMAP-Rule:MF_01470}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01470}; GN Name=cas1 {ECO:0000255|HAMAP-Rule:MF_01470}; OrderedLocusNames=MJ0378; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA). Acts as a dsDNA CC endonuclease. Involved in the integration of spacer DNA into the CC CRISPR cassette. {ECO:0000255|HAMAP-Rule:MF_01470}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01470}; CC -!- SUBUNIT: Homodimer, forms a heterotetramer with a Cas2 homodimer. CC {ECO:0000255|HAMAP-Rule:MF_01470}. CC -!- SIMILARITY: Belongs to the CRISPR-associated endonuclease Cas1 CC family. {ECO:0000255|HAMAP-Rule:MF_01470}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98367.1; -; Genomic_DNA. DR PIR; B64347; B64347. DR ProteinModelPortal; Q57823; -. DR STRING; 243232.MJ_0378; -. DR EnsemblBacteria; AAB98367; AAB98367; MJ_0378. DR KEGG; mja:MJ_0378; -. DR eggNOG; arCOG01452; Archaea. DR eggNOG; COG1518; LUCA. DR InParanoid; Q57823; -. DR KO; K15342; -. DR OMA; ENTLYFE; -. DR PhylomeDB; Q57823; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-HAMAP. DR GO; GO:0043571; P:maintenance of CRISPR repeat elements; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01470; Cas1; 1. DR InterPro; IPR002729; CRISPR-assoc_Cas1. DR InterPro; IPR019858; CRISPR-assoc_Cas1_HMARI/TNEAP. DR Pfam; PF01867; Cas_Cas1; 1. DR TIGRFAMs; TIGR00287; cas1; 1. DR TIGRFAMs; TIGR03641; cas1_HMARI; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; DNA-binding; Endonuclease; KW Hydrolase; Magnesium; Manganese; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 322 CRISPR-associated endonuclease Cas1. FT /FTId=PRO_0000106841. FT METAL 149 149 Manganese or magnesium. FT {ECO:0000255|HAMAP-Rule:MF_01470}. FT METAL 214 214 Manganese or magnesium. FT {ECO:0000255|HAMAP-Rule:MF_01470}. FT METAL 229 229 Manganese or magnesium. FT {ECO:0000255|HAMAP-Rule:MF_01470}. SQ SEQUENCE 322 AA; 38147 MW; 6E1833962A77EA3D CRC64; MRKKSLTLLS DGYLFRKENT IYFENARGKK PLAIEGIYDI YIYGKVSISS QALHYLAQKG IALHFFNHYG YYDGSFYPRE SLHSGYLVVN QVEHYLDKDK RLELAKLFII GGIKNMEWNL LKFKNKTKFS SYIEELNNCN KITEVMNVEG RVRTEYYRLW DETLPDDFKI VKRTRRPPKN EMNALISFLN SRLYPAIITE LYNTQLTPTV SYLHEPHERR FSLALDLSEI FKPMIADRLA NRLVKQGIIQ KKHFRDDLNG VLLNKEGMKV VLEHFNKEMD KTVNHKKLKK NVSKRRLIRL EAYKLVKHLV GQKRYEPLVA WF // ID CAS8A_METJA Reviewed; 375 AA. AC Q57830; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=CRISPR-associated protein Cas8a2/Csa4; DE AltName: Full=CRISPR-associated protein Cas8a2/Csa4, subtype I-A/Apern; GN Name=cas8a2; OrderedLocusNames=MJ0385; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein Cas8a2/Csa4 CC family. Subtype I-A/Apern subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98380.1; -; Genomic_DNA. DR PIR; A64348; A64348. DR ProteinModelPortal; Q57830; -. DR STRING; 243232.MJ_0385; -. DR EnsemblBacteria; AAB98380; AAB98380; MJ_0385. DR KEGG; mja:MJ_0385; -. DR eggNOG; arCOG01441; Archaea. DR eggNOG; ENOG410YJTR; LUCA. DR InParanoid; Q57830; -. DR KO; K19086; -. DR OMA; KLMDFLW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR010184; CRISPR-assoc_prot_MJ0385. DR Pfam; PF09703; Cas_Csa4; 1. DR TIGRFAMs; TIGR01914; cas_Csa4; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 375 CRISPR-associated protein Cas8a2/Csa4. FT /FTId=PRO_0000106848. SQ SEQUENCE 375 AA; 43187 MW; 9A2853EA2CBEBE51 CRC64; MIIKGLRVEK EKLQSLQKFW RLRVMLFETP GYNEILDLYI AYGVVECLVR EGVENLRFFP IGNKYCIVVE EPTNVNIKNR IEKGMLNALE DMLSLHKAIG KYISTKEDIK IISDVDFSAG ANINNVYWDG IPKTLEKIKE NIKKGKLSTK SKNTVPLTLM PAAGKYMPKI YGVKGGNPIK IDDSNYALAW IGFHYYAPYI NISDNRATYI HIYAIKPLEE LGLIEILALK DLKKKINNYQ LGKYKFFVNK KLALLYHLTH TESISALEIV TKKNFSVVSY TLENVDNNQA IRSFGEYDLS KLMDFLWYLK ATDFYNTIQF VDNILRGDLE VSLTFIDGIL YDDLDAVYSA IRKLKSVRIS PLIIQSILEW FGNFY // ID CBIL_METJA Reviewed; 230 AA. AC Q58181; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Probable cobalt-precorrin-2 C(20)-methyltransferase; DE EC=2.1.1.151; DE AltName: Full=S-adenosyl-L-methionine--cobalt-precorrin-2 methyltransferase; GN Name=cbiL; OrderedLocusNames=MJ0771; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Methylates cobalt-precorrin-2 at the C-20 position to CC produce cobalt-precorrin-3A in the anaerobic cobalamin CC biosynthesis pathway. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cobalt-factor II = CC S-adenosyl-L-homocysteine + cobalt-factor III. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 2/10. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98764.1; -; Genomic_DNA. DR PIR; C64396; C64396. DR ProteinModelPortal; Q58181; -. DR STRING; 243232.MJ_0771; -. DR EnsemblBacteria; AAB98764; AAB98764; MJ_0771. DR KEGG; mja:MJ_0771; -. DR eggNOG; arCOG00648; Archaea. DR eggNOG; COG2243; LUCA. DR InParanoid; Q58181; -. DR KO; K03394; -. DR OMA; STFSYVW; -. DR PhylomeDB; Q58181; -. DR UniPathway; UPA00148; UER00224. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043781; F:cobalt-factor II C20-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004164; F:diphthine synthase activity; IBA:GO_Central. DR GO; GO:0030788; F:precorrin-2 C20-methyltransferase activity; IEA:InterPro. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1010.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR012382; CobI/CbiL. DR InterPro; IPR006364; CobI/CbiL/CobIJ_dom. DR InterPro; IPR003043; Uropor_MeTrfase_CS. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036427; Precrrn-2_mtase; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01467; cobI_cbiL; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 230 Probable cobalt-precorrin-2 C(20)- FT methyltransferase. FT /FTId=PRO_0000150411. SQ SEQUENCE 230 AA; 26267 MW; 4FFD926E9B441FFB CRC64; MNKLVKKVYG VGVGVGDKKL LTLKALEVLK KVDKIFVPVS KKGKKSIAYE IIKDYVDGKN IEELLFPMIK DKERLKKYWE NALEKVLKED GEVAIITIGD PTLYSTFSYV WKLLKERGVE VEIVNGISSI FASAAALNIP LVEGDEKLCI LPQGKDLEKY IDEFDTIIIM KTKNLNEKLS VIKNRDDYII GLVKRATFED EKVVIGKLDE INFDEFNDYL SLAIIKRFKR // ID CBIA_METJA Reviewed; 443 AA. AC Q58816; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Cobyrinate a,c-diamide synthase {ECO:0000255|HAMAP-Rule:MF_00027}; DE EC=6.3.5.11 {ECO:0000255|HAMAP-Rule:MF_00027}; DE AltName: Full=Cobyrinic acid a,c-diamide synthetase {ECO:0000255|HAMAP-Rule:MF_00027}; GN Name=cbiA {ECO:0000255|HAMAP-Rule:MF_00027}; OrderedLocusNames=MJ1421; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent amidation of the two CC carboxylate groups at positions a and c of cobyrinate, using CC either L-glutamine or ammonia as the nitrogen source. CC {ECO:0000255|HAMAP-Rule:MF_00027}. CC -!- CATALYTIC ACTIVITY: 2 ATP + cobyrinate + 2 L-glutamine + 2 H(2)O = CC 2 ADP + 2 phosphate + cobyrinate a,c-diamide + 2 L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00027}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00027}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 10/10. {ECO:0000255|HAMAP-Rule:MF_00027}. CC -!- DOMAIN: Comprises of two domains. The C-terminal domain contains CC the binding site for glutamine and catalyzes the hydrolysis of CC this substrate to glutamate and ammonia. The N-terminal domain is CC anticipated to bind ATP and cobyrinate and catalyzes the ultimate CC synthesis of the diamide product. The ammonia produced via the CC glutaminase domain is probably translocated to the adjacent domain CC via a molecular tunnel, where it reacts with an activated CC intermediate. {ECO:0000255|HAMAP-Rule:MF_00027}. CC -!- MISCELLANEOUS: The a and c carboxylates of cobyrinate are CC activated for nucleophilic attack via formation of a CC phosphorylated intermediate by ATP. CbiA catalyzes first the CC amidation of the c-carboxylate, and then that of the a- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_00027}. CC -!- SIMILARITY: Belongs to the CobB/CbiA family. {ECO:0000255|HAMAP- CC Rule:MF_00027}. CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain. CC {ECO:0000255|HAMAP-Rule:MF_00027}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99432.1; -; Genomic_DNA. DR PIR; D64477; D64477. DR ProteinModelPortal; Q58816; -. DR STRING; 243232.MJ_1421; -. DR EnsemblBacteria; AAB99432; AAB99432; MJ_1421. DR KEGG; mja:MJ_1421; -. DR eggNOG; arCOG00106; Archaea. DR eggNOG; COG1797; LUCA. DR InParanoid; Q58816; -. DR KO; K02224; -. DR OMA; RWYGALS; -. DR PhylomeDB; Q58816; -. DR UniPathway; UPA00148; UER00231. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042242; F:cobyrinic acid a,c-diamide synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00027; CobB_CbiA; 1. DR InterPro; IPR004484; CbiA_synth. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017929; CobB/CobQ_GATase. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00379; cobB; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 3: Inferred from homology; KW ATP-binding; Cobalamin biosynthesis; Complete proteome; KW Glutamine amidotransferase; Ligase; Magnesium; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 443 Cobyrinate a,c-diamide synthase. FT /FTId=PRO_0000141276. FT DOMAIN 248 433 GATase cobBQ-type. {ECO:0000255|HAMAP- FT Rule:MF_00027}. FT ACT_SITE 327 327 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00027}. FT SITE 425 425 Increases nucleophilicity of active site FT Cys. {ECO:0000255|HAMAP-Rule:MF_00027}. SQ SEQUENCE 443 AA; 50206 MW; EA8D66D0FC9ED212 CRC64; MIMKRVVIAG TSSEVGKTVI STGIMKALSK KYNVQGYKVG PDYIDPTYHT IATGNKSRNL DSFFMNKEQI KYLFQKHSKD KDISVIEGVR GLYEGISAID DIGSTASVAK ALDSPIILLV NAKSLTRSAI AIIKGFMSFD NVKIKGVIFN FVRSENHIKK LKDAMSYYLP DIEIIGFIPR NEDFKVEGRH LGLVPTPENL KEIESKIVLW GELVEKYLDL DKIVEIADED FEEVDDVFLW EVNENYKKIA VAYDKAFNFY YWDNFEALKE NKAKIEFFSP LKDSEVPDAD ILYIGGGYPE LFKEELSRNK EMIESIKEFD GYIYGECGGL MYITKSIDNV PMVGLLNCSA VMTKHVQGLS YVKAEFLEDC LIGRKGLKFK GHEFHYSKLV NIKEERFAYK IERGRGIINN LDGIFNGKVL AGYLHNHAVA NPYFASSMVN FGE // ID CBIN_METJA Reviewed; 95 AA. AC Q58490; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Cobalt transport protein CbiN {ECO:0000255|HAMAP-Rule:MF_00330}; DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein CbiN {ECO:0000255|HAMAP-Rule:MF_00330}; DE Short=ECF transporter S component CbiN {ECO:0000255|HAMAP-Rule:MF_00330}; GN Name=cbiN {ECO:0000255|HAMAP-Rule:MF_00330}; OrderedLocusNames=MJ1090; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter CC complex CbiMNOQ involved in cobalt import. {ECO:0000255|HAMAP- CC Rule:MF_00330}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00330}. CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex CC composed of an ATP-binding protein (A component, CbiO), a CC transmembrane protein (T component, CbiQ) and 2 possible CC substrate-capture proteins (S components, CbiM and CbiN) of CC unknown stoichimetry. {ECO:0000255|HAMAP-Rule:MF_00330}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00330}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00330}. CC -!- SIMILARITY: Belongs to the CbiN family. {ECO:0000255|HAMAP- CC Rule:MF_00330}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99091.1; -; Genomic_DNA. DR PIR; A64436; A64436. DR STRING; 243232.MJ_1090; -. DR EnsemblBacteria; AAB99091; AAB99091; MJ_1090. DR KEGG; mja:MJ_1090; -. DR eggNOG; arCOG04384; Archaea. DR eggNOG; COG1930; LUCA. DR InParanoid; Q58490; -. DR KO; K02009; -. DR OMA; SSIWEPP; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00330; CbiN; 1. DR InterPro; IPR003705; CbiN. DR Pfam; PF02553; CbiN; 1. DR TIGRFAMs; TIGR01165; cbiN; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalamin biosynthesis; Cobalt; Cobalt transport; KW Complete proteome; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 95 Cobalt transport protein CbiN. FT /FTId=PRO_0000134702. FT TRANSMEM 5 25 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00330}. FT TRANSMEM 67 87 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00330}. SQ SEQUENCE 95 AA; 10428 MW; FE9CFCE9EE6A62A9 CRC64; METKHIILLA IVAIIIALPL IIYAGKGEEE GYFGGSDDQG CEVVEELGYK PWFHPIWEPP SGEIESLLFA LQAAIGAIII GYYIGYYNAK RQVAA // ID CAS6A_METJA Reviewed; 254 AA. AC Q57820; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=CRISPR-associated endoribonuclease Cas6 1; DE EC=3.1.-.-; GN Name=cas6a; OrderedLocusNames=MJ0375; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). This protein processes pre- CC crRNA into individual crRNA units. {ECO:0000250|UniProtKB:Q8U1S4}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein CC Cas6/Cse3/CasE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98364.1; -; Genomic_DNA. DR PIR; G64346; G64346. DR STRING; 243232.MJ_0375; -. DR EnsemblBacteria; AAB98364; AAB98364; MJ_0375. DR KEGG; mja:MJ_0375; -. DR eggNOG; arCOG04342; Archaea. DR eggNOG; COG1583; LUCA. DR InParanoid; Q57820; -. DR KO; K19091; -. DR OMA; IMEVAYY; -. DR PhylomeDB; Q57820; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6. DR Pfam; PF01881; Cas_Cas6; 1. DR PIRSF; PIRSF005054; PF1131; 1. DR TIGRFAMs; TIGR01877; cas_cas6; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Endonuclease; Hydrolase; KW Nuclease; Reference proteome. FT CHAIN 1 254 CRISPR-associated endoribonuclease Cas6 FT 1. FT /FTId=PRO_0000106838. FT ACT_SITE 32 32 Proton acceptor. FT {ECO:0000250|UniProtKB:Q8U1S4}. FT ACT_SITE 47 47 Proton donor. FT {ECO:0000250|UniProtKB:Q8U1S4}. FT SITE 53 53 Transition state stabilizer. FT {ECO:0000250|UniProtKB:Q8U1S4}. SQ SEQUENCE 254 AA; 30184 MW; D9BCD0EB681148E5 CRC64; MRESMRIELE LQTDNFTVIP YNHQYYLASA IYNKIHSANP AYAKRLHNYQ KFKFFTFSLL QIRKRVIRKE GIETIDGKAY LYISSPNNEF IENFVAGLLE DGKLRVGNVE FFVRKAKILP IPKKFNILKT ISPIYLKTMI ETEDGLKTYD LLPNNSKFYE NLKNNLKKKY EAFYNEKCDM NFEFEVLKFR PKRMRIKNDI YCRCSEMVFK VWGDYDLIKF GYECGFGEKN SMGFGMVVNV EDKNQKNKKL KTKI // ID CAS6B_METJA Reviewed; 241 AA. AC Q58631; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=CRISPR-associated endoribonuclease Cas6 2; DE EC=3.1.-.-; GN Name=cas6b; OrderedLocusNames=MJ1234; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). This protein processes pre- CC crRNA into individual crRNA units. {ECO:0000250|UniProtKB:Q8U1S4}. CC -!- SIMILARITY: Belongs to the CRISPR-associated protein CC Cas6/Cse3/CasE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99238.1; -; Genomic_DNA. DR PIR; A64454; A64454. DR ProteinModelPortal; Q58631; -. DR STRING; 243232.MJ_1234; -. DR EnsemblBacteria; AAB99238; AAB99238; MJ_1234. DR KEGG; mja:MJ_1234; -. DR eggNOG; arCOG04342; Archaea. DR eggNOG; COG1583; LUCA. DR InParanoid; Q58631; -. DR KO; K19091; -. DR OMA; HAVQGFI; -. DR PhylomeDB; Q58631; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR010156; CRISPR-assoc_prot_Cas6. DR Pfam; PF01881; Cas_Cas6; 1. DR PIRSF; PIRSF005054; PF1131; 1. DR TIGRFAMs; TIGR01877; cas_cas6; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Endonuclease; Hydrolase; KW Nuclease; Reference proteome. FT CHAIN 1 241 CRISPR-associated endoribonuclease Cas6 FT 2. FT /FTId=PRO_0000107230. FT ACT_SITE 28 28 Proton acceptor. FT {ECO:0000250|UniProtKB:Q8U1S4}. FT ACT_SITE 40 40 Proton donor. FT {ECO:0000250|UniProtKB:Q8U1S4}. FT SITE 46 46 Transition state stabilizer. FT {ECO:0000250|UniProtKB:Q8U1S4}. SQ SEQUENCE 241 AA; 28840 MW; 23AD8F19448CBFC6 CRC64; MRLKLSLTPK QDFSFDKINK HTIQGFIYSL LKDTEFGEMH NQPRFKFWCF SDIFPPNDFV KGEDKYLLIS SPREEFINVL YERLDNLEEV NLNNFKFEVS ELKKFDLKVK NKFITGSPIV LYKDKDRGEY IKFYDDDFDL MFFVQRLQDN AVKKYKAFYN EEPVLNGFIF DRISPRVRNG RVDVYVRIAK KGREFLVVGT TWKLLEKIKI RKEERKFYKF IMDCGLGEKN SLGFGFINPI K // ID CBIJ_METJA Reviewed; 249 AA. AC Q57972; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Cobalt-precorrin-6A reductase; DE EC=1.3.1.106; GN Name=cbiJ; OrderedLocusNames=MJ0552; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reduction of the macrocycle of cobalt- CC precorrin-6A to cobalt-precorrin-6B. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cobalt-precorrin-6B + NAD(+) = cobalt- CC precorrin-6A + NADH. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC cob(II)yrinate a,c-diamide from sirohydrochlorin (anaerobic CC route): step 7/10. CC -!- SIMILARITY: Belongs to the precorrin-6x reductase family. CC {ECO:0000255|PROSITE-ProRule:PRU00356}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98544.1; -; Genomic_DNA. DR PIR; H64368; H64368. DR ProteinModelPortal; Q57972; -. DR STRING; 243232.MJ_0552; -. DR EnsemblBacteria; AAB98544; AAB98544; MJ_0552. DR KEGG; mja:MJ_0552; -. DR eggNOG; arCOG04852; Archaea. DR eggNOG; COG2099; LUCA. DR InParanoid; Q57972; -. DR KO; K05895; -. DR OMA; IPYLRYE; -. DR PhylomeDB; Q57972; -. DR UniPathway; UPA00148; UER00228. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016994; F:precorrin-6A reductase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003723; Precorrin-6x_reduct. DR Pfam; PF02571; CbiJ; 1. DR TIGRFAMs; TIGR00715; precor6x_red; 1. DR PROSITE; PS51014; COBK_CBIJ; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 249 Cobalt-precorrin-6A reductase. FT /FTId=PRO_0000135917. SQ SEQUENCE 249 AA; 28177 MW; 7271551E24AB05FE CRC64; MNLLLMGGTK DSVEIGKKLR DLGDLFILYT STTDYGGKLG EEFANKVITK PLDKNELKEV IKKYNIDILV DATHPFAINA SKNAIEVCKE LNIKYVRFER KEEKINHPNI IYVKDFEEAA RLAKKANKVF HMAGIKNLKM VVDIVGKDKV IARVLPISVS EALKILPQKQ IVAMYGTFSK ELNKYLIRDY NCDVIITKDS GESGGFKEKV YGALEAEAKV IVVERPKIDY PVCFDDIDEL IKYIANLKI // ID CBIM_METJA Reviewed; 233 AA. AC Q58491; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Putative cobalt transport protein CbiM {ECO:0000255|HAMAP-Rule:MF_01462}; DE AltName: Full=Energy-coupling factor transporter probable substrate-capture protein CbiM {ECO:0000255|HAMAP-Rule:MF_01462}; DE Short=ECF transporter S component CbiM {ECO:0000255|HAMAP-Rule:MF_01462}; GN Name=cbiM {ECO:0000255|HAMAP-Rule:MF_01462}; OrderedLocusNames=MJ1091; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the energy-coupling factor (ECF) transporter CC complex CbiMNOQ involved in cobalt import. {ECO:0000255|HAMAP- CC Rule:MF_01462}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01462}. CC -!- SUBUNIT: Forms an energy-coupling factor (ECF) transporter complex CC composed of an ATP-binding protein (A component, CbiO), a CC transmembrane protein (T component, CbiQ) and 2 possible CC substrate-capture proteins (S components, CbiM and CbiN) of CC unknown stoichimetry. {ECO:0000255|HAMAP-Rule:MF_01462}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01462}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01462}. CC -!- SIMILARITY: Belongs to the CbiM family. {ECO:0000255|HAMAP- CC Rule:MF_01462}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99092.1; -; Genomic_DNA. DR PIR; B64436; B64436. DR ProteinModelPortal; Q58491; -. DR STRING; 243232.MJ_1091; -. DR EnsemblBacteria; AAB99092; AAB99092; MJ_1091. DR KEGG; mja:MJ_1091; -. DR eggNOG; arCOG02248; Archaea. DR eggNOG; COG0310; LUCA. DR InParanoid; Q58491; -. DR KO; K02007; -. DR OMA; TAGTCSH; -. DR PhylomeDB; Q58491; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_01462; CbiM; 1. DR InterPro; IPR018024; CbiM. DR InterPro; IPR002751; CbiM_fam. DR Pfam; PF01891; CbiM; 1. DR TIGRFAMs; TIGR00123; cbiM; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalamin biosynthesis; Cobalt; Cobalt transport; KW Complete proteome; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 233 Putative cobalt transport protein CbiM. FT /FTId=PRO_0000089374. FT TRANSMEM 9 29 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. FT TRANSMEM 43 63 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. FT TRANSMEM 75 95 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. FT TRANSMEM 107 127 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. FT TRANSMEM 138 158 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. FT TRANSMEM 177 197 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01462}. SQ SEQUENCE 233 AA; 24914 MW; FDC194B58AA2CF9B CRC64; MHIMEGYLPP MWCAVWWVLS GIVIAYGIVK LKKLLEESPE MKPLVAISGA YMFILSSLKM PSVTGSCSHP CGNGLGAVLF GVPITAVLAA IVLLFQALFL AHGGLTTLGA NDFSMGIVGP AAAVIVYRLC MKAGLSSTVG IFFAALFGDW LTYVTTAVQL ALAFPIPSFT AAFTKFIVIY AYTQVPLAIA EGILTVIIWD YIKKLRPDLL LKLGVVPEEE LKPYLTPSPA GGE // ID CDPAS_METJA Reviewed; 177 AA. AC Q58995; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 86. DE RecName: Full=CDP-archaeol synthase {ECO:0000255|HAMAP-Rule:MF_01117}; DE EC=2.7.7.67 {ECO:0000255|HAMAP-Rule:MF_01117}; DE AltName: Full=CDP-2,3-bis-(O-geranylgeranyl)-sn-glycerol synthase {ECO:0000255|HAMAP-Rule:MF_01117}; GN Name=carS {ECO:0000255|HAMAP-Rule:MF_01117}; OrderedLocusNames=MJ1600; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the formation of CDP-2,3-bis-(O- CC geranylgeranyl)-sn-glycerol (CDP-archaeol) from 2,3-bis-(O- CC geranylgeranyl)-sn-glycerol 1-phosphate (DGGGP) and CTP. This CC reaction is the third ether-bond-formation step in the CC biosynthesis of archaeal membrane lipids. {ECO:0000255|HAMAP- CC Rule:MF_01117}. CC -!- CATALYTIC ACTIVITY: CTP + 2,3-bis-(O-geranylgeranyl)-sn-glycerol CC 1-phosphate = diphosphate + CDP-2,3-bis-(O-geranylgeranyl)-sn- CC glycerol. {ECO:0000255|HAMAP-Rule:MF_01117}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01117}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_01117}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01117}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01117}. CC -!- SIMILARITY: Belongs to the CDP-archaeol synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01117}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99620.1; -; Genomic_DNA. DR PIR; G64499; G64499. DR STRING; 243232.MJ_1600; -. DR EnsemblBacteria; AAB99620; AAB99620; MJ_1600. DR KEGG; mja:MJ_1600; -. DR eggNOG; arCOG04106; Archaea. DR eggNOG; COG0575; LUCA. DR InParanoid; Q58995; -. DR KO; K19664; -. DR OMA; PAYVPNN; -. DR PhylomeDB; Q58995; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01117; CDP_archaeol_synth; 1. DR InterPro; IPR032690; CarS. DR InterPro; IPR002726; CarS_archaea. DR Pfam; PF01864; DUF46; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 177 CDP-archaeol synthase. FT /FTId=PRO_0000094170. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01117}. FT TRANSMEM 54 74 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01117}. FT TRANSMEM 90 110 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01117}. FT TRANSMEM 124 144 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01117}. FT TRANSMEM 148 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01117}. SQ SEQUENCE 177 AA; 19460 MW; 2F10ABA3951396E2 CRC64; MFYRLLFASL WYILPAYVAN ASACIFGGGT PVDLGKNFID GRRLIGNGVT YRGCIFGILC GTLVGLIQGI LVDFNIFNSL DFYGTVLDHV ILAFFLSVGA IVGDAVGSFI KRRLNIERGK PAPLLDQLDF VIGALAFGYI VAPIPYEMII IICLFTVFVH LLGNIIAYKL GIKDVWW // ID CHMU_METJA Reviewed; 99 AA. AC Q57696; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Chorismate mutase; DE Short=CM; DE EC=5.4.99.5; DE AltName: Full=Monofunctional chorismate mutase AroQ(f); GN Name=aroQ; Synonyms=aroQ(f); OrderedLocusNames=MJ0246; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9665711; DOI=10.1021/bi980449t; RA MacBeath G., Kast P., Hilvert D.; RT "A small, thermostable, and monofunctional chorismate mutase from the RT archaeon Methanococcus jannaschii."; RL Biochemistry 37:10062-10073(1998). RN [3] RP STRUCTURE BY NMR OF 1-93. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17994104; DOI=10.1038/nsmb1325; RA Pervushin K., Vamvaca K., Vogeli B., Hilvert D.; RT "Structure and dynamics of a molten globular enzyme."; RL Nat. Struct. Mol. Biol. 14:1202-1206(2007). CC -!- FUNCTION: Catalyzes the conversion of chorismate into prephenate CC via a Claisen rearrangement. {ECO:0000269|PubMed:9665711}. CC -!- CATALYTIC ACTIVITY: Chorismate = prephenate. CC {ECO:0000269|PubMed:9665711}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=41 uM for chorismate (at 30 degrees Celsius) CC {ECO:0000269|PubMed:9665711}; CC Note=kcat is 5.7 sec(-1) (at 30 degrees Celsius).; CC pH dependence: CC Activity is independent of pH in the range of pH 5-9. CC {ECO:0000269|PubMed:9665711}; CC Temperature dependence: CC Thermostable. The midpoint for its thermal unfolding transition CC (Tm) is 88 degrees Celsius. {ECO:0000269|PubMed:9665711}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; prephenate CC biosynthesis; prephenate from chorismate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9665711}. CC -!- SIMILARITY: Contains 1 chorismate mutase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00515}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98234.1; -; Genomic_DNA. DR PIR; G64330; G64330. DR PDB; 2GTV; NMR; -; X=1-93. DR PDBsum; 2GTV; -. DR DisProt; DP00465; -. DR ProteinModelPortal; Q57696; -. DR SMR; Q57696; 1-93. DR STRING; 243232.MJ_0246; -. DR EnsemblBacteria; AAB98234; AAB98234; MJ_0246. DR KEGG; mja:MJ_0246; -. DR eggNOG; arCOG02098; Archaea. DR eggNOG; COG1605; LUCA. DR InParanoid; Q57696; -. DR KO; K04093; -. DR OMA; FQILIEH; -. DR PhylomeDB; Q57696; -. DR SABIO-RK; Q57696; -. DR UniPathway; UPA00120; UER00203. DR EvolutionaryTrace; Q57696; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004106; F:chorismate mutase activity; IEA:UniProtKB-EC. DR GO; GO:0046417; P:chorismate metabolic process; IEA:InterPro. DR Gene3D; 1.20.59.10; -; 1. DR InterPro; IPR002701; Chorismate_mutase. DR InterPro; IPR010950; Chorismate_mutase_arc. DR InterPro; IPR020822; Chorismate_mutase_type_II. DR Pfam; PF01817; CM_2; 1. DR SMART; SM00830; CM_2; 1. DR SUPFAM; SSF48600; SSF48600; 1. DR TIGRFAMs; TIGR01791; CM_archaeal; 1. DR PROSITE; PS51168; CHORISMATE_MUT_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome. FT CHAIN 1 99 Chorismate mutase. FT /FTId=PRO_0000119202. FT DOMAIN 1 90 Chorismate mutase. {ECO:0000255|PROSITE- FT ProRule:PRU00515}. FT BINDING 26 26 Substrate. {ECO:0000250}. FT BINDING 37 37 Substrate. {ECO:0000250}. FT BINDING 46 46 Substrate. {ECO:0000250}. FT BINDING 50 50 Substrate. {ECO:0000250}. FT BINDING 86 86 Substrate. {ECO:0000250}. FT HELIX 4 20 {ECO:0000244|PDB:2GTV}. FT HELIX 23 39 {ECO:0000244|PDB:2GTV}. FT HELIX 47 64 {ECO:0000244|PDB:2GTV}. FT HELIX 69 93 {ECO:0000244|PDB:2GTV}. SQ SEQUENCE 99 AA; 11782 MW; 9759018D0A07E76C CRC64; MIEKLAEIRK KIDEIDNKIL KLIAERNSLA KDVAEIKNQL GIPINDPERE KYIYDRIRKL CKEHNVDENI GIKIFQILIE HNKALQKQYL EETQNKNKK // ID CG121_METJA Reviewed; 145 AA. AC Q57646; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Regulatory protein Cgi121; DE AltName: Full=Positive regulator of Bud32 kinase activity; GN Name=cgi121; OrderedLocusNames=MJ0187; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.60 ANGSTROMS) IN COMPLEX WITH KAE1-BUD32, RP STRUCTURE BY NMR, FUNCTION, SUBUNIT, AND MUTAGENESIS OF LEU-134; RP ALA-138 AND LEU-139. RX PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002; RA Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z., RA Ceccarelli D.F., Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L., RA Fares C., Rumpel S., Kurinov I., Arrowsmith C.H., Durocher D., RA Sicheri F.; RT "Atomic structure of the KEOPS complex: an ancient protein kinase- RT containing molecular machine."; RL Mol. Cell 32:259-275(2008). CC -!- FUNCTION: Component of the KEOPS complex that is probably involved CC in the transfer of the threonylcarbamoyl moiety of CC threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37, a step in CC the formation of a threonylcarbamoyl group on adenosine at CC position 37 (t(6)A37) in tRNAs that read codons beginning with CC adenine. Cgi121 stimulates Bud32 kinase activity via an activation CC of Bud32 autophosphorylation. {ECO:0000269|PubMed:18951093}. CC -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, CC Bud32, Cgi121 and Pcc1; the whole complex dimerizes. CC {ECO:0000269|PubMed:18951093}. CC -!- SIMILARITY: Belongs to the CGI121/TPRKB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98167.1; -; Genomic_DNA. DR PIR; D64323; D64323. DR PDB; 2K8Y; NMR; -; A=1-145. DR PDB; 3ENH; X-ray; 3.60 A; C/D=1-145. DR PDBsum; 2K8Y; -. DR PDBsum; 3ENH; -. DR ProteinModelPortal; Q57646; -. DR STRING; 243232.MJ_0187; -. DR EnsemblBacteria; AAB98167; AAB98167; MJ_0187. DR KEGG; mja:MJ_0187; -. DR eggNOG; arCOG02197; Archaea. DR eggNOG; COG1617; LUCA. DR InParanoid; Q57646; -. DR OMA; FWMEILV; -. DR EvolutionaryTrace; Q57646; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR013926; CGI121/TPRKB. DR Pfam; PF08617; CGI-121; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 145 Regulatory protein Cgi121. FT /FTId=PRO_0000106735. FT MUTAGEN 134 134 L->E: No effect on Bud32 binding. FT {ECO:0000269|PubMed:18951093}. FT MUTAGEN 134 134 L->E: Severely affects Bud32 binding and FT does not stimulate Bud32 kinase activity; FT when associated with R-138. FT {ECO:0000269|PubMed:18951093}. FT MUTAGEN 138 138 A->R: No effect on Bud32 binding. FT {ECO:0000269|PubMed:18951093}. FT MUTAGEN 138 138 A->R: Severely affects Bud32 binding and FT does not stimulate Bud32 kinase activity; FT when associated with E-134. FT {ECO:0000269|PubMed:18951093}. FT MUTAGEN 139 139 L->R: No effect on Bud32 binding. FT {ECO:0000269|PubMed:18951093}. FT STRAND 1 9 {ECO:0000244|PDB:2K8Y}. FT HELIX 14 17 {ECO:0000244|PDB:2K8Y}. FT STRAND 21 29 {ECO:0000244|PDB:2K8Y}. FT HELIX 33 45 {ECO:0000244|PDB:2K8Y}. FT HELIX 53 60 {ECO:0000244|PDB:2K8Y}. FT TURN 61 63 {ECO:0000244|PDB:2K8Y}. FT HELIX 67 74 {ECO:0000244|PDB:2K8Y}. FT STRAND 78 86 {ECO:0000244|PDB:2K8Y}. FT HELIX 88 98 {ECO:0000244|PDB:2K8Y}. FT HELIX 104 107 {ECO:0000244|PDB:2K8Y}. FT HELIX 111 120 {ECO:0000244|PDB:2K8Y}. FT HELIX 129 140 {ECO:0000244|PDB:2K8Y}. SQ SEQUENCE 145 AA; 16593 MW; E7CB7330D1E1003F CRC64; MIIRGIRGAR INNEIFNLGL KFQILNADVV ATKKHVLHAI NQAKTKKPIA KSFWMEILVR ASGQRQIHEA IKIIGAKDGN VCLICEDEET FRKIYELIGG EIDDSVLEIN EDKERLIREI FKIRGFGNVV ERVLEKIALI ELKKE // ID CIMA_METJA Reviewed; 491 AA. AC Q58787; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=(R)-citramalate synthase CimA; DE EC=2.3.1.182; GN Name=cimA; OrderedLocusNames=MJ1392; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, PATHWAY, AND RP SUBUNIT. RX PubMed=9864346; RA Howell D.M., Xu H., White R.H.; RT "(R)-citramalate synthase in methanogenic archaea."; RL J. Bacteriol. 181:331-333(1999). CC -!- FUNCTION: Catalyzes the condensation of pyruvate and acetyl- CC coenzyme A to form (R)-citramalate. {ECO:0000269|PubMed:9864346}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + pyruvate + H(2)O = CoA + (2R)-2- CC hydroxy-2-methylbutanedioate. {ECO:0000269|PubMed:9864346}. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 1/3. CC {ECO:0000269|PubMed:9864346}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:9864346}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99402.1; -; Genomic_DNA. DR PIR; G64473; G64473. DR ProteinModelPortal; Q58787; -. DR STRING; 243232.MJ_1392; -. DR EnsemblBacteria; AAB99402; AAB99402; MJ_1392. DR KEGG; mja:MJ_1392; -. DR eggNOG; arCOG02092; Archaea. DR eggNOG; COG0119; LUCA. DR InParanoid; Q58787; -. DR KO; K09011; -. DR OMA; GEMFRIV; -. DR PhylomeDB; Q58787; -. DR BioCyc; MetaCyc:MONOMER-11899; -. DR UniPathway; UPA00047; UER00066. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043714; F:(R)-citramalate synthase activity; IEA:InterPro. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:InterPro. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01028; CimA; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR024890; Citramalate_synthase_CimA. DR InterPro; IPR011830; LEU1_arch. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR02090; LEU1_arch; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Direct protein sequencing; Isoleucine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 491 (R)-citramalate synthase CimA. FT /FTId=PRO_0000140450. FT CONFLICT 2 2 M -> L (in Ref. 2; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 491 AA; 53493 MW; 9D4FA0EA6F8F3BE5 CRC64; MMVRIFDTTL RDGEQTPGVS LTPNDKLEIA KKLDELGVDV IEAGSAITSK GEREGIKLIT KEGLNAEICS FVRALPVDID AALECDVDSV HLVVPTSPIH MKYKLRKTED EVLETALKAV EYAKEHGLIV ELSAEDATRS DVNFLIKLFN EGEKVGADRV CVCDTVGVLT PQKSQELFKK ITENVNLPVS VHCHNDFGMA TANTCSAVLG GAVQCHVTVN GIGERAGNAS LEEVVAALKI LYGYDTKIKM EKLYEVSRIV SRLMKLPVPP NKAIVGDNAF AHEAGIHVDG LIKNTETYEP IKPEMVGNRR RIILGKHSGR KALKYKLDLM GINVSDEQLN KIYERVKEFG DLGKYISDAD LLAIVREVTG KLVEEKIKLD ELTVVSGNKI TPIASVKLHY KGEDITLIET AYGVGPVDAA INAVRKAISG VADIKLVEYR VEAIGGGTDA LIEVVVKLRK GTEIVEVRKS DADIIRASVD AVMEGINMLL N // ID COBD_METJA Reviewed; 307 AA. AC Q58710; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Probable cobalamin biosynthesis protein CobD; GN Name=cobD; OrderedLocusNames=MJ1314; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Converts cobyric acid to cobinamide by the addition of CC aminopropanol on the F carboxylic group. {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CobD/CbiB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99321.1; -; Genomic_DNA. DR PIR; A64464; A64464. DR STRING; 243232.MJ_1314; -. DR EnsemblBacteria; AAB99321; AAB99321; MJ_1314. DR KEGG; mja:MJ_1314; -. DR eggNOG; arCOG04274; Archaea. DR eggNOG; COG1270; LUCA. DR InParanoid; Q58710; -. DR KO; K02227; -. DR OMA; IGNNERA; -. DR PhylomeDB; Q58710; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0048472; F:threonine-phosphate decarboxylase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00024; CobD_CbiB; 1. DR InterPro; IPR004485; Cobalamin_biosynth_CobD/CbiB. DR Pfam; PF03186; CobD_Cbib; 1. DR TIGRFAMs; TIGR00380; cobD; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalamin biosynthesis; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 307 Probable cobalamin biosynthesis protein FT CobD. FT /FTId=PRO_0000150941. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. SQ SEQUENCE 307 AA; 34502 MW; D24DDA2B50ECC1B1 CRC64; MLNPIILFLA IIFDRIIGEL PESIHPTVWI GKLIAFLENI FKSTNCKNKY RDFLFGSLTT FITLLVVGVI AFFVDKCIML LPFPLNYIIY GFLLSTTIGY KSLFEFCKKP IEYIKNGDLE GARKAVQHIV SRDASKLDKE HVLSAAVESL SENITDSIIG ALFYAIFFGL PGAFVYRAIN TLDAMIGYKN EKYLWYGKLA ARLDDIANFI PSRIAGILLI ITAPFYKGDV KKAIYGFLKE ANKVPSPNSG YTMATLANAL NITLEKIGYY KLGSGKIDVE KSLNAFKAVD YTVVVFLIIY TLIWWIT // ID COBQ_METJA Reviewed; 492 AA. AC Q57908; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=Probable cobyric acid synthase; GN Name=cobQ; OrderedLocusNames=MJ0484; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes amidations at positions B, D, E, and G on CC adenosylcobyrinic A,C-diamide. NH(2) groups are provided by CC glutamine, and one molecule of ATP is hydrogenolyzed for each CC amidation (By similarity). {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SIMILARITY: Belongs to the CobB/CobQ family. CobQ subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GATase cobBQ-type domain. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98475.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98475.1; ALT_INIT; Genomic_DNA. DR PIR; D64360; D64360. DR ProteinModelPortal; Q57908; -. DR STRING; 243232.MJ_0484; -. DR EnsemblBacteria; AAB98475; AAB98475; MJ_0484. DR KEGG; mja:MJ_0484; -. DR eggNOG; arCOG00105; Archaea. DR eggNOG; COG1492; LUCA. DR InParanoid; Q57908; -. DR KO; K02232; -. DR OMA; GLAWQNA; -. DR PhylomeDB; Q57908; -. DR UniPathway; UPA00148; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015420; F:cobalamin-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00028; CobQ; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017929; CobB/CobQ_GATase. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR004459; CobQ_synth. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; SSF52317; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00313; cobQ; 1. DR PROSITE; PS51274; GATASE_COBBQ; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Glutamine amidotransferase; KW Reference proteome. FT CHAIN 1 492 Probable cobyric acid synthase. FT /FTId=PRO_0000141348. FT DOMAIN 252 444 GATase cobBQ-type. FT ACT_SITE 330 330 Nucleophile. {ECO:0000250}. FT ACT_SITE 436 436 {ECO:0000250}. SQ SEQUENCE 492 AA; 55419 MW; 0B8E8803B12E5F44 CRC64; MAEFIMVVGT SSNSGKTTIT AGLCRILANK GYKVAPFKSQ NMSLNSRVAK EDGEIAIAQY TQSLACRVEP SVHFNPILLK PKGNFISQVI VHGRPYKDMN YNEYRKNKDF FLKKIKESLE ILDREYDYVI MEGAGSCCEI NLLKDDIANL RIAELVNAKA ILVADIDRGG VFASIYGTIK LLPENWRKLI KGIIINKFRG NVEVLKEGIE KIEELTGIPV LGIVPYDENL VLPEEDSQVL QSMRSFGNAK SGVEINVVRF SKISNFTDLD PLRYDAFIKF IDFDDDITGD ILIFPGTRSS TKEAYYLKQH NFDEKVLEFL KDGGIVIGIC GGYQVLGKEL IDKEKKESDV GDIEGLKIFD AKTYFGNDKV VKNSCGFLEI DNKTFNVKGY EIHEGFTYSK EKPLIKIERG FGNCGNGFDG SIKKFGDGLA IGTYFHGIFE NYEFRNYIIN LIRKRKGLDE IYGDSYKDSI EKSLNYFAEV VERSVNLKPL GI // ID COOS_METJA Reviewed; 624 AA. AC Q58138; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 91. DE RecName: Full=Carbon monoxide dehydrogenase; DE Short=CODH; DE EC=1.2.99.2; GN Name=cooS; OrderedLocusNames=MJ0728; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP REVIEW. RX PubMed=11841199; DOI=10.1021/bi015932+; RA Lindahl P.A.; RT "The Ni-containing carbon monoxide dehydrogenase family: light at the RT end of the tunnel?"; RL Biochemistry 41:2097-2105(2002). CC -!- CATALYTIC ACTIVITY: CO + H(2)O + A = CO(2) + AH(2). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 3 [4Fe-4S] clusters per homodimer. {ECO:0000250}; CC -!- COFACTOR: CC Name=[Ni-Fe-S] cluster; Xref=ChEBI:CHEBI:60400; CC Evidence={ECO:0000250}; CC Note=Binds 2 [Ni-Fe-S] clusters per homodimer. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- DOMAIN: Cluster B is an all-cysteinyl-liganded 4Fe4S cluster; CC cluster C is a mixed Ni-Fe-S cluster which appears to be the CC active site of CO oxidation. Cluster D is also an all-cysteinyl- CC liganded 4Fe4S cluster that bridges the two subunits of the CODH CC dimer (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the Ni-containing carbon monoxide CC dehydrogenase family. {ECO:0000305}. CC -!- CAUTION: This protein lacks the conserved Cys in position 45; it CC is replaced by a Tyr. It is therefore possible that the D-cluster CC is either altered or missing in this protein, which may not form CC homodimers. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98724.1; -; Genomic_DNA. DR PIR; H64390; H64390. DR ProteinModelPortal; Q58138; -. DR STRING; 243232.MJ_0728; -. DR EnsemblBacteria; AAB98724; AAB98724; MJ_0728. DR KEGG; mja:MJ_0728; -. DR eggNOG; arCOG02429; Archaea. DR eggNOG; COG1151; LUCA. DR InParanoid; Q58138; -. DR KO; K00198; -. DR OMA; TTHPIAK; -. DR PhylomeDB; Q58138; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:UniProtKB-EC. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0006091; P:generation of precursor metabolites and energy; IEA:InterPro. DR Gene3D; 1.20.1270.30; -; 1. DR Gene3D; 3.40.50.2030; -; 2. DR InterPro; IPR016101; CO_DH_a-bundle. DR InterPro; IPR010047; CODH. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF005023; CODH; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR01702; CO_DH_cata; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; Nickel; KW Oxidoreductase; Reference proteome. FT CHAIN 1 624 Carbon monoxide dehydrogenase. FT /FTId=PRO_0000157143. FT METAL 37 37 Iron-sulfur 1 (4Fe-4S); shared with FT dimeric partner. {ECO:0000250}. FT METAL 46 46 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 49 49 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 65 65 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 256 256 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 292 292 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 336 336 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 444 444 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 475 475 Nickel-iron-sulfur. {ECO:0000250}. FT METAL 516 516 Nickel-iron-sulfur. {ECO:0000250}. SQ SEQUENCE 624 AA; 67408 MW; FFB6AA3376D1050E CRC64; MKNCIAAIPE VKEMVEKAKL KGIETPHTRF PNQFPKCPYG LKGVYCILCA NGPCRITEKT PYGVCGATAD VIVARNLCRA VAAGTSCYVH CAENAARALL SAGKGEGSYE IRNEKKLKFL AKKLGFDANK DAKQLAVEVA EFILDDMYKP RWEKSELVPK LCPEKRLEVF EKLDILPGGA KGEIVDALTK TSTNLNSNPM DLLVHCLRLG LHAGFTGLLM TCWLNDILFG SPKITVVENG FSSVKPNNVN IMITGHQHAL IQPLCEAAME EDLIKMAKEA GADEIKIIGA TCNGQDMETR IAHLPESFVG YIANNFTTEP LVATGLIDAV VSEFNCTFHG LKFVAEKTKT KLICIDDMAY VEGAEYIPWE PENAKEKARE IIKKAIEAFK ERKGMQKDYY DEKVKSVVGV GEESLVEFLG GSVKPLIELI ASGKIKGVVG VVGCSNLASG GHDNIIVTLT KELIKRDILV LAGGCVNSPL KHAGLFDPAS AELAGENLKE VCKSLGIPPV LNFGACLSIA RIEQVAVAIA EELGVDIPDL PVAASAPQWL EEQALADATY AVDMGFTVHV SPVPFVTGSE LVTKVLTEAV EGLTGGKLIP EPNPYKAADL LEQTIMEKRK KLGI // ID COAD_METJA Reviewed; 147 AA. AC Q58436; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Phosphopantetheine adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647}; DE EC=2.7.7.3 {ECO:0000255|HAMAP-Rule:MF_00647}; DE AltName: Full=Dephospho-CoA pyrophosphorylase {ECO:0000255|HAMAP-Rule:MF_00647}; DE AltName: Full=Pantetheine-phosphate adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_00647}; DE Short=PPAT {ECO:0000255|HAMAP-Rule:MF_00647}; GN Name=coaD {ECO:0000255|HAMAP-Rule:MF_00647}; OrderedLocusNames=MJ1030; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reversibly transfers an adenylyl group from ATP to 4'- CC phosphopantetheine, yielding dephospho-CoA (dPCoA) and CC pyrophosphate. {ECO:0000255|HAMAP-Rule:MF_00647}. CC -!- CATALYTIC ACTIVITY: ATP + pantetheine 4'-phosphate = diphosphate + CC 3'-dephospho-CoA. {ECO:0000255|HAMAP-Rule:MF_00647}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 4/5. {ECO:0000255|HAMAP-Rule:MF_00647}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00647}. CC -!- SIMILARITY: Belongs to the eukaryotic CoaD family. CC {ECO:0000255|HAMAP-Rule:MF_00647}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99034.1; -; Genomic_DNA. DR PIR; E64428; E64428. DR ProteinModelPortal; Q58436; -. DR STRING; 243232.MJ_1030; -. DR EnsemblBacteria; AAB99034; AAB99034; MJ_1030. DR KEGG; mja:MJ_1030; -. DR eggNOG; arCOG01223; Archaea. DR eggNOG; COG1019; LUCA. DR InParanoid; Q58436; -. DR KO; K02201; -. DR OMA; FKPILAE; -. DR PhylomeDB; Q58436; -. DR UniPathway; UPA00241; UER00355. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central. DR GO; GO:0004595; F:pantetheine-phosphate adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IBA:GOC. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00647; PPAT_arch; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR023540; Ppantetheine_adenylTrfase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Coenzyme A biosynthesis; Complete proteome; Cytoplasm; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 147 Phosphopantetheine adenylyltransferase. FT /FTId=PRO_0000156320. SQ SEQUENCE 147 AA; 16669 MW; 999471C211B1B1C9 CRC64; MKVVVGGTFD ILHRGHKELL KFASSLGKLT IGITSDEFAK KYKTHKINDL KTRIENLKKF LDSIKADYEI KVINDAYGDA ITEDYDIIVV TQETLKNAEK INKIRESKGL KPLKIVIFKP ILAEDGKPIS TTRIRKGEID EEGRIIK // ID COFE_METJA Reviewed; 249 AA. AC Q58178; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Coenzyme F420:L-glutamate ligase; DE EC=6.3.2.31; DE EC=6.3.2.34; DE AltName: Full=Coenzyme F420-0:L-glutamate ligase; DE AltName: Full=Coenzyme F420-1:gamma-L-glutamate ligase; DE AltName: Full=F420:glutamyl ligase; GN Name=cofE; OrderedLocusNames=MJ0768; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND REACTION MECHANISM. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12911320; DOI=10.1021/bi034779b; RA Li H., Graupner M., Xu H., White R.H.; RT "CofE catalyzes the addition of two glutamates to F420-0 in F420 RT coenzyme biosynthesis in Methanococcus jannaschii."; RL Biochemistry 42:9771-9778(2003). CC -!- FUNCTION: Catalyzes the GTP-dependent successive addition of two CC L-glutamates to the L-lactyl phosphodiester of 7,8-didemethyl-8- CC hydroxy-5-deazariboflavin (F420-0) to form coenzyme F420-0- CC glutamyl-glutamate (F420-2), with a gamma-linkage between the two CC glutamates. Cannot use F420-2 as substrate to add more glutamates. CC Exhibits maximum activity with GTP, compared with UTP (66%) and CC dGTP (25%); with ATP, only F420-1 is observed as the product; CTP CC and TTP support no activity. {ECO:0000269|PubMed:12911320}. CC -!- CATALYTIC ACTIVITY: GTP + coenzyme F420-0 + L-glutamate = GDP + CC phosphate + coenzyme F420-1. {ECO:0000269|PubMed:12911320}. CC -!- CATALYTIC ACTIVITY: GTP + coenzyme F420-1 + L-glutamate = GDP + CC phosphate + coenzyme gamma-F420-2. {ECO:0000269|PubMed:12911320}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12911320}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:12911320}; CC Note=Binds 2 divalent metal cations per subunit. The ions could be CC magnesium and/or manganese. {ECO:0000269|PubMed:12911320}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000269|PubMed:12911320}; CC Note=Monovalent cation. The ion could be potassium. CC {ECO:0000269|PubMed:12911320}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.0 uM for F420-0 {ECO:0000269|PubMed:12911320}; CC KM=0.21 uM for F420-1 {ECO:0000269|PubMed:12911320}; CC Vmax=2.4 nmol/min/mg enzyme with F420-0 as substrate CC {ECO:0000269|PubMed:12911320}; CC Vmax=0.96 nmol/min/mg enzyme with F420-1 as substrate CC {ECO:0000269|PubMed:12911320}; CC pH dependence: CC Optimum pH is 8.5. {ECO:0000269|PubMed:12911320}; CC Temperature dependence: CC Optimum temperature is 60 degrees Celsius. Thermostable. Retains CC 70% of its activity after heating at 80 degrees Celsius for 15 CC minutes. {ECO:0000269|PubMed:12911320}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12911320}. CC -!- SIMILARITY: Belongs to the CofE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98763.1; -; Genomic_DNA. DR PIR; H64395; H64395. DR ProteinModelPortal; Q58178; -. DR STRING; 243232.MJ_0768; -. DR EnsemblBacteria; AAB98763; AAB98763; MJ_0768. DR KEGG; mja:MJ_0768; -. DR eggNOG; arCOG02714; Archaea. DR eggNOG; COG1478; LUCA. DR InParanoid; Q58178; -. DR KO; K12234; -. DR OMA; LTETRFG; -. DR PhylomeDB; Q58178; -. DR BioCyc; MetaCyc:MONOMER-12187; -. DR BRENDA; 6.3.2.31; 3260. DR BRENDA; 6.3.2.34; 3260. DR SABIO-RK; Q58178; -. DR UniPathway; UPA00071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043773; F:coenzyme F420-0 gamma-glutamyl ligase activity; IEA:InterPro. DR GO; GO:0052618; F:coenzyme F420-0:L-glutamate ligase activity; IDA:MENGO. DR GO; GO:0052619; F:coenzyme F420-1:gamma-L-glutamate ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009108; P:coenzyme biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0052645; P:F420-0 metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01258; F420_ligase_CofE; 1. DR InterPro; IPR008225; F420-0_g-glutamyl_ligase. DR InterPro; IPR002847; F420-0_gamma-glut_ligase-dom. DR InterPro; IPR023659; F420_ligase_CofE_arc. DR Pfam; PF01996; F420_ligase; 1. DR TIGRFAMs; TIGR01916; F420_cofE; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Potassium; Reference proteome. FT CHAIN 1 249 Coenzyme F420:L-glutamate ligase. FT /FTId=PRO_0000145789. FT NP_BIND 15 18 GTP. {ECO:0000250}. FT NP_BIND 45 46 GTP. {ECO:0000250}. FT NP_BIND 211 218 GTP. {ECO:0000250}. FT METAL 115 115 Divalent metal cation 1. {ECO:0000250}. FT METAL 155 155 Divalent metal cation 1. {ECO:0000250}. FT METAL 156 156 Divalent metal cation 2. {ECO:0000250}. FT METAL 213 213 Divalent metal cation 2. {ECO:0000250}. FT BINDING 50 50 GTP. {ECO:0000250}. FT BINDING 118 118 GTP. {ECO:0000250}. SQ SEQUENCE 249 AA; 27148 MW; A6B66FF4B52C15A2 CRC64; MIKEKRKVEV IGLELPIFKG GEQINLSELI AQYPIEDGDI IVIAETLISK LEGGVIDRDK IIPSKEAIEL AKKTGKDPKV VQVILDEAKE IVKVGKNFII TETKHGFVCA NSGVDESNIY KGIKILPKNP DESAEKIRKE IEKLTGKRVG VIISDSVGRP FRKGAVGIAI GVSGILALWD RKGEKDLFGR ELKTTEVAIA DELASMANVV MGEADEGIPV VIIRGANVPF GNGKGRDLIR PKEEDVFRN // ID COMB_METJA Reviewed; 224 AA. AC Q58540; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 2. DT 09-DEC-2015, entry version 101. DE RecName: Full=2-phosphosulfolactate phosphatase; DE EC=3.1.3.71; GN Name=comB; OrderedLocusNames=MJ1140; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11589710; DOI=10.1046/j.0014-2956.2001.02451.x; RA Graham D.E., Graupner M., Xu H., White R.H.; RT "Identification of coenzyme M biosynthetic 2-phosphosulfolactate RT phosphatase. A member of a new class of Mg2+-dependent acid RT phosphatases."; RL Eur. J. Biochem. 268:5176-5188(2001). CC -!- FUNCTION: Hydrolyzes both enantiomers of 2-phosphosulfolactate. CC Able to hydrolyze both enantiomers of 2-hydroxycarboxylic acids CC with pseudosymmetric centers of inversion. Specifically hydrolyzes CC (S)-phospholactate and (S)-phosphoglycerate. CC -!- CATALYTIC ACTIVITY: (2R)-2-phospho-3-sulfolactate + H(2)O = (2R)- CC 3-sulfolactate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ENZYME REGULATION: Inhibited by vanadate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 5.5.; CC Temperature dependence: CC Optimum temperature is 75 degrees Celsius.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis; CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 2/4. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the ComB family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99140.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99140.1; ALT_INIT; Genomic_DNA. DR PIR; C64442; C64442. DR ProteinModelPortal; Q58540; -. DR STRING; 243232.MJ_1140; -. DR EnsemblBacteria; AAB99140; AAB99140; MJ_1140. DR KEGG; mja:MJ_1140; -. DR eggNOG; arCOG04871; Archaea. DR eggNOG; COG2045; LUCA. DR InParanoid; Q58540; -. DR KO; K05979; -. DR OMA; MKISISF; -. DR PhylomeDB; Q58540; -. DR BioCyc; MetaCyc:MONOMER-2263; -. DR UniPathway; UPA00355; UER00470. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050532; F:2-phosphosulfolactate phosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1560.10; -; 1. DR HAMAP; MF_00490; ComB; 1. DR InterPro; IPR005238; ComB-like. DR InterPro; IPR027639; ComB_archaeal. DR InterPro; IPR022995; ProB_Pase_ComB. DR Pfam; PF04029; 2-ph_phosp; 1. DR SUPFAM; SSF142823; SSF142823; 1. DR TIGRFAMs; TIGR00298; TIGR00298; 1. PE 1: Evidence at protein level; KW Coenzyme M biosynthesis; Complete proteome; Hydrolase; Magnesium; KW Reference proteome. FT CHAIN 1 224 2-phosphosulfolactate phosphatase. FT /FTId=PRO_0000081459. SQ SEQUENCE 224 AA; 25114 MW; B981C5B5635404E9 CRC64; MITLCNRFTE YKCGNVAIVV DVLRASTTIT TLLSFIDEVY ITTSTSKKEN AIYIGERKGR KIEGFDFGNS PTEILANKDI IKERYENGEK VILTTTNGTR VLKSLDAEHI FIGAIVNAKY VAKAVEDFED VSLVPCHREN NFAIDDFIGC GVIAKYLNGE FDEFIKAALE LTKHDWMSLI LNSSSAENLK NLGYEKDVTF AILENSIDAV GIYKKDKSKV VRFK // ID COME_METJA Reviewed; 188 AA. AC P58416; Q57704; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Sulfopyruvate decarboxylase subunit beta {ECO:0000303|PubMed:10940029}; DE EC=4.1.1.79 {ECO:0000269|PubMed:10940029}; GN Name=comE {ECO:0000303|PubMed:10940029}; OrderedLocusNames=MJ0256; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME RP REGULATION, SUBUNIT, AND COFACTOR. RX PubMed=10940029; DOI=10.1128/JB.182.17.4862-4867.2000; RA Graupner M., Xu H., White R.H.; RT "Identification of the gene encoding sulfopyruvate decarboxylase, an RT enzyme involved in biosynthesis of coenzyme M."; RL J. Bacteriol. 182:4862-4867(2000). CC -!- FUNCTION: Involved in the biosynthesis of the coenzyme M (2- CC mercaptoethanesulfonic acid). Catalyzes the decarboxylation of CC sulfopyruvate to sulfoacetaldehyde. {ECO:0000269|PubMed:10940029}. CC -!- CATALYTIC ACTIVITY: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO(2). CC {ECO:0000269|PubMed:10940029}. CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000269|PubMed:10940029}; CC Note=Binds 1 thiamine pyrophosphate per subunit. CC {ECO:0000269|PubMed:10940029}; CC -!- ENZYME REGULATION: Inhibited by oxygen when heated in air at 80 CC degrees Celsius. The enzyme is reactivated by addition of CC dithionite. {ECO:0000269|PubMed:10940029}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.64 mM for 3-sulfopyruvate {ECO:0000269|PubMed:10940029}; CC Vmax=52 umol/min/mg enzyme {ECO:0000269|PubMed:10940029}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis; CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4. CC {ECO:0000305|PubMed:10940029}. CC -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 CC subunits beta. {ECO:0000269|PubMed:10940029}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. CC -!- CAUTION: The sequence corresponding to this entry was originally CC entered in Swiss-Prot as AC Q57704 in November 1997 and was CC deleted in July 1999 because TIGR removed the CDS for that ORF. We CC have recreated it because of the evidence (PubMed:10940029) that CC it really exists. {ECO:0000305|PubMed:10940029}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A64332; A64332. DR ProteinModelPortal; P58416; -. DR InParanoid; P58416; -. DR OMA; NCAYGST; -. DR PhylomeDB; P58416; -. DR BioCyc; MetaCyc:MONOMER-2266; -. DR UniPathway; UPA00355; UER00472. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IDA:UniProtKB. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR022494; Sulfopyruvate_deCO2ase_bsu. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR03846; sulfopy_beta; 1. PE 1: Evidence at protein level; KW Coenzyme M biosynthesis; Complete proteome; Decarboxylase; Lyase; KW Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 188 Sulfopyruvate decarboxylase subunit beta. FT /FTId=PRO_0000090839. SQ SEQUENCE 188 AA; 20980 MW; 52A6C91E2D43B97D CRC64; MYPKRIDIIK KIVENVGEKE IIVSNIGIPS KELYYVKDRE RNFYMLGSMG LASSIGLGLA LNCEDKVIVI DGDGSILMNL GSLSTIGYMN PKNYILVIID NSAYGSTGNQ KTHTGKNTNL EEIAKGCGLD TITTESLEEF EKEFKNALNE EKCKVIIAKT IPYNEKCSNI EIPPVVLKYR FMEAIKRS // ID COFH_METJA Reviewed; 359 AA. AC Q58826; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=FO synthase subunit 2; DE EC=2.5.1.77; DE AltName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase subunit 2; GN Name=cofH; OrderedLocusNames=MJ1431; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=14593448; DOI=10.1007/s00203-003-0614-8; RA Graham D.E., Xu H., White R.H.; RT "Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin RT synthase required for coenzyme F(420) biosynthesis."; RL Arch. Microbiol. 180:455-464(2003). CC -!- FUNCTION: Catalyzes the radical-mediated transfer of the CC hydroxybenzyl group from 4-hydroxyphenylpyruvate (HPP) to 5-amino- CC 6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 7,8-didemethyl- CC 8-hydroxy-5-deazariboflavin (FO). {ECO:0000269|PubMed:14593448}. CC -!- CATALYTIC ACTIVITY: 5-amino-6-(D-ribitylamino)uracil + 3-(4- CC hydroxyphenyl)pyruvate + 2 S-adenosyl-L-methionine + H(2)O = 7,8- CC didemethyl-8-hydroxy-5-deazariboflavin + 2 L-methionine + 2 5'- CC deoxyadenosine + oxalate + NH(3). {ECO:0000269|PubMed:14593448}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis. CC -!- SUBUNIT: Consists of two subunits, CofG and CofH. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofH family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99441.1; -; Genomic_DNA. DR PIR; F64478; F64478. DR ProteinModelPortal; Q58826; -. DR STRING; 243232.MJ_1431; -. DR EnsemblBacteria; AAB99441; AAB99441; MJ_1431. DR KEGG; mja:MJ_1431; -. DR eggNOG; arCOG00656; Archaea. DR eggNOG; COG1060; LUCA. DR InParanoid; Q58826; -. DR KO; K11781; -. DR OMA; MNEAEMI; -. DR PhylomeDB; Q58826; -. DR BioCyc; MetaCyc:MONOMER-12179; -. DR BRENDA; 2.5.1.77; 3260. DR UniPathway; UPA00072; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IDA:MENGO. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009108; P:coenzyme biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01612; FO_synth_sub2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR019940; CofH_family. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR020050; FO_synthase_su2. DR InterPro; IPR005244; FO_synthase_su2-like. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004762; CHP00423; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03551; F420_cofH; 1. DR TIGRFAMs; TIGR00423; TIGR00423; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 359 FO synthase subunit 2. FT /FTId=PRO_0000141718. FT METAL 59 59 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 63 63 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 66 66 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. SQ SEQUENCE 359 AA; 40806 MW; 10B91CA7D9E18E13 CRC64; MDPNKFREKE ISKKEALELF EDNEIIFELF KFADSLRREE VGDIVTYVVN RNINFTNICV GNCRFCAFRA NENDKHAYFL DIDEIAKRAV EAKKFGCTEV CIQGGLHPKI DTYYQAEILK AVHEATKPYG DIHIHAFSPM EVYFGAENAG LDIKEALKIL KENGLNSMPG TAAEILDDDI RAELCPNKIK TKEWIYIIKE AHKLGIPTTA TMMYGHIEEY KHWVNHLFII KEIQEETNGF TEFVPLSFMH KYAPIYKEGK AKAGATGIED LKVFAVSRII FKGLIKNIQA SWVKLGKKMV QVALRCGAND VGGTLIEESI SRSAGAEHGV YMSVEEIRDM IKRVGLIPKE RTTLYKILE // ID COBS_METJA Reviewed; 258 AA. AC Q58833; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Adenosylcobinamide-GDP ribazoletransferase {ECO:0000255|HAMAP-Rule:MF_00719}; DE EC=2.7.8.26 {ECO:0000255|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin synthase {ECO:0000255|HAMAP-Rule:MF_00719}; DE AltName: Full=Cobalamin-5'-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00719}; GN Name=cobS {ECO:0000255|HAMAP-Rule:MF_00719}; OrderedLocusNames=MJ1438; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Joins adenosylcobinamide-GDP and alpha-ribazole to CC generate adenosylcobalamin (Ado-cobalamin). Also synthesizes CC adenosylcobalamin 5'-phosphate from adenosylcobinamide-GDP and CC alpha-ribazole 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00719}. CC -!- CATALYTIC ACTIVITY: Adenosylcobinamide-GDP + alpha-ribazole = GMP CC + adenosylcobalamin. {ECO:0000255|HAMAP-Rule:MF_00719}. CC -!- CATALYTIC ACTIVITY: Adenosylcobinamide-GDP + alpha-ribazole 5'- CC phosphate = GMP + adenosylcobalamin 5'-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00719}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00719}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC adenosylcobalamin from cob(II)yrinate a,c-diamide: step 7/7. CC {ECO:0000255|HAMAP-Rule:MF_00719}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00719}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00719}. CC -!- SIMILARITY: Belongs to the CobS family. {ECO:0000255|HAMAP- CC Rule:MF_00719}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99447.1; -; Genomic_DNA. DR PIR; E64479; E64479. DR ProteinModelPortal; Q58833; -. DR STRING; 243232.MJ_1438; -. DR EnsemblBacteria; AAB99447; AAB99447; MJ_1438. DR KEGG; mja:MJ_1438; -. DR eggNOG; arCOG04338; Archaea. DR eggNOG; COG0368; LUCA. DR InParanoid; Q58833; -. DR KO; K02233; -. DR OMA; CACCGIP; -. DR PhylomeDB; Q58833; -. DR UniPathway; UPA00148; UER00238. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0051073; F:adenosylcobinamide-GDP ribazoletransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008818; F:cobalamin 5'-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00719; CobS; 1. DR InterPro; IPR003805; CobS. DR Pfam; PF02654; CobS; 1. DR TIGRFAMs; TIGR00317; cobS; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalamin biosynthesis; Complete proteome; Magnesium; KW Membrane; Reference proteome; Transferase; Transmembrane; KW Transmembrane helix. FT CHAIN 1 258 Adenosylcobinamide-GDP FT ribazoletransferase. FT /FTId=PRO_0000146910. FT TRANSMEM 35 55 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 56 76 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 113 133 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 137 157 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 175 195 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 198 218 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. FT TRANSMEM 238 258 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00719}. SQ SEQUENCE 258 AA; 28778 MW; 3C395D39A5DA1169 CRC64; MGITMFKEFK ALLSFFTRIP IYVEDFDFEN IANYFYLIIL IGYVFGIFSL ILGYIFSFLL PNFLSAVLIL FFIEYLNGFH HIDGLIDFGD GWMAVGDKRK KLMAMKDRYI GCGGVVFAIF FNLMAVISLS YILDINILYL LVGEVCAKLG MLSCSTFGNP LIEGTGRYFV KKADEKFLTI GIILSLPLLL IFSGIERKIV IIAIITTIIT GLCMAKIAKR HFGGVNGDVL GASNEITRVV VLLSIIASIK VFSIYLLG // ID CORA_METJA Reviewed; 317 AA. AC Q58439; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 103. DE RecName: Full=Cobalt/magnesium transport protein CorA; GN Name=corA; OrderedLocusNames=MJ1033; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND SUBCELLULAR LOCATION. RX PubMed=9573171; RA Smith R.L., Gottlieb E., Kucharski L.M., Maguire M.E.; RT "Functional similarity between archaeal and bacterial CorA magnesium RT transporters."; RL J. Bacteriol. 180:2788-2791(1998). RN [3] RP FUNCTION, ENZYME REGULATION, INHIBITION BY CATION HEXAAMMINES, AND RP SUBCELLULAR LOCATION. RX PubMed=10748031; DOI=10.1074/jbc.M001507200; RA Kucharski L.M., Lubbe W.J., Maguire M.E.; RT "Cation hexaammines are selective and potent inhibitors of the CorA RT magnesium transport system."; RL J. Biol. Chem. 275:16767-16773(2000). RN [4] RP SUBUNIT. RX PubMed=15231793; DOI=10.1128/JB.186.14.4605-4612.2004; RA Warren M.A., Kucharski L.M., Veenstra A., Shi L., Grulich P.F., RA Maguire M.E.; RT "The CorA Mg2+ transporter is a homotetramer."; RL J. Bacteriol. 186:4605-4612(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 1-317 IN COMPLEX WITH RP MAGNESIUM IONS, SUBCELLULAR LOCATION, TOPOLOGY, SUBUNIT, MOTIF, AND RP DOMAIN. RX PubMed=23091000; DOI=10.1073/pnas.1210076109; RA Guskov A., Nordin N., Reynaud A., Engman H., Lundback A.K., Jong A.J., RA Cornvik T., Phua T., Eshaghi S.; RT "Structural insights into the mechanisms of Mg2+ uptake, transport, RT and gating by CorA."; RL Proc. Natl. Acad. Sci. U.S.A. 109:18459-18464(2012). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY (21.60 ANGSTROMS), SUBCELLULAR RP LOCATION, SUBUNIT, AND DOMAIN. RX PubMed=26051127; DOI=10.1016/j.bbamem.2015.06.002; RA Cleverley R.M., Kean J., Shintre C.A., Baldock C., Derrick J.P., RA Ford R.C., Prince S.M.; RT "The Cryo-EM structure of the CorA channel from Methanocaldococcus RT jannaschii in low magnesium conditions."; RL Biochim. Biophys. Acta 1848:2206-2215(2015). CC -!- FUNCTION: Mediates influx of magnesium ions (PubMed:9573171, CC PubMed:10748031). Alternates between open and closed states. CC Activated by low cytoplasmic Mg(2+) levels. Inactive when CC cytoplasmic Mg(2+) levels are high. Can also mediate Co(2+) uptake CC (By similarity). {ECO:0000250|UniProtKB:Q9WZ31, CC ECO:0000269|PubMed:10748031, ECO:0000269|PubMed:9573171}. CC -!- ENZYME REGULATION: Inhibited by cation hexaammines. CC {ECO:0000269|PubMed:10748031}. CC -!- SUBUNIT: Homopentamer (PubMed:23091000, PubMed:26051127). In the CC absence of Mg(2+), interactions between subunits are weakened, and CC dimers, trimers and tetramers can be observed in vitro (By CC similarity). Was initially proposed to be a homotetramer, based on CC the cross-linking studies (PubMed:15231793). This is in CC contradiction with current 3D-structures that clearly show it is a CC homopentamer (PubMed:23091000, PubMed:26051127). CC {ECO:0000250|UniProtKB:Q9WZ31, ECO:0000269|PubMed:15231793, CC ECO:0000269|PubMed:23091000, ECO:0000269|PubMed:26051127}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:10748031, CC ECO:0000305|PubMed:26051127, ECO:0000305|PubMed:9573171}; Multi- CC pass membrane protein {ECO:0000269|PubMed:23091000, CC ECO:0000269|PubMed:26051127}. CC -!- DOMAIN: The central ion permeation pathway is formed by the first CC transmembrane domain from each of the five subunits. Mg(2+) CC binding strengthens interactions between subunits and leads to the CC formation of a symmetrical homopentamer surrounding a closed ion CC permeation pathway (PubMed:23091000). Low cytoplasmic Mg(2+) CC concentrations trigger both a conformation change within each CC subunit and a loosening of the interactions between subunits. This CC results in an open ion conduction pathway. In addition, this CC results in a less symmetrical shape of the whole complex CC (PubMed:26051127). {ECO:0000269|PubMed:23091000, CC ECO:0000269|PubMed:26051127, ECO:0000305}. CC -!- SIMILARITY: Belongs to the CorA metal ion transporter (MIT) CC (TC 1.A.35) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99037.1; -; Genomic_DNA. DR PIR; H64428; H64428. DR PDB; 4CY4; EM; 21.60 A; A/B/C/D/E=1-317. DR PDB; 4EGW; X-ray; 2.50 A; A/B=1-258. DR PDB; 4EV6; X-ray; 3.20 A; A/B/C/D/E=1-317. DR PDBsum; 4CY4; -. DR PDBsum; 4EGW; -. DR PDBsum; 4EV6; -. DR ProteinModelPortal; Q58439; -. DR DIP; DIP-60086N; -. DR STRING; 243232.MJ_1033; -. DR TCDB; 1.A.35.3.1; the cora metal ion transporter (mit) family. DR EnsemblBacteria; AAB99037; AAB99037; MJ_1033. DR KEGG; mja:MJ_1033; -. DR eggNOG; arCOG02265; Archaea. DR eggNOG; COG0598; LUCA. DR InParanoid; Q58439; -. DR KO; K03284; -. DR OMA; NIKMNQI; -. DR PhylomeDB; Q58439; -. DR BRENDA; 3.6.3.2; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015087; F:cobalt ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015095; F:magnesium ion transmembrane transporter activity; IEA:InterPro. DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0098655; P:cation transmembrane transport; IBA:GO_Central. DR GO; GO:0015693; P:magnesium ion transport; IEA:InterPro. DR InterPro; IPR004488; Mg/Co-transport_prot_CorA. DR InterPro; IPR002523; MgTranspt_CorA/ZnTranspt_ZntB. DR Pfam; PF01544; CorA; 1. DR TIGRFAMs; TIGR00383; corA; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Ion transport; KW Magnesium; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 317 Cobalt/magnesium transport protein CorA. FT /FTId=PRO_0000201534. FT TOPO_DOM 1 258 Cytoplasmic. {ECO:0000305}. FT TRANSMEM 259 279 Helical. {ECO:0000269|PubMed:23091000}. FT TOPO_DOM 280 290 Extracellular. {ECO:0000305}. FT TRANSMEM 291 311 Helical. {ECO:0000269|PubMed:23091000}. FT TOPO_DOM 312 317 Cytoplasmic. {ECO:0000305}. FT MOTIF 278 280 Probable selectivity filter. FT {ECO:0000305|PubMed:23091000}. FT SITE 254 254 Essential for ion permeation. FT {ECO:0000250|UniProtKB:Q9WZ31}. FT SITE 260 260 Important for closing the ion permeation FT pathway in the closed state. FT {ECO:0000269|PubMed:23091000}. FT SITE 261 261 Threonine that confers selectivity for FT Co(2+) transport. FT {ECO:0000250|UniProtKB:Q9WZ31}. FT STRAND 6 11 {ECO:0000244|PDB:4EGW}. FT TURN 12 14 {ECO:0000244|PDB:4EGW}. FT STRAND 25 27 {ECO:0000244|PDB:4EGW}. FT STRAND 29 35 {ECO:0000244|PDB:4EGW}. FT HELIX 38 48 {ECO:0000244|PDB:4EGW}. FT HELIX 52 58 {ECO:0000244|PDB:4EGW}. FT STRAND 66 68 {ECO:0000244|PDB:4EGW}. FT STRAND 71 82 {ECO:0000244|PDB:4EGW}. FT STRAND 84 86 {ECO:0000244|PDB:4EGW}. FT STRAND 88 97 {ECO:0000244|PDB:4EGW}. FT STRAND 100 107 {ECO:0000244|PDB:4EGW}. FT HELIX 110 121 {ECO:0000244|PDB:4EGW}. FT STRAND 125 127 {ECO:0000244|PDB:4EGW}. FT TURN 129 133 {ECO:0000244|PDB:4EGW}. FT HELIX 134 164 {ECO:0000244|PDB:4EGW}. FT TURN 165 167 {ECO:0000244|PDB:4EGW}. FT HELIX 171 203 {ECO:0000244|PDB:4EGW}. FT HELIX 211 248 {ECO:0000244|PDB:4EGW}. FT HELIX 269 276 {ECO:0000244|PDB:4EV6}. FT HELIX 292 312 {ECO:0000244|PDB:4EV6}. FT TURN 313 315 {ECO:0000244|PDB:4EV6}. SQ SEQUENCE 317 AA; 37142 MW; 552A0B3738131E0D CRC64; MITVIAIAKD GSIVEPKLDE ISFEDYRLIW IDCYDPKDEE LYKLSKKIGI SVSDLQIGLD EQEIPRVEED EDFYLIIYKA PLFEEDITTT SLGIYIKNNL LLTIHSDKIK AIGRLHKLIS TKKPRIVFER GIGFLLYHIL NEITRSYSRI LMNLEDELEE LEDKLLAGYD REVMEKILGL RKTLVYFHKS LIANRDVLVL LKRKYLPITT KEDRENFEDL YYDTLQLIDM SATYREVLTS MMDITLSLEN IKMNQIMKIL TMVTTIFAVP MWITGIYGMN FSYLPLANNP QGFWLVMALM VVIIMIFVYI FRRSGWI // ID COBY_METJA Reviewed; 196 AA. AC Q58517; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Adenosylcobinamide-phosphate guanylyltransferase; DE Short=AdoCbi-P guanylyltransferase; DE EC=2.7.7.62; GN Name=cobY; OrderedLocusNames=MJ1117; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A NUCLEOTIDYLTRANSFERASE, AND KINETIC PARAMETERS. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18260642; DOI=10.1021/bi702475t; RA Grochowski L.L., Xu H., White R.H.; RT "Identification and characterization of the 2-phospho-L-lactate RT guanylyltransferase involved in coenzyme F420 biosynthesis."; RL Biochemistry 47:3033-3037(2008). RN [3] RP FUNCTION IN ADENOSYLCOBALAMIN BIOSYNTHESIS, CATALYTIC ACTIVITY, RP GTP-BINDING, SUBSTRATE SPECIFICITY, SUBUNIT, ORDER OF SUBSTRATE RP BINDING, AND KINETIC PARAMETERS. RX PubMed=19489548; DOI=10.1021/bi8023114; RA Otte M.M., Escalante-Semerena J.C.; RT "Biochemical characterization of the GTP:adenosylcobinamide-phosphate RT guanylyltransferase (CobY) enzyme of the hyperthermophilic archaeon RT Methanocaldococcus jannaschii."; RL Biochemistry 48:5882-5889(2009). CC -!- FUNCTION: Guanylyltransferase that catalyzes the synthesis of CC adenosylcobinamide-GDP (AdoCbi-GDP) from adenosylcobinamide- CC phosphate (AdoCbi-P) and GTP. Is involved in adenosylcobalamin CC biosynthesis. Binds one GTP per dimer. Can not use other NTPs or CC GDP. Does not display AdoCbi kinase activity. Is also able to CC catalyze the condensation of 2-phospho-L-lactate (LP) with GTP in CC vitro to form PPi and (2S)-lactyl-2-diphospho-5'-guanosine (LPPG), CC but is much less efficient than CofC, the presumed enzyme CC catalyzing this reaction in vivo. {ECO:0000269|PubMed:18260642, CC ECO:0000269|PubMed:19489548}. CC -!- CATALYTIC ACTIVITY: GTP + adenosylcobinamide phosphate = CC diphosphate + adenosylcobinamide-GDP. CC {ECO:0000269|PubMed:19489548}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=18.4 uM for adenosylcobinamide phosphate CC {ECO:0000269|PubMed:18260642, ECO:0000269|PubMed:19489548}; CC KM=2.4 uM for GTP {ECO:0000269|PubMed:18260642, CC ECO:0000269|PubMed:19489548}; CC KM=6 mM for (2S)-2-phospholactate {ECO:0000269|PubMed:18260642, CC ECO:0000269|PubMed:19489548}; CC Vmax=115 nmol/min/mg enzyme with (2S)-2-phospholactate as CC substrate {ECO:0000269|PubMed:18260642, CC ECO:0000269|PubMed:19489548}; CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:19489548}. CC -!- MISCELLANEOUS: Binds GTP first, before binding AdoCbi-P. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99118.1; -; Genomic_DNA. DR PIR; D64439; D64439. DR PDB; 2MZB; NMR; -; A=1-196. DR PDB; 3RSB; X-ray; 2.80 A; A/B/C/D=1-196. DR PDBsum; 2MZB; -. DR PDBsum; 3RSB; -. DR ProteinModelPortal; Q58517; -. DR STRING; 243232.MJ_1117; -. DR EnsemblBacteria; AAB99118; AAB99118; MJ_1117. DR KEGG; mja:MJ_1117; -. DR eggNOG; arCOG01871; Archaea. DR eggNOG; COG2266; LUCA. DR InParanoid; Q58517; -. DR KO; K19712; -. DR OMA; FNINTKD; -. DR PhylomeDB; Q58517; -. DR BRENDA; 2.7.7.62; 3260. DR SABIO-RK; Q58517; -. DR UniPathway; UPA00148; -. DR EvolutionaryTrace; Q58517; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008820; F:cobinamide phosphate guanylyltransferase activity; IDA:UniProtKB. DR GO; GO:0005525; F:GTP binding; IDA:UniProtKB. DR GO; GO:0016779; F:nucleotidyltransferase activity; IDA:UniProtKB. DR GO; GO:0009236; P:cobalamin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005245; CHP00454. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR00454; TIGR00454; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalamin biosynthesis; Complete proteome; GTP-binding; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 196 Adenosylcobinamide-phosphate FT guanylyltransferase. FT /FTId=PRO_0000107174. FT STRAND 2 7 {ECO:0000244|PDB:3RSB}. FT HELIX 13 16 {ECO:0000244|PDB:3RSB}. FT HELIX 19 21 {ECO:0000244|PDB:3RSB}. FT HELIX 29 38 {ECO:0000244|PDB:3RSB}. FT STRAND 39 41 {ECO:0000244|PDB:3RSB}. FT STRAND 45 49 {ECO:0000244|PDB:3RSB}. FT HELIX 54 63 {ECO:0000244|PDB:3RSB}. FT TURN 64 68 {ECO:0000244|PDB:3RSB}. FT STRAND 69 72 {ECO:0000244|PDB:3RSB}. FT TURN 86 90 {ECO:0000244|PDB:3RSB}. FT STRAND 95 99 {ECO:0000244|PDB:3RSB}. FT STRAND 102 104 {ECO:0000244|PDB:3RSB}. FT HELIX 107 121 {ECO:0000244|PDB:3RSB}. FT STRAND 129 135 {ECO:0000244|PDB:3RSB}. FT TURN 136 138 {ECO:0000244|PDB:3RSB}. FT STRAND 146 157 {ECO:0000244|PDB:3RSB}. FT STRAND 166 170 {ECO:0000244|PDB:3RSB}. FT HELIX 181 189 {ECO:0000244|PDB:3RSB}. SQ SEQUENCE 196 AA; 21746 MW; 6E5F4F07A0F509D4 CRC64; MDALIMAGGK GTRMGGVEKP LIKLCGRCLI DYVVSPLLKS KVNNIFIATS PNTPKTKEYI NSAYKDYKNI VVIDTSGKGY IEDLNECIGY FSEPFLVVSS DLINLKSKII NSIVDYFYCI KAKTPDVEAL AVMIPKEKYP NPSIDFNGLV PAGINVVSPK HGYQKEEIMV IDELIFNINT KDDLKLAEML LKKDGL // ID COABC_METJA Reviewed; 403 AA. AC Q58323; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Coenzyme A biosynthesis bifunctional protein CoaBC; DE AltName: Full=DNA/pantothenate metabolism flavoprotein; DE Includes: DE RecName: Full=Phosphopantothenoylcysteine decarboxylase; DE Short=PPCDC; DE EC=4.1.1.36; DE AltName: Full=CoaC; DE Includes: DE RecName: Full=Phosphopantothenate--cysteine ligase; DE EC=6.3.2.5; DE AltName: Full=CoaB; DE AltName: Full=PPC synthetase; DE Short=PPCS; DE AltName: Full=Phosphopantothenoylcysteine synthase; GN Name=coaBC; OrderedLocusNames=MJ0913; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes two steps in the biosynthesis of coenzyme A. CC In the first step cysteine is conjugated to 4'-phosphopantothenate CC to form 4-phosphopantothenoylcysteine, in the latter compound is CC decarboxylated to form 4'-phosphopantotheine (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: N-((R)-4'-phosphopantothenoyl)-L-cysteine = CC pantotheine 4'-phosphate + CO(2). CC -!- CATALYTIC ACTIVITY: CTP + (R)-4'-phosphopantothenate + L-cysteine CC = CMP + diphosphate + N-((R)-4'-phosphopantothenoyl)-L-cysteine. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 2/5. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis; CoA from CC (R)-pantothenate: step 3/5. CC -!- SUBUNIT: Homododecamer, the CoaB domains form homodimers. CC -!- SIMILARITY: In the N-terminal section; belongs to the HFCD (homo- CC oligomeric flavin containing Cys decarboxylase) superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the PPC CC synthetase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98918.1; -; Genomic_DNA. DR PIR; A64414; A64414. DR ProteinModelPortal; Q58323; -. DR STRING; 243232.MJ_0913; -. DR EnsemblBacteria; AAB98918; AAB98918; MJ_0913. DR KEGG; mja:MJ_0913; -. DR eggNOG; arCOG01704; Archaea. DR eggNOG; COG0452; LUCA. DR InParanoid; Q58323; -. DR KO; K13038; -. DR OMA; TGYYFAR; -. DR PhylomeDB; Q58323; -. DR UniPathway; UPA00241; UER00353. DR UniPathway; UPA00241; UER00354. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004632; F:phosphopantothenate--cysteine ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004633; F:phosphopantothenoylcysteine decarboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0015941; P:pantothenate catabolic process; IEA:InterPro. DR Gene3D; 3.40.50.10300; -; 1. DR Gene3D; 3.40.50.1950; -; 1. DR InterPro; IPR005252; CoaBC. DR InterPro; IPR007085; DNA/pantothenate-metab_flavo_C. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF04127; DFP; 1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF102645; SSF102645; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00521; coaBC_dfp; 1. PE 3: Inferred from homology; KW Complete proteome; Decarboxylase; Flavoprotein; FMN; Ligase; Lyase; KW Reference proteome. FT CHAIN 1 403 Coenzyme A biosynthesis bifunctional FT protein CoaBC. FT /FTId=PRO_0000232696. FT REGION 1 195 Phosphopantothenoylcysteine FT decarboxylase. FT REGION 196 403 Phosphopantothenate--cysteine ligase. SQ SEQUENCE 403 AA; 45671 MW; B8B51AA81A115B94 CRC64; MISEIMHPTK LLKGTKSKLL ENKKILVAVT SSIAAIETPK LMRELIRHGA EVYCIITEET KKIIGKEALK FGCGNEVYEE ITGDIEHILL YNECDCLLIY PATANIISKI NLGIADNIVN TTALMFFGNK PIFIVPAMHE NMFNAIKRHI DKLKEKDKIY IISPKFEEGK AKVANIEDVV KAVIEKIGNN LKKEGNRVLI LNGGTVEFID KVRVISNLSS GKMGVALAEA FCKEGFYVEV ITAMGLEPPY YIKNHKVLTA KEMLNKAIEL AKDFDIIISS AAISDFTVES FEGKLSSEEE LILKLKRNPK VLEELRRIYK DKVIIGFKAE YNLDEKELIN RAKERLNKYN LNMIIANDLS KHYFGDDYIE VYIITKYEVE KISGSKKEIS ERIVEKVKKL VKS // ID COFD_METJA Reviewed; 311 AA. AC Q58653; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=2-phospho-L-lactate transferase; DE EC=2.7.8.28; DE AltName: Full=LPPG:FO 2-phospho-L-lactate transferase; GN Name=cofD; OrderedLocusNames=MJ1256; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CHARACTERIZATION, SUBUNIT, AND MUTAGENESIS OF SER-211. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11888293; DOI=10.1021/bi011937v; RA Graupner M., Xu H., White R.H.; RT "Characterization of the 2-phospho-L-lactate transferase enzyme RT involved in coenzyme F(420) biosynthesis in Methanococcus RT jannaschii."; RL Biochemistry 41:3754-3761(2002). CC -!- FUNCTION: Catalyzes the transfer of the 2-phospholactate moiety CC from lactyl (2) diphospho-(5')guanosine (LPPG) to 7,8-didemethyl- CC 8-hydroxy-5-deazariboflavin (FO) with the formation of the L- CC lactyl phosphodiester of 7,8-didemethyl-8-hydroxy-5- CC deazariboflavin (F420-0) and GMP. To a lesser extent CofD also CC catalyzes a number of additional reactions that include the CC formation of FO-P, when the enzyme is incubated with FO and GDP, CC GTP, pyrophosphate, or tripolyphosphate and the hydrolysis of CC F420-0 to FO. {ECO:0000269|PubMed:11888293}. CC -!- CATALYTIC ACTIVITY: (2S)-lactyl-2-diphospho-5'-guanosine + 7,8- CC didemethyl-8-hydroxy-5-deazariboflavin = guanosine 5'-phosphate + CC coenzyme F420-0. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ENZYME REGULATION: Inhibited by EDTA. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=32 uM for FO; CC KM=17 uM for LPPG; CC KM=515 uM for LPPA; CC Vmax=1.4 umol/min/mg enzyme with LPPG as substrate; CC Vmax=0.1 umol/min/mg enzyme with LPPA as substrate; CC Temperature dependence: CC Optimum temperature is about 37 degrees Celsius. Thermostable. CC Still fully active after heating at 80 degrees Celsius for 24 CC hours. Activity begins to decrease after heating at 98 degrees CC Celsius for 30 minutes. Inactive after heating at 110 degrees CC Celsius for 30 minutes.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11888293}. CC -!- SIMILARITY: Belongs to the CofD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99260.1; -; Genomic_DNA. DR PIR; G64456; G64456. DR ProteinModelPortal; Q58653; -. DR STRING; 243232.MJ_1256; -. DR EnsemblBacteria; AAB99260; AAB99260; MJ_1256. DR KEGG; mja:MJ_1256; -. DR eggNOG; arCOG04395; Archaea. DR eggNOG; COG0391; LUCA. DR InParanoid; Q58653; -. DR KO; K11212; -. DR OMA; HFQEYWV; -. DR PhylomeDB; Q58653; -. DR BioCyc; MetaCyc:MONOMER-12181; -. DR BRENDA; 2.7.8.28; 3260. DR SABIO-RK; Q58653; -. DR UniPathway; UPA00071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043743; F:LPPG:FO 2-phospho-L-lactate transferase activity; IDA:MENGO. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0016780; F:phosphotransferase activity, for other substituted phosphate groups; IEA:InterPro. DR GO; GO:0009108; P:coenzyme biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01257; CofD; 1. DR InterPro; IPR002882; CofD/UPF0052. DR InterPro; IPR010115; P-lactate_Trfase. DR Pfam; PF01933; UPF0052; 1. DR TIGRFAMs; TIGR01819; F420_cofD; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Reference proteome; Transferase. FT CHAIN 1 311 2-phospho-L-lactate transferase. FT /FTId=PRO_0000145772. FT MUTAGEN 211 211 S->A: No change in activity. FT {ECO:0000269|PubMed:11888293}. SQ SEQUENCE 311 AA; 34599 MW; A2830E42C824F64F CRC64; MIFVITVLSG GTGTPKLLQG LKRVVNNEEL AVIVNTGEDT WIGDLYLSPD VDTVLYTLAD LINEETWYGV KEDTFYTHEQ LKNLGFDEVL RIGDKDRALK MHKTYYLKRG HKLSEVVDME KVALGIKAKV IPMTDDRVET KILAKVDGKV DLLKFHDFWV KRKGDVEVLD VIYENSLYAK PCEKAVEAIK NSDLVIIGPS NPITSIGPIL SLNGIKELLK DKKVVVVSPI VGNSAVSGPA GKLMKAKGYD VSVKGIYEFY KDIVDVLVID NVDKEIAKEI PCEVLITNTI MKTLDDKVRL AKNIIEFCGS L // ID COFF_METJA Reviewed; 288 AA. AC Q58407; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 26-APR-2005, sequence version 2. DT 11-NOV-2015, entry version 89. DE RecName: Full=Coenzyme gamma-F420-2:alpha-L-glutamate ligase; DE EC=6.3.2.32; GN Name=cofF; OrderedLocusNames=MJ1001; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, COFACTOR, ENZYME RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12909715; DOI=10.1073/pnas.1733391100; RA Li H., Xu H., Graham D.E., White R.H.; RT "Glutathione synthetase homologs encode alpha-L-glutamate ligases for RT methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9785-9790(2003). CC -!- FUNCTION: Catalyzes the ATP-dependent addition of one alpha-linked CC L-glutamate molecule to coenzyme gamma-F420-2, producing alpha- CC F420-3, the major form of coenzyme F420 found in M.jannaschii. CC Thus, caps the gamma-polyglutamate tail of coenzyme F420 with a CC terminal alpha-linked glutamate. Prefers ATP to other purine CC nucleotide triphosphates; GTP gives about 25% of the activity CC observed with ATP. Can not catalyze the addition of the following CC amino acids or analogs: D-glutamate, beta-glutamate, L-aspartate, CC L-glutamine, L-alpha-aminoadipate, or D,L-2-amino-4-phosphono- CC butyrate. {ECO:0000269|PubMed:12909715}. CC -!- CATALYTIC ACTIVITY: ATP + coenzyme gamma-F420-2 + L-glutamate = CC ADP + phosphate + coenzyme alpha-F420-3. CC {ECO:0000269|PubMed:12909715}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:12909715}; CC Note=Binds 2 manganese ions per subunit. CC {ECO:0000269|PubMed:12909715}; CC -!- ENZYME REGULATION: Inhibited by KCl. CC {ECO:0000269|PubMed:12909715}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.2 uM for coenzyme F420-2 {ECO:0000269|PubMed:12909715}; CC Vmax=0.72 nmol/min/mg enzyme {ECO:0000269|PubMed:12909715}; CC Temperature dependence: CC Thermostable. {ECO:0000269|PubMed:12909715}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:12909715}. CC -!- SIMILARITY: Belongs to the RimK family. CofF subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99004.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99004.1; ALT_INIT; Genomic_DNA. DR PIR; H64424; H64424. DR ProteinModelPortal; Q58407; -. DR STRING; 243232.MJ_1001; -. DR EnsemblBacteria; AAB99004; AAB99004; MJ_1001. DR KEGG; mja:MJ_1001; -. DR eggNOG; arCOG01589; Archaea. DR eggNOG; COG0189; LUCA. DR InParanoid; Q58407; -. DR KO; K14940; -. DR OMA; MNGYIMG; -. DR PhylomeDB; Q58407; -. DR BioCyc; MetaCyc:MONOMER-12190; -. DR BRENDA; 6.3.2.32; 3260. DR SABIO-RK; Q58407; -. DR UniPathway; UPA00071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043774; F:coenzyme F420-2 alpha-glutamyl ligase activity; IDA:MENGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR031039; F420_CofF. DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX. DR Pfam; PF08443; RimK; 1. DR TIGRFAMs; TIGR04443; F420_CofF; 1. DR TIGRFAMs; TIGR00768; rimK_fam; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Ligase; Manganese; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 288 Coenzyme gamma-F420-2:alpha-L-glutamate FT ligase. FT /FTId=PRO_0000205498. FT DOMAIN 101 287 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 173 186 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT METAL 245 245 Manganese 1. {ECO:0000250}. FT METAL 257 257 Manganese 1. {ECO:0000250}. FT METAL 257 257 Manganese 2. {ECO:0000250}. FT METAL 259 259 Manganese 2. {ECO:0000250}. FT BINDING 139 139 ATP. {ECO:0000250}. FT BINDING 202 202 ATP. {ECO:0000250}. SQ SEQUENCE 288 AA; 33112 MW; 08443376FDC5E61D CRC64; MVKITILSPE GRSCSVWSLK NEIEKLGAKC DIFLLSSPEN LMSHDFKLET DLIHSRCGIG DYFDRLTLYS WQFINALEVE GCRFINPIKT LYLTSDKFKC IKLLAKNKIK TPKTALIRDY EDAVKFIEKY NLRFPVVIKN SFSKCGLKVF MARNYDELKQ LTKNAIWEGK LIQEFIDFKE NDLYRDMRIL VVDGEVVGGY RRVSRDFRTN LYLGNVVEKL NIDEELEELA LKCADLSEAV ILGVDILPTK DNYYVIELNS SPGTKGFRDI GINADKKIAE ALVRYAKS // ID COFG_METJA Reviewed; 358 AA. AC Q57888; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-MAR-2009, sequence version 2. DT 11-MAY-2016, entry version 96. DE RecName: Full=FO synthase subunit 1; DE EC=2.5.1.77; DE AltName: Full=7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase subunit 1; GN Name=cofG; OrderedLocusNames=MJ0446; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND CHARACTERIZATION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=14593448; DOI=10.1007/s00203-003-0614-8; RA Graham D.E., Xu H., White R.H.; RT "Identification of the 7,8-didemethyl-8-hydroxy-5-deazariboflavin RT synthase required for coenzyme F(420) biosynthesis."; RL Arch. Microbiol. 180:455-464(2003). CC -!- FUNCTION: Catalyzes the radical-mediated transfer of the CC hydroxybenzyl group from 4-hydroxyphenylpyruvate (HPP) to 5-amino- CC 6-ribitylamino-2,4(1H,3H)-pyrimidinedione to form 7,8-didemethyl- CC 8-hydroxy-5-deazariboflavin (FO). {ECO:0000269|PubMed:14593448}. CC -!- CATALYTIC ACTIVITY: 5-amino-6-(D-ribitylamino)uracil + 3-(4- CC hydroxyphenyl)pyruvate + 2 S-adenosyl-L-methionine + H(2)O = 7,8- CC didemethyl-8-hydroxy-5-deazariboflavin + 2 L-methionine + 2 5'- CC deoxyadenosine + oxalate + NH(3). {ECO:0000269|PubMed:14593448}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F0 biosynthesis. CC -!- SUBUNIT: Consists of two subunits, CofG and CofH. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. CofG family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98436.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98436.1; ALT_INIT; Genomic_DNA. DR PIR; F64355; F64355. DR ProteinModelPortal; Q57888; -. DR STRING; 243232.MJ_0446; -. DR EnsemblBacteria; AAB98436; AAB98436; MJ_0446. DR KEGG; mja:MJ_0446; -. DR eggNOG; arCOG00657; Archaea. DR eggNOG; COG1060; LUCA. DR InParanoid; Q57888; -. DR KO; K11780; -. DR OMA; LTTACRY; -. DR PhylomeDB; Q57888; -. DR BioCyc; MetaCyc:MONOMER-12178; -. DR BRENDA; 2.5.1.77; 3260. DR UniPathway; UPA00072; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0044689; F:7,8-didemethyl-8-hydroxy-5-deazariboflavin synthase activity; IDA:MENGO. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009108; P:coenzyme biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01611; FO_synth_sub1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR019939; CofG_family. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03550; F420_cofG; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 358 FO synthase subunit 1. FT /FTId=PRO_0000147764. FT METAL 49 49 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 53 53 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 56 56 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. SQ SEQUENCE 358 AA; 41582 MW; F10602568AEB449F CRC64; MISREEAINF LNSTSSKDIL DKLAQINNTF KREYITYSKN VFIPLSKWCR NKCGYCIFRE DKPSLMKPNE VKEILLKGDR LGCREALFTF GEHVDENKEI KEQLKSMGYD NILEYLYDLE EWTLNNTSLL PHTNCGILNY DELKMLKDVN ASMGLMLENA SERLMNTIAH KHSPGKHPKL RIEMIENAGK LKIPFTTGLL IGIGETNEEI VDSLFKIKEI HEKYGHIQEV IIQNFRAKKG IPMENFKEPS PIKMLKVIIL AKLILDDISI QIPPNLNRET GQLFLLAGVD DWGGVSPLTR DYVNPEAEWP EIKELREWTE ELGLKLKMRL PVYDKYISEE WLSEKVYNKI IEMGWLKE // ID CSM3_METJA Reviewed; 248 AA. AC Q59063; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=CRISPR type III-associated RAMP protein Csm3; DE AltName: Full=CRISPR type III-A/Mtube-associated RAMP protein Csm3; GN Name=csm3; OrderedLocusNames=MJ1669; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm3 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99689.1; -; Genomic_DNA. DR PIR; C64508; C64508. DR PDB; 4QTS; X-ray; 3.10 A; C/D=1-248. DR PDBsum; 4QTS; -. DR ProteinModelPortal; Q59063; -. DR STRING; 243232.MJ_1669; -. DR EnsemblBacteria; AAB99689; AAB99689; MJ_1669. DR KEGG; mja:MJ_1669; -. DR eggNOG; arCOG02658; Archaea. DR eggNOG; COG1337; LUCA. DR InParanoid; Q59063; -. DR KO; K09002; -. DR OMA; KFENTIN; -. DR PhylomeDB; Q59063; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR013412; CRISPR-assoc_RAMP_Csm3. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR02582; cas7_TM1809; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Complete proteome; KW Reference proteome. FT CHAIN 1 248 CRISPR type III-associated RAMP protein FT Csm3. FT /FTId=PRO_0000107466. FT STRAND 8 20 {ECO:0000244|PDB:4QTS}. FT STRAND 40 42 {ECO:0000244|PDB:4QTS}. FT STRAND 48 50 {ECO:0000244|PDB:4QTS}. FT HELIX 52 65 {ECO:0000244|PDB:4QTS}. FT STRAND 84 86 {ECO:0000244|PDB:4QTS}. FT HELIX 87 91 {ECO:0000244|PDB:4QTS}. FT HELIX 97 99 {ECO:0000244|PDB:4QTS}. FT STRAND 106 108 {ECO:0000244|PDB:4QTS}. FT STRAND 111 113 {ECO:0000244|PDB:4QTS}. FT STRAND 156 165 {ECO:0000244|PDB:4QTS}. FT TURN 168 170 {ECO:0000244|PDB:4QTS}. FT HELIX 171 185 {ECO:0000244|PDB:4QTS}. FT STRAND 189 192 {ECO:0000244|PDB:4QTS}. FT STRAND 195 197 {ECO:0000244|PDB:4QTS}. FT STRAND 200 211 {ECO:0000244|PDB:4QTS}. FT HELIX 212 215 {ECO:0000244|PDB:4QTS}. FT HELIX 219 221 {ECO:0000244|PDB:4QTS}. FT STRAND 228 230 {ECO:0000244|PDB:4QTS}. FT HELIX 231 233 {ECO:0000244|PDB:4QTS}. FT HELIX 234 239 {ECO:0000244|PDB:4QTS}. SQ SEQUENCE 248 AA; 28159 MW; C68C09C5FC256BB1 CRC64; MENLTLKGKV ILEGIIELET GMHIGGTKET LKIGGTDNPV IRDAFGRILI PGSSLKGKIR ALLERKDGKY KEDGRGNYLP HDCGECEICK IFGPHDSKNI KEPVRVIVRD AYLQPEENKK DYDYLEIKVE NTIDRLKGTT IKGGIRNMER VVAGSKFKFE VVFNIYKESD KELIKKFIEG MKLLEDDYLG GSGSRGYGKI KFRDIKLICK PKEYYEGNEN SKKESDEVES LNELESELDK IWGGINFN // ID COFC_METJA Reviewed; 224 AA. AC Q58297; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=2-phospho-L-lactate guanylyltransferase; DE Short=LP guanylyltransferase; DE EC=2.7.7.68; GN Name=cofC; OrderedLocusNames=MJ0887; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ROLE IN F420 RP BIOSYNTHESIS, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18260642; DOI=10.1021/bi702475t; RA Grochowski L.L., Xu H., White R.H.; RT "Identification and characterization of the 2-phospho-L-lactate RT guanylyltransferase involved in coenzyme F420 biosynthesis."; RL Biochemistry 47:3033-3037(2008). CC -!- FUNCTION: Guanylyltransferase that catalyzes the activation of 2- CC phospho-L-lactate (LP) as (2S)-lactyl-2-diphospho-5'-guanosine CC (LPPG), via the condensation of LP with GTP. Is involved in the CC biosynthesis of coenzyme F420, a hydride carrier cofactor. Is able CC to utilize other purine nucleotides including dGTP and ITP as CC cosubstrates in place of GTP but with a lower activity. Does not CC display lactate kinase activity. {ECO:0000269|PubMed:18260642}. CC -!- CATALYTIC ACTIVITY: (2S)-2-phospholactate + GTP = (2S)-lactyl-2- CC diphospho-5'-guanosine + diphosphate. CC {ECO:0000269|PubMed:18260642}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=36 uM for (2S)-2-phospholactate CC {ECO:0000269|PubMed:18260642}; CC KM=56 uM for GTP {ECO:0000269|PubMed:18260642}; CC Vmax=3 umol/min/mg enzyme {ECO:0000269|PubMed:18260642}; CC Temperature dependence: CC Retains all activity when heated up to 90 degrees Celsius for 10 CC minutes and retained 38% activity after 10 minutes at 100 CC degrees Celsius. {ECO:0000269|PubMed:18260642}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18260642}. CC -!- SIMILARITY: Belongs to the CofC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98891.1; -; Genomic_DNA. DR PIR; G64410; G64410. DR ProteinModelPortal; Q58297; -. DR STRING; 243232.MJ_0887; -. DR EnsemblBacteria; AAB98891; AAB98891; MJ_0887. DR KEGG; mja:MJ_0887; -. DR eggNOG; arCOG04472; Archaea. DR eggNOG; COG1920; LUCA. DR InParanoid; Q58297; -. DR KO; K14941; -. DR OMA; RAVIPYK; -. DR PhylomeDB; Q58297; -. DR BioCyc; MetaCyc:MONOMER-14615; -. DR BRENDA; 2.7.7.68; 3260. DR SABIO-RK; Q58297; -. DR UniPathway; UPA00071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0043814; F:phospholactate guanylyltransferase activity; IDA:UniProtKB. DR GO; GO:0009108; P:coenzyme biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_02114; CofC; 1. DR InterPro; IPR002835; Coenzyme_F420_CofC. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF01983; CofC; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR03552; F420_cofC; 1. PE 1: Evidence at protein level; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase. FT CHAIN 1 224 2-phospho-L-lactate guanylyltransferase. FT /FTId=PRO_0000107091. SQ SEQUENCE 224 AA; 25683 MW; 0565EDD51F313278 CRC64; MNCGIKMKVI IPVSPINSLK TRLSEFLSGE ERKNLLLNML KDIIKALDGL DIVIVSRDEE ILDFAKNELK AETIKEKYKG LNNAIKQAFE EIEDKEVIII PADIPLIKKK HIEDILKLSK NYDLIIAPSR GGGTNLLYLK SKDLIEIKYE GFSFLKHLEE AKKRNLRYYI YDSFLISVDI NTPEDLGEIF IHGNDTYTKN YLKSLGIDVE PKHSSAGRFV VKRR // ID COMD_METJA Reviewed; 169 AA. AC P58415; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 05-DEC-2001, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Sulfopyruvate decarboxylase subunit alpha {ECO:0000303|PubMed:10940029}; DE EC=4.1.1.79 {ECO:0000269|PubMed:10940029}; GN Name=comD {ECO:0000303|PubMed:10940029}; OrderedLocusNames=MJ0255.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME RP REGULATION, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10940029; DOI=10.1128/JB.182.17.4862-4867.2000; RA Graupner M., Xu H., White R.H.; RT "Identification of the gene encoding sulfopyruvate decarboxylase, an RT enzyme involved in biosynthesis of coenzyme M."; RL J. Bacteriol. 182:4862-4867(2000). CC -!- FUNCTION: Involved in the biosynthesis of the coenzyme M (2- CC mercaptoethanesulfonic acid). Catalyzes the decarboxylation of CC sulfopyruvate to sulfoacetaldehyde. {ECO:0000269|PubMed:10940029}. CC -!- CATALYTIC ACTIVITY: 3-sulfopyruvate = 2-sulfoacetaldehyde + CO(2). CC {ECO:0000269|PubMed:10940029}. CC -!- ENZYME REGULATION: Inhibited by oxygen when heated in air at 80 CC degrees Celsius. The enzyme is reactivated by addition of CC dithionite. {ECO:0000269|PubMed:10940029}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.64 mM for 3-sulfopyruvate {ECO:0000269|PubMed:10940029}; CC Vmax=52 umol/min/mg enzyme {ECO:0000269|PubMed:10940029}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis; CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 4/4. CC {ECO:0000305|PubMed:10940029}. CC -!- SUBUNIT: Heterododecamer composed of 6 subunits alpha and 6 CC subunits beta. {ECO:0000269|PubMed:10940029}. CC -!- SIMILARITY: Belongs to the ComD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P58415; -. DR InParanoid; P58415; -. DR OMA; EEGIGVC; -. DR PhylomeDB; P58415; -. DR BioCyc; MetaCyc:MONOMER-2265; -. DR BRENDA; 4.1.1.79; 3260. DR UniPathway; UPA00355; UER00472. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR022502; Sulfopyruvate_deCO2ase_alpha. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR TIGRFAMs; TIGR03845; sulfopyru_alph; 1. PE 1: Evidence at protein level; KW Coenzyme M biosynthesis; Complete proteome; Decarboxylase; Lyase; KW Reference proteome. FT CHAIN 1 169 Sulfopyruvate decarboxylase subunit FT alpha. FT /FTId=PRO_0000090837. SQ SEQUENCE 169 AA; 19059 MW; 2FB248306F7D211C CRC64; MRGSLAIYNA LKDSNIDFIC SVPCANLKNL LKLIEEDKNI INIPATREEE AFGICAGAYL AGKKTAILMQ NSGIGNSINA IASLYKTFQI PTLLIISHRG DLKEQIPAQI PMGRWIEKLL DVCEIPTYKP KTPEEAYKLI KYASSYMYKI SYPVALLFDA LYWEYDLEK // ID CS3HE_METJA Reviewed; 614 AA. AC Q57828; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=CRISPR-associated helicase Cas3; DE EC=3.6.4.-; GN Name=cas3; Synonyms=cas3'; OrderedLocusNames=MJ0383; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE FUNCTION, AND ATP-DEPENDENCE. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=22009198; DOI=10.1038/emboj.2011.377; RA Beloglazova N., Petit P., Flick R., Brown G., Savchenko A., RA Yakunin A.F.; RT "Structure and activity of the Cas3 HD nuclease MJ0384, an effector RT enzyme of the CRISPR interference."; RL EMBO J. 30:4616-4627(2011). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate CC in CRISPR interference, the third stage of CRISPR immunity. CC Probably unwinds dsDNA templates, thus providing substrates for CC CRISPR-associated endonuclease Cas3-HD. Unwinding is strongly CC increased in the presence of ATP, implying the helicase uses ATP CC to unwind substrate. CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain CC and a C-terminal helicase/ATPase domain. In some CRISPR/Cas CC systems the domains are swapped, in others they are encoded CC separately. CC -!- SIMILARITY: Belongs to the CRISPR-associated helicase Cas3 family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98371.1; -; Genomic_DNA. DR PIR; G64347; G64347. DR ProteinModelPortal; Q57828; -. DR STRING; 243232.MJ_0383; -. DR EnsemblBacteria; AAB98371; AAB98371; MJ_0383. DR KEGG; mja:MJ_0383; -. DR eggNOG; arCOG01444; Archaea. DR eggNOG; COG1203; LUCA. DR KO; K07012; -. DR OMA; IQRIGRC; -. DR PhylomeDB; Q57828; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR006474; Helicase_Cas3_CRISPR-ass_core. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01587; cas3_core; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 614 CRISPR-associated helicase Cas3. FT /FTId=PRO_0000106846. FT DOMAIN 27 219 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 244 386 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. SQ SEQUENCE 614 AA; 71568 MW; 016CF1A6F4EDEF1A CRC64; MDIINFFKQI TDHEPYDYQI RAWEKINKIM ELGGRVVIEI PTAGGKTEAA IIPYLYQFIS NDWKVPRLIY VLPTRSLVEK QVERIRNYIK KILEIKGYSK DKVEELAKKI VQVEYGLEET HAFLGFVVLT TWDTFLYGLA AHRTVGDRFT FPCGAIAQSL VVFDEIQMYQ DESLYMPRLI GLVVKRLVEA NVPLVFMTAT LPTELKKILG IHDEEPITVN PEDTKKPERG EVVVEFKEKL SDEELSNEIK KAINEGKKVL IIKNTVNSAI EVYEKVKQLG NSLLLHSRFT VEDRAEKEKD IDKAEIIVAT QVVEAGLDLT NVGLVITDLA PLDALIQRIG RCARRKGERG KVIVVLPNFN EKINEDHREK VILGFKNIPF ENAYVTLVNN KDYGRVIELT IETIEEKKGK SKIVPKKFYI GDLGNKTIRK LIENNKILKK KDLYFIPYST QPYDPLIMIK SFDEVESVSE YLYDIIKARE ALDRVYKEYY ENNIVPKDYY SAYIYFRELK LFSTPPEYEL KARPEMFAIL YPLENAEEKV KNKEIIEFNP KYVIRVSYNW LKNKWEKFDK KFELIKEYDE KGWICSLKKA GKLQPYKIYI IDDKYYSKET GIII // ID COMC_METJA Reviewed; 344 AA. AC Q58820; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=L-sulfolactate dehydrogenase; DE EC=1.1.1.337; DE AltName: Full=(R)-2-hydroxyacid dehydrogenase; DE AltName: Full=(R)-sulfolactate dehydrogenase; DE AltName: Full=L-2-hydroxycarboxylate dehydrogenase (NAD(+)); GN Name=comC; Synonyms=mdh; OrderedLocusNames=MJ1425; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=10850983; DOI=10.1128/JB.182.13.3688-3692.2000; RA Graupner M., Xu H., White R.H.; RT "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing RT reactions involved in coenzyme biosynthesis in methanoarchaea."; RL J. Bacteriol. 182:3688-3692(2000). CC -!- FUNCTION: Catalyzes the reduction of sulfopyruvate to (R)- CC sulfolactate much more efficiently than the reverse reaction. Also CC catalyzes the reduction of oxaloacetate, alpha-ketoglutarate, and CC to a much lower extent, KHTCA, but not pyruvate. Involved in the CC biosynthesis of both coenzyme M (with (R)-sulfolactate) and CC methanopterin (with alpha-ketoglutarate). CC {ECO:0000269|PubMed:10850983}. CC -!- CATALYTIC ACTIVITY: A (2S)-2-hydroxycarboxylate + NAD(+) = a 2- CC oxocarboxylate + NADH. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis; CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 3/4. CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the LDH2/MDH2 oxidoreductase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99436.1; -; Genomic_DNA. DR PIR; H64477; H64477. DR PDB; 2X06; X-ray; 2.50 A; A/B/C/D/E/F/G/H=1-344. DR PDBsum; 2X06; -. DR ProteinModelPortal; Q58820; -. DR SMR; Q58820; 1-344. DR STRING; 243232.MJ_1425; -. DR EnsemblBacteria; AAB99436; AAB99436; MJ_1425. DR KEGG; mja:MJ_1425; -. DR eggNOG; arCOG04874; Archaea. DR eggNOG; COG2055; LUCA. DR InParanoid; Q58820; -. DR KO; K05884; -. DR OMA; SSHCGAL; -. DR PhylomeDB; Q58820; -. DR BioCyc; MetaCyc:MONOMER-2264; -. DR BioCyc; RETL1328306-WGS:GSTH-4783-MONOMER; -. DR BRENDA; 1.1.1.337; 3260. DR SABIO-RK; Q58820; -. DR UniPathway; UPA00065; -. DR UniPathway; UPA00355; UER00471. DR EvolutionaryTrace; Q58820; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003767; Malate/L-lactate_DH. DR PANTHER; PTHR11091; PTHR11091; 1. DR Pfam; PF02615; Ldh_2; 1. DR SUPFAM; SSF89733; SSF89733; 1. PE 1: Evidence at protein level; KW 3D-structure; Coenzyme M biosynthesis; Complete proteome; Cytoplasm; KW NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 344 L-sulfolactate dehydrogenase. FT /FTId=PRO_0000083824. FT HELIX 5 18 {ECO:0000244|PDB:2X06}. FT HELIX 23 39 {ECO:0000244|PDB:2X06}. FT HELIX 42 44 {ECO:0000244|PDB:2X06}. FT HELIX 46 48 {ECO:0000244|PDB:2X06}. FT HELIX 49 57 {ECO:0000244|PDB:2X06}. FT STRAND 60 64 {ECO:0000244|PDB:2X06}. FT STRAND 68 72 {ECO:0000244|PDB:2X06}. FT STRAND 74 80 {ECO:0000244|PDB:2X06}. FT HELIX 86 104 {ECO:0000244|PDB:2X06}. FT STRAND 105 113 {ECO:0000244|PDB:2X06}. FT HELIX 121 128 {ECO:0000244|PDB:2X06}. FT TURN 129 131 {ECO:0000244|PDB:2X06}. FT STRAND 132 138 {ECO:0000244|PDB:2X06}. FT STRAND 158 164 {ECO:0000244|PDB:2X06}. FT STRAND 169 179 {ECO:0000244|PDB:2X06}. FT HELIX 182 189 {ECO:0000244|PDB:2X06}. FT STRAND 198 200 {ECO:0000244|PDB:2X06}. FT STRAND 202 206 {ECO:0000244|PDB:2X06}. FT HELIX 210 215 {ECO:0000244|PDB:2X06}. FT STRAND 216 218 {ECO:0000244|PDB:2X06}. FT STRAND 220 222 {ECO:0000244|PDB:2X06}. FT HELIX 223 236 {ECO:0000244|PDB:2X06}. FT TURN 237 241 {ECO:0000244|PDB:2X06}. FT HELIX 245 247 {ECO:0000244|PDB:2X06}. FT STRAND 261 267 {ECO:0000244|PDB:2X06}. FT HELIX 269 271 {ECO:0000244|PDB:2X06}. FT HELIX 275 290 {ECO:0000244|PDB:2X06}. FT HELIX 305 313 {ECO:0000244|PDB:2X06}. FT TURN 314 316 {ECO:0000244|PDB:2X06}. FT HELIX 322 334 {ECO:0000244|PDB:2X06}. FT HELIX 339 341 {ECO:0000244|PDB:2X06}. SQ SEQUENCE 344 AA; 37358 MW; DD6B9086923CD298 CRC64; MILKPENEKK LIIDVLKKFG VPEEDAKITA DVFVDADLKG FTSHGIGRFP QYITALKLGN INPKPDIKIV KESPATAVID GDLGLGQVVG KKAMELAIKK AKNVGVGVVA TRNANHFGIA GYYSELAMNQ DMIGITITNT EPAMAPFGGK EKILGTNPIA IAFKGNKYKF SLDMATASIA RGKILEALRK KIKIPEGCAV DKDGKPTTDP AKALEGCILP FGGPKGYGLA LAIEMLSAIG GAEVGTKVKG TANPEERCTK GDLFIAINPE FFMGKEEFKR KVDELLDEIK NSEPAEGFEI LIPGEIEERN KMKRKDGFEI DKNLYNQLKE ICNELGLNIE DYIE // ID CSG_METJA Reviewed; 558 AA. AC Q58232; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=S-layer protein; DE AltName: Full=Cell surface glycoprotein; DE AltName: Full=Surface layer protein; DE Flags: Precursor; GN Name=sla; Synonyms=slmJ1; OrderedLocusNames=MJ0822; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12382110; DOI=10.1007/s00792-001-0264-1; RA Akca E., Claus H., Schultz N., Karbach G., Schlott B., RA Debaerdemaeker T., Declercq J.P., Konig H.; RT "Genes and derived amino acid sequences of S-layer proteins from RT mesophilic, thermophilic, and extremely thermophilic methanococci."; RL Extremophiles 6:351-358(2002). RN [3] RP PROTEIN SEQUENCE OF 29-39. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RA Graham D.E.; RT "Archaeal gene identification."; RL Thesis (2000), University of Illinois, United States. CC -!- FUNCTION: The S-layer is a paracrystalline mono-layered assembly CC of proteins which coat the surface of the cell. CC -!- SUBCELLULAR LOCATION: Secreted, cell wall, S-layer. CC -!- SIMILARITY: Belongs to the Mj S-layer protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98821.1; -; Genomic_DNA. DR EMBL; AJ311636; CAC84089.1; -; Genomic_DNA. DR PIR; F64402; F64402. DR ProteinModelPortal; Q58232; -. DR STRING; 243232.MJ_0822; -. DR EnsemblBacteria; AAB98821; AAB98821; MJ_0822. DR KEGG; mja:MJ_0822; -. DR eggNOG; arCOG03418; Archaea. DR eggNOG; ENOG410YG7N; LUCA. DR InParanoid; Q58232; -. DR OMA; MAMSMKK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005618; C:cell wall; IEA:UniProtKB-KW. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0030115; C:S-layer; IEA:UniProtKB-SubCell. DR GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW. DR InterPro; IPR022651; S_layer_C. DR InterPro; IPR006454; S_layer_MJ. DR InterPro; IPR022650; S_layer_N. DR Pfam; PF05124; S_layer_C; 1. DR Pfam; PF05123; S_layer_N; 1. DR TIGRFAMs; TIGR01564; S_layer_MJ; 1. PE 1: Evidence at protein level; KW Cell wall; Cell wall biogenesis/degradation; Complete proteome; KW Direct protein sequencing; Glycoprotein; Reference proteome; S-layer; KW Secreted; Signal. FT SIGNAL 1 28 {ECO:0000269|Ref.3}. FT CHAIN 29 558 S-layer protein. FT /FTId=PRO_0000032620. FT CARBOHYD 112 112 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 138 138 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 158 158 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 197 197 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 226 226 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 291 291 N-linked (GlcNAc...). {ECO:0000255}. FT CARBOHYD 374 374 N-linked (GlcNAc...). {ECO:0000255}. SQ SEQUENCE 558 AA; 60548 MW; CF46C69302BBFB01 CRC64; MAMSLKKIGA IAVGGAMVAT ALASGVAAEV TTSGFSDYKE LKDILVKDGQ PNCYVVVGAD APSTMDVVSA ADIAAKIGSL CYKEGTVEDG SADITVHAEA NSDDFDLKKD WNNSAMPANA YALFVAASDG DYSEKFENDT GKPSFMDNGV LGDADKINKT VDLGDIATMM KVDDVDPSDW YDSDDDAGEI VMVELKNDTS DGFTVYKKNM LYETLVYKDD EENFANTTKM EEGMRIPFLG KEMVVVDIDK DDDAIYLGTP VYDGIIKEGE TYDLGNGYQV KIKAILKTTV NNTDVYKVDV QILKDGKVVA EKYDKAPLEL EYKDDVGVTV HKAWENVGGD YGYAELVISK DLKKLELDEE YVTDWKAYAV LNDNGTMKLE DDLNDNNVDK VVGIALRYDG DKLDDLDSGD EVDILDYVKF KLDDEDSNDK LKVYFSMDKD VDATLNIGEK VKALNAEVKL KDIKANAVEP VSLTAPIAKL DTEVSLDTAD KNLVLVGGPV ANKLTKELVD AGKLALDNNS PATIALIPDA ANGHDVIVVA GGDREKTREA ALELIKNL // ID CSM4_METJA Reviewed; 376 AA. AC Q59062; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=CRISPR type III-associated RAMP protein Csm4; DE AltName: Full=CRISPR type III-A/Mtube-associated RAMP protein Csm4; GN Name=csm4; OrderedLocusNames=MJ1668; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm4 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99688.1; -; Genomic_DNA. DR PIR; B64508; B64508. DR PDB; 4QTS; X-ray; 3.10 A; A/B=1-376. DR PDBsum; 4QTS; -. DR ProteinModelPortal; Q59062; -. DR STRING; 243232.MJ_1668; -. DR EnsemblBacteria; AAB99688; AAB99688; MJ_1668. DR KEGG; mja:MJ_1668; -. DR eggNOG; arCOG03222; Archaea. DR eggNOG; COG1567; LUCA. DR InParanoid; Q59062; -. DR KO; K19139; -. DR OMA; FFSIKAY; -. DR PhylomeDB; Q59062; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR005510; DUF314. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01903; cas5_csm4; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Complete proteome; KW Reference proteome. FT CHAIN 1 376 CRISPR type III-associated RAMP protein FT Csm4. FT /FTId=PRO_0000107465. FT STRAND 2 8 {ECO:0000244|PDB:4QTS}. FT HELIX 30 50 {ECO:0000244|PDB:4QTS}. FT HELIX 54 57 {ECO:0000244|PDB:4QTS}. FT STRAND 66 69 {ECO:0000244|PDB:4QTS}. FT STRAND 72 76 {ECO:0000244|PDB:4QTS}. FT HELIX 81 83 {ECO:0000244|PDB:4QTS}. FT TURN 95 98 {ECO:0000244|PDB:4QTS}. FT STRAND 102 104 {ECO:0000244|PDB:4QTS}. FT HELIX 105 110 {ECO:0000244|PDB:4QTS}. FT TURN 111 114 {ECO:0000244|PDB:4QTS}. FT TURN 118 120 {ECO:0000244|PDB:4QTS}. FT HELIX 122 128 {ECO:0000244|PDB:4QTS}. FT STRAND 129 131 {ECO:0000244|PDB:4QTS}. FT TURN 132 134 {ECO:0000244|PDB:4QTS}. FT HELIX 139 148 {ECO:0000244|PDB:4QTS}. FT STRAND 154 156 {ECO:0000244|PDB:4QTS}. FT STRAND 164 173 {ECO:0000244|PDB:4QTS}. FT STRAND 188 198 {ECO:0000244|PDB:4QTS}. FT STRAND 202 209 {ECO:0000244|PDB:4QTS}. FT HELIX 215 226 {ECO:0000244|PDB:4QTS}. FT HELIX 228 231 {ECO:0000244|PDB:4QTS}. FT STRAND 244 251 {ECO:0000244|PDB:4QTS}. FT HELIX 254 260 {ECO:0000244|PDB:4QTS}. FT HELIX 265 268 {ECO:0000244|PDB:4QTS}. FT STRAND 270 276 {ECO:0000244|PDB:4QTS}. FT HELIX 284 287 {ECO:0000244|PDB:4QTS}. FT STRAND 288 291 {ECO:0000244|PDB:4QTS}. FT STRAND 293 296 {ECO:0000244|PDB:4QTS}. FT HELIX 304 306 {ECO:0000244|PDB:4QTS}. FT STRAND 310 316 {ECO:0000244|PDB:4QTS}. FT STRAND 321 324 {ECO:0000244|PDB:4QTS}. FT STRAND 364 367 {ECO:0000244|PDB:4QTS}. SQ SEQUENCE 376 AA; 43851 MW; F5DC850CA5FF7DF2 CRC64; MKMVVLKPKI NSKFHFGEGS LERNSKIFHS NSLFSAIVNN YIKLYGREDL EKNIEKIKNI RLSSLLYKIK NIYLIPKPEH PEFYKLKGNP GIKPKDIKKI QFFSIKAYKE LLDNELDWKN KIKHIVDYQT INKSIVISEK EIEEIKRIFG IKAEKLKHAK ISLISKHLEQ KVAIDRLKDI TLEKDDKGQL YNIEFIKLNE NVEFYFLIDY NNEDKEFIKK LEASIKLIED EGLGGKRSIG AGFFEKVEIV DLPEDFNEIL DENSKYNNLE YKMLLGVGIP NKDDIKNIEY YKLIEIGGYI YSLECLTKPK RNILALTEGS IVKNDFIGDV KDISPQNDDD EQNKNNENNN KLNHKVYTHG KPILLPFNPK RDNYGS // ID CSX1B_METJA Reviewed; 634 AA. AC Q59068; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=CRISPR-associated protein Csx1 2; GN Name=csx1b; OrderedLocusNames=MJ1674; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (Potential). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csx1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99696.1; -; Genomic_DNA. DR PIR; H64508; H64508. DR ProteinModelPortal; Q59068; -. DR STRING; 243232.MJ_1674; -. DR EnsemblBacteria; AAB99696; AAB99696; MJ_1674. DR KEGG; mja:MJ_1674; -. DR eggNOG; arCOG07641; Archaea. DR eggNOG; ENOG4111HA0; LUCA. DR InParanoid; Q59068; -. DR OMA; IFEISEW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR019016; CRISPR-assoc_DxTHG_prot. DR InterPro; IPR013383; CRISPR-assoc_prot_DxTHG_CS. DR InterPro; IPR011742; CRISPR-assoc_prot_TM1812. DR Pfam; PF09455; Cas_DxTHG; 1. DR TIGRFAMs; TIGR02221; cas_TM1812; 1. DR TIGRFAMs; TIGR02549; CRISPR_DxTHG; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 634 CRISPR-associated protein Csx1 2. FT /FTId=PRO_0000107472. SQ SEQUENCE 634 AA; 74782 MW; E91877838C81AB7F CRC64; MLKVLISPLG VGDTNTDVYK RQYKTAEYKF EGDIDGIESP FVLSVLIEKL KVDKVIVVGT AKSMWEKLYE YYAKEVGEFD EEYWIEIGKK VGMSKYDNYA LSEEDLKKIE KVIDKYLKKI NPNAVGGSKC KIIKYGIDKD EIWENFDLFM SLINEVNDGD EIYLDITHSF RSIPLFMYVM LEFMRYFKNV KLKGIYYGML DVIRELGHAP VVDLSPIFEI SEWIRGMYEF TTYGNSYLIS KLLENEDKEI AEKLQKISRY IDANYLKELR EEVKTLKPLL NEKKDTGRFL KYFIPELHKF IDKLKYEDSD FEFQISMAKW NFDNKKYSSG YLCLTDSIFW KLCELYNLPS VYKNREVMKG IIYNPSLNKK YSAFGSIKDM HYKRLRNIRN KIAHADVSKK GDDFNPENDL EDVVNLLKNV NLPDFDKIIE DLLLDVKNNQ NNKTLKLLKN ILNIQIIRKI IKAYNFESNE IYWDFVSGYL LNKNNKCNNE KLREIIEIFH KNIEDAGELE EAFNFVKNTE DEELLDSLAL QNAIMHYALF KLSNAYNIKN KEDKEAIKWV LLNQNLCSKH PILKEINNNY HKIFKNKDKP MSNEILEASK NIIRLLNSDL SEIKDSVPLN LIIIRYRSYK NNRR // ID CRCB_METJA Reviewed; 124 AA. AC Q58918; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Putative fluoride ion transporter CrcB {ECO:0000255|HAMAP-Rule:MF_00454}; GN Name=crcB {ECO:0000255|HAMAP-Rule:MF_00454}; OrderedLocusNames=MJ1523; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Important for reducing fluoride concentration in the CC cell, thus reducing its toxicity. {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00454}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00454}. CC -!- SIMILARITY: Belongs to the CrcB (TC 9.B.71) family. CC {ECO:0000255|HAMAP-Rule:MF_00454}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99542.1; -; Genomic_DNA. DR PIR; B64490; B64490. DR STRING; 243232.MJ_1523; -. DR EnsemblBacteria; AAB99542; AAB99542; MJ_1523. DR KEGG; mja:MJ_1523; -. DR eggNOG; arCOG04701; Archaea. DR eggNOG; COG0239; LUCA. DR InParanoid; Q58918; -. DR KO; K06199; -. DR OMA; SLRYFVG; -. DR PhylomeDB; Q58918; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0015103; F:inorganic anion transmembrane transporter activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00454; CrcB; 1. DR InterPro; IPR003691; CrcB. DR Pfam; PF02537; CRCB; 1. DR TIGRFAMs; TIGR00494; crcB; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 124 Putative fluoride ion transporter CrcB. FT /FTId=PRO_0000110228. FT TRANSMEM 6 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 37 57 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 69 89 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. FT TRANSMEM 92 112 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00454}. SQ SEQUENCE 124 AA; 13534 MW; E5B702BC06104B9D CRC64; MIRELLLIGV GGFFGAIFRY LISGIVPVKF GLPTGTLAVN LIGSFILGFL LYCSLFAPIP TEYKLFIGTG FCGALTTFST FSYETFVLVD EGLLFKALLN ILINVVGCLI MVYFGRVLAL AIFR // ID CSM2_METJA Reviewed; 133 AA. AC Q59064; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=CRISPR type III-associated protein Csm2; DE AltName: Full=CRISPR type III-A/Mtube-associated protein Csm2; GN Name=csm2; OrderedLocusNames=MJ1670; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm2 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99693.1; -; Genomic_DNA. DR PIR; D64508; D64508. DR ProteinModelPortal; Q59064; -. DR STRING; 243232.MJ_1670; -. DR EnsemblBacteria; AAB99693; AAB99693; MJ_1670. DR KEGG; mja:MJ_1670; -. DR eggNOG; arCOG06487; Archaea. DR eggNOG; COG1421; LUCA. DR InParanoid; Q59064; -. DR KO; K19138; -. DR OMA; KPKLAYN; -. DR PhylomeDB; Q59064; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR010149; CRISPR-assoc_prot_TM1810_C. DR Pfam; PF03750; DUF310; 1. DR TIGRFAMs; TIGR01870; cas_TM1810_Csm2; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 133 CRISPR type III-associated protein Csm2. FT /FTId=PRO_0000107468. SQ SEQUENCE 133 AA; 15670 MW; EF803498557B6898 CRC64; MSKIGKCILN PNEINLILNI NSQNANEIID IAENLAKEFE QIPATKMRDF YDYVLRIDEK NENWYKELVL LKPKLAYNYG KETNRRKKEA LEKLAGTFSE IIDKIDNDLN KFKNFKTFFE ALVAYHKIYA KSQ // ID CSM5_METJA Reviewed; 418 AA. AC Q59061; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=CRISPR type III-associated RAMP protein Csm5; DE AltName: Full=CRISPR type III-A/Mtube-associated RAMP protein Csm5; GN Name=csm5; OrderedLocusNames=MJ1667; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csm5 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99692.1; -; Genomic_DNA. DR PIR; A64508; A64508. DR ProteinModelPortal; Q59061; -. DR STRING; 243232.MJ_1667; -. DR EnsemblBacteria; AAB99692; AAB99692; MJ_1667. DR KEGG; mja:MJ_1667; -. DR eggNOG; arCOG03718; Archaea. DR eggNOG; COG1332; LUCA. DR InParanoid; Q59061; -. DR KO; K19140; -. DR OMA; IRTAYIF; -. DR PhylomeDB; Q59061; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR010173; CRISPR-assoc_prot_TM1807. DR InterPro; IPR005537; RAMP_III_fam. DR Pfam; PF03787; RAMPs; 1. DR TIGRFAMs; TIGR01899; cas_TM1807_csm5; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 418 CRISPR type III-associated RAMP protein FT Csm5. FT /FTId=PRO_0000107464. SQ SEQUENCE 418 AA; 48804 MW; 14C31107463948D2 CRC64; MLKTYPLKMM MTSRIRIMKT TINLIIRSIP MENQYYSHLI QRGITMEVKC ELITPIFIGC GEEYSQLDYF IEDGLAHIID LEKAVSDLDD LEKVDYISGL IVSNIDNNRL NLTAKDILES VGLNPYDYVI RKIESEIFSN KKTRVKKFIN QNNTYYIPGS SIKGAIRTAY IFNYYDKNLP ELLKILDDRN IKLHDKGKEL EKNAISKDIP KDFFKYLKIS DSLNLEGEFK FIHTKRWNYR KKKFDVPINM EGMTKGTFSI NIKIEDEFFK NINKRLKTNY NPKDDEKKFD ILKNLCNNFS KTVVEFELKK NNPVYVEKSY EKLLADINKD DAIYLNLGFG GGFLNKTVYP LLWKNDENHL YFRKIKSLFI ALSGGNKNLK NAWLKANSYL DFPTTKTVYV KNNSAIAPLG WIKMTLVE // ID CS3HD_METJA Reviewed; 244 AA. AC Q57829; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=CRISPR-associated endonuclease Cas3-HD; DE EC=3.1.-.-; DE AltName: Full=CRISPR-associated ssDNA/ssRNA endonuclease Cas3-HD; GN Name=cas3; Synonyms=cas3''; OrderedLocusNames=MJ0384; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION AS A NUCLEASE, RP COFACTOR, SUBSTRATES, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME RP REGULATION, SUBUNIT, AND MUTAGENESIS OF HIS-20; HIS-66; ASP-67; RP HIS-91; HIS-123; HIS-124 AND ASP-219. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=22009198; DOI=10.1038/emboj.2011.377; RA Beloglazova N., Petit P., Flick R., Brown G., Savchenko A., RA Yakunin A.F.; RT "Structure and activity of the Cas3 HD nuclease MJ0384, an effector RT enzyme of the CRISPR interference."; RL EMBO J. 30:4616-4627(2011). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat), is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC sequences complementary to antecedent mobile elements and target CC invading nucleic acids. CRISPR clusters are transcribed and CC processed into CRISPR RNA (crRNA). Cas3 plus Cascade participate CC in CRISPR interference, the third stage of CRISPR immunity. Acts CC as a ssDNA and ssRNA nuclease, with both endo- and 3' to 5' CC exonuclease activities, acting on substrates with free single- CC stranded 3' ends. Double-stranded nucleic acids are not CC substrates. Activity is higher for DNA than RNA. Templates include CC R-loops (a bubble-like structure formed when ssRNA replaces one CC strand in a dsDNA, such as crRNA is thought to form with CRISPR CC target DNA), circular ssDNA, 2',3'-cAMP and 2',3'-cGMP. Probably CC generates 3'-phosphate and 5'-hydroxyl ends. In the presence of CC the Cas3 helicase and ATP dsDNA templates are also degraded. CC {ECO:0000269|PubMed:22009198}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:22009198}; CC Note=ssDNase activity requires Mg(2+), ssRNase activity does not CC require cations. A second loosely associated metal ion is visible CC in the crystal structure. {ECO:0000269|PubMed:22009198}; CC -!- ENZYME REGULATION: Both ssDNase and ssRNase are inhibited by EDTA. CC {ECO:0000269|PubMed:22009198}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7-9, varying somewhat depending on the substrate. CC {ECO:0000269|PubMed:22009198}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:22009198}. CC -!- DOMAIN: Proteins of this family have an N-terminal nuclease domain CC and a C-terminal helicase/ATPase domain. In some CRISPR/Cas CC systems the domains are swapped, in others they are encoded CC separately. CC -!- SIMILARITY: Belongs to the CRISPR-associated nuclease Cas3-HD CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HD Cas3-type domain. {ECO:0000255|PROSITE- CC ProRule:PRU00974}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98379.1; -; Genomic_DNA. DR PIR; H64347; H64347. DR PDB; 3S4L; X-ray; 2.30 A; A=1-244. DR PDBsum; 3S4L; -. DR STRING; 243232.MJ_0384; -. DR DNASU; 1451241; -. DR EnsemblBacteria; AAB98379; AAB98379; MJ_0384. DR KEGG; mja:MJ_0384; -. DR eggNOG; arCOG01442; Archaea. DR eggNOG; COG2254; LUCA. DR KO; K07475; -. DR OMA; HEPILMG; -. DR EvolutionaryTrace; Q57829; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR InterPro; IPR006483; CRISPR-assoc_Cas3_HD. DR TIGRFAMs; TIGR01596; cas3_HD; 1. DR PROSITE; PS51643; HD_CAS3; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiviral defense; Complete proteome; Endonuclease; KW Exonuclease; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 244 CRISPR-associated endonuclease Cas3-HD. FT /FTId=PRO_0000106847. FT DOMAIN 10 221 HD Cas3-type. {ECO:0000255|PROSITE- FT ProRule:PRU00974}. FT METAL 67 67 Magnesium; catalytic. FT METAL 91 91 Magnesium; via tele nitrogen; catalytic. FT METAL 123 123 Magnesium; via tele nitrogen; catalytic. FT METAL 124 124 Magnesium; via tele nitrogen; catalytic. FT MUTAGEN 20 20 H->A: Loss of all nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 66 66 H->A: Loss of all nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 67 67 D->A: Loss of all nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 67 67 D->E: Very little nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 91 91 H->A: Very little ssDNA exonuclease FT activity. {ECO:0000269|PubMed:22009198}. FT MUTAGEN 123 123 H->A: Very little nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 124 124 H->A: Very little nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT MUTAGEN 219 219 D->A: Loss of all nuclease activity. FT {ECO:0000269|PubMed:22009198}. FT STRAND 10 12 {ECO:0000244|PDB:3S4L}. FT HELIX 17 31 {ECO:0000244|PDB:3S4L}. FT HELIX 32 34 {ECO:0000244|PDB:3S4L}. FT HELIX 36 43 {ECO:0000244|PDB:3S4L}. FT HELIX 44 46 {ECO:0000244|PDB:3S4L}. FT HELIX 52 65 {ECO:0000244|PDB:3S4L}. FT HELIX 68 71 {ECO:0000244|PDB:3S4L}. FT HELIX 73 80 {ECO:0000244|PDB:3S4L}. FT STRAND 82 84 {ECO:0000244|PDB:3S4L}. FT HELIX 91 107 {ECO:0000244|PDB:3S4L}. FT HELIX 110 121 {ECO:0000244|PDB:3S4L}. FT TURN 122 124 {ECO:0000244|PDB:3S4L}. FT HELIX 142 149 {ECO:0000244|PDB:3S4L}. FT HELIX 159 167 {ECO:0000244|PDB:3S4L}. FT HELIX 181 197 {ECO:0000244|PDB:3S4L}. FT TURN 201 203 {ECO:0000244|PDB:3S4L}. FT HELIX 204 215 {ECO:0000244|PDB:3S4L}. SQ SEQUENCE 244 AA; 28406 MW; 09CE6E74BB8621C3 CRC64; MILGEIMEVL AFKNQSLIDH VNDMVKYWER IKYRYLKTIK RALEALNIKL DIEKVDEFMK ILIKLHDIGK ASKIYQRAII NDQEKLMGFR HELVSAYYTY HILLKKFGDK NLAFIGALTV MLHHEPIIMG QIRNLKKKEL TAEVVLDKLK KFDGMIEDFE DLIKKLIGYS IGDIIKNDSN KDDIIRFVIE MSVRARHTPN SEKLRFIVGT LLLPLVMCDY KGAESREGKA PKFAEVLEVE SYVI // ID CSA3_METJA Reviewed; 208 AA. AC Q57824; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=CRISPR locus-related putative DNA-binding protein Csa3; GN Name=csa3; OrderedLocusNames=MJ0379; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csa3 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98369.1; -; Genomic_DNA. DR PIR; C64347; C64347. DR ProteinModelPortal; Q57824; -. DR STRING; 243232.MJ_0379; -. DR EnsemblBacteria; AAB98369; AAB98369; MJ_0379. DR KEGG; mja:MJ_0379; -. DR eggNOG; arCOG01446; Archaea. DR eggNOG; COG0640; LUCA. DR InParanoid; Q57824; -. DR KO; K07725; -. DR OMA; YASLYEF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR010163; Csa3. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR01884; cas_HTH; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 208 CRISPR locus-related putative DNA-binding FT protein Csa3. FT /FTId=PRO_0000106842. SQ SEQUENCE 208 AA; 24080 MW; 163D155C47FA2623 CRC64; MVRYMRYIAT FGYHTNHIFD KNGKIIGIDD EKISNMILIY SLDVDADENT VNSIKNTKNY IESKLKEYNI PYLFVEVNPY EFNTNVKNFR KYIVPKTIIN LTGGKRIVGY ALFYAAVLEK ENVEKVFYVS KLGDIIEFPL IPPDIKLTEL EMKILNLLDK EGEMSVSNIA HKLERSLSTI SEYVSQLEKK GLVKKLSKGR RKIVKKVI // ID CYDE_METJA Reviewed; 388 AA. AC Q58431; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=L-cysteine desulfidase {ECO:0000303|PubMed:15683250}; DE EC=4.4.1.28 {ECO:0000269|PubMed:15683250}; DE AltName: Full=L-cysteine desulfhydrase; GN OrderedLocusNames=MJ1025; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, RP SUBSTRATE SPECIFICITY, COFACTOR, MUTAGENESIS OF CYS-25; HIS-139; RP CYS-282; CYS-322; ASP-323 AND CYS-329, AND REACTION MECHANISM. RX PubMed=15683250; DOI=10.1021/bi0484769; RA Tchong S.I., Xu H., White R.H.; RT "L-cysteine desulfidase: an [4Fe-4S] enzyme isolated from RT Methanocaldococcus jannaschii that catalyzes the breakdown of L- RT cysteine into pyruvate, ammonia, and sulfide."; RL Biochemistry 44:1659-1670(2005). CC -!- FUNCTION: Catalyzes the cleavage of L-cysteine to form 2- CC aminoprop-2-enoate and sulfide. The former then spontaneously CC hydrolyzes to pyruvate and NH(3). May be responsible for the CC production of sulfide required for the biosynthesis of iron-sulfur CC centers in this archaea. Is very specific for L-cysteine, with no CC activity being detected with D-cysteine, L-homocysteine, 3- CC mercaptopropionate (cysteine without the amino group), cysteamine CC (cysteine without the carboxylate), or mercaptolactate (the CC hydroxyl analog of cysteine). {ECO:0000269|PubMed:15683250}. CC -!- CATALYTIC ACTIVITY: L-cysteine + H(2)O = sulfide + NH(3) + CC pyruvate. {ECO:0000269|PubMed:15683250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000269|PubMed:15683250}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000269|PubMed:15683250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.78 mM for L-cysteine (at 65 degrees Celsius) CC {ECO:0000269|PubMed:15683250}; CC Note=kcat is 39.6 sec(-1) (at 65 degrees Celsius). CC {ECO:0000269|PubMed:15683250}; CC pH dependence: CC Optimum pH is 7.6. {ECO:0000269|PubMed:15683250}; CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:15683250}. CC -!- SIMILARITY: Belongs to the L-cysteine desulfidase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99029.1; -; Genomic_DNA. DR PIR; H64427; H64427. DR ProteinModelPortal; Q58431; -. DR STRING; 243232.MJ_1025; -. DR EnsemblBacteria; AAB99029; AAB99029; MJ_1025. DR KEGG; mja:MJ_1025; -. DR eggNOG; arCOG05065; Archaea. DR eggNOG; COG3681; LUCA. DR InParanoid; Q58431; -. DR OMA; TINTAII; -. DR PhylomeDB; Q58431; -. DR BRENDA; 4.4.1.B3; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR005130; Ser_deHydtase-like_asu. DR InterPro; IPR021144; UPF0597. DR Pfam; PF03313; SDH_alpha; 1. DR PIRSF; PIRSF006054; UCP006054; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 388 L-cysteine desulfidase. FT /FTId=PRO_0000107148. FT ACT_SITE 25 25 Proton acceptor. FT {ECO:0000305|PubMed:15683250}. FT METAL 282 282 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:15683250}. FT METAL 322 322 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:15683250}. FT METAL 329 329 Iron-sulfur (4Fe-4S). FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 25 25 C->A: No activity. FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 139 139 H->N: Almost no effect. FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 282 282 C->A: Retains 5% of wild-type activity. FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 322 322 C->A: No activity; when associated with FT Ala-329. {ECO:0000269|PubMed:15683250}. FT MUTAGEN 322 322 C->S: Retains 10% of wild-type activity. FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 323 323 D->N: Retains 50% of wild-type activity. FT {ECO:0000269|PubMed:15683250}. FT MUTAGEN 329 329 C->A: No activity; when associated with FT Ala-322. {ECO:0000269|PubMed:15683250}. FT MUTAGEN 329 329 C->S: Retains 10% of wild-type activity. FT {ECO:0000269|PubMed:15683250}. SQ SEQUENCE 388 AA; 42645 MW; 80CA180E1061315C CRC64; MVSIMNKNEL ITEILKNEVV KALGCTEVGL IGYTVAKAKP EDLYSIKEIK LILDKGTFKN AFSVGVPNTN KFGILPAVVG GLLGREENKL EVFKDIKYDE KLEEFIENKL KIEVIDSDVY CKVIIKANKV YEAETKGSHS GKSLSDDLKN AYKSLTLKDF IDYIEDIPEE VIKIIKETIE TNKNLSTPEV PEDFISLDLK DEILNHMLKK TVSAVYNRMI GINKPAMAIA GSGNMGLTAT LPIIAYDEIK GHDEEKLTKS ITLSALTTIY SAYHSSYISA MCGCVNRGGI GAVSGLSYYI FGFDRIEESI KSFTANLPGI VCDGGKIGCA LKIASGVFAI YLSLFSKVPY TNGIVGKDFK ECIENIGKIG KAMKPVDDEI IEILKNKK // ID DAPA_METJA Reviewed; 289 AA. AC Q57695; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE Short=HTPA synthase {ECO:0000255|HAMAP-Rule:MF_00418}; DE EC=4.3.3.7 {ECO:0000255|HAMAP-Rule:MF_00418}; GN Name=dapA {ECO:0000255|HAMAP-Rule:MF_00418}; OrderedLocusNames=MJ0244; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=20054116; DOI=10.1107/S174430910904651X; RA Padmanabhan B., Strange R.W., Antonyuk S.V., Ellis M.J., Hasnain S.S., RA Iino H., Agari Y., Bessho Y., Yokoyama S.; RT "Structure of dihydrodipicolinate synthase from Methanocaldococcus RT jannaschii."; RL Acta Crystallogr. F 65:1222-1226(2009). CC -!- FUNCTION: Catalyzes the condensation of (S)-aspartate-beta- CC semialdehyde [(S)-ASA] and pyruvate to 4-hydroxy- CC tetrahydrodipicolinate (HTPA). {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- CATALYTIC ACTIVITY: Pyruvate + L-aspartate-4-semialdehyde = (4S)- CC 4-hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 3/4. CC {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00418, ECO:0000269|PubMed:20054116}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00418}. CC -!- SIMILARITY: Belongs to the DapA family. {ECO:0000255|HAMAP- CC Rule:MF_00418}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC synthase (DHDPS), catalyzing the condensation of (S)-aspartate- CC beta-semialdehyde [(S)-ASA] and pyruvate to dihydrodipicolinate CC (DHDP). However, it was shown in E.coli that the product of the CC enzymatic reaction is not dihydrodipicolinate but in fact (4S)-4- CC hydroxy-2,3,4,5-tetrahydro-(2S)-dipicolinic acid (HTPA), and that CC the consecutive dehydration reaction leading to DHDP is not CC spontaneous but catalyzed by DapB. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98232.1; -; Genomic_DNA. DR PIR; E64330; E64330. DR PDB; 2YXG; X-ray; 2.20 A; A/B/C/D=1-289. DR PDBsum; 2YXG; -. DR ProteinModelPortal; Q57695; -. DR SMR; Q57695; 1-289. DR STRING; 243232.MJ_0244; -. DR EnsemblBacteria; AAB98232; AAB98232; MJ_0244. DR KEGG; mja:MJ_0244; -. DR eggNOG; arCOG04172; Archaea. DR eggNOG; COG0329; LUCA. DR InParanoid; Q57695; -. DR KO; K01714; -. DR OMA; GMDACVP; -. DR PhylomeDB; Q57695; -. DR BRENDA; 4.3.3.7; 3260. DR UniPathway; UPA00034; UER00017. DR EvolutionaryTrace; Q57695; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008840; F:4-hydroxy-tetrahydrodipicolinate synthase; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00418; DapA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005263; DapA. DR InterPro; IPR002220; DapA-like. DR InterPro; IPR020625; Schiff_base-form_aldolases_AS. DR InterPro; IPR020624; Schiff_base-form_aldolases_CS. DR PANTHER; PTHR12128; PTHR12128; 1. DR Pfam; PF00701; DHDPS; 1. DR PIRSF; PIRSF001365; DHDPS; 1. DR PRINTS; PR00146; DHPICSNTHASE. DR SMART; SM01130; DHDPS; 1. DR TIGRFAMs; TIGR00674; dapA; 1. DR PROSITE; PS00665; DHDPS_1; 1. DR PROSITE; PS00666; DHDPS_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lyase; Lysine biosynthesis; KW Reference proteome; Schiff base. FT CHAIN 1 289 4-hydroxy-tetrahydrodipicolinate FT synthase. FT /FTId=PRO_0000103197. FT ACT_SITE 132 132 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT ACT_SITE 161 161 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT BINDING 44 44 Pyruvate. {ECO:0000255|HAMAP- FT Rule:MF_00418}. FT BINDING 201 201 Pyruvate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 43 43 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT SITE 106 106 Part of a proton relay during catalysis. FT {ECO:0000255|HAMAP-Rule:MF_00418}. FT STRAND 4 8 {ECO:0000244|PDB:2YXG}. FT HELIX 20 32 {ECO:0000244|PDB:2YXG}. FT STRAND 36 42 {ECO:0000244|PDB:2YXG}. FT TURN 43 46 {ECO:0000244|PDB:2YXG}. FT HELIX 47 49 {ECO:0000244|PDB:2YXG}. FT HELIX 52 66 {ECO:0000244|PDB:2YXG}. FT STRAND 69 75 {ECO:0000244|PDB:2YXG}. FT HELIX 81 94 {ECO:0000244|PDB:2YXG}. FT STRAND 97 102 {ECO:0000244|PDB:2YXG}. FT HELIX 111 124 {ECO:0000244|PDB:2YXG}. FT STRAND 129 133 {ECO:0000244|PDB:2YXG}. FT HELIX 135 138 {ECO:0000244|PDB:2YXG}. FT HELIX 144 153 {ECO:0000244|PDB:2YXG}. FT STRAND 157 162 {ECO:0000244|PDB:2YXG}. FT HELIX 168 176 {ECO:0000244|PDB:2YXG}. FT STRAND 179 184 {ECO:0000244|PDB:2YXG}. FT HELIX 186 188 {ECO:0000244|PDB:2YXG}. FT HELIX 189 194 {ECO:0000244|PDB:2YXG}. FT STRAND 199 203 {ECO:0000244|PDB:2YXG}. FT HELIX 204 206 {ECO:0000244|PDB:2YXG}. FT HELIX 209 221 {ECO:0000244|PDB:2YXG}. FT HELIX 224 240 {ECO:0000244|PDB:2YXG}. FT STRAND 243 245 {ECO:0000244|PDB:2YXG}. FT HELIX 248 256 {ECO:0000244|PDB:2YXG}. FT HELIX 273 285 {ECO:0000244|PDB:2YXG}. SQ SEQUENCE 289 AA; 31580 MW; 34CD8619C4A53CCA CRC64; MFKGVYPAII TPFKNKEVDF DGLEENINFL IENGVSGIVA VGTTGESPTL SHEEHKKVIE KVVDVVNGRV QVIAGAGSNC TEEAIELSVF AEDVGADAVL SITPYYNKPT QEGLRKHFGK VAESINLPIV LYNVPSRTAV NLEPKTVKLL AEEYSNISAV KEANPNLSQV SELIHDAKIT VLSGNDELTL PIIALGGKGV ISVVANIVPK EFVEMVNYAL EGDFEKAREI HYKLFPLMKA MFIETNPIPV KTALNMMGRP AGELRLPLCE MSEEHKKILE NVLKDLGLI // ID CSX1A_METJA Reviewed; 465 AA. AC Q59060; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=CRISPR-associated protein Csx1 1; GN Name=csx1a; OrderedLocusNames=MJ1666; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: CRISPR (clustered regularly interspaced short CC palindromic repeat) is an adaptive immune system that provides CC protection against mobile genetic elements (viruses, transposable CC elements and conjugative plasmids). CRISPR clusters contain CC spacers, sequences complementary to antecedent mobile elements, CC and target invading nucleic acids. CRISPR clusters are transcribed CC and processed into CRISPR RNA (crRNA) (Potential). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CRISPR-associated Csx1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99691.1; -; Genomic_DNA. DR PIR; H64507; H64507. DR ProteinModelPortal; Q59060; -. DR STRING; 243232.MJ_1666; -. DR EnsemblBacteria; AAB99691; AAB99691; MJ_1666. DR KEGG; mja:MJ_1666; -. DR eggNOG; arCOG03433; Archaea. DR eggNOG; COG1517; LUCA. DR InParanoid; Q59060; -. DR KO; K19143; -. DR OMA; ILIAPWG; -. DR PhylomeDB; Q59060; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW. DR Gene3D; 1.10.3740.10; -; 1. DR InterPro; IPR027419; CRISPR-assoc_Csx1_C. DR InterPro; IPR019016; CRISPR-assoc_DxTHG_prot. DR InterPro; IPR013383; CRISPR-assoc_prot_DxTHG_CS. DR InterPro; IPR010171; CRISPR-assoc_prot_MJ1666. DR Pfam; PF09455; Cas_DxTHG; 1. DR TIGRFAMs; TIGR01897; cas_MJ1666; 1. DR TIGRFAMs; TIGR02549; CRISPR_DxTHG; 1. PE 3: Inferred from homology; KW Antiviral defense; Complete proteome; Reference proteome. FT CHAIN 1 465 CRISPR-associated protein Csx1 1. FT /FTId=PRO_0000107463. SQ SEQUENCE 465 AA; 54500 MW; ACB9E442EEF94173 CRC64; MQKILIAPWG NFSSWKKVIY SFNGVEKESK SSLSAIYDKI NPDKVYILVL DTLSNLESEN YGDIVKEVKE KTENFIKENL NIDNYEVIVC PGVGTFYNKD FEKYFKFYGN LTDYYSFALY ELSKRLDGDL EVHLDLTHGL NYMPVLTYRV IKDLLEILAI KNKVRLVVYN SDPYVGREKE ILNIHTVEDV IIKPSYDIKG MTLDFLDATK FVDKKEIGKI KKEINMNPKI KELRIMKQNI NAFIASIVYA LPLVYSTFFV KKDKIEIYLN ELIGAFISNI KINPEDKILK RYLYFGEGFN SLVKAYFASK ISEIPQLIKD ELSLEEIDEL KNTLFKENPN SQYIKNEISS LYNIINTKYK EEELSEILGN WTPIYKIRRE NIDKFKIRNF LAHAGFEKSV TEIYISVENK NGKIELSEKT SLRYNKNYIE EKNGIKRFIF KYKDKNGKVE EINILEKIEE ILLNK // ID DAPB_METJA Reviewed; 274 AA. AC Q57865; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 108. DE RecName: Full=4-hydroxy-tetrahydrodipicolinate reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE Short=HTPA reductase {ECO:0000255|HAMAP-Rule:MF_00102}; DE EC=1.17.1.8 {ECO:0000255|HAMAP-Rule:MF_00102}; GN Name=dapB {ECO:0000255|HAMAP-Rule:MF_00102}; OrderedLocusNames=MJ0422; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of 4-hydroxy- CC tetrahydrodipicolinate (HTPA) to tetrahydrodipicolinate. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- CATALYTIC ACTIVITY: (S)-2,3,4,5-tetrahydropyridine-2,6- CC dicarboxylate + NAD(P)(+) + H(2)O = (2S,4S)-4-hydroxy-2,3,4,5- CC tetrahydrodipicolinate + NAD(P)H. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 4/4. CC {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00102}. CC -!- SIMILARITY: Belongs to the DapB family. {ECO:0000255|HAMAP- CC Rule:MF_00102}. CC -!- CAUTION: Was originally thought to be a dihydrodipicolinate CC reductase (DHDPR), catalyzing the conversion of CC dihydrodipicolinate to tetrahydrodipicolinate. However, it was CC shown in E.coli that the substrate of the enzymatic reaction is CC not dihydrodipicolinate (DHDP) but in fact (2S,4S)-4-hydroxy- CC 2,3,4,5-tetrahydrodipicolinic acid (HTPA), the product released by CC the DapA-catalyzed reaction. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98410.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98410.1; ALT_INIT; Genomic_DNA. DR PIR; F64352; F64352. DR ProteinModelPortal; Q57865; -. DR STRING; 243232.MJ_0422; -. DR EnsemblBacteria; AAB98410; AAB98410; MJ_0422. DR KEGG; mja:MJ_0422; -. DR eggNOG; arCOG04393; Archaea. DR eggNOG; COG0289; LUCA. DR InParanoid; Q57865; -. DR KO; K00215; -. DR OMA; KEEIGIH; -. DR PhylomeDB; Q57865; -. DR UniPathway; UPA00034; UER00018. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016726; F:oxidoreductase activity, acting on CH or CH2 groups, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IBA:GO_Central. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00102; DapB; 1. DR InterPro; IPR022663; DapB_C. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR022664; DapB_N_CS. DR InterPro; IPR023940; DHDPR_bac. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR20836; PTHR20836; 1. DR Pfam; PF05173; DapB_C; 1. DR Pfam; PF01113; DapB_N; 1. DR PIRSF; PIRSF000161; DHPR; 1. DR SUPFAM; SSF51735; SSF51735; 2. DR TIGRFAMs; TIGR00036; dapB; 1. DR PROSITE; PS01298; DAPB; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Diaminopimelate biosynthesis; Lysine biosynthesis; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 274 4-hydroxy-tetrahydrodipicolinate FT reductase. FT /FTId=PRO_0000141518. FT NP_BIND 8 13 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 102 104 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT NP_BIND 128 131 NAD(P). {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT REGION 170 171 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT ACT_SITE 160 160 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00102}. FT ACT_SITE 164 164 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00102}. FT BINDING 34 34 NAD. {ECO:0000255|HAMAP-Rule:MF_00102}. FT BINDING 161 161 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00102}. SQ SEQUENCE 274 AA; 29955 MW; D943FB6CF3DC706E CRC64; MIKVAVTGAL GRMGSNIIKT ITQQEDMKVV CAFEVPNHPK KGEDVGELIG IGKIGVPLST ADELDKVLKE TKPDVLVDFT IAHACVENVK IAAKNGVNLV IGTTGFTEEQ KAEIEKAIKE NNVAAVISQN FAIGVNIFFK TLEFLAKKLG DYDIEIIEMH HRYKKDAPSG TALRAAEIIK ANRGIESVFV YGRYGMTGER KKEEIGIHAL RGGDVVGDHT VIFAGDGERI ELTHRASSRQ AFVNGVILAI RYIADKKEGI YNTFDVLGLN EIKF // ID DCDA_METJA Reviewed; 438 AA. AC Q58497; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 113. DE RecName: Full=Diaminopimelate decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAP decarboxylase {ECO:0000255|HAMAP-Rule:MF_02120}; DE Short=DAPDC {ECO:0000255|HAMAP-Rule:MF_02120}; DE EC=4.1.1.20 {ECO:0000255|HAMAP-Rule:MF_02120, ECO:0000269|PubMed:12429091}; GN Name=lysA {ECO:0000255|HAMAP-Rule:MF_02120}; OrderedLocusNames=MJ1097; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 5-438 IN COMPLEXES WITH PLP; RP L-LYSINE AND SUBSTRATE ANALOG, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP ENZYME REGULATION, KINETIC PARAMETERS, AND SUBUNIT. RX PubMed=12429091; DOI=10.1016/S0969-2126(02)00880-8; RA Ray S.S., Bonanno J.B., Rajashankar K.R., Pinho M.G., He G., RA De Lencastre H., Tomasz A., Burley S.K.; RT "Cocrystal structures of diaminopimelate decarboxylase: mechanism, RT evolution, and inhibition of an antibiotic resistance accessory RT factor."; RL Structure 10:1499-1508(2002). CC -!- FUNCTION: Specifically catalyzes the decarboxylation of meso- CC diaminopimelate (meso-DAP) to L-lysine. CC {ECO:0000269|PubMed:12429091}. CC -!- CATALYTIC ACTIVITY: Meso-2,6-diaminoheptanedioate = L-lysine + CC CO(2). {ECO:0000269|PubMed:12429091}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:12429091}; CC -!- ENZYME REGULATION: Competitively inhibited by the substrate analog CC azelaic acid in vitro but not in vivo. CC {ECO:0000269|PubMed:12429091}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=588 uM for meso-2,6-diaminoheptanedioate CC {ECO:0000269|PubMed:12429091}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; L-lysine from DL-2,6-diaminopimelate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02120}. CC -!- SUBUNIT: Homodimer. {ECO:0000305|PubMed:12429091}. CC -!- SIMILARITY: Belongs to the Orn/Lys/Arg decarboxylase class-II CC family. LysA subfamily. {ECO:0000255|HAMAP-Rule:MF_02120}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99100.1; -; Genomic_DNA. DR PIR; H64436; H64436. DR PDB; 1TUF; X-ray; 2.40 A; A/B=5-438. DR PDB; 1TWI; X-ray; 2.00 A; A/B/C/D=6-438. DR PDBsum; 1TUF; -. DR PDBsum; 1TWI; -. DR ProteinModelPortal; Q58497; -. DR SMR; Q58497; 6-438. DR STRING; 243232.MJ_1097; -. DR EnsemblBacteria; AAB99100; AAB99100; MJ_1097. DR KEGG; mja:MJ_1097; -. DR eggNOG; arCOG02268; Archaea. DR eggNOG; COG0019; LUCA. DR InParanoid; Q58497; -. DR KO; K01586; -. DR OMA; LKGNKFG; -. DR PhylomeDB; Q58497; -. DR UniPathway; UPA00034; UER00027. DR EvolutionaryTrace; Q58497; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008836; F:diaminopimelate decarboxylase activity; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.37.10; -; 1. DR Gene3D; 3.20.20.10; -; 1. DR HAMAP; MF_02120; LysA; 1. DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C. DR InterPro; IPR002986; DAP_deCOOHase_LysA. DR InterPro; IPR022643; De-COase2_C. DR InterPro; IPR022657; De-COase2_CS. DR InterPro; IPR022644; De-COase2_N. DR InterPro; IPR022653; De-COase2_pyr-phos_BS. DR InterPro; IPR000183; Orn/DAP/Arg_de-COase. DR InterPro; IPR029066; PLP-binding_barrel. DR Pfam; PF02784; Orn_Arg_deC_N; 1. DR Pfam; PF00278; Orn_DAP_Arg_deC; 1. DR PRINTS; PR01181; DAPDCRBXLASE. DR PRINTS; PR01179; ODADCRBXLASE. DR SUPFAM; SSF50621; SSF50621; 2. DR SUPFAM; SSF51419; SSF51419; 1. DR TIGRFAMs; TIGR01048; lysA; 1. DR PROSITE; PS00878; ODR_DC_2_1; 1. DR PROSITE; PS00879; ODR_DC_2_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Decarboxylase; Lyase; Lysine biosynthesis; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 438 Diaminopimelate decarboxylase. FT /FTId=PRO_0000149941. FT REGION 294 297 Pyridoxal phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_02120, FT ECO:0000269|PubMed:12429091}. FT ACT_SITE 362 362 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT BINDING 217 217 Pyridoxal phosphate. FT {ECO:0000269|PubMed:12429091}. FT BINDING 254 254 Pyridoxal phosphate; via amide nitrogen. FT {ECO:0000269|PubMed:12429091}. FT BINDING 297 297 Substrate. {ECO:0000305|PubMed:12429091}. FT BINDING 333 333 Substrate. {ECO:0000305|PubMed:12429091}. FT BINDING 337 337 Substrate. {ECO:0000305|PubMed:12429091}. FT BINDING 363 363 Substrate. {ECO:0000305|PubMed:12429091}. FT BINDING 391 391 Pyridoxal phosphate. FT {ECO:0000269|PubMed:12429091}. FT BINDING 391 391 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02120}. FT MOD_RES 73 73 N6-(pyridoxal phosphate)lysine. FT {ECO:0000269|PubMed:12429091}. FT STRAND 11 14 {ECO:0000244|PDB:1TWI}. FT STRAND 17 20 {ECO:0000244|PDB:1TWI}. FT HELIX 25 32 {ECO:0000244|PDB:1TWI}. FT STRAND 34 40 {ECO:0000244|PDB:1TWI}. FT HELIX 41 62 {ECO:0000244|PDB:1TWI}. FT STRAND 66 71 {ECO:0000244|PDB:1TWI}. FT HELIX 72 74 {ECO:0000244|PDB:1TWI}. FT HELIX 78 86 {ECO:0000244|PDB:1TWI}. FT STRAND 90 93 {ECO:0000244|PDB:1TWI}. FT HELIX 96 104 {ECO:0000244|PDB:1TWI}. FT HELIX 109 111 {ECO:0000244|PDB:1TWI}. FT STRAND 112 114 {ECO:0000244|PDB:1TWI}. FT HELIX 121 129 {ECO:0000244|PDB:1TWI}. FT STRAND 133 137 {ECO:0000244|PDB:1TWI}. FT HELIX 140 153 {ECO:0000244|PDB:1TWI}. FT STRAND 157 164 {ECO:0000244|PDB:1TWI}. FT TURN 169 171 {ECO:0000244|PDB:1TWI}. FT HELIX 173 181 {ECO:0000244|PDB:1TWI}. FT STRAND 185 188 {ECO:0000244|PDB:1TWI}. FT HELIX 192 202 {ECO:0000244|PDB:1TWI}. FT STRAND 204 212 {ECO:0000244|PDB:1TWI}. FT STRAND 217 219 {ECO:0000244|PDB:1TWI}. FT HELIX 223 241 {ECO:0000244|PDB:1TWI}. FT STRAND 247 250 {ECO:0000244|PDB:1TWI}. FT STRAND 259 263 {ECO:0000244|PDB:1TWI}. FT HELIX 268 280 {ECO:0000244|PDB:1TWI}. FT TURN 281 285 {ECO:0000244|PDB:1TWI}. FT STRAND 290 293 {ECO:0000244|PDB:1TWI}. FT HELIX 297 300 {ECO:0000244|PDB:1TWI}. FT HELIX 301 303 {ECO:0000244|PDB:1TWI}. FT STRAND 304 315 {ECO:0000244|PDB:1TWI}. FT STRAND 320 325 {ECO:0000244|PDB:1TWI}. FT TURN 328 330 {ECO:0000244|PDB:1TWI}. FT HELIX 333 337 {ECO:0000244|PDB:1TWI}. FT STRAND 343 347 {ECO:0000244|PDB:1TWI}. FT STRAND 352 358 {ECO:0000244|PDB:1TWI}. FT STRAND 360 362 {ECO:0000244|PDB:1TWI}. FT STRAND 367 375 {ECO:0000244|PDB:1TWI}. FT STRAND 382 386 {ECO:0000244|PDB:1TWI}. FT STRAND 389 392 {ECO:0000244|PDB:1TWI}. FT HELIX 393 395 {ECO:0000244|PDB:1TWI}. FT TURN 399 401 {ECO:0000244|PDB:1TWI}. FT STRAND 406 411 {ECO:0000244|PDB:1TWI}. FT STRAND 414 419 {ECO:0000244|PDB:1TWI}. FT HELIX 424 427 {ECO:0000244|PDB:1TWI}. FT TURN 428 430 {ECO:0000244|PDB:1TWI}. FT HELIX 435 437 {ECO:0000244|PDB:1TWI}. SQ SEQUENCE 438 AA; 48900 MW; DE031EC50FD57326 CRC64; MKIMFLGNDT VEIKDGRFFI DGYDAIELAE KFGTPLYVMS EEQIKINYNR YIEAFKRWEE ETGKEFIVAY AYKANANLAI TRLLAKLGCG ADVVSGGELY IAKLSNVPSK KIVFNGNCKT KEEIIMGIEA NIRAFNVDSI SELILINETA KELGETANVA FRINPNVNPK THPKISTGLK KNKFGLDVES GIAMKAIKMA LEMEYVNVVG VHCHIGSQLT DISPFIEETR KVMDFVVELK EEGIEIEDVN LGGGLGIPYY KDKQIPTQKD LADAIINTML KYKDKVEMPN LILEPGRSLV ATAGYLLGKV HHIKETPVTK WVMIDAGMND MMRPAMYEAY HHIINCKVKN EKEVVSIAGG LCESSDVFGR DRELDKVEVG DVLAIFDVGA YGISMANNYN ARGRPRMVLT SKKGVFLIRE RETYADLIAK DIVPPHLL // ID DAPAT_METJA Reviewed; 418 AA. AC Q58786; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=LL-diaminopimelate aminotransferase; DE Short=DAP-AT; DE Short=DAP-aminotransferase; DE Short=LL-DAP-aminotransferase; DE EC=2.6.1.83; GN Name=dapL; OrderedLocusNames=MJ1391; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A DIAMINOPIMELATE AMINOTRANSFERASE, BIOPHYSICOCHEMICAL RP PROPERTIES, AND COFACTOR. RX PubMed=20418392; DOI=10.1128/JB.00172-10; RA Liu Y., White R.H., Whitman W.B.; RT "Methanococci use the diaminopimelate aminotransferase (DapL) pathway RT for lysine biosynthesis."; RL J. Bacteriol. 192:3304-3310(2010). CC -!- FUNCTION: Involved in the synthesis of meso-diaminopimelate (m-DAP CC or DL-DAP), required for both lysine and peptidoglycan CC biosynthesis. Catalyzes the direct conversion of CC tetrahydrodipicolinate to LL-diaminopimelate, a reaction that CC requires three enzymes in E.coli. {ECO:0000269|PubMed:20418392}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate + 2-oxoglutarate = CC (S)-2,3,4,5-tetrahydropyridine-2,6-dicarboxylate + L-glutamate + CC H(2)O. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:20418392}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.42 uM for alpha-ketoglutarate (alpha-KG)(at pH 8.8 and at CC 70 degrees Celsius) {ECO:0000269|PubMed:20418392}; CC KM=82.8 uM for LL-2,6-diaminopimelate (L,L-DAP)(at pH 8.8 and at CC 70 degrees Celsius) {ECO:0000269|PubMed:20418392}; CC Vmax=0.39 umol/min/mg enzyme (at pH 8.8 and at 70 degrees CC Celsius) {ECO:0000269|PubMed:20418392}; CC pH dependence: CC Optimum pH is 8.5. About 40% and 50% of the maximum activity are CC observed at pH 7.0 and 10.0, respectively. CC {ECO:0000269|PubMed:20418392}; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. No activity is CC detected at temperatures below 45 degrees Celsius. At 85 degrees CC Celsius, the activity is 85% of the maximum activity. CC {ECO:0000269|PubMed:20418392}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; LL-2,6-diaminopimelate from (S)-tetrahydrodipicolinate CC (aminotransferase route): step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99401.1; -; Genomic_DNA. DR PIR; F64473; F64473. DR ProteinModelPortal; Q58786; -. DR STRING; 243232.MJ_1391; -. DR EnsemblBacteria; AAB99401; AAB99401; MJ_1391. DR KEGG; mja:MJ_1391; -. DR eggNOG; arCOG01133; Archaea. DR eggNOG; COG0436; LUCA. DR InParanoid; Q58786; -. DR KO; K10206; -. DR OMA; LVELPQC; -. DR PhylomeDB; Q58786; -. DR BioCyc; MetaCyc:MONOMER-15639; -. DR UniPathway; UPA00034; UER00466. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0010285; F:L,L-diaminopimelate aminotransferase activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0033362; P:lysine biosynthetic process via diaminopimelate, diaminopimelate-aminotransferase pathway; ISS:UniProtKB. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 1: Evidence at protein level; KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 418 LL-diaminopimelate aminotransferase. FT /FTId=PRO_0000123929. FT BINDING 52 52 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 140 140 Substrate. {ECO:0000250}. FT BINDING 190 190 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 190 190 Substrate. {ECO:0000250}. FT BINDING 218 218 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 221 221 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 248 248 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 250 250 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 259 259 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 251 251 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 418 AA; 47709 MW; 73CFBC48B4CA23F6 CRC64; MESYIQNLFA ERIGGKKFGK EDVIYKFEKI KRAKQEAMKR HPDMELIDMG VGEPDEMADP EVIRVLCEEA KKWENRGYAD NGIQELKDAV PPYMEKVYGV KDIDPVNEVI HSIGSKPALA YITSAFINPG DVCLMTVPGY PVTATHTKWY GGEVYNLPLL EENDFLPDLE SIPEDIKKRA KILYLNYPNN PTGAQATKKF YKEVVDFAFE NEVIVVQDAA YGALVYDGKP LSFLSVKDAK EVGVEIHSFS KAFNMTGWRL AFLVGNELII KAFATVKDNF DSGQFIPIQK AGIYCLQHPE ITERVRQKYE RRLRKMVKIL NEVGFKARMP GGTFYLYVKS PTKANGIEFK TAEDFSQYLI KEKLISTVPW DDAGHYLRLA ACFVAKDENG NPTTEEKYED MVLEEFKRRL EGMDLEFE // ID DADD_METJA Reviewed; 420 AA. AC Q58936; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 99. DE RecName: Full=5'-deoxyadenosine deaminase {ECO:0000255|HAMAP-Rule:MF_01281, ECO:0000303|PubMed:24375099}; DE Short=5'-dA deaminase {ECO:0000255|HAMAP-Rule:MF_01281, ECO:0000303|PubMed:24375099}; DE EC=3.5.4.41 {ECO:0000255|HAMAP-Rule:MF_01281, ECO:0000269|PubMed:24375099}; GN Name=dadD {ECO:0000255|HAMAP-Rule:MF_01281, GN ECO:0000303|PubMed:24375099}; OrderedLocusNames=MJ1541; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND MUTAGENESIS OF TYR-136; RP GLU-150 AND CYS-294. RX PubMed=24375099; DOI=10.1128/JB.01308-13; RA Miller D., O'Brien K., Xu H., White R.H.; RT "Identification of a 5'-deoxyadenosine deaminase in Methanocaldococcus RT jannaschii and its possible role in recycling the radical S- RT adenosylmethionine enzyme reaction product 5'-deoxyadenosine."; RL J. Bacteriol. 196:1064-1072(2014). CC -!- FUNCTION: Catalyzes the deamination of 5'-deoxyadenosine into 5'- CC deoxyinosine. May be involved in the recycling of 5'- CC deoxyadenosine, whereupon the 5'-deoxyribose moiety of 5'- CC deoxyinosine is further metabolized to deoxyhexoses used for the CC biosynthesis of aromatic amino acids in methanogens. Is also able CC to deaminate 5-methylthioadenosine, S-adenosyl-L-homocysteine and CC adenosine to a small extent. {ECO:0000255|HAMAP-Rule:MF_01281, CC ECO:0000269|PubMed:24375099}. CC -!- CATALYTIC ACTIVITY: 5'-deoxyadenosine + H(2)O = 5'-deoxyinosine + CC NH(3). {ECO:0000255|HAMAP-Rule:MF_01281, CC ECO:0000269|PubMed:24375099}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01281}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01281}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.014 mM for 5'-deoxyadenosine (at pH 9 and 60 degrees CC Celsius) {ECO:0000269|PubMed:24375099}; CC KM=0.11 mM for S-methyl-5'-thioadenosine (at pH 9 and 60 degrees CC Celsius) {ECO:0000269|PubMed:24375099}; CC KM=1.1 mM for S-adenosyl-L-homocysteine (at pH 9 and 60 degrees CC Celsius) {ECO:0000269|PubMed:24375099}; CC KM=0.15 mM for adenosine (at pH 9 and 60 degrees Celsius) CC {ECO:0000269|PubMed:24375099}; CC Note=kcat is 120000 sec(-1) for 5'-deoxyadenosine deamination. CC kcat is 160 sec(-1) for S-methyl-5'-thioadenosine deamination. CC kcat is 1300 sec(-1) for S-adenosyl-L-homocysteine deamination. CC kcat is 110 sec(-1) for adenosine deamination. At pH 9 and 60 CC degrees Celsius. {ECO:0000269|PubMed:24375099}; CC pH dependence: CC Optimum pH is 9.0. {ECO:0000269|PubMed:24375099}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:24375099}. CC -!- SIMILARITY: Belongs to the MTA/SAH deaminase family. CC {ECO:0000255|HAMAP-Rule:MF_01281}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99560.1; -; Genomic_DNA. DR PIR; D64492; D64492. DR ProteinModelPortal; Q58936; -. DR STRING; 243232.MJ_1541; -. DR EnsemblBacteria; AAB99560; AAB99560; MJ_1541. DR KEGG; mja:MJ_1541; -. DR eggNOG; arCOG00695; Archaea. DR eggNOG; COG0402; LUCA. DR InParanoid; Q58936; -. DR KO; K12960; -. DR OMA; HMNETLD; -. DR PhylomeDB; Q58936; -. DR BRENDA; 3.5.4.4; 3260. DR BRENDA; 3.5.4.41; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0090613; F:5'-deoxyadenosine deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IBA:GO_Central. DR GO; GO:0019700; P:organic phosphonate catabolic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 2. DR HAMAP; MF_01281; MTA_SAH_deamin; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR023512; Deaminase_MtaD/DadD. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 420 5'-deoxyadenosine deaminase. FT /FTId=PRO_0000122311. FT METAL 55 55 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01281}. FT METAL 57 57 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01281}. FT METAL 203 203 Zinc; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01281}. FT METAL 292 292 Zinc. {ECO:0000255|HAMAP-Rule:MF_01281}. FT BINDING 84 84 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01281}. FT BINDING 176 176 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01281}. FT BINDING 206 206 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01281}. FT BINDING 292 292 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01281}. FT MUTAGEN 136 136 Y->R: Lowers temperature stability by 10 FT degrees Celsius and decreases activity by FT 364-fold with 5'-deoxyadenosine as FT substrate. Lowers temperature stability FT by 35 degrees Celsius and decreases FT activity by 100000-fold with 5'- FT deoxyadenosine as substrate; when FT associated with R-150. FT {ECO:0000269|PubMed:24375099}. FT MUTAGEN 150 150 E->R: Lowers temperature stability by 10 FT degrees Celsius and decreases activity by FT 571-fold with 5'-deoxyadenosine as FT substrate. Lowers temperature stability FT by 35 degrees Celsius and decreases FT activity by 100000-fold with 5'- FT deoxyadenosine as substrate; when FT associated with R-136. FT {ECO:0000269|PubMed:24375099}. FT MUTAGEN 294 294 C->S: No effect on temperature stability. FT {ECO:0000269|PubMed:24375099}. SQ SEQUENCE 420 AA; 47468 MW; 2458E0E14AF91731 CRC64; MILIKNVFVN GKRQDILIEG NKIKKIGEVK KEEIENAEII DGKNKIAIPG LINTHTHIPM TLFRGVADDL PLMEWLNNYI WPMEAKLNEE IVYWGTLLGC IEMIRSGTTT FNDMYFFLEG IAKAVDESGM RAVLAYGMID LFDEERRERE LKNAEKYINY INSLNNSRIM PALGPHAPYT CSKELLMEVN NLAKKYNVPI HIHLNETLDE IKMVKEKTGM EPFIYLNSFG FFDDVRAIAA HCVHLTDEEI KIMKQKNINV SHNPISNLKL ASGVAPIPKL LAEGINVTLG TDGCGSNNNL NLFEEIKVSA ILHKGVNLNP TVVKAEEAFN FATKNGAKAL NIKAGEIREG YLADIVLINL DKPYLYPKEN IMSHLVYAFN GFVDDVIIDG NIVMRDGEIL TVDEEKVYEK AEEMYEILRS // ID DAPF_METJA Reviewed; 295 AA. AC Q58519; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Diaminopimelate epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE Short=DAP epimerase {ECO:0000255|HAMAP-Rule:MF_00197}; DE EC=5.1.1.7 {ECO:0000255|HAMAP-Rule:MF_00197}; GN Name=dapF {ECO:0000255|HAMAP-Rule:MF_00197}; OrderedLocusNames=MJ1119; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the stereoinversion of LL-2,6- CC diaminoheptanedioate (L,L-DAP) to meso-diaminoheptanedioate (meso- CC DAP), a precursor of L-lysine. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- CATALYTIC ACTIVITY: LL-2,6-diaminoheptanedioate = meso- CC diaminoheptanedioate. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; DL-2,6-diaminopimelate from LL-2,6-diaminopimelate: step CC 1/1. {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00197}. CC -!- SIMILARITY: Belongs to the diaminopimelate epimerase family. CC {ECO:0000255|HAMAP-Rule:MF_00197}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99120.1; -; Genomic_DNA. DR PIR; F64439; F64439. DR ProteinModelPortal; Q58519; -. DR STRING; 243232.MJ_1119; -. DR EnsemblBacteria; AAB99120; AAB99120; MJ_1119. DR KEGG; mja:MJ_1119; -. DR eggNOG; arCOG02255; Archaea. DR eggNOG; COG0253; LUCA. DR InParanoid; Q58519; -. DR KO; K01778; -. DR OMA; RFTKMQG; -. DR PhylomeDB; Q58519; -. DR UniPathway; UPA00034; UER00025. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008837; F:diaminopimelate epimerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00197; DAP_epimerase; 1. DR InterPro; IPR018510; DAP_epimerase_AS. DR InterPro; IPR001653; DAP_epimerase_DapF. DR PANTHER; PTHR31689; PTHR31689; 1. DR Pfam; PF01678; DAP_epimerase; 2. DR TIGRFAMs; TIGR00652; DapF; 1. DR PROSITE; PS01326; DAP_EPIMERASE; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; Disulfide bond; KW Isomerase; Lysine biosynthesis; Reference proteome. FT CHAIN 1 295 Diaminopimelate epimerase. FT /FTId=PRO_0000149886. FT REGION 8 9 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 76 78 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 228 229 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT REGION 238 239 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT ACT_SITE 76 76 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT ACT_SITE 237 237 Proton donor/acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT BINDING 11 11 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 47 47 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 67 67 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 171 171 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT BINDING 210 210 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00197}. FT SITE 173 173 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT SITE 228 228 Important for catalytic activity. FT {ECO:0000255|HAMAP-Rule:MF_00197}. FT DISULFID 76 237 SQ SEQUENCE 295 AA; 33442 MW; 8CB87BF46806982A CRC64; MEFTKMHALG NDYIVINEFD GEKVKEEEKA EFSRKICRRG FSVGADGVIF IQKPTSDEYD VRFRIFNSDG SEAEMCGNGI RCFSKYVYER IMKKNPLKVE TKGGLRVSEM EIEGDEVKKI KVYMGVPKFK LKDIPMVVDG YKEDDEFLNG ELKLKNPYLP KVKLSVVNVG NPHAVIFVED NNIDLDFVRE HLDVIGKEIE HHEAFPERIN VHFVKVLNPN EIRIVTWERG AGYTTACGTG TTASVIMAHK LGKTNNRVLA HLDGGDLEIE IKDDGVYMIG DAVMVYDAKL INIGW // ID DCD_METJA Reviewed; 204 AA. AC Q57872; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 125. DE RecName: Full=dCTP deaminase, dUMP-forming; DE EC=3.5.4.30; DE AltName: Full=Bifunctional deaminase/diphosphatase; DE AltName: Full=MjDCD-DUT; DE Short=DCD/DUT; GN Name=dcd; OrderedLocusNames=MJ0430; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-10, AND CHARACTERIZATION. RX PubMed=12670946; DOI=10.1074/jbc.M213010200; RA Bjoernberg O., Neuhard J., Nyman P.O.; RT "A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the RT hyperthermophilic archaeon Methanocaldococcus jannaschii."; RL J. Biol. Chem. 278:20667-20672(2003). RN [3] RP CHARACTERIZATION, MASS SPECTROMETRY, AND MUTAGENESIS OF ASP-135 AND RP GLU-145. RX PubMed=12538648; DOI=10.1074/jbc.M212460200; RA Li H., Xu H., Graham D.E., White R.H.; RT "The Methanococcus jannaschii dCTP deaminase is a bifunctional RT deaminase and diphosphatase."; RL J. Biol. Chem. 278:11100-11106(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.88 ANGSTROMS) OF 30-204. RX PubMed=12756253; DOI=10.1074/jbc.M304361200; RA Johansson E., Bjoernberg O., Nyman P.O., Larsen S.; RT "Structure of the bifunctional dCTP deaminase-dUTPase from RT Methanocaldococcus jannaschii and its relation to other homotrimeric RT dUTPases."; RL J. Biol. Chem. 278:27916-27922(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.42 ANGSTROMS) OF 23-204. RX PubMed=12909016; DOI=10.1016/S0022-2836(03)00789-7; RA Huffman J.L., Li H., White R.H., Tainer J.A.; RT "Structural basis for recognition and catalysis by the bifunctional RT dCTP deaminase and dUTPase from Methanococcus jannaschii."; RL J. Mol. Biol. 331:885-896(2003). CC -!- FUNCTION: Catalyzes two consecutive reactions to form dUMP using CC dCTP as substrate. CC -!- CATALYTIC ACTIVITY: dCTP + 2 H(2)O = dUMP + diphosphate + NH(3). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ENZYME REGULATION: Inhibited by dTTP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5.; CC Temperature dependence: CC Retains over 70% of its activity after heating at 90 degrees CC Celsius for 10 min.; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP: CC step 1/1. CC -!- SUBUNIT: Homohexamer. CC -!- MASS SPECTROMETRY: Mass=23619; Mass_error=94; Method=MALDI; CC Range=1-204; Evidence={ECO:0000269|PubMed:12538648}; CC -!- SIMILARITY: Belongs to the dCTP deaminase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98415.1; -; Genomic_DNA. DR PIR; F64353; F64353. DR PDB; 1OGH; X-ray; 1.88 A; A/B=1-204. DR PDB; 1PKH; X-ray; 1.42 A; A/B=1-204. DR PDB; 1PKJ; X-ray; 2.10 A; A/B=1-204. DR PDB; 1PKK; X-ray; 1.77 A; A/B=1-204. DR PDB; 2HXB; X-ray; 2.55 A; A=1-204. DR PDB; 2HXD; X-ray; 2.30 A; A=1-204. DR PDB; 3GF0; X-ray; 2.62 A; A=1-204. DR PDBsum; 1OGH; -. DR PDBsum; 1PKH; -. DR PDBsum; 1PKJ; -. DR PDBsum; 1PKK; -. DR PDBsum; 2HXB; -. DR PDBsum; 2HXD; -. DR PDBsum; 3GF0; -. DR ProteinModelPortal; Q57872; -. DR SMR; Q57872; 1-182. DR STRING; 243232.MJ_0430; -. DR MoonProt; Q57872; -. DR EnsemblBacteria; AAB98415; AAB98415; MJ_0430. DR KEGG; mja:MJ_0430; -. DR eggNOG; arCOG04048; Archaea. DR eggNOG; COG0717; LUCA. DR InParanoid; Q57872; -. DR KO; K09887; -. DR OMA; GWIDAGF; -. DR PhylomeDB; Q57872; -. DR BioCyc; MetaCyc:MONOMER-17894; -. DR BRENDA; 3.5.4.13; 3260. DR BRENDA; 3.5.4.30; 3260. DR BRENDA; 3.6.1.23; 3260. DR SABIO-RK; Q57872; -. DR UniPathway; UPA00610; UER00667. DR EvolutionaryTrace; Q57872; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033973; F:dCTP deaminase (dUMP-forming) activity; IEA:UniProtKB-EC. DR GO; GO:0008829; F:dCTP deaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006226; P:dUMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006229; P:dUTP biosynthetic process; IEA:InterPro. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IBA:GO_Central. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00146; dCTP_deaminase; 1. DR InterPro; IPR011962; dCTP_deam. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR008180; dUTPase/dCTP_deaminase. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. DR TIGRFAMs; TIGR02274; dCTP_deam; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Hydrolase; KW Magnesium; Nucleotide metabolism; Reference proteome. FT CHAIN 1 204 dCTP deaminase, dUMP-forming. FT /FTId=PRO_0000156029. FT MUTAGEN 135 135 D->N: Loss of activity. FT {ECO:0000269|PubMed:12538648}. FT MUTAGEN 145 145 E->Q: Loss of dCTP deaminase activity, FT but retains 25% dUTP pyrophosphatase FT activity. {ECO:0000269|PubMed:12538648}. FT HELIX 5 13 {ECO:0000244|PDB:1PKH}. FT STRAND 16 21 {ECO:0000244|PDB:1PKH}. FT HELIX 24 26 {ECO:0000244|PDB:1PKH}. FT STRAND 32 36 {ECO:0000244|PDB:1PKH}. FT STRAND 38 43 {ECO:0000244|PDB:1PKH}. FT STRAND 45 47 {ECO:0000244|PDB:1OGH}. FT STRAND 56 60 {ECO:0000244|PDB:1PKH}. FT STRAND 62 68 {ECO:0000244|PDB:1PKH}. FT HELIX 76 86 {ECO:0000244|PDB:1PKH}. FT STRAND 89 94 {ECO:0000244|PDB:1PKH}. FT STRAND 96 105 {ECO:0000244|PDB:1PKH}. FT STRAND 110 116 {ECO:0000244|PDB:1PKH}. FT HELIX 118 121 {ECO:0000244|PDB:1PKH}. FT TURN 122 124 {ECO:0000244|PDB:1PKH}. FT STRAND 125 127 {ECO:0000244|PDB:1PKH}. FT STRAND 139 151 {ECO:0000244|PDB:1PKH}. FT STRAND 153 156 {ECO:0000244|PDB:1PKH}. FT STRAND 160 168 {ECO:0000244|PDB:1PKH}. FT STRAND 176 180 {ECO:0000244|PDB:1PKH}. FT HELIX 196 198 {ECO:0000244|PDB:2HXD}. SQ SEQUENCE 204 AA; 23432 MW; 1218368057723371 CRC64; MILSDKDIID YVTSKRIIIK PFNKDFVGPC SYDVTLGDEF IIYDDEVYDL SKELNYKRIK IKNSILVCPL NYNLTEEKIN YFKEKYNVDY VVEGGVLGTT NEYIELPNDI SAQYQGRSSL GRVFLTSHQT AGWIDAGFKG KITLEIVAFD KPVILYKNQR IGQLIFSKLL SPADVGYSER KTSKYAYQKS VMPSLIHLDN HKKD // ID DHQS_METJA Reviewed; 361 AA. AC Q58646; DT 16-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=3-dehydroquinate synthase; DE Short=DHQ synthase; DE EC=1.4.1.24; DE AltName: Full=3-dehydroquinate synthase II; GN Name=aroB'; OrderedLocusNames=MJ1249; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A DHQ SYNTHASE, AND CATALYTIC ACTIVITY. RX PubMed=15182204; DOI=10.1021/bi0495127; RA White R.H.; RT "L-aspartate semialdehyde and a 6-deoxy-5-ketohexose 1-phosphate are RT the precursors to the aromatic amino acids in Methanocaldococcus RT jannaschii."; RL Biochemistry 43:7618-7627(2004). CC -!- FUNCTION: Catalyzes the oxidative deamination and cyclization of CC 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonic acid (ADH) to yield 3- CC dehydroquinate (DHQ), which is fed into the canonical shikimic CC pathway of aromatic amino acid biosynthesis. CC {ECO:0000269|PubMed:15182204}. CC -!- CATALYTIC ACTIVITY: 2-amino-3,7-dideoxy-D-threo-hept-6-ulosonate + CC H(2)O + NAD(+) = 3-dehydroquinate + NH(3) + NADH. CC {ECO:0000269|PubMed:15182204}. CC -!- SIMILARITY: Belongs to the archaeal-type DHQ synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99252.1; -; Genomic_DNA. DR PIR; H64455; H64455. DR ProteinModelPortal; Q58646; -. DR STRING; 243232.MJ_1249; -. DR EnsemblBacteria; AAB99252; AAB99252; MJ_1249. DR KEGG; mja:MJ_1249; -. DR eggNOG; arCOG04353; Archaea. DR eggNOG; COG1465; LUCA. DR InParanoid; Q58646; -. DR KO; K11646; -. DR OMA; GDRVCID; -. DR PhylomeDB; Q58646; -. DR BioCyc; MetaCyc:MONOMER-14595; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003856; F:3-dehydroquinate synthase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016639; F:oxidoreductase activity, acting on the CH-NH2 group of donors, NAD or NADP as acceptor; IEA:UniProtKB-HAMAP. DR GO; GO:0009073; P:aromatic amino acid family biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01244; Arch_DHQ_synthase; 1. DR InterPro; IPR002812; DHQ_synth. DR Pfam; PF01959; DHQS; 1. DR PIRSF; PIRSF006655; DHQ_synth; 1. DR ProDom; PD017907; DHQ_synth_pro-type; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 361 3-dehydroquinate synthase. FT /FTId=PRO_0000058769. SQ SEQUENCE 361 AA; 40260 MW; 8A072D5A4712D7FE CRC64; MKFGWVNVIG DNWEEKKKIV TTALESSIPV VVAEPEDIEK IKELGNIKVA SHSLDADIVL VNKNDNIEFL KEAKNLGKET AIYIPIESKE DEEFASEVAR FGFVDNIILE GRDWTIIPLE NLIADLFHRD VKIVASVNSV DEAKVAYEIL EKGTDGVLLN PKNLEDIKEL SKLIEEMNKE KVALDVATVT KVEPIGSGDR VCIDTCSLMK IGEGMLIGSY SRALFLVHSE TVENPYVATR PFRVNAGPVH AYILCPGNKT KYLSELKAGD KVLIVDKDGN TREAIVGRVK IERRPLVLIE AEYKGDIIRT ILQNAETIRL VNEKGEPISV VDLKPGDKVL IKPEEYARHF GMAIKETIIE K // ID DGGGP_METJA Reviewed; 283 AA. AC Q57727; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Digeranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286}; DE Short=DGGGP synthase {ECO:0000255|HAMAP-Rule:MF_01286}; DE Short=DGGGPS {ECO:0000255|HAMAP-Rule:MF_01286}; DE EC=2.5.1.42 {ECO:0000255|HAMAP-Rule:MF_01286}; DE AltName: Full=(S)-2,3-di-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01286}; DE AltName: Full=Geranylgeranylglycerol-phosphate geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_01286}; GN OrderedLocusNames=MJ0279; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the CC C2 hydroxyl of (S)-3-O-geranylgeranylglyceryl phosphate (GGGP). CC This reaction is the second ether-bond-formation step in the CC biosynthesis of archaeal membrane lipids. {ECO:0000255|HAMAP- CC Rule:MF_01286}. CC -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + sn-3-O- CC (geranylgeranyl)glycerol 1-phosphate = diphosphate + 2,3-bis-O- CC (geranylgeranyl)glycerol 1-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01286}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01286}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_01286}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01286}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01286}. CC -!- SIMILARITY: Belongs to the UbiA prenyltransferase family. DGGGP CC synthase subfamily. {ECO:0000255|HAMAP-Rule:MF_01286}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98267.1; -; Genomic_DNA. DR PIR; H64334; H64334. DR ProteinModelPortal; Q57727; -. DR STRING; 243232.MJ_0279; -. DR EnsemblBacteria; AAB98267; AAB98267; MJ_0279. DR KEGG; mja:MJ_0279; -. DR eggNOG; arCOG00476; Archaea. DR eggNOG; COG0382; LUCA. DR InParanoid; Q57727; -. DR KO; K17105; -. DR OMA; ALIIMND; -. DR PhylomeDB; Q57727; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0047295; F:geranylgeranylglycerol-phosphate geranylgeranyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004659; F:prenyltransferase activity; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01286; DGGGP_synth; 1. DR InterPro; IPR023547; DGGGP_synth. DR InterPro; IPR000537; UbiA_prenyltransferase. DR Pfam; PF01040; UbiA; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Magnesium; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 283 Digeranylgeranylglyceryl phosphate FT synthase. FT /FTId=PRO_0000106770. FT TRANSMEM 21 41 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 45 65 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 97 117 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 135 155 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 158 178 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 204 224 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 226 246 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. FT TRANSMEM 261 281 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01286}. SQ SEQUENCE 283 AA; 31754 MW; 9C98641137661413 CRC64; MGVFMEKLKT YLELIRVKNC ITASIGGIIG YLISSNFEID ILKSLLVFFV VFFVCAYGNV INDIFDIEID RINKPSRPLP SGKIKLNEAK KFSAILLILG LVLSLFINIY ALIIAVINAL FLYLYAKKYK KYKPIGNFII GYLTGSVFLF GGVAGKNVMP VVILFLCSLL SIWGREIVKD FEDMEGDKKE GVISLPIKYG KKSLYFATFL VVLAVILSPL PYILKIFGIW YLILIAICDI LFIYAMALLL KEPNKETASK VSKFLKIIMN IVLLAFIVGA IKL // ID DHOM_METJA Reviewed; 336 AA. AC Q58997; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Homoserine dehydrogenase; DE Short=HDH; DE EC=1.1.1.3; GN Name=hom; OrderedLocusNames=MJ1602; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: L-homoserine + NAD(P)(+) = L-aspartate 4- CC semialdehyde + NAD(P)H. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 3/3. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 3/5. CC -!- SIMILARITY: Belongs to the homoserine dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99622.1; -; Genomic_DNA. DR PIR; A64500; A64500. DR ProteinModelPortal; Q58997; -. DR STRING; 243232.MJ_1602; -. DR EnsemblBacteria; AAB99622; AAB99622; MJ_1602. DR KEGG; mja:MJ_1602; -. DR eggNOG; arCOG01351; Archaea. DR eggNOG; COG0460; LUCA. DR InParanoid; Q58997; -. DR KO; K00003; -. DR OMA; PSHITAV; -. DR PhylomeDB; Q58997; -. DR UniPathway; UPA00050; UER00063. DR UniPathway; UPA00051; UER00465. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004412; F:homoserine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009086; P:methionine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR005106; Asp/hSer_DH_NAD-bd. DR InterPro; IPR001342; HDH_cat. DR InterPro; IPR019811; HDH_CS. DR InterPro; IPR022697; HDH_short. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF00742; Homoserine_dh; 1. DR Pfam; PF03447; NAD_binding_3; 1. DR PIRSF; PIRSF036497; HDH_short; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS01042; HOMOSER_DHGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Isoleucine biosynthesis; Methionine biosynthesis; KW NADP; Oxidoreductase; Reference proteome; Threonine biosynthesis. FT CHAIN 1 336 Homoserine dehydrogenase. FT /FTId=PRO_0000066705. FT NP_BIND 6 13 NADP. {ECO:0000250}. FT ACT_SITE 223 223 Proton donor. {ECO:0000255}. FT BINDING 94 94 NADP. {ECO:0000250}. FT BINDING 123 123 NADP. {ECO:0000250}. FT BINDING 208 208 Substrate. {ECO:0000250}. SQ SEQUENCE 336 AA; 36462 MW; EDAEFA1998439B48 CRC64; MDIIIVGFGA IGKGIAKVLY DKKDYLKKNY EEFKVVAITD SSGAAIDEDG LDLLKAIEVK EKTGKIKNYP EKGREMSSID VIKEVDADVV VEVTPSNLET GDPAKTHILE SFKNKKHVVT ANKGPLALCY KELIEEAKKH GVIFRHEASV GGAMPIINLA KETLAGNEIL SIRGILNGTT NYILTKMEKE GLDFETALKE AKELGIAETD PTQDIEGLDT AAKIVILANS IMGMNKTIKD VKVKGISRIT PEALFLANKR GYTIKLIGQI KDGYLIVEPM LVPIDSPLNV KGTLNVAMFE TDLAKEVVVV GRGAGPIETA SAILSDLIHI YNSTKK // ID DHYS_METJA Reviewed; 330 AA. AC Q58224; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-OCT-2002, sequence version 3. DT 11-NOV-2015, entry version 101. DE RecName: Full=Probable deoxyhypusine synthase; DE Short=DHS; DE EC=2.5.1.46; GN Name=dys; OrderedLocusNames=MJ0814; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the NAD-dependent oxidative cleavage of CC spermidine and the subsequent transfer of the butylamine moiety of CC spermidine to the epsilon-amino group of a specific lysine residue CC of the eIF-5A precursor protein to form the intermediate CC deoxyhypusine residue. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: [eIF5A-precursor]-lysine + spermidine = CC [eIF5A-precursor]-deoxyhypusine + propane-1,3-diamine. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- PATHWAY: Protein modification; eIF5A hypusination. CC -!- SIMILARITY: Belongs to the deoxyhypusine synthase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98813.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98813.1; ALT_INIT; Genomic_DNA. DR PIR; F64401; F64401. DR ProteinModelPortal; Q58224; -. DR STRING; 243232.MJ_0814; -. DR EnsemblBacteria; AAB98813; AAB98813; MJ_0814. DR KEGG; mja:MJ_0814; -. DR eggNOG; arCOG04142; Archaea. DR eggNOG; COG1899; LUCA. DR InParanoid; Q58224; -. DR KO; K00809; -. DR OMA; IWEMGKW; -. DR PhylomeDB; Q58224; -. DR UniPathway; UPA00354; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0034038; F:deoxyhypusine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050983; P:deoxyhypusine biosynthetic process from spermidine; IEA:UniProtKB-HAMAP. DR GO; GO:0008612; P:peptidyl-lysine modification to peptidyl-hypusine; IEA:UniProtKB-KW. DR Gene3D; 3.40.910.10; -; 1. DR HAMAP; MF_00153; DHS; 1. DR InterPro; IPR022899; Deoxyhypus_synthase_arc. DR InterPro; IPR002773; Deoxyhypusine_synthase. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR PANTHER; PTHR11703; PTHR11703; 1. DR Pfam; PF01916; DS; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR TIGRFAMs; TIGR00321; dhys; 1. PE 3: Inferred from homology; KW Complete proteome; Hypusine biosynthesis; NAD; Reference proteome; KW Transferase. FT CHAIN 1 330 Probable deoxyhypusine synthase. FT /FTId=PRO_0000134495. FT ACT_SITE 303 303 Nucleophile. {ECO:0000250}. SQ SEQUENCE 330 AA; 37581 MW; FADF38ED01F5D9F9 CRC64; MLKESEDIEG IAIEGPWLED DISLEEIIKK YYLKIGFQAS HIGKAIKIWK HIEEKRKKGD EITVFFGYTS NIVSSGLREI IAYLVKHKKI DIIVTTAGGV EEDFIKCLKP FILGDWEVDG KMLREKGINR IGNIFVPNDR YIAFEEYMME FFEEILNLQR ETGKIITASE FCYKLGEFMD KKLKSKEKEK SILYWAYKNN IPIFCPAITD GSIGDMLYFF KKYNKDEELK IDVANDIVKL NDIAINSKET ACIVLGGSLP KHSIINANLF REGTDYAIYV TTALPWDGSL SGAPPEEGVS WGKIGAKADY VEIWGDATII FPLLVYCVMK // ID DNAG_METJA Reviewed; 424 AA. AC Q58603; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=DNA primase DnaG {ECO:0000255|HAMAP-Rule:MF_00007}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00007}; GN Name=dnaG {ECO:0000255|HAMAP-Rule:MF_00007}; OrderedLocusNames=MJ1206; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: RNA polymerase that catalyzes the synthesis of short RNA CC molecules used as primers for DNA polymerase during DNA CC replication. {ECO:0000255|HAMAP-Rule:MF_00007}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00007}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00007}; CC -!- SUBUNIT: Forms a ternary complex with MCM helicase and DNA. CC {ECO:0000255|HAMAP-Rule:MF_00007}. CC -!- SIMILARITY: Belongs to the archaeal DnaG primase family. CC {ECO:0000255|HAMAP-Rule:MF_00007}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99210.1; -; Genomic_DNA. DR PIR; E64450; E64450. DR ProteinModelPortal; Q58603; -. DR STRING; 243232.MJ_1206; -. DR EnsemblBacteria; AAB99210; AAB99210; MJ_1206. DR KEGG; mja:MJ_1206; -. DR eggNOG; arCOG04281; Archaea. DR eggNOG; COG0358; LUCA. DR InParanoid; Q58603; -. DR OMA; KESVRMG; -. DR PhylomeDB; Q58603; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000178; C:exosome (RNase complex); IEA:InterPro. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008143; F:poly(A) binding; IEA:InterPro. DR HAMAP; MF_00007; DNA_primase_DnaG_arc; 1. DR InterPro; IPR020607; Primase_DnaG_arc. DR InterPro; IPR006171; Toprim_domain. DR Pfam; PF13662; Toprim_4; 1. DR SMART; SM00493; TOPRIM; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-directed RNA polymerase; KW Magnesium; Metal-binding; Nucleotidyltransferase; Primosome; KW Reference proteome; Transcription; Transferase. FT CHAIN 1 424 DNA primase DnaG. FT /FTId=PRO_0000144125. FT DOMAIN 171 245 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00007}. FT METAL 177 177 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00007}. FT METAL 219 219 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00007}. FT METAL 219 219 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00007}. FT METAL 221 221 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00007}. SQ SEQUENCE 424 AA; 47388 MW; C55BC7A05B0EB2C3 CRC64; MIIMDLGTTK YIIYAELIAD GYVEKHDVIG AIFGQTEGLL GDELDLRELQ KTGRVGRIDV ELTNINGKSI AKITVPSSLD RIETSILAAT LETIDRVGPC VATVKVIDIE DIRKKKREYI VERAKEILKQ LMSNIDVNTI IEEVKESVRM GEIIEYGPER LPAGPAVDSS DDIIVVEGRA DVLNLLRCGI KNVIAVEGTS VPKTIIELSK KKIVTVFTDG DRGGELILKE LLQVCDVDFV ARAPPGKEVE ELSKKEIMKC LRSKIPAEHI LAQILKDKQK IDEKVCKDEI RNMGIQTIPE IKPEISITSN DDVEVSSVEC NPSNNEELPP KYNKYRKFYE KLIELEDSKV LIINGDKEEI VSIEELINNT DNYKSIDAII INGTVTQKLI DILYEKTNLI FCKDAKIIKK PVNLTLITFG DLNA // ID DHAS_METJA Reviewed; 354 AA. AC Q57658; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 112. DE RecName: Full=Aspartate-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASA dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; DE Short=ASADH {ECO:0000255|HAMAP-Rule:MF_02121}; DE EC=1.2.1.11; DE AltName: Full=Aspartate-beta-semialdehyde dehydrogenase {ECO:0000255|HAMAP-Rule:MF_02121}; GN Name=asd {ECO:0000255|HAMAP-Rule:MF_02121}; OrderedLocusNames=MJ0205; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.29 ANGSTROMS) IN COMPLEX WITH NADP, FUNCTION, RP CATALYTIC ACTIVITY, COENZYME SPECIFICITY, BIOPHYSICOCHEMICAL RP PROPERTIES, DOMAIN, AND SUBUNIT. RX PubMed=16225889; DOI=10.1016/j.jmb.2005.09.027; RA Faehnle C.R., Ohren J.F., Viola R.E.; RT "A new branch in the family: structure of aspartate-beta-semialdehyde RT dehydrogenase from Methanococcus jannaschii."; RL J. Mol. Biol. 353:1055-1068(2005). CC -!- FUNCTION: Catalyzes the NADPH-dependent formation of L-aspartate- CC semialdehyde (L-ASA) by the reductive dephosphorylation of L- CC aspartyl-4-phosphate. To a lesser extent, is able to use NAD CC instead of NADP. {ECO:0000269|PubMed:16225889}. CC -!- CATALYTIC ACTIVITY: L-aspartate 4-semialdehyde + phosphate + CC NADP(+) = L-4-aspartyl phosphate + NADPH. CC {ECO:0000269|PubMed:16225889}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=13 uM for NADP(+) {ECO:0000269|PubMed:16225889}; CC KM=1700 uM for NAD(+) {ECO:0000269|PubMed:16225889}; CC Note=kcat is 4 sec(-1) for the L-4-aspartyl-phosphate-forming CC reaction (at 70 degrees Celsius).; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:16225889}; CC -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP CC pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway; L-homoserine from L-aspartate: step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_02121}. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_02121}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16225889}. CC -!- DOMAIN: Consists of two domains, an N-terminal nucleotide-binding CC domain and a C-terminal dimerization domain. CC {ECO:0000269|PubMed:16225889}. CC -!- SIMILARITY: Belongs to the aspartate-semialdehyde dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_02121}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98189.1; -; Genomic_DNA. DR PIR; F64325; F64325. DR PDB; 1YS4; X-ray; 2.29 A; A/B=1-354. DR PDBsum; 1YS4; -. DR ProteinModelPortal; Q57658; -. DR SMR; Q57658; 7-354. DR STRING; 243232.MJ_0205; -. DR EnsemblBacteria; AAB98189; AAB98189; MJ_0205. DR KEGG; mja:MJ_0205; -. DR eggNOG; arCOG00494; Archaea. DR eggNOG; COG0136; LUCA. DR InParanoid; Q57658; -. DR KO; K00133; -. DR OMA; ASCHRVP; -. DR PhylomeDB; Q57658; -. DR UniPathway; UPA00034; UER00016. DR UniPathway; UPA00050; UER00463. DR UniPathway; UPA00051; UER00464. DR EvolutionaryTrace; Q57658; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004073; F:aspartate-semialdehyde dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003942; F:N-acetyl-gamma-glutamyl-phosphate reductase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0071266; P:'de novo' L-methionine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006531; P:aspartate metabolic process; IEA:InterPro. DR GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:InterPro. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_02121; ASADH; 1. DR InterPro; IPR000319; Asp-semialdehyde_DH_CS. DR InterPro; IPR005676; Asp_semi-ald_DH_pep-lack. DR InterPro; IPR012080; Asp_semialdehyde_DH. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000534; Semialdehyde_DH_NAD-bd. DR InterPro; IPR012280; Semialdhyde_DH_dimer_dom. DR Pfam; PF01118; Semialdhyde_dh; 1. DR Pfam; PF02774; Semialdhyde_dhC; 1. DR PIRSF; PIRSF000148; ASA_dh; 1. DR SMART; SM00859; Semialdhyde_dh; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00978; asd_EA; 1. DR PROSITE; PS01103; ASD; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; KW Diaminopimelate biosynthesis; Lysine biosynthesis; KW Methionine biosynthesis; NAD; NADP; Oxidoreductase; KW Reference proteome; Threonine biosynthesis. FT CHAIN 1 354 Aspartate-semialdehyde dehydrogenase. FT /FTId=PRO_0000141397. FT NP_BIND 17 20 NADP. {ECO:0000269|PubMed:16225889}. FT NP_BIND 42 45 NADP. {ECO:0000269|PubMed:16225889}. FT NP_BIND 187 188 NADP. {ECO:0000269|PubMed:16225889}. FT NP_BIND 333 334 NADP. {ECO:0000269|PubMed:16225889}. FT ACT_SITE 157 157 Acyl-thioester intermediate. FT {ECO:0000305|PubMed:16225889}. FT ACT_SITE 250 250 Proton acceptor. FT {ECO:0000305|PubMed:16225889}. FT BINDING 118 118 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 184 184 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 210 210 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 213 213 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT BINDING 243 243 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02121}. FT STRAND 9 14 {ECO:0000244|PDB:1YS4}. FT TURN 15 17 {ECO:0000244|PDB:1YS4}. FT HELIX 19 28 {ECO:0000244|PDB:1YS4}. FT STRAND 32 41 {ECO:0000244|PDB:1YS4}. FT TURN 43 47 {ECO:0000244|PDB:1YS4}. FT HELIX 50 53 {ECO:0000244|PDB:1YS4}. FT TURN 64 68 {ECO:0000244|PDB:1YS4}. FT STRAND 72 74 {ECO:0000244|PDB:1YS4}. FT HELIX 79 81 {ECO:0000244|PDB:1YS4}. FT STRAND 86 89 {ECO:0000244|PDB:1YS4}. FT HELIX 93 105 {ECO:0000244|PDB:1YS4}. FT STRAND 109 112 {ECO:0000244|PDB:1YS4}. FT TURN 116 119 {ECO:0000244|PDB:1YS4}. FT HELIX 128 131 {ECO:0000244|PDB:1YS4}. FT HELIX 132 136 {ECO:0000244|PDB:1YS4}. FT HELIX 137 145 {ECO:0000244|PDB:1YS4}. FT STRAND 148 153 {ECO:0000244|PDB:1YS4}. FT HELIX 157 173 {ECO:0000244|PDB:1YS4}. FT STRAND 176 184 {ECO:0000244|PDB:1YS4}. FT HELIX 187 189 {ECO:0000244|PDB:1YS4}. FT TURN 191 193 {ECO:0000244|PDB:1YS4}. FT HELIX 196 199 {ECO:0000244|PDB:1YS4}. FT HELIX 210 221 {ECO:0000244|PDB:1YS4}. FT STRAND 223 226 {ECO:0000244|PDB:1YS4}. FT STRAND 229 231 {ECO:0000244|PDB:1YS4}. FT STRAND 236 240 {ECO:0000244|PDB:1YS4}. FT STRAND 250 257 {ECO:0000244|PDB:1YS4}. FT HELIX 264 273 {ECO:0000244|PDB:1YS4}. FT TURN 276 279 {ECO:0000244|PDB:1YS4}. FT STRAND 288 291 {ECO:0000244|PDB:1YS4}. FT HELIX 300 303 {ECO:0000244|PDB:1YS4}. FT HELIX 306 309 {ECO:0000244|PDB:1YS4}. FT STRAND 311 319 {ECO:0000244|PDB:1YS4}. FT STRAND 321 331 {ECO:0000244|PDB:1YS4}. FT TURN 333 338 {ECO:0000244|PDB:1YS4}. FT HELIX 339 352 {ECO:0000244|PDB:1YS4}. SQ SEQUENCE 354 AA; 39439 MW; 5C412CA5C39B166E CRC64; MSKGEKMKIK VGVLGATGSV GQRFVQLLAD HPMFELTALA ASERSAGKKY KDACYWFQDR DIPENIKDMV VIPTDPKHEE FEDVDIVFSA LPSDLAKKFE PEFAKEGKLI FSNASAYRME EDVPLVIPEV NADHLELIEI QREKRGWDGA IITNPNCSTI CAVITLKPIM DKFGLEAVFI ATMQAVSGAG YNGVPSMAIL DNLIPFIKNE EEKMQTESLK LLGTLKDGKV ELANFKISAS CNRVAVIDGH TESIFVKTKE GAEPEEIKEV MDKFDPLKDL NLPTYAKPIV IREEIDRPQP RLDRNEGNGM SIVVGRIRKD PIFDVKYTAL EHNTIRGAAG ASVLNAEYFV KKYI // ID DPHB_METJA Reviewed; 257 AA. AC Q58670; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Diphthine synthase {ECO:0000255|HAMAP-Rule:MF_01084}; DE EC=2.1.1.98 {ECO:0000255|HAMAP-Rule:MF_01084}; DE AltName: Full=Diphthamide biosynthesis methyltransferase {ECO:0000255|HAMAP-Rule:MF_01084}; GN Name=dphB {ECO:0000255|HAMAP-Rule:MF_01084}; OrderedLocusNames=MJ1274; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC catalyzes the trimethylation of the amino group of the modified CC target histidine residue in translation elongation factor 2 (EF- CC 2), to form an intermediate called diphthine. The three successive CC methylation reactions represent the second step of diphthamide CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01084}. CC -!- CATALYTIC ACTIVITY: 3 S-adenosyl-L-methionine + 2-((3S)-3-carboxy- CC 3-aminopropyl)-L-histidine-[translation elongation factor 2] = 3 CC S-adenosyl-L-homocysteine + diphthine-[translation elongation CC factor 2]. {ECO:0000255|HAMAP-Rule:MF_01084}. CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01084}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01084}. CC -!- SIMILARITY: Belongs to the diphthine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01084}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99280.1; -; Genomic_DNA. DR PIR; A64459; A64459. DR ProteinModelPortal; Q58670; -. DR SMR; Q58670; 1-254. DR STRING; 243232.MJ_1274; -. DR EnsemblBacteria; AAB99280; AAB99280; MJ_1274. DR KEGG; mja:MJ_1274; -. DR eggNOG; arCOG04161; Archaea. DR eggNOG; COG1798; LUCA. DR InParanoid; Q58670; -. DR KO; K00586; -. DR OMA; TLQQMCT; -. DR PhylomeDB; Q58670; -. DR UniPathway; UPA00559; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004164; F:diphthine synthase activity; IBA:GO_Central. DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR HAMAP; MF_01084; Diphthine_synth; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR004551; Dphthn_synthase. DR Pfam; PF00590; TP_methylase; 1. DR PIRSF; PIRSF036432; Diphthine_synth; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR00522; dph5; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 257 Diphthine synthase. FT /FTId=PRO_0000156118. FT REGION 113 114 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_01084}. FT BINDING 9 9 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01084}. FT BINDING 85 85 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01084}. FT BINDING 88 88 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01084}. FT BINDING 164 164 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01084}. FT BINDING 209 209 S-adenosyl-L-methionine; via amide FT nitrogen and carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01084}. FT BINDING 234 234 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01084}. SQ SEQUENCE 257 AA; 29037 MW; 467B1CC2720108B7 CRC64; MLILAGLGLY DENDMTLKTL KFAKKAEKIY AEFYTAVLTG TTTEKIEEVL GKKIHVLSRK DVEYNGYKLI EEAKDKDIMF LTAGDPMVAT THVDLAIEAK KKGIEVLIIN APSIYSAVGI TGLQLYKFGK TTSIVFPEEN YFPETPYNVI KENLERGLHT LCLLDIRIDE NEKRFMTANE GLKVLLELEN RKKEGIINED TKAVVVARAG SLKPKLVYGK IKDLINYDFG EPLHCIIIPG KLHFMEEDAL KYLCENI // ID DKFP_METJA Reviewed; 310 AA. AC Q58980; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Fructose-bisphosphate aldolase/6-deoxy-5-ketofructose 1-phosphate synthase; DE EC=2.2.1.11; DE EC=4.1.2.13; DE AltName: Full=DKFP synthase; DE AltName: Full=Fructose-bisphosphate aldolase class 1; DE AltName: Full=Fructose-bisphosphate aldolase class I; DE Short=FBP aldolase; GN OrderedLocusNames=MJ1585; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A FRUCTOSE-BISPHOSPHATE ALDOLASE AND DKFP SYNTHASE, AND RP CATALYTIC ACTIVITY. RX PubMed=17014089; DOI=10.1021/bi061018a; RA White R.H., Xu H.; RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5- RT ketofructose-1-phosphate: a precursor for aromatic amino acid RT biosynthesis in Methanocaldococcus jannaschii."; RL Biochemistry 45:12366-12379(2006). CC -!- FUNCTION: Catalyzes the transaldolisation of either fructose-1-P CC or fructose-1,6-bisphosphate with methylglyoxal to produce 6- CC deoxy-5-ketofructose-1-phosphate (DKFP). Also catalyzes the CC reversible aldol condensation of dihydroxyacetone phosphate (DHAP CC or glycerone-phosphate) with glyceraldehyde 3-phosphate (G3P or CC GAP) to produce fructose 1,6-bisphosphate (FBP). CC {ECO:0000269|PubMed:17014089}. CC -!- CATALYTIC ACTIVITY: D-fructose 1,6-bisphosphate = glycerone CC phosphate + D-glyceraldehyde 3-phosphate. CC {ECO:0000269|PubMed:17014089}. CC -!- CATALYTIC ACTIVITY: Methylglyoxal + D-fructose 1,6-bisphosphate = CC D-glyceraldehyde 3-phosphate + 1-deoxy-D-threo-hexo-2,5-diulose 6- CC phosphate. {ECO:0000269|PubMed:17014089}. CC -!- CATALYTIC ACTIVITY: Methylglyoxal + D-fructose 1-phosphate = D- CC glyceraldehyde + 1-deoxy-D-threo-hexo-2,5-diulose 6-phosphate. CC {ECO:0000269|PubMed:17014089}. CC -!- PATHWAY: Aromatic compound metabolism. CC -!- SIMILARITY: Belongs to the DeoC/FbaB aldolase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99604.1; -; Genomic_DNA. DR PIR; H64497; H64497. DR ProteinModelPortal; Q58980; -. DR STRING; 243232.MJ_1585; -. DR EnsemblBacteria; AAB99604; AAB99604; MJ_1585. DR KEGG; mja:MJ_1585; -. DR eggNOG; arCOG04044; Archaea. DR eggNOG; COG1830; LUCA. DR InParanoid; Q58980; -. DR KO; K16305; -. DR OMA; RNIHQRP; -. DR PhylomeDB; Q58980; -. DR BioCyc; MetaCyc:MONOMER-14590; -. DR BRENDA; 2.2.1.11; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004332; F:fructose-bisphosphate aldolase activity; IDA:UniProtKB. DR GO; GO:0016744; F:transferase activity, transferring aldehyde or ketonic groups; IDA:UniProtKB. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR002915; DeoC/FbaB/lacD_aldolase. DR Pfam; PF01791; DeoC; 1. DR PIRSF; PIRSF038992; Aldolase_Ia; 1. DR SMART; SM01133; DeoC; 1. PE 1: Evidence at protein level; KW Complete proteome; Lyase; Reference proteome; Schiff base; KW Transferase. FT CHAIN 1 310 Fructose-bisphosphate aldolase/6-deoxy-5- FT ketofructose 1-phosphate synthase. FT /FTId=PRO_0000138958. FT REGION 48 49 Substrate binding. {ECO:0000250}. FT REGION 213 215 Substrate binding. {ECO:0000250}. FT REGION 241 243 Substrate binding. {ECO:0000250}. FT REGION 270 271 Substrate binding. {ECO:0000250}. FT ACT_SITE 182 182 Proton donor. {ECO:0000250}. FT ACT_SITE 213 213 Schiff-base intermediate with FT dihydroxyacetone-P. {ECO:0000250}. FT ACT_SITE 213 213 Schiff-base intermediate with substrate. FT {ECO:0000250}. FT BINDING 53 53 Substrate. {ECO:0000250}. FT BINDING 57 57 Substrate. {ECO:0000250}. FT BINDING 180 180 Substrate. {ECO:0000250}. FT BINDING 184 184 Substrate. {ECO:0000250}. SQ SEQUENCE 310 AA; 34574 MW; 4AB6286F888049C0 CRC64; MGIFMIKRLK KRDVKVPLTV PEDRKEEYIK NYLELTKRTG NVMLFAGDQK IEHLNDDFFG EGIAKDDASP EHLFNIASKG KICGFATQLG LIARYGMDYK KIPYIVKINS KTHLVKTRDP ISRALVHVKD VVDLKENSGL KILGVGYTIY PGSEYEHIMF EEASRVILEA HKHGLIAIIW SYPRGKNVKD EKDPHLIAGA AGVAACLGAD FVKVNYPKCD NPAERFKEAV LAAGRTGVLC AGGKSIEPEK FLKQIWEQIN ISGARGNATG RNIHQKPLDA AIRMCNAIYA ITIEGKSLEE ALKIYYGDRK // ID DP2S_METJA Reviewed; 594 AA. AC Q58113; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=DNA polymerase II small subunit; DE Short=Pol II; DE EC=2.7.7.7; GN Name=polB; OrderedLocusNames=MJ0702; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) CC and an exonucleolytic activity that degrades single-stranded DNA CC in the 3' to 5' direction. Has a template-primer preference which CC is characteristic of a replicative DNA polymerase (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts CC progressively in a 3'- to 5'-direction, releasing nucleoside 5'- CC phosphates. CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DNA polymerase delta/II small subunit CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98694.1; -; Genomic_DNA. DR PIR; F64387; F64387. DR ProteinModelPortal; Q58113; -. DR STRING; 243232.MJ_0702; -. DR DNASU; 1451569; -. DR EnsemblBacteria; AAB98694; AAB98694; MJ_0702. DR KEGG; mja:MJ_0702; -. DR eggNOG; arCOG04455; Archaea. DR eggNOG; COG1311; LUCA. DR InParanoid; Q58113; -. DR KO; K02323; -. DR OMA; GRVNHRP; -. DR PhylomeDB; Q58113; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 1. DR HAMAP; MF_00325; DNApol_II_A_arch; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR024826; DNA_pol_delta/II_ssu. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR011149; Pol2_small_arc. DR PANTHER; PTHR10416; PTHR10416; 1. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000803; Arc_Pol2_small; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 594 DNA polymerase II small subunit. FT /FTId=PRO_0000096177. SQ SEQUENCE 594 AA; 69145 MW; FA8F24702F2DE8FD CRC64; MEIINKFLDL EALLSPTVYE KLKNFDEEKL KRLIQKIREF KKYNNAFILL DEKFLDIFLQ KDLDEIINEY KDFDFIFYYT GEEEKEKPKE VKKEIKKETE EKIEKEKIEF VKKEEKEQFI KKSDEDVEEK LKQLISKEEK KEDFDAERAK RYEHITKIKE SVNSRIKWIA KDIDAVIEIY EDSDVSGKST CTGTIEDFVK YFRDRFERLK VFIERKAQRK GYPLKDIKKM KGQKDIFVVG IVSDVDSTRN GNLIVRIEDT EDEATLILPK EKIEAGKIPD DILLDEVIGA IGTVSKSGSS IYVDEIIRPA LPPKEPKRID EEIYMAFLSD IHVGSKEFLH KEFEKFIRFL NGDVDNELEE KVVSRLKYIC IAGDLVDGVG VYPGQEEDLY EVDIIEQYRE IAMYLDQIPE HISIIISPGN HDAVRPAEPQ PKLPEKITKL FNRDNIYFVG NPCTLNIHGF DTLLYHGRSF DDLVGQIRAA SYENPVTIMK ELIKRRLLCP TYGGRCPIAP EHKDYLVIDR DIDILHTGHI HINGYGIYRG VVMVNSGTFQ EQTDFQKRMG ISPTPAIVPI INMAKVGEKG HYLEWDRGVL EVRY // ID DPH2_METJA Reviewed; 340 AA. AC Q57907; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=2-(3-amino-3-carboxypropyl)histidine synthase; DE EC=2.5.1.108; DE AltName: Full=Diphthamide biosynthesis protein Dph2; DE AltName: Full=S-adenosyl-L-methionine:L-histidine 3-amino-3-carboxypropyltransferase; GN Name=dph2; OrderedLocusNames=MJ0483; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the first step of diphthamide biosynthesis, CC i.e. the transfer of the 3-amino-3-carboxypropyl group from S- CC adenosyl-L-methionine (SAM) to the C2 position of the imidazole CC ring of the target histidine residue in translation elongation CC factor 2 (EF-2) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-histidine-[translation elongation factor 2] CC + S-adenosyl-L-methionine = 2-((3S)-3-amino-3-carboxypropyl)-L- CC histidine-[translation elongation factor 2] + S-methyl-5'- CC thioadenosine. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000250}; CC -!- PATHWAY: Protein modification; peptidyl-diphthamide biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- MISCELLANEOUS: Unlike the enzymes in the radical SAM superfamily, CC Dph2 does not form the canonical 5'-deoxyadenosyl radical. CC Instead, it breaks the C(gamma)-S bond of SAM and generates a 3- CC amino-3-carboxypropyl radical intermediate (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DPH1/DPH2 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98474.1; -; Genomic_DNA. DR PIR; C64360; C64360. DR ProteinModelPortal; Q57907; -. DR STRING; 243232.MJ_0483; -. DR EnsemblBacteria; AAB98474; AAB98474; MJ_0483. DR KEGG; mja:MJ_0483; -. DR eggNOG; arCOG04112; Archaea. DR eggNOG; COG1736; LUCA. DR InParanoid; Q57907; -. DR KO; K07561; -. DR OMA; TCFGACD; -. DR PhylomeDB; Q57907; -. DR UniPathway; UPA00559; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0017183; P:peptidyl-diphthamide biosynthetic process from peptidyl-histidine; IBA:GO_Central. DR InterPro; IPR016435; DPH1/DPH2. DR InterPro; IPR022428; DPH2_arc. DR PANTHER; PTHR10762; PTHR10762; 1. DR Pfam; PF01866; Diphthamide_syn; 1. DR TIGRFAMs; TIGR03682; arCOG04112; 1. DR TIGRFAMs; TIGR00322; diphth2_R; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 340 2-(3-amino-3-carboxypropyl)histidine FT synthase. FT /FTId=PRO_0000106891. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 173 173 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 299 299 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 340 AA; 40014 MW; 9BBFA6B67179F392 CRC64; MLFKTIFYQK LQKKVTTLFN LETERVIREI ENLNKNNPKV IFQAPEGLKL KVEKEIEKIK QYFKQKNINI EIYLWGNTCF GACDLIDNHV KNLNVDLIIH YGHEKLSYAN PEIKTLFIPA YHIFNKDEEE KILNDIKNFI EKHKSGGKKV AIATTIQYKK LLKDFNPSII LGCRGEVKEG DVILFVGTGR FHPLMIAYKY QKEVFIYNPL SKCFDKISEE EINKFIKKRI LAISKLLLNK PKKVGVVLST KKGQCRKRVF DEIIKLLEEN DVNYLPILVD NISPDILFYD VDCYIIVACP RIVLDDYILY KKPIYTPEEF KLFLKNSFKY KFDEIKEDDF // ID DHPSL_METJA Reviewed; 294 AA. AC Q57749; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 86. DE RecName: Full=7,8-dihydropterin-6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate synthase; DE EC=2.5.1.105; GN OrderedLocusNames=MJ0301; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A PTEROATE SYNTHASE, CATALYTIC ACTIVITY, AND SUBSTRATE RP SPECIFICITY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10426953; DOI=10.1038/11525; RA Xu H., Aurora R., Rose G.D., White R.H.; RT "Identifying two ancient enzymes in Archaea using predicted secondary RT structure alignment."; RL Nat. Struct. Biol. 6:750-754(1999). CC -!- FUNCTION: Catalyzes the condensation of 6-hydroxymethyl-7,8- CC dihydropterin pyrophosphate (DHPP) with 4-(beta-D-ribofuranosyl)- CC aminobenzene-5'-phosphate (beta-RFA-P) to form 7,8-dihydropterin- CC 6-methyl-4-(beta-D-ribofuranosyl)-aminobenzene-5'-phosphate, a CC precursor in the biosynthesis of 5,6,7,8-tetrahydromethanopterin CC (H4MPT). To a lesser extent, is able to condense beta-RFA-P with CC another arylamine, 1-(4-aminophenyl)-1-deoxy-D-ribitol (APDR), to CC form 7,8-dihydropterin-6-methyl-1-(4-aminophenyl)-1-deoxy-D- CC ribitol. Dephosphorylated beta-RFA-P is not a substrate. CC {ECO:0000269|PubMed:10426953}. CC -!- CATALYTIC ACTIVITY: (7,8-dihydropterin-6-yl)methyl diphosphate + CC 4-(beta-D-ribofuranosyl)aniline 5'-phosphate = N-((7,8- CC dihydropterin-6-yl)methyl)-4-(beta-D-ribofuranosyl)aniline 5'- CC phosphate + diphosphate. {ECO:0000269|PubMed:10426953}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98288.1; -; Genomic_DNA. DR PIR; F64337; F64337. DR ProteinModelPortal; Q57749; -. DR STRING; 243232.MJ_0301; -. DR EnsemblBacteria; AAB98288; AAB98288; MJ_0301. DR KEGG; mja:MJ_0301; -. DR eggNOG; arCOG00503; Archaea. DR eggNOG; COG1237; LUCA. DR InParanoid; Q57749; -. DR KO; K06897; -. DR OMA; QFRHEIA; -. DR PhylomeDB; Q57749; -. DR BioCyc; MetaCyc:MONOMER-14570; -. DR BRENDA; 2.5.1.105; 3260. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB. DR GO; GO:0009108; P:coenzyme biosynthetic process; IDA:UniProtKB. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IDA:UniProtKB. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 1: Evidence at protein level; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1 294 7,8-dihydropterin-6-methyl-4-(beta-D- FT ribofuranosyl)-aminobenzene-5'-phosphate FT synthase. FT /FTId=PRO_0000106783. FT BINDING 116 116 Substrate. {ECO:0000250}. FT BINDING 186 186 Substrate. {ECO:0000250}. FT BINDING 228 228 Substrate. {ECO:0000250}. FT BINDING 265 265 Substrate. {ECO:0000250}. SQ SEQUENCE 294 AA; 33076 MW; 0FC92953FF9E005A CRC64; MLMNIGKVDN IKIYTLAEDY AGYNSPFWSQ HGLSFLIEVE SNGIKKRILF DTATYAEPIL FNMKLLNINP KSIDMIILSH NHFDHTGGLF GIMKEINKEI PIFAHPNIFK VSFATEPEFM LAGTLNKTLK EDIEKLGGRW VLSRDPIRLM PGIFTLGEIE DEEKINFEKK PTIGLYKLEN GRVVLDNVED EIGLAIVTEK GLIIVSGCSH PGIVSMVKKS IKISGINKVY AVIGGFHLID ADNERIVSTI KALKKLGVKK ICTGHCTGFK AENMFMEEFK EDFERLHAGK IIKF // ID DNLI_METJA Reviewed; 573 AA. AC Q57635; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=DNA ligase {ECO:0000255|HAMAP-Rule:MF_00407}; DE EC=6.5.1.1 {ECO:0000255|HAMAP-Rule:MF_00407}; DE AltName: Full=Polydeoxyribonucleotide synthase [ATP] {ECO:0000255|HAMAP-Rule:MF_00407}; GN Name=lig {ECO:0000255|HAMAP-Rule:MF_00407}; OrderedLocusNames=MJ0171; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA ligase that seals nicks in double-stranded DNA CC during DNA replication, DNA recombination and DNA repair. CC {ECO:0000255|HAMAP-Rule:MF_00407}. CC -!- CATALYTIC ACTIVITY: ATP + (deoxyribonucleotide)(n) + CC (deoxyribonucleotide)(m) = AMP + diphosphate + CC (deoxyribonucleotide)(n+m). {ECO:0000255|HAMAP-Rule:MF_00407}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00407}; CC -!- SIMILARITY: Belongs to the ATP-dependent DNA ligase family. CC {ECO:0000255|HAMAP-Rule:MF_00407}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98156.1; -; Genomic_DNA. DR PIR; D64321; D64321. DR ProteinModelPortal; Q57635; -. DR STRING; 243232.MJ_0171; -. DR EnsemblBacteria; AAB98156; AAB98156; MJ_0171. DR KEGG; mja:MJ_0171; -. DR eggNOG; arCOG01347; Archaea. DR eggNOG; COG1793; LUCA. DR InParanoid; Q57635; -. DR KO; K10747; -. DR OMA; EWGYGRR; -. DR PhylomeDB; Q57635; -. DR BRENDA; 6.5.1.1; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003910; F:DNA ligase (ATP) activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW. DR GO; GO:0071897; P:DNA biosynthetic process; IEA:InterPro. DR GO; GO:0051103; P:DNA ligation involved in DNA repair; IBA:GO_Central. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006273; P:lagging strand elongation; IBA:GO_Central. DR Gene3D; 1.10.3260.10; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00407; DNA_ligase; 1. DR InterPro; IPR022865; DNA_ligae_ATP-dep_bac/arc. DR InterPro; IPR000977; DNA_ligase_ATP-dep. DR InterPro; IPR012309; DNA_ligase_ATP-dep_C. DR InterPro; IPR012310; DNA_ligase_ATP-dep_cent. DR InterPro; IPR016059; DNA_ligase_ATP-dep_CS. DR InterPro; IPR012308; DNA_ligase_ATP-dep_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF04679; DNA_ligase_A_C; 1. DR Pfam; PF01068; DNA_ligase_A_M; 1. DR Pfam; PF04675; DNA_ligase_A_N; 1. DR SUPFAM; SSF117018; SSF117018; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00574; dnl1; 1. DR PROSITE; PS00697; DNA_LIGASE_A1; 1. DR PROSITE; PS00333; DNA_LIGASE_A2; 1. DR PROSITE; PS50160; DNA_LIGASE_A3; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Cell division; Complete proteome; DNA damage; KW DNA recombination; DNA repair; DNA replication; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 573 DNA ligase. FT /FTId=PRO_0000059604. FT ACT_SITE 250 250 N6-AMP-lysine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 248 248 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 255 255 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 270 270 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 299 299 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 340 340 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 432 432 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. FT BINDING 438 438 ATP. {ECO:0000255|HAMAP-Rule:MF_00407}. SQ SEQUENCE 573 AA; 66790 MW; 6F95434EE968038C CRC64; MLWRDVCEIF NKIEKTTKRL EKRDYFIKLI DMVKEKGKPE DLKKICYMAI GRVYPEYDER ELGIGEKLLI NAVTSIGIKK DELLEKIKET GDIGLAIEQL KSKIKQASLF FQPLTVDEVY ETLKRVGEIE GEGSQKKKLR LISSLFLRAS PIECRYLARL ILEDMRIGMN VPTILDALSV YFNVPKEKLE KIYAITNDIG LLAEKLLMGD LESEELKLKL FRPIKPMLAQ LTPSIEEALL EMGRAQFETK YDGARVQIHK DGNKVKIYSR RLEDVTNALP EIVEAVKNIN VDKLIVEGEC VAIDKQTGKP RPFQDILRRF RRKYDIGKMM KEINLRVYLF DILYKDGVSF IDEEFEKRRK VLEEIVGYEN DWRTERKRIE KELKSDKIID ISYKLVTNDA KEAREFYNWS LSIGHEGVMI KNLKAPYTPG SRVRTMYKFK PTLESLDVVI TKAKRGMGKR KDWYGSFEIC VRDEEGNLYP IGHVGTGLTE ADLEFLKEEI DKIIIRDLGE EVEVEPKIVI EVAYEEIQKS DKYPCGYALR FPRVVRFRFD KGVNEINTIE DVERIYEIQR GRK // ID DPOL_METJA Reviewed; 1634 AA. AC Q58295; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 115. DE RecName: Full=DNA polymerase; DE EC=2.7.7.7; DE Contains: DE RecName: Full=Mja pol-1 intein; DE Contains: DE RecName: Full=Mja pol-2 intein; GN Name=pol; OrderedLocusNames=MJ0885; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the DNA polymerase type-B family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 DOD-type homing endonuclease domains. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98889.1; -; Genomic_DNA. DR PIR; E64410; E64410. DR ProteinModelPortal; Q58295; -. DR STRING; 243232.MJ_0885; -. DR EnsemblBacteria; AAB98889; AAB98889; MJ_0885. DR KEGG; mja:MJ_0885; -. DR eggNOG; arCOG00328; Archaea. DR eggNOG; arCOG00329; Archaea. DR eggNOG; arCOG03145; Archaea. DR eggNOG; COG0417; LUCA. DR InParanoid; Q58295; -. DR KO; K02319; -. DR OMA; LDCECCK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 4. DR Gene3D; 3.10.28.10; -; 2. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR006172; DNA-dir_DNA_pol_B. DR InterPro; IPR017964; DNA-dir_DNA_pol_B_CS. DR InterPro; IPR006133; DNA-dir_DNA_pol_B_exonuc. DR InterPro; IPR006134; DNA-dir_DNA_pol_B_multi_dom. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF00136; DNA_pol_B; 2. DR Pfam; PF03104; DNA_pol_B_exo1; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 2. DR SMART; SM00306; HintN; 2. DR SMART; SM00486; POLBc; 1. DR SUPFAM; SSF51294; SSF51294; 4. DR SUPFAM; SSF53098; SSF53098; 1. DR SUPFAM; SSF55608; SSF55608; 2. DR TIGRFAMs; TIGR01443; intein_Cterm; 2. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS00116; DNA_POLYMERASE_B; 1. DR PROSITE; PS50818; INTEIN_C_TER; 2. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2. DR PROSITE; PS50817; INTEIN_N_TER; 2. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; DNA replication; KW DNA-binding; DNA-directed DNA polymerase; Nucleotidyltransferase; KW Protein splicing; Reference proteome; Repeat; Transferase. FT CHAIN 1 425 DNA polymerase, 1st part. {ECO:0000255}. FT /FTId=PRO_0000007317. FT CHAIN 426 794 Mja pol-1 intein. {ECO:0000255}. FT /FTId=PRO_0000007318. FT CHAIN 795 882 DNA polymerase, 2nd part. {ECO:0000255}. FT /FTId=PRO_0000007319. FT CHAIN 883 1358 Mja pol-2 intein. {ECO:0000255}. FT /FTId=PRO_0000007320. FT CHAIN 1359 1634 DNA polymerase, 3rd part. {ECO:0000255}. FT /FTId=PRO_0000007321. FT DOMAIN 552 693 DOD-type homing endonuclease 1. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT DOMAIN 1163 1295 DOD-type homing endonuclease 2. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 1634 AA; 191710 MW; 84A1FAFAB1F97DDD CRC64; MGMSMGKIKI DALIDNTYKT IEDKAVIYLY LINSILKDRD FKPYFYVELH KEKVENEDIE KIKEFLLKND LLKFVENIEV VKKIILRKEK EVIKIIATHP QKVPKLRKIK ECEIVKEIYE HDIPFAKRYL IDNEIIPMTY WDFENKKPVS IEIPKLKSVA FDMEVYNRDT EPNPERDPIL MASFWDENGG KVITYKEFNH PNIEVVKNEK ELIKKIIETL KEYDVIYTYN GDNFDFPYLK ARAKIYGIDI NLGKDGEELK IKRGGMEYRS YIPGRVHIDL YPISRRLLKL TKYTLEDVVY NLFGIEKLKI PHTKIVDYWA NNDKTLIEYS LQDAKYTYKI GKYFFPLEVM FSRIVNQTPF EITRMSSGQM VEYLLMKRAF KENMIVPNKP DEEEYRRRVL TTYEGGYVKE PEKGMFEDII SMDFRCHPKG TKVVVKGKGI VNIEDVKEGN YVLGIDGWQK VKKVWKYEYE GELINVNGLK CTPNHKIPLR YKIKHKKINK NDYLVRDIYA KSLLTKFKGE GKLILCKDFE TIGNYEKYIN DMDEDFILKS ELIGILLAEG HLLRRDIEYF DSSRGKKRIS HQYRVEITVN EDEKDFIEKI KYIFKKLFNY ELYVRRKKGT KAITLGCAKK DIYLKIEEIL KNKEKYLPNA ILRGFFEGDG YVNTVRRAVV VNQGTNNYDK IKFIASLLDR LGIKYSFYTY SYEERGKKLK RYVIEIFSKG DLIKFSILIS FISRRKNNLL NEIIRQKTLY KIGDYGFYDL DDVCVSLESY KGEVYDLTLE GRPYYFANGI LTHNSLYPSI IISYNISPDT LDCECCKDVS EKILGHWFCK KKEGLIPKTL RNLIERRINI KRRMKKMAEI GEINEEYNLL DYEQKSLKIL ANSILPDEYL TIIEEDGIKV VKIGEYIDDL MRKHKDKIKF SGISEILETK NLKTFSFDKI TKKCEIKKVK ALIRHPYFGK AYKIKLRSGR TIKVTRGHSL FKYENGKIVE VKGDDVRFGD LIVVPKKLTC VDKEVVINIP KRLINADEEE IKDLVITKHK DKAFFVKLKK TLEDIENNKL KVIFDDCILY LKELGLIDYN IIKKINKVDI KILDEEKFKA YKKYFDTVIE HGNFKKGRCN IQYIKIKDYI ANIPDKEFED CEIGAYSGKI NALLKLDEKL AKFLGFFVTR GRLKKQKLKG ETVYEISVYK SLPEYQKEIA ETFKEVFGAG SMVKDKVTMD NKIVYLVLKY IFKCGDKDKK HIPEELFLAS ESVIKSFLDG FLKAKKNSHK GTSTFMAKDE KYLNQLMILF NLVGIPTRFT PVKNKGYKLT LNPKYGTVKD LMLDEVKEIE AFEYSGYVYD LSVEDNENFL VNNIYAHNSV YGYLAFPRAR FYSRECAEIV TYLGRKYILE TVKEAEKFGF KVLYIDTDGF YAIWKEKISK EELIKKAMEF VEYINSKLPG TMELEFEGYF KRGIFVTKKR YALIDENGRV TVKGLEFVRR DWSNIAKITQ RRVLEALLVE GSIEKAKKII QDVIKDLREK KIKKEDLIIY TQLTKDPKEY KTTAPHVEIA KKLMREGKRI KVGDIIGYII VKGTKSISER AKLPEEVDID DIDVNYYIDN QILPPVLRIM EAVGVSKNEL KKEGAQLTLD KFFK // ID DUT_METJA Reviewed; 156 AA. AC Q58502; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 4. DT 17-FEB-2016, entry version 92. DE RecName: Full=Deoxyuridine 5'-triphosphate nucleotidohydrolase {ECO:0000305}; DE Short=dUTPase {ECO:0000255|HAMAP-Rule:MF_00635}; DE EC=3.6.1.23 {ECO:0000255|HAMAP-Rule:MF_00635, ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946}; DE AltName: Full=MjDUT; DE AltName: Full=dUTP pyrophosphatase {ECO:0000255|HAMAP-Rule:MF_00635}; GN Name=dut {ECO:0000255|HAMAP-Rule:MF_00635}; OrderedLocusNames=MJ1102; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 2-10, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=12670946; DOI=10.1074/jbc.M213010200; RA Bjoernberg O., Neuhard J., Nyman P.O.; RT "A bifunctional dCTP deaminase-dUTP nucleotidohydrolase from the RT hyperthermophilic archaeon Methanocaldococcus jannaschii."; RL J. Biol. Chem. 278:20667-20672(2003). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, RP AND SUBUNIT. RX PubMed=12538648; DOI=10.1074/jbc.M212460200; RA Li H., Xu H., Graham D.E., White R.H.; RT "The Methanococcus jannaschii dCTP deaminase is a bifunctional RT deaminase and diphosphatase."; RL J. Biol. Chem. 278:11100-11106(2003). CC -!- FUNCTION: This enzyme is involved in nucleotide metabolism: it CC produces dUMP, the immediate precursor of thymidine nucleotides CC and it decreases the intracellular concentration of dUTP so that CC uracil cannot be incorporated into DNA. {ECO:0000255|HAMAP- CC Rule:MF_00635, ECO:0000269|PubMed:12538648, CC ECO:0000269|PubMed:12670946}. CC -!- CATALYTIC ACTIVITY: dUTP + H(2)O = dUMP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_00635, ECO:0000269|PubMed:12538648, CC ECO:0000269|PubMed:12670946}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.4 uM for dUTP {ECO:0000269|PubMed:12670946}; CC KM=103 uM for dUTP {ECO:0000269|PubMed:12538648}; CC Note=kcat is 4.6 sec(-1). {ECO:0000269|PubMed:12538648}; CC -!- PATHWAY: Pyrimidine metabolism; dUMP biosynthesis; dUMP from dCTP CC (dUTP route): step 2/2. {ECO:0000255|HAMAP-Rule:MF_00635, CC ECO:0000269|PubMed:12538648, ECO:0000269|PubMed:12670946}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:12538648}. CC -!- SIMILARITY: Belongs to the dCTP deaminase family. Archaeal dUTPase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00635, ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99105.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99105.1; ALT_INIT; Genomic_DNA. DR PIR; E64437; E64437. DR ProteinModelPortal; Q58502; -. DR STRING; 243232.MJ_1102; -. DR EnsemblBacteria; AAB99105; AAB99105; MJ_1102. DR KEGG; mja:MJ_1102; -. DR eggNOG; arCOG04048; Archaea. DR eggNOG; COG0717; LUCA. DR InParanoid; Q58502; -. DR KO; K01520; -. DR OMA; ENVAGFA; -. DR PhylomeDB; Q58502; -. DR SABIO-RK; Q58502; -. DR UniPathway; UPA00610; UER00666. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004170; F:dUTP diphosphatase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0006226; P:dUMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046081; P:dUTP catabolic process; IBA:GO_Central. DR Gene3D; 2.70.40.10; -; 1. DR HAMAP; MF_00635; dUTPase_arch; 1. DR InterPro; IPR029054; dUTPase-like. DR InterPro; IPR008180; dUTPase/dCTP_deaminase. DR InterPro; IPR023537; dUTPase_archaeal. DR Pfam; PF00692; dUTPase; 1. DR SUPFAM; SSF51283; SSF51283; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Hydrolase; KW Nucleotide metabolism; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000269|PubMed:12670946}. FT CHAIN 2 156 Deoxyuridine 5'-triphosphate FT nucleotidohydrolase. FT /FTId=PRO_0000153638. SQ SEQUENCE 156 AA; 18070 MW; AF6E28A4CF91FF3D CRC64; MIIGANTSKN FFDNLEEEQI QQCGIDLRVW KIFKIEGEGV IDFSNEKRKL PNYIEIFNSE KDEHIKLDRG VYIVKVADYI KIPENVAGFA YPRSSLLRMG ATLYSAVHDP GYEGRPEYLM QVFNPITIYK YARIAQIVFV ECRDVKGVYE GIYKGR // ID DMRX_METJA Reviewed; 246 AA. AC Q57661; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Dihydromethanopterin reductase (acceptor) {ECO:0000303|PubMed:23995635}; DE Short=H(2)MPT reductase {ECO:0000303|PubMed:23995635}; DE EC=1.5.99.15 {ECO:0000269|PubMed:23995635}; GN Name=dmrX {ECO:0000303|PubMed:23995635}; OrderedLocusNames=MJ0208; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND COFACTOR. RX PubMed=23995635; DOI=10.1128/JB.00457-13; RA Wang S., Tiongson J., Rasche M.E.; RT "Discovery and characterization of the first archaeal RT dihydromethanopterin reductase, an iron-sulfur flavoprotein from RT Methanosarcina mazei."; RL J. Bacteriol. 196:203-209(2014). CC -!- FUNCTION: Involved in the biosynthesis of tetrahydromethanopterin, CC a coenzyme used in methanogenesis. Catalyzes the reduction of CC dihydromethanopterin (H(2)MPT) to tetrahydromethanopterin CC (H(4)MPT). Ferredoxin may serve as an electron donor. CC {ECO:0000269|PubMed:23995635}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydromethanopterin + oxidized CC acceptor = 7,8-dihydromethanopterin + reduced acceptor. CC {ECO:0000269|PubMed:23995635}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000303|PubMed:23995635}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. CC {ECO:0000303|PubMed:23995635}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000305}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:23995635}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98191.1; -; Genomic_DNA. DR PIR; A64326; A64326. DR ProteinModelPortal; Q57661; -. DR STRING; 243232.MJ_0208; -. DR EnsemblBacteria; AAB98191; AAB98191; MJ_0208. DR KEGG; mja:MJ_0208; -. DR eggNOG; arCOG01705; Archaea. DR eggNOG; COG1036; LUCA. DR InParanoid; Q57661; -. DR KO; K18853; -. DR OMA; ILEREHP; -. DR PhylomeDB; Q57661; -. DR BRENDA; 1.5.99.15; 3260. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IDA:UniProtKB. DR GO; GO:1901285; P:5,6,7,8-tetrahydromethanopterin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.50.1950; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR014073; DmrX. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF00037; Fer4; 2. DR Pfam; PF02441; Flavoprotein; 1. DR TIGRFAMs; TIGR02700; flavo_MJ0208; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport. FT CHAIN 1 246 Dihydromethanopterin reductase FT (acceptor). FT /FTId=PRO_0000159308. FT DOMAIN 150 178 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 179 208 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 159 159 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 162 162 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 165 165 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 169 169 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 188 188 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 191 191 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 194 194 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 198 198 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 246 AA; 27697 MW; 41DAC513C3212721 CRC64; MNYRFGINMK IVWCITGAGH LLRESFQVMK RLKEEIEDLK VTTLVSRAGE EVVKMYGLFG ELYNISNGNY YEELILEREH PYSSPITGRL SLGKYDYLIC SPATGNTVAK VVNGIADSLV TNAIAQAGKG FVKSLIVPVD YKAGIVTTKL PYAIDKKKCK LCLKCINVCP NGAIVKRDNF VEILLSKCLG CGNCKKVCPY NAIIEGKEIK MRVRKIDAEN TRKLMELEDV IVLKHPYEIL EFFNIR // ID DTDA_METJA Reviewed; 255 AA. AC Q57630; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00562}; DE EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00562}; DE AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase; GN Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; OrderedLocusNames=MJ0166; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate CC specificity. By recycling D-aminoacyl-tRNA to D-amino acids and CC free tRNA molecules, this enzyme counteracts the toxicity CC associated with the formation of D-aminoacyl-tRNA entities in CC vivo. {ECO:0000255|HAMAP-Rule:MF_00562}. CC -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid + CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00562}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00562}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00562}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562}. CC -!- SIMILARITY: Belongs to the DtdA deacylase family. CC {ECO:0000255|HAMAP-Rule:MF_00562}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98148.1; -; Genomic_DNA. DR PIR; G64320; G64320. DR ProteinModelPortal; Q57630; -. DR STRING; 243232.MJ_0166; -. DR EnsemblBacteria; AAB98148; AAB98148; MJ_0166. DR KEGG; mja:MJ_0166; -. DR eggNOG; arCOG01616; Archaea. DR eggNOG; COG1650; LUCA. DR InParanoid; Q57630; -. DR KO; K09716; -. DR OMA; EATHHTP; -. DR PhylomeDB; Q57630; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00562; Deacylase_DtdA; 1. DR InterPro; IPR018033; Deacylase_DtdA_archaea. DR InterPro; IPR007508; DtdA. DR Pfam; PF04414; tRNA_deacylase; 1. DR PIRSF; PIRSF016210; UCP016210; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 255 D-aminoacyl-tRNA deacylase. FT /FTId=PRO_0000158966. SQ SEQUENCE 255 AA; 29072 MW; 6428DF7AEC802CE4 CRC64; MKFLLIASNK DLASKNIANH IKEYFDVFET DKELLSLTAE DLEYADYYIF LSKHKSIANK PSLTVHTPGN LTEDNTFGGN PKEVCPCDAV LNTLLLKNIY KNYKTYYEDG KIGEFDVSFE VVHHSPTGLK APTVFVEIGS SEKEWILKEA GEIIAKSVLE TIDAMKSKNY DKKVRAIGFG GGHYAPKFTK LALEDKYYFG YLVPKYASVS EDVLNQLISK MEVDKALIDW KGCRGDDKRR YIEFFENNGI EWERV // ID DP2L_METJA Reviewed; 1139 AA. AC Q59024; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=DNA polymerase II large subunit; DE Short=Pol II; DE EC=2.7.7.7; GN Name=polC; OrderedLocusNames=MJ1630; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=9555910; RA Ishino Y., Komori K., Cann I.K.O., Koga Y.; RT "A novel DNA polymerase family found in Archaea."; RL J. Bacteriol. 180:2232-2236(1998). CC -!- FUNCTION: Possesses two activities: a DNA synthesis (polymerase) CC and an exonucleolytic activity that degrades single-stranded DNA CC in the 3'- to 5'-direction. Has a template-primer preference which CC is characteristic of a replicative DNA polymerase. CC -!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) = CC diphosphate + DNA(n+1). CC -!- CATALYTIC ACTIVITY: Degradation of single-stranded DNA. It acts CC progressively in a 3'- to 5'-direction, releasing nucleoside 5'- CC phosphates. CC -!- SUBUNIT: Heterodimer of a large subunit and a small subunit. CC -!- SIMILARITY: Belongs to the archaeal DNA polymerase II family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99651.1; -; Genomic_DNA. DR PIR; D64503; D64503. DR STRING; 243232.MJ_1630; -. DR EnsemblBacteria; AAB99651; AAB99651; MJ_1630. DR KEGG; mja:MJ_1630; -. DR eggNOG; arCOG04447; Archaea. DR eggNOG; COG1933; LUCA. DR InParanoid; Q59024; -. DR KO; K02322; -. DR OMA; RNCDGDE; -. DR PhylomeDB; Q59024; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000738; P:DNA catabolic process, exonucleolytic; IEA:UniProtKB-HAMAP. DR GO; GO:0006261; P:DNA-dependent DNA replication; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00324; DNApol_II_L_arch; 1. DR InterPro; IPR004475; PolC_DP2. DR InterPro; IPR016033; PolC_DP2_N. DR Pfam; PF03833; PolC_DP2; 1. DR PIRSF; PIRSF016275; PolC_DP2; 1. DR TIGRFAMs; TIGR00354; polC; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA replication; DNA-binding; KW DNA-directed DNA polymerase; Exonuclease; Hydrolase; KW Multifunctional enzyme; Nuclease; Nucleotidyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 1139 DNA polymerase II large subunit. FT /FTId=PRO_0000152575. SQ SEQUENCE 1139 AA; 129402 MW; 3B7968A013AAC45A CRC64; MIVMVHVACS ENMKKYFENI VDEVKKIYRI AEECRKKGFD PTDEVEIPLA ADMADRVEGL VGPKGVAERI RELVKELGKE PAALEIAKEI VEGKFGNFDK EKKAEQAVRT ALAVLTEGIV AAPLEGIADV KIKKNPDGTE YLAIYYAGPI RSAGGTAQAL SVLVGDFVRK AMGLDRYKPT EDEIERYVEE VELYQSEVGS FQYNPTADEI RTAIRNIPIE ITGEATDDVE VSGHRDLPRV ETNQLRGGAL LVLVEGVLLK APKILRHVDK LGIEGWDWLK DLMSKKEEKE EEKDEKVDDE EIDEEEEEIS GYWRDVKIEA NKKFISEVIA GRPVFAHPSK VGGFRLRYGR SRNTGFATQG FHPALMYLVD EFMAVGTQLK TERPGKATCV VPVDSIEPPI VKLKNGDVIR VDTIEKAMDV RNRVEEILFL GDVLVNYGDF LENNHPLLPS CWCEEWYEKI LIANNIEYDK DFIKNPKPEE AVKFALETKT PLHPRFTYHW HDVSKEDIIL LRNWLLKGKE DSLEGKKVWI VDLEIEEDKK AKRILELIGC CHLVRNKKVI IEEYYPLLYS LGFDVENKKD LVENIEKILE SAKNSMHLIN LLAPFEVRRN TYVYVGARMG RPEKAAPRKM KPPVNGLFPI GNAGGQVRLI NKAVEENNTD DVDVSYTRCP NCGKISLYRV CPFCGTKVEL DNFGRIKAPL KDYWYAALKR LGINKPGDVK CIKGMTSKQK IVEPLEKAIL RAINEVYVFK DGTTRFDCTD VPVTHFKPNE INVTVEKLRE LGYDKDIYGN ELVDGEQVVE LKPQDVIIPE SCAEYFVKVA NFIDDLLEKF YKVERFYNVK KKEDLIGHLV IGMAPHTSAG MVGRIIGYTK ANVGYAHPYF HAAKRRNCDG DEDSFFLLLD AFLNFSKKFL PDKRGGQMDA PLVLTTILDP KEVDGEVHNM DTMWSYPLEF YEKTLEMPSP KEVKEFMETV EDRLGKPEQY EGIGYTHETS RIDLGPKVCA YKTLGSMLEK TTSQLSVAKK IRATDERDVA EKVIQSHFIP DLIGNLRAFS RQAVRCKCGA KYRRIPLKGK CPKCGSNLIL TVSKGAVEKY MDVAEKMAEE YNVNDYIKQR LKIIKEGINS IFENEKSRQV KLSDFFKIG // ID EF1A_METJA Reviewed; 428 AA. AC Q57770; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Elongation factor 1-alpha {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-1-alpha {ECO:0000255|HAMAP-Rule:MF_00118}; DE AltName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118}; DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118}; GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=MJ0324; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This protein promotes the GTP-dependent binding of CC aminoacyl-tRNA to the A-site of ribosomes during protein CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98308.1; -; Genomic_DNA. DR PIR; D64340; D64340. DR ProteinModelPortal; Q57770; -. DR SMR; Q57770; 5-424. DR STRING; 243232.MJ_0324; -. DR EnsemblBacteria; AAB98308; AAB98308; MJ_0324. DR KEGG; mja:MJ_0324; -. DR eggNOG; arCOG01561; Archaea. DR eggNOG; COG5256; LUCA. DR InParanoid; Q57770; -. DR KO; K03231; -. DR OMA; PASTIFH; -. DR PhylomeDB; Q57770; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00118_A; EF_Tu_A; 1. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004539; Transl_elong_EF1A_euk/arc. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004160; Transl_elong_EFTu/EF1A_C. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF03143; GTP_EFTU_D3; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00483; EF-1_alpha; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 428 Elongation factor 1-alpha. FT /FTId=PRO_0000090980. FT DOMAIN 5 225 tr-type G. FT NP_BIND 14 21 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 91 95 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT NP_BIND 149 152 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}. FT REGION 14 21 G1. {ECO:0000250}. FT REGION 70 74 G2. {ECO:0000250}. FT REGION 91 94 G3. {ECO:0000250}. FT REGION 149 152 G4. {ECO:0000250}. FT REGION 189 191 G5. {ECO:0000250}. SQ SEQUENCE 428 AA; 47280 MW; 0E375F776B8BA82E CRC64; MAKQKPVLNV AFIGHVDAGK STTVGRLLYD SGAIDPQLLE KLKREAQERG KAGFEFAYVM DNLKEERERG VTIDVAHKKF ETQKYEVTIV DCPGHRDFIK NMITGASQAD AAVLVVDVND AKTGIQPQTR EHMFLARTLG IKQIAVAINK MDTVNYSQEE YEKMKKMLSE QLLKVLGYNP DQIDFIPTAS LKGDNVVKRS ENMPWYKGPT LVEALDKFQP PEKPTNLPLR IPIQDVYSIT GVGTVPVGRV ETGILRPGDK VVFEPAGVSG EVKSIEMHHE QIPQAEPGDN IGFNVRGVSK KDIKRGDVCG HPDNPPTVAE EFTAQIVVLQ HPTAITVGYT PVFHAHTAQV ACTFIELLKK LDPRTGQVIE ENPQFLKTGD AAIVKIKPTK PMVIENVREI PQLGRFAIRD MGMTIAAGMA IDVKAKNK // ID EF1B_METJA Reviewed; 89 AA. AC Q57901; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Elongation factor 1-beta; DE Short=EF-1-beta; DE AltName: Full=aEF-1beta; GN Name=ef1b; OrderedLocusNames=MJ0459; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, CC thus allowing the regeneration of EF-1-alpha/GTP that could then CC be used to form the ternary complex EF-1-alpha/GTP/AAtRNA. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98467.1; -; Genomic_DNA. DR PIR; C64357; C64357. DR ProteinModelPortal; Q57901; -. DR STRING; 243232.MJ_0459; -. DR EnsemblBacteria; AAB98467; AAB98467; MJ_0459. DR KEGG; mja:MJ_0459; -. DR eggNOG; arCOG01988; Archaea. DR eggNOG; COG2092; LUCA. DR InParanoid; Q57901; -. DR KO; K03232; -. DR OMA; AKIKIMP; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.60; -; 1. DR HAMAP; MF_00043; EF1_beta; 1. DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6. DR InterPro; IPR004542; Transl_elong_EF1B_B_arc. DR InterPro; IPR014038; Transl_elong_fac_EF1B_bsu/dsu. DR Pfam; PF00736; EF1_GNE; 1. DR PIRSF; PIRSF006521; Transl_elong_EF1B_B_arc; 1. DR SMART; SM00888; EF1_GNE; 1. DR SUPFAM; SSF54984; SSF54984; 1. DR TIGRFAMs; TIGR00489; aEF-1_beta; 1. PE 3: Inferred from homology; KW Complete proteome; Elongation factor; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 89 Elongation factor 1-beta. FT /FTId=PRO_0000155058. SQ SEQUENCE 89 AA; 9921 MW; 0153FB4067D36980 CRC64; MATVLAKIKI MPTSPEVNKE KLKEKIKEVL EKQDVAIRGL FDEPLAFGLY AIYTVIEMEE REGGTEPIEN ALAEIDEVES VETVEVSLA // ID ECFA_METJA Reviewed; 279 AA. AC Q58488; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Energy-coupling factor transporter ATP-binding protein EcfA {ECO:0000255|HAMAP-Rule:MF_01710}; DE Short=ECF transporter A component EcfA {ECO:0000255|HAMAP-Rule:MF_01710}; DE EC=3.6.3.- {ECO:0000255|HAMAP-Rule:MF_01710}; GN Name=ecfA {ECO:0000255|HAMAP-Rule:MF_01710}; Synonyms=cbiO; GN OrderedLocusNames=MJ1088; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: ATP-binding (A) component of a common energy-coupling CC factor (ECF) ABC-transporter complex. Unlike classic ABC CC transporters this ECF transporter provides the energy necessary to CC transport a number of different substrates. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBUNIT: Forms a stable energy-coupling factor (ECF) transporter CC complex composed of 2 membrane-embedded substrate-binding proteins CC (S component), 2 ATP-binding proteins (A component) and 2 CC transmembrane proteins (T component). {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01710}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Energy- CC coupling factor EcfA family. {ECO:0000255|HAMAP-Rule:MF_01710}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01710}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99089.1; -; Genomic_DNA. DR PIR; G64435; G64435. DR ProteinModelPortal; Q58488; -. DR STRING; 243232.MJ_1088; -. DR EnsemblBacteria; AAB99089; AAB99089; MJ_1088. DR KEGG; mja:MJ_1088; -. DR eggNOG; arCOG00202; Archaea. DR eggNOG; COG1122; LUCA. DR InParanoid; Q58488; -. DR KO; K02006; -. DR OMA; RIGHKPV; -. DR PhylomeDB; Q58488; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015856; ABC_transpr_CbiO/EcfA_su. DR InterPro; IPR005876; Co_trans_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01166; cbiO; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51246; CBIO; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 279 Energy-coupling factor transporter ATP- FT binding protein EcfA. FT /FTId=PRO_0000092141. FT DOMAIN 4 239 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01710}. FT NP_BIND 37 44 ATP. {ECO:0000255|HAMAP-Rule:MF_01710}. SQ SEQUENCE 279 AA; 31121 MW; 7A2DF31BE68CFA81 CRC64; MYIVETKDLY FRYPDGTAVL KGINFKVKKG EMVSLLGPNG AGKSTLFLHF NGILRPTKGE VLIKGKPIKY DKKSLVEVRK TVGLVFQNPD DQIFAPTVKE DVAFGPLNLG LPKEEVEKRV KEALKAVGME GFENKPPHHL SGGQKKRVAI AGILAMQPEV IVLDEPTAGL DPVGASKIMK LLYDLNKKGM TIIISTHDVD LVPVYADKVY VMYDGKILKE GTPKEVFSDV ETIRKANLRL PRVAHLIEIL NKKDNIPIEW GFTIGEVRRN IVNYLKEKC // ID EF2_METJA Reviewed; 726 AA. AC Q58448; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=Elongation factor 2; DE Short=EF-2; GN Name=fusA; Synonyms=fus; OrderedLocusNames=MJ1048; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the GTP-dependent ribosomal translocation step CC during translation elongation. During this step, the ribosome CC changes from the pre-translocational (PRE) to the post- CC translocational (POST) state as the newly formed A-site-bound CC peptidyl-tRNA and P-site-bound deacylated tRNA move to the P and E CC sites, respectively. Catalyzes the coordinated movement of the two CC tRNA molecules, the mRNA and conformational changes in the CC ribosome (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EF-G/EF-2 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99052.1; -; Genomic_DNA. DR PIR; G64430; G64430. DR ProteinModelPortal; Q58448; -. DR STRING; 243232.MJ_1048; -. DR EnsemblBacteria; AAB99052; AAB99052; MJ_1048. DR KEGG; mja:MJ_1048; -. DR eggNOG; arCOG01559; Archaea. DR eggNOG; COG0480; LUCA. DR InParanoid; Q58448; -. DR KO; K03234; -. DR OMA; FTGHVTR; -. DR PhylomeDB; Q58448; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.240; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00054_A; EF_G_EF_2_A; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR000640; EFG_V. DR InterPro; IPR031157; G_TR_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004543; Transl_elong_EFG/EF2_arc. DR InterPro; IPR005517; Transl_elong_EFG/EF2_IV. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF00679; EFG_C; 1. DR Pfam; PF14492; EFG_II; 1. DR Pfam; PF03764; EFG_IV; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SMART; SM00838; EFG_C; 1. DR SMART; SM00889; EFG_IV; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF54980; SSF54980; 2. DR TIGRFAMs; TIGR00490; aEF-2; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS00301; G_TR_1; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Elongation factor; GTP-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 726 Elongation factor 2. FT /FTId=PRO_0000091032. FT DOMAIN 19 260 tr-type G. FT NP_BIND 28 35 GTP. {ECO:0000250}. FT NP_BIND 94 98 GTP. {ECO:0000250}. FT NP_BIND 148 151 GTP. {ECO:0000250}. FT MOD_RES 602 602 Diphthamide. {ECO:0000250}. SQ SEQUENCE 726 AA; 80989 MW; E5C9D63DB0971D31 CRC64; MGKRAKMIAK IKELMEKYDR IRNIGICAHI DHGKTTLSDN LLAGAGMISK ELAGEQLALD FDEEEAQRGI TIFAANVSMV HTYEGNEYLI NLIDTPGHVD FGGDVTRAMR AIDGAIVVVC AVEGVMPQTE TVLRQALRER VKPVLFINKV DRLINELKLT PEELQSRFIK IINDINNLIR KMAPEEFKDK WLVRVEDGSV AFGSAYNNWA ISVPFMKKSG ITFKDIIKYC EEDRQDELAE KAPLHEVVLD MVIKHLPSPP EAQKYRIPHL WKGDLNSEAG KAMLNCDPNG PLAGVITKII VDKHAGAVSV CRLFSGRIKQ GDEVYMVNNQ QKAKIQQVSV FMGPERIPVD SISAGNICAL VGLKEASAGE TICSPDKIIE PFEAITHISE PVITVAIEAK NTKDLPKLIE VLRQVAREDP TVKVEINEET GEHLLSGMGE LHIEIITKLK IERDAGIPVE VGQPIVVYRE TVTGQSPVVE SKSPNKHNKL YFVVEPLEES VLQAYKEGRI PDVDTKRKLD DKIVQELIKA GMDPEEAKRV MCIYEGNVLI NMTRGIVHLD EVKELIIQGF KEAMRNGPLA AEKCQGVKVK LMDAVLHEDA IHRGPAQMIP AARFGIRDAM MQANPVLLEP MQFVYINTPQ DFMGAAMREI SNRRGQILDM EQEGDMAIIK AKCPVAEMFG FAGAIRGATQ GRCLWSIEFA GYEKVPRDMQ EQLIKQIRER KGLKLE // ID END3_METJA Reviewed; 344 AA. AC Q58030; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 97. DE RecName: Full=Endonuclease III {ECO:0000255|HAMAP-Rule:MF_00942}; DE EC=4.2.99.18 {ECO:0000255|HAMAP-Rule:MF_00942}; DE AltName: Full=DNA-(apurinic or apyrimidinic site) lyase {ECO:0000255|HAMAP-Rule:MF_00942}; GN Name=nth {ECO:0000255|HAMAP-Rule:MF_00942}; OrderedLocusNames=MJ0613; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA repair enzyme that has both DNA N-glycosylase CC activity and AP-lyase activity. The DNA N-glycosylase activity CC releases various damaged pyrimidines from DNA by cleaving the N- CC glycosidic bond, leaving an AP (apurinic/apyrimidinic) site. The CC AP-lyase activity cleaves the phosphodiester bond 3' to the AP CC site by a beta-elimination, leaving a 3'-terminal unsaturated CC sugar and a product with a terminal 5'-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. {ECO:0000255|HAMAP-Rule:MF_00942}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00942}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00942}; CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC -!- SIMILARITY: Contains 1 GIY-YIG domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HhH domain. {ECO:0000255|HAMAP- CC Rule:MF_00942}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98606.1; -; Genomic_DNA. DR ProteinModelPortal; Q58030; -. DR STRING; 243232.MJ_0613; -. DR EnsemblBacteria; AAB98606; AAB98606; MJ_0613. DR KEGG; mja:MJ_0613; -. DR eggNOG; arCOG00459; Archaea. DR eggNOG; COG0177; LUCA. DR eggNOG; COG1833; LUCA. DR InParanoid; Q58030; -. DR KO; K10773; -. DR OMA; KLPKKYW; -. DR PhylomeDB; Q58030; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019104; F:DNA N-glycosylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR HAMAP; MF_00942; Nth; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR002837; DUF123. DR InterPro; IPR004036; Endonuclease-III-like_CS2. DR InterPro; IPR000305; GIY-YIG_SF. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR000445; HhH_motif. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF01986; DUF123; 1. DR Pfam; PF00633; HHH; 1. DR Pfam; PF00730; HhH-GPD; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00465; GIYc; 1. DR SUPFAM; SSF48150; SSF48150; 1. DR PROSITE; PS01155; ENDONUCLEASE_III_2; 1. DR PROSITE; PS50164; GIY_YIG; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA damage; DNA repair; DNA-binding; KW Glycosidase; Hydrolase; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 344 Endonuclease III. FT /FTId=PRO_0000102243. FT DOMAIN 105 124 HhH. {ECO:0000255|HAMAP-Rule:MF_00942}. FT DOMAIN 229 328 GIY-YIG. FT METAL 184 184 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 190 190 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 193 193 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. FT METAL 201 201 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00942}. SQ SEQUENCE 344 AA; 40568 MW; BC3BEFE1DE778B85 CRC64; MELIEILLKK LNKNAVVTEI AKDKDPFKVL ISTIISARTK DEVTEEVSKK LFKEIKDVDD LLNIDEEKLA DLIYPAGFYK NKAKNLKKLA KILKENYNGK VPDSLEELLK LPGVGRKTAN LVITLAFNKD GICVDTHVHR ICNRWEIVDT ETPEETEFEL RKKLPKKYWK VINNLLVVFG REICSSKSKC DKCFKEIKEK CPYYEKIKHF ENILKKFNFR KVSKNKIPNE KGTYILKIRL KEGKKIKFGK TERFFKKGYY FYIGSAFGNS MNLKNRIERH LKDDKKMHWH IDYLLKYGKI EEIYITNERV ECEVANEFIK KFDFVENFGC SDCKCKSHLF YLKP // ID ENDA_METJA Reviewed; 179 AA. AC Q58819; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=tRNA-splicing endonuclease; DE EC=4.6.1.16; DE AltName: Full=tRNA-intron endonuclease; GN Name=endA; OrderedLocusNames=MJ1424; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, SUBUNIT, AND MUTAGENESIS OF HIS-125. RX PubMed=9321408; DOI=10.1093/emboj/16.20.6290; RA Lykke-Andersen J., Garrett R.A.; RT "RNA-protein interactions of an archaeal homotetrameric splicing RT endoribonuclease with an exceptional evolutionary history."; RL EMBO J. 16:6290-6300(1997). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=9535656; DOI=10.1126/science.280.5361.279; RA Li H., Trotta C.R., Abelson J.; RT "Crystal structure and evolution of a transfer RNA splicing enzyme."; RL Science 280:279-284(1998). CC -!- FUNCTION: Endonuclease that removes tRNA introns. Cleaves pre-tRNA CC at the 5'- and 3'-splice sites to release the intron. The products CC are an intron and two tRNA half-molecules bearing 2',3' cyclic CC phosphate and 5'-OH termini. Recognizes a pseudosymmetric CC substrate in which 2 bulged loops of 3 bases are separated by a CC stem of 4 bp. {ECO:0000269|PubMed:9321408}. CC -!- CATALYTIC ACTIVITY: PretRNA = a 3'-half-tRNA molecule with a 5'-OH CC end + a 5'-half-tRNA molecule with a 2',3'-cyclic phosphate end + CC an intron with a 2',3'-cyclic phosphate and a 5'-hydroxyl CC terminus. CC -!- SUBUNIT: Homotetramer; although the tetramer contains four active CC sites, only two participate in the cleavage. Therefore, it should CC be considered as a dimer of dimers. {ECO:0000269|PubMed:9321408}. CC -!- SIMILARITY: Belongs to the tRNA-intron endonuclease family. CC Archaeal short subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99435.1; -; Genomic_DNA. DR PIR; G64477; G64477. DR PDB; 1A79; X-ray; 2.28 A; A/B/C/D=9-179. DR PDBsum; 1A79; -. DR ProteinModelPortal; Q58819; -. DR SMR; Q58819; 9-179. DR STRING; 243232.MJ_1424; -. DR EnsemblBacteria; AAB99435; AAB99435; MJ_1424. DR KEGG; mja:MJ_1424; -. DR eggNOG; arCOG01701; Archaea. DR eggNOG; COG1676; LUCA. DR InParanoid; Q58819; -. DR KO; K01170; -. DR OMA; DFRLYER; -. DR PhylomeDB; Q58819; -. DR EvolutionaryTrace; Q58819; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000213; F:tRNA-intron endonuclease activity; IBA:GO_Central. DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GOC. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR GO; GO:0000379; P:tRNA-type intron splice site recognition and cleavage; IBA:GO_Central. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_01833; EndA_short; 1. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR InterPro; IPR006677; tRNA_intron_Endonuc_cat-like. DR InterPro; IPR006678; tRNA_intron_Endonuc_N. DR InterPro; IPR006676; tRNA_splic. DR InterPro; IPR016442; tRNA_splic_arch_short. DR PANTHER; PTHR21227; PTHR21227; 1. DR Pfam; PF01974; tRNA_int_endo; 1. DR Pfam; PF02778; tRNA_int_endo_N; 1. DR PIRSF; PIRSF005285; tRNA_splic_archaea; 1. DR SUPFAM; SSF53032; SSF53032; 1. DR SUPFAM; SSF55267; SSF55267; 1. DR TIGRFAMs; TIGR00324; endA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Reference proteome; KW tRNA processing. FT CHAIN 1 179 tRNA-splicing endonuclease. FT /FTId=PRO_0000109470. FT ACT_SITE 115 115 FT ACT_SITE 125 125 FT ACT_SITE 156 156 FT MUTAGEN 125 125 H->A: Induces a strong decrease in FT activity. {ECO:0000269|PubMed:9321408}. FT STRAND 10 15 {ECO:0000244|PDB:1A79}. FT STRAND 18 21 {ECO:0000244|PDB:1A79}. FT HELIX 24 32 {ECO:0000244|PDB:1A79}. FT STRAND 36 38 {ECO:0000244|PDB:1A79}. FT STRAND 43 46 {ECO:0000244|PDB:1A79}. FT HELIX 47 55 {ECO:0000244|PDB:1A79}. FT STRAND 59 62 {ECO:0000244|PDB:1A79}. FT STRAND 64 67 {ECO:0000244|PDB:1A79}. FT HELIX 71 81 {ECO:0000244|PDB:1A79}. FT HELIX 85 97 {ECO:0000244|PDB:1A79}. FT STRAND 101 104 {ECO:0000244|PDB:1A79}. FT HELIX 106 108 {ECO:0000244|PDB:1A79}. FT STRAND 110 115 {ECO:0000244|PDB:1A79}. FT TURN 121 123 {ECO:0000244|PDB:1A79}. FT STRAND 127 134 {ECO:0000244|PDB:1A79}. FT STRAND 137 139 {ECO:0000244|PDB:1A79}. FT HELIX 142 153 {ECO:0000244|PDB:1A79}. FT STRAND 157 163 {ECO:0000244|PDB:1A79}. FT STRAND 169 177 {ECO:0000244|PDB:1A79}. SQ SEQUENCE 179 AA; 20664 MW; BCC4675E4AD21BE6 CRC64; MVRDKMGKKI TGLLDGDRVI VFDKNGISKL SARHYGNVEG NFLSLSLVEA LYLINLGWLE VKYKDNKPLS FEELYEYARN VEERLCLKYL VYKDLRTRGY IVKTGLKYGA DFRLYERGAN IDKEHSVYLV KVFPEDSSFL LSELTGFVRV AHSVRKKLLI AIVDADGDIV YYNMTYVKP // ID ENGB_METJA Reviewed; 219 AA. AC Q57768; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Probable GTP-binding protein EngB {ECO:0000255|HAMAP-Rule:MF_00321}; GN Name=engB {ECO:0000255|HAMAP-Rule:MF_00321}; OrderedLocusNames=MJ0320; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Necessary for normal cell division and for the CC maintenance of normal septation. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00321}; CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. EngB GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00321}. CC -!- SIMILARITY: Contains 1 EngB-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_00321}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98305.1; -; Genomic_DNA. DR PIR; A64340; A64340. DR ProteinModelPortal; Q57768; -. DR STRING; 243232.MJ_0320; -. DR EnsemblBacteria; AAB98305; AAB98305; MJ_0320. DR KEGG; mja:MJ_0320; -. DR eggNOG; arCOG00355; Archaea. DR eggNOG; COG0218; LUCA. DR InParanoid; Q57768; -. DR OMA; IDRHSGP; -. DR PhylomeDB; Q57768; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00321; GTPase_EngB; 1. DR InterPro; IPR030393; G_ENGB_dom. DR InterPro; IPR019987; GTP-bd_ribosome_bio_YsxC. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51706; G_ENGB; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; GTP-binding; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 219 Probable GTP-binding protein EngB. FT /FTId=PRO_0000157810. FT DOMAIN 23 211 EngB-type G. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT NP_BIND 31 38 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 57 61 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 74 77 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 154 157 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT NP_BIND 189 191 GTP. {ECO:0000255|HAMAP-Rule:MF_00321}. FT METAL 38 38 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. FT METAL 59 59 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00321}. SQ SEQUENCE 219 AA; 25615 MW; 0603A761767B117E CRC64; MCETMDFFER YKNLKEKYEE KKTKPKVIVV GRSNVGKSTF VRLMTGRKDI RVGKKPGVTL KINEYDMGEY ILVDMPGFGY MAGLPKKVQE KIKDEIVHYI EEHADEIAAA VQIIDTKSFF EIVERWKGRG EIPIDLEMFD FITDLKISPI LVANKMDKIK KEEWDAVLDG ICEYLKCQPP WHQWKFIVPA ILKEGKGIEE IKKKILERVR LFKKLRGIE // ID ENO_METJA Reviewed; 423 AA. AC Q60173; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 11-MAY-2016, entry version 113. DE RecName: Full=Enolase {ECO:0000255|HAMAP-Rule:MF_00318}; DE EC=4.2.1.11 {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phospho-D-glycerate hydro-lyase {ECO:0000255|HAMAP-Rule:MF_00318}; DE AltName: Full=2-phosphoglycerate dehydratase {ECO:0000255|HAMAP-Rule:MF_00318}; GN Name=eno {ECO:0000255|HAMAP-Rule:MF_00318}; OrderedLocusNames=MJ0232; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible conversion of 2- CC phosphoglycerate into phosphoenolpyruvate. It is essential for the CC degradation of carbohydrates via glycolysis. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- CATALYTIC ACTIVITY: 2-phospho-D-glycerate = phosphoenolpyruvate + CC H(2)O. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00318}; CC -!- ENZYME REGULATION: The covalent binding to the substrate causes CC inactivation of the enzyme, and possibly serves as a signal for CC the export of the protein. {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 4/5. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00318}. CC Secreted {ECO:0000255|HAMAP-Rule:MF_00318}. Cell surface CC {ECO:0000255|HAMAP-Rule:MF_00318}. Note=Fractions of enolase are CC present in both the cytoplasm and on the cell surface. The export CC of enolase possibly depends on the covalent binding to the CC substrate; once secreted, it remains attached to the cell surface. CC {ECO:0000255|HAMAP-Rule:MF_00318}. CC -!- SIMILARITY: Belongs to the enolase family. {ECO:0000255|HAMAP- CC Rule:MF_00318}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98220.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98220.1; ALT_INIT; Genomic_DNA. DR PIR; A64329; A64329. DR PDB; 2PA6; X-ray; 1.85 A; A/B=1-423. DR PDBsum; 2PA6; -. DR ProteinModelPortal; Q60173; -. DR SMR; Q60173; 1-423. DR STRING; 243232.MJ_0232; -. DR EnsemblBacteria; AAB98220; AAB98220; MJ_0232. DR KEGG; mja:MJ_0232; -. DR eggNOG; arCOG01169; Archaea. DR eggNOG; COG0148; LUCA. DR InParanoid; Q60173; -. DR KO; K01689; -. DR OMA; EFMIIPV; -. DR PhylomeDB; Q60173; -. DR UniPathway; UPA00109; UER00187. DR EvolutionaryTrace; Q60173; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009986; C:cell surface; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.120; -; 1. DR Gene3D; 3.30.390.10; -; 1. DR HAMAP; MF_00318; Enolase; 1. DR InterPro; IPR000941; Enolase. DR InterPro; IPR020810; Enolase_C. DR InterPro; IPR029065; Enolase_C-like. DR InterPro; IPR020809; Enolase_CS. DR InterPro; IPR020811; Enolase_N. DR InterPro; IPR029017; Enolase_N-like. DR PANTHER; PTHR11902; PTHR11902; 1. DR Pfam; PF00113; Enolase_C; 1. DR Pfam; PF03952; Enolase_N; 1. DR PIRSF; PIRSF001400; Enolase; 1. DR PRINTS; PR00148; ENOLASE. DR SMART; SM01192; Enolase_C; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF51604; SSF51604; 1. DR SUPFAM; SSF54826; SSF54826; 1. DR TIGRFAMs; TIGR01060; eno; 1. DR PROSITE; PS00164; ENOLASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Glycolysis; Lyase; KW Magnesium; Metal-binding; Reference proteome; Secreted. FT CHAIN 1 423 Enolase. FT /FTId=PRO_0000134024. FT REGION 362 365 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 209 209 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT ACT_SITE 335 335 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 244 244 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 285 285 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT METAL 310 310 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 157 157 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 166 166 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 285 285 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 310 310 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT BINDING 335 335 Substrate (covalent); in inhibited form. FT {ECO:0000255|HAMAP-Rule:MF_00318}. FT BINDING 386 386 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00318}. FT HELIX 3 5 {ECO:0000244|PDB:2PA6}. FT STRAND 6 16 {ECO:0000244|PDB:2PA6}. FT STRAND 22 30 {ECO:0000244|PDB:2PA6}. FT STRAND 35 39 {ECO:0000244|PDB:2PA6}. FT STRAND 48 50 {ECO:0000244|PDB:2PA6}. FT HELIX 60 63 {ECO:0000244|PDB:2PA6}. FT HELIX 67 75 {ECO:0000244|PDB:2PA6}. FT HELIX 77 81 {ECO:0000244|PDB:2PA6}. FT HELIX 89 100 {ECO:0000244|PDB:2PA6}. FT TURN 106 108 {ECO:0000244|PDB:2PA6}. FT HELIX 110 128 {ECO:0000244|PDB:2PA6}. FT HELIX 132 137 {ECO:0000244|PDB:2PA6}. FT STRAND 149 153 {ECO:0000244|PDB:2PA6}. FT TURN 156 158 {ECO:0000244|PDB:2PA6}. FT STRAND 159 161 {ECO:0000244|PDB:2PA6}. FT STRAND 163 170 {ECO:0000244|PDB:2PA6}. FT HELIX 177 199 {ECO:0000244|PDB:2PA6}. FT HELIX 219 233 {ECO:0000244|PDB:2PA6}. FT TURN 236 238 {ECO:0000244|PDB:2PA6}. FT STRAND 240 244 {ECO:0000244|PDB:2PA6}. FT HELIX 247 250 {ECO:0000244|PDB:2PA6}. FT STRAND 255 258 {ECO:0000244|PDB:2PA6}. FT STRAND 261 263 {ECO:0000244|PDB:2PA6}. FT HELIX 265 278 {ECO:0000244|PDB:2PA6}. FT STRAND 281 285 {ECO:0000244|PDB:2PA6}. FT HELIX 293 302 {ECO:0000244|PDB:2PA6}. FT STRAND 303 310 {ECO:0000244|PDB:2PA6}. FT TURN 311 315 {ECO:0000244|PDB:2PA6}. FT HELIX 317 326 {ECO:0000244|PDB:2PA6}. FT STRAND 330 334 {ECO:0000244|PDB:2PA6}. FT HELIX 336 339 {ECO:0000244|PDB:2PA6}. FT HELIX 342 353 {ECO:0000244|PDB:2PA6}. FT TURN 354 356 {ECO:0000244|PDB:2PA6}. FT STRAND 358 362 {ECO:0000244|PDB:2PA6}. FT HELIX 372 379 {ECO:0000244|PDB:2PA6}. FT STRAND 383 386 {ECO:0000244|PDB:2PA6}. FT HELIX 393 408 {ECO:0000244|PDB:2PA6}. FT STRAND 409 411 {ECO:0000244|PDB:2PA6}. FT HELIX 416 418 {ECO:0000244|PDB:2PA6}. SQ SEQUENCE 423 AA; 46298 MW; 9C9BB163E64BF577 CRC64; MDERFEIKDI VAREVIDSRG NPTVEVEVIT KGNGYGSAIV PSGASTGTHE ALELRDKEKR FGGKGVLMAV ENVNSIIRPE ILGYDARMQR EIDTIMIELD GTPNKSRLGA NAILAVSLAV AKAAAATAKI PLYKYLGGFN SYVMPVPMMN VINGGKHAGN DLDLQEFMIM PVGATSISEA VRMGSEVYHV LKNVILEKYG KNAVNVGDEG GFAPPLKTSR EALDLLTESV KKAGYEDEVV FALDAAASEF YKDGYYYVEG KKLTREELLD YYKALVDEYP IVSIEDPFHE EDFEGFAMIT KELDIQIVGD DLFVTNVERL RKGIEMKAAN ALLLKVNQIG TLSEAVDAAQ LAFRNGYGVV VSHRSGETED TTIADLSVAL NSGQIKTGAP ARGERTAKYN QLIRIEQELG LSKYAGRNFR CPF // ID EHAA_METJA Reviewed; 98 AA. AC Q57948; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Probable [NiFe]-hydrogenase-type-3 Eha complex membrane subunit A; GN Name=ehaA; OrderedLocusNames=MJ0528; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the integral membrane subunits of multisubunit CC membrane-bound [NiFe]-hydrogenase eha. Eha is predicted to form CC large electron transfer complex and might catalyze energy-driven CC reduction of low-potential redox carriers (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Putative multisubunit membrane-bound [NiFe]-hydrogenase CC eha is composed of at least 20 subunits. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the EhaA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98519.1; -; Genomic_DNA. DR PIR; H64365; H64365. DR ProteinModelPortal; Q57948; -. DR STRING; 243232.MJ_0528; -. DR EnsemblBacteria; AAB98519; AAB98519; MJ_0528. DR KEGG; mja:MJ_0528; -. DR eggNOG; arCOG05035; Archaea. DR eggNOG; COG4042; LUCA. DR KO; K14092; -. DR OMA; NLFGDYI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011306; Prd_NiFe_hyd_3_EhaA. DR PIRSF; PIRSF005019; EhaA; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 98 Probable [NiFe]-hydrogenase-type-3 Eha FT complex membrane subunit A. FT /FTId=PRO_0000138112. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. SQ SEQUENCE 98 AA; 10936 MW; B024D42F4239FE96 CRC64; MVYNNSLLVR VMDIIILYLI ALITSVIVAL VLKLPIIPKE KPIRFSFETS IIFPTPILAL GIEAIFRNLF GDYISLAFFA GLFGALLSKY ADKLFGEP // ID FAEHP_METJA Reviewed; 381 AA. AC Q58842; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Bifunctional enzyme Fae/Hps {ECO:0000255|HAMAP-Rule:MF_01268}; DE Includes: DE RecName: Full=5,6,7,8-tetrahydromethanopterin hydro-lyase {ECO:0000255|HAMAP-Rule:MF_01268}; DE EC=4.2.1.147 {ECO:0000255|HAMAP-Rule:MF_01268}; DE AltName: Full=Formaldehyde-activating enzyme {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021}; DE Short=Fae {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021}; DE Includes: DE RecName: Full=3-hexulose-6-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021}; DE Short=HPS {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000303|PubMed:16237021}; DE EC=4.1.2.43 {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16237021}; DE AltName: Full=D-arabino-3-hexulose-6-phosphate formaldehyde lyase {ECO:0000255|HAMAP-Rule:MF_01268}; GN Name=fae-hps {ECO:0000255|HAMAP-Rule:MF_01268}; GN OrderedLocusNames=MJ1447; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A HPS, AND PATHWAY. RX PubMed=16237021; DOI=10.1128/JB.187.21.7382-7389.2005; RA Grochowski L.L., Xu H., White R.H.; RT "Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii RT occurs in the absence of a pentose-phosphate pathway."; RL J. Bacteriol. 187:7382-7389(2005). CC -!- FUNCTION: Catalyzes the condensation of formaldehyde with CC tetrahydromethanopterin (H(4)MPT) to 5,10- CC methylenetetrahydromethanopterin. {ECO:0000255|HAMAP- CC Rule:MF_01268, ECO:0000303|PubMed:16237021}. CC -!- FUNCTION: Catalyzes the reversible formation of ribulose-5- CC phosphate and formaldehyde from 3-hexulose-6-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01268, ECO:0000269|PubMed:16237021}. CC -!- CATALYTIC ACTIVITY: 5,6,7,8-tetrahydromethanopterin + formaldehyde CC = 5,10-methylenetetrahydromethanopterin + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01268}. CC -!- CATALYTIC ACTIVITY: D-arabino-hex-3-ulose 6-phosphate = D-ribulose CC 5-phosphate + formaldehyde. {ECO:0000255|HAMAP-Rule:MF_01268, CC ECO:0000269|PubMed:16237021}. CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01268, CC ECO:0000269|PubMed:16237021}. CC -!- SIMILARITY: In the N-terminal section; belongs to the CC formaldehyde-activating enzyme family. {ECO:0000255|HAMAP- CC Rule:MF_01268}. CC -!- SIMILARITY: In the C-terminal section; belongs to the HPS/KGPDC CC family. HPS subfamily. {ECO:0000255|HAMAP-Rule:MF_01268}. CC -!- CAUTION: Ile-16 is present instead of the conserved His which is CC expected to be an active site residue. Substrate-binding sites are CC also not conserved. Thus, this enzyme may not display fae CC activity. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99456.1; -; Genomic_DNA. DR PIR; F64480; F64480. DR ProteinModelPortal; Q58842; -. DR STRING; 243232.MJ_1447; -. DR DNASU; 1452351; -. DR EnsemblBacteria; AAB99456; AAB99456; MJ_1447. DR KEGG; mja:MJ_1447; -. DR eggNOG; arCOG00053; Archaea. DR eggNOG; arCOG00103; Archaea. DR eggNOG; COG0269; LUCA. DR eggNOG; COG1795; LUCA. DR InParanoid; Q58842; -. DR KO; K13812; -. DR OMA; LWDPPYL; -. DR PhylomeDB; Q58842; -. DR UniPathway; UPA00293; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:InterPro. DR GO; GO:0043801; F:hexulose-6-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:InterPro. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.30.230.60; -; 1. DR HAMAP; MF_01268; Fae_Hps; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR020868; Fae/Hps. DR InterPro; IPR014826; HCHO-activating_enzyme. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF08714; Fae; 1. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR SUPFAM; SSF54211; SSF54211; 1. PE 1: Evidence at protein level; KW Carbohydrate metabolism; Complete proteome; Lyase; KW Multifunctional enzyme; Reference proteome. FT CHAIN 1 381 Bifunctional enzyme Fae/Hps. FT /FTId=PRO_0000212107. FT REGION 1 150 Formaldehyde-activating enzyme. FT {ECO:0000255|HAMAP-Rule:MF_01268}. FT REGION 151 381 3-hexulose-6-phosphate synthase. FT {ECO:0000255|HAMAP-Rule:MF_01268}. SQ SEQUENCE 381 AA; 42990 MW; BB4C460AE796FAA3 CRC64; MIKFGEAVLG NEIKAIVNVA LGKGELIENT FTNALTRGNC VFANLRPNLI VKPLTLVVPR HNIESEIQDE LFQGVIQYAV AKAVADLDLD EDLKVVVSVN VPEVPITNLN KRKLFQYFYA SAKLAINRAL NEYPSKEKVK KEKYRALHPL VGFRDVRLEY PPYLQIALDV PTMENLEFLL QTIPNSDHII LEAGTPLIKK FGLEVIEIMR EYFDGFIVAD LKTLDTGRVE VRLAFEATAN AVAISGVAPK STIIKAIHEC QKCGLISYLD MMNVSEPQKL YDSLKLKPDV VILHRGIDEE TFGIKKEWKF KENCLLAIAG GVGVENVEEL LKEYQILIVG RAITKSKDPG RVIRMFINKM GYDIDTYRLY FDEDEDIGEE L // ID FER8_METJA Reviewed; 151 AA. AC Q57619; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Uncharacterized ferredoxin MJ0155; GN OrderedLocusNames=MJ0155; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98137.1; -; Genomic_DNA. DR PIR; D64319; D64319. DR ProteinModelPortal; Q57619; -. DR STRING; 243232.MJ_0155; -. DR EnsemblBacteria; AAB98137; AAB98137; MJ_0155. DR KEGG; mja:MJ_0155; -. DR eggNOG; ENOG4102TA7; Archaea. DR eggNOG; COG1142; LUCA. DR InParanoid; Q57619; -. DR OMA; AACMQVC; -. DR PhylomeDB; Q57619; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR000813; 7Fe_ferredoxin. DR Pfam; PF13247; Fer4_11; 1. DR PRINTS; PR00354; 7FE8SFRDOXIN. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 151 Uncharacterized ferredoxin MJ0155. FT /FTId=PRO_0000159136. FT DOMAIN 4 32 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 33 63 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 64 93 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 13 13 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 16 16 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 23 23 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 42 42 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 45 45 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 50 50 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 73 73 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 76 76 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 79 79 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 83 83 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 98 98 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 101 101 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 111 111 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 115 115 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 151 AA; 16985 MW; 86EC9B27DEFAEAF1 CRC64; MNPKIIVLNP EKCTKCYDCI NICKEIHGES RVRKVDGIPI FCMQCENAPC KEICPVDAIY LKDGIPIVDK ERCIACGMCA IACPIGAIFI KNRVAHKCTL CLDVDRITPA CVEACKDKAL LLVSEETLDM MKEEKRKKIL KILREEAKEN L // ID FER7_METJA Reviewed; 77 AA. AC Q58132; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uncharacterized ferredoxin MJ0722; GN OrderedLocusNames=MJ0722; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons probably in the CO-dehydrogenase complex. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98718.1; -; Genomic_DNA. DR PIR; B64390; B64390. DR ProteinModelPortal; Q58132; -. DR STRING; 243232.MJ_0722; -. DR EnsemblBacteria; AAB98718; AAB98718; MJ_0722. DR KEGG; mja:MJ_0722; -. DR eggNOG; arCOG02587; Archaea. DR eggNOG; COG1146; LUCA. DR InParanoid; Q58132; -. DR OMA; CAGRCPT; -. DR PhylomeDB; Q58132; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 77 Uncharacterized ferredoxin MJ0722. FT /FTId=PRO_0000159135. FT DOMAIN 3 32 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 36 65 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 12 12 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 15 15 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 18 18 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 45 45 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 48 48 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 51 51 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 55 55 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 77 AA; 8847 MW; 7514C8E87906A879 CRC64; MAVEIIVDRE KCIGCGRCYD VCPKGPLIWT KDENGKYYAY DVEYCHNCKF CAGRCPTNAI LIKVVKPKKK DENKNKK // ID FERA_METJA Reviewed; 56 AA. AC Q57953; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Uncharacterized ferredoxin MJ0533; GN OrderedLocusNames=MJ0533; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons in a wide variety of metabolic reactions. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98524.1; -; Genomic_DNA. DR PIR; E64366; E64366. DR ProteinModelPortal; Q57953; -. DR STRING; 243232.MJ_0533; -. DR EnsemblBacteria; AAB98524; AAB98524; MJ_0533. DR KEGG; mja:MJ_0533; -. DR eggNOG; arCOG00958; Archaea. DR eggNOG; COG1145; LUCA. DR InParanoid; Q57953; -. DR OMA; HIIVIDE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 56 Uncharacterized ferredoxin MJ0533. FT /FTId=PRO_0000159138. FT DOMAIN 2 28 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 29 56 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 9 9 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 12 12 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 15 15 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 38 38 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 41 41 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 44 44 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 48 48 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 56 AA; 6160 MW; A2DD7651E00B2AC1 CRC64; MVKIDYKKCG YCGACVGVCE KLAINLIEHI IVIDEKKCNN CKLCTIVCPL NALEGE // ID FKBP1_METJA Reviewed; 157 AA. AC Q57726; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative FKBP-type peptidyl-prolyl cis-trans isomerase MJ0278; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Rotamase; GN OrderedLocusNames=MJ0278; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: PPIases accelerate the folding of proteins. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98266.1; -; Genomic_DNA. DR PIR; G64334; G64334. DR ProteinModelPortal; Q57726; -. DR SMR; Q57726; 4-151. DR STRING; 243232.MJ_0278; -. DR EnsemblBacteria; AAB98266; AAB98266; MJ_0278. DR KEGG; mja:MJ_0278; -. DR eggNOG; arCOG00981; Archaea. DR eggNOG; COG1047; LUCA. DR InParanoid; Q57726; -. DR KO; K03775; -. DR OMA; QEIPKEM; -. DR PhylomeDB; Q57726; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005528; F:FK506 binding; IBA:GO_Central. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central. DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GOC. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PTHR10516; 1. DR Pfam; PF00254; FKBP_C; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; Rotamase. FT CHAIN 1 157 Putative FKBP-type peptidyl-prolyl cis- FT trans isomerase MJ0278. FT /FTId=PRO_0000075376. FT DOMAIN 1 95 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. SQ SEQUENCE 157 AA; 17680 MW; 36C895C541FA0D44 CRC64; MINLIKKGDY VKVDYILEVD GKVIDTSIEE VAKENKIYYP EREYEPIGFI VGNGELIEGF EEAVIGMEVG EEKTVTIPPE KGYGLRDERL IQEIPKEMFA DADFEPQEGM LILASGIPAK IIKVTDDTVT LDFNHELAGK ELKFTIKVRD VQPAESE // ID FER3_METJA Reviewed; 69 AA. AC Q57610; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized ferredoxin MJ0146; GN OrderedLocusNames=MJ0146; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98129.1; -; Genomic_DNA. DR PIR; C64318; C64318. DR ProteinModelPortal; Q57610; -. DR STRING; 243232.MJ_0146; -. DR EnsemblBacteria; AAB98129; AAB98129; MJ_0146. DR KEGG; mja:MJ_0146; -. DR eggNOG; arCOG00959; Archaea. DR eggNOG; COG1146; LUCA. DR InParanoid; Q57610; -. DR KO; K00176; -. DR OMA; FCKGCDI; -. DR PhylomeDB; Q57610; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 69 Uncharacterized ferredoxin MJ0146. FT /FTId=PRO_0000159131. FT DOMAIN 2 30 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 38 67 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 10 10 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 13 13 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 16 16 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 20 20 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 47 47 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 50 50 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 53 53 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 57 57 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 69 AA; 7756 MW; 19FBAACD8A6FEEFB CRC64; MKIEINENFC KGCDICIVVC PRGVFEKSKK LNKKGIYPPI PVNPEKCTKC NLCILQCPDQ AISIELSQE // ID FER4_METJA Reviewed; 62 AA. AC Q57652; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized ferredoxin MJ0199; GN OrderedLocusNames=MJ0199; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98183.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98183.1; ALT_INIT; Genomic_DNA. DR PIR; H64324; H64324. DR ProteinModelPortal; Q57652; -. DR STRING; 243232.MJ_0199; -. DR EnsemblBacteria; AAB98183; AAB98183; MJ_0199. DR KEGG; mja:MJ_0199; -. DR eggNOG; arCOG00959; Archaea. DR eggNOG; COG1146; LUCA. DR InParanoid; Q57652; -. DR OMA; VDVCPME; -. DR PhylomeDB; Q57652; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 62 Uncharacterized ferredoxin MJ0199. FT /FTId=PRO_0000159132. FT DOMAIN 2 31 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 32 62 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 10 10 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 15 15 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 18 18 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 22 22 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 42 42 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 45 45 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 48 48 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 52 52 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 62 AA; 6650 MW; C46FA4A11722276A CRC64; MAVTIDYSLC KGAECAECVN NCPMEVFEIE GDKVVVARPD DCTYCGVCED VCPTGAVKVE PE // ID FKBP2_METJA Reviewed; 231 AA. AC Q58235; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative FKBP-type peptidyl-prolyl cis-trans isomerase MJ0825; DE Short=PPIase; DE EC=5.2.1.8; DE AltName: Full=Rotamase; GN OrderedLocusNames=MJ0825; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: PPIases accelerate the folding of proteins. CC -!- CATALYTIC ACTIVITY: Peptidylproline (omega=180) = peptidylproline CC (omega=0). CC -!- SIMILARITY: Belongs to the FKBP-type PPIase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PPIase FKBP-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00277}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98824.1; -; Genomic_DNA. DR PDB; 3PR9; X-ray; 1.95 A; A=1-150. DR PDB; 3PRA; X-ray; 2.40 A; A/B=1-150. DR PDB; 3PRB; X-ray; 2.20 A; A/B=1-231. DR PDB; 3PRD; X-ray; 3.30 A; A=1-231. DR PDBsum; 3PR9; -. DR PDBsum; 3PRA; -. DR PDBsum; 3PRB; -. DR PDBsum; 3PRD; -. DR ProteinModelPortal; Q58235; -. DR STRING; 243232.MJ_0825; -. DR EnsemblBacteria; AAB98824; AAB98824; MJ_0825. DR KEGG; mja:MJ_0825; -. DR eggNOG; arCOG00980; Archaea. DR eggNOG; COG1047; LUCA. DR InParanoid; Q58235; -. DR KO; K03775; -. DR OMA; NIQTAKM; -. DR PhylomeDB; Q58235; -. DR EvolutionaryTrace; Q58235; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005528; F:FK506 binding; IBA:GO_Central. DR GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IBA:GO_Central. DR GO; GO:0061077; P:chaperone-mediated protein folding; IBA:GO_Central. DR GO; GO:0000413; P:protein peptidyl-prolyl isomerization; IBA:GOC. DR InterPro; IPR023566; PPIase_FKBP. DR InterPro; IPR001179; PPIase_FKBP_dom. DR PANTHER; PTHR10516; PTHR10516; 1. DR Pfam; PF00254; FKBP_C; 1. DR PROSITE; PS50059; FKBP_PPIASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome; KW Rotamase. FT CHAIN 1 231 Putative FKBP-type peptidyl-prolyl cis- FT trans isomerase MJ0825. FT /FTId=PRO_0000075377. FT DOMAIN 5 92 PPIase FKBP-type. {ECO:0000255|PROSITE- FT ProRule:PRU00277}. FT STRAND 7 16 {ECO:0000244|PDB:3PR9}. FT STRAND 19 24 {ECO:0000244|PDB:3PR9}. FT HELIX 26 31 {ECO:0000244|PDB:3PR9}. FT STRAND 44 47 {ECO:0000244|PDB:3PR9}. FT STRAND 50 53 {ECO:0000244|PDB:3PR9}. FT HELIX 55 63 {ECO:0000244|PDB:3PR9}. FT STRAND 69 74 {ECO:0000244|PDB:3PR9}. FT HELIX 76 78 {ECO:0000244|PDB:3PR9}. FT HELIX 85 87 {ECO:0000244|PDB:3PR9}. FT STRAND 88 92 {ECO:0000244|PDB:3PR9}. FT HELIX 93 98 {ECO:0000244|PDB:3PR9}. FT STRAND 108 111 {ECO:0000244|PDB:3PR9}. FT STRAND 114 122 {ECO:0000244|PDB:3PR9}. FT STRAND 125 129 {ECO:0000244|PDB:3PR9}. FT TURN 133 136 {ECO:0000244|PDB:3PR9}. FT STRAND 139 149 {ECO:0000244|PDB:3PR9}. FT HELIX 152 163 {ECO:0000244|PDB:3PRB}. FT STRAND 171 175 {ECO:0000244|PDB:3PRB}. FT STRAND 178 182 {ECO:0000244|PDB:3PRB}. FT HELIX 187 189 {ECO:0000244|PDB:3PRB}. FT HELIX 193 207 {ECO:0000244|PDB:3PRB}. FT STRAND 213 221 {ECO:0000244|PDB:3PRB}. SQ SEQUENCE 231 AA; 25947 MW; ABD9AD1DB1B6C420 CRC64; MVEKGKMVKI SYDGYVDGKL FDTTNEELAK KEGIYNPAMI YGPVAIFAGE GQVLPGLDEA ILEMDVGEER EVVLPPEKAF GKRDPSKIKL IPLSEFTKRG IKPIKGLTIT IDGIPGKIVS INSGRVLVDF NHELAGKEVK YRIKIEEVVD DKKNIVKEIV KMYVPRLSDV KVTIRNGTVK IELPEFAPFI PNIQTAKMAI ANEILKRLED AEKVSFVETF ERKKETKEEN K // ID FLAH_METJA Reviewed; 233 AA. AC Q58309; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Putative flagella-related protein H; GN Name=flaH; OrderedLocusNames=MJ0899; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaH. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98902.1; -; Genomic_DNA. DR PIR; C64412; C64412. DR PDB; 4WIA; X-ray; 2.20 A; A/B/C=1-233. DR PDBsum; 4WIA; -. DR ProteinModelPortal; Q58309; -. DR STRING; 243232.MJ_0899; -. DR EnsemblBacteria; AAB98902; AAB98902; MJ_0899. DR KEGG; mja:MJ_0899; -. DR eggNOG; arCOG04148; Archaea. DR eggNOG; COG2874; LUCA. DR InParanoid; Q58309; -. DR KO; K07331; -. DR OMA; KRFAGMG; -. DR PhylomeDB; Q58309; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR014774; KaiC-like_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF06745; ATPase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure; Archaeal flagellum; ATP-binding; Complete proteome; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 233 Putative flagella-related protein H. FT /FTId=PRO_0000087278. FT NP_BIND 34 41 ATP. {ECO:0000255}. FT HELIX 16 19 {ECO:0000244|PDB:4WIA}. FT STRAND 22 25 {ECO:0000244|PDB:4WIA}. FT STRAND 29 33 {ECO:0000244|PDB:4WIA}. FT HELIX 40 53 {ECO:0000244|PDB:4WIA}. FT STRAND 58 64 {ECO:0000244|PDB:4WIA}. FT HELIX 67 76 {ECO:0000244|PDB:4WIA}. FT HELIX 82 86 {ECO:0000244|PDB:4WIA}. FT STRAND 89 94 {ECO:0000244|PDB:4WIA}. FT HELIX 96 100 {ECO:0000244|PDB:4WIA}. FT HELIX 108 114 {ECO:0000244|PDB:4WIA}. FT HELIX 116 119 {ECO:0000244|PDB:4WIA}. FT STRAND 121 127 {ECO:0000244|PDB:4WIA}. FT HELIX 129 134 {ECO:0000244|PDB:4WIA}. FT HELIX 142 153 {ECO:0000244|PDB:4WIA}. FT TURN 154 156 {ECO:0000244|PDB:4WIA}. FT STRAND 158 163 {ECO:0000244|PDB:4WIA}. FT HELIX 165 167 {ECO:0000244|PDB:4WIA}. FT HELIX 170 179 {ECO:0000244|PDB:4WIA}. FT STRAND 181 191 {ECO:0000244|PDB:4WIA}. FT STRAND 194 204 {ECO:0000244|PDB:4WIA}. FT STRAND 213 220 {ECO:0000244|PDB:4WIA}. FT TURN 221 223 {ECO:0000244|PDB:4WIA}. FT STRAND 224 227 {ECO:0000244|PDB:4WIA}. SQ SEQUENCE 233 AA; 26010 MW; 6225E2B2E8DD22CA CRC64; MGIMELARID LSRDDLDKRI GGGIPHGSLI IIEGEESTGK SVLCQRLAYG FLQNRYSVTY VSTQLTTLEF IKQMNSLNYS INKKLLSGAL LYIPVYPLIA DNKKKDGFLK KVMETRAFYE KDVIIFDSIS ALIANDASEV NVDDLMAFFK RITALKKIII CTVNPKELPE SVLTIIRTSA TMLIRTELFT FGGDLKNLAK ILKYNMAPGS YQKNIVFRVE PKIGIAVEIA SVA // ID FDHD_METJA Reviewed; 227 AA. AC Q57743; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 96. DE RecName: Full=Protein FdhD {ECO:0000255|HAMAP-Rule:MF_00187}; GN Name=fdhD {ECO:0000255|HAMAP-Rule:MF_00187}; OrderedLocusNames=MJ0295; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Required for formate dehydrogenase (FDH) activity. CC {ECO:0000255|HAMAP-Rule:MF_00187}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00187}. CC -!- SIMILARITY: Belongs to the FdhD family. {ECO:0000255|HAMAP- CC Rule:MF_00187}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98280.1; -; Genomic_DNA. DR PIR; H64336; H64336. DR ProteinModelPortal; Q57743; -. DR STRING; 243232.MJ_0295; -. DR EnsemblBacteria; AAB98280; AAB98280; MJ_0295. DR KEGG; mja:MJ_0295; -. DR eggNOG; arCOG04358; Archaea. DR eggNOG; COG1526; LUCA. DR InParanoid; Q57743; -. DR KO; K02379; -. DR OMA; SPSTDKG; -. DR PhylomeDB; Q57743; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR HAMAP; MF_00187; FdhD; 1. DR InterPro; IPR016193; Cytidine_deaminase-like. DR InterPro; IPR003786; FdhD. DR Pfam; PF02634; FdhD-NarQ; 1. DR SUPFAM; SSF53927; SSF53927; 1. DR TIGRFAMs; TIGR00129; fdhD_narQ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 227 Protein FdhD. FT /FTId=PRO_0000152936. FT REGION 210 215 Molybdenum binding. {ECO:0000255|HAMAP- FT Rule:MF_00187}. FT BINDING 190 190 Molybdenum. {ECO:0000255|HAMAP- FT Rule:MF_00187}. SQ SEQUENCE 227 AA; 26119 MW; 80CCC2FCF90D43CC CRC64; MIKKVKIKKF NGRDFYDMED YVAVEESYNI FINGEFVKSL SMSPNFLNEF AVGFAISEGF LNKIDKVEVD KNNINIFGEK NDREIKNNKN NKEIKIDIEI IKKIISYEIK AKYWEITGSF HWASMFDLKG NSIIFVEDIG RHNAVDKVIG YAILNNYNLN KLILRYSGRI PSDIVKKAIN SGLNIIISKS PPTDKAIELA EENNILLIGF ARNGKFNIYT SGRLWEE // ID FER1_METJA Reviewed; 80 AA. AC Q60368; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized ferredoxin MJ0061; GN OrderedLocusNames=MJ0061; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98043.1; -; Genomic_DNA. DR PIR; E64307; E64307. DR ProteinModelPortal; Q60368; -. DR STRING; 243232.MJ_0061; -. DR EnsemblBacteria; AAB98043; AAB98043; MJ_0061. DR KEGG; mja:MJ_0061; -. DR eggNOG; arCOG00959; Archaea. DR eggNOG; COG1146; LUCA. DR InParanoid; Q60368; -. DR OMA; CKNNVFA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR Pfam; PF13187; Fer4_9; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 80 Uncharacterized ferredoxin MJ0061. FT /FTId=PRO_0000159129. FT DOMAIN 21 49 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 50 80 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 30 30 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 33 33 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 36 36 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 40 40 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 60 60 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 63 63 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 66 66 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 70 70 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 80 AA; 9185 MW; BE7C286649604918 CRC64; MLSKILGIFK GKEKIEEKSN KIIEIDYNKC KNCLSCYRVC KNNVFAIKNN RVVVKNENNC TKCGECLKVC RYGAIILYDA // ID FLAF_METJA Reviewed; 139 AA. AC Q58307; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Putative flagella-related protein F; DE Flags: Precursor; GN Name=flaF; OrderedLocusNames=MJ0897; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000305}. Membrane CC {ECO:0000305}; Lipid-anchor {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaF. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98900.1; -; Genomic_DNA. DR PIR; A64412; A64412. DR STRING; 243232.MJ_0897; -. DR EnsemblBacteria; AAB98900; AAB98900; MJ_0897. DR KEGG; mja:MJ_0897; -. DR eggNOG; arCOG01824; Archaea. DR eggNOG; COG3353; LUCA. DR KO; K07329; -. DR OMA; QTNITIY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. PE 3: Inferred from homology; KW Acetylation; Archaeal flagellum; Complete proteome; Lipoprotein; KW Membrane; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 139 Putative flagella-related protein F. FT /FTId=PRO_0000021270. FT MOD_RES 19 19 N-acetylcysteine. {ECO:0000305}. FT LIPID 19 19 S-archaeol cysteine. {ECO:0000305}. SQ SEQUENCE 139 AA; 15624 MW; 4FB4BB7170E40C06 CRC64; MGFSSVVGAT VMIIALLVCG AYLYVTMDSY YENVDEAYTT YYSHVHAKLN EKLVITDVKS STSQTNITIY NNGSVVVEPD KFTILFDGTV VPEENISYYP KLKKYLVPLD SITIVVNWTQ PSRICIVSDN GNKYFYSLT // ID FLAK_METJA Reviewed; 234 AA. AC Q58312; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2012, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=Preflagellin peptidase; DE Short=PFP; DE EC=3.4.23.52; GN Name=flaK; OrderedLocusNames=MJ0902; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Cleaves the N-terminal leader peptide from CC preflagellins. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Cleaves the signal peptide of 3 to 12 amino CC acids from the N-terminal of preflagellin, usually at Arg-Gly-|- CC or Lys-Gly-|-, to release flagellin. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase A24 family. Archaeal CC preflagellin peptidase subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98907.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98907.1; ALT_INIT; Genomic_DNA. DR PIR; F64412; F64412. DR STRING; 243232.MJ_0902; -. DR MEROPS; A24.016; -. DR EnsemblBacteria; AAB98907; AAB98907; MJ_0902. DR KEGG; mja:MJ_0902; -. DR eggNOG; arCOG02298; Archaea. DR eggNOG; COG1989; LUCA. DR InParanoid; Q58312; -. DR KO; K07991; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR009655; Preflagellin_peptidase_C. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF06847; Arc_PepC_II; 1. DR Pfam; PF01478; Peptidase_A24; 1. PE 3: Inferred from homology; KW Archaeal flagellum biogenesis; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Protease; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 234 Preflagellin peptidase. FT /FTId=PRO_0000107094. FT TOPO_DOM 1 1 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 2 18 Helical. {ECO:0000250}. FT TOPO_DOM 19 23 Extracellular. {ECO:0000250}. FT TRANSMEM 24 46 Helical. {ECO:0000250}. FT TOPO_DOM 47 49 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 50 72 Helical. {ECO:0000250}. FT TOPO_DOM 73 78 Extracellular. {ECO:0000250}. FT TRANSMEM 79 89 Helical. {ECO:0000250}. FT TOPO_DOM 90 110 Cytoplasmic. {ECO:0000250}. FT TRANSMEM 111 139 Helical. {ECO:0000250}. FT TOPO_DOM 140 205 Extracellular. {ECO:0000250}. FT TRANSMEM 206 217 Helical. {ECO:0000250}. FT TOPO_DOM 218 234 Cytoplasmic. {ECO:0000250}. FT SITE 18 18 Essential for catalysis. {ECO:0000250}. FT SITE 79 79 Essential for catalysis. {ECO:0000250}. SQ SEQUENCE 234 AA; 26294 MW; A0F94DDCA7F7D2D4 CRC64; MINFIVGAIG LLIASIYDLK SREIEDYVWV SMVIFGLIYN GYLSFISHDM LYVIQSIVGF IVCFFLGFFM FLLGVGGGDG KLIMGLGALI PKYNMPIHTP LGAILNYLYL PSFPIMVVIN AMFFSITLPI IIFLRNVIRG VKPKTKKEVL CMFLGEKMKV SEAIKKERLI LGNHENLKLL PSAEKDCDFS KFDKNEEIWV TPAIPFVVPI FLSYLLTSII GDKIIGIFLS VFGL // ID FDHA_METJA Reviewed; 673 AA. AC P61159; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 67. DE RecName: Full=Formate dehydrogenase subunit alpha; DE EC=1.2.1.2; GN Name=fdhA; OrderedLocusNames=MJ1353; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-131. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- FUNCTION: Catalyzes the oxidation of formate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH. CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SUBUNIT: Dimer of an alpha and a beta subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P61159; -. DR InParanoid; P61159; -. DR OMA; EIGFFSS; -. DR PhylomeDB; P61159; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0015942; P:formate metabolic process; IEA:InterPro. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR006478; Formate_DH_asu. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR TIGRFAMs; TIGR01591; Fdh-alpha; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; Molybdenum; NAD; Oxidoreductase; Reference proteome; KW Selenocysteine; Zinc. FT CHAIN 1 673 Formate dehydrogenase subunit alpha. FT /FTId=PRO_0000063226. FT DOMAIN 3 59 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 10 10 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 13 13 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 17 17 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 45 45 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT NON_STD 131 131 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 673 AA; 75770 MW; B87A668BDF6B98D5 CRC64; MEFKIVNTIC PYCGVGCGLG LVVKDGRVIG IHPNKRHPIN EGKLCAKGNY CYQFIHSKDR LTKPLIKKES GFVETTWNKA LEVIAENLKT YKDEIGFFSS ARCTNEDNYI LQKFARVALK TNNIDHCARL UHSATVTGMS ACFGSGAMTN SIEDIELADC ILIIGSNTFE QHPLIARRIM RAKDKGAKII VIDPRRTITA KNSDIYLQII PGTNVALINA MINVIIKENL IDKEFIKNRT EGFEKLKEII KKYTPEYASK ICGVDKELII ESAKIYGNAE RASIIYCMGV TQFTHGVDAV KALCNLAMIT GNIGKEGTGV NPLRGQNNVQ GACDMGALPN VFPGYQKVED GYKLFEEYWK TDLNPNSGLT IPEMIDESGK NIKFLYIMGE NPIVSDPDVK HVEKALKSLD FLVVQDIFLT ETAKLADVVL PAACWAEKDG TFTNTERRVQ LIRKAVNPPG EALEDWIIIK KLAEKLGYGD KFNYNKVEDI FNEIRKVTPQ YRGITYKRLK IDGIHWPCLD ENHSGTKILH KDKFLTDNGR GKIFPVEYRE VAELPDKDYP FILTTGRIIF HYHTGTMTRR CKNLVEEINE PFIEINPDDA KSLKIENGDL VKVISRRGEI TAKARITEDI KKGVVFMPFH FVEANPNVLT NTALDELCKI PELKVCAVKI ERI // ID FDHB_METJA Reviewed; 379 AA. AC Q60316; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Formate dehydrogenase subunit beta; DE EC=1.2.1.2; GN Name=fdhB; OrderedLocusNames=MJ0005; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the oxidation of formate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305}; CC -!- SUBUNIT: Dimer of an alpha and a beta subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97986.1; -; Genomic_DNA. DR PIR; E64300; E64300. DR ProteinModelPortal; Q60316; -. DR STRING; 243232.MJ_0005; -. DR EnsemblBacteria; AAB97986; AAB97986; MJ_0005. DR KEGG; mja:MJ_0005; -. DR eggNOG; arCOG02653; Archaea. DR eggNOG; COG1035; LUCA. DR eggNOG; COG1145; LUCA. DR InParanoid; Q60316; -. DR KO; K00125; -. DR OMA; CAPTMFG; -. DR PhylomeDB; Q60316; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR007525; FrhB_FdhB_C. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Repeat; KW Transport. FT CHAIN 1 379 Formate dehydrogenase subunit beta. FT /FTId=PRO_0000159224. FT DOMAIN 271 301 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 321 351 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 280 280 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 283 283 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 286 286 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 290 290 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 330 330 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 333 333 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 336 336 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 340 340 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 379 AA; 43014 MW; 9C257CCAD5547F5A CRC64; MKYVLIQATD NGILRRAECG GAVTALFKYL LDKKLVDGVL ALKRGEDVYD GIPTFITNSN ELVETAGSLH CAPTNFGKLI AKYLADKKIA VPAKPCDAMA IRELAKLNQI NLDNVYMIGL NCGGTISPIT AMKMIELFYE VNPLDVVKEE IDKGKFIIEL KNGEHKAVKI EELEEKGFGR RKNCQRCEIM IPRMADLACG NWGAEKGWTF VEICSERGRK LVEDAEKDGY IKIKQPSEKA IQVREKIESI MIKLAKKFQK KHLEEEYPSL EKWKKYWNRC IKCYGCRDNC PLCFCVECSL EKDYIEEKGK IPPNPLIFQG IRLSHISQSC INCGQCEDAC PMDIPLAYIF HRMQLKIRDT LGYIPGVDNS LPPLFNIER // ID FER5_METJA Reviewed; 147 AA. AC Q57699; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized ferredoxin MJ0251; GN OrderedLocusNames=MJ0251; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98238.1; -; Genomic_DNA. DR PIR; D64331; D64331. DR ProteinModelPortal; Q57699; -. DR STRING; 243232.MJ_0251; -. DR EnsemblBacteria; AAB98238; AAB98238; MJ_0251. DR KEGG; mja:MJ_0251; -. DR eggNOG; arCOG02461; Archaea. DR eggNOG; COG1146; LUCA. DR InParanoid; Q57699; -. DR OMA; CCENNAI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 147 Uncharacterized ferredoxin MJ0251. FT /FTId=PRO_0000159133. FT DOMAIN 80 109 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 110 141 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 89 89 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 92 92 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 95 95 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 99 99 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 119 119 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 123 123 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 126 126 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 130 130 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 147 AA; 17654 MW; B01B3945B736D072 CRC64; MENLEKKIEL LKKIREFLIL NLEIKKLMQE LNVDSDIYEA YEKVTKIVRE PNIKLYRQYY DAIKEMFYEE YGKKRKDISW YPKIDYNRCK NCEKCISFCP RGVYDAENGK VVVKYPYSCI VNCNACSIMC CENNAIIFPD EKIPRRN // ID FLAD_METJA Reviewed; 342 AA. AC Q58305; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 78. DE RecName: Full=Putative flagella-related protein D; GN Name=flaD; OrderedLocusNames=MJ0895; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaD, also to FlaE. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98898.1; -; Genomic_DNA. DR PIR; G64411; G64411. DR ProteinModelPortal; Q58305; -. DR STRING; 243232.MJ_0895; -. DR EnsemblBacteria; AAB98898; AAB98898; MJ_0895. DR KEGG; mja:MJ_0895; -. DR eggNOG; arCOG02964; Archaea. DR eggNOG; COG3351; LUCA. DR InParanoid; Q58305; -. DR KO; K07327; -. DR OMA; VFKWLEF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR InterPro; IPR006752; Arch_fla_DE. DR Pfam; PF04659; Arch_fla_DE; 1. DR ProDom; PD012942; Arch_fla_DE; 1. PE 4: Predicted; KW Archaeal flagellum; Complete proteome; Reference proteome. FT CHAIN 1 342 Putative flagella-related protein D. FT /FTId=PRO_0000087269. SQ SEQUENCE 342 AA; 39951 MW; B384DDDE1775566C CRC64; MIQKTISETS PPPMFSDEEI LTEDEIEEYL DNLKSKLPSF VIILLKNNLR GKRVTKKQLD KIVERITEVL SKGRRDDKTE ELNKKLQTLE QKLDAIMKLT TMAVSTKTSE EIEKIKTNEK IEIENAPIKI KSEEKPEKPV EIEVSKKKET MDTGKKTETE EKVKEIEVPK PVEKTHEKVE ETKTKGEIKK EVKKEVKLKK YELPKESPMG GSFMTPIEEE KEYRLNDIPE DAVSMTLVFK WLEFLISRGG MTYLPDILDY YNKIGWISNR VILKLLRFAK NMKITFDEEE LRPRDKLSPS DHIVSLLYIE KLAGRPIDSE ILEMLEIEIR RIKKWAIELQ SI // ID FLAG_METJA Reviewed; 154 AA. AC Q58308; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Putative flagella-related protein G; GN Name=flaG; OrderedLocusNames=MJ0898; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaG. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98901.1; -; Genomic_DNA. DR PIR; B64412; B64412. DR STRING; 243232.MJ_0898; -. DR EnsemblBacteria; AAB98901; AAB98901; MJ_0898. DR KEGG; mja:MJ_0898; -. DR eggNOG; arCOG01822; Archaea. DR eggNOG; COG3354; LUCA. DR InParanoid; Q58308; -. DR KO; K07330; -. DR OMA; ATHIIFF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR InterPro; IPR002774; Flagellin_arc. DR Pfam; PF01917; Arch_flagellin; 1. PE 4: Predicted; KW Archaeal flagellum; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 154 Putative flagella-related protein G. FT /FTId=PRO_0000087273. FT TRANSMEM 12 32 Helical. {ECO:0000255}. SQ SEQUENCE 154 AA; 16537 MW; 67C5C67B3C7885BC CRC64; MIYLASSAMS EIVMFVAVLL IAAFVAGILT TSTYKISLNI NKKGDALATK LSQDFEIIND PGDIVRNSSA GTIALYIKNT GKDPIIFTND SFTVIIDGSI VEINTTNQLT SPGSNILSPG DVGEIVVNYN ETGYHRIKVI SECGISRIIR GYIS // ID FLAB3_METJA Reviewed; 216 AA. AC Q58303; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Flagellin B3; DE Flags: Precursor; GN Name=flaB3; OrderedLocusNames=MJ0893; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to CC form the filaments of archaeal flagella. CC -!- SUBCELLULAR LOCATION: Archaeal flagellum. CC -!- SIMILARITY: Belongs to the archaeal flagellin family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98896.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98896.1; ALT_INIT; Genomic_DNA. DR PIR; E64411; E64411. DR STRING; 243232.MJ_0893; -. DR PRIDE; Q58303; -. DR DNASU; 1451782; -. DR EnsemblBacteria; AAB98896; AAB98896; MJ_0893. DR KEGG; mja:MJ_0893; -. DR eggNOG; arCOG01829; Archaea. DR eggNOG; COG1681; LUCA. DR InParanoid; Q58303; -. DR KO; K07325; -. DR OMA; HKASTVG; -. DR PhylomeDB; Q58303; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR InterPro; IPR013373; Flagellin/pilin_N. DR InterPro; IPR002774; Flagellin_arc. DR Pfam; PF01917; Arch_flagellin; 1. DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1. PE 3: Inferred from homology; KW Archaeal flagellum; Complete proteome; Reference proteome. FT PROPEP 1 11 {ECO:0000250}. FT /FTId=PRO_0000009377. FT CHAIN 12 216 Flagellin B3. FT /FTId=PRO_0000009378. SQ SEQUENCE 216 AA; 23053 MW; A1B36EC8C761DCE0 CRC64; MLLDYIKSRR GAIGIGTLII FIALVLVAAV AAAVIINTAA NLQHKAARVG EESTRQVASG IQVLKITGYA VNTKNITKLA ILVSPNVGDE IDLSSTIVTI SNGDYKASLV YGGQITYVNT NGTRDIFNES WPNIANPTTE FGVIVLQDAD GSMNNTEHPT MNFGDKAIIA INVGDVFGGI MPRERIYGEV IPEFGASGII EFRAPSTFSE HVVTLQ // ID FLAJ_METJA Reviewed; 562 AA. AC Q58311; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Flagella accessory protein J; GN Name=flaJ; OrderedLocusNames=MJ0901; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaJ. {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1286. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98904.1; -; Genomic_DNA. DR PIR; E64412; E64412. DR STRING; 243232.MJ_0901; -. DR EnsemblBacteria; AAB98904; AAB98904; MJ_0901. DR KEGG; mja:MJ_0901; -. DR eggNOG; arCOG01809; Archaea. DR eggNOG; COG1955; LUCA. DR InParanoid; Q58311; -. DR KO; K07333; -. DR OMA; DRLWHTG; -. DR PhylomeDB; Q58311; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR018076; T2SS_F. DR Pfam; PF00482; T2SSF; 2. PE 4: Predicted; KW Archaeal flagellum; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 562 Flagella accessory protein J. FT /FTId=PRO_0000087280. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 302 322 Helical. {ECO:0000255}. FT TRANSMEM 446 466 Helical. {ECO:0000255}. FT TRANSMEM 498 518 Helical. {ECO:0000255}. FT TRANSMEM 527 547 Helical. {ECO:0000255}. SQ SEQUENCE 562 AA; 63601 MW; F87DC2BDB763A351 CRC64; MVIVVFDLLP RVGLKPRDYL LRIVLPALIT SIVLILLGFM LFSGIILYIY LLLPIIILVS AIGYPYIALD SQKNKINERL HIFITKFGTL SITDLNRKDL LKILSEEREE LGELAKESEK LYVLTDKWGR SLAEACRFLA QRTPSSEFAD FLDRLAYALD SGEELKEFLI KEQDIVMDDY AAFYKRMLYS LDMYKELYVS AMTSIAFFLA FSILVPFLLP YNFVFMATIA LFAFFAVELL IVVVIRNRLP FDRLWHTGEK PTETDIKLRK WLIISVILVV ILLPFLLWAK YIVGLSPFSQ MPYMILVALG FTPLAIGGFV ALKEEEKVKR KEFVFPDFLR SLGDSVSAKG GGMVSSLEYL SNHDFGPLTH DIKRLYKRLA LGIDSNKSWR LFGFDSCSYL IQLFSDIFSR CIYFGGDPKT AAEIISKNFR KIVQLRKSKY QNIQQFVGVV YGLGGGLALA LFASLGVAKM INDLYSSLSI PETVIHILNI APISNVDVVE YIIFGSLIVY SIISAILIKI MDGGHKFVSL LHFVAILWIC AIVAYITKLI VSQVLGVSVP LY // ID FLPA_METJA Reviewed; 230 AA. AC Q58108; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Fibrillarin-like rRNA/tRNA 2'-O-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00351}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00351}; GN Name=flpA {ECO:0000255|HAMAP-Rule:MF_00351}; OrderedLocusNames=MJ0697; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND MASS SPECTROMETRY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10089444; DOI=10.1107/S0907444998007513; RA Wang H., Yokota H., Kim R., Kim S.-H.; RT "Expression, purification and preliminary X-ray analysis of a RT fibrillarin homolog from Methanococcus jannaschii, a RT hyperthermophile."; RL Acta Crystallogr. D 55:338-340(1999). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS), AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10654930; DOI=10.1093/emboj/19.3.317; RA Wang H., Boisvert D., Kim K.K., Kim R., Kim S.-H.; RT "Crystal structure of a fibrillarin homologue from Methanococcus RT jannaschii, a hyperthermophile, at 1.6-A resolution."; RL EMBO J. 19:317-323(2000). CC -!- FUNCTION: Involved in pre-rRNA and tRNA processing. Utilizes the CC methyl donor S-adenosyl-L-methionine to catalyze the site-specific CC 2'-hydroxyl methylation of ribose moieties in rRNA and tRNA. Site CC specificity is provided by a guide RNA that base pairs with the CC substrate. Methylation occurs at a characteristic distance from CC the sequence involved in base pairing with the guide RNA. CC {ECO:0000255|HAMAP-Rule:MF_00351}. CC -!- SUBUNIT: Interacts with nop5. Component of box C/D small CC ribonucleoprotein (sRNP) particles that contain rpl7ae, FlpA and CC nop5, plus a guide RNA. {ECO:0000255|HAMAP-Rule:MF_00351}. CC -!- MASS SPECTROMETRY: Mass=25971; Method=Electrospray; Range=1-230; CC Evidence={ECO:0000269|PubMed:10089444}; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC Fibrillarin family. {ECO:0000255|HAMAP-Rule:MF_00351}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98690.1; -; Genomic_DNA. DR PIR; A64387; A64387. DR PDB; 1FBN; X-ray; 1.60 A; A=1-230. DR PDB; 1G8S; X-ray; 1.60 A; A=1-230. DR PDBsum; 1FBN; -. DR PDBsum; 1G8S; -. DR ProteinModelPortal; Q58108; -. DR SMR; Q58108; 1-230. DR IntAct; Q58108; 2. DR STRING; 243232.MJ_0697; -. DR EnsemblBacteria; AAB98690; AAB98690; MJ_0697. DR KEGG; mja:MJ_0697; -. DR eggNOG; arCOG00078; Archaea. DR eggNOG; COG1889; LUCA. DR InParanoid; Q58108; -. DR KO; K04795; -. DR OMA; EYREWNL; -. DR PhylomeDB; Q58108; -. DR EvolutionaryTrace; Q58108; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:1990259; F:histone-glutamine methyltransferase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0008649; F:rRNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0000494; P:box C/D snoRNA 3'-end processing; IBA:GO_Central. DR GO; GO:1990258; P:histone glutamine methylation; IBA:GO_Central. DR GO; GO:0031167; P:rRNA methylation; IBA:GO_Central. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00351; RNA_methyltransf_FlpA; 1. DR InterPro; IPR000692; Fibrillarin. DR InterPro; IPR020813; Fibrillarin_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01269; Fibrillarin; 1. DR PIRSF; PIRSF006540; Nop17p; 1. DR PRINTS; PR00052; FIBRILLARIN. DR SMART; SM01206; Fibrillarin; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00566; FIBRILLARIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; RNA-binding; rRNA processing; Transferase; KW tRNA processing. FT CHAIN 1 230 Fibrillarin-like rRNA/tRNA 2'-O- FT methyltransferase. FT /FTId=PRO_0000148533. FT REGION 87 88 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00351}. FT REGION 105 106 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00351}. FT REGION 130 131 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00351}. FT REGION 150 153 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00351}. FT STRAND 5 9 {ECO:0000244|PDB:1FBN}. FT TURN 10 12 {ECO:0000244|PDB:1FBN}. FT STRAND 13 17 {ECO:0000244|PDB:1FBN}. FT STRAND 19 21 {ECO:0000244|PDB:1FBN}. FT STRAND 25 28 {ECO:0000244|PDB:1FBN}. FT STRAND 36 38 {ECO:0000244|PDB:1FBN}. FT STRAND 41 44 {ECO:0000244|PDB:1FBN}. FT STRAND 47 51 {ECO:0000244|PDB:1FBN}. FT TURN 54 56 {ECO:0000244|PDB:1FBN}. FT HELIX 58 64 {ECO:0000244|PDB:1FBN}. FT STRAND 77 82 {ECO:0000244|PDB:1FBN}. FT HELIX 87 95 {ECO:0000244|PDB:1FBN}. FT TURN 96 98 {ECO:0000244|PDB:1FBN}. FT STRAND 99 106 {ECO:0000244|PDB:1FBN}. FT HELIX 108 117 {ECO:0000244|PDB:1FBN}. FT TURN 118 120 {ECO:0000244|PDB:1FBN}. FT STRAND 124 128 {ECO:0000244|PDB:1FBN}. FT HELIX 134 137 {ECO:0000244|PDB:1FBN}. FT TURN 138 140 {ECO:0000244|PDB:1FBN}. FT STRAND 144 149 {ECO:0000244|PDB:1FBN}. FT HELIX 156 167 {ECO:0000244|PDB:1FBN}. FT STRAND 168 179 {ECO:0000244|PDB:1FBN}. FT HELIX 180 182 {ECO:0000244|PDB:1FBN}. FT STRAND 185 187 {ECO:0000244|PDB:1FBN}. FT HELIX 189 203 {ECO:0000244|PDB:1FBN}. FT STRAND 205 212 {ECO:0000244|PDB:1FBN}. FT TURN 214 216 {ECO:0000244|PDB:1FBN}. FT STRAND 220 227 {ECO:0000244|PDB:1FBN}. SQ SEQUENCE 230 AA; 25966 MW; 9ECAAD7C4C606756 CRC64; MEDIKIKEIF ENIYEVDLGD GLKRIATKSI VKGKKVYDEK IIKIGDEEYR IWNPNKSKLA AAIIKGLKVM PIKRDSKILY LGASAGTTPS HVADIADKGI VYAIEYAPRI MRELLDACAE RENIIPILGD ANKPQEYANI VEKVDVIYED VAQPNQAEIL IKNAKWFLKK GGYGMIAIKA RSIDVTKDPK EIFKEQKEIL EAGGFKIVDE VDIEPFEKDH VMFVGIWEGK // ID FRHD_METJA Reviewed; 183 AA. AC Q60339; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Coenzyme F420 hydrogenase subunit delta; DE AltName: Full=Putative coenzyme F420 hydrogenase-processing subunit; GN Name=frhD; OrderedLocusNames=MJ0030; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98009.1; -; Genomic_DNA. DR PIR; F64303; F64303. DR ProteinModelPortal; Q60339; -. DR STRING; 243232.MJ_0030; -. DR EnsemblBacteria; AAB98009; AAB98009; MJ_0030. DR KEGG; mja:MJ_0030; -. DR eggNOG; arCOG04429; Archaea. DR eggNOG; COG0680; LUCA. DR InParanoid; Q60339; -. DR KO; K00442; -. DR OMA; CGNILFA; -. DR PhylomeDB; Q60339; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 3.40.50.1450; -; 1. DR InterPro; IPR004411; Pept_A31_F420-red_hyd_d. DR InterPro; IPR023430; Pept_HybD-like_dom. DR InterPro; IPR000671; Peptidase_A31. DR Pfam; PF01750; HycI; 1. DR PRINTS; PR00446; HYDRGNUPTAKE. DR SUPFAM; SSF53163; SSF53163; 1. DR TIGRFAMs; TIGR00130; frhD; 1. DR TIGRFAMs; TIGR00072; hydrog_prot; 1. PE 3: Inferred from homology; KW Aspartyl protease; Complete proteome; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 183 Coenzyme F420 hydrogenase subunit delta. FT /FTId=PRO_0000201946. SQ SEQUENCE 183 AA; 20628 MW; DD79B2FB9DEFE5A7 CRC64; MNETMKAEIE SQDDELFDLT PSYLKKEIMV LACGNILFAD DGFSVHVIEK LNKILTDKEK QKIALVDAGA GAPQQVLTLI DENSKTKKII VVDVIDWGIK PGEIKIIEKD ELPNPKYHRL DSHDWPLAPL LREVAEKYNI EVKVVGCQAK YISEPDVYIG LSEEVEKAVD KAVEIILREL RGD // ID FEOB_METJA Reviewed; 668 AA. AC Q57986; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Ferrous iron transport protein B homolog; GN OrderedLocusNames=MJ0566; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probable GTP-driven transporter of Fe(2+) ion. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TRAFAC class TrmE-Era-EngA-EngB-Septin- CC like GTPase superfamily. FeoB GTPase (TC 9.A.8) family. CC {ECO:0000255|PROSITE-ProRule:PRU01048}. CC -!- SIMILARITY: Contains 1 FeoB-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01048}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98557.1; -; Genomic_DNA. DR PIR; F64370; F64370. DR PDB; 2WJG; X-ray; 2.20 A; A/B=1-184. DR PDB; 2WJH; X-ray; 2.10 A; A/B=1-165. DR PDB; 2WJI; X-ray; 1.90 A; A/B=1-165. DR PDB; 2WJJ; X-ray; 2.40 A; A/B=1-167. DR PDBsum; 2WJG; -. DR PDBsum; 2WJH; -. DR PDBsum; 2WJI; -. DR PDBsum; 2WJJ; -. DR ProteinModelPortal; Q57986; -. DR STRING; 243232.MJ_0566; -. DR TCDB; 9.A.8.1.9; the ferrous iron uptake (feob) family. DR EnsemblBacteria; AAB98557; AAB98557; MJ_0566. DR KEGG; mja:MJ_0566; -. DR eggNOG; arCOG00359; Archaea. DR eggNOG; COG0370; LUCA. DR InParanoid; Q57986; -. DR KO; K04759; -. DR OMA; RQITIID; -. DR PhylomeDB; Q57986; -. DR EvolutionaryTrace; Q57986; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015093; F:ferrous iron transmembrane transporter activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0055072; P:iron ion homeostasis; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003373; Fe2_transport_prot-B. DR InterPro; IPR011640; Fe2_transport_prot_B_C. DR InterPro; IPR011619; Fe2_transport_prot_B_N. DR InterPro; IPR030389; G_FEOB_dom. DR InterPro; IPR011642; Gate_dom. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR11649:SF37; PTHR11649:SF37; 2. DR Pfam; PF07664; FeoB_C; 1. DR Pfam; PF02421; FeoB_N; 1. DR Pfam; PF07670; Gate; 2. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00437; feoB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51711; G_FEOB; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; GTP-binding; KW Ion transport; Iron; Iron transport; Membrane; Nucleotide-binding; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 668 Ferrous iron transport protein B homolog. FT /FTId=PRO_0000210848. FT TRANSMEM 344 364 Helical. {ECO:0000255}. FT TRANSMEM 386 406 Helical. {ECO:0000255}. FT TRANSMEM 418 438 Helical. {ECO:0000255}. FT TRANSMEM 450 470 Helical. {ECO:0000255}. FT TRANSMEM 515 535 Helical. {ECO:0000255}. FT TRANSMEM 574 594 Helical. {ECO:0000255}. FT TRANSMEM 613 633 Helical. {ECO:0000255}. FT TRANSMEM 643 663 Helical. {ECO:0000255}. FT DOMAIN 3 165 FeoB-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01048}. FT NP_BIND 10 17 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01048}. FT NP_BIND 56 60 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01048}. FT STRAND 3 9 {ECO:0000244|PDB:2WJI}. FT HELIX 16 24 {ECO:0000244|PDB:2WJI}. FT STRAND 29 32 {ECO:0000244|PDB:2WJH}. FT STRAND 42 47 {ECO:0000244|PDB:2WJI}. FT STRAND 50 56 {ECO:0000244|PDB:2WJI}. FT STRAND 63 67 {ECO:0000244|PDB:2WJI}. FT HELIX 68 80 {ECO:0000244|PDB:2WJI}. FT STRAND 83 90 {ECO:0000244|PDB:2WJI}. FT HELIX 91 93 {ECO:0000244|PDB:2WJG}. FT HELIX 94 106 {ECO:0000244|PDB:2WJI}. FT STRAND 111 116 {ECO:0000244|PDB:2WJI}. FT HELIX 118 123 {ECO:0000244|PDB:2WJI}. FT HELIX 130 137 {ECO:0000244|PDB:2WJI}. FT STRAND 141 143 {ECO:0000244|PDB:2WJI}. FT HELIX 146 148 {ECO:0000244|PDB:2WJI}. FT HELIX 152 162 {ECO:0000244|PDB:2WJI}. FT HELIX 163 166 {ECO:0000244|PDB:2WJJ}. SQ SEQUENCE 668 AA; 74455 MW; 2145495E1150C19E CRC64; MKSYEIALIG NPNVGKSTIF NALTGENVYI GNWPGVTVEK KEGEFEYNGE KFKVVDLPGV YSLTANSIDE IIARDYIINE KPDLVVNIVD ATALERNLYL TLQLMEMGAN LLLALNKMDL AKSLGIEIDV DKLEKILGVK VVPLSAAKKM GIEDLKKAIS IAVKDKKTAE IKYPNFEPYI KKITSILQKD EDLKKYNLRY LAIKLLENDK YVEEIVKNSK VWNELKPVLD SIINELSKKY GEAELGIVEE RYKVIDKIVK EVMKKTSGKL TTTEMLDDVL TDEKIGTLLI IPFLWMLFKF TFDVSKPFSA MIEYFFGFLS EVVKSSISNK FIASLLADGI ISGVGAVLVF FPILAFLFFA ISFLEDSGYM ARIPFITDRI MNKFGLPGKA VISMVMGFGC NVPAIMATRT IEDEKDRILT ILINPLLSCS ARLPIYALFA GALFSKYQGV VILSMYALGV VLALITAFLF RKLIFKTSPS YLIVELPPYH IPHLNVVLKN TWERVYDFLR KAGTIIVFGV ILVWVLSVYG PSGYLGEEVF ENPQLIANSW VAVIGKTLAP LFSPMGWDWR ACSALVFGII AKEVVVGSLA MLYGTGEENL SSVIAHAFSP VSAYAFMAFS LIYLPCIATL AVIKQEIGWK WALFAVTYEM ILAYVVALVI SVIGNLLF // ID FLAB1_METJA Reviewed; 217 AA. AC Q58301; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Flagellin B1; DE Flags: Precursor; GN Name=flaB1; OrderedLocusNames=MJ0891; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to CC form the filaments of archaeal flagella. CC -!- SUBCELLULAR LOCATION: Archaeal flagellum. CC -!- SIMILARITY: Belongs to the archaeal flagellin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98894.1; -; Genomic_DNA. DR PIR; C64411; C64411. DR ProteinModelPortal; Q58301; -. DR STRING; 243232.MJ_0891; -. DR EnsemblBacteria; AAB98894; AAB98894; MJ_0891. DR KEGG; mja:MJ_0891; -. DR eggNOG; arCOG01829; Archaea. DR eggNOG; COG1681; LUCA. DR InParanoid; Q58301; -. DR KO; K07325; -. DR OMA; DNAVINK; -. DR PhylomeDB; Q58301; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR InterPro; IPR013373; Flagellin/pilin_N. DR InterPro; IPR002774; Flagellin_arc. DR Pfam; PF01917; Arch_flagellin; 1. DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1. PE 3: Inferred from homology; KW Archaeal flagellum; Complete proteome; Reference proteome. FT PROPEP 1 12 {ECO:0000250}. FT /FTId=PRO_0000009373. FT CHAIN 13 217 Flagellin B1. FT /FTId=PRO_0000009374. SQ SEQUENCE 217 AA; 22700 MW; 4374437380061565 CRC64; MKVFEFLKGK RGAMGIGTLI IFIAMVLVAA VAAAVLINTS GFLQQKAMAT GKESTEQVAS GLMCIGVTGH YDKTLGGIDK LAIYITPNAG SAPIDLKNAK LFLIYDGESH VLNYSTVTTA TLGADDIFNS SAITDWSLAD SSSYVVGVIQ DADGSLSNGV INKGDIAVLL VNANAVFNKA IPTRSEVSGQ FQPEFGAPAV IQFTTPAAYT QTVIELQ // ID FLAC_METJA Reviewed; 141 AA. AC Q58304; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Putative flagella-related protein C; GN Name=flaC; OrderedLocusNames=MJ0894; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaC. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98897.1; -; Genomic_DNA. DR PIR; F64411; F64411. DR ProteinModelPortal; Q58304; -. DR STRING; 243232.MJ_0894; -. DR EnsemblBacteria; AAB98897; AAB98897; MJ_0894. DR KEGG; mja:MJ_0894; -. DR eggNOG; arCOG05119; Archaea. DR eggNOG; COG3352; LUCA. DR InParanoid; Q58304; -. DR KO; K07822; -. DR OMA; VMMLYEV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR InterPro; IPR009205; FlaC_arc. DR Pfam; PF05377; FlaC_arch; 1. DR PIRSF; PIRSF018660; Archl_flaC; 1. PE 4: Predicted; KW Archaeal flagellum; Complete proteome; Reference proteome. FT CHAIN 1 141 Putative flagella-related protein C. FT /FTId=PRO_0000087267. SQ SEQUENCE 141 AA; 16244 MW; A634B2A299355FA2 CRC64; METTEGLLAK VNDIESKLPK LESSINNLRK ENEMLRVELN KINENLQDIM ALYEVVSNQI NPFIGVSKIT ATSLEKLERL ETEYKRLKKT VEELTNDLII LGSLYLHQLD INLDEIIEEV LEEEIIKSMS GEDTHDTKDN K // ID FTR_METJA Reviewed; 301 AA. AC Q57766; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Formylmethanofuran--tetrahydromethanopterin formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579}; DE EC=2.3.1.101 {ECO:0000255|HAMAP-Rule:MF_00579}; DE AltName: Full=H4MPT formyltransferase {ECO:0000255|HAMAP-Rule:MF_00579}; GN Name=ftr {ECO:0000255|HAMAP-Rule:MF_00579}; OrderedLocusNames=MJ0318; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible transfer of a formyl group from CC formylmethanofuran (formyl-MFR) to tetrahydromethanopterin CC (H(4)MPT) so as to produce 5-formyl tetrahydromethanopterin (5- CC formyl-H(4)MPT) and methanofuran (MFR). {ECO:0000255|HAMAP- CC Rule:MF_00579}. CC -!- CATALYTIC ACTIVITY: Formylmethanofuran + 5,6,7,8- CC tetrahydromethanopterin = methanofuran + 5-formyl-5,6,7,8- CC tetrahydromethanopterin. {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 2/3. CC {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00579}. CC -!- SIMILARITY: Belongs to the FTR family. {ECO:0000255|HAMAP- CC Rule:MF_00579}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98303.1; -; Genomic_DNA. DR PIR; G64339; G64339. DR ProteinModelPortal; Q57766; -. DR SMR; Q57766; 1-300. DR STRING; 243232.MJ_0318; -. DR EnsemblBacteria; AAB98303; AAB98303; MJ_0318. DR KEGG; mja:MJ_0318; -. DR eggNOG; arCOG02695; Archaea. DR eggNOG; COG2037; LUCA. DR InParanoid; Q57766; -. DR KO; K00672; -. DR OMA; SVIMCPA; -. DR PhylomeDB; Q57766; -. DR UniPathway; UPA00640; UER00693. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030270; F:formylmethanofuran-tetrahydromethanopterin N-formyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.520; -; 2. DR HAMAP; MF_00579; FTR; 1. DR InterPro; IPR014053; ForMFR_H4MPT_ForTrfase. DR InterPro; IPR002770; ForMFR_H4MPT_ForTrfase_C. DR InterPro; IPR023447; ForMFR_H4MPT_ForTrfase_fd-like. DR InterPro; IPR022667; ForMFR_H4MPT_ForTrfase_N. DR Pfam; PF01913; FTR; 1. DR Pfam; PF02741; FTR_C; 1. DR PIRSF; PIRSF006414; Ftr_formyl_trnsf; 1. DR SUPFAM; SSF55112; SSF55112; 2. DR TIGRFAMs; TIGR03119; one_C_fhcD; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Methanogenesis; KW One-carbon metabolism; Reference proteome; Transferase. FT CHAIN 1 301 Formylmethanofuran-- FT tetrahydromethanopterin FT formyltransferase. FT /FTId=PRO_0000138119. SQ SEQUENCE 301 AA; 32445 MW; 28207E48812B0296 CRC64; MEINGVYIED TFAEAFPIWV SRVLITAATK KWAKIAATEA TGFGCSVIMC PAEAGIEKYV PPSKTPDGRP GFIIQICHPK KSELEHQMLE RLGQCVLTCP TTAIFDAMGD MADEQLKVGF KLKFFGDGYE KKDELYGRKV YKIPIMGGEF ITEAKFGIKK GVAGGNFFIM ADTNASALIA AEAAVNAIAS VDGVITPFPG GVVASGSKVG ASNPKYKFMV ATTNHKMCPT LKGVVEDSEI PEDVNGVYEI VIDGVDEESV KEAMKQGILA ATRVKGVKKI TAGNYGGKLG KYQFNLRELF E // ID FTSY_METJA Reviewed; 409 AA. AC Q57739; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Signal recognition particle receptor FtsY {ECO:0000255|HAMAP-Rule:MF_00920}; DE Short=SRP receptor {ECO:0000255|HAMAP-Rule:MF_00920}; GN Name=ftsY {ECO:0000255|HAMAP-Rule:MF_00920}; OrderedLocusNames=MJ0291; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Acts as a receptor for the CC complex formed by the signal recognition particle (SRP) and the CC ribosome-nascent chain (RNC). {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Peripheral membrane protein; CC Cytoplasmic side. Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00920}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. FtsY subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00920}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98276.1; -; Genomic_DNA. DR PIR; D64336; D64336. DR ProteinModelPortal; Q57739; -. DR STRING; 243232.MJ_0291; -. DR EnsemblBacteria; AAB98276; AAB98276; MJ_0291. DR KEGG; mja:MJ_0291; -. DR eggNOG; arCOG01227; Archaea. DR eggNOG; COG0552; LUCA. DR InParanoid; Q57739; -. DR KO; K03110; -. DR OMA; KPTVIVF; -. DR PhylomeDB; Q57739; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031226; C:intrinsic component of plasma membrane; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00920; FtsY; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004390; SR_rcpt_FtsY. DR InterPro; IPR000897; SRP54_GTPase_dom. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00064; ftsY; 1. DR PROSITE; PS00300; SRP54; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Cytoplasm; GTP-binding; Membrane; KW Nucleotide-binding; Receptor; Reference proteome. FT CHAIN 1 409 Signal recognition particle receptor FT FtsY. FT /FTId=PRO_0000101218. FT NP_BIND 209 216 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 291 295 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. FT NP_BIND 349 352 GTP. {ECO:0000255|HAMAP-Rule:MF_00920}. SQ SEQUENCE 409 AA; 45755 MW; 4FBCFF8290693EEC CRC64; MFGKLKEKLL ETASKITEKI YSKGEAEEVK EEKEEKSKIS FTSLFKKEPK KEEVKKEKAE EEIKKSEIVK TEPSEKVEEA KEEIKEIKEE KEEKKITFFD RFGLTRAIKK VLKKEVVILE EDIEDVLEEL EIALLEADVA LEVVEKLIEN IKNELVGRKI SPDDNVEEIT INAVKNAIKN ILSQEKIDIE EIIKKNKAEG KPTVIVFVGI NGTGKTTTIA KLAYKLKQKG YSVVLAAGDT FRAGAIEQLE QHAKNVGVKV IKHKPGADSA AVIYDAIQHA KARGIDVVLA DTAGRQATNV NLMEEIKKVV RVTKPDLVIF VGDALTGNDA VYQAEEFNRA VNIDGIILTK VDADAKGGAA LSIGYAIGKP ILYLGVGQRY QDLIEFDADW MVRKLFGEEE FEFSTEREF // ID FEN_METJA Reviewed; 326 AA. AC Q58839; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Flap endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614}; DE Short=FEN-1 {ECO:0000255|HAMAP-Rule:MF_00614}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00614}; DE AltName: Full=Flap structure-specific endonuclease 1 {ECO:0000255|HAMAP-Rule:MF_00614}; GN Name=fen {ECO:0000255|HAMAP-Rule:MF_00614}; OrderedLocusNames=MJ1444; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=9765572; RA Rao H.G., Rosenfeld A., Wetmur J.G.; RT "Methanococcus jannaschii flap endonuclease: expression, purification, RT and substrate requirements."; RL J. Bacteriol. 180:5406-5412(1998). RN [3] RP CHARACTERIZATION, AND X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10102570; RA Bae K.W., Baek K.W., Cho C.S., Hwang K.Y., Kim H.-R., Sung H.-C., RA Cho Y.; RT "Expression, purification, characterization and crystallization of RT flap endonuclease-1 from Methanococcus jannaschii."; RL Mol. Cells 9:45-48(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9699635; DOI=10.1038/1406; RA Hwang K.Y., Baek K., Kim H.-Y., Cho Y.; RT "The crystal structure of flap endonuclease-1 from Methanococcus RT jannaschii."; RL Nat. Struct. Biol. 5:707-713(1998). CC -!- FUNCTION: Structure-specific nuclease with 5'-flap endonuclease CC and 5'-3' exonuclease activities involved in DNA replication and CC repair. During DNA replication, cleaves the 5'-overhanging flap CC structure that is generated by displacement synthesis when DNA CC polymerase encounters the 5'-end of a downstream Okazaki fragment. CC Binds the unpaired 3'-DNA end and kinks the DNA to facilitate 5' CC cleavage specificity. Cleaves one nucleotide into the double- CC stranded DNA from the junction in flap DNA, leaving a nick for CC ligation. Also involved in the base excision repair (BER) pathway. CC Acts as a genome stabilization factor that prevents flaps from CC equilibrating into structures that lead to duplications and CC deletions. Also possesses 5'-3' exonuclease activity on nicked or CC gapped double-stranded DNA. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00614}; CC Note=Binds 2 magnesium ions per subunit. They probably participate CC in the reaction catalyzed by the enzyme. May bind an additional CC third magnesium ion after substrate binding. {ECO:0000255|HAMAP- CC Rule:MF_00614}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6-7.; CC -!- SUBUNIT: Interacts with PCNA. PCNA stimulates the nuclease CC activity without altering cleavage specificity. CC -!- SIMILARITY: Belongs to the XPG/RAD2 endonuclease family. FEN1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00614}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99454.1; -; Genomic_DNA. DR PIR; C64480; C64480. DR PDB; 1A76; X-ray; 2.00 A; A=1-326. DR PDB; 1A77; X-ray; 2.00 A; A=1-326. DR PDBsum; 1A76; -. DR PDBsum; 1A77; -. DR ProteinModelPortal; Q58839; -. DR SMR; Q58839; 2-316. DR STRING; 243232.MJ_1444; -. DR EnsemblBacteria; AAB99454; AAB99454; MJ_1444. DR KEGG; mja:MJ_1444; -. DR eggNOG; arCOG04050; Archaea. DR eggNOG; COG0258; LUCA. DR InParanoid; Q58839; -. DR KO; K04799; -. DR OMA; GSQDYDS; -. DR PhylomeDB; Q58839; -. DR BRENDA; 3.1.99.B1; 3260. DR EvolutionaryTrace; Q58839; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008409; F:5'-3' exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0017108; F:5'-flap endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00614; Fen; 1. DR InterPro; IPR020045; 5-3_exonuclease_C. DR InterPro; IPR023426; Flap_endonuc. DR InterPro; IPR019973; Flap_structure-sp_endonuc_arc. DR InterPro; IPR008918; HhH2. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR006086; XPG-I_dom. DR InterPro; IPR006084; XPG/Rad2. DR InterPro; IPR006085; XPG_DNA_repair_N. DR PANTHER; PTHR11081; PTHR11081; 1. DR Pfam; PF00867; XPG_I; 1. DR Pfam; PF00752; XPG_N; 1. DR PRINTS; PR00853; XPGRADSUPER. DR SMART; SM00279; HhH2; 1. DR SMART; SM00484; XPGI; 1. DR SMART; SM00485; XPGN; 1. DR SUPFAM; SSF47807; SSF47807; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR TIGRFAMs; TIGR03674; fen_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; KW DNA replication; Endonuclease; Exonuclease; Hydrolase; Magnesium; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 326 Flap endonuclease 1. FT /FTId=PRO_0000154053. FT REGION 1 98 N-domain. FT REGION 116 245 I-domain. FT REGION 317 325 Interaction with PCNA. FT {ECO:0000255|HAMAP-Rule:MF_00614}. FT METAL 27 27 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00614}. FT METAL 80 80 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00614}. FT METAL 152 152 Magnesium 1. FT METAL 154 154 Magnesium 1. FT METAL 173 173 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00614}. FT METAL 175 175 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00614}. FT METAL 224 224 Magnesium 2. FT HELIX 6 8 {ECO:0000244|PDB:1A76}. FT HELIX 17 19 {ECO:0000244|PDB:1A76}. FT STRAND 23 27 {ECO:0000244|PDB:1A76}. FT HELIX 28 38 {ECO:0000244|PDB:1A76}. FT HELIX 56 70 {ECO:0000244|PDB:1A76}. FT STRAND 74 79 {ECO:0000244|PDB:1A76}. FT STRAND 96 98 {ECO:0000244|PDB:1A76}. FT HELIX 111 115 {ECO:0000244|PDB:1A76}. FT HELIX 121 124 {ECO:0000244|PDB:1A76}. FT HELIX 129 142 {ECO:0000244|PDB:1A76}. FT STRAND 146 148 {ECO:0000244|PDB:1A76}. FT HELIX 153 162 {ECO:0000244|PDB:1A76}. FT STRAND 165 170 {ECO:0000244|PDB:1A76}. FT STRAND 172 174 {ECO:0000244|PDB:1A76}. FT HELIX 175 179 {ECO:0000244|PDB:1A76}. FT STRAND 182 190 {ECO:0000244|PDB:1A76}. FT STRAND 196 199 {ECO:0000244|PDB:1A76}. FT HELIX 200 207 {ECO:0000244|PDB:1A76}. FT HELIX 211 221 {ECO:0000244|PDB:1A76}. FT TURN 227 232 {ECO:0000244|PDB:1A76}. FT HELIX 235 243 {ECO:0000244|PDB:1A76}. FT HELIX 247 254 {ECO:0000244|PDB:1A76}. FT HELIX 258 266 {ECO:0000244|PDB:1A76}. FT HELIX 283 290 {ECO:0000244|PDB:1A76}. FT TURN 291 294 {ECO:0000244|PDB:1A76}. FT HELIX 298 315 {ECO:0000244|PDB:1A76}. SQ SEQUENCE 326 AA; 37527 MW; 311427F2B4B67580 CRC64; MGVQFGDFIP KNIISFEDLK GKKVAIDGMN ALYQFLTSIR LRDGSPLRNR KGEITSAYNG VFYKTIHLLE NDITPIWVFD GEPPKLKEKT RKVRREMKEK AELKMKEAIK KEDFEEAAKY AKRVSYLTPK MVENCKYLLS LMGIPYVEAP SEGEAQASYM AKKGDVWAVV SQDYDALLYG APRVVRNLTT TKEMPELIEL NEVLEDLRIS LDDLIDIAIF MGTDYNPGGV KGIGFKRAYE LVRSGVAKDV LKKEVEYYDE IKRIFKEPKV TDNYSLSLKL PDKEGIIKFL VDENDFNYDR VKKHVDKLYN LIANKTKQKT LDAWFK // ID FER2_METJA Reviewed; 131 AA. AC Q57563; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized ferredoxin MJ0099; GN OrderedLocusNames=MJ0099; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98079.1; -; Genomic_DNA. DR PIR; C64312; C64312. DR ProteinModelPortal; Q57563; -. DR STRING; 243232.MJ_0099; -. DR EnsemblBacteria; AAB98079; AAB98079; MJ_0099. DR KEGG; mja:MJ_0099; -. DR eggNOG; arCOG02460; Archaea. DR eggNOG; ENOG4111S1Q; LUCA. DR InParanoid; Q57563; -. DR OMA; TGVCPTE; -. DR PhylomeDB; Q57563; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR018449; NIL_domain. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF09383; NIL; 1. DR SMART; SM00930; NIL; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 131 Uncharacterized ferredoxin MJ0099. FT /FTId=PRO_0000159130. FT DOMAIN 73 102 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 103 131 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 82 82 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 85 85 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 88 88 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 92 92 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 112 112 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 115 115 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 118 118 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 122 122 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 131 AA; 15105 MW; BDE45A4CD055B78E CRC64; MRKRVYYWTD SEHINKPVIS DTILNTGVKI NILKAKVEPQ EAFLILELFG SKETIEKALN YLSKFGEVEE ISKVIKRDLE KCVHCGCCIT QCPINVIYMD EDYNVVFKEE DCVGCKNCLK ACPFKAIEIF E // ID FER6_METJA Reviewed; 58 AA. AC Q58041; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized ferredoxin MJ0624; GN OrderedLocusNames=MJ0624; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Ferredoxins are iron-sulfur proteins that transfer CC electrons probably in the CO-dehydrogenase complex. {ECO:0000250}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98619.1; -; Genomic_DNA. DR PIR; H64377; H64377. DR ProteinModelPortal; Q58041; -. DR STRING; 243232.MJ_0624; -. DR EnsemblBacteria; AAB98619; AAB98619; MJ_0624. DR KEGG; mja:MJ_0624; -. DR eggNOG; arCOG02060; Archaea. DR eggNOG; ENOG410Y01Y; LUCA. DR InParanoid; Q58041; -. DR OMA; CAVCKDY; -. DR PhylomeDB; Q58041; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 58 Uncharacterized ferredoxin MJ0624. FT /FTId=PRO_0000159134. FT DOMAIN 2 27 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 28 57 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 9 9 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 12 12 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 15 15 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 37 37 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 40 40 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 43 43 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 47 47 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 58 AA; 6256 MW; 27057B367F75BE37 CRC64; MGIKILEKCV GCGNCVVFCP RRAIKTYGVA IVDENKCSNC GICARYCPIN AIKVDTSL // ID FER9_METJA Reviewed; 166 AA. AC Q57713; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 17-FEB-2016, entry version 96. DE RecName: Full=Uncharacterized ferredoxin MJ0265; GN OrderedLocusNames=MJ0265; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98252.1; -; Genomic_DNA. DR ProteinModelPortal; Q57713; -. DR STRING; 243232.MJ_0265; -. DR EnsemblBacteria; AAB98252; AAB98252; MJ_0265. DR KEGG; mja:MJ_0265; -. DR eggNOG; arCOG01502; Archaea. DR eggNOG; COG1142; LUCA. DR InParanoid; Q57713; -. DR KO; K00196; -. DR OMA; SCAMDAN; -. DR PhylomeDB; Q57713; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF13247; Fer4_11; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 3. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 166 Uncharacterized ferredoxin MJ0265. FT /FTId=PRO_0000159137. FT DOMAIN 3 33 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 37 67 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 68 97 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 13 13 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 16 16 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 23 23 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 46 46 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 49 49 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 54 54 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 58 58 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 77 77 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 80 80 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 83 83 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 87 87 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 101 101 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 104 104 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 111 111 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 115 115 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 166 AA; 18229 MW; 9173A1857002D7F6 CRC64; MVMKKIIMTN FNCDNCGDCV KACMEKNKVG RIAIMEKDGK YIPIVCQHCA SAPCKEVCPV SAIEHKDGYV YLNEDVCIGC GLCALACPFG AILMEDKAYK CILCNGDEPA CVKACSKRCL ELVDVNELIF AKRDKSLDLF SKMSLPTQKS DNSLISKITI DAKVKP // ID FLAE_METJA Reviewed; 140 AA. AC Q58306; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Putative flagella-related protein E; GN Name=flaE; OrderedLocusNames=MJ0896; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Archaeal flagellum {ECO:0000305}. CC -!- SIMILARITY: To M.voltae FlaE, also to FlaD. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98899.1; -; Genomic_DNA. DR PIR; H64411; H64411. DR STRING; 243232.MJ_0896; -. DR EnsemblBacteria; AAB98899; AAB98899; MJ_0896. DR KEGG; mja:MJ_0896; -. DR eggNOG; arCOG02964; Archaea. DR eggNOG; COG3351; LUCA. DR InParanoid; Q58306; -. DR KO; K07328; -. DR OMA; YMLGWLG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0097588; P:archaeal or bacterial-type flagellum-dependent cell motility; IEA:InterPro. DR InterPro; IPR006752; Arch_fla_DE. DR Pfam; PF04659; Arch_fla_DE; 1. DR ProDom; PD012942; Arch_fla_DE; 1. PE 4: Predicted; KW Archaeal flagellum; Complete proteome; Reference proteome. FT CHAIN 1 140 Putative flagella-related protein E. FT /FTId=PRO_0000087271. SQ SEQUENCE 140 AA; 15892 MW; 2CF9E580E9D09146 CRC64; MGEVFKMDGL ASTILEVHKP AKLEDIPDED PIAIILALKW LEYLCERAGV ENVSDILDFY YMLGWLGDKA LAKLLKFLKG IKVDEENVVE GSGKLNITDH IISLLFIERL NGKKISAELL DKIEWELRKI KKGAEQFYGI // ID FTSZ1_METJA Reviewed; 364 AA. AC Q57816; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 113. DE RecName: Full=Cell division protein FtsZ 1 {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ1 {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=MJ0370; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=9428770; DOI=10.1038/34472; RA Loewe J., Amos L.A.; RT "Crystal structure of the bacterial cell-division protein ftsZ."; RL Nature 391:203-206(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 23-356. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10049809; DOI=10.1006/jsbi.1998.4041; RA Loewe J.; RT "Crystal structure determination of FtsZ from Methanococcus RT jannaschii."; RL J. Struct. Biol. 124:235-243(1998). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH GTP, AND RP SUBUNIT. RX PubMed=15558053; DOI=10.1038/nsmb855; RA Oliva M.A., Cordell S.C., Lowe J.; RT "Structural insights into FtsZ protofilament formation."; RL Nat. Struct. Mol. Biol. 11:1243-1250(2004). RN [5] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) IN COMPLEX WITH GDP. RX PubMed=17900614; DOI=10.1016/j.jmb.2007.08.056; RA Oliva M.A., Trambaiolo D., Lowe J.; RT "Structural insights into the conformational variability of FtsZ."; RL J. Mol. Biol. 373:1229-1242(2007). CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SUBUNIT: Homodimer (PubMed:15558053). Polymerizes to form a CC dynamic ring structure in a strictly GTP-dependent manner. CC Interacts directly with several other division proteins (By CC similarity). {ECO:0000255|HAMAP-Rule:MF_00909, CC ECO:0000269|PubMed:15558053}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98359.1; -; Genomic_DNA. DR PIR; B64346; B64346. DR PDB; 1FSZ; X-ray; 2.80 A; A=1-364. DR PDB; 1W58; X-ray; 2.50 A; 1=1-364. DR PDB; 1W59; X-ray; 2.70 A; A/B=1-364. DR PDB; 1W5A; X-ray; 2.40 A; A/B=1-364. DR PDB; 1W5B; X-ray; 2.20 A; A/B=1-364. DR PDB; 1W5E; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I=1-364. DR PDB; 2VAP; X-ray; 1.70 A; A=1-364. DR PDBsum; 1FSZ; -. DR PDBsum; 1W58; -. DR PDBsum; 1W59; -. DR PDBsum; 1W5A; -. DR PDBsum; 1W5B; -. DR PDBsum; 1W5E; -. DR PDBsum; 2VAP; -. DR ProteinModelPortal; Q57816; -. DR SMR; Q57816; 22-364. DR STRING; 243232.MJ_0370; -. DR EnsemblBacteria; AAB98359; AAB98359; MJ_0370. DR KEGG; mja:MJ_0370; -. DR eggNOG; arCOG02201; Archaea. DR eggNOG; COG0206; LUCA. DR InParanoid; Q57816; -. DR KO; K03531; -. DR OMA; GMAMMGI; -. DR PhylomeDB; Q57816; -. DR BRENDA; 3.6.5.6; 3260. DR EvolutionaryTrace; Q57816; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell cycle; Cell division; Complete proteome; Cytoplasm; KW GTP-binding; Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 364 Cell division protein FtsZ 1. FT /FTId=PRO_0000114401. FT NP_BIND 47 48 GTP. {ECO:0000269|PubMed:15558053, FT ECO:0000269|PubMed:17900614, FT ECO:0000269|PubMed:9428770}. FT NP_BIND 97 99 GTP. {ECO:0000269|PubMed:15558053}. FT NP_BIND 134 136 GTP. {ECO:0000255|HAMAP-Rule:MF_00909, FT ECO:0000269|PubMed:15558053, FT ECO:0000269|PubMed:17900614, FT ECO:0000269|PubMed:9428770}. FT BINDING 165 165 GTP. {ECO:0000255|HAMAP-Rule:MF_00909, FT ECO:0000269|PubMed:15558053, FT ECO:0000269|PubMed:17900614, FT ECO:0000269|PubMed:9428770}. FT BINDING 169 169 GTP. {ECO:0000255|HAMAP-Rule:MF_00909, FT ECO:0000269|PubMed:15558053, FT ECO:0000269|PubMed:9428770}. FT BINDING 212 212 GTP. {ECO:0000255|HAMAP-Rule:MF_00909, FT ECO:0000269|PubMed:15558053, FT ECO:0000269|PubMed:17900614, FT ECO:0000269|PubMed:9428770}. FT HELIX 4 16 {ECO:0000244|PDB:1W59}. FT HELIX 24 34 {ECO:0000244|PDB:2VAP}. FT STRAND 40 45 {ECO:0000244|PDB:2VAP}. FT HELIX 46 59 {ECO:0000244|PDB:2VAP}. FT STRAND 64 72 {ECO:0000244|PDB:2VAP}. FT HELIX 73 77 {ECO:0000244|PDB:2VAP}. FT STRAND 82 86 {ECO:0000244|PDB:2VAP}. FT TURN 89 91 {ECO:0000244|PDB:2VAP}. FT STRAND 93 95 {ECO:0000244|PDB:1W59}. FT HELIX 101 110 {ECO:0000244|PDB:2VAP}. FT HELIX 112 119 {ECO:0000244|PDB:2VAP}. FT STRAND 123 130 {ECO:0000244|PDB:2VAP}. FT HELIX 135 149 {ECO:0000244|PDB:2VAP}. FT STRAND 153 160 {ECO:0000244|PDB:2VAP}. FT HELIX 163 165 {ECO:0000244|PDB:2VAP}. FT HELIX 167 181 {ECO:0000244|PDB:2VAP}. FT STRAND 185 191 {ECO:0000244|PDB:2VAP}. FT HELIX 192 194 {ECO:0000244|PDB:2VAP}. FT HELIX 195 198 {ECO:0000244|PDB:2VAP}. FT STRAND 199 201 {ECO:0000244|PDB:1W58}. FT HELIX 204 227 {ECO:0000244|PDB:2VAP}. FT HELIX 236 243 {ECO:0000244|PDB:2VAP}. FT STRAND 247 256 {ECO:0000244|PDB:2VAP}. FT STRAND 258 260 {ECO:0000244|PDB:1W58}. FT HELIX 261 270 {ECO:0000244|PDB:2VAP}. FT HELIX 279 281 {ECO:0000244|PDB:2VAP}. FT STRAND 284 291 {ECO:0000244|PDB:2VAP}. FT HELIX 297 310 {ECO:0000244|PDB:2VAP}. FT STRAND 316 323 {ECO:0000244|PDB:2VAP}. FT TURN 326 329 {ECO:0000244|PDB:1W5B}. FT STRAND 331 338 {ECO:0000244|PDB:2VAP}. FT HELIX 341 343 {ECO:0000244|PDB:2VAP}. FT STRAND 344 347 {ECO:0000244|PDB:2VAP}. FT STRAND 350 353 {ECO:0000244|PDB:2VAP}. SQ SEQUENCE 364 AA; 38924 MW; 3BB386A5D2FCA107 CRC64; MKFLKNVLEE GSKLEEFNEL ELSPEDKELL EYLQQTKAKI TVVGCGGAGN NTITRLKMEG IEGAKTVAIN TDAQQLIRTK ADKKILIGKK LTRGLGAGGN PKIGEEAAKE SAEEIKAAIQ DSDMVFITCG LGGGTGTGSA PVVAEISKKI GALTVAVVTL PFVMEGKVRM KNAMEGLERL KQHTDTLVVI PNEKLFEIVP NMPLKLAFKV ADEVLINAVK GLVELITKDG LINVDFADVK AVMNNGGLAM IGIGESDSEK RAKEAVSMAL NSPLLDVDID GATGALIHVM GPEDLTLEEA REVVATVSSR LDPNATIIWG ATIDENLENT VRVLLVITGV QSRIEFTDTG LKRKKLELTG IPKI // ID FWDE_METJA Reviewed; 146 AA. AC Q58565; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Ferredoxin-type protein FwdE; GN Name=fwdE; OrderedLocusNames=MJ1165; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99167.1; -; Genomic_DNA. DR PIR; D64445; D64445. DR ProteinModelPortal; Q58565; -. DR STRING; 243232.MJ_1165; -. DR EnsemblBacteria; AAB99167; AAB99167; MJ_1165. DR KEGG; mja:MJ_1165; -. DR eggNOG; arCOG04891; Archaea. DR eggNOG; COG1146; LUCA. DR KO; K00204; -. DR OMA; KAIVAMK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF00037; Fer4; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1 146 Ferredoxin-type protein FwdE. FT /FTId=PRO_0000159139. FT DOMAIN 90 115 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 116 145 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 125 125 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 128 128 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 131 131 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 135 135 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 146 AA; 16403 MW; 5BB26ED1CB2FDADD CRC64; MPEHILSGIK AIVAMKLRRK GLLQKEIAKI IKSDRSIVSH YLSGRYPKEK ILNVAKIIEE MPPQYGAKFI HSLTDNKELA KNLIKELYGI KLFWDENSCI ACGSCLGCAA LTLDNFTVGI DEDTCHLCAS CIFRCPTNSL KFIKEE // ID FWDF_METJA Reviewed; 355 AA. AC Q58566; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Polyferredoxin protein FwdF; GN Name=fwdF; OrderedLocusNames=MJ1166; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 8 [4Fe-4S] clusters. {ECO:0000305}; CC -!- SIMILARITY: Contains 8 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99168.1; -; Genomic_DNA. DR PIR; E64445; E64445. DR ProteinModelPortal; Q58566; -. DR STRING; 243232.MJ_1166; -. DR EnsemblBacteria; AAB99168; AAB99168; MJ_1166. DR KEGG; mja:MJ_1166; -. DR eggNOG; arCOG02180; Archaea. DR eggNOG; ENOG410ZN2K; LUCA. DR InParanoid; Q58566; -. DR KO; K00205; -. DR OMA; CVTCGWC; -. DR PhylomeDB; Q58566; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR016459; Formylmethanofuran_DH_fsu. DR Pfam; PF00037; Fer4; 2. DR Pfam; PF13237; Fer4_10; 1. DR Pfam; PF12838; Fer4_7; 2. DR PIRSF; PIRSF005658; FwdF; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 8. DR PROSITE; PS51379; 4FE4S_FER_2; 8. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1 355 Polyferredoxin protein FwdF. FT /FTId=PRO_0000159140. FT DOMAIN 24 53 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 64 93 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 108 137 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 147 176 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 187 216 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 235 264 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 267 296 4Fe-4S ferredoxin-type 7. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 304 333 4Fe-4S ferredoxin-type 8. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 33 33 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 36 36 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 39 39 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 43 43 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 73 73 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 76 76 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 79 79 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 117 117 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 120 120 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 123 123 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 127 127 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 156 156 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 159 159 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 162 162 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 166 166 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 196 196 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 199 199 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 202 202 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 206 206 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 244 244 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 247 247 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 250 250 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 254 254 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 276 276 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 279 279 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 282 282 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 286 286 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 313 313 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 316 316 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 319 319 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 323 323 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 355 AA; 39343 MW; 15EACA0A9B3B02EB CRC64; MIEQIKEVYE NGFTIYRDGE VEKRELCWND ELCVGCGICA DICPVNAIAM GPLGAIAKGD IIAPKLDIDK DVCVLCGMCA SACPFDALDL KINGKSIKED ERYPKIKRDI KVYQDKCVLC EQCEMVCPQG AIVVERELAE REKFVIGEIN INKEKCVLCG ICAEYCPADA INLKYNYPTP SNPKPITDIE VDKDKCVFCK VCEFVCPHDA IEVICYKCPM MKRIPQAKLY EDITGKTVID KDACVTCGWC AFICPAEAIE VEKPFKGELI IDVNACNACG ACISICPCSA LEFPKPKDKA EKVPRIIVNQ NLCVLCGACA KACPVNAIKV KRTEINFERE PKAIAWKEAF KKLMG // ID FPRA_METJA Reviewed; 416 AA. AC Q58158; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Type A flavoprotein FprA; DE EC=1.-.-.-; DE AltName: Full=FMN protein FprA; DE AltName: Full=Flavoprotein A; GN Name=fprA; OrderedLocusNames=MJ0748; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP DISCUSSION OF FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9660187; DOI=10.1046/j.1432-1327.1998.2540325.x; RA Wasserfallen A., Ragettli S., Jouanneau Y., Leisinger T.; RT "A family of flavoproteins in the domains Archaea and Bacteria."; RL Eur. J. Biochem. 254:325-332(1998). CC -!- FUNCTION: Probably functions as an electron acceptor for a CC hydrogenase; however there is an uncharacterized intermediate CC between the hydrogenase and flavoprotein A. {ECO:0000250}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; CC Note=Binds 2 iron ions per subunit.; CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000250}. CC -!- SIMILARITY: In the N-terminal section; belongs to the zinc CC metallo-hydrolase group 3 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98741.1; -; Genomic_DNA. DR PIR; D64393; D64393. DR ProteinModelPortal; Q58158; -. DR SMR; Q58158; 10-411. DR STRING; 243232.MJ_0748; -. DR EnsemblBacteria; AAB98741; AAB98741; MJ_0748. DR KEGG; mja:MJ_0748; -. DR eggNOG; arCOG00509; Archaea. DR eggNOG; COG0426; LUCA. DR InParanoid; Q58158; -. DR KO; K19817; -. DR OMA; IYCTEIA; -. DR PhylomeDB; Q58158; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR000014; PAS. DR InterPro; IPR016440; Rubredoxin-O_OxRdtase. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00753; Lactamase_B; 1. DR PIRSF; PIRSF005243; ROO; 1. DR SMART; SM00849; Lactamase_B; 1. DR SMART; SM00091; PAS; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Flavoprotein; FMN; Iron; KW Metal-binding; Oxidoreductase; Reference proteome; Transport. FT CHAIN 1 416 Type A flavoprotein FprA. FT /FTId=PRO_0000216809. FT DOMAIN 266 407 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. FT REGION 33 212 Zinc metallo-hydrolase. FT METAL 87 87 Iron 1. {ECO:0000250}. FT METAL 89 89 Iron 1. {ECO:0000250}. FT METAL 91 91 Iron 2. {ECO:0000250}. FT METAL 155 155 Iron 1. {ECO:0000250}. FT METAL 174 174 Iron 1. {ECO:0000250}. FT METAL 174 174 Iron 2. {ECO:0000250}. FT METAL 239 239 Iron 2. {ECO:0000250}. SQ SEQUENCE 416 AA; 47380 MW; DA2C17F0647A2255 CRC64; MKKYESRRSK IADGVYWVGV LDWDIRMYHG YTLKGTTYNA YLVFGDEKVA LIDNTYPGTS AQMWGRIKDA FEKEGREFKI DVIVQNHVEK DHSGALPEIH KKFPDAPIYC TEVAVEGLKK HYPSLKDAQF KVVHTGDTVD LGGKTLTFLE APLLHWPDSM FTFYNEGGIL FSNDAFGQHL CFPAHKRFDK DIPEYVLMDA NQKFYANLIT PLSKLVLKKF EEVIQLGLLE KIKMIAPSHG QIWTDPMKVI KAYQDFATGK AAKDKAVIVY DTMHYSTQKM AHAFAEGLMS EGIDVVMYFL HYDERSEIVK DILDAKAVLF GIPTIYDEPY PSIGDIIYYL RGLKFNRTGF KRLAVTFGSM GGEGGAVAKI AEDLAKCGFE VINQYELYYV PTEDELTNCY NMGKELAKRI KEMKIE // ID FRHA_METJA Reviewed; 415 AA. AC Q60338; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Coenzyme F420 hydrogenase subunit alpha; DE EC=1.12.98.1; DE AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit alpha; DE Short=FRH; GN Name=frhA; OrderedLocusNames=MJ0029; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduces the physiological low-potential two-electron CC acceptor coenzyme F420, and the artificial one-electron acceptor CC methylviologen. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: H(2) + oxidized coenzyme F420 = reduced CC coenzyme F420. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; CC Evidence={ECO:0000250}; CC Note=There are 12-13 Fe atoms/(alpha(1)beta(1)gamma(1)) unit of CC the FRH. {ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large CC subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; A64299; A64299. DR ProteinModelPortal; Q60338; -. DR InParanoid; Q60338; -. DR OMA; HASHGIA; -. DR PhylomeDB; Q60338; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 1. DR InterPro; IPR017682; Coenz_F420_hydrogenase_asu. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00374; NiFeSe_Hases; 2. DR SUPFAM; SSF56762; SSF56762; 1. DR TIGRFAMs; TIGR03295; frhA; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. DR PROSITE; PS00508; NI_HGENASE_L_2; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Metal-binding; Nickel; KW Oxidoreductase; Reference proteome. FT CHAIN 1 415 Coenzyme F420 hydrogenase subunit alpha. FT /FTId=PRO_0000199722. FT METAL 68 68 Nickel. {ECO:0000255}. FT METAL 71 71 Nickel. {ECO:0000255}. FT METAL 391 391 Nickel. {ECO:0000255}. FT METAL 394 394 Nickel. {ECO:0000255}. SQ SEQUENCE 415 AA; 46784 MW; 8DD9A94CBABE35C4 CRC64; MEVNFVTNRI EIAPTTRHEG HAKLILEVDE EGIVNKAYYL NTTPVRGFET MLKGKPAEFA PIAVMRICGI CQTTHGIASC EAIENAIDCE VPDDGLLLRE LVGIGNRLHS HPLHHLLTID DFLKPDETDL KIELIKLIQR MRKVGQLVVD IVGGEGIHPP NIVIGGMRTN ITERAKSRLY YALRQYEKDA YELYEKYTEL IERYLEEIGI PDLGAHEYPY IATHTTYGDR YAINWDDVTE IPAQRYYDDE EAKQTTTIQI PLYAGVPAEG GPRARMVKFG NFREGGSAMD INIARAQENL GAVYRALEIL DELDLNGKTR AEVEYKDGFG IGVHEAPRAT NTHMAEVGKD GKIKSYRIIA ASTWNFPIVE KAIEGYPQQY AEVIMRAYDI CASCATHVIV KDEETKEIIE VRKML // ID FRHB_METJA Reviewed; 287 AA. AC Q60341; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Coenzyme F420 hydrogenase subunit beta; DE EC=1.12.98.1; DE AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit beta; DE Short=FRH; GN Name=frhB; OrderedLocusNames=MJ0032; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduces the physiological low-potential two-electron CC acceptor coenzyme F420, and the artificial one-electron acceptor CC methylviologen. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: H(2) + oxidized coenzyme F420 = reduced CC coenzyme F420. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; CC Evidence={ECO:0000250}; CC Note=There are 12-13 Fe atoms per alpha/beta/gamma unit of the CC FRH. {ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98011.1; -; Genomic_DNA. DR PIR; H64303; H64303. DR STRING; 243232.MJ_0032; -. DR EnsemblBacteria; AAB98011; AAB98011; MJ_0032. DR KEGG; mja:MJ_0032; -. DR eggNOG; arCOG02651; Archaea. DR eggNOG; COG1035; LUCA. DR InParanoid; Q60341; -. DR KO; K00441; -. DR OMA; REYGCEK; -. DR PhylomeDB; Q60341; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR017679; Coenz_F420_hydrogenase_bsu. DR InterPro; IPR007525; FrhB_FdhB_C. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. DR TIGRFAMs; TIGR03289; frhB; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Iron-sulfur; Metal-binding; Oxidoreductase; KW Reference proteome. FT CHAIN 1 287 Coenzyme F420 hydrogenase subunit beta. FT /FTId=PRO_0000159226. SQ SEQUENCE 287 AA; 32054 MW; 7CE7D4E6E970940E CRC64; MRWNRMNPFG SYKKVVSARS TLKEVLKKAQ DGGIVSTAFI YGLENNLLDG VIVADNAGEF KAVPKVATTP EEVLEAAGTK YTVCPNISVL KSAVREYGCE KIGVVGTPCQ VRAVRKLMKY PVGFRHVPDK IALIIGIFCM ENFPYYGLKL IVEEHCGVKM EDVVKMDIGK GKFWVYTRWG ETKAIKLKET HPYEQIACHV CTDYTAELAD ISTGSVGSPD GWSTVFIRTA KGEEIFNKMV EDGYLEVKPI EEVKPGLGLV EKLALQKKEK NMKEIEHRKE LGLPIPY // ID FRHG_METJA Reviewed; 230 AA. AC Q60340; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=Coenzyme F420 hydrogenase subunit gamma; DE EC=1.12.98.1; DE AltName: Full=8-hydroxy-5-deazaflavin-reducing hydrogenase subunit gamma; DE Short=FRH; GN Name=frhG; OrderedLocusNames=MJ0031; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduces the physiological low-potential two-electron CC acceptor coenzyme F420, and the artificial one-electron acceptor CC methylviologen. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: H(2) + oxidized coenzyme F420 = reduced CC coenzyme F420. CC -!- SUBUNIT: Heterocomplex of the form (alpha(1)beta(1)gamma(1))(8). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FrhG family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98010.1; -; Genomic_DNA. DR PIR; G64303; G64303. DR ProteinModelPortal; Q60340; -. DR STRING; 243232.MJ_0031; -. DR EnsemblBacteria; AAB98010; AAB98010; MJ_0031. DR KEGG; mja:MJ_0031; -. DR eggNOG; arCOG02473; Archaea. DR eggNOG; COG1941; LUCA. DR InParanoid; Q60340; -. DR KO; K00443; -. DR OMA; RDLCIKC; -. DR PhylomeDB; Q60340; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009375; C:ferredoxin hydrogenase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050454; F:coenzyme F420 hydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR017681; Coenz_F420_hydrogenase_gsu. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR001821; NiFe_hydrogenase_ssu. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR PRINTS; PR00614; NIHGNASESMLL. DR TIGRFAMs; TIGR03294; FrhG; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport. FT CHAIN 1 230 Coenzyme F420 hydrogenase subunit gamma. FT /FTId=PRO_0000159232. FT DOMAIN 169 197 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 198 228 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 178 178 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 181 181 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 184 184 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 188 188 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 207 207 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 210 210 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 213 213 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 217 217 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 230 AA; 24534 MW; 6C9936D3A20ED356 CRC64; MIKVVKVAHV QLCSCCGCLV SLADTYEKLL DVLNSIELVY CQTLADAREI PECDIALVEG SVCLDDHHSL EVAQEVRKKA KIVVALGACA ATGGVTRYCK GNQLSKPVHS SFSPLTEVIK VDLAIPGCPP SPEAIVGVIT AALNGDMEYL QPYAELAEKG SEACGCDVIY KVVNKSLCMG CGTCAAACPT RAIEMLDGRP NVLKELCIKC GACSVQCPRI RFPELIEKIE // ID FUCA_METJA Reviewed; 181 AA. AC Q58813; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=L-fuculose phosphate aldolase; DE EC=4.1.2.17; DE AltName: Full=L-fuculose-1-phosphate aldolase; GN Name=fucA; OrderedLocusNames=MJ1418; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16585745; DOI=10.1128/JB.188.8.2836-2844.2006; RA Grochowski L.L., Xu H., White R.H.; RT "Identification of lactaldehyde dehydrogenase in Methanocaldococcus RT jannaschii and its involvement in production of lactate for F420 RT biosynthesis."; RL J. Bacteriol. 188:2836-2844(2006). CC -!- FUNCTION: Catalyzes the reversible aldol cleavage of L-fuculose-1- CC phosphate to dihydroxyacetone phosphate (DHAP) and L-lactaldehyde. CC The substrate preference order is glyceraldehyde > DL- CC lactaldehyde, glycolaldehyde > acrolein > formaldehyde, CC methylglyoxal > acetaldehyde > crotonaldehyde. No activity was CC observed towards propionaldehyde. {ECO:0000269|PubMed:16585745}. CC -!- CATALYTIC ACTIVITY: L-fuculose 1-phosphate = glycerone phosphate + CC (S)-lactaldehyde. {ECO:0000269|PubMed:16585745}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=570 nmol/min/mg enzyme with glyceraldehyde as substrate (at CC pH 7.4 and at 70 degrees Celsius) {ECO:0000269|PubMed:16585745}; CC Vmax=501 nmol/min/mg enzyme with DL-lactaldehyde as substrate CC (at pH 7.4 and at 70 degrees Celsius) CC {ECO:0000269|PubMed:16585745}; CC -!- PATHWAY: Carbohydrate degradation; L-fucose degradation; L- CC lactaldehyde and glycerone phosphate from L-fucose: step 3/3. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16585745}. CC -!- SIMILARITY: Belongs to the aldolase class II family. AraD/FucA CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99428.1; -; Genomic_DNA. DR PIR; A64477; A64477. DR ProteinModelPortal; Q58813; -. DR STRING; 243232.MJ_1418; -. DR EnsemblBacteria; AAB99428; AAB99428; MJ_1418. DR KEGG; mja:MJ_1418; -. DR eggNOG; arCOG04226; Archaea. DR eggNOG; COG0235; LUCA. DR InParanoid; Q58813; -. DR KO; K01628; -. DR OMA; KIGYVDY; -. DR PhylomeDB; Q58813; -. DR BioCyc; MetaCyc:MONOMER-12176; -. DR BRENDA; 4.1.2.17; 3260. DR UniPathway; UPA00071; -. DR UniPathway; UPA00563; UER00626. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016832; F:aldehyde-lyase activity; IBA:GO_Central. DR GO; GO:0008738; F:L-fuculose-phosphate aldolase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019317; P:fucose catabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR Pfam; PF00596; Aldolase_II; 1. DR SMART; SM01007; Aldolase_II; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 1: Evidence at protein level; KW Complete proteome; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 181 L-fuculose phosphate aldolase. FT /FTId=PRO_0000162932. FT METAL 68 68 Zinc. {ECO:0000250}. FT METAL 87 87 Zinc. {ECO:0000250}. FT METAL 89 89 Zinc. {ECO:0000250}. FT METAL 147 147 Zinc. {ECO:0000250}. SQ SEQUENCE 181 AA; 20470 MW; E5F3BF13722145B0 CRC64; MDKKQFIKIC RKLYDRKYVV GSGGNVSVKE GDKIYLTPTG SILGFLKEDD IAEMDLDGNV IKGKPTSEKN LHLMIYRKRN DINAIIHTHS LISTFLSTIN KEIELLTPEG KIFLKKIGYV DYYEAGSLKL AEETAKRDED VIILKNHGVV CLGKDLIDAY IKVEVLEEQA KLTLLNLLVK K // ID G3P_METJA Reviewed; 343 AA. AC Q58546; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 114. DE RecName: Full=Glyceraldehyde-3-phosphate dehydrogenase; DE Short=GAPDH; DE EC=1.2.1.59; DE AltName: Full=NAD(P)-dependent glyceraldehyde-3-phosphate dehydrogenase; GN Name=gap; OrderedLocusNames=MJ1146; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate + phosphate + CC NAD(P)(+) = 3-phospho-D-glyceroyl phosphate + NAD(P)H. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 1/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the glyceraldehyde-3-phosphate CC dehydrogenase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99147.1; -; Genomic_DNA. DR PIR; A64443; A64443. DR PDB; 2YYY; X-ray; 1.85 A; A/B=1-343. DR PDBsum; 2YYY; -. DR ProteinModelPortal; Q58546; -. DR SMR; Q58546; 2-343. DR STRING; 243232.MJ_1146; -. DR EnsemblBacteria; AAB99147; AAB99147; MJ_1146. DR KEGG; mja:MJ_1146; -. DR eggNOG; arCOG00493; Archaea. DR eggNOG; COG0057; LUCA. DR InParanoid; Q58546; -. DR KO; K00150; -. DR OMA; VTVPSHH; -. DR PhylomeDB; Q58546; -. DR BRENDA; 1.2.1.59; 3260. DR UniPathway; UPA00109; UER00184. DR EvolutionaryTrace; Q58546; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008839; F:4-hydroxy-tetrahydrodipicolinate reductase; IEA:InterPro. DR GO; GO:0004365; F:glyceraldehyde-3-phosphate dehydrogenase (NAD+) (phosphorylating) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009089; P:lysine biosynthetic process via diaminopimelate; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00559; G3P_dehdrog_arch; 1. DR InterPro; IPR000846; DapB_N. DR InterPro; IPR020831; GlycerAld/Erythrose_P_DH. DR InterPro; IPR020830; GlycerAld_3-P_DH_AS. DR InterPro; IPR020829; GlycerAld_3-P_DH_cat. DR InterPro; IPR020828; GlycerAld_3-P_DH_NAD(P)-bd. DR InterPro; IPR006436; Glyceraldehyde-3-P_DH_2_arc. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01113; DapB_N; 1. DR Pfam; PF02800; Gp_dh_C; 1. DR PIRSF; PIRSF000149; GAP_DH; 1. DR SMART; SM00846; Gp_dh_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01546; GAPDH-II_archae; 1. DR PROSITE; PS00071; GAPDH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Glycolysis; NAD; NADP; KW Oxidoreductase; Reference proteome. FT CHAIN 1 343 Glyceraldehyde-3-phosphate dehydrogenase. FT /FTId=PRO_0000145723. FT NP_BIND 12 13 NAD. {ECO:0000250}. FT REGION 143 145 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250}. FT REGION 198 199 Glyceraldehyde 3-phosphate binding. FT {ECO:0000250}. FT ACT_SITE 144 144 Nucleophile. {ECO:0000250}. FT BINDING 114 114 NAD; via amide nitrogen. {ECO:0000250}. FT BINDING 172 172 NAD. {ECO:0000250}. FT BINDING 307 307 NAD; via carbonyl oxygen. {ECO:0000250}. FT STRAND 3 8 {ECO:0000244|PDB:2YYY}. FT HELIX 12 23 {ECO:0000244|PDB:2YYY}. FT STRAND 24 36 {ECO:0000244|PDB:2YYY}. FT HELIX 39 46 {ECO:0000244|PDB:2YYY}. FT STRAND 51 55 {ECO:0000244|PDB:2YYY}. FT HELIX 58 66 {ECO:0000244|PDB:2YYY}. FT HELIX 75 77 {ECO:0000244|PDB:2YYY}. FT HELIX 79 81 {ECO:0000244|PDB:2YYY}. FT STRAND 83 87 {ECO:0000244|PDB:2YYY}. FT HELIX 93 100 {ECO:0000244|PDB:2YYY}. FT TURN 101 106 {ECO:0000244|PDB:2YYY}. FT STRAND 108 111 {ECO:0000244|PDB:2YYY}. FT HELIX 117 119 {ECO:0000244|PDB:2YYY}. FT STRAND 120 124 {ECO:0000244|PDB:2YYY}. FT TURN 126 128 {ECO:0000244|PDB:2YYY}. FT HELIX 130 133 {ECO:0000244|PDB:2YYY}. FT STRAND 137 141 {ECO:0000244|PDB:2YYY}. FT HELIX 144 157 {ECO:0000244|PDB:2YYY}. FT STRAND 160 174 {ECO:0000244|PDB:2YYY}. FT STRAND 188 195 {ECO:0000244|PDB:2YYY}. FT HELIX 198 205 {ECO:0000244|PDB:2YYY}. FT HELIX 207 209 {ECO:0000244|PDB:2YYY}. FT STRAND 212 221 {ECO:0000244|PDB:2YYY}. FT STRAND 226 236 {ECO:0000244|PDB:2YYY}. FT HELIX 240 249 {ECO:0000244|PDB:2YYY}. FT STRAND 253 256 {ECO:0000244|PDB:2YYY}. FT HELIX 258 260 {ECO:0000244|PDB:2YYY}. FT HELIX 265 275 {ECO:0000244|PDB:2YYY}. FT HELIX 278 280 {ECO:0000244|PDB:2YYY}. FT STRAND 284 288 {ECO:0000244|PDB:2YYY}. FT HELIX 289 291 {ECO:0000244|PDB:2YYY}. FT STRAND 293 295 {ECO:0000244|PDB:2YYY}. FT STRAND 298 305 {ECO:0000244|PDB:2YYY}. FT TURN 307 311 {ECO:0000244|PDB:2YYY}. FT HELIX 312 322 {ECO:0000244|PDB:2YYY}. FT HELIX 329 340 {ECO:0000244|PDB:2YYY}. SQ SEQUENCE 343 AA; 38102 MW; 81EB5810A9C838C5 CRC64; MPAKVLINGY GSIGKRVADA VSMQDDMEVI GVTKTKPDFE ARLAVEKGYK LFVAIPDNER VKLFEDAGIP VEGTILDIIE DADIVVDGAP KKIGKQNLEN IYKPHKVKAI LQGGEKAKDV EDNFNALWSY NRCYGKDYVR VVSCNTTGLC RILYAINSIA DIKKARIVLV RRAADPNDDK TGPVNAITPN PVTVPSHHGP DVVSVVPEFE GKILTSAVIV PTTLMHMHTL MVEVDGDVSR DDILEAIKKT PRIITVRAED GFSSTAKIIE YGRDLGRLRY DINELVVWEE SINVLENEIF LMQAVHQESI VIPENIDCIR AMLQMEEDNF KSIEKTNKAM GIQ // ID FLAB2_METJA Reviewed; 217 AA. AC Q58302; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Flagellin B2; DE Flags: Precursor; GN Name=flaB2; OrderedLocusNames=MJ0892; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Flagellin is the subunit protein which polymerizes to CC form the filaments of archaeal flagella. CC -!- SUBCELLULAR LOCATION: Archaeal flagellum. CC -!- SIMILARITY: Belongs to the archaeal flagellin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98895.1; -; Genomic_DNA. DR PIR; D64411; D64411. DR ProteinModelPortal; Q58302; -. DR STRING; 243232.MJ_0892; -. DR EnsemblBacteria; AAB98895; AAB98895; MJ_0892. DR KEGG; mja:MJ_0892; -. DR eggNOG; arCOG01829; Archaea. DR eggNOG; COG1681; LUCA. DR InParanoid; Q58302; -. DR KO; K07325; -. DR OMA; YLAIYIT; -. DR PhylomeDB; Q58302; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009288; C:bacterial-type flagellum; IEA:UniProtKB-KW. DR GO; GO:0005198; F:structural molecule activity; IEA:InterPro. DR InterPro; IPR013373; Flagellin/pilin_N. DR InterPro; IPR002774; Flagellin_arc. DR Pfam; PF01917; Arch_flagellin; 1. DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1. PE 3: Inferred from homology; KW Archaeal flagellum; Complete proteome; Reference proteome. FT PROPEP 1 12 {ECO:0000250}. FT /FTId=PRO_0000009375. FT CHAIN 13 217 Flagellin B2. FT /FTId=PRO_0000009376. SQ SEQUENCE 217 AA; 22577 MW; 6E9D9435C243A82D CRC64; MKVFEFLKGK RGAMGIGTLI IFIAMVLVAA VAAAVLINTS GFLQQKAMAT GKESTEQVAS GLSTLQVIGI HDNKAINYLA IYITPNAGSA AIDLNQTKIL ITDGEKKAVL RYNSNAYADL TTGGEVTNTS LAAWNLSGGE FGIIVLQDAD GSCKSTTPVI NKGDIVALTI NASAVGLNLV PRTTVTGSVI PEFGAPAVIE FTTPAAYLST QEVIQLQ // ID FTSZ2_METJA Reviewed; 380 AA. AC Q58039; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 20-JAN-2016, entry version 98. DE RecName: Full=Cell division protein FtsZ 2 {ECO:0000255|HAMAP-Rule:MF_00909}; GN Name=ftsZ2 {ECO:0000255|HAMAP-Rule:MF_00909}; GN OrderedLocusNames=MJ0622; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Essential cell division protein that forms a contractile CC ring structure (Z ring) at the future cell division site. The CC regulation of the ring assembly controls the timing and the CC location of cell division. One of the functions of the FtsZ ring CC is to recruit other cell division proteins to the septum to CC produce a new cell wall between the dividing cells. Binds GTP and CC shows GTPase activity. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SUBUNIT: Homodimer. Polymerizes to form a dynamic ring structure CC in a strictly GTP-dependent manner. Interacts directly with CC several other division proteins. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00909}. CC Note=Assembles at midcell at the inner surface of the cytoplasmic CC membrane. {ECO:0000255|HAMAP-Rule:MF_00909}. CC -!- SIMILARITY: Belongs to the FtsZ family. {ECO:0000255|HAMAP- CC Rule:MF_00909}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98617.1; -; Genomic_DNA. DR PIR; F64377; F64377. DR ProteinModelPortal; Q58039; -. DR SMR; Q58039; 37-355. DR STRING; 243232.MJ_0622; -. DR EnsemblBacteria; AAB98617; AAB98617; MJ_0622. DR KEGG; mja:MJ_0622; -. DR eggNOG; arCOG02201; Archaea. DR eggNOG; COG0206; LUCA. DR InParanoid; Q58039; -. DR KO; K03531; -. DR OMA; WGARIQD; -. DR PhylomeDB; Q58039; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0032153; C:cell division site; IEA:UniProtKB-HAMAP. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000917; P:barrier septum assembly; IEA:UniProtKB-KW. DR GO; GO:0043093; P:FtsZ-dependent cytokinesis; IEA:UniProtKB-HAMAP. DR GO; GO:0051258; P:protein polymerization; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.20; -; 1. DR Gene3D; 3.40.50.1440; -; 1. DR HAMAP; MF_00909; FtsZ; 1. DR InterPro; IPR000158; Cell_div_FtsZ. DR InterPro; IPR020805; Cell_div_FtsZ_CS. DR InterPro; IPR024757; FtsZ_C. DR InterPro; IPR008280; Tub_FtsZ_C. DR InterPro; IPR018316; Tubulin/FtsZ_2-layer-sand-dom. DR InterPro; IPR003008; Tubulin_FtsZ_GTPase. DR Pfam; PF12327; FtsZ_C; 1. DR Pfam; PF00091; Tubulin; 1. DR PRINTS; PR00423; CELLDVISFTSZ. DR SMART; SM00864; Tubulin; 1. DR SMART; SM00865; Tubulin_C; 1. DR SUPFAM; SSF52490; SSF52490; 1. DR SUPFAM; SSF55307; SSF55307; 1. DR TIGRFAMs; TIGR00065; ftsZ; 1. DR PROSITE; PS01134; FTSZ_1; 1. DR PROSITE; PS01135; FTSZ_2; 1. PE 3: Inferred from homology; KW Cell cycle; Cell division; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Septation. FT CHAIN 1 380 Cell division protein FtsZ 2. FT /FTId=PRO_0000114402. FT NP_BIND 47 51 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT NP_BIND 134 136 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 165 165 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 168 168 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. FT BINDING 211 211 GTP. {ECO:0000255|HAMAP-Rule:MF_00909}. SQ SEQUENCE 380 AA; 40658 MW; 2A3AD01CCB54FB8C CRC64; MIYKFNIRNL RMIIMKLVKD ALSRSDTTRY LKDEFGEARI VVVGCGGAGN NTINRLMEIG IQGAETIAIN TDKQHLEVIQ ADKKILIGAT LTRGLGAGGY PEIGRKAAEM AKNILEEQLK GADLVFVTAG MGGGTGTGSA PVVAEVAKEN GAIVVGVVTY PFKIERARMK KADEGIARMS EVCDTVIIID NNKLLDLVPN LPINDAFKVA DEIIAQAVKG ITETIAVPSL INIDFADVKA VMSGGGVAMI GVGEVDSSDR GDRVQNVVRE TLSCPLLDVD YRGAKGALIH ITGGPDLTLK EANDIGEGIT KELDPEANVI WGARIDPEME GCIRVMAIIT GVKSPNIVGK DTKPKRIIPK VSKEQSQRKE RKIGGIDFIV // ID FNO_METJA Reviewed; 223 AA. AC Q58896; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=F420-dependent NADP reductase; DE EC=1.5.1.40; DE AltName: Full=F420H2:NADP oxidoreductase; GN Name=fno; OrderedLocusNames=MJ1501; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reduction of NADP(+) with F420H(2) via CC hydride transfer, and the reverse reaction, i.e. the reduction of CC F420 with NADPH. Probably functions in the regeneration of NADPH CC required in biosynthetic reactions. CC {ECO:0000250|UniProtKB:D9PVP5}. CC -!- CATALYTIC ACTIVITY: Reduced coenzyme F420 + NADP(+) = oxidized CC coenzyme F420 + NADPH. {ECO:0000250|UniProtKB:D9PVP5}. CC -!- SIMILARITY: Belongs to the F420-dependent NADP reductase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99514.1; -; Genomic_DNA. DR PIR; D64487; D64487. DR ProteinModelPortal; Q58896; -. DR STRING; 243232.MJ_1501; -. DR EnsemblBacteria; AAB99514; AAB99514; MJ_1501. DR KEGG; mja:MJ_1501; -. DR eggNOG; arCOG00457; Archaea. DR eggNOG; COG2085; LUCA. DR InParanoid; Q58896; -. DR KO; K06988; -. DR OMA; HAGIRIW; -. DR PhylomeDB; Q58896; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0070967; F:coenzyme F420 binding; IEA:InterPro. DR GO; GO:0008823; F:cupric reductase activity; IBA:GO_Central. DR GO; GO:0052851; F:ferric-chelate reductase (NADPH) activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0015677; P:copper ion import; IBA:GO_Central. DR GO; GO:0006740; P:NADPH regeneration; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR010185; NpdG. DR InterPro; IPR028939; ProC_N. DR Pfam; PF03807; F420_oxidored; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01915; npdG; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 223 F420-dependent NADP reductase. FT /FTId=PRO_0000087152. FT NP_BIND 9 12 NADP. {ECO:0000250|UniProtKB:O29370}. FT NP_BIND 30 31 NADP. {ECO:0000250|UniProtKB:O29370}. FT BINDING 35 35 NADP. {ECO:0000250|UniProtKB:O29370}. FT BINDING 75 75 NADP; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:O29370}. FT BINDING 101 101 NADP; via amide nitrogen. FT {ECO:0000250|UniProtKB:O29370}. SQ SEQUENCE 223 AA; 24068 MW; 2370BBD6F5BBD3D9 CRC64; MKIAILGGTG DQGFGLALRL AKNNKIIIGS RKKEKAEEAA KKAKEILKQR GIEADIIGLE NKDAAKEGDV VILSLPYEYT LSTIKQLKEE LKGKIVVSIG VPLATAIGDK PTRLLFPPDG SVAEMVQNVL KESKVVSAFQ NVCHAVLEDL DNPVDCDILV CGNDEEAKKV VIDLANQIDG VRAIDCGNLE KSRIIEAITP LLIGLNIKYK SKGTGIRITN LEI // ID FWDB_METJA Reviewed; 435 AA. AC P61154; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 16-MAR-2016, entry version 55. DE RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit B; DE EC=1.2.99.5; DE AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit B; GN Name=fwdB; OrderedLocusNames=MJ1194; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-121. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and CC methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme CC is oxygen-labile (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2) CC + methanofuran + reduced acceptor. CC -!- COFACTOR: CC Name=W-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60537; Evidence={ECO:0000305}; CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3. CC -!- SUBUNIT: This enzyme is composed of six subunits FwdA, FwdC, FwdD, CC FwdE, FwdF and FwdG. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FwdB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P61154; -. DR InParanoid; P61154; -. DR OMA; VCIDPHE; -. DR PhylomeDB; P61154; -. DR UniPathway; UPA00640; UER00692. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR InterPro; IPR016457; Formylmethanofuran_DH_bsu. DR InterPro; IPR006656; Mopterin_OxRdtase. DR Pfam; PF00384; Molybdopterin; 1. DR PIRSF; PIRSF005646; FwdB; 1. DR TIGRFAMs; TIGR03129; one_C_dehyd_B; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Oxidoreductase; Reference proteome; KW Selenocysteine; Tungsten. FT CHAIN 1 435 Tungsten-containing formylmethanofuran FT dehydrogenase 2 subunit B. FT /FTId=PRO_0000087392. FT NON_STD 121 121 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 435 AA; 48718 MW; C1652D23FFC20970 CRC64; MVKVVRNVVC PFCGTLCDDL EILVEDNHIV GTRHACRIGN AKFMHFEGAV RYTEPLMREN KKDDFKKVDY ETAIEETARL LTEATLPLIY GWSATECHAH MYGVELAELV GAVIDNTASV UHGPSLLAVQ DVGYPVCTLG EVKNRADVII FWGSNPMHAH PRHMSRYSVF ARGFFRERGR EDRTLIVVDP RETDTAKLAD IHLQVEPHKD YELVSAMRAV LKGFELQVDK VAGVPADLIY EAVEVCKNAQ FGELFFAMGV TMTRGKHRNI DNAIQLVIDL NAYTKFGLMP MRGHYNVNGF NQVLTWVTGY PFGVDFSRGY PRYNPGETTA NDLLQRGETD MMLNIASDPG AHFPQKAVQH MAKIPLVCID PHETPTTQLA NIIIPPAIAG VEVEGTAYRM DGVPIQLRKV IDPPEGVLPD REILKILIKK VKEML // ID FWDA_METJA Reviewed; 567 AA. AC Q58569; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Protein FwdA; GN Name=fwdA; OrderedLocusNames=MJ1169; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FwdA/FmdA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99171.1; -; Genomic_DNA. DR PIR; H64445; H64445. DR ProteinModelPortal; Q58569; -. DR STRING; 243232.MJ_1169; -. DR DNASU; 1452067; -. DR EnsemblBacteria; AAB99171; AAB99171; MJ_1169. DR KEGG; mja:MJ_1169; -. DR eggNOG; arCOG04461; Archaea. DR eggNOG; COG1229; LUCA. DR InParanoid; Q58569; -. DR KO; K00200; -. DR OMA; GEKMDIC; -. DR PhylomeDB; Q58569; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR Gene3D; 2.30.40.10; -; 3. DR InterPro; IPR013108; Amidohydro_3. DR InterPro; IPR012027; Formylmethanofuran_DH_asu. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF07969; Amidohydro_3; 1. DR PIRSF; PIRSF006453; FwdA; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR03121; one_C_dehyd_A; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 567 Protein FwdA. FT /FTId=PRO_0000087391. SQ SEQUENCE 567 AA; 63411 MW; EB6B1A37DFB4737C CRC64; MEYIIKNGIV YDPLNGINGE KMDICVKDGK IVESVSDNAK VIDASGCVVM PGGIDSHSHV AGAKVNVGRI FRPEDSKREI YAKKGLRTGT GFSVPSTYKT GYQYSEMGYT TVIEAAMPPL IARHTHEEFM ETPQIDKAAM PLFGNNWMVL EYLKEGDIKA CAAFVAWLLK AVKGFAIKIV NPGGTEAWGW GKNVHSLDDP VPYFDITPRE IVRGLAEVNE LLGLPHSIHV HPNNLGHPGN WETTLETMKC VEGVEAKPRV GERETSYYNT HCQFHSYGGT SWKDFESKAI EIAEYVNKSK HVVIDVGQVT LDETTTMTAD GPMEYDLHMT NGLKWANCDV ELETGSGVVP FIYSPKGPVY AVQWAIGLEL FLNTNTDKVL LTTDHPNAGP FTRYPRVIAW LMSKKYRDEW LYNKVHKWAQ QRSHVADADK EYDLYEIAKI TRANQAKVLG LSETKGHLGV GAEADIAIYA IDPEEKDGKK IEKAFRYAKY VLKGGEVVVK DGNVVKEVFG DTIYVDVQVG EDLMNEVLKD VGEKFRRYYS VNLENYPVSD EYANSWRVIK IDATDIN // ID FWDD_METJA Reviewed; 133 AA. AC Q58568; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Protein FwdD; GN Name=fwdD; OrderedLocusNames=MJ1168; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99170.1; -; Genomic_DNA. DR PIR; G64445; G64445. DR ProteinModelPortal; Q58568; -. DR STRING; 243232.MJ_1168; -. DR EnsemblBacteria; AAB99170; AAB99170; MJ_1168. DR KEGG; mja:MJ_1168; -. DR eggNOG; arCOG02674; Archaea. DR eggNOG; COG1153; LUCA. DR InParanoid; Q58568; -. DR KO; K00203; -. DR OMA; YIPMGPW; -. DR PhylomeDB; Q58568; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR012040; Formylmethanofuran_DH_dsu. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR Pfam; PF01568; Molydop_binding; 1. DR PIRSF; PIRSF015873; FwdD; 1. DR SUPFAM; SSF50692; SSF50692; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 133 Protein FwdD. FT /FTId=PRO_0000087393. SQ SEQUENCE 133 AA; 15207 MW; 39D14E35D18E935F CRC64; MKFFLNTGRT IWQGEAMEAG KNLDLYVKAA GVVYINEEDM EKLGVKEGDK VKVKSEYGEV VVYVKKATER MPEGMIYIPM GPWANCVVKP DTHSTGMPTF KGYPGFYVEV EKTDEEFLDM RSLMRKKYIE AVE // ID G3PP_METJA Reviewed; 228 AA. AC Q58832; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 86. DE RecName: Full=Glyceraldehyde 3-phosphate phosphatase {ECO:0000303|PubMed:25848029}; DE EC=3.1.3.- {ECO:0000305|PubMed:25848029}; GN OrderedLocusNames=MJ1437; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND COFACTOR. RX PubMed=25848029; DOI=10.1073/pnas.1423570112; RA Huang H., Pandya C., Liu C., Al-Obaidi N.F., Wang M., Zheng L., RA Toews Keating S., Aono M., Love J.D., Evans B., Seidel R.D., RA Hillerich B.S., Garforth S.J., Almo S.C., Mariano P.S., RA Dunaway-Mariano D., Allen K.N., Farelli J.D.; RT "Panoramic view of a superfamily of phosphatases through substrate RT profiling."; RL Proc. Natl. Acad. Sci. U.S.A. 112:E1974-E1983(2015). CC -!- FUNCTION: Catalyzes the dephosphorylation of D,L-glyceraldehyde 3- CC phosphate in vitro. {ECO:0000269|PubMed:25848029}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:25848029}; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99446.1; -; Genomic_DNA. DR PIR; D64479; D64479. DR ProteinModelPortal; Q58832; -. DR STRING; 243232.MJ_1437; -. DR DNASU; 1452341; -. DR EnsemblBacteria; AAB99446; AAB99446; MJ_1437. DR KEGG; mja:MJ_1437; -. DR eggNOG; arCOG02291; Archaea. DR eggNOG; COG1011; LUCA. DR InParanoid; Q58832; -. DR KO; K07025; -. DR OMA; HEENPNI; -. DR PhylomeDB; Q58832; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006439; HAD-SF_hydro_IA. DR InterPro; IPR011950; HAD-SF_hydro_IA_CTE7. DR Pfam; PF13419; HAD_2; 1. DR PRINTS; PR00413; HADHALOGNASE. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR02253; CTE7; 1. DR TIGRFAMs; TIGR01549; HAD-SF-IA-v1; 1. DR TIGRFAMs; TIGR01509; HAD-SF-IA-v3; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Reference proteome. FT CHAIN 1 228 Glyceraldehyde 3-phosphate phosphatase. FT /FTId=PRO_0000107329. SQ SEQUENCE 228 AA; 26064 MW; C832F9F435ABC3FF CRC64; MIKGILFDLD DTLYNSSEFV EIARREAVKS MIDAGLNIDF EEAMNILNKI IKDKGSNYGK HFDDLVKAVL GKYDPKIITT GIITYHNVKV ALLRPYPHTI KTLMELKAMG LKLGVITDGL TIKQWEKLIR LGIHPFFDDV ITSEEFGLGK PHLEFFKYGL KRMGLKAEET VYVGDRVDKD IKPAKELGMI TVRILKGKYK DMEDDEYSDY TINSLQELVD IVKNLKKD // ID GATB_METJA Reviewed; 472 AA. AC Q57624; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Aspartyl/glutamyl-tRNA(Asn/Gln) amidotransferase subunit B; DE Short=Asp/Glu-ADT subunit B; DE EC=6.3.5.-; GN Name=gatB; OrderedLocusNames=MJ0160; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatB subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98144.1; -; Genomic_DNA. DR PIR; A64320; A64320. DR ProteinModelPortal; Q57624; -. DR STRING; 243232.MJ_0160; -. DR EnsemblBacteria; AAB98144; AAB98144; MJ_0160. DR KEGG; mja:MJ_0160; -. DR eggNOG; arCOG01718; Archaea. DR eggNOG; COG0064; LUCA. DR InParanoid; Q57624; -. DR KO; K02434; -. DR OMA; ESADYRY; -. DR PhylomeDB; Q57624; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.410; -; 1. DR HAMAP; MF_00121; GatB; 1. DR InterPro; IPR004413; Apn/Gln-ADT_bsu. DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E. DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat. DR InterPro; IPR018027; Asn/Gln_amidotransferase. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR023168; GatB_Yqey_C. DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS. DR PANTHER; PTHR11659; PTHR11659; 1. DR Pfam; PF02934; GatB_N; 1. DR Pfam; PF02637; GatB_Yqey; 1. DR SMART; SM00845; GatB_Yqey; 1. DR SUPFAM; SSF89095; SSF89095; 1. DR TIGRFAMs; TIGR00133; gatB; 1. DR PROSITE; PS01234; GATB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 472 Aspartyl/glutamyl-tRNA(Asn/Gln) FT amidotransferase subunit B. FT /FTId=PRO_0000148871. SQ SEQUENCE 472 AA; 53736 MW; 2C14856409CBF03A CRC64; MGGNMEDVKM KCGLEIHVQI DTKSKLFCNC STNYLDAEPN TNVCPVCLGL PGAKPLPPNK KAVEVAIMVA KMLGCKIVVD EDIYFQRKHY DYPDLPSGYQ RTSTPIGVDG EFMGIGIHEV HLEEDPGQYN PSFGIVDYNR SGTPLIEIVT KPDIKSPEEA REFLKQLMTL FRYLGCLRGE GTMRADVNIS IEYMGVQGNR VEVKNVNSIK GVYKVLKYEL IRQKNIIKRG GEVKRETRAF LESQMITKAM RSKETAEDYR YIPDPDIQPI VISEKWVKEI EEKMPETPLA KKKRFVEEYG IDEEDAKVLV SDLDMAEMFE EVVKSLGVNK ENVDLAVTWI RNELRRSLQY HKVDLYESGV KAEHIVELIK LIKEGVISQK IAKEIVDLLV INRGKKMPKE LVEELGLTVI RDEDALVKAV EEAIKNNPKA VEDYLNGKKE ALNFLMGQVM RLTRGRADPK RVIELLKERL DK // ID FWDG_METJA Reviewed; 82 AA. AC Q58567; DT 10-MAY-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Polyferredoxin protein FwdG; GN Name=fwdG; OrderedLocusNames=MJ1167; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000305}; CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99169.1; -; Genomic_DNA. DR PIR; F64445; F64445. DR ProteinModelPortal; Q58567; -. DR STRING; 243232.MJ_1167; -. DR EnsemblBacteria; AAB99169; AAB99169; MJ_1167. DR KEGG; mja:MJ_1167; -. DR eggNOG; arCOG00292; Archaea. DR eggNOG; ENOG4111IC0; LUCA. DR InParanoid; Q58567; -. DR KO; K11260; -. DR OMA; ETWGGKG; -. DR PhylomeDB; Q58567; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1 82 Polyferredoxin protein FwdG. FT /FTId=PRO_0000159141. FT DOMAIN 4 33 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 51 80 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 13 13 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 16 16 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 19 19 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 23 23 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 60 60 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 63 63 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 66 66 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 70 70 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 82 AA; 8797 MW; 6747750CF20F6805 CRC64; MKAYELVVYP ERCHGCGNCV VSCPVNAKHP ETWGGKGPYS DDVVIRVENG VVTVVNQDLC GGCGACIEAC PVNAIELVFK RK // ID G6PI_METJA Reviewed; 401 AA. AC Q59000; DT 02-NOV-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Glucose-6-phosphate isomerase; DE Short=GPI; DE EC=5.3.1.9; DE AltName: Full=Phosphoglucose isomerase; DE Short=PGI; DE AltName: Full=Phosphohexose isomerase; DE Short=PHI; GN Name=pgi; OrderedLocusNames=MJ1605; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE, BIOPHYSICOCHEMICAL RP PROPERTIES, ENZYME REGULATION, AND SUBUNIT. RX PubMed=14655001; DOI=10.1007/s00203-003-0626-4; RA Rudolph B., Hansen T., Schonheit P.; RT "Glucose-6-phosphate isomerase from the hyperthermophilic archaeon RT Methanococcus jannaschii: characterization of the first archaeal RT member of the phosphoglucose isomerase superfamily."; RL Arch. Microbiol. 181:82-87(2004). RN [3] RP FUNCTION AS A GLUCOSE-6-PHOSPHATE ISOMERASE. RX PubMed=17014089; DOI=10.1021/bi061018a; RA White R.H., Xu H.; RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5- RT ketofructose-1-phosphate: a precursor for aromatic amino acid RT biosynthesis in Methanocaldococcus jannaschii."; RL Biochemistry 45:12366-12379(2006). CC -!- FUNCTION: Catalyzes the isomerization of glucose-6-P to fructose- CC 6-P. {ECO:0000269|PubMed:14655001, ECO:0000269|PubMed:17014089}. CC -!- CATALYTIC ACTIVITY: D-glucose 6-phosphate = D-fructose 6- CC phosphate. CC -!- ENZYME REGULATION: Competively inhibited by 6-phosphogluconate and CC erythrose 4-phosphate. {ECO:0000269|PubMed:14655001}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.04 mM for F6P (at pH 6.3 and 50 degrees Celsius) CC {ECO:0000269|PubMed:14655001}; CC KM=1 mM for G6P (at pH 6.3 and 50 degrees Celsius) CC {ECO:0000269|PubMed:14655001}; CC Vmax=9 umol/min/mg enzyme for G6P (at pH 6.3 and 50 degrees CC Celsius) {ECO:0000269|PubMed:14655001}; CC Vmax=21 umol/min/mg enzyme for F6P (at pH 6.3 and 50 degrees CC Celsius) {ECO:0000269|PubMed:14655001}; CC pH dependence: CC Optimum pH is 6.3. 50% remaining activity is observed at pH 5.3 CC and pH 7. {ECO:0000269|PubMed:14655001}; CC Temperature dependence: CC Optimum temperature is 89 degrees Celsius. It does not lose CC activity upon incubation at 80 degrees Celsius for about 120 min CC and still has a half-life at 95 degrees Celsius of 40 min. At CC 100 degrees Celsius, an almost complete loss of activity is CC observed after 30 min. {ECO:0000269|PubMed:14655001}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate and glycerone phosphate from D-glucose: step 2/4. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14655001}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GPI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99624.1; -; Genomic_DNA. DR PIR; D64500; D64500. DR ProteinModelPortal; Q59000; -. DR STRING; 243232.MJ_1605; -. DR EnsemblBacteria; AAB99624; AAB99624; MJ_1605. DR KEGG; mja:MJ_1605; -. DR eggNOG; arCOG00052; Archaea. DR eggNOG; COG0166; LUCA. DR InParanoid; Q59000; -. DR KO; K01810; -. DR OMA; EQPAVEW; -. DR PhylomeDB; Q59000; -. DR SABIO-RK; Q59000; -. DR UniPathway; UPA00109; UER00181. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004347; F:glucose-6-phosphate isomerase activity; IDA:UniProtKB. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00473; G6P_isomerase; 1. DR InterPro; IPR001672; G6P_Isomerase. DR InterPro; IPR018189; Phosphoglucose_isomerase_CS. DR PANTHER; PTHR11469; PTHR11469; 1. DR Pfam; PF00342; PGI; 1. DR PRINTS; PR00662; G6PISOMERASE. DR PROSITE; PS00765; P_GLUCOSE_ISOMERASE_1; 1. DR PROSITE; PS00174; P_GLUCOSE_ISOMERASE_2; 1. DR PROSITE; PS51463; P_GLUCOSE_ISOMERASE_3; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Gluconeogenesis; Glycolysis; Isomerase; KW Reference proteome. FT CHAIN 1 401 Glucose-6-phosphate isomerase. FT /FTId=PRO_0000180780. FT ACT_SITE 261 261 Proton donor. {ECO:0000250}. FT ACT_SITE 282 282 {ECO:0000250}. FT ACT_SITE 392 392 {ECO:0000250}. SQ SEQUENCE 401 AA; 45675 MW; D5B766A9F2230ED9 CRC64; MLSYDYENAL KVGEISLEDI NKVDFANAYS NLMEKLDNGV VGFRDVIYDE NLDKYKSLNG YENVVVIGMG GSILGTMAIY YAISPFNNNA YFIDNSDPEK TLSILKKVDL NESIIYIISK SGNTLETLVN YYLIKKRIEK LNSFKGKLVF ITNGGKLKRE AEKNNYDIFS IPENVPGRFS VFTAVGLAPL YSLGVDISKI LEGAREMDKI CQNEDILKNP ALLNGVIHYL YDKRGKDISV IMSYVESLKY FGDWYKQLIG ESLGKNKHGI TPLLSIGAKD QHSLLQLYMD GKKDKIITFM VAKKYRLDEE IEFEDINDEK ISCRYSDIIR SQQKATEIAL TNNGVPNVRI TLDEINEMAM GALLYMYEMQ VGFMGELYNI NAYNQPAVEE EKKICWRLIK Q // ID FWDC_METJA Reviewed; 273 AA. AC Q58571; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Tungsten-containing formylmethanofuran dehydrogenase 2 subunit C; DE EC=1.2.99.5; DE AltName: Full=Tungsten-containing formylmethanofuran dehydrogenase II subunit C; GN Name=fwdC; OrderedLocusNames=MJ1171; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible oxidation of CO(2) and CC methanofuran (MFR) to N-formylmethanofuran (CHO-MFR). This enzyme CC is oxygen-labile (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Formylmethanofuran + H(2)O + acceptor = CO(2) CC + methanofuran + reduced acceptor. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 1/3. CC -!- SUBUNIT: This enzyme is composed of six subunits FwdA, FwdC, FwdD, CC FwdE, FwdF and FwdG. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FwdC/FmdC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99173.1; -; Genomic_DNA. DR PIR; B64446; B64446. DR ProteinModelPortal; Q58571; -. DR STRING; 243232.MJ_1171; -. DR EnsemblBacteria; AAB99173; AAB99173; MJ_1171. DR KEGG; mja:MJ_1171; -. DR eggNOG; arCOG00097; Archaea. DR eggNOG; COG2218; LUCA. DR InParanoid; Q58571; -. DR KO; K00202; -. DR OMA; KFSGDYV; -. DR PhylomeDB; Q58571; -. DR UniPathway; UPA00640; UER00692. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0018493; F:formylmethanofuran dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR Gene3D; 2.160.20.60; -; 1. DR InterPro; IPR017550; Formylmethanofuran_DH_suC. DR InterPro; IPR002489; Glu_synth_asu_C. DR Pfam; PF01493; GXGXG; 1. DR SUPFAM; SSF69336; SSF69336; 1. DR TIGRFAMs; TIGR03122; one_C_dehyd_C; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Oxidoreductase; Reference proteome; KW Repeat. FT CHAIN 1 273 Tungsten-containing formylmethanofuran FT dehydrogenase 2 subunit C. FT /FTId=PRO_0000144194. FT REPEAT 78 90 1. FT REPEAT 97 109 2. FT REPEAT 116 128 3. FT REPEAT 142 154 4. FT REPEAT 161 173 5. FT REPEAT 180 192 6. FT REPEAT 199 211 7. FT REGION 78 211 7 X 13 AA repeats of [GW]-X-X-[MQ]-X-X-G- FT X-[IL]-X-[IV]-X-G. FT COMPBIAS 187 190 Poly-Ile. SQ SEQUENCE 273 AA; 29461 MW; B34219D170D9C1AD CRC64; MKELILTLQK EIIVPVEMDK VLPEVIENMS LEEIKNIELV QGRKRIKVAD IFDVELNDIE GEPRIVIKNS SPKLKYIGSK MTKGEIVVEG DAGMYVGAEM KGGKIVVNGN AESWAGQNMK GGELLIKGNA GDYVGSAYRG DWRGMSGGTI IVEGNAGNEI GEFMSKGLIH IKGNVGIMAG IHQNGGIIII DGDVDVRVGG EMKAGAIVVY GKVEEILPSF KFEGIVENPV IKLSKKDAGT PIAGTFYKFS GDYVYNKPKG QLYISVDSNP DLI // ID GATA_METJA Reviewed; 434 AA. AC Q58560; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit A; DE Short=Glu-ADT subunit A; DE EC=6.3.5.7; GN Name=gatA; OrderedLocusNames=MJ1160; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln) (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the amidase family. GatA subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99163.1; -; Genomic_DNA. DR PIR; G64444; G64444. DR ProteinModelPortal; Q58560; -. DR STRING; 243232.MJ_1160; -. DR EnsemblBacteria; AAB99163; AAB99163; MJ_1160. DR KEGG; mja:MJ_1160; -. DR eggNOG; arCOG01717; Archaea. DR eggNOG; COG0154; LUCA. DR InParanoid; Q58560; -. DR KO; K02433; -. DR OMA; HASPLEM; -. DR PhylomeDB; Q58560; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.1300.10; -; 1. DR HAMAP; MF_00120; GatA; 1. DR InterPro; IPR000120; Amidase. DR InterPro; IPR020556; Amidase_CS. DR InterPro; IPR023631; Amidase_dom. DR InterPro; IPR004412; GatA. DR PANTHER; PTHR11895; PTHR11895; 1. DR Pfam; PF01425; Amidase; 1. DR SUPFAM; SSF75304; SSF75304; 1. DR TIGRFAMs; TIGR00132; gatA; 1. DR PROSITE; PS00571; AMIDASES; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 434 Glutamyl-tRNA(Gln) amidotransferase FT subunit A. FT /FTId=PRO_0000105233. FT ACT_SITE 57 57 Charge relay system. {ECO:0000250}. FT ACT_SITE 132 132 Charge relay system. {ECO:0000250}. FT ACT_SITE 156 156 Acyl-ester intermediate. {ECO:0000250}. SQ SEQUENCE 434 AA; 48008 MW; 0A95BF0C62161F5F CRC64; MIVERVEEYL DRIEKINKDI NALIEVKPEK VLEEAKKLEK DEKAKKKPLY GKIIVVKANI NVEGYTISCA SKTLENYIAP YDATVIEKIK ENGGLIIGIA NMDEFACGSS GETSYFGPTK NPRAKDRIPG GSSSGSAAAV SADLCDMALG SDTGGSIRNP ASHCGVVGFK PSYGVVSRYG LCDLAMSFDQ IGPLTKTAED ALLLTNIIKG KDLRDTTTVE TKPFEKKDIK GFKVGVVKEF MDVADEKIRD KVEKAIEVFK DLGCEIVELS YKYVDLALPT YYLINYVEFF SSTRRYDGRR YGYKIEEVCG EEVLRRIMIG SMISQKEYSG KYYKNALKAR NLMRNEMIKI MKDVDIIVGA TVPKLPHKLG EKLTPMEMYS YDVLTVPANI CGLCAGVVPC GDINGIPVGL QIQGKPFEDE KVLSAMIAFE KAME // ID GATE_METJA Reviewed; 630 AA. AC Q60325; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit E {ECO:0000255|HAMAP-Rule:MF_00588}; DE Short=Glu-ADT subunit E {ECO:0000255|HAMAP-Rule:MF_00588}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00588}; GN Name=gatE {ECO:0000255|HAMAP-Rule:MF_00588}; OrderedLocusNames=MJ0019; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is CC specific for glutamate and does not act on aspartate. CC {ECO:0000255|HAMAP-Rule:MF_00588}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00588}. CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP- CC Rule:MF_00588}. CC -!- SIMILARITY: Belongs to the GatB/GatE family. GatE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00588}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97995.1; -; Genomic_DNA. DR PIR; C64302; C64302. DR ProteinModelPortal; Q60325; -. DR SMR; Q60325; 2-510. DR STRING; 243232.MJ_0019; -. DR EnsemblBacteria; AAB97995; AAB97995; MJ_0019. DR KEGG; mja:MJ_0019; -. DR eggNOG; arCOG01719; Archaea. DR eggNOG; COG2511; LUCA. DR InParanoid; Q60325; -. DR KO; K03330; -. DR OMA; TSGFQRT; -. DR PhylomeDB; Q60325; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0004812; F:aminoacyl-tRNA ligase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IBA:GO_Central. DR GO; GO:0070681; P:glutaminyl-tRNAGln biosynthesis via transamidation; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.410; -; 1. DR Gene3D; 3.30.1360.30; -; 1. DR HAMAP; MF_00588; GatE; 1. DR InterPro; IPR017959; Asn/Gln-tRNA_amidoTrfase_suB/E. DR InterPro; IPR006075; Asn/Gln-tRNA_Trfase_suB/E_cat. DR InterPro; IPR018027; Asn/Gln_amidotransferase. DR InterPro; IPR003789; Asn/Gln_tRNA_amidoTrfrase-rel. DR InterPro; IPR004115; GAD-like. DR InterPro; IPR029351; GAD_dom. DR InterPro; IPR023168; GatB_Yqey_C. DR InterPro; IPR004414; GatE. DR InterPro; IPR017958; Gln-tRNA_amidoTrfase_suB_CS. DR PANTHER; PTHR11659; PTHR11659; 3. DR Pfam; PF02938; GAD; 1. DR Pfam; PF02934; GatB_N; 1. DR Pfam; PF02637; GatB_Yqey; 1. DR SMART; SM00845; GatB_Yqey; 1. DR SUPFAM; SSF55261; SSF55261; 1. DR SUPFAM; SSF89095; SSF89095; 1. DR TIGRFAMs; TIGR00134; gatE_arch; 1. DR PROSITE; PS01234; GATB; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 630 Glutamyl-tRNA(Gln) amidotransferase FT subunit E. FT /FTId=PRO_0000140072. SQ SEQUENCE 630 AA; 71225 MW; 43D401B61B88F7AF CRC64; MEINYEKVGL KVGLEIHQQL NTKRKLFCHC PTILRDDEPD GEIVRVLRPS LSEMGEVDRA ALIEARKGKK FIYQFYNDTT CLVELDEEPP HPPSEEALRI ALEVALLMNM NVVDVAYTMR KIVIDGSNTS GFQRTIFLAR DGYIETSEGK VGITSLCLEE DAARKIEDRG DAVVYNLDRL GIPLVEISTA PDIKTPKMAK EAARRIGEIL RATGKVKRGL GTIRQDINIS IKDGARIEVK GVQDLDLIEK VVENEVIRQL NLLKIRDELR ERNAEVVEKI FDVTEIFKDC KSKIIQNALK KKNGKVKAVL LKGFAGLVGK EIQPGRRLGT EFSDRAKVIA GVGGLFHTDE LPKYGITEEE VKKLKEFVNA EENDAVIIVA DEESKVDRAL EAVIERAKEA LIGVPEETRR ALEDGNTAYL RPLPGAARMY PETDIPPIII KKEFIEEIRA NLPELPEEKF ERFKKEYKLN DELAKKMVLS YYVDLFEDLC KKFKNVKPVL IATTLEGTLK EIKREGYDID KLEDRHLEET FKALSEGKIA KEGIVEVLKG FCEFPDKSID EILEIKGLKG LSKEEVEKII EGIIKEHLNV VKEKGEKAYG FLMGRCMAKL RGKADGKLVN DILRKKLKEI // ID G1PDH_METJA Reviewed; 335 AA. AC Q58122; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 106. DE RecName: Full=Glycerol-1-phosphate dehydrogenase [NAD(P)+] {ECO:0000255|HAMAP-Rule:MF_00497}; DE Short=G1P dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497}; DE Short=G1PDH {ECO:0000255|HAMAP-Rule:MF_00497}; DE EC=1.1.1.261 {ECO:0000255|HAMAP-Rule:MF_00497}; DE AltName: Full=Enantiomeric glycerophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00497}; DE AltName: Full=sn-glycerol-1-phosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_00497}; GN Name=egsA {ECO:0000255|HAMAP-Rule:MF_00497}; OrderedLocusNames=MJ0712; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the NAD(P)H-dependent reduction of CC dihydroxyacetonephosphate (DHAP or glycerone phosphate) to CC glycerol 1-phosphate (G1P). The G1P thus generated is used as the CC glycerophosphate backbone of phospholipids in the cellular CC membranes of Archaea. {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- CATALYTIC ACTIVITY: sn-glycerol 1-phosphate + NAD(P)(+) = CC glycerone phosphate + NAD(P)H. {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00497}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00497}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00497}. CC -!- SIMILARITY: Belongs to the glycerol-1-phosphate dehydrogenase CC family. {ECO:0000255|HAMAP-Rule:MF_00497}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98707.1; -; Genomic_DNA. DR PIR; H64388; H64388. DR PDB; 4RFL; X-ray; 2.20 A; A/B/C/D=1-335. DR PDB; 4RGQ; X-ray; 2.23 A; A/B/C/D=1-335. DR PDB; 4RGV; X-ray; 2.45 A; A/B=1-335. DR PDBsum; 4RFL; -. DR PDBsum; 4RGQ; -. DR PDBsum; 4RGV; -. DR ProteinModelPortal; Q58122; -. DR STRING; 243232.MJ_0712; -. DR EnsemblBacteria; AAB98707; AAB98707; MJ_0712. DR KEGG; mja:MJ_0712; -. DR eggNOG; arCOG00982; Archaea. DR eggNOG; COG0371; LUCA. DR InParanoid; Q58122; -. DR KO; K00096; -. DR OMA; MIVIPRY; -. DR PhylomeDB; Q58122; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0050492; F:glycerol-1-phosphate dehydrogenase [NAD(P)+] activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00497_A; G1P_dehydrogenase_A; 1. DR InterPro; IPR023002; G1P_dehydrogenase_arc. DR InterPro; IPR032837; G1PDH. DR Pfam; PF13685; Fe-ADH_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Lipid biosynthesis; KW Lipid metabolism; Metal-binding; NAD; NADP; Oxidoreductase; KW Phospholipid biosynthesis; Phospholipid metabolism; KW Reference proteome; Zinc. FT CHAIN 1 335 Glycerol-1-phosphate dehydrogenase FT [NAD(P)+]. FT /FTId=PRO_0000157342. FT NP_BIND 78 82 NAD. {ECO:0000255|HAMAP-Rule:MF_00497}. FT NP_BIND 100 103 NAD. {ECO:0000255|HAMAP-Rule:MF_00497}. FT METAL 148 148 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT METAL 226 226 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT METAL 247 247 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT BINDING 105 105 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT BINDING 109 109 NAD. {ECO:0000255|HAMAP-Rule:MF_00497}. FT BINDING 148 148 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT BINDING 230 230 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00497}. FT STRAND 7 12 {ECO:0000244|PDB:4RFL}. FT HELIX 15 18 {ECO:0000244|PDB:4RFL}. FT HELIX 19 25 {ECO:0000244|PDB:4RFL}. FT STRAND 31 35 {ECO:0000244|PDB:4RFL}. FT TURN 37 39 {ECO:0000244|PDB:4RFL}. FT HELIX 40 42 {ECO:0000244|PDB:4RFL}. FT STRAND 45 51 {ECO:0000244|PDB:4RFL}. FT HELIX 52 57 {ECO:0000244|PDB:4RFL}. FT HELIX 64 66 {ECO:0000244|PDB:4RFL}. FT STRAND 70 77 {ECO:0000244|PDB:4RFL}. FT HELIX 78 91 {ECO:0000244|PDB:4RFL}. FT STRAND 95 101 {ECO:0000244|PDB:4RFL}. FT HELIX 105 107 {ECO:0000244|PDB:4RFL}. FT STRAND 110 112 {ECO:0000244|PDB:4RFL}. FT STRAND 114 117 {ECO:0000244|PDB:4RFL}. FT STRAND 125 130 {ECO:0000244|PDB:4RFL}. FT HELIX 131 135 {ECO:0000244|PDB:4RFL}. FT HELIX 139 166 {ECO:0000244|PDB:4RFL}. FT HELIX 172 191 {ECO:0000244|PDB:4RFL}. FT HELIX 197 215 {ECO:0000244|PDB:4RFL}. FT TURN 219 221 {ECO:0000244|PDB:4RFL}. FT HELIX 224 238 {ECO:0000244|PDB:4RFL}. FT HELIX 247 265 {ECO:0000244|PDB:4RFL}. FT HELIX 267 269 {ECO:0000244|PDB:4RFL}. FT HELIX 272 282 {ECO:0000244|PDB:4RFL}. FT HELIX 289 292 {ECO:0000244|PDB:4RFL}. FT HELIX 296 305 {ECO:0000244|PDB:4RFL}. FT HELIX 306 308 {ECO:0000244|PDB:4RFL}. FT STRAND 309 311 {ECO:0000244|PDB:4RFL}. FT TURN 315 318 {ECO:0000244|PDB:4RFL}. FT HELIX 322 331 {ECO:0000244|PDB:4RFL}. SQ SEQUENCE 335 AA; 37275 MW; A99C777C3126367B CRC64; MIIVTPRYTI IEDGAINKIE EILKKLNLKN PLVITGKNTK KYCRFFYDIV YYDEILNNLE IELKKYTAYD CVIGIGGGRS IDTGKYLAYK LGIPFISVPT TASNDGIASP IVSIRQPSFM VDAPIAIIAD TEIIKKSPRR LLSAGMGDIV SNITAVLDWK LAYKEKGEKY SESSAIFSKT IAKELISYVL NSDLSEYHNK LVKALVGSGI AIAIANSSRP ASGSEHLFSH ALDKLKEEYN LNINSLHGEQ CGIGTIMMSY LHEKENKKLS GLHEKIKMSL KKVDAPTTAK ELGFDEDIII EALTMAHKIR NRWTILRDGL SREEARKLAE ETGVI // ID GCH1L_METJA Reviewed; 244 AA. AC Q58337; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2002, sequence version 2. DT 17-FEB-2016, entry version 86. DE RecName: Full=GTP cyclohydrolase 1 type 2 homolog; GN OrderedLocusNames=MJ0927; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CRYSTALLIZATION. RX PubMed=23295494; DOI=10.1107/S1744309112049408; RA Kuan S.M., Chen H.C., Huang C.H., Chang C.H., Chen S.C., Yang C.S., RA Chen Y.; RT "Crystallization and preliminary X-ray diffraction analysis of the RT Nif3-family protein MJ0927 from Methanocaldococcus jannaschii."; RL Acta Crystallogr. F 69:80-82(2013). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.47 ANGSTROMS), AND DNA-BINDING. RX PubMed=25243119; DOI=10.1155/2014/171263; RA Chen S.C., Huang C.H., Yang C.S., Kuan S.M., Lin C.T., Chou S.H., RA Chen Y.; RT "Crystal structure of a conserved hypothetical protein MJ0927 from RT Methanocaldococcus jannaschii reveals a novel quaternary assembly in RT the Nif3 family."; RL Biomed. Res. Int. 2014:171263-171263(2014). CC -!- FUNCTION: DNA-binding protein exhibiting the ability to bind to CC both single-stranded and double-stranded DNA. CC {ECO:0000269|PubMed:25243119}. CC -!- SUBUNIT: Homohexamer; trimer of dimers, that forms a hollow cage- CC like architecture. {ECO:0000269|PubMed:25243119}. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase I type 2/NIF3 CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98929.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98929.1; ALT_INIT; Genomic_DNA. DR PIR; G64415; G64415. DR PDB; 4IWG; X-ray; 2.47 A; A/B/C=1-244. DR PDB; 4IWM; X-ray; 2.70 A; A/B/C/D/E/F=1-244. DR PDBsum; 4IWG; -. DR PDBsum; 4IWM; -. DR ProteinModelPortal; Q58337; -. DR STRING; 243232.MJ_0927; -. DR EnsemblBacteria; AAB98929; AAB98929; MJ_0927. DR KEGG; mja:MJ_0927; -. DR eggNOG; arCOG04454; Archaea. DR eggNOG; COG0327; LUCA. DR InParanoid; Q58337; -. DR OMA; GHHATEM; -. DR PhylomeDB; Q58337; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002678; GTP_cyclohydrolase_I/Nif3. DR PANTHER; PTHR13799; PTHR13799; 1. DR Pfam; PF01784; NIF3; 1. DR SUPFAM; SSF102705; SSF102705; 1. DR TIGRFAMs; TIGR00486; YbgI_SA1388; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Metal-binding; KW Reference proteome. FT CHAIN 1 244 GTP cyclohydrolase 1 type 2 homolog. FT /FTId=PRO_0000147348. FT METAL 65 65 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 66 66 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 102 102 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 216 216 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 220 220 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFP6}. FT METAL 220 220 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFP6}. FT HELIX 3 13 {ECO:0000244|PDB:4IWG}. FT HELIX 16 18 {ECO:0000244|PDB:4IWG}. FT STRAND 26 29 {ECO:0000244|PDB:4IWG}. FT STRAND 39 44 {ECO:0000244|PDB:4IWG}. FT HELIX 48 56 {ECO:0000244|PDB:4IWG}. FT STRAND 60 66 {ECO:0000244|PDB:4IWG}. FT HELIX 78 89 {ECO:0000244|PDB:4IWG}. FT STRAND 93 96 {ECO:0000244|PDB:4IWG}. FT HELIX 99 103 {ECO:0000244|PDB:4IWG}. FT HELIX 108 115 {ECO:0000244|PDB:4IWG}. FT STRAND 119 125 {ECO:0000244|PDB:4IWG}. FT STRAND 131 134 {ECO:0000244|PDB:4IWG}. FT HELIX 139 149 {ECO:0000244|PDB:4IWG}. FT STRAND 155 157 {ECO:0000244|PDB:4IWG}. FT STRAND 167 174 {ECO:0000244|PDB:4IWG}. FT HELIX 178 184 {ECO:0000244|PDB:4IWG}. FT TURN 185 187 {ECO:0000244|PDB:4IWG}. FT STRAND 189 194 {ECO:0000244|PDB:4IWG}. FT HELIX 198 207 {ECO:0000244|PDB:4IWG}. FT STRAND 210 213 {ECO:0000244|PDB:4IWG}. FT HELIX 216 234 {ECO:0000244|PDB:4IWG}. FT STRAND 237 242 {ECO:0000244|PDB:4IWG}. SQ SEQUENCE 244 AA; 27363 MW; BC42E5E29AAE399F CRC64; MKAKEIIEFI ETFAPKDLAI EGDNIGLQVG DNLDKEIKKL GIALDPSLSV IKKAEKEGVD FLFTHHPLLK DPIRNFTGVI YKKLKILMEN DIILYSAHTN LDICKNGLND ALAELYNLEN PKPLYDNGLG RVGIFKGSFE EFLEITKKYI HKNPIVVKSK EVDDNFKLAV LSGYGLSQSS IKYVAEKADV YLSGDLTHHS KILAEELGLV VVDATHYSTE VFGLKKFKEF LSSNLDLEII SLDF // ID GGGPS_METJA Reviewed; 253 AA. AC Q58647; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112}; DE Short=GGGP synthase {ECO:0000255|HAMAP-Rule:MF_00112}; DE Short=GGGPS {ECO:0000255|HAMAP-Rule:MF_00112}; DE EC=2.5.1.41 {ECO:0000255|HAMAP-Rule:MF_00112}; DE AltName: Full=(S)-3-O-geranylgeranylglyceryl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00112}; DE AltName: Full=Phosphoglycerol geranylgeranyltransferase {ECO:0000255|HAMAP-Rule:MF_00112}; GN OrderedLocusNames=MJ1250; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Prenyltransferase that catalyzes the transfer of the CC geranylgeranyl moiety of geranylgeranyl diphosphate (GGPP) to the CC C3 hydroxyl of sn-glycerol-1-phosphate (G1P). This reaction is the CC first ether-bond-formation step in the biosynthesis of archaeal CC membrane lipids. {ECO:0000255|HAMAP-Rule:MF_00112}. CC -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + sn-glycerol 1- CC phosphate = diphosphate + sn-3-O-(geranylgeranyl)glycerol 1- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00112}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00112}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_00112}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00112}. CC -!- SIMILARITY: Belongs to the GGGP/HepGP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00112}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99253.1; -; Genomic_DNA. DR PIR; A64456; A64456. DR ProteinModelPortal; Q58647; -. DR STRING; 243232.MJ_1250; -. DR DNASU; 1452148; -. DR EnsemblBacteria; AAB99253; AAB99253; MJ_1250. DR KEGG; mja:MJ_1250; -. DR eggNOG; arCOG01085; Archaea. DR eggNOG; COG1646; LUCA. DR InParanoid; Q58647; -. DR KO; K17104; -. DR OMA; EPIPMAY; -. DR PhylomeDB; Q58647; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0047294; F:phosphoglycerol geranylgeranyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046474; P:glycerophospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.390; -; 1. DR HAMAP; MF_00112; GGGP_HepGP_synthase; 1. DR InterPro; IPR008205; GGGP_HepGP_synthase. DR InterPro; IPR010946; GGGP_synth. DR Pfam; PF01884; PcrB; 1. DR TIGRFAMs; TIGR01769; GGGP; 1. DR TIGRFAMs; TIGR01768; GGGP-family; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Metal-binding; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase. FT CHAIN 1 253 Geranylgeranylglyceryl phosphate FT synthase. FT /FTId=PRO_0000138732. FT REGION 172 174 Glycerol-1-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00112}. FT METAL 28 28 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00112}. FT METAL 53 53 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00112}. FT BINDING 204 204 Glycerol-1-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00112}. SQ SEQUENCE 253 AA; 27797 MW; 02EA882E3D718C0F CRC64; MKIKIGKVEK RLNQIIEEEG AVYLTLLDPE EENIEEIAEN VKDYADAIMV GGSIGIVNLD ETVKKIKKIT KLPIILFPGN VDGLSRYADA VFYMSLMNSA NTYWVVTAPT LGAITILKYN LEPIPMAYLC IEPAKKTAVG YVGEIREIPQ NKPKITAMYC LSAKFFGMRW AYLEAGSGAS YPVNNETIAL SKKLSGINII VGGGIRKPEI AYEKVLAGAD AIVTGNLLEE NPKAVEMMYD AIKKAGKEKL KNK // ID GALE_METJA Reviewed; 305 AA. AC Q57664; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=Putative UDP-glucose 4-epimerase; DE EC=5.1.3.2; DE AltName: Full=Galactowaldenase; DE AltName: Full=UDP-galactose 4-epimerase; GN OrderedLocusNames=MJ0211; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the metabolism of galactose. Catalyzes the CC conversion of UDP-galactose (UDP-Gal) to UDP-glucose (UDP-Glc) CC through a mechanism involving the transient reduction of NAD (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-alpha-D-glucose = UDP-alpha-D-galactose. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate metabolism; galactose metabolism. CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98196.1; -; Genomic_DNA. DR PIR; D64326; D64326. DR ProteinModelPortal; Q57664; -. DR STRING; 243232.MJ_0211; -. DR PRIDE; Q57664; -. DR EnsemblBacteria; AAB98196; AAB98196; MJ_0211. DR KEGG; mja:MJ_0211; -. DR eggNOG; arCOG01369; Archaea. DR eggNOG; COG0451; LUCA. DR InParanoid; Q57664; -. DR KO; K01784; -. DR OMA; NRTWYGA; -. DR PhylomeDB; Q57664; -. DR BioCyc; RETL1328306-WGS:GSTH-1375-MONOMER; -. DR UniPathway; UPA00214; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0003978; F:UDP-glucose 4-epimerase activity; IEA:UniProtKB-EC. DR GO; GO:0006012; P:galactose metabolic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF01370; Epimerase; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Galactose metabolism; KW Isomerase; NAD; Reference proteome. FT CHAIN 1 305 Putative UDP-glucose 4-epimerase. FT /FTId=PRO_0000183225. FT NP_BIND 10 11 NAD. {ECO:0000250}. FT NP_BIND 30 35 NAD. {ECO:0000250}. FT NP_BIND 50 51 NAD. {ECO:0000250}. FT NP_BIND 71 75 NAD. {ECO:0000250}. FT REGION 183 184 Substrate binding. {ECO:0000250}. FT REGION 198 200 Substrate binding. {ECO:0000250}. FT REGION 263 266 Substrate binding. {ECO:0000250}. FT ACT_SITE 140 140 Proton acceptor. {ECO:0000250}. FT BINDING 115 115 Substrate. {ECO:0000250}. FT BINDING 140 140 NAD. {ECO:0000250}. FT BINDING 140 140 Substrate. {ECO:0000250}. FT BINDING 144 144 NAD. {ECO:0000250}. FT BINDING 169 169 Substrate. {ECO:0000250}. FT BINDING 207 207 Substrate. {ECO:0000250}. SQ SEQUENCE 305 AA; 34542 MW; 2756773CF95D50BD CRC64; MILVTGGAGF IGSHIVDKLI ENNYDVIILD NLTTGNKNNI NPKAEFVNAD IRDKDLDEKI NFKDVEVVIH QAAQINVRNS VENPVYDGDI NVLGTINILE MMRKYDIDKI VFASSGGAVY GEPNYLPVDE NHPINPLSPY GLSKYVGEEY IKLYNRLYGI EYAILRYSNV YGERQDPKGE AGVISIFIDK MLKNQSPIIF GDGNQTRDFV YVGDVAKANL MALNWKNEIV NIGTGKETSV NELFDIIKHE IGFRGEAIYD KPREGEVYRI YLDIKKAESL GWKPEIDLKE GIKRVVNWMK NNNRT // ID GATC_METJA Reviewed; 82 AA. AC Q57694; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Probable glutamyl-tRNA(Gln) amidotransferase subunit C; DE Short=Glu-ADT subunit C; DE EC=6.3.5.-; GN OrderedLocusNames=MJ0243; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Allows the formation of correctly charged Asn-tRNA(Asn) CC or Gln-tRNA(Gln) through the transamidation of misacylated Asp- CC tRNA(Asn) or Glu-tRNA(Gln) in organisms which lack either or both CC of asparaginyl-tRNA or glutaminyl-tRNA synthetases. The reaction CC takes place in the presence of glutamine and ATP through an CC activated phospho-Asp-tRNA(Asn) or phospho-Glu-tRNA(Gln) (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartyl-tRNA(Asn) + L-glutamine = ADP CC + phosphate + L-asparaginyl-tRNA(Asn) + L-glutamate. CC -!- SUBUNIT: Heterotrimer of A, B and C subunits. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GatC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98231.1; -; Genomic_DNA. DR PIR; D64330; D64330. DR ProteinModelPortal; Q57694; -. DR STRING; 243232.MJ_0243; -. DR EnsemblBacteria; AAB98231; AAB98231; MJ_0243. DR KEGG; mja:MJ_0243; -. DR eggNOG; arCOG02726; Archaea. DR eggNOG; COG0721; LUCA. DR KO; K02435; -. DR OMA; MEESYYI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR InterPro; IPR003837; Asp/Glu-ADT_csu. DR InterPro; IPR010120; Glu-ADT_subunit_C_archaea. DR Pfam; PF02686; Glu-tRNAGln; 1. DR SUPFAM; SSF141000; SSF141000; 1. DR TIGRFAMs; TIGR01827; gatC_rel; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 82 Probable glutamyl-tRNA(Gln) FT amidotransferase subunit C. FT /FTId=PRO_0000105359. SQ SEQUENCE 82 AA; 9786 MW; D400012E5D3C201B CRC64; MDEKTIEKIK KEAEEIINKF SEVLEKFNLE MEESYYIIDT RNVLREDEAV ESNPEFREKF LKIAPKVNKE GYVVVEKGSW LK // ID GCH3_METJA Reviewed; 268 AA. AC Q57609; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=GTP cyclohydrolase III; DE EC=3.5.4.29; DE AltName: Full=MjGC; GN Name=gch3; OrderedLocusNames=MJ0145; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION, MUTAGENESIS OF HIS-136, AND MASS SPECTROMETRY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12475257; DOI=10.1021/bi0268798; RA Graham D.E., Xu H., White R.H.; RT "A member of a new class of GTP cyclohydrolases produces RT formylaminopyrimidine nucleotide monophosphates."; RL Biochemistry 41:15074-15084(2002). CC -!- FUNCTION: Catalyzes the formation of 2-amino-5-formylamino-6- CC ribofuranosylamino-4(3H)-pyrimidinone ribonucleotide monophosphate CC and inorganic phosphate from GTP. Also has an independent CC pyrophosphate phosphohydrolase activity. CC -!- CATALYTIC ACTIVITY: GTP + 3 H(2)O = 2-amino-5-formylamino-6-(5- CC phospho-D-ribosylamino)pyrimidin-4(3H)-one + 2 phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- SUBUNIT: Homotrimer. CC -!- MASS SPECTROMETRY: Mass=30359; Mass_error=114; Method=MALDI; CC Range=1-268; Evidence={ECO:0000269|PubMed:12475257}; CC -!- MISCELLANEOUS: This enzyme couples pyrophosphate hydrolysis to the CC guanine ring-opening reaction. GTP cyclohydrolase and CC pyrophosphate phosphoydrolase activities probably occur at CC independent sites. CC -!- SIMILARITY: Belongs to the archaeal-type GTP cyclohydrolase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98128.1; -; Genomic_DNA. DR PIR; B64318; B64318. DR PDB; 2QV6; X-ray; 2.00 A; A/B/C/D=1-268. DR PDBsum; 2QV6; -. DR ProteinModelPortal; Q57609; -. DR SMR; Q57609; 1-253. DR STRING; 243232.MJ_0145; -. DR EnsemblBacteria; AAB98128; AAB98128; MJ_0145. DR KEGG; mja:MJ_0145; -. DR eggNOG; arCOG04202; Archaea. DR eggNOG; COG2429; LUCA. DR InParanoid; Q57609; -. DR KO; K08096; -. DR OMA; GYVFFTR; -. DR PhylomeDB; Q57609; -. DR BioCyc; MetaCyc:MONOMER-14598; -. DR BRENDA; 3.5.4.29; 3260. DR EvolutionaryTrace; Q57609; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0043740; F:GTP cyclohydrolase IIa activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR HAMAP; MF_00608; GTP_cyclohydro_3; 1. DR InterPro; IPR007839; GTP_CycHdrlase_3. DR Pfam; PF05165; GCH_III; 1. DR PIRSF; PIRSF009265; GTP_cyclohydro_3; 1. DR ProDom; PD313320; GTP_CycHdrlase_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; GTP-binding; Hydrolase; Magnesium; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 268 GTP cyclohydrolase III. FT /FTId=PRO_0000145754. FT MUTAGEN 136 136 H->Q: Decrease in GTP cyclohydrolase and FT pyrophosphate phosphohydrolase FT activities. FT {ECO:0000269|PubMed:12475257}. FT STRAND 2 9 {ECO:0000244|PDB:2QV6}. FT HELIX 12 17 {ECO:0000244|PDB:2QV6}. FT STRAND 18 20 {ECO:0000244|PDB:2QV6}. FT HELIX 24 43 {ECO:0000244|PDB:2QV6}. FT TURN 44 46 {ECO:0000244|PDB:2QV6}. FT STRAND 48 50 {ECO:0000244|PDB:2QV6}. FT STRAND 54 60 {ECO:0000244|PDB:2QV6}. FT HELIX 66 79 {ECO:0000244|PDB:2QV6}. FT STRAND 80 82 {ECO:0000244|PDB:2QV6}. FT STRAND 84 93 {ECO:0000244|PDB:2QV6}. FT HELIX 94 108 {ECO:0000244|PDB:2QV6}. FT STRAND 120 124 {ECO:0000244|PDB:2QV6}. FT STRAND 132 139 {ECO:0000244|PDB:2QV6}. FT HELIX 142 145 {ECO:0000244|PDB:2QV6}. FT TURN 146 149 {ECO:0000244|PDB:2QV6}. FT HELIX 152 171 {ECO:0000244|PDB:2QV6}. FT TURN 172 174 {ECO:0000244|PDB:2QV6}. FT STRAND 178 181 {ECO:0000244|PDB:2QV6}. FT STRAND 184 188 {ECO:0000244|PDB:2QV6}. FT HELIX 194 208 {ECO:0000244|PDB:2QV6}. FT STRAND 212 221 {ECO:0000244|PDB:2QV6}. FT HELIX 222 237 {ECO:0000244|PDB:2QV6}. FT STRAND 241 249 {ECO:0000244|PDB:2QV6}. SQ SEQUENCE 268 AA; 30286 MW; 627BBD523868B05B CRC64; MIQITVIQID NYGPWTVTPN PRRESDLQAL QSRLYADLNL MFGAHKGLVF YTRFDNLIAI TNGIDLITHK RIQESIRNRY PFTVSMVIAS AETPYEAQKL ATETLQEYGS AQDENRKEVL DVANELVVDG YVQIAHIDIN NITGTLTDIV SAYDTYLNVN KVKLALMEEL LKYNALLFFI GGDNFMAPSN GMSEEDFLDI FNRINKKYKI ELKAGIGIGR TAEDASNLAD IGLEKIRGKL VDKNVCTLKQ DDFLESKMGM GKIYHPQF // ID GATD_METJA Reviewed; 417 AA. AC Q60331; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Glutamyl-tRNA(Gln) amidotransferase subunit D {ECO:0000255|HAMAP-Rule:MF_00586}; DE Short=Glu-ADT subunit D {ECO:0000255|HAMAP-Rule:MF_00586}; DE EC=6.3.5.- {ECO:0000255|HAMAP-Rule:MF_00586}; GN Name=gatD {ECO:0000255|HAMAP-Rule:MF_00586}; OrderedLocusNames=MJ0020; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Allows the formation of correctly charged Gln-tRNA(Gln) CC through the transamidation of misacylated Glu-tRNA(Gln) in CC organisms which lack glutaminyl-tRNA synthetase. The reaction CC takes place in the presence of glutamine and ATP through an CC activated gamma-phospho-Glu-tRNA(Gln). The GatDE system is CC specific for glutamate and does not act on aspartate. CC {ECO:0000255|HAMAP-Rule:MF_00586}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamyl-tRNA(Gln) + L-glutamine = ADP CC + phosphate + L-glutaminyl-tRNA(Gln) + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00586}. CC -!- SUBUNIT: Heterodimer of GatD and GatE. {ECO:0000255|HAMAP- CC Rule:MF_00586}. CC -!- SIMILARITY: Belongs to the asparaginase 1 family. GatD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00586}. CC -!- SIMILARITY: Contains 1 asparaginase/glutaminase domain. CC {ECO:0000255|PROSITE-ProRule:PRU01068}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97996.1; -; Genomic_DNA. DR PIR; D64302; D64302. DR ProteinModelPortal; Q60331; -. DR SMR; Q60331; 1-417. DR STRING; 243232.MJ_0020; -. DR EnsemblBacteria; AAB97996; AAB97996; MJ_0020. DR KEGG; mja:MJ_0020; -. DR eggNOG; arCOG01924; Archaea. DR eggNOG; COG0252; LUCA. DR InParanoid; Q60331; -. DR KO; K09482; -. DR OMA; MHGETGD; -. DR PhylomeDB; Q60331; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004067; F:asparaginase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0050567; F:glutaminyl-tRNA synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR GO; GO:0006450; P:regulation of translational fidelity; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1170; -; 1. DR Gene3D; 3.40.50.40; -; 1. DR HAMAP; MF_00586; GatD; 1. DR InterPro; IPR006033; AsnASEI. DR InterPro; IPR006034; Asparaginase/glutaminase. DR InterPro; IPR020827; Asparaginase/glutaminase_AS1. DR InterPro; IPR027475; Asparaginase/glutaminase_AS2. DR InterPro; IPR011878; GatD. DR InterPro; IPR027473; L-asparaginase_C. DR InterPro; IPR027474; L-asparaginase_N. DR Pfam; PF00710; Asparaginase; 1. DR PIRSF; PIRSF500175; Glu_ADT_D; 1. DR PIRSF; PIRSF001220; L-ASNase_gatD; 1. DR PRINTS; PR00139; ASNGLNASE. DR SMART; SM00870; Asparaginase; 1. DR SUPFAM; SSF53774; SSF53774; 1. DR TIGRFAMs; TIGR00519; asnASE_I; 1. DR TIGRFAMs; TIGR02153; gatD_arch; 1. DR PROSITE; PS00144; ASN_GLN_ASE_1; 1. DR PROSITE; PS00917; ASN_GLN_ASE_2; 1. DR PROSITE; PS51732; ASN_GLN_ASE_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 417 Glutamyl-tRNA(Gln) amidotransferase FT subunit D. FT /FTId=PRO_0000140052. FT DOMAIN 74 403 Asparaginase/glutaminase. FT {ECO:0000255|PROSITE-ProRule:PRU01068}. FT ACT_SITE 84 84 {ECO:0000255|HAMAP-Rule:MF_00586}. FT ACT_SITE 160 160 {ECO:0000255|HAMAP-Rule:MF_00586}. FT ACT_SITE 161 161 {ECO:0000255|HAMAP-Rule:MF_00586}. FT ACT_SITE 237 237 {ECO:0000255|HAMAP-Rule:MF_00586}. SQ SEQUENCE 417 AA; 46344 MW; 27FFF41E62F41EE3 CRC64; MNVGDVIRVE TDKGIFEGIL LPSTNENIIT IKMKNGYNVG ILKENVKNIE IIAKGEKPKY ELPPLNIEKN EKLKTISILS TGGTVASKVD YKTGAVHPSF TADDLIRAVP ELLDIANIKG RAVMNILSEN MKPEYWRKIA EEIKKEIEEG ADGIVIAHGT DTMSYTASAL SFMVKADVPI ILVGAQRSSD RPSSDAALNL ISAVLAAREP IKGVYVVMHG ESGDTFCYLH KGVKVRKCHS SRRDAFKSIN SIPVAKINPF TKEIIYLQEV EKSDNSKKVE INTNLEEKVA LIKVYPGMDG EIIRFYVDKE YKGIVLEGTG LGHAPEYIFE HIKYATDKGV VVVMTTQTIN GRVNMNVYSN GRELQKLGVI GCEDMPPEVA LVKLMYLLGN YEPEEVKKLI NKNLVGEIEY RSRFDAY // ID GLGA_METJA Reviewed; 521 AA. AC Q59001; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Probable glycogen synthase; DE EC=2.4.1.21; DE AltName: Full=Starch [bacterial glycogen] synthase; GN Name=glgA; OrderedLocusNames=MJ1606; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Synthesizes alpha-1,4-glucan chains using ADP-glucose. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ADP-glucose + (1,4-alpha-D-glucosyl)(n) = ADP CC + (1,4-alpha-D-glucosyl)(n+1). CC -!- PATHWAY: Glycan biosynthesis; glycogen biosynthesis. CC -!- SIMILARITY: Belongs to the glycosyltransferase 1 family. CC Bacterial/plant glycogen synthase subfamily. {ECO:0000305}. CC -!- CAUTION: Could lack activity as the potential ADP-glucose binding CC site Arg/Lys residue in position 15 is replaced by an Ser. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99625.1; -; Genomic_DNA. DR PIR; E64500; E64500. DR ProteinModelPortal; Q59001; -. DR STRING; 243232.MJ_1606; -. DR CAZy; GT5; Glycosyltransferase Family 5. DR EnsemblBacteria; AAB99625; AAB99625; MJ_1606. DR KEGG; mja:MJ_1606; -. DR eggNOG; arCOG01420; Archaea. DR eggNOG; COG0297; LUCA. DR InParanoid; Q59001; -. DR KO; K00703; -. DR OMA; DAFNTVS; -. DR PhylomeDB; Q59001; -. DR UniPathway; UPA00164; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033201; F:alpha-1,4-glucan synthase activity; IEA:UniProtKB-EC. DR GO; GO:0004373; F:glycogen (starch) synthase activity; IEA:InterPro. DR GO; GO:0009011; F:starch synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005978; P:glycogen biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00484; Glycogen_synth; 1. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR011835; GS/SS. DR InterPro; IPR013534; Starch_synth_cat_dom. DR Pfam; PF08323; Glyco_transf_5; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycogen biosynthesis; Glycosyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 521 Probable glycogen synthase. FT /FTId=PRO_0000188668. SQ SEQUENCE 521 AA; 59736 MW; 68B1E0DE40715CC2 CRC64; MKIVILAPTI TPIVSYGGLG DVMRDLPKFL KKGNEVVVLT LNHYNRYFTL PYEDIKKITV IYKGAKITFD VLRTKHPTTG VDLIVFSNES VNNLNVWDPI KYEIFADLVI TYLDEVKDID VVSGHDWMCG LAIAKCNDIL DLPTTLTIHN EAFKGEMIEY KGEVMTFLEL GIKYADAVNT VSPSHAEEIK NYPYIKKYLN NKPFCGILNG IDIDEYDPMK IIERMCNLSN NKLDPRNYAY ISPYSAEDSH NIKPKIKYSW FYRGGVYEYV EDWNKIDKGI SATDVEVHGG VDGDIETPLI GFVGRATHQK GFNTMFEAIP ELLEKHDIRF VFLTKGDRDI EERLKNLANE HDGRILALIG YSLPLSSLVF AGSDWIIMPS YWEPCGLVQM EAMAYCTPVI ATETGGLKDT IIPLHPNPYE HPNFDKATGV LFKVPDKVGF MWGVEHALNW TFYKLNEICM FMQYIRYKCP KHPYDENSPL SMMMKNCYYH VFRNLSWQNS PSIRKYKGLF GGAIYNHYLQ P // ID GLMM_METJA Reviewed; 448 AA. AC Q58500; B1A8K6; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Phosphoglucosamine mutase; DE EC=5.4.2.10; GN Name=glmM; OrderedLocusNames=MJ1100; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18263721; DOI=10.1128/JB.01970-07; RA Namboori S.C., Graham D.E.; RT "Acetamido sugar biosynthesis in the Euryarchaea."; RL J. Bacteriol. 190:2987-2996(2008). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of glucosamine-6-phosphate to CC glucosamine-1-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Alpha-D-glucosamine 1-phosphate = D- CC glucosamine 6-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Forms large aggregates. {ECO:0000269|PubMed:18263721}. CC -!- PTM: Activated by phosphorylation. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; EU430076; ABZ91903.1; -; Genomic_DNA. DR EMBL; L77117; AAB99103.1; -; Genomic_DNA. DR PIR; C64437; C64437. DR ProteinModelPortal; Q58500; -. DR STRING; 243232.MJ_1100; -. DR EnsemblBacteria; AAB99103; AAB99103; MJ_1100. DR KEGG; mja:MJ_1100; -. DR eggNOG; arCOG00767; Archaea. DR eggNOG; COG1109; LUCA. DR InParanoid; Q58500; -. DR KO; K03431; -. DR OMA; NSHCDGR; -. DR PhylomeDB; Q58500; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004610; F:phosphoacetylglucosamine mutase activity; IBA:GO_Central. DR GO; GO:0008966; F:phosphoglucosamine mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR HAMAP; MF_01554_A; GlmM_A; 1. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR InterPro; IPR023666; GlmM_arc. DR InterPro; IPR024086; GlmM_arc-type. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR TIGRFAMs; TIGR03990; Arch_GlmM; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 448 Phosphoglucosamine mutase. FT /FTId=PRO_0000148029. FT ACT_SITE 89 89 Phosphoserine intermediate. FT {ECO:0000250}. FT METAL 89 89 Magnesium; via phosphate group. FT {ECO:0000250}. FT METAL 232 232 Magnesium. {ECO:0000250}. FT METAL 234 234 Magnesium. {ECO:0000250}. FT METAL 236 236 Magnesium. {ECO:0000250}. FT MOD_RES 89 89 Phosphoserine. {ECO:0000250}. FT CONFLICT 209 209 L -> I (in Ref. 1; ABZ91903). FT {ECO:0000305}. SQ SEQUENCE 448 AA; 50099 MW; FBC7EF17A73DF9B4 CRC64; MGRLFGTSGI RMKNLSPKIA YKVGLAVAKK YKKVVVGRDT RTTGKLIETA LTAGILNGGG EVTTINIVPT PVLGFNARNY DVGIMITASH NPPEYNGIKL FNKNGLAFNK KEEDEIEEII FKEDFIEVEW HSVGEIWEDS RAIRNYMEHI LKNVEINEKF NVVIDCANAS ACLVSPYLFT DLGCHVISVN SHMDGRFIGR LPEPDEKNLK KTMDMIKGLN MSGDNYIGIA HDGDADRMVA IDEKGRLADF DKLLAAFSRY MVEKTGNKKI VTTVDASMII DEYLKDLDVE IIRTKVGDVA VAEEMIKNSA VFGGEPSGTW IHADIHLTPD GILSGLRVLE MLDFYNKKLY EILDEIPSYV NLREKIPCED DKKEKVMSYV IENGESLFKT VPETVDGARF NLENGWVLIR PSGTEPYIRV RVEAKNNKDA KELLEKGIKL VKEALSAL // ID GMHA_METJA Reviewed; 187 AA. AC Q58731; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 97. DE RecName: Full=Probable phosphoheptose isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; DE EC=5.3.1.28 {ECO:0000255|HAMAP-Rule:MF_00067}; DE AltName: Full=Sedoheptulose 7-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00067}; GN Name=gmhA {ECO:0000255|HAMAP-Rule:MF_00067}; OrderedLocusNames=MJ1335; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the isomerization of sedoheptulose 7-phosphate CC in D-glycero-D-manno-heptose 7-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- CATALYTIC ACTIVITY: D-sedoheptulose 7-phosphate = D-glycero-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00067}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00067}; CC -!- PATHWAY: Carbohydrate biosynthesis; D-glycero-D-manno-heptose 7- CC phosphate biosynthesis; D-glycero-alpha-D-manno-heptose 7- CC phosphate and D-glycero-beta-D-manno-heptose 7-phosphate from CC sedoheptulose 7-phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- MISCELLANEOUS: The reaction produces a racemic mixture of D- CC glycero-alpha-D-manno-heptose 7-phosphate and D-glycero-beta-D- CC manno-heptose 7-phosphate. {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Belongs to the SIS family. GmhA subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00067}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|HAMAP- CC Rule:MF_00067}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99342.1; Type=Frameshift; Positions=49; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99342.1; ALT_FRAME; Genomic_DNA. DR PIR; F64466; F64466. DR ProteinModelPortal; Q58731; -. DR STRING; 243232.MJ_1335; -. DR EnsemblBacteria; AAB99342; AAB99342; MJ_1335. DR KEGG; mja:MJ_1335; -. DR eggNOG; arCOG05355; Archaea. DR eggNOG; COG0279; LUCA. DR InParanoid; Q58731; -. DR KO; K03271; -. DR OMA; EMHILMI; -. DR PhylomeDB; Q58731; -. DR UniPathway; UPA00041; UER00436. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0008968; F:D-sedoheptulose 7-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:2001061; P:D-glycero-D-manno-heptose 7-phosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00067; GmhA; 1. DR InterPro; IPR004515; Phosphoheptose_Isoase. DR InterPro; IPR001347; SIS. DR Pfam; PF13580; SIS_2; 1. DR TIGRFAMs; TIGR00441; gmhA; 1. DR PROSITE; PS51464; SIS; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Cytoplasm; Isomerase; KW Metal-binding; Reference proteome; Zinc. FT CHAIN 1 187 Probable phosphoheptose isomerase. FT /FTId=PRO_0000136552. FT DOMAIN 32 187 SIS. {ECO:0000255|HAMAP-Rule:MF_00067}. FT REGION 47 49 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 89 90 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT REGION 115 117 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT METAL 56 56 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 60 60 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 167 167 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT METAL 175 175 Zinc. {ECO:0000255|HAMAP-Rule:MF_00067}. FT BINDING 60 60 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 120 120 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. FT BINDING 167 167 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00067}. SQ SEQUENCE 187 AA; 20399 MW; 38440D7520757DB4 CRC64; MIMKKYFEES ANVKLKFIEE DEEKLKKAIE VIYNALKNGN KILICGNGGS AANSQHFAAE IVGRFKLERK GLPAIALTTD ISILTAIGND YGFDRIFERQ VEALGKEGDV LAGISTSGNS ENVIKAANKA KEMGIYTIGL LGKGGGKLKD IVDLALVVPS NDTARIQECH LTIYHVICEE VEKKLVK // ID GGR_METJA Reviewed; 391 AA. AC Q57952; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 100. DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000255|HAMAP-Rule:MF_01287}; DE Short=DGGGPL reductase {ECO:0000255|HAMAP-Rule:MF_01287}; DE EC=1.3.7.11 {ECO:0000255|HAMAP-Rule:MF_01287}; DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01287}; DE AltName: Full=Geranylgeranyl reductase {ECO:0000255|HAMAP-Rule:MF_01287}; DE Short=GGR {ECO:0000255|HAMAP-Rule:MF_01287}; GN OrderedLocusNames=MJ0532; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Is involved in the reduction of 2,3- CC digeranylgeranylglycerophospholipids (unsaturated archaeols) into CC 2,3-diphytanylglycerophospholipids (saturated archaeols) in the CC biosynthesis of archaeal membrane lipids. Catalyzes the formation CC of archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from CC 2,3-di-O-geranylgeranylglyceryl phosphate (DGGGP) via the CC hydrogenation of each double bond of the isoprenoid chains. CC {ECO:0000255|HAMAP-Rule:MF_01287}. CC -!- CATALYTIC ACTIVITY: A 2,3-bis-(O-phytanyl)-sn-glycero-phospholipid CC + 16 oxidized ferredoxin [iron-sulfur] cluster = a 2,3-bis-(O- CC geranylgeranyl)-sn-glycero-phospholipid + 16 reduced ferredoxin CC [iron-sulfur] cluster + 16 H(+). {ECO:0000255|HAMAP- CC Rule:MF_01287}. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287}; CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01287}; CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid CC metabolism. {ECO:0000255|HAMAP-Rule:MF_01287}. CC -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of CC hydrogen for double bonds. {ECO:0000255|HAMAP-Rule:MF_01287}. CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL CC reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_01287}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98523.1; -; Genomic_DNA. DR PIR; D64366; D64366. DR ProteinModelPortal; Q57952; -. DR STRING; 243232.MJ_0532; -. DR EnsemblBacteria; AAB98523; AAB98523; MJ_0532. DR KEGG; mja:MJ_0532; -. DR eggNOG; arCOG00570; Archaea. DR eggNOG; COG0644; LUCA. DR InParanoid; Q57952; -. DR KO; K17830; -. DR OMA; NVIVEFL; -. DR PhylomeDB; Q57952; -. DR UniPathway; UPA00940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0045550; F:geranylgeranyl reductase activity; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway. DR GO; GO:0046467; P:membrane lipid biosynthetic process; IEA:InterPro. DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_01287; DGGGPL_reductase; 1. DR InterPro; IPR023590; DGGGPL_reductase. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR011777; Geranylgeranyl_Rdtase_fam. DR Pfam; PF12831; FAD_oxidored; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR02032; GG-red-SF; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Lipid biosynthesis; KW Lipid metabolism; Oxidoreductase; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome. FT CHAIN 1 391 Digeranylgeranylglycerophospholipid FT reductase. FT /FTId=PRO_0000005342. FT NP_BIND 14 18 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. FT NP_BIND 37 39 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. FT NP_BIND 48 51 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. FT NP_BIND 291 292 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. FT REGION 206 212 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01287}. FT REGION 287 290 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01287}. FT BINDING 98 98 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. FT BINDING 279 279 FAD. {ECO:0000255|HAMAP-Rule:MF_01287}. SQ SEQUENCE 391 AA; 43094 MW; A2F69AEEF8940EF2 CRC64; MRELNDVYDV VVVGAGPGGS MASYASAKNG AKTLLIEKSQ EIGEPVRCAE AIPSIEEFGL KPEPEFVRNI IKGGILFSPS GKKVTVTQDK AQGYVVERKI FDKYLAIRAA KAGAKVAVKT TAIGLERDGD YWNVIVEFLG EEYVIKTKVV IAADGVESNI AEYAGLKAKK KPLEICSCAE YEMTNVELLD KNMMEFYFGN EVAPGGYVWI FPKGETANVG LGVRDKKKKA IEYLEEFIEN GLAKDRLKDA TPIEFKVGGA PVSGPIEKTY TDGLLVVGDA AGQISPLTGG GIYLAMDCGL IAGEVASKAI KLNDWSEETL KEYERRWKEK HYEYLMSHLK YRKILEKMSD DELDALAEAL GESLDGIDLK KFVKRIITKK PSLLKYFKDL L // ID GLMS_METJA Reviewed; 1099 AA. AC Q58815; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-MAY-2016, entry version 125. DE RecName: Full=Glutamine--fructose-6-phosphate aminotransferase [isomerizing]; DE EC=2.6.1.16; DE AltName: Full=D-fructose-6-phosphate amidotransferase; DE AltName: Full=GFAT; DE AltName: Full=Glucosamine-6-phosphate synthase; DE AltName: Full=Hexosephosphate aminotransferase; DE AltName: Full=L-glutamine--D-fructose-6-phosphate amidotransferase; DE Contains: DE RecName: Full=Mja gf6p intein; GN Name=glmS; OrderedLocusNames=MJ1420; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the first step in hexosamine metabolism, CC converting fructose-6P into glucosamine-6P using glutamine as a CC nitrogen source. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-glutamine + D-fructose 6-phosphate = L- CC glutamate + D-glucosamine 6-phosphate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the SIS family. CC GFAT subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC -!- SIMILARITY: Contains 2 SIS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99430.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99430.1; ALT_INIT; Genomic_DNA. DR PIR; C64477; C64477. DR ProteinModelPortal; Q58815; -. DR STRING; 243232.MJ_1420; -. DR EnsemblBacteria; AAB99430; AAB99430; MJ_1420. DR KEGG; mja:MJ_1420; -. DR eggNOG; arCOG00057; Archaea. DR eggNOG; arCOG03151; Archaea. DR eggNOG; COG0449; LUCA. DR InParanoid; Q58815; -. DR KO; K00820; -. DR OMA; NSRWATH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 3.10.28.10; -; 2. DR Gene3D; 3.60.20.10; -; 2. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR005855; GlmS_trans. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR001347; SIS. DR PANTHER; PTHR10937:SF0; PTHR10937:SF0; 2. DR Pfam; PF13537; GATase_7; 1. DR Pfam; PF01381; HTH_3; 1. DR Pfam; PF14528; LAGLIDADG_3; 2. DR Pfam; PF01380; SIS; 2. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF51294; SSF51294; 3. DR SUPFAM; SSF55608; SSF55608; 1. DR SUPFAM; SSF56235; SSF56235; 2. DR TIGRFAMs; TIGR01135; glmS; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS50943; HTH_CROC1; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS51464; SIS; 2. PE 3: Inferred from homology; KW Aminotransferase; Autocatalytic cleavage; Complete proteome; KW Cytoplasm; DNA-binding; Glutamine amidotransferase; Protein splicing; KW Reference proteome; Repeat; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 71 Glutamine--fructose-6-phosphate FT aminotransferase [isomerizing], 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000010848. FT CHAIN 72 570 Mja gf6p intein. {ECO:0000255}. FT /FTId=PRO_0000010849. FT CHAIN 571 1099 Glutamine--fructose-6-phosphate FT aminotransferase [isomerizing], 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000010850. FT DOMAIN 2 71 Glutamine amidotransferase type-2; first FT part. {ECO:0000255|PROSITE- FT ProRule:PRU00609}. FT DOMAIN 198 253 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DOMAIN 278 413 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT DOMAIN 571 723 Glutamine amidotransferase type-2; second FT part. {ECO:0000255|PROSITE- FT ProRule:PRU00609}. FT DOMAIN 786 923 SIS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT DOMAIN 948 1089 SIS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT ACT_SITE 2 2 Nucleophile; for GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT ACT_SITE 1094 1094 For Fru-6P isomerization activity. FT {ECO:0000250}. SQ SEQUENCE 1099 AA; 125501 MW; A4CFE30CB3894F16 CRC64; MCGIIGYIGN DKAPKILLNG LRRLEYRGYD SCGIGVVDNN KLIIKKNVGK VEEVAKKERF LDIDGNIGIG HCLHPDTYVI LPDGRMKKIS EIDEDEVLSV NFEDLKLYNK KIKKFKHKAP KILYKIKTAF SELITTGEHK LFVVENGKIV EKCVKDLNGS ELIGVVRKLN YSFNDNVEFK DVYVERHYKL DETIRNKLRK VREKLGLTRK DVEKLCGVKE IYIVKIETGK LESIEEERLK KLCSLYGINF EEIIYRDNLH YTNPVKFPKT PTPELMQIIG YIIGDGHFPS NRMLRLKDER KEVLEEYNQL FKTVFNLEGN IKKGDGNYYI LEINSKYLID WFRENIPELF NKTGNERTPE FVFRLNNDLV ASYLRGIFDA EGYIRAEAKQ IGIGMTSKCF IKEIQFLLLR FGILASYSKI KRKEENWNNT HKLLISDKKS FELFKKYIGF TAKDKMEKLE AILNKMKGLN FRYISIPLTK KEIREFVGVP LKTIKNGDNY CTDYTIEKII EELNSKGLYD KAEYLKRFLD ADIVWTKFKI EEVESDVEYV YDLEVEDYHN FIGNLIINHN SRWATHGNVC KENAHPHTDC KEEIAVVHNG IISNYKELKD ELMKKGHKFK SETDTEVVPH LIEEELKKFK EINEENYIKA VKNAIKKLKG TYALVIINKN FPNLLIGARN ESPLILGIND DGYFLGSDIT AFLDYTNKAI PLEDGDVVVI KKKENGYEVT IENNGNTVER EMMEINWDIS SAEKMGYPHF MLKEIMEQPE VLKVSAKISA EEIKELAKCI KDYDRVYFVA MGTSLHAAMV VEYLFAKLGK LVIACDASEF LNKGVVDDKT LVIGITQSGE TYDTLKALRF AKKNKAKTGA IVNVLGSTAT READITVMMG AGIEIAVCAT KTYTSQLMIL YRLFIEYGKL LGRDMSEYEK EIDKIPNYIK EVLDKKETIK EIANNLKVNN YIFISKGINI ASALEGALKF KEITYLHAEG MSGGLLKHGT ISLIDENMDT VAIVPPRDSA VFNSILSNIE EVKARGGKVI AITPTEIDGA ENILVPEVIE EISPIVYAPA FQLLAYYKAV ELGRDVDKPR GLAKSVTVE // ID GLNA_METJA Reviewed; 454 AA. AC Q60182; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Glutamine synthetase; DE Short=GS; DE EC=6.3.1.2; DE AltName: Full=Glutamate--ammonia ligase; GN Name=glnA; OrderedLocusNames=MJ1346; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + NH(3) = ADP + phosphate + CC L-glutamine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glutamine synthetase family. CC {ECO:0000305}. CC -!- CAUTION: Lacks the tyrosine conserved in bacteria and other CC archaea, involved in feedback inhibition. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99355.1; -; Genomic_DNA. DR PIR; A64468; A64468. DR ProteinModelPortal; Q60182; -. DR STRING; 243232.MJ_1346; -. DR EnsemblBacteria; AAB99355; AAB99355; MJ_1346. DR KEGG; mja:MJ_1346; -. DR eggNOG; arCOG01909; Archaea. DR eggNOG; COG0174; LUCA. DR InParanoid; Q60182; -. DR KO; K01915; -. DR OMA; KVLNQVG; -. DR PhylomeDB; Q60182; -. DR BRENDA; 6.3.1.2; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004356; F:glutamate-ammonia ligase activity; IEA:UniProtKB-EC. DR GO; GO:0006542; P:glutamine biosynthetic process; IEA:InterPro. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR Gene3D; 3.10.20.70; -; 1. DR Gene3D; 3.30.590.10; -; 1. DR InterPro; IPR008147; Gln_synt_b-grasp. DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom. DR InterPro; IPR008146; Gln_synth_cat_dom. DR InterPro; IPR027303; Gln_synth_gly_rich_site. DR InterPro; IPR004809; Gln_synth_I. DR InterPro; IPR027302; Gln_synth_N_conserv_site. DR Pfam; PF00120; Gln-synt_C; 1. DR Pfam; PF03951; Gln-synt_N; 1. DR SMART; SM01230; Gln-synt_C; 1. DR SUPFAM; SSF54368; SSF54368; 1. DR TIGRFAMs; TIGR00653; GlnA; 1. DR PROSITE; PS00180; GLNA_1; 1. DR PROSITE; PS00181; GLNA_ATP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 454 Glutamine synthetase. FT /FTId=PRO_0000153204. SQ SEQUENCE 454 AA; 51399 MW; 3222CBA464D18120 CRC64; MHWGMEMNVE QAIEYVKKNN VKFIRFQFVD ILGFPKNVAY PVKAGEKGIE ELREIFENGV WFDGSSITGF VGIEESDMLL KPDLSTLSVL PWRPEEKSVA RVICDVYKDE KTPFEGDPRS RLKAILEELK KEMNGEYFVG PEPEFFLLKR DPHNPHRWVP ADDGGYFDVE PLDDAPDIRR DIVLALENLG FHVEASHHEV APGQHEVDFK FDNALKTADS VITFKMTIKN IAKKHGLKAT FMPKPFFGMN GNGMHCHQSV WFNGEPSFYD PEGPYNGLSE TCLSYIAGIL SHAKALVAIT NPTVNSYKRL VPGYEAPVNI AWANKNRSAI IRVPAARGKA TRIEFRAPDP TCNPYLAFAC MLAAGLDGIK KKMTAPEPVE RNIFKMSEEE KKQLGIESVP ANLAAALDEL ECDEVLQKAL GKHIYENYME IKRAEWDDFR TAVTDWETGK YLIY // ID GLMU_METJA Reviewed; 408 AA. AC Q58501; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Bifunctional protein GlmU; DE Includes: DE RecName: Full=UDP-N-acetylglucosamine pyrophosphorylase; DE EC=2.7.7.23; DE AltName: Full=N-acetylglucosamine-1-phosphate uridyltransferase; DE Includes: DE RecName: Full=Glucosamine-1-phosphate N-acetyltransferase; DE EC=2.3.1.157; GN Name=glmU; OrderedLocusNames=MJ1101; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS AN URIDYLYLTRANSFERASE. RX PubMed=17014089; DOI=10.1021/bi061018a; RA White R.H., Xu H.; RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5- RT ketofructose-1-phosphate: a precursor for aromatic amino acid RT biosynthesis in Methanocaldococcus jannaschii."; RL Biochemistry 45:12366-12379(2006). RN [3] RP FUNCTION AS A PYROPHOSPHORYLASE AND ACETYLTRANSFERASE, CATALYTIC RP ACTIVITY, SUBSTRATE SPECIFICITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=900; RX PubMed=18263721; DOI=10.1128/JB.01970-07; RA Namboori S.C., Graham D.E.; RT "Acetamido sugar biosynthesis in the Euryarchaea."; RL J. Bacteriol. 190:2987-2996(2008). CC -!- FUNCTION: Catalyzes the last two sequential reactions in the de CC novo biosynthetic pathway for UDP-N-acetyl-glucosamine (UDP- CC GlcNAc). Responsible for the acetylation of GlcN-1-P to GlcNAc-1- CC P, and for the uridyl transfer from UTP to GlcNAc-1-P, to produce CC UDP-GlcNAc and pyrophosphate. Also catalyzes the reverse reaction, CC i.e. the cleavage of UDP-GlcNAc with pyrophosphate to form UTP and CC GlcNAc-1-P. To a lesser extent, is also able to use dUTP or dTTP CC as the nucleotide substrate, but not CTP, ATP or GTP. CC {ECO:0000269|PubMed:17014089, ECO:0000269|PubMed:18263721}. CC -!- CATALYTIC ACTIVITY: UTP + N-acetyl-alpha-D-glucosamine 1-phosphate CC = diphosphate + UDP-N-acetyl-alpha-D-glucosamine. CC {ECO:0000269|PubMed:18263721}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + alpha-D-glucosamine 1-phosphate = CC CoA + N-acetyl-alpha-D-glucosamine 1-phosphate. CC {ECO:0000269|PubMed:18263721}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:18263721}; CC Temperature dependence: CC Optimum temperature is 50-60 degrees Celsius. Activity is 22% CC lower at 60 degrees Celsius and 60% lower at 100 degrees. CC Thermostable. {ECO:0000269|PubMed:18263721}; CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; N-acetyl-alpha-D-glucosamine 1-phosphate CC from alpha-D-glucosamine 6-phosphate (route II): step 2/2. CC -!- PATHWAY: Nucleotide-sugar biosynthesis; UDP-N-acetyl-alpha-D- CC glucosamine biosynthesis; UDP-N-acetyl-alpha-D-glucosamine from N- CC acetyl-alpha-D-glucosamine 1-phosphate: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the N- CC acetylglucosamine-1-phosphate uridyltransferase family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transferase CC hexapeptide repeat family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99104.1; -; Genomic_DNA. DR PIR; D64437; D64437. DR ProteinModelPortal; Q58501; -. DR STRING; 243232.MJ_1101; -. DR PRIDE; Q58501; -. DR EnsemblBacteria; AAB99104; AAB99104; MJ_1101. DR KEGG; mja:MJ_1101; -. DR eggNOG; arCOG00666; Archaea. DR eggNOG; COG1208; LUCA. DR InParanoid; Q58501; -. DR KO; K04042; -. DR OMA; CNTITAN; -. DR PhylomeDB; Q58501; -. DR UniPathway; UPA00113; UER00532. DR UniPathway; UPA00113; UER00533. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0019134; F:glucosamine-1-phosphate N-acetyltransferase activity; IDA:UniProtKB. DR GO; GO:0003977; F:UDP-N-acetylglucosamine diphosphorylase activity; IDA:UniProtKB. DR GO; GO:0006048; P:UDP-N-acetylglucosamine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR023915; Bifunctiontional_GlmU_arc-type. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR SUPFAM; SSF53448; SSF53448; 2. DR TIGRFAMs; TIGR03992; Arch_glmU; 1. PE 1: Evidence at protein level; KW Acyltransferase; Complete proteome; Multifunctional enzyme; KW Nucleotidyltransferase; Reference proteome; Repeat; Transferase. FT CHAIN 1 408 Bifunctional protein GlmU. FT /FTId=PRO_0000068761. FT NP_BIND 6 9 UTP. {ECO:0000250}. FT REGION 1 202 Pyrophosphorylase. FT REGION 203 222 Linker. FT REGION 223 408 N-acetyltransferase. FT ACT_SITE 306 306 Proton acceptor. {ECO:0000250}. FT BINDING 74 74 UTP. {ECO:0000250}. FT BINDING 79 79 UTP; via amide nitrogen. {ECO:0000250}. FT BINDING 80 80 GlcNAc-1-P. {ECO:0000250}. FT BINDING 130 130 GlcNAc-1-P; via amide nitrogen. FT {ECO:0000250}. FT BINDING 142 142 GlcNAc-1-P. {ECO:0000250}. FT BINDING 156 156 GlcNAc-1-P. {ECO:0000250}. FT BINDING 382 382 Acetyl-CoA; via amide nitrogen. FT {ECO:0000250}. FT BINDING 399 399 Acetyl-CoA. {ECO:0000250}. SQ SEQUENCE 408 AA; 46056 MW; 03280F372CCD299A CRC64; MDAIILCAGK GERLRPLTEN RPKPMIPIAG KPILQHIIEK VEDLVDNIYL IVKYKKEKIV DYFKNHPKIK FLEQGEIDGT GQAVLTAKDY VDDEFLVING DIIFEDDLEE FLKYKYAVAV KEVKNPENFG VVVLDDENNI IELQEKPENP KSNLINAGIY KFDKKIFELI EKTKISERGE RELTDAIKHL IKEEKVKGIK LNGYWNDVGR PWDILEANKY LLDKINTDIK GKIEENVVIK GEVIIEEGAI VKANSVIEGP AIIKKGAVVG PLAYIRPYTV LMENTFVGNS SEVKASIIMK NTKIPHLSYV GDSIIGENCN FGCNTITANL RFDDKPVKVN IKSKRVESVR KLGVIMGDNV KTGIQVSFMP GVKVGSNCWI GASCLIDRDI ESNTFVYKRD ELIFRKLK // ID GLYA_METJA Reviewed; 429 AA. AC Q58992; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Serine hydroxymethyltransferase; DE Short=SHMT; DE Short=Serine methylase; DE EC=2.1.2.-; DE AltName: Full=L-allo-threonine aldolase; DE EC=4.1.2.49; GN Name=glyA; OrderedLocusNames=MJ1597; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, H4MPT-DEPENDENT SERINE HYDROXYMETHYLTRANSFERASE ACTIVITY, RP ALDOLASE ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12902326; DOI=10.1074/jbc.M306747200; RA Angelaccio S., Chiaraluce R., Consalvi V., Buchenau B., RA Giangiacomo L., Bossa F., Contestabile R.; RT "Catalytic and thermodynamic properties of tetrahydromethanopterin- RT dependent serine hydroxymethyltransferase from Methanococcus RT jannaschii."; RL J. Biol. Chem. 278:41789-41797(2003). CC -!- FUNCTION: Catalyzes the reversible interconversion of serine and CC glycine with tetrahydromethanopterin (H4MPT) serving as the one- CC carbon carrier. The use of tetrahydrofolate (THF or H4PteGlu) as CC the pteridine substrate is 450-fold less efficient than that of CC H4MPT. Also exhibits a pteridine-independent aldolase activity CC toward beta-hydroxyamino acids, producing glycine and aldehydes, CC via a retro-aldol mechanism. Thus, is able to catalyze the CC cleavage of L-allo-threonine and L-threo-beta-phenylserine. CC {ECO:0000269|PubMed:12902326}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydromethanopterin + CC glycine + H(2)O = tetrahydromethanopterin + L-serine. CC -!- CATALYTIC ACTIVITY: L-allo-threonine = glycine + acetaldehyde. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|PubMed:12902326}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.8 mM for L-serine (at 37 degrees Celsius) CC {ECO:0000269|PubMed:12902326}; CC KM=0.1 mM for tetrahydromethanopterin (at 37 degrees Celsius) CC {ECO:0000269|PubMed:12902326}; CC KM=1.3 mM for L-allo-threonine (at 60 degrees Celsius) CC {ECO:0000269|PubMed:12902326}; CC KM=95 mM for DL-threo-beta-phenylserine (at 60 degrees Celsius) CC {ECO:0000269|PubMed:12902326}; CC Note=kcat is 212 min(-1) for the L-serine CC hydroxymethyltransferase reaction, and 687 min(-1) for the L- CC allo-threonine cleavage, at 37 and 60 degrees Celsius, CC respectively. The presence of oxygen does not seem to affect CC significantly the kinetic parameters of the reactions.; CC Temperature dependence: CC Optimum temperature is 70-80 degrees Celsius for the retro-aldol CC cleavage of L-allo-threonine. {ECO:0000269|PubMed:12902326}; CC -!- PATHWAY: Amino-acid biosynthesis; glycine biosynthesis; glycine CC from L-serine: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12902326}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the SHMT family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99615.1; -; Genomic_DNA. DR PIR; D64499; D64499. DR PDB; 4BHD; X-ray; 2.83 A; A/B=3-429. DR PDB; 4UQV; X-ray; 3.00 A; A/B/C/D/E/F/G/H/I/J/K/L=1-429. DR PDBsum; 4BHD; -. DR PDBsum; 4UQV; -. DR ProteinModelPortal; Q58992; -. DR STRING; 243232.MJ_1597; -. DR EnsemblBacteria; AAB99615; AAB99615; MJ_1597. DR KEGG; mja:MJ_1597; -. DR eggNOG; arCOG00070; Archaea. DR eggNOG; COG0112; LUCA. DR InParanoid; Q58992; -. DR KO; K00600; -. DR OMA; MYEEANI; -. DR PhylomeDB; Q58992; -. DR UniPathway; UPA00288; UER01023. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004372; F:glycine hydroxymethyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019264; P:glycine biosynthetic process from serine; IEA:UniProtKB-HAMAP. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_00051; SHMT; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR001085; Ser_HO-MeTrfase. DR InterPro; IPR019798; Ser_HO-MeTrfase_PLP_BS. DR PANTHER; PTHR11680; PTHR11680; 1. DR Pfam; PF00464; SHMT; 1. DR PIRSF; PIRSF000412; SHMT; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00096; SHMT; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Lyase; One-carbon metabolism; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 429 Serine hydroxymethyltransferase. FT /FTId=PRO_0000113713. FT REGION 120 122 Substrate binding. {ECO:0000250}. FT BINDING 30 30 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 50 50 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 52 52 Substrate. {ECO:0000250}. FT BINDING 60 60 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 171 171 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 199 199 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 225 225 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 363 363 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 226 226 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT HELIX 3 5 {ECO:0000244|PDB:4UQV}. FT HELIX 6 22 {ECO:0000244|PDB:4BHD}. FT STRAND 24 26 {ECO:0000244|PDB:4BHD}. FT HELIX 36 43 {ECO:0000244|PDB:4BHD}. FT HELIX 45 47 {ECO:0000244|PDB:4UQV}. FT STRAND 60 62 {ECO:0000244|PDB:4UQV}. FT HELIX 65 81 {ECO:0000244|PDB:4BHD}. FT STRAND 84 87 {ECO:0000244|PDB:4BHD}. FT HELIX 93 104 {ECO:0000244|PDB:4BHD}. FT STRAND 111 113 {ECO:0000244|PDB:4BHD}. FT TURN 116 119 {ECO:0000244|PDB:4BHD}. FT HELIX 122 124 {ECO:0000244|PDB:4BHD}. FT TURN 130 132 {ECO:0000244|PDB:4BHD}. FT STRAND 137 139 {ECO:0000244|PDB:4BHD}. FT TURN 144 147 {ECO:0000244|PDB:4BHD}. FT HELIX 151 161 {ECO:0000244|PDB:4BHD}. FT STRAND 164 168 {ECO:0000244|PDB:4BHD}. FT HELIX 179 189 {ECO:0000244|PDB:4BHD}. FT STRAND 192 196 {ECO:0000244|PDB:4BHD}. FT TURN 198 200 {ECO:0000244|PDB:4BHD}. FT HELIX 201 205 {ECO:0000244|PDB:4BHD}. FT HELIX 212 214 {ECO:0000244|PDB:4BHD}. FT STRAND 218 223 {ECO:0000244|PDB:4BHD}. FT STRAND 226 228 {ECO:0000244|PDB:4BHD}. FT STRAND 234 238 {ECO:0000244|PDB:4BHD}. FT HELIX 240 249 {ECO:0000244|PDB:4BHD}. FT STRAND 250 254 {ECO:0000244|PDB:4UQV}. FT HELIX 262 296 {ECO:0000244|PDB:4BHD}. FT TURN 297 299 {ECO:0000244|PDB:4BHD}. FT HELIX 305 307 {ECO:0000244|PDB:4BHD}. FT STRAND 311 319 {ECO:0000244|PDB:4BHD}. FT TURN 323 325 {ECO:0000244|PDB:4BHD}. FT HELIX 329 338 {ECO:0000244|PDB:4BHD}. FT STRAND 344 346 {ECO:0000244|PDB:4BHD}. FT STRAND 360 365 {ECO:0000244|PDB:4BHD}. FT HELIX 367 371 {ECO:0000244|PDB:4BHD}. FT HELIX 376 390 {ECO:0000244|PDB:4BHD}. FT HELIX 396 408 {ECO:0000244|PDB:4BHD}. FT STRAND 415 418 {ECO:0000244|PDB:4BHD}. FT STRAND 421 423 {ECO:0000244|PDB:4UQV}. SQ SEQUENCE 429 AA; 48084 MW; C115CECA4E649C7A CRC64; MEYSDVPKFI RDVSIKQHEW MRESIKLIAS ENITSLAVRE ACATDFMHRY AEGLPGKRLY QGCKYIDEVE TLCIELSKEL FKAEHANVQP TSGVVANLAV FFAETKPGDK LMALSVPDGG HISHWKVSAA GIRGLKVINH PFDPEEMNID ADAMVKKILE EKPKLILFGG SLFPFPHPVA DAYEAAQEVG AKIAYDGAHV LGLIAGKQFQ DPLREGAEYL MGSTHKTFFG PQGGVILTTK ENADKIDSHV FPGVVSNHHL HHKAGLAIAL AEMLEFGEAY AKQVIKNAKA LAQALYERGF NVLCEHKDFT ESHQVIIDIE SSPDIEFSAS ELAKMYEEAN IILNKNLLPW DDVNNSDNPS GIRLGTQECT RLGMKEKEME EIAEFMKRIA IDKEKPEKVR EDVKEFAKEY STIHYSFDEG DGFKYLRFY // ID GSA_METJA Reviewed; 426 AA. AC Q58020; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 17-FEB-2016, entry version 106. DE RecName: Full=Glutamate-1-semialdehyde 2,1-aminomutase; DE Short=GSA; DE EC=5.4.3.8; DE AltName: Full=Glutamate-1-semialdehyde aminotransferase; DE Short=GSA-AT; GN Name=hemL; OrderedLocusNames=MJ0603; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: (S)-4-amino-5-oxopentanoate = 5- CC aminolevulinate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent CC aminotransferase family. HemL subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98593.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98593.1; ALT_INIT; Genomic_DNA. DR PIR; C64375; C64375. DR ProteinModelPortal; Q58020; -. DR STRING; 243232.MJ_0603; -. DR EnsemblBacteria; AAB98593; AAB98593; MJ_0603. DR KEGG; mja:MJ_0603; -. DR eggNOG; arCOG00918; Archaea. DR eggNOG; COG0001; LUCA. DR InParanoid; Q58020; -. DR KO; K01845; -. DR OMA; CGHAHPE; -. DR PhylomeDB; Q58020; -. DR UniPathway; UPA00251; UER00317. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0042286; F:glutamate-1-semialdehyde 2,1-aminomutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042802; F:identical protein binding; IBA:GO_Central. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0008483; F:transaminase activity; IEA:InterPro. DR GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IBA:GO_Central. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 2. DR HAMAP; MF_00375; HemL_aminotrans_3; 1. DR InterPro; IPR004639; 4pyrrol_synth_GluAld_NH2Trfase. DR InterPro; IPR005814; Aminotrans_3. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR PANTHER; PTHR11986; PTHR11986; 1. DR Pfam; PF00202; Aminotran_3; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR00713; hemL; 1. DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Isomerase; Porphyrin biosynthesis; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1 426 Glutamate-1-semialdehyde 2,1-aminomutase. FT /FTId=PRO_0000120482. FT MOD_RES 266 266 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 426 AA; 47451 MW; DDFFC01FCF52080C CRC64; MALKMDKSKE LFEEAKKYLV GGVNSPVRYF KPYPFFVEKA KDCYLFDVDG NCYIDYCLAY GPMVLGHAND AVIKAVKEQL ELGSAYGCPT EKEIILAKEV VKRVPCAEMV RFVNSGTEAT MSAIRLARGV TGRKKIIKFD GAYHGAHDYV LVKSGSGALT HGHPNSPGIP EETTKNTILI PFNDEDAVKK AINENKDEIA CIIVEPIMGN VGCILPKEGY LEFLREITEE NDILLIFDEV ITGFRLAKGG AQEYFGVVPD IATLGKILGG GFPIGAIVGR RELMEQFSPL GAIYQAGTFN GNPISITAGI ATLKQLDDRF YKETARTAKI LADTLRELAD KHNIKAKVYN IASMFQIYFN DKEVVNYEIA KQSDTEKFMK YFWRLLEKGV FVPPSQFECC FTSIKHDDEV VDKTIKAMED VFEGLE // ID GUAAA_METJA Reviewed; 188 AA. AC Q58970; DT 01-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit A {ECO:0000255|HAMAP-Rule:MF_01510}; DE EC=6.3.5.2 {ECO:0000255|HAMAP-Rule:MF_01510}; DE AltName: Full=Glutamine amidotransferase {ECO:0000255|HAMAP-Rule:MF_01510}; GN Name=guaAA {ECO:0000255|HAMAP-Rule:MF_01510}; GN OrderedLocusNames=MJ1575; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. CC {ECO:0000255|HAMAP-Rule:MF_01510}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. {ECO:0000255|HAMAP- CC Rule:MF_01510}. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01510}. CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase CC subunit (A) and a GMP-binding subunit (B). {ECO:0000255|HAMAP- CC Rule:MF_01510}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_01510}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99597.1; -; Genomic_DNA. DR PIR; F64496; F64496. DR PDB; 2LXN; NMR; -; A=1-188. DR PDBsum; 2LXN; -. DR ProteinModelPortal; Q58970; -. DR STRING; 243232.MJ_1575; -. DR MEROPS; C26.A31; -. DR EnsemblBacteria; AAB99597; AAB99597; MJ_1575. DR KEGG; mja:MJ_1575; -. DR eggNOG; arCOG00087; Archaea. DR eggNOG; COG0518; LUCA. DR InParanoid; Q58970; -. DR KO; K01951; -. DR OMA; GGPDMDR; -. DR PhylomeDB; Q58970; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01510; GMP_synthase_A; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR004739; GMP_synth_N. DR InterPro; IPR023686; GMP_synthase_A. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00888; guaA_Nterm; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; KW Glutamine amidotransferase; GMP biosynthesis; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 188 GMP synthase [glutamine-hydrolyzing] FT subunit A. FT /FTId=PRO_0000140221. FT DOMAIN 1 188 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_01510}. FT ACT_SITE 76 76 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01510}. FT ACT_SITE 163 163 {ECO:0000255|HAMAP-Rule:MF_01510}. FT ACT_SITE 165 165 {ECO:0000255|HAMAP-Rule:MF_01510}. FT STRAND 2 5 {ECO:0000244|PDB:2LXN}. FT HELIX 13 22 {ECO:0000244|PDB:2LXN}. FT STRAND 26 29 {ECO:0000244|PDB:2LXN}. FT STRAND 31 33 {ECO:0000244|PDB:2LXN}. FT HELIX 36 39 {ECO:0000244|PDB:2LXN}. FT STRAND 47 49 {ECO:0000244|PDB:2LXN}. FT HELIX 61 66 {ECO:0000244|PDB:2LXN}. FT STRAND 72 75 {ECO:0000244|PDB:2LXN}. FT HELIX 78 86 {ECO:0000244|PDB:2LXN}. FT STRAND 90 93 {ECO:0000244|PDB:2LXN}. FT STRAND 100 103 {ECO:0000244|PDB:2LXN}. FT STRAND 109 112 {ECO:0000244|PDB:2LXN}. FT STRAND 117 122 {ECO:0000244|PDB:2LXN}. FT STRAND 126 129 {ECO:0000244|PDB:2LXN}. FT STRAND 134 140 {ECO:0000244|PDB:2LXN}. FT STRAND 142 144 {ECO:0000244|PDB:2LXN}. FT STRAND 148 152 {ECO:0000244|PDB:2LXN}. FT TURN 153 156 {ECO:0000244|PDB:2LXN}. FT STRAND 157 162 {ECO:0000244|PDB:2LXN}. FT STRAND 166 169 {ECO:0000244|PDB:2LXN}. FT TURN 170 172 {ECO:0000244|PDB:2LXN}. FT HELIX 173 182 {ECO:0000244|PDB:2LXN}. SQ SEQUENCE 188 AA; 21020 MW; 3F1DDB0FA1F2D850 CRC64; MIVILDNGGQ YVHRIHRSLK YIGVSSKIVP NTTPLEEIES NKEVKGIILS GGPDIEKAKN CIDIALNAKL PILGICLGHQ LIALAYGGEV GRAEAEEYAL TKVYVDKEND LFKNVPREFN AWASHKDEVK KVPEGFEILA HSDICQVEAM KHKTKPIYGV QFHPEVAHTE YGNEILKNFC KVCGYKFE // ID H669_METJA Reviewed; 367 AA. AC Q58083; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=Probable ATP-dependent RNA helicase MJ0669; DE EC=3.6.4.13; GN OrderedLocusNames=MJ0669; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=11171974; DOI=10.1073/pnas.98.4.1465; RA Story R.M., Li H., Abelson J.N.; RT "Crystal structure of a DEAD box protein from the hyperthermophile RT Methanococcus jannaschii."; RL Proc. Natl. Acad. Sci. U.S.A. 98:1465-1470(2001). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98663.1; -; Genomic_DNA. DR PIR; E64383; E64383. DR PDB; 1HV8; X-ray; 3.00 A; A/B=1-367. DR PDBsum; 1HV8; -. DR ProteinModelPortal; Q58083; -. DR SMR; Q58083; 3-365. DR STRING; 243232.MJ_0669; -. DR EnsemblBacteria; AAB98663; AAB98663; MJ_0669. DR KEGG; mja:MJ_0669; -. DR eggNOG; arCOG00558; Archaea. DR eggNOG; COG0513; LUCA. DR InParanoid; Q58083; -. DR KO; K05592; -. DR OMA; KYENHTA; -. DR PhylomeDB; Q58083; -. DR EvolutionaryTrace; Q58083; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR000629; RNA-helicase_DEAD-box_CS. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00039; DEAD_ATP_HELICASE; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 367 Probable ATP-dependent RNA helicase FT MJ0669. FT /FTId=PRO_0000055116. FT DOMAIN 38 206 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 213 367 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 51 58 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 6 34 Q motif. FT MOTIF 154 157 DEAD box. FT HELIX 8 10 {ECO:0000244|PDB:1HV8}. FT HELIX 15 24 {ECO:0000244|PDB:1HV8}. FT HELIX 31 42 {ECO:0000244|PDB:1HV8}. FT STRAND 45 50 {ECO:0000244|PDB:1HV8}. FT STRAND 53 56 {ECO:0000244|PDB:1HV8}. FT HELIX 57 68 {ECO:0000244|PDB:1HV8}. FT STRAND 71 74 {ECO:0000244|PDB:1HV8}. FT STRAND 77 80 {ECO:0000244|PDB:1HV8}. FT HELIX 84 98 {ECO:0000244|PDB:1HV8}. FT STRAND 105 108 {ECO:0000244|PDB:1HV8}. FT HELIX 114 122 {ECO:0000244|PDB:1HV8}. FT STRAND 125 129 {ECO:0000244|PDB:1HV8}. FT HELIX 131 139 {ECO:0000244|PDB:1HV8}. FT STRAND 150 155 {ECO:0000244|PDB:1HV8}. FT HELIX 156 160 {ECO:0000244|PDB:1HV8}. FT TURN 161 164 {ECO:0000244|PDB:1HV8}. FT HELIX 165 173 {ECO:0000244|PDB:1HV8}. FT STRAND 180 184 {ECO:0000244|PDB:1HV8}. FT HELIX 190 199 {ECO:0000244|PDB:1HV8}. FT STRAND 202 207 {ECO:0000244|PDB:1HV8}. FT STRAND 210 220 {ECO:0000244|PDB:1HV8}. FT HELIX 223 225 {ECO:0000244|PDB:1HV8}. FT HELIX 226 234 {ECO:0000244|PDB:1HV8}. FT STRAND 241 244 {ECO:0000244|PDB:1HV8}. FT HELIX 248 260 {ECO:0000244|PDB:1HV8}. FT STRAND 265 268 {ECO:0000244|PDB:1HV8}. FT STRAND 270 272 {ECO:0000244|PDB:1HV8}. FT HELIX 274 285 {ECO:0000244|PDB:1HV8}. FT STRAND 288 294 {ECO:0000244|PDB:1HV8}. FT HELIX 298 301 {ECO:0000244|PDB:1HV8}. FT STRAND 308 314 {ECO:0000244|PDB:1HV8}. FT HELIX 319 325 {ECO:0000244|PDB:1HV8}. FT STRAND 332 334 {ECO:0000244|PDB:1HV8}. FT STRAND 337 342 {ECO:0000244|PDB:1HV8}. FT HELIX 347 357 {ECO:0000244|PDB:1HV8}. SQ SEQUENCE 367 AA; 41920 MW; 1B9102E8DF50CB37 CRC64; MEVEYMNFNE LNLSDNILNA IRNKGFEKPT DIQMKVIPLF LNDEYNIVAQ ARTGSGKTAS FAIPLIELVN ENNGIEAIIL TPTRELAIQV ADEIESLKGN KNLKIAKIYG GKAIYPQIKA LKNANIVVGT PGRILDHINR GTLNLKNVKY FILDEADEML NMGFIKDVEK ILNACNKDKR ILLFSATMPR EILNLAKKYM GDYSFIKAKI NANIEQSYVE VNENERFEAL CRLLKNKEFY GLVFCKTKRD TKELASMLRD IGFKAGAIHG DLSQSQREKV IRLFKQKKIR ILIATDVMSR GIDVNDLNCV INYHLPQNPE SYMHRIGRTG RAGKKGKAIS IINRREYKKL RYIERAMKLK IKKLKFG // ID HCP_METJA Reviewed; 539 AA. AC Q58175; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=Hydroxylamine reductase {ECO:0000255|HAMAP-Rule:MF_00069}; DE EC=1.7.99.1 {ECO:0000255|HAMAP-Rule:MF_00069}; DE AltName: Full=Hybrid-cluster protein {ECO:0000255|HAMAP-Rule:MF_00069}; DE Short=HCP {ECO:0000255|HAMAP-Rule:MF_00069}; DE AltName: Full=Prismane protein {ECO:0000255|HAMAP-Rule:MF_00069}; GN Name=hcp {ECO:0000255|HAMAP-Rule:MF_00069}; OrderedLocusNames=MJ0765; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reduction of hydroxylamine to form NH(3) CC and H(2)O. {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- CATALYTIC ACTIVITY: NH(3) + H(2)O + acceptor = hydroxylamine + CC reduced acceptor. {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00069}; CC -!- COFACTOR: CC Name=hybrid [4Fe-2O-2S] cluster; Xref=ChEBI:CHEBI:60519; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00069}; CC Note=Binds 1 hybrid [4Fe-2O-2S] cluster. {ECO:0000255|HAMAP- CC Rule:MF_00069}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00069}. CC -!- SIMILARITY: Belongs to the HCP family. {ECO:0000255|HAMAP- CC Rule:MF_00069}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98761.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98761.1; ALT_INIT; Genomic_DNA. DR PIR; E64395; E64395. DR ProteinModelPortal; Q58175; -. DR SMR; Q58175; 1-537. DR STRING; 243232.MJ_0765; -. DR EnsemblBacteria; AAB98761; AAB98761; MJ_0765. DR KEGG; mja:MJ_0765; -. DR eggNOG; arCOG02430; Archaea. DR eggNOG; COG1151; LUCA. DR InParanoid; Q58175; -. DR KO; K05601; -. DR OMA; CAYAQGM; -. DR PhylomeDB; Q58175; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050418; F:hydroxylamine reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.20.1270.20; -; 2. DR Gene3D; 3.40.50.2030; -; 2. DR HAMAP; MF_00069; Hydroxylam_reduct; 1. DR InterPro; IPR004137; HCP/CODH. DR InterPro; IPR010048; Hydroxylam_reduct. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR016099; Prismane-like_a/b-sand. DR InterPro; IPR016100; Prismane_a-bundle. DR Pfam; PF03063; Prismane; 1. DR PIRSF; PIRSF000076; HCP; 1. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR01703; hybrid_clust; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 539 Hydroxylamine reductase. FT /FTId=PRO_0000151691. FT METAL 3 3 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 6 6 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 15 15 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 21 21 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 68 68 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 235 235 Iron-oxo-sulfur (4Fe-2O-2S); via tele FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 259 259 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 303 303 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 394 394 Iron-oxo-sulfur (4Fe-2O-2S); via FT persulfide group. {ECO:0000255|HAMAP- FT Rule:MF_00069}. FT METAL 422 422 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 447 447 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 482 482 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT METAL 484 484 Iron-oxo-sulfur (4Fe-2O-2S). FT {ECO:0000255|HAMAP-Rule:MF_00069}. FT MOD_RES 394 394 Cysteine persulfide. {ECO:0000255|HAMAP- FT Rule:MF_00069}. SQ SEQUENCE 539 AA; 60458 MW; 46442DD4FCBCE5A5 CRC64; MFCFQCQEAA KNEGCTIKGV CGKDDVVANL QDLLIYTIKG LCYVCDKGNY LDDEVMDYIP KALFVTITNV NFDDKDVINW IKKGVALREK IIEKNNLNKE ELPYCATWAY ETDEDLINLA NTKEVSVLAE DNEDIRSLKE LITYGIKGIG AYLSHAMHLG YNNEDIHKFI IKAFTKIVDS KDADELFNLA METGKYAVET LALLDKANTE TYGHPEITEV NLGVRDRPGI LISGHDLKDL EQLLEQSKDA GVDIYTHCEM LPAHYYPFFK KYEHFVGNYG GSWPFQREEF EKFNGPIVMT TNCLVPPKDS YKDRVYVTNE VGYPGLKRIP VKEDGTKDFS EVIEHAKKCK PPTPLENGKI VGGFAHNQVL ALADKVIEAV KSGKIRKFVV MAGCDGRHKT REYYTEFAKK LPKDTVILTC GCAKYRFIKL DLGDIDGIPR VLDAGQCNDS YSLVKIALAL KDAFGLNDVN ELPIAYNISW YEQKAVTVLL ALLYLGVKNI VLGPTLPAFL SPNVTKVLVE KFGISTISTV DEDIKRLVG // ID HDRA_METJA Reviewed; 657 AA. AC P60200; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-MAY-2016, entry version 80. DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit A; DE EC=1.8.98.1; GN Name=hdrA; OrderedLocusNames=MJ1190; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-196. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- FUNCTION: Part of a complex that catalyzes the reversible CC reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme CC M) and H-S-CoB (coenzyme B). May act as the catalytic subunit (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = CC N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + CC dihydromethanophenazine. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B CC heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme CC M-coenzyme B heterodisulfide: step 1/1. CC -!- SUBUNIT: The heterodisulfide reductase is composed of three CC subunits; HdrA, HdrB and HdrC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HdrA family. {ECO:0000305}. CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PRIDE; P60200; -. DR InParanoid; P60200; -. DR OMA; CTPKIHE; -. DR PhylomeDB; P60200; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IDA:MENGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.50.50.60; -; 4. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF13187; Fer4_9; 1. DR Pfam; PF07992; Pyr_redox_2; 1. DR SUPFAM; SSF51905; SSF51905; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 4. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; FAD; Flavoprotein; Iron; Iron-sulfur; KW Metal-binding; Methanogenesis; Oxidoreductase; Reference proteome; KW Repeat; Selenocysteine. FT CHAIN 1 657 CoB--CoM heterodisulfide reductase iron- FT sulfur subunit A. FT /FTId=PRO_0000150057. FT DOMAIN 235 266 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 283 312 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 574 603 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 607 636 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT NP_BIND 149 172 FAD. {ECO:0000255}. FT METAL 245 245 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 248 248 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 251 251 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 255 255 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 292 292 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 295 295 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 298 298 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 302 302 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 583 583 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 586 586 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 589 589 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT METAL 593 593 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 616 616 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 619 619 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 622 622 Iron-sulfur 4 (4Fe-4S). {ECO:0000255}. FT METAL 626 626 Iron-sulfur 3 (4Fe-4S). {ECO:0000255}. FT NON_STD 196 196 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 657 AA; 71922 MW; D3607042434DBC32 CRC64; MSPRVGVFVC YCGANINGVV DCEAVRDFAE KLDGVVVAKT YPFMCADPGQ NLIKEAIKEY NLDRVVVAAC TPKIHEPTFR NCIKEAGLSP YYLEFVNIRE HCSFVHMNDR EKATKKAMEL VAGAVERAKR LEDVPQKIVE VDKSCLIIGG GIAGIQAALD LGDQGYKVYL VEKEPSIGGR MAQLAKTFPT DDCALUILAP KMVSVANHPN VELITYAEVK NVEGFIGNFE VTIEKKPRYV DENICTGCGA CAAVCPIEVP NEFDLGLGTR KAIYVPFAQA VPLVYTIDMD HCIRCGLCEK ACGPGAIRYD QKPEEIKLKV GTIICAVGYD EFDATLKEEY GYGVYDNVIT TLELERMINP AGPTGGHEIR PSDGKHPHRV VFIQCVGSRD AKVGKHYCSR ICCMFALKNA QLIKQHDPST EVYICYMDIR SFGKGYEEYY RRAQEQFGVK FIRGRPACIM EDPETKNLIV RVEDTLLGEI VEIEADLVVL SAGLSPRPDN PKLAKMLGLE LSPDGFFKEL HPKLAPVNTK VDGIAIAGVA QGPKDIPDTV AQAKGAASAV SIPMAQGQFR IEMIRAVVDE DVCGGCQVCA KMCPYNAITY VEKDGHLVAQ VNDVACKGCG SCAGACPSGA MQLRYYRDEQ IISFIDGVLE AHQKLES // ID HDRB1_METJA Reviewed; 294 AA. AC Q58153; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=CoB--CoM heterodisulfide reductase subunit B 1; DE EC=1.8.98.1; GN Name=hdrB1; OrderedLocusNames=MJ0743; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible CC reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme CC M) and H-S-CoB (coenzyme B). HdrB may have a function in energy CC transduction (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = CC N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + CC dihydromethanophenazine. CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B CC heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme CC M-coenzyme B heterodisulfide: step 1/1. CC -!- SUBUNIT: The heterodisulfide reductase is composed of three CC subunits; HdrA, HdrB and HdrC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98737.1; -; Genomic_DNA. DR PIR; G64392; G64392. DR STRING; 243232.MJ_0743; -. DR EnsemblBacteria; AAB98737; AAB98737; MJ_0743. DR KEGG; mja:MJ_0743; -. DR eggNOG; arCOG00338; Archaea. DR eggNOG; COG2048; LUCA. DR InParanoid; Q58153; -. DR KO; K03389; -. DR OMA; HFISADP; -. DR PhylomeDB; Q58153; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0051186; P:cofactor metabolic process; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR017678; CoB/CoM_hetero-S_Rdtase_bsu. DR InterPro; IPR004017; Cys_rich_dom. DR Pfam; PF02754; CCG; 2. DR TIGRFAMs; TIGR03288; CoB_CoM_SS_B; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Oxidoreductase; Reference proteome. FT CHAIN 1 294 CoB--CoM heterodisulfide reductase FT subunit B 1. FT /FTId=PRO_0000150065. SQ SEQUENCE 294 AA; 33310 MW; C8D5DDCE6FDC8560 CRC64; MEFVFFLGCI APNRYPGIEK ATYITMEKLG IKLHPFEKAS CCPAPGVFGS FDLKTWLTLA ARNLCMAEEV EMDILTICNG CYGSLYEANH LLKENEKARK MVNEILSKYG LEYKGKVRVR HLPEVLYYDL GVDRIKEEIT NPLNVNVAVH YGCHYLKPTD IKKLESSERP RSFDELVEAL GAVSVNYKDK NMCCGAGGGV RARNLDVALK MTKTKLENIK EAKADCITEV CPFCHLQFDR GQVEIKEKFG EEYNIPVIHY SQLLGLAMGM SPKDVALDLH FIPTDEFIKK IDRH // ID HDRC1_METJA Reviewed; 194 AA. AC Q58154; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit C 1; DE EC=1.8.98.1; GN Name=hdrC1; OrderedLocusNames=MJ0744; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible CC reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme CC M) and H-S-CoB (coenzyme B). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = CC N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + CC dihydromethanophenazine. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B CC heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme CC M-coenzyme B heterodisulfide: step 1/1. CC -!- SUBUNIT: The heterodisulfide reductase is composed of three CC subunits; HdrA, HdrB and HdrC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98738.1; -; Genomic_DNA. DR PIR; H64392; H64392. DR ProteinModelPortal; Q58154; -. DR STRING; 243232.MJ_0744; -. DR EnsemblBacteria; AAB98738; AAB98738; MJ_0744. DR KEGG; mja:MJ_0744; -. DR eggNOG; arCOG00964; Archaea. DR eggNOG; COG1150; LUCA. DR InParanoid; Q58154; -. DR KO; K03390; -. DR OMA; WLCTTCY; -. DR PhylomeDB; Q58154; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051186; P:cofactor metabolic process; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR017680; CoB/CoM_hetero-S_Rdtase_csu. DR InterPro; IPR009051; Helical_ferredxn. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR03290; CoB_CoM_SS_C; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 194 CoB--CoM heterodisulfide reductase iron- FT sulfur subunit C 1. FT /FTId=PRO_0000150073. FT DOMAIN 25 55 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 67 98 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 35 35 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 38 38 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 41 41 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 45 45 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 79 79 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 82 82 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 85 85 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 89 89 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 194 AA; 22016 MW; 8871167DFD0C83AD CRC64; MVIYAQKDIS NDFIKEIIKT GEILGEGHVS SFKACYQCGT CTGSCPSGRI TAFRTRKLIR YAQFGMKSAI IDSEDLWMCT TCYECYERCP RTVKITDIIK VLRNIAAREG KMAEAHKKTA LYVFKTGHAV PINDQIKKAR KEIGLTEIPP TTHKYPDALE VVRGIMKDLR FCDMVGICTE TMQLKPVEWK DMSE // ID HEM1_METJA Reviewed; 392 AA. AC Q60172; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 115. DE RecName: Full=Glutamyl-tRNA reductase {ECO:0000255|HAMAP-Rule:MF_00087}; DE Short=GluTR {ECO:0000255|HAMAP-Rule:MF_00087}; DE EC=1.2.1.70 {ECO:0000255|HAMAP-Rule:MF_00087}; GN Name=hemA {ECO:0000255|HAMAP-Rule:MF_00087}; OrderedLocusNames=MJ0143; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the NADPH-dependent reduction of glutamyl- CC tRNA(Glu) to glutamate 1-semialdehyde (GSA). {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- CATALYTIC ACTIVITY: L-glutamate 1-semialdehyde + NADP(+) + CC tRNA(Glu) = L-glutamyl-tRNA(Glu) + NADPH. {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; 5-aminolevulinate from L-glutamyl-tRNA(Glu): step CC 1/2. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- DOMAIN: Possesses an unusual extended V-shaped dimeric structure CC with each monomer consisting of three distinct domains arranged CC along a curved 'spinal' alpha-helix. The N-terminal catalytic CC domain specifically recognizes the glutamate moiety of the CC substrate. The second domain is the NADPH-binding domain, and the CC third C-terminal domain is responsible for dimerization. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC -!- MISCELLANEOUS: During catalysis, the active site Cys acts as a CC nucleophile attacking the alpha-carbonyl group of tRNA-bound CC glutamate with the formation of a thioester intermediate between CC enzyme and glutamate, and the concomitant release of tRNA(Glu). CC The thioester intermediate is finally reduced by direct hydride CC transfer from NADPH, to form the product GSA. {ECO:0000255|HAMAP- CC Rule:MF_00087}. CC -!- SIMILARITY: Belongs to the glutamyl-tRNA reductase family. CC {ECO:0000255|HAMAP-Rule:MF_00087}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98126.1; -; Genomic_DNA. DR PIR; H64317; H64317. DR ProteinModelPortal; Q60172; -. DR STRING; 243232.MJ_0143; -. DR PRIDE; Q60172; -. DR EnsemblBacteria; AAB98126; AAB98126; MJ_0143. DR KEGG; mja:MJ_0143; -. DR eggNOG; arCOG01036; Archaea. DR eggNOG; COG0373; LUCA. DR InParanoid; Q60172; -. DR KO; K02492; -. DR OMA; GMDSMIL; -. DR PhylomeDB; Q60172; -. DR UniPathway; UPA00251; UER00316. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008883; F:glutamyl-tRNA reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00087; Glu_tRNA_reductase; 1. DR InterPro; IPR000343; 4pyrrol_synth_GluRdtase. DR InterPro; IPR015896; 4pyrrol_synth_GluRdtase_dimer. DR InterPro; IPR015895; 4pyrrol_synth_GluRdtase_N. DR InterPro; IPR018214; GluRdtase_CS. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006151; Shikm_DH/Glu-tRNA_Rdtase. DR Pfam; PF00745; GlutR_dimer; 1. DR Pfam; PF05201; GlutR_N; 1. DR Pfam; PF01488; Shikimate_DH; 1. DR PIRSF; PIRSF000445; 4pyrrol_synth_GluRdtase; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF69075; SSF69075; 1. DR SUPFAM; SSF69742; SSF69742; 1. DR TIGRFAMs; TIGR01035; hemA; 1. DR PROSITE; PS00747; GLUTR; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Porphyrin biosynthesis; KW Reference proteome. FT CHAIN 1 392 Glutamyl-tRNA reductase. FT /FTId=PRO_0000114101. FT NP_BIND 165 170 NADP. {ECO:0000255|HAMAP-Rule:MF_00087}. FT REGION 38 41 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT REGION 91 93 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT ACT_SITE 39 39 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT BINDING 86 86 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT BINDING 97 97 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00087}. FT SITE 76 76 Important for activity. FT {ECO:0000255|HAMAP-Rule:MF_00087}. SQ SEQUENCE 392 AA; 44847 MW; 952E1CFDCDA3874C CRC64; MIILKADYKK YNVSELEKLR MDEEKFYETF DNAILLQTCN RVEIIFDADS LEEIKGIENI DLEKFDILFG DKAIEHLFRV ACGLESMIVG EDQILGQLKN AYLKAKEKGR ISKKLEKIIL KAIHTGQRAR VETKINEGGV SIGSAAVELA EKIFGLEGKN VLLIGAGEMA NLVIKALKEK NIKAIIVANR TYEKAEKLAK ELGGMAIKFD KLEEALRYAD IVISATGAPH PILNKERLKN AGKTIIIDIA NPRDTTDDIR ELPDIFLFTI DDLRLVAEEN LKKRKEEIPK VEMIICEELE RLKEFLDKMR FETAIKELGQ YIENVRKKEV EKAKKILKNK NKPVEEVLED FSKALCKRII YDIIKIFENV EDKEVFECLA KEFKKLGNKN KN // ID GUAAB_METJA Reviewed; 310 AA. AC Q58531; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=GMP synthase [glutamine-hydrolyzing] subunit B; DE EC=6.3.5.2; DE AltName: Full=GMP synthetase; GN Name=guaAB; OrderedLocusNames=MJ1131; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the synthesis of GMP from XMP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + XMP + L-glutamine + H(2)O = AMP + CC diphosphate + GMP + L-glutamate. CC -!- PATHWAY: Purine metabolism; GMP biosynthesis; GMP from XMP (L-Gln CC route): step 1/1. CC -!- SUBUNIT: Heterodimer composed of a glutamine amidotransferase CC subunit (A) and a GMP-binding subunit (B). {ECO:0000305}. CC -!- SIMILARITY: Contains 1 GMPS ATP-PPase (ATP pyrophosphatase) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99133.1; -; Genomic_DNA. DR PIR; B64441; B64441. DR ProteinModelPortal; Q58531; -. DR SMR; Q58531; 3-310. DR STRING; 243232.MJ_1131; -. DR EnsemblBacteria; AAB99133; AAB99133; MJ_1131. DR KEGG; mja:MJ_1131; -. DR eggNOG; arCOG00085; Archaea. DR eggNOG; COG0519; LUCA. DR InParanoid; Q58531; -. DR KO; K01951; -. DR OMA; GGIKSHH; -. DR PhylomeDB; Q58531; -. DR UniPathway; UPA00189; UER00296. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003922; F:GMP synthase (glutamine-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016462; F:pyrophosphatase activity; IEA:InterPro. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00345; GMP_synthase_B; 1. DR InterPro; IPR001674; GMP_synth_C. DR InterPro; IPR026598; GMP_synthase_B. DR InterPro; IPR025777; GMPS_ATP_PPase_dom. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00958; GMP_synt_C; 1. DR Pfam; PF02540; NAD_synthase; 1. DR TIGRFAMs; TIGR00884; guaA_Cterm; 1. DR PROSITE; PS51553; GMPS_ATP_PPASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; GMP biosynthesis; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 310 GMP synthase [glutamine-hydrolyzing] FT subunit B. FT /FTId=PRO_0000140241. FT DOMAIN 2 185 GMPS ATP-PPase. FT NP_BIND 29 35 ATP. {ECO:0000250}. SQ SEQUENCE 310 AA; 34806 MW; 77F966F92FC62B12 CRC64; MFDPKKFIDE AVEEIKQQIS DRKAIIALSG GVDSSVAAVL THKAIGDKLT AVFVDTGLMR KGEREEVEKT FRDKLGLNLI VVDAKDRFLN ALKGVTDPEE KRKIIGKLFI DVFEEIAEDI KAEVLVQGTI APDWIETQGK IKSHHNVALP HGMVLEVVEP LRELYKDEVR LLAKELGLPD SIVYRQPFPG PGLAVRVLGE VTEEKLNICR EANAIVEEEV KKANLDKDLW QYFAVVLDCK ATGVKGDERE YNWIVALRMV KSLDAMTAHV PEIPFDLLKR ISKRITSEIP NVARVVFDIT DKPPATIEFE // ID HACB_METJA Reviewed; 170 AA. AC Q58667; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Methanogen homoaconitase small subunit; DE Short=HACN; DE EC=4.2.1.114; DE AltName: Full=Homoaconitate hydratase; GN Name=hacB; OrderedLocusNames=MJ1271; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PUTATIVE FUNCTION AS A HOMOACONITASE, LACK OF FUNCTION AS A RP ISOPROPYLMALATE ISOMERASE, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17449626; DOI=10.1128/JB.00166-07; RA Drevland R.M., Waheed A., Graham D.E.; RT "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in RT Methanocaldococcus jannaschii."; RL J. Bacteriol. 189:4391-4400(2007). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18765671; DOI=10.1074/jbc.M802159200; RA Drevland R.M., Jia Y., Palmer D.R.J., Graham D.E.; RT "Methanogen homoaconitase catalyzes both hydrolyase reactions in RT coenzyme B biosynthesis."; RL J. Biol. Chem. 283:28888-28896(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS), FUNCTION, SUBSTRATE RP SPECIFICITY, KINETIC PARAMETERS, AND MUTAGENESIS OF ARG-26 AND THR-27. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=20170198; DOI=10.1021/bi901766z; RA Jeyakanthan J., Drevland R.M., Gayathri D.R., Velmurugan D., RA Shinkai A., Kuramitsu S., Yokoyama S., Graham D.E.; RT "Substrate specificity determinants of the methanogen homoaconitase RT enzyme: structure and function of the small subunit."; RL Biochemistry 49:2687-2696(2010). CC -!- FUNCTION: Hydro-lyase with broad substrate specificity for cis- CC unsaturated tricarboxylic acids. Catalyzes both the reversible CC dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- CC tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- CC tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- CC hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the CC analogous longer chain substrates cis-homo(2)-aconitate, cis- CC homo(3)-aconitate, and even the non-physiological cis-homo(4)- CC aconitate with similar efficiency. These reactions are part of the CC biosynthesis pathway of coenzyme B. Can also catalyze the CC hydration of maleate to (R)-malate, and that of cis-aconitate. Can CC not catalyze the hydration of citraconate and the dehydration of CC (S)-homocitrate, citramalate, 2-isopropylmalate, 3- CC isopropylmalate, citrate or threo-DL-isocitrate. CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}. CC -!- CATALYTIC ACTIVITY: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = CC (Z)-but-1-ene-1,2,4-tricarboxylate + H(2)O. CC {ECO:0000269|PubMed:18765671}. CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxybutane-1,2,4-tricarboxylate = CC (Z)-but-1-ene-1,2,4-tricarboxylate + H(2)O. CC {ECO:0000269|PubMed:18765671}. CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxybutane-1,2,4-tricarboxylate = CC (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate. CC {ECO:0000269|PubMed:18765671}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=22 uM for cis-homoaconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=30 uM for cis-homo(2)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=36 uM for cis-homo(3)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=175 uM for cis-homo(4)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=330 uM for maleate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=1500 uM for (R)-homocitrate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=300 uM for cis-aconitate {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.68 umol/min/mg enzyme for cis-homoaconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.60 umol/min/mg enzyme for cis-homo(2)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=2.2 umol/min/mg enzyme for cis-homo(3)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=5.1 umol/min/mg enzyme for cis-homo(4)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=5.5 umol/min/mg enzyme for maleate hydration reaction (at CC 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.59 umol/min/mg enzyme for (R)-homocitrate dehydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Note=kcat is 0.75 sec(-1) for cis-aconitate hydration reaction CC (PubMed:20170198). Kinetic parameters measured using the HacAB CC complex. {ECO:0000269|PubMed:20170198}; CC pH dependence: CC Optimum pH is 9. Active from pH 8 to 10. CC {ECO:0000269|PubMed:18765671}; CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis. CC -!- SUBUNIT: Heterotetramer of 2 HacA and 2 HacB proteins. Can not CC form a complex with LeuC. {ECO:0000269|PubMed:17449626}. CC -!- SIMILARITY: Belongs to the LeuD family. LeuD type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99277.1; -; Genomic_DNA. DR PIR; F64458; F64458. DR PDB; 2PKP; X-ray; 2.10 A; A=1-170. DR PDBsum; 2PKP; -. DR DisProt; DP00619; -. DR ProteinModelPortal; Q58667; -. DR SMR; Q58667; 1-167. DR STRING; 243232.MJ_1271; -. DR EnsemblBacteria; AAB99277; AAB99277; MJ_1271. DR KEGG; mja:MJ_1271; -. DR eggNOG; arCOG02230; Archaea. DR eggNOG; COG0066; LUCA. DR InParanoid; Q58667; -. DR KO; K16793; -. DR OMA; YRNCINI; -. DR PhylomeDB; Q58667; -. DR SABIO-RK; Q58667; -. DR UniPathway; UPA00919; -. DR EvolutionaryTrace; Q58667; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016836; F:hydro-lyase activity; IEA:InterPro. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01032; LeuD_type2; 1. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR InterPro; IPR011827; LeuD_type2/HacB/DmdB. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR02087; LEUD_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Reference proteome. FT CHAIN 1 170 Methanogen homoaconitase small subunit. FT /FTId=PRO_0000141936. FT MOTIF 24 27 YLRT. FT SITE 26 26 Critical for substrate specificity. FT MUTAGEN 26 27 RT->VY: Creates a promiscuous enzyme with FT both HACN and IPMI activities. FT MUTAGEN 26 26 R->K,V: Allows the recognition of FT substrates of IPMI enzymes since it FT becomes able to efficiently catalyze FT citraconate hydration and 3- FT isopropylmalate dehydration. Largely FT decreases substrate affinity for cis- FT homo(1-3)-aconitate. FT {ECO:0000269|PubMed:20170198}. FT MUTAGEN 27 27 T->A: Largely decreases substrate FT affinity for cis-homo(1-3)-aconitate FT while slightly increases activity on FT these substrates, and also decreases FT substrate affinity for maleate. Gains the FT ability to hydrate citraconate, an IPMI FT substrate. {ECO:0000269|PubMed:20170198}. FT STRAND 2 9 {ECO:0000244|PDB:2PKP}. FT HELIX 16 19 {ECO:0000244|PDB:2PKP}. FT HELIX 22 25 {ECO:0000244|PDB:2PKP}. FT HELIX 30 34 {ECO:0000244|PDB:2PKP}. FT TURN 35 41 {ECO:0000244|PDB:2PKP}. FT HELIX 45 48 {ECO:0000244|PDB:2PKP}. FT STRAND 54 57 {ECO:0000244|PDB:2PKP}. FT STRAND 59 61 {ECO:0000244|PDB:2PKP}. FT STRAND 63 65 {ECO:0000244|PDB:2PKP}. FT HELIX 68 75 {ECO:0000244|PDB:2PKP}. FT TURN 76 78 {ECO:0000244|PDB:2PKP}. FT STRAND 81 85 {ECO:0000244|PDB:2PKP}. FT HELIX 89 97 {ECO:0000244|PDB:2PKP}. FT STRAND 101 104 {ECO:0000244|PDB:2PKP}. FT HELIX 107 109 {ECO:0000244|PDB:2PKP}. FT STRAND 115 119 {ECO:0000244|PDB:2PKP}. FT TURN 120 123 {ECO:0000244|PDB:2PKP}. FT STRAND 124 127 {ECO:0000244|PDB:2PKP}. FT HELIX 128 130 {ECO:0000244|PDB:2PKP}. FT STRAND 132 135 {ECO:0000244|PDB:2PKP}. FT HELIX 141 148 {ECO:0000244|PDB:2PKP}. FT HELIX 152 164 {ECO:0000244|PDB:2PKP}. SQ SEQUENCE 170 AA; 18665 MW; 58146C478777ECB7 CRC64; MIIKGRAHKF GDDVDTDAII PGPYLRTTDP YELASHCMAG IDENFPKKVK EGDVIVAGEN FGCGSSREQA VIAIKYCGIK AVIAKSFARI FYRNAINVGL IPIIANTDEI KDGDIVEIDL DKEEIVITNK NKTIKCETPK GLEREILAAG GLVNYLKKRK LIQSKKGVKT // ID HEMTB_METJA Reviewed; 147 AA. AC Q58157; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 27-MAY-2002, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=Bacteriohemerythrin {ECO:0000255|HAMAP-Rule:MF_00556}; GN OrderedLocusNames=MJ0747; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Oxygen-binding protein. May be involved in a storage CC mechanism or for delivery to oxygen-requiring enzymes. The oxygen- CC binding site contains two iron atoms. {ECO:0000255|HAMAP- CC Rule:MF_00556}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00556}. CC -!- SIMILARITY: Belongs to the hemerythrin family. {ECO:0000255|HAMAP- CC Rule:MF_00556}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98740.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98740.1; ALT_INIT; Genomic_DNA. DR PIR; C64393; C64393. DR ProteinModelPortal; Q58157; -. DR STRING; 243232.MJ_0747; -. DR EnsemblBacteria; AAB98740; AAB98740; MJ_0747. DR KEGG; mja:MJ_0747; -. DR eggNOG; arCOG06577; Archaea. DR eggNOG; COG2703; LUCA. DR InParanoid; Q58157; -. DR KO; K07216; -. DR OMA; WSKDFET; -. DR PhylomeDB; Q58157; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005344; F:oxygen transporter activity; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.50; -; 1. DR HAMAP; MF_00556; Hemerythrin; 1. DR InterPro; IPR023504; Bacteriohemerythrin-like. DR InterPro; IPR012312; Haemerythrin-like. DR InterPro; IPR016131; Haemerythrin_Fe_BS. DR InterPro; IPR012827; Haemerythrin_metal-bd. DR Pfam; PF01814; Hemerythrin; 1. DR SUPFAM; SSF47188; SSF47188; 1. DR TIGRFAMs; TIGR02481; hemeryth_dom; 1. DR PROSITE; PS00550; HEMERYTHRINS; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Metal-binding; Oxygen transport; KW Reference proteome; Transport. FT CHAIN 1 147 Bacteriohemerythrin. FT /FTId=PRO_0000191844. FT METAL 23 23 Iron 1. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 60 60 Iron 1. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 64 64 Iron 1. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 64 64 Iron 2. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 79 79 Iron 2. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 83 83 Iron 2. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 120 120 Iron 2. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 125 125 Iron 1. {ECO:0000255|HAMAP- FT Rule:MF_00556}. FT METAL 125 125 Iron 2. {ECO:0000255|HAMAP- FT Rule:MF_00556}. SQ SEQUENCE 147 AA; 17478 MW; A7B85A8542C17670 CRC64; MKKEIIKWSK DFETGIKAFD DEHKILVKTL NDIYNLLNEG KRDEAKELLK RRVVNYAAKH FKHEEEVMEK YGYPDLERHR KTHEIFVKTV IEKLLPKIEE GSENDFRSAL SFLVGWLTMH IAKPDKKYGE WFKEKGIVIE DEAVKID // ID HFLX_METJA Reviewed; 402 AA. AC Q58526; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=GTPase HflX {ECO:0000255|HAMAP-Rule:MF_00900}; DE AltName: Full=GTP-binding protein HflX {ECO:0000255|HAMAP-Rule:MF_00900}; GN Name=hflX {ECO:0000255|HAMAP-Rule:MF_00900}; OrderedLocusNames=MJ1126; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: GTPase that associates with the 50S ribosomal subunit CC and may have a role during protein synthesis or ribosome CC biogenesis. {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00900}; CC -!- SUBUNIT: Monomer. Associates with the 50S ribosomal subunit. CC {ECO:0000255|HAMAP-Rule:MF_00900}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00900}. CC Note=May associate with membranes. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. HflX GTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00900}. CC -!- SIMILARITY: Contains 1 Hflx-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|HAMAP-Rule:MF_00900}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99128.1; -; Genomic_DNA. DR PIR; E64440; E64440. DR ProteinModelPortal; Q58526; -. DR STRING; 243232.MJ_1126; -. DR EnsemblBacteria; AAB99128; AAB99128; MJ_1126. DR KEGG; mja:MJ_1126; -. DR eggNOG; arCOG00353; Archaea. DR eggNOG; COG2262; LUCA. DR InParanoid; Q58526; -. DR KO; K03665; -. DR OMA; KWQLVLE; -. DR PhylomeDB; Q58526; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00900; GTPase_HflX; 1. DR InterPro; IPR030394; G_HFLX_dom. DR InterPro; IPR032305; GTP-bd_M. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR016496; GTPase_HflX. DR InterPro; IPR025121; GTPase_HflX_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR PANTHER; PTHR10229; PTHR10229; 1. DR Pfam; PF16360; GTP-bdg_M; 1. DR Pfam; PF13167; GTP-bdg_N; 1. DR Pfam; PF01926; MMR_HSR1; 1. DR PIRSF; PIRSF006809; GTP-binding_hflX_prd; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03156; GTP_HflX; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51705; G_HFLX; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 402 GTPase HflX. FT /FTId=PRO_0000205444. FT DOMAIN 181 350 Hflx-type G. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT NP_BIND 187 194 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 212 216 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 233 236 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 300 303 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT NP_BIND 328 330 GTP. {ECO:0000255|HAMAP-Rule:MF_00900}. FT METAL 194 194 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. FT METAL 214 214 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00900}. SQ SEQUENCE 402 AA; 46482 MW; 4DA94B9D200B77AF CRC64; MLILRKDSKF DRKSIEELKE LAEVLYNPVK TIVQIRKADP KYQIGSGLVE RIAENIKEEN IEIVIVGNIL TPSQKYNLAK KFKVEVIDKI ELVLRIFYKH ARTKEAQLQV RLAELQYELP RAREKVRLAK MGEQPGFGGY GDYEVEKYYQ KVKREIATIK RKLEKLREHR RVARKGRAKF DTVGLIGYTN AGKTSLLNAL TGENKESKNQ VFTTLTTTTR AIKGIKRKIL VTDTVGFIDD LPPFMIEAFL STIEESADSD LILIVVDASD DIEEIKRKLK VNHEILSKIN CKAPIITVFN KVDKITKEKK RKILEELDRY IVNPIFVSAK YDINMDLLKE MIIEHLNLSI GTIETDNPRL ISYLYENTEI IEDILEDNKH IITFRAKERD VNRILKLHKS AV // ID HIS1_METJA Reviewed; 288 AA. AC Q58601; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=ATP phosphoribosyltransferase; DE Short=ATP-PRT; DE Short=ATP-PRTase; DE EC=2.4.2.17; GN Name=hisG; OrderedLocusNames=MJ1204; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the condensation of ATP and 5-phosphoribose 1- CC diphosphate to form N'-(5'-phosphoribosyl)-ATP (PR-ATP). Has a CC crucial role in the pathway because the rate of histidine CC biosynthesis seems to be controlled primarily by regulation of CC HisG enzymatic activity (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + diphosphate CC = ATP + 5-phospho-alpha-D-ribose 1-diphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- ENZYME REGULATION: Feedback inhibited by histidine. {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 1/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATP phosphoribosyltransferase family. CC Long subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99208.1; -; Genomic_DNA. DR PIR; C64450; C64450. DR ProteinModelPortal; Q58601; -. DR STRING; 243232.MJ_1204; -. DR EnsemblBacteria; AAB99208; AAB99208; MJ_1204. DR KEGG; mja:MJ_1204; -. DR eggNOG; arCOG02208; Archaea. DR eggNOG; COG0040; LUCA. DR InParanoid; Q58601; -. DR KO; K00765; -. DR OMA; CDIVSSG; -. DR PhylomeDB; Q58601; -. DR UniPathway; UPA00031; UER00006. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003879; F:ATP phosphoribosyltransferase activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.120; -; 1. DR HAMAP; MF_00079; HisG_Long; 1. DR InterPro; IPR013820; ATP_PRibTrfase_cat. DR InterPro; IPR018198; ATP_PRibTrfase_CS. DR InterPro; IPR001348; ATP_PRibTrfase_HisG. DR InterPro; IPR020621; ATP_PRibTrfase_HisG_long. DR InterPro; IPR013115; HisG_C. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR PANTHER; PTHR21403; PTHR21403; 1. DR Pfam; PF01634; HisG; 1. DR Pfam; PF08029; HisG_C; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR TIGRFAMs; TIGR00070; hisG; 1. DR TIGRFAMs; TIGR03455; HisG_C-term; 1. DR PROSITE; PS01316; ATP_P_PHORIBOSYLTR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Glycosyltransferase; Histidine biosynthesis; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 288 ATP phosphoribosyltransferase. FT /FTId=PRO_0000151882. SQ SEQUENCE 288 AA; 31860 MW; 121E6F9D44A61858 CRC64; MIMFALPNKG RISEPVMKVL EKAGLKITVK GRSLFANTVD DNIKVMFARA RDIPEFVADG VADIGVTGYD LVLERNVEDK VDFLLDFGFG FAKLVLAAPE SSNINSIDDI KEGMRVATEF PNLTKKYFEK LNKKVEIIEL SGATEIAPFI GIADLISDLT STGTTLRLNR LKVIDEIVSS TTRLIANKNS LKDKEKREKI NQIVIAIKSV LFAETKRLIM MNAPKDKVEE IRKLIPGMAG PTVSKVLSDD NMVAIHAVVN EDEIFTLVPK LHALGARDIL VVPIERIL // ID HACA_METJA Reviewed; 420 AA. AC Q58409; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=Methanogen homoaconitase large subunit; DE Short=HACN; DE EC=4.2.1.114; DE AltName: Full=Homoaconitate hydratase; GN Name=hacA; OrderedLocusNames=MJ1003; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PUTATIVE FUNCTION AS A HOMOACONITASE, LACK OF FUNCTION AS A RP ISOPROPYLMALATE ISOMERASE, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17449626; DOI=10.1128/JB.00166-07; RA Drevland R.M., Waheed A., Graham D.E.; RT "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in RT Methanocaldococcus jannaschii."; RL J. Bacteriol. 189:4391-4400(2007). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=18765671; DOI=10.1074/jbc.M802159200; RA Drevland R.M., Jia Y., Palmer D.R.J., Graham D.E.; RT "Methanogen homoaconitase catalyzes both hydrolyase reactions in RT coenzyme B biosynthesis."; RL J. Biol. Chem. 283:28888-28896(2008). RN [4] RP FUNCTION, SUBSTRATE SPECIFICITY, AND KINETIC PARAMETERS. RX PubMed=20170198; DOI=10.1021/bi901766z; RA Jeyakanthan J., Drevland R.M., Gayathri D.R., Velmurugan D., RA Shinkai A., Kuramitsu S., Yokoyama S., Graham D.E.; RT "Substrate specificity determinants of the methanogen homoaconitase RT enzyme: structure and function of the small subunit."; RL Biochemistry 49:2687-2696(2010). CC -!- FUNCTION: Hydro-lyase with broad substrate specificity for cis- CC unsaturated tricarboxylic acids. Catalyzes both the reversible CC dehydration of (R)-homocitrate ((R)-2-hydroxybutane-1,2,4- CC tricarboxylate) to produce cis-homoaconitate ((Z)-but-1-ene-1,2,4- CC tricarboxylate), and its hydration to homoisocitrate ((1R,2S)-1- CC hydroxybutane-1,2,4-tricarboxylate). Is also able to hydrate the CC analogous longer chain substrates cis-homo(2)-aconitate, cis- CC homo(3)-aconitate, and even the non-physiological cis-homo(4)- CC aconitate with similar efficiency. These reactions are part of the CC biosynthesis pathway of coenzyme B. Can also catalyze the CC hydration of maleate to (R)-malate, and that of cis-aconitate. Can CC not catalyze the hydration of citraconate and the dehydration of CC (S)-homocitrate, citramalate, 2-isopropylmalate, 3- CC isopropylmalate, citrate or threo-DL-isocitrate. CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}. CC -!- CATALYTIC ACTIVITY: (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = CC (Z)-but-1-ene-1,2,4-tricarboxylate + H(2)O. CC {ECO:0000269|PubMed:18765671}. CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxybutane-1,2,4-tricarboxylate = CC (Z)-but-1-ene-1,2,4-tricarboxylate + H(2)O. CC {ECO:0000269|PubMed:18765671}. CC -!- CATALYTIC ACTIVITY: (R)-2-hydroxybutane-1,2,4-tricarboxylate = CC (1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate. CC {ECO:0000269|PubMed:18765671}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01027, CC ECO:0000269|PubMed:18765671}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01027, ECO:0000269|PubMed:18765671}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=22 uM for cis-homoaconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=30 uM for cis-homo(2)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=36 uM for cis-homo(3)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=175 uM for cis-homo(4)-aconitate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=330 uM for maleate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=1500 uM for (R)-homocitrate (at 60 degrees Celsius) CC {ECO:0000269|PubMed:18765671, ECO:0000269|PubMed:20170198}; CC KM=300 uM for cis-aconitate {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.68 umol/min/mg enzyme for cis-homoaconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.60 umol/min/mg enzyme for cis-homo(2)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=2.2 umol/min/mg enzyme for cis-homo(3)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=5.1 umol/min/mg enzyme for cis-homo(4)aconitate hydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=5.5 umol/min/mg enzyme for maleate hydration reaction (at CC 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Vmax=0.59 umol/min/mg enzyme for (R)-homocitrate dehydration CC reaction (at 60 degrees Celsius) {ECO:0000269|PubMed:18765671, CC ECO:0000269|PubMed:20170198}; CC Note=kcat is 0.75 sec(-1) for cis-aconitate hydration reaction CC (PubMed:20170198). Kinetic parameters measured using the HacAB CC complex. {ECO:0000269|PubMed:20170198}; CC pH dependence: CC Optimum pH is 9. Active from pH 8 to 10. CC {ECO:0000269|PubMed:18765671}; CC -!- PATHWAY: Organic acid metabolism; 2-oxosuberate biosynthesis. CC -!- SUBUNIT: Heterotetramer of 2 HacA and 2 HacB proteins. CC {ECO:0000269|PubMed:17449626}. CC -!- MISCELLANEOUS: The heterotetramer that can be formed in vitro CC between HacA and LeuD can not catalyze citraconate hydration or CC the dehydration of 2-isopropylmalate or 3-isopropylmalate. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99007.1; -; Genomic_DNA. DR PIR; B64425; B64425. DR PDB; 4KP2; X-ray; 2.50 A; A/B=1-420. DR PDBsum; 4KP2; -. DR ProteinModelPortal; Q58409; -. DR STRING; 243232.MJ_1003; -. DR EnsemblBacteria; AAB99007; AAB99007; MJ_1003. DR KEGG; mja:MJ_1003; -. DR eggNOG; arCOG01698; Archaea. DR eggNOG; COG0065; LUCA. DR InParanoid; Q58409; -. DR KO; K16792; -. DR OMA; ANLCVEA; -. DR PhylomeDB; Q58409; -. DR BioCyc; MetaCyc:MONOMER-2003; -. DR BRENDA; 4.2.1.114; 3260. DR SABIO-RK; Q58409; -. DR UniPathway; UPA00919; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01027; LeuC_type2; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok. DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR01343; hacA_fam; 1. DR TIGRFAMs; TIGR02086; IPMI_arch; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; KW Metal-binding; Reference proteome. FT CHAIN 1 420 Methanogen homoaconitase large subunit. FT /FTId=PRO_0000076868. FT METAL 302 302 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 362 362 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 365 365 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT HELIX 3 12 {ECO:0000244|PDB:4KP2}. FT STRAND 21 25 {ECO:0000244|PDB:4KP2}. FT STRAND 27 32 {ECO:0000244|PDB:4KP2}. FT TURN 33 35 {ECO:0000244|PDB:4KP2}. FT HELIX 36 46 {ECO:0000244|PDB:4KP2}. FT HELIX 53 55 {ECO:0000244|PDB:4KP2}. FT STRAND 56 59 {ECO:0000244|PDB:4KP2}. FT HELIX 69 85 {ECO:0000244|PDB:4KP2}. FT STRAND 88 91 {ECO:0000244|PDB:4KP2}. FT HELIX 98 105 {ECO:0000244|PDB:4KP2}. FT STRAND 112 117 {ECO:0000244|PDB:4KP2}. FT HELIX 120 126 {ECO:0000244|PDB:4KP2}. FT STRAND 129 132 {ECO:0000244|PDB:4KP2}. FT HELIX 135 144 {ECO:0000244|PDB:4KP2}. FT STRAND 145 150 {ECO:0000244|PDB:4KP2}. FT STRAND 153 159 {ECO:0000244|PDB:4KP2}. FT STRAND 164 166 {ECO:0000244|PDB:4KP2}. FT HELIX 168 179 {ECO:0000244|PDB:4KP2}. FT STRAND 187 193 {ECO:0000244|PDB:4KP2}. FT HELIX 194 198 {ECO:0000244|PDB:4KP2}. FT HELIX 201 209 {ECO:0000244|PDB:4KP2}. FT HELIX 210 214 {ECO:0000244|PDB:4KP2}. FT STRAND 216 221 {ECO:0000244|PDB:4KP2}. FT HELIX 225 233 {ECO:0000244|PDB:4KP2}. FT HELIX 239 246 {ECO:0000244|PDB:4KP2}. FT STRAND 262 265 {ECO:0000244|PDB:4KP2}. FT STRAND 273 275 {ECO:0000244|PDB:4KP2}. FT STRAND 283 285 {ECO:0000244|PDB:4KP2}. FT HELIX 286 289 {ECO:0000244|PDB:4KP2}. FT STRAND 295 299 {ECO:0000244|PDB:4KP2}. FT STRAND 301 304 {ECO:0000244|PDB:4KP2}. FT HELIX 307 317 {ECO:0000244|PDB:4KP2}. FT STRAND 327 330 {ECO:0000244|PDB:4KP2}. FT HELIX 335 342 {ECO:0000244|PDB:4KP2}. FT TURN 343 345 {ECO:0000244|PDB:4KP2}. FT HELIX 346 353 {ECO:0000244|PDB:4KP2}. FT STRAND 364 367 {ECO:0000244|PDB:4KP2}. FT STRAND 369 371 {ECO:0000244|PDB:4KP2}. FT STRAND 378 384 {ECO:0000244|PDB:4KP2}. FT STRAND 390 392 {ECO:0000244|PDB:4KP2}. FT STRAND 397 400 {ECO:0000244|PDB:4KP2}. FT HELIX 403 412 {ECO:0000244|PDB:4KP2}. FT STRAND 413 415 {ECO:0000244|PDB:4KP2}. SQ SEQUENCE 420 AA; 46063 MW; ABDBAD2E101616B6 CRC64; MTLVEKILSK KVGYEVCAGD SIEVEVDLAM THDGTTPLAY KALKEMSDSV WNPDKIVVAF DHNVPPNTVK AAEMQKLALE FVKRFGIKNF HKGGEGICHQ ILAENYVLPN MFVAGGDSHT CTHGAFGAFA TGFGATDMAY IYATGETWIK VPKTIRVDIV GKNENVSAKD IVLRVCKEIG RRGATYMAIE YGGEVVKNMD MDGRLTLCNM AIEMGGKTGV IEADEITYDY LKKERGLSDE DIAKLKKERI TVNRDEANYY KEIEIDITDM EEQVAVPHHP DNVKPISDVE GTEINQVFIG SCTNGRLSDL REAAKYLKGR EVHKDVKLIV IPASKKVFLQ ALKEGIIDIF VKAGAMICTP GCGPCLGAHQ GVLAEGEICL STTNRNFKGR MGHINSYIYL ASPKIAAISA VKGYITNKLD // ID HDRC2_METJA Reviewed; 186 AA. AC Q58274; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=CoB--CoM heterodisulfide reductase iron-sulfur subunit C 2; DE EC=1.8.98.1; GN Name=hdrC2; OrderedLocusNames=MJ0864; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible CC reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme CC M) and H-S-CoB (coenzyme B). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = CC N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + CC dihydromethanophenazine. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 2 [4Fe-4S] clusters per subunit. {ECO:0000250}; CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B CC heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme CC M-coenzyme B heterodisulfide: step 1/1. CC -!- SUBUNIT: The heterodisulfide reductase is composed of three CC subunits; HdrA, HdrB and HdrC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HdrC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98869.1; -; Genomic_DNA. DR PIR; H64407; H64407. DR ProteinModelPortal; Q58274; -. DR STRING; 243232.MJ_0864; -. DR PRIDE; Q58274; -. DR EnsemblBacteria; AAB98869; AAB98869; MJ_0864. DR KEGG; mja:MJ_0864; -. DR eggNOG; arCOG00964; Archaea. DR eggNOG; COG1150; LUCA. DR InParanoid; Q58274; -. DR KO; K03390; -. DR OMA; TAQFSEK; -. DR PhylomeDB; Q58274; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051186; P:cofactor metabolic process; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR017680; CoB/CoM_hetero-S_Rdtase_csu. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR TIGRFAMs; TIGR03290; CoB_CoM_SS_C; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methanogenesis; Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 186 CoB--CoM heterodisulfide reductase iron- FT sulfur subunit C 2. FT /FTId=PRO_0000150074. FT DOMAIN 26 56 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 67 99 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 36 36 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 39 39 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 42 42 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 46 46 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 79 79 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 82 82 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 85 85 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 89 89 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 186 AA; 21049 MW; DCF74D7A6996117A CRC64; MAVIKLDEVN KNFVNEVIEA GKLVLGEDIV KSIKACYQCG TCTGSCPSGR RTAYRTRKVL RKVLLGLDDV LDSDDIWYCT TCYTCYERCP RDVKITEIIK TLRNIAAQKG NMALAHRKTA SYVLRFGHAV PANNQIVELR GKLGLPAKSP TAQFSEKDLE EVRTLIKELK FDKLIAFDWE KMDLKE // ID HELS_METJA Reviewed; 1195 AA. AC Q58524; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 117. DE RecName: Full=ATP-dependent DNA helicase Hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_00442}; DE Contains: DE RecName: Full=Endonuclease PI-MjaHel; DE EC=3.1.-.-; DE AltName: Full=Mja Hel intein; DE AltName: Full=Mja Pep3 intein; GN Name=hel308 {ECO:0000255|HAMAP-Rule:MF_00442}; GN OrderedLocusNames=MJ1124; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent ATPase and 3'-5' DNA helicase that may be CC involved in repair of stalled replication forks. CC {ECO:0000255|HAMAP-Rule:MF_00442}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00442}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00442}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the helicase family. Hel308 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00442}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00442}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99126.1; -; Genomic_DNA. DR PIR; C64440; C64440. DR ProteinModelPortal; Q58524; -. DR STRING; 243232.MJ_1124; -. DR EnsemblBacteria; AAB99126; AAB99126; MJ_1124. DR KEGG; mja:MJ_1124; -. DR eggNOG; arCOG00553; Archaea. DR eggNOG; arCOG03157; Archaea. DR eggNOG; COG1204; LUCA. DR eggNOG; COG1372; LUCA. DR InParanoid; Q58524; -. DR KO; K03726; -. DR OMA; CLNANTE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. DR Gene3D; 3.40.50.300; -; 5. DR HAMAP; MF_00442; Helicase_Hel308; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR022965; Helicase_Hel308. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW ATP-binding; Autocatalytic cleavage; Complete proteome; DNA damage; KW DNA repair; DNA-binding; Endonuclease; Helicase; Hydrolase; KW Intron homing; Nuclease; Nucleotide-binding; Protein splicing; KW Reference proteome. FT CHAIN 1 337 ATP-dependent DNA helicase Hel308, 1st FT part. {ECO:0000255}. FT /FTId=PRO_0000013299. FT CHAIN 338 838 Endonuclease PI-MjaHel. {ECO:0000255}. FT /FTId=PRO_0000013300. FT CHAIN 839 1195 ATP-dependent DNA helicase Hel308, 2nd FT part. {ECO:0000255}. FT /FTId=PRO_0000013301. FT DOMAIN 26 196 Helicase ATP-binding. {ECO:0000255|HAMAP- FT Rule:MF_00442}. FT DOMAIN 451 584 DOD-type homing endonuclease. FT NP_BIND 39 46 ATP. {ECO:0000255|HAMAP-Rule:MF_00442}. FT MOTIF 143 146 DEAH box. FT COMPBIAS 137 142 Poly-Val. FT BINDING 20 20 ATP. {ECO:0000255|HAMAP-Rule:MF_00442}. SQ SEQUENCE 1195 AA; 138674 MW; 87C9CF1A87EFB52D CRC64; MDKILEILKD FGIVELRPPQ KKALERGLLD KNKNFLISIP TASGKTLIGE MALINHLLDG NKNPTNKKGI FIVPLKALAS EKYEEFKSKY ERYGLRIALS IGDYDEDEDL SKYHLIITTA EKLDSLWRHK IDWINDVSVV VVDEIHLIND ETRGGTLEIL LTKLKEFNVQ IIGLSATIGN PDELAEWLNA ELIVDDWRPV ELKKGIYKNE AIEFINGEIR EIKAVDNNDI YNLVVDCVKE GGCCLVFCNT KRNAVNEAKK LNLKKFLTEE EKIRLKEIAE EILSILEPPT EMCKTLAECI LNGSAFHHAG LTYQHRKIVE DAFRKRLIKV ICCTPTLCLN ANTEILQESG FRKITELNKD EKVFALCGKE IKPVDGWKVH KTPQHEYNIV VKTVNGLEIT TTPNHIFLVK ENGSLKEKEA KDLKVGDYVA TVDRIRVKEK DIDLSNGDLY FIGYFIGDGY TGVIEKNTLK ATPDLAFNPK YPPNFDDSEL HKKYFLKCRI SKGVAHYIYS KKLRKIFNKL NMLTKDNKNI DAFCNLPLDK LAYLIAGLFD SDGYIYLNRK NIEFYSISEK LVEQLQFVLL RFGIHSSIRK KKTKTMVSPT NGKEYKCKDI YVLTIRDFMS IKRFYENIPL RHEEKRRKLE EIIKNKEIGQ IPSEFVALRF TPIAKIWCDC GFSVDLTMFK PRTKRQRELN KKRVKLLFEL LDGKKLITNY KEYYSKRKNP YFDFIVREKI NGNNYYSLNE KGRVLMSLLN KHIKDKENLE EMYNFLVNLE KCPICGKPIH KEMRYSWKKE CYDGDIYWDR IKEIKKIKVN DKYAYDIELP DDGSNSHYIV ANGFIVHNSA GLNLPCRRAI VKDLTRFTNK GMRYIPIMEI QQCIGRAGRP GLDPYGEGII VAKNDRDYLR AYQALTQKPE PIYSKLSNQA VLRTQLLGLI ATGEIRDEYD LEWFIRNTFY AHQYGNLREV AKNINEVIRF LEENEFIIDF MPTELGKRVS ELYIDPLSAK FIIDGLEEME NEEEIYYLYL ISKTLEMMPN LRVYNSEELN LIDEMDSLGI KSFEIEDLEA FKTAKMLYDW INEVPEDEIL KRYKIEPGIL RYKVENAVWI MHALKEIAKL IGKSSDIPEK LEIRLEYGAK EDIIELLSIK YIGRVRARKL YNAGIRSIED IINNPSKVAS IIGEKIAKKI LDELGVKFGQ QKLSF // ID HEM4_METJA Reviewed; 240 AA. AC Q58401; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Putative uroporphyrinogen-III synthase; DE Short=UROS; DE EC=4.2.1.75; DE AltName: Full=Hydroxymethylbilane hydrolyase [cyclizing]; DE AltName: Full=Uroporphyrinogen-III cosynthase; GN Name=hemD; OrderedLocusNames=MJ0994; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes cyclization of the linear tetrapyrrole, CC hydroxymethylbilane, to the macrocyclic uroporphyrinogen III. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Hydroxymethylbilane = uroporphyrinogen III + CC H(2)O. CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 3/4. CC -!- SIMILARITY: Belongs to the uroporphyrinogen-III synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98999.1; -; Genomic_DNA. DR PIR; B64424; B64424. DR ProteinModelPortal; Q58401; -. DR STRING; 243232.MJ_0994; -. DR EnsemblBacteria; AAB98999; AAB98999; MJ_0994. DR KEGG; mja:MJ_0994; -. DR eggNOG; arCOG02048; Archaea. DR eggNOG; COG1587; LUCA. DR InParanoid; Q58401; -. DR KO; K01719; -. DR OMA; YIVAIGP; -. DR PhylomeDB; Q58401; -. DR UniPathway; UPA00251; UER00320. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004852; F:uroporphyrinogen-III synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003754; 4pyrrol_synth_uPrphyn_synth. DR Pfam; PF02602; HEM4; 1. DR SUPFAM; SSF69618; SSF69618; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Porphyrin biosynthesis; Reference proteome. FT CHAIN 1 240 Putative uroporphyrinogen-III synthase. FT /FTId=PRO_0000135249. SQ SEQUENCE 240 AA; 27614 MW; F0AA2E8CCEF9BAE8 CRC64; MKVVITRPKE RADVFASLLK KEGFEPIIFP TLEIVYNKDL DVNLDSYDWI AFTSPSGVIG LYNILTENER ENVKNKKIAV IGEKTAKTFK KYFGRDPDIM PNEYTAESLL REIKKVSKEE EKFLIPTTPS TRDVLKNNLN ADLLFVYKSA EPENLKEDIK KLKELIAKDK FILTFTSGLT AKNFFKYVDD EFAEIIKDNY IVAIGPITAK VIEKFGFKPL IPKVYTIEGM LEVIRTLKER // ID HELX_METJA Reviewed; 841 AA. AC Q57742; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Uncharacterized ATP-dependent helicase MJ0294; DE EC=3.6.4.-; GN OrderedLocusNames=MJ0294; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98279.1; -; Genomic_DNA. DR PIR; G64336; G64336. DR ProteinModelPortal; Q57742; -. DR STRING; 243232.MJ_0294; -. DR EnsemblBacteria; AAB98279; AAB98279; MJ_0294. DR KEGG; mja:MJ_0294; -. DR eggNOG; arCOG00557; Archaea. DR eggNOG; COG1201; LUCA. DR InParanoid; Q57742; -. DR KO; K03724; -. DR OMA; YPFEGRF; -. DR PhylomeDB; Q57742; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR013701; DEAD/DEAH_assoc. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR017170; Lhr-like_ATP-dep_RNA_helic_prd. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF08494; DEAD_assoc; 1. DR Pfam; PF00271; Helicase_C; 1. DR PIRSF; PIRSF037307; Lhr-like_helic_prd; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 841 Uncharacterized ATP-dependent helicase FT MJ0294. FT /FTId=PRO_0000102196. FT DOMAIN 43 234 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 266 416 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 56 63 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 181 184 DEVH box. SQ SEQUENCE 841 AA; 97268 MW; 4C28AA8AA9459505 CRC64; MGRVEYLKKE YSDEEIYEIL EKPVKEWFKR KYKTFTPPQR YAIKEIHEGK NVLICSPTGS GKTLSAFLAG INELIKLSME NKLEDRIYIL YVSPLRALNN DIERNLKEPL KEIYDVAKEI GIELDEIRVA VRTSDTTSSQ KQRMLKKPPH ILITTPESLA IALNSPKFSQ LLSGIKYVIV DEIHALTNKR GVHLSLSLER LNRIANFIRI GLSATIHPLT EVAKFLVGNG RDCYIVDVSY KKEIEIKVIS PVDDFIYTPS EEISKRLYNL LKKLIEEHKT TLIFTNTRSA TERVAFYLKQ LGVEKVETHH SSLSREHRLE VEEKLKKGEI RVCISSTSLE LGVDIGSIDL VILLGSPKSV SRALQRIGRS GHRLHEKSKG IIIPFDRDDL VENVVLAYDA KIGKIDRIHI PKNCLDVLAQ HLVGMALEKV WDVDEAYNLI KKAYPYKDLS KKDFLDVLNY LAGGIEEKNV YAKIWLKDNK FGKRGKSVRA IYYMNVGTIP DETAVDVIAD GKYVGEVEEE FAEKLMKGDI FVLGGKTYKY LGGRGNKIRV KEVFDEKPTI PAWFSEQLPL AYDLALDIEK FRKEVLSSDI EEIREKYDID EKTAKAIKNY MDEQNKFAIV PDDEKVLIEN FDEEKRRYYI FHFVAGRRAN EALARAFANY ISKIKKCNVR ISVNDYGFAL ILPKNRKIKR ADITELFNLD VVKNVKESIE RSEILKRRFR HVATRGFMIL RRYMNRKISV DRQQFNAEML LKYCKEVNHP LYRETLREIL EDSLDIDNAL DYFEKIKRRK IYYLELPSPS PFAFNLVVSA SSDVIFMEDK KKMIAELHKK VMEFISMKGK K // ID HERA_METJA Reviewed; 503 AA. AC Q58824; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Probable DNA double-strand break repair helicase HerA {ECO:0000250|UniProtKB:F2Z5Z6}; DE EC=3.6.4.12 {ECO:0000250|UniProtKB:F2Z5Z6}; GN Name=herA {ECO:0000250|UniProtKB:F2Z5Z6}; GN OrderedLocusNames=MJ1429 {ECO:0000312|EMBL:AAB99439.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair (By CC similarity). Acts probably with NurA to stimulate resection of the CC 5' strand and produce the long 3' single-strand that is required CC for RadA loading (By similarity). Exhibits DNA-dependent ATPase CC activity and DNA helicase activity (By similarity). CC {ECO:0000250|UniProtKB:F2Z5Z6, ECO:0000250|UniProtKB:Q8U1P0}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000250|UniProtKB:F2Z5Z6}. CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99439.1; -; Genomic_DNA. DR PIR; D64478; D64478. DR ProteinModelPortal; Q58824; -. DR STRING; 243232.MJ_1429; -. DR EnsemblBacteria; AAB99439; AAB99439; MJ_1429. DR KEGG; mja:MJ_1429; -. DR eggNOG; arCOG00280; Archaea. DR eggNOG; COG0433; LUCA. DR InParanoid; Q58824; -. DR KO; K06915; -. DR OMA; EPNDQRY; -. DR PhylomeDB; Q58824; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR008571; HerA. DR InterPro; IPR018538; HerA_barrel_dom. DR InterPro; IPR033186; HerA_C. DR InterPro; IPR002789; HerA_central. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR30121:SF2; PTHR30121:SF2; 2. DR Pfam; PF05872; DUF853; 1. DR Pfam; PF01935; DUF87; 1. DR Pfam; PF09378; HAS-barrel; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 503 Probable DNA double-strand break repair FT helicase HerA. FT /FTId=PRO_0000107323. FT NP_BIND 131 136 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT NP_BIND 478 479 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT BINDING 122 122 ATP. {ECO:0000250|UniProtKB:Q97WG8}. SQ SEQUENCE 503 AA; 56697 MW; BBDADC0E52849657 CRC64; MYVMKVVGKT TTTHFTFESL EKIRFGEYVI AKNVDGRDVL GVIKNVVADV EKFVGEVKVI GVLDGNKIIP NRTPILPNSE VRLCDDEILN NIYLTPDGLN IGHLLTRDNV RVYLDTNKLV SRHFAILSIT GGGKSNTASV LCRELAKKNG TVIMIDPHGE YISLYHEDME GKIKVINPII NPVLLAPSEF ANLIGIGDNE IEKRVYVEFA YHTVKHECPD AKGIEFIEKI ENLLYEWSKI ASVGWEIKYY NPLRRNYDRR KLEKEDFVIL MSLIDTISKF KLDYALNIGD RDVIEEFEIG KINIVNLSGL EIPQMVTFVG FIAKHLLLKR ITYLKSLKDV YSINEEIRRV AQSNLNIIES HYKVVTKPVL LIVEEAHIFI PVNEQNSASL WLGKIAREGR KFGVGLGLVS QRPKQLHPDV LSQTNTKIIL KIVEPEDQKY IQRASEELGE DLVKDLASLG IGEAVIVGAA ISLPSIVKID KFDGVYGGKD INIVGEWMGL DDW // ID HIS2_METJA Reviewed; 95 AA. AC Q57750; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Phosphoribosyl-ATP pyrophosphatase; DE Short=PRA-PH; DE EC=3.6.1.31; GN Name=hisE; OrderedLocusNames=MJ0302; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-ATP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-AMP + diphosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 2/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PRA-PH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98289.1; -; Genomic_DNA. DR PIR; G64337; G64337. DR ProteinModelPortal; Q57750; -. DR STRING; 243232.MJ_0302; -. DR DNASU; 1451157; -. DR EnsemblBacteria; AAB98289; AAB98289; MJ_0302. DR KEGG; mja:MJ_0302; -. DR eggNOG; arCOG02677; Archaea. DR eggNOG; COG0140; LUCA. DR InParanoid; Q57750; -. DR KO; K01523; -. DR OMA; THRKGID; -. DR PhylomeDB; Q57750; -. DR UniPathway; UPA00031; UER00007. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004636; F:phosphoribosyl-ATP diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01020; HisE; 1. DR InterPro; IPR008179; PRib-ATP_PPHydrolase. DR InterPro; IPR021130; PRib-ATP_PPHydrolase-like. DR Pfam; PF01503; PRA-PH; 1. DR TIGRFAMs; TIGR03188; histidine_hisI; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; ATP-binding; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 95 Phosphoribosyl-ATP pyrophosphatase. FT /FTId=PRO_0000136391. SQ SEQUENCE 95 AA; 11181 MW; 7A7853EE3171919E CRC64; MILEEVYEII KQRIKEKPEG SYVAKLTTDD KKTAINKICE KIGEESTELI LAAKDDKKDE IIYEAADLIF HTMVLLAYKN IEFEELLKEF ERRKK // ID HIS6_METJA Reviewed; 272 AA. AC Q57854; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisF; DE EC=4.1.3.-; DE AltName: Full=IGP synthase cyclase subunit; DE AltName: Full=IGP synthase subunit HisF; DE AltName: Full=ImGP synthase subunit HisF; DE Short=IGPS subunit HisF; GN Name=hisF; OrderedLocusNames=MJ0411; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisF subunit catalyzes the CC cyclization activity that produces IGP and AICAR from PRFAR using CC the ammonia provided by the HisH subunit (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98400.1; -; Genomic_DNA. DR PIR; C64351; C64351. DR ProteinModelPortal; Q57854; -. DR SMR; Q57854; 2-271. DR STRING; 243232.MJ_0411; -. DR EnsemblBacteria; AAB98400; AAB98400; MJ_0411. DR KEGG; mja:MJ_0411; -. DR eggNOG; arCOG00617; Archaea. DR eggNOG; COG0107; LUCA. DR InParanoid; Q57854; -. DR KO; K02500; -. DR OMA; KGTNFVN; -. DR PhylomeDB; Q57854; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01013; HisF; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004651; HisF. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00735; hisF; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 272 Imidazole glycerol phosphate synthase FT subunit HisF. FT /FTId=PRO_0000142279. FT ACT_SITE 11 11 {ECO:0000255}. FT ACT_SITE 130 130 {ECO:0000255}. SQ SEQUENCE 272 AA; 30168 MW; 84943CA540A0FECB CRC64; MLTKRIIPCL DIKDGRVVKG TKFLNLRDAG DPVELAQYYD DEGADELVFL DITASAEKRD IIIDVVERTA EKVFIPLTVG GGIKSIEDFR RILRAGADKV SINTAAVKNP NLIKEASEIF GSQCVVVAID AKRHYVNEDE IDKINKNVVK VEDGYCWFEV YIYGGRKETG IDAINWAKKV EELGAGEILL TSIDKDGTKS GYDLILTKEI SKSVKLPVIA SGGCGKPEHV YEAFVYGKAD AALMAGILHY REYTIEEIKK YCADRGIPMR LL // ID HJA2_METJA Reviewed; 67 AA. AC Q58342; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Probable archaeal histone 2; GN OrderedLocusNames=MJ0932; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds and compact DNA (95 to 150 base pairs) to form CC nucleosome-like structures that contain positive DNA supercoils. CC Increases the resistance of DNA to thermal denaturation (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98934.1; -; Genomic_DNA. DR PIR; D64416; D64416. DR ProteinModelPortal; Q58342; -. DR SMR; Q58342; 2-66. DR STRING; 243232.MJ_0932; -. DR EnsemblBacteria; AAB98934; AAB98934; MJ_0932. DR KEGG; mja:MJ_0932; -. DR eggNOG; arCOG02144; Archaea. DR eggNOG; COG2036; LUCA. DR InParanoid; Q58342; -. DR OMA; MANDLPI; -. DR PhylomeDB; Q58342; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR004823; TAF_TATA-bd. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 3: Inferred from homology; KW Chromosome; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 67 Probable archaeal histone 2. FT /FTId=PRO_0000154988. SQ SEQUENCE 67 AA; 7384 MW; 05DE8B391D9C927C CRC64; MAELPVAPFE RILKKAGAER VSRAAAEYLA EAVEEIALEI AKEAVELAKH AKRKTVKVED IKLALKQ // ID HJC_METJA Reviewed; 133 AA. AC Q57920; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Holliday junction resolvase Hjc {ECO:0000255|HAMAP-Rule:MF_01490}; DE Short=Hjc {ECO:0000255|HAMAP-Rule:MF_01490}; DE EC=3.1.22.4 {ECO:0000255|HAMAP-Rule:MF_01490}; GN Name=hjc {ECO:0000255|HAMAP-Rule:MF_01490}; OrderedLocusNames=MJ0497; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: A structure-specific endonuclease that resolves Holliday CC junction (HJ) intermediates during genetic recombination. Cleaves CC 4-way DNA junctions introducing paired nicks in opposing strands, CC leaving a 5'-terminal phosphate and a 3'-terminal hydroxyl group CC that are ligated to produce recombinant products. CC {ECO:0000255|HAMAP-Rule:MF_01490}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage at a junction such as CC a reciprocal single-stranded crossover between two homologous DNA CC duplexes (Holliday junction). {ECO:0000255|HAMAP-Rule:MF_01490}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01490}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01490}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01490}. CC -!- SIMILARITY: Belongs to the Holliday junction resolvase Hjc family. CC {ECO:0000255|HAMAP-Rule:MF_01490}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98490.1; -; Genomic_DNA. DR PIR; A64362; A64362. DR ProteinModelPortal; Q57920; -. DR STRING; 243232.MJ_0497; -. DR EnsemblBacteria; AAB98490; AAB98490; MJ_0497. DR KEGG; mja:MJ_0497; -. DR eggNOG; arCOG00919; Archaea. DR eggNOG; COG1591; LUCA. DR InParanoid; Q57920; -. DR KO; K03552; -. DR OMA; KNYALDY; -. DR PhylomeDB; Q57920; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008821; F:crossover junction endodeoxyribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-HAMAP. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1350.10; -; 1. DR HAMAP; MF_01490; HJ_Resolv_Hjc; 1. DR InterPro; IPR002732; Hjc. DR InterPro; IPR014428; Hjc_arc. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF01870; Hjc; 1. DR PIRSF; PIRSF004985; Hlld_jn_rslvs_ar; 1. DR ProDom; PD015874; PD015874; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA recombination; DNA repair; KW DNA-binding; Endonuclease; Hydrolase; Magnesium; Metal-binding; KW Nuclease; Reference proteome. FT CHAIN 1 133 Holliday junction resolvase Hjc. FT /FTId=PRO_0000106899. FT ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_01490}. FT METAL 12 12 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01490}. FT METAL 36 36 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01490}. FT METAL 49 49 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01490}. FT SITE 51 51 Transition state stabilizer. FT {ECO:0000255}. SQ SEQUENCE 133 AA; 15232 MW; E49A8A128AF16506 CRC64; MRHKYRKGSS FERELKRLLE KEGFAVIRSA GSKGVDLIAG RKGEVLIFEC KTSSKTKFYI NKEDIEKLIS FSEIFGGKPY LAIKFNGEML FINPFLLSTN GKNYVIDERI KAIAIDFYEV IGRGKQLKID DLI // ID HDRB2_METJA Reviewed; 295 AA. AC Q58273; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=CoB--CoM heterodisulfide reductase subunit B 2; DE EC=1.8.98.1; GN Name=hdrB2; OrderedLocusNames=MJ0863; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the reversible CC reduction of CoM-S-S-CoB to the thiol-coenzymes H-S-CoM (coenzyme CC M) and H-S-CoB (coenzyme B). HdrB may have a function in energy CC transduction (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Coenzyme B + coenzyme M + methanophenazine = CC N-(7-((2-sulfoethyl)dithio)heptanoyl)-O(3)-phospho-L-threonine + CC dihydromethanophenazine. CC -!- PATHWAY: Cofactor metabolism; coenzyme M-coenzyme B CC heterodisulfide reduction; coenzyme B and coenzyme M from coenzyme CC M-coenzyme B heterodisulfide: step 1/1. CC -!- SUBUNIT: The heterodisulfide reductase is composed of three CC subunits; HdrA, HdrB and HdrC. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HdrB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98868.1; -; Genomic_DNA. DR PIR; G64407; G64407. DR STRING; 243232.MJ_0863; -. DR EnsemblBacteria; AAB98868; AAB98868; MJ_0863. DR KEGG; mja:MJ_0863; -. DR eggNOG; arCOG00338; Archaea. DR eggNOG; COG2048; LUCA. DR InParanoid; Q58273; -. DR KO; K03389; -. DR OMA; CQTVRAL; -. DR PhylomeDB; Q58273; -. DR UniPathway; UPA00647; UER00700. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051912; F:CoB--CoM heterodisulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0051186; P:cofactor metabolic process; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR017678; CoB/CoM_hetero-S_Rdtase_bsu. DR InterPro; IPR004017; Cys_rich_dom. DR Pfam; PF02754; CCG; 2. DR TIGRFAMs; TIGR03288; CoB_CoM_SS_B; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Oxidoreductase; Reference proteome. FT CHAIN 1 295 CoB--CoM heterodisulfide reductase FT subunit B 2. FT /FTId=PRO_0000150066. SQ SEQUENCE 295 AA; 32789 MW; 35A2A278491E8ED0 CRC64; MKYAFFLGCI MPHRYPGVEK ATKIVMEELG VELEYMPGAS CCPAPGVFGS FDQKTWLTLA ARNLCIAEEM GLDIVTVCNG CYGSLFEAAH ILHENKEALD FVNEKLDKIG KQYKGTIKVR HFAELIYKDI GVDKIKEKVV KPLDVLNVAI HYGCHFLKPS DVKHLDSPER PKLLEEIVAA TGAKPVMYRD YLMCCGAGGG VRARFLPTAL DMTKEKIRNM LEAGADCTVN VCPFCHLQFD RGQVEIKEKF GEEYKLPVLH LSQLLGLAFG MKPEDLAVSV HAIPVDPVLK KLGIE // ID HEM3_METJA Reviewed; 292 AA. AC Q57989; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Probable porphobilinogen deaminase; DE Short=PBG; DE EC=2.5.1.61; DE AltName: Full=Hydroxymethylbilane synthase; DE Short=HMBS; DE AltName: Full=Pre-uroporphyrinogen synthase; GN Name=hemC; OrderedLocusNames=MJ0569; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Tetrapolymerization of the monopyrrole PBG into the CC hydroxymethylbilane pre-uroporphyrinogen in several discrete CC steps. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 4 porphobilinogen + H(2)O = CC hydroxymethylbilane + 4 NH(3). CC -!- COFACTOR: CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342; CC Evidence={ECO:0000250}; CC Note=Binds 1 dipyrromethane group covalently. {ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 2/4. CC -!- MISCELLANEOUS: The porphobilinogen subunits are added to the CC dipyrromethane group. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HMBS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98563.1; -; Genomic_DNA. DR PIR; A64371; A64371. DR ProteinModelPortal; Q57989; -. DR STRING; 243232.MJ_0569; -. DR EnsemblBacteria; AAB98563; AAB98563; MJ_0569. DR KEGG; mja:MJ_0569; -. DR eggNOG; arCOG04299; Archaea. DR eggNOG; COG0181; LUCA. DR InParanoid; Q57989; -. DR KO; K01749; -. DR OMA; VATRINK; -. DR PhylomeDB; Q57989; -. DR UniPathway; UPA00251; UER00319. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0018160; P:peptidyl-pyrromethane cofactor linkage; IEA:InterPro. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.160.40; -; 1. DR HAMAP; MF_00260; Porphobil_deam; 1. DR InterPro; IPR000860; HemC. DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS. DR InterPro; IPR022417; Porphobilin_deaminase_N. DR InterPro; IPR022418; Porphobilinogen_deaminase_C. DR PANTHER; PTHR11557; PTHR11557; 1. DR Pfam; PF01379; Porphobil_deam; 1. DR Pfam; PF03900; Porphobil_deamC; 1. DR PIRSF; PIRSF001438; 4pyrrol_synth_OHMeBilane_synth; 1. DR PRINTS; PR00151; PORPHBDMNASE. DR SUPFAM; SSF54782; SSF54782; 1. DR TIGRFAMs; TIGR00212; hemC; 1. DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1. PE 3: Inferred from homology; KW Complete proteome; Porphyrin biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 292 Probable porphobilinogen deaminase. FT /FTId=PRO_0000143024. FT MOD_RES 233 233 S-(dipyrrolylmethanemethyl)cysteine. FT {ECO:0000250}. SQ SEQUENCE 292 AA; 32783 MW; F8E9823E484D2C06 CRC64; MIRIGTRGSK LALYQANKVA ELLKNLGYKV EIKIIKTTGD RVLDKKLSDI GIGVFTKELD LAMLNNEIDI AVHSLKDIPT IWNENLMVGA VLERDSYHDL LIWNKDIDFN EDSKIVIGTS SMRRRAFLKF IYPNAKFELL RGNVDTRLRK LKEGLYDAIV LSEAGIIRLG VSLEDFNYKR LDILPAPAQG IIAVACKRDD EEMKSILKEI NHERTYLESL CERTALNEFG GGCSVPFGAL AVYDEKNELL KLKAAVVTND ELKNASGEVK CKIDEIDKAV ELGKKIGLKL KN // ID HJA3_METJA Reviewed; 67 AA. AC Q58655; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Probable archaeal histone 3; GN OrderedLocusNames=MJ1258; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds and compact DNA (95 to 150 base pairs) to form CC nucleosome-like structures that contain positive DNA supercoils. CC Increases the resistance of DNA to thermal denaturation (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99261.1; -; Genomic_DNA. DR PIR; A64457; A64457. DR ProteinModelPortal; Q58655; -. DR SMR; Q58655; 2-66. DR STRING; 243232.MJ_1258; -. DR EnsemblBacteria; AAB99261; AAB99261; MJ_1258. DR KEGG; mja:MJ_1258; -. DR eggNOG; arCOG02144; Archaea. DR eggNOG; COG2036; LUCA. DR InParanoid; Q58655; -. DR OMA; EIEQHAR; -. DR PhylomeDB; Q58655; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR009072; Histone-fold. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 3: Inferred from homology; KW Chromosome; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 67 Probable archaeal histone 3. FT /FTId=PRO_0000154989. SQ SEQUENCE 67 AA; 7245 MW; 802E4C34E239DAB7 CRC64; MAELPVAPCV RILKKAGAQR VSEAAGKYFA EALEEIALEI ARKSVDLAKH AKRKTVKVED VKAALRG // ID HMPTM_METJA Reviewed; 506 AA. AC Q58036; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=7,8-dihydro-6-hydroxymethylpterin dimethyltransferase {ECO:0000305|PubMed:25002541}; DE Short=6-hydroxymethyl-H(2)pterin dimethyltransferase {ECO:0000305|PubMed:25002541}; DE EC=2.1.1.- {ECO:0000269|PubMed:25002541}; GN OrderedLocusNames=MJ0619; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A METHYLTRANSFERASE, REACTION MECHANISM, AND MUTAGENESIS RP OF CYS-77 AND CYS-102. RX PubMed=25002541; DOI=10.1128/JB.01903-14; RA Allen K.D., Xu H., White R.H.; RT "Identification of a unique radical S-Adenosylmethionine methylase RT likely involved in methanopterin biosynthesis in Methanocaldococcus RT jannaschii."; RL J. Bacteriol. 196:3315-3323(2014). CC -!- FUNCTION: Is responsible for the addition of methyl groups at C-7 CC and C-9 of the pterin ring during methanopterin (MPT) CC biosynthesis. Catalyzes methylation of 7,8-dihydro-6- CC hydroxymethylpterin, likely using methylenetetrahydromethanopterin CC as a methyl group donor, via a radical-based mechanism. CC {ECO:0000269|PubMed:25002541}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305|PubMed:25002541}; CC Note=Binds 2 [4Fe-4S] clusters. The clusters are coordinated with CC 3 cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305|PubMed:25002541}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000305|PubMed:25002541}; CC Note=Binds 2 S-adenosyl-L-methionine per subunit. CC {ECO:0000305|PubMed:25002541}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000303|PubMed:25002541}. CC -!- MISCELLANEOUS: The most N-terminal iron-sulfur cluster is involved CC in C-9 methylation, while the second cluster is required for C-7 CC methylation of the pterin ring. Moreover, C-7 methylation occurs CC before C-9 methylation. {ECO:0000269|PubMed:25002541}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98614.1; -; Genomic_DNA. DR PIR; C64377; C64377. DR ProteinModelPortal; Q58036; -. DR STRING; 243232.MJ_0619; -. DR DNASU; 1451485; -. DR EnsemblBacteria; AAB98614; AAB98614; MJ_0619. DR KEGG; mja:MJ_0619; -. DR eggNOG; arCOG00933; Archaea. DR eggNOG; COG1964; LUCA. DR InParanoid; Q58036; -. DR KO; K06937; -. DR OMA; GVRHIQL; -. DR PhylomeDB; Q58036; -. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 506 7,8-dihydro-6-hydroxymethylpterin FT dimethyltransferase. FT /FTId=PRO_0000106960. FT METAL 73 73 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT METAL 77 77 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT METAL 80 80 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT METAL 98 98 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT METAL 102 102 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT METAL 105 105 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000303|PubMed:25002541}. FT MUTAGEN 77 77 C->A: Loss of C9-methylation but C7- FT methylation is still observed. FT {ECO:0000269|PubMed:25002541}. FT MUTAGEN 102 102 C->A: Loss of methylation activity. FT {ECO:0000269|PubMed:25002541}. SQ SEQUENCE 506 AA; 57482 MW; 25FA1F6A380398D8 CRC64; MEKKTLSLCP ICLKRIPATI LEEDGKIIIK KTCPEHGEFK DIYWGDAELY KKFDKYEFIG KIEVTNTKVK NGCPYDCGLC PNHKSTTILA NIDVTNRCNL NCPICFANAN KSGKVYEPSF EDIKRMMENL RKEIPPTPAI QFAGGEPTVR SDLPELIKLA RDMGFLHVQL ATNGIKLKNI NYLKKLKEAG LSTIYLQFDG ISEKPYLVAR GKNLLPIKQK VIENCKKVGF DSVVLVPTLV RGVNDNEVGG IIRYAAENVD VVRGINFQPV SFTGRVDEKT LLEGRITIPD FIKLVEEQTD GEITEEDFYP VPSVAPISVL VEKLTNDRKP TLSSHQHCGT STYVFVDEDG KLIPITRFID VEGFLEIVKE KIEEIGKSKM HDVKVLGEIA LKLPSLIDLD KAPKSVNIKK IIDLILSVLK SDYSALAELH YHMLMISCMH FMDAYNFDVK RVMRCCIHYA TPDDRIIPFC TYNTLHRQEV EEKFSIPLEE WKRMHKIGGE DDREDY // ID HIS7_METJA Reviewed; 197 AA. AC Q58109; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Imidazoleglycerol-phosphate dehydratase {ECO:0000255|HAMAP-Rule:MF_00076}; DE Short=IGPD {ECO:0000255|HAMAP-Rule:MF_00076}; DE EC=4.2.1.19 {ECO:0000255|HAMAP-Rule:MF_00076}; GN Name=hisB {ECO:0000255|HAMAP-Rule:MF_00076}; OrderedLocusNames=MJ0698; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: D-erythro-1-(imidazol-4-yl)glycerol 3- CC phosphate = 3-(imidazol-4-yl)-2-oxopropyl phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 6/9. CC {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00076}. CC -!- SIMILARITY: Belongs to the imidazoleglycerol-phosphate dehydratase CC family. {ECO:0000255|HAMAP-Rule:MF_00076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98691.1; -; Genomic_DNA. DR PIR; B64387; B64387. DR ProteinModelPortal; Q58109; -. DR STRING; 243232.MJ_0698; -. DR EnsemblBacteria; AAB98691; AAB98691; MJ_0698. DR KEGG; mja:MJ_0698; -. DR eggNOG; arCOG04398; Archaea. DR eggNOG; COG0131; LUCA. DR InParanoid; Q58109; -. DR KO; K01693; -. DR OMA; HYEVIGK; -. DR PhylomeDB; Q58109; -. DR UniPathway; UPA00031; UER00011. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004424; F:imidazoleglycerol-phosphate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00076; HisB; 1. DR InterPro; IPR000807; ImidazoleglycerolP_deHydtase. DR InterPro; IPR020565; ImidazoleglycerP_deHydtase_CS. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR PANTHER; PTHR23133:SF2; PTHR23133:SF2; 1. DR Pfam; PF00475; IGPD; 1. DR SUPFAM; SSF54211; SSF54211; 2. DR PROSITE; PS00954; IGP_DEHYDRATASE_1; 1. DR PROSITE; PS00955; IGP_DEHYDRATASE_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Lyase; Reference proteome. FT CHAIN 1 197 Imidazoleglycerol-phosphate dehydratase. FT /FTId=PRO_0000158189. SQ SEQUENCE 197 AA; 22158 MW; B4E5500ADB4A5D01 CRC64; MFGGNMRIFE VMRETKETNI YLKINIDGTG KYKIDTGIPF FDHLLASFAK HGCFDLIVKA RGDLEIDDHH TVEDVGICLG LALNQIEKRN IFRFGWAIIP MDDARATVAI DLSGRSYCVG NYEPKREFVG DLATENINHF FESVASYGML NIHYEVIGKN EHHKAEALFK AFGVALDLAT KIDERKGVIS TKGEVKL // ID HIS8_METJA Reviewed; 373 AA. AC Q58365; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Histidinol-phosphate aminotransferase; DE EC=2.6.1.9; DE AltName: Full=Imidazole acetol-phosphate transaminase; GN Name=hisC; OrderedLocusNames=MJ0955; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: L-histidinol phosphate + 2-oxoglutarate = 3- CC (imidazol-4-yl)-2-oxopropyl phosphate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 7/9. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. Histidinol-phosphate aminotransferase CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98960.1; -; Genomic_DNA. DR PIR; C64419; C64419. DR ProteinModelPortal; Q58365; -. DR STRING; 243232.MJ_0955; -. DR EnsemblBacteria; AAB98960; AAB98960; MJ_0955. DR KEGG; mja:MJ_0955; -. DR eggNOG; arCOG04273; Archaea. DR eggNOG; COG0079; LUCA. DR InParanoid; Q58365; -. DR KO; K00817; -. DR OMA; YPSEANY; -. DR PhylomeDB; Q58365; -. DR UniPathway; UPA00031; UER00012. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004400; F:histidinol-phosphate transaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0080130; F:L-phenylalanine:2-oxoglutarate aminotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01023; HisC_aminotrans_2; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR005861; HisP_aminotrans. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR01141; hisC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; Complete proteome; KW Histidine biosynthesis; Pyridoxal phosphate; Reference proteome; KW Transferase. FT CHAIN 1 373 Histidinol-phosphate aminotransferase. FT /FTId=PRO_0000153496. FT MOD_RES 231 231 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 373 AA; 42962 MW; 369DB5EB4C671218 CRC64; MGDWMIENKV RDVVKKLKPY VPGKSKEEIA RAYGIKPEDI IKLGSNENPW GPSPKIKEKI LDEIDKIHQY PEPVNPILMK ELSKFLNVDE ENIIVGGDGA DEIIDTIFRT FVDDGDEVII PIPTFTQYRV SATIHNAKIK YAKYDKEKDF KLNVESVLNN ITDKTKVIFL CTPNNPTGNI IENRDVERVI NETDALVVID HAYIEYAKKE YDWTQKAPEY DNVIVLRTFS KVFGLAGMRV GYGVANKKII DYMMRVKPIF SLTRLSQVCA ITALRDREFF ERCVRDGIKS REMLYNGLKK FKDIKVYPSE ANYLLVELKT MKAKEFCEEL LKRGVIVRDC TSFDGLGDNY VRVSIGTFEE VERFLKILEE IIS // ID HMDH_METJA Reviewed; 405 AA. AC Q58116; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=3-hydroxy-3-methylglutaryl-coenzyme A reductase; DE Short=HMG-CoA reductase; DE EC=1.1.1.34; GN Name=hmgA; OrderedLocusNames=MJ0705; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Converts HMG-CoA to mevalonate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (R)-mevalonate + CoA + 2 NADP(+) = (S)-3- CC hydroxy-3-methylglutaryl-CoA + 2 NADPH. CC -!- PATHWAY: Metabolic intermediate biosynthesis; (R)-mevalonate CC biosynthesis; (R)-mevalonate from acetyl-CoA: step 3/3. CC -!- SIMILARITY: Belongs to the HMG-CoA reductase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98699.1; -; Genomic_DNA. DR PIR; A64388; A64388. DR ProteinModelPortal; Q58116; -. DR STRING; 243232.MJ_0705; -. DR EnsemblBacteria; AAB98699; AAB98699; MJ_0705. DR KEGG; mja:MJ_0705; -. DR eggNOG; arCOG04260; Archaea. DR eggNOG; COG1257; LUCA. DR InParanoid; Q58116; -. DR KO; K00021; -. DR OMA; FKTGDAM; -. DR PhylomeDB; Q58116; -. DR UniPathway; UPA00058; UER00103. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0004420; F:hydroxymethylglutaryl-CoA reductase (NADPH) activity; IBA:GO_Central. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR GO; GO:0015936; P:coenzyme A metabolic process; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central. DR GO; GO:0016126; P:sterol biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.420; -; 1. DR Gene3D; 3.90.770.10; -; 2. DR InterPro; IPR002202; HMG_CoA_Rdtase. DR InterPro; IPR023074; HMG_CoA_Rdtase_cat. DR InterPro; IPR023076; HMG_CoA_Rdtase_CS. DR InterPro; IPR004554; HMG_CoA_Rdtase_eu_arc. DR InterPro; IPR009023; HMG_CoA_Rdtase_NAD(P)-bd_dom. DR InterPro; IPR009029; HMG_CoA_Rdtase_sub-bd_dom. DR PANTHER; PTHR10572; PTHR10572; 1. DR Pfam; PF00368; HMG-CoA_red; 1. DR PRINTS; PR00071; HMGCOARDTASE. DR SUPFAM; SSF55035; SSF55035; 1. DR SUPFAM; SSF56542; SSF56542; 2. DR TIGRFAMs; TIGR00533; HMG_CoA_R_NADP; 1. DR PROSITE; PS00066; HMG_COA_REDUCTASE_1; 1. DR PROSITE; PS00318; HMG_COA_REDUCTASE_2; 1. DR PROSITE; PS50065; HMG_COA_REDUCTASE_4; 1. PE 3: Inferred from homology; KW Complete proteome; Isoprene biosynthesis; NADP; Oxidoreductase; KW Reference proteome. FT CHAIN 1 405 3-hydroxy-3-methylglutaryl-coenzyme A FT reductase. FT /FTId=PRO_0000114461. FT ACT_SITE 100 100 Charge relay system. {ECO:0000250}. FT ACT_SITE 310 310 Charge relay system. {ECO:0000250}. FT ACT_SITE 400 400 Proton donor. {ECO:0000250}. SQ SEQUENCE 405 AA; 44128 MW; F8F8E4729A77DFC9 CRC64; MENYNDILEK MLNGEIKPYQ LDKMFGSKIA TEIRRKFIEK KVGIEFKHIC NYSIDEEMAM KKNIENMIGA IQIPLGFAGP LKINGEYAKG EFYIPLATTE GALVASVNRG CSIITKCGGA TVRVIDDKMT RAPCLKTKSV VDAIKVRDWI RENFERIKEV AESTTRHGKL IKIEPILIVG RNLYPRFVFK TGDAMGMNMV TIATEKACNF IEGELKKEGI FVKTVAVSGN ACVDKKPSGM NLINGRGKSI VAEVFLTEKE VNKYLKTTSQ AIAEVNRLKN YIGSAISNSM GFNAHYANII GAIFLATGQD EAHIVEGSLG ITMAEVEDDG LYFSVTLPDV PIGTVGGGTR VETQKECLEM LGCYGDNKAL KFAEIVGAAV LAGELSLLGA LAAGHLGKAH QELGR // ID HEM2_METJA Reviewed; 335 AA. AC Q60178; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Delta-aminolevulinic acid dehydratase; DE Short=ALAD; DE Short=ALADH; DE EC=4.2.1.24; DE AltName: Full=Porphobilinogen synthase; GN Name=hemB; OrderedLocusNames=MJ0643; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes an early step in the biosynthesis of CC tetrapyrroles. Binds two molecules of 5-aminolevulinate per CC subunit, each at a distinct site, and catalyzes their condensation CC to form porphobilinogen (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 5-aminolevulinate = porphobilinogen + 2 CC H(2)O. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per monomer. {ECO:0000250}; CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin- CC IX biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: CC step 1/4. CC -!- SUBUNIT: Homooctamer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ALAD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98637.1; -; Genomic_DNA. DR PIR; C64380; C64380. DR ProteinModelPortal; Q60178; -. DR SMR; Q60178; 11-330. DR STRING; 243232.MJ_0643; -. DR PRIDE; Q60178; -. DR EnsemblBacteria; AAB98637; AAB98637; MJ_0643. DR KEGG; mja:MJ_0643; -. DR eggNOG; arCOG04300; Archaea. DR eggNOG; COG0113; LUCA. DR InParanoid; Q60178; -. DR KO; K01698; -. DR OMA; MDPANSN; -. DR PhylomeDB; Q60178; -. DR UniPathway; UPA00251; UER00318. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004655; F:porphobilinogen synthase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006783; P:heme biosynthetic process; IBA:GO_Central. DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR001731; ALAD. DR InterPro; IPR030656; ALAD_AS. DR InterPro; IPR013785; Aldolase_TIM. DR PANTHER; PTHR11458; PTHR11458; 1. DR Pfam; PF00490; ALAD; 1. DR PIRSF; PIRSF001415; Porphbilin_synth; 1. DR PRINTS; PR00144; DALDHYDRTASE. DR SMART; SM01004; ALAD; 1. DR PROSITE; PS00169; D_ALA_DEHYDRATASE; 1. PE 3: Inferred from homology; KW Complete proteome; Heme biosynthesis; Lyase; Magnesium; Metal-binding; KW Porphyrin biosynthesis; Reference proteome; Zinc. FT CHAIN 1 335 Delta-aminolevulinic acid dehydratase. FT /FTId=PRO_0000140523. FT ACT_SITE 204 204 Schiff-base intermediate with substrate. FT {ECO:0000250}. FT ACT_SITE 257 257 Schiff-base intermediate with substrate. FT {ECO:0000250}. FT METAL 129 129 Zinc; catalytic. {ECO:0000250}. FT METAL 131 131 Zinc; catalytic. {ECO:0000250}. FT METAL 139 139 Zinc; catalytic. {ECO:0000250}. FT METAL 242 242 Magnesium. {ECO:0000250}. FT BINDING 214 214 Substrate 1. {ECO:0000250}. FT BINDING 226 226 Substrate 1. {ECO:0000250}. FT BINDING 283 283 Substrate 2. {ECO:0000250}. FT BINDING 322 322 Substrate 2. {ECO:0000250}. SQ SEQUENCE 335 AA; 37396 MW; 4D097DAB45F3705D CRC64; MFKINLGDFM LIRPRRLRKN QKIRDLVRET ILTKNDLIMP IFVDENLKGN EKKEISSMPN QYRFSVEGAI EEAKEIADLG IPAVILFGIP KHKDEIASSA YDKNGVVQRT IRGIKEELGD ELLVIADCCL CEYTSHGHCG IVKDGKILND ATLPILAKIA LSYADAGVDI VAPSDMMDGR VRAIREILEE NGYDDVAIMS YSAKYASSFY GPFREAAESA PKFGDRKSYQ MDIGNAREAL KEIALDIEEG ADLILVKPAL PYLDIIRMAK DRFDVPIGGY CVSGEYAMVE AAARNGWLDR EKVIYEILLS IKRAGADFII TYWAKEVAEI GLSQE // ID HIS3_METJA Reviewed; 127 AA. AC Q58825; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Phosphoribosyl-AMP cyclohydrolase {ECO:0000255|HAMAP-Rule:MF_01021}; DE Short=PRA-CH {ECO:0000255|HAMAP-Rule:MF_01021}; DE EC=3.5.4.19 {ECO:0000255|HAMAP-Rule:MF_01021}; GN Name=hisI {ECO:0000255|HAMAP-Rule:MF_01021}; OrderedLocusNames=MJ1430; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the hydrolysis of the adenine ring of CC phosphoribosyl-AMP. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-AMP + H(2)O = 1- CC (5-phospho-beta-D-ribosyl)-5-((5-phospho-beta-D- CC ribosylamino)methylideneamino)imidazole-4-carboxamide. CC {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01021}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01021}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 3/9. CC {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01021}. CC -!- SIMILARITY: Belongs to the PRA-CH family. {ECO:0000255|HAMAP- CC Rule:MF_01021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99440.1; -; Genomic_DNA. DR PIR; E64478; E64478. DR ProteinModelPortal; Q58825; -. DR SMR; Q58825; 11-121. DR STRING; 243232.MJ_1430; -. DR EnsemblBacteria; AAB99440; AAB99440; MJ_1430. DR KEGG; mja:MJ_1430; -. DR eggNOG; arCOG02676; Archaea. DR eggNOG; COG0139; LUCA. DR InParanoid; Q58825; -. DR KO; K01496; -. DR OMA; VACHEGY; -. DR PhylomeDB; Q58825; -. DR UniPathway; UPA00031; UER00008. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004635; F:phosphoribosyl-AMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01021; HisI; 1. DR InterPro; IPR026660; PRA-CH. DR InterPro; IPR002496; PRib_AMP_CycHydrolase_dom. DR Pfam; PF01502; PRA-CH; 1. DR ProDom; PD002610; PRA_CycHdrlase; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Hydrolase; Magnesium; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 127 Phosphoribosyl-AMP cyclohydrolase. FT /FTId=PRO_0000136507. FT METAL 83 83 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 84 84 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 85 85 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 87 87 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01021}. FT METAL 100 100 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. FT METAL 107 107 Zinc; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_01021}. SQ SEQUENCE 127 AA; 14926 MW; DEDB2D6D46431B2B CRC64; MDVEDTVKKL NLKFRNIEGE RLILAITCDE NKNVLMVAFM NEEALKKTLE TGYMHYYSTS RKKLWRKGEE SGNVQKLIKF YRDCDGDALL FIVEQKGVAC HEGYYSCFHY KIEDGELKIT GEYYSKR // ID HIS4_METJA Reviewed; 237 AA. AC Q58927; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino] imidazole-4-carboxamide isomerase; DE EC=5.3.1.16; DE AltName: Full=Phosphoribosylformimino-5-aminoimidazole carboxamide ribotide isomerase; GN Name=hisA; OrderedLocusNames=MJ1532; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 1-(5-phospho-beta-D-ribosyl)-5-((5-phospho- CC beta-D-ribosylamino)methylideneamino)imidazole-4-carboxamide = 5- CC ((5-phospho-1-deoxy-D-ribulos-1-ylamino)methylideneamino)-1-(5- CC phospho-beta-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 4/9. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99553.1; -; Genomic_DNA. DR PIR; C64491; C64491. DR ProteinModelPortal; Q58927; -. DR STRING; 243232.MJ_1532; -. DR EnsemblBacteria; AAB99553; AAB99553; MJ_1532. DR KEGG; mja:MJ_1532; -. DR eggNOG; arCOG00618; Archaea. DR eggNOG; COG0106; LUCA. DR InParanoid; Q58927; -. DR KO; K01814; -. DR OMA; EWLHLVD; -. DR PhylomeDB; Q58927; -. DR UniPathway; UPA00031; UER00009. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01014; HisA; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR006063; HisA. DR InterPro; IPR023016; Isoase_HisA. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00007; TIGR00007; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Histidine biosynthesis; Isomerase; Reference proteome. FT CHAIN 1 237 1-(5-phosphoribosyl)-5-[(5- FT phosphoribosylamino)methylideneamino] FT imidazole-4-carboxamide isomerase. FT /FTId=PRO_0000142092. FT ACT_SITE 8 8 Proton acceptor. {ECO:0000250}. FT ACT_SITE 129 129 Proton donor. {ECO:0000250}. SQ SEQUENCE 237 AA; 26132 MW; D11E3AD24C01AC2A CRC64; MIIIPAVDLK DKKCVQLIQG DPNKKHLELN NPVEVAKKFV DEGAEYLHII DLDAAFGTGN NRDVIKNIIK EVNVPVEVGG GIRNLEIAKE LISLGVDRVI VGTKAILEPK FIDDLNKEIG KDKIVLAVEC KEGKVVIKGW KEKVDKTPIE VIKEFEDKVG YILFTNVDVE GLLKGINVDI IKELIEKTDI PIIYSGGITT LEDIKALKEL GIYGVVIGSA LYKGLIDLKK ALEIVKN // ID HIS5_METJA Reviewed; 196 AA. AC Q57929; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 08-DEC-2000, sequence version 2. DT 17-FEB-2016, entry version 99. DE RecName: Full=Imidazole glycerol phosphate synthase subunit HisH; DE EC=2.4.2.-; DE AltName: Full=IGP synthase glutamine amidotransferase subunit; DE AltName: Full=IGP synthase subunit HisH; DE AltName: Full=ImGP synthase subunit HisH; DE Short=IGPS subunit HisH; GN Name=hisH; OrderedLocusNames=MJ0506; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: IGPS catalyzes the conversion of PRFAR and glutamine to CC IGP, AICAR and glutamate. The HisH subunit provides the glutamine CC amidotransferase activity that produces the ammonia necessary to CC HisF for the synthesis of IGP and AICAR (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-[(5-phospho-1-deoxyribulos-1- CC ylamino)methylideneamino]-1-(5-phosphoribosyl)imidazole-4- CC carboxamide + L-glutamine = imidazole-glycerol phosphate + 5- CC aminoimidazol-4-carboxamide ribonucleotide + L-glutamate + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 5/9. CC -!- SUBUNIT: Heterodimer of HisH and HisF. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98496.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98496.1; ALT_INIT; Genomic_DNA. DR PIR; B64363; B64363. DR ProteinModelPortal; Q57929; -. DR STRING; 243232.MJ_0506; -. DR MEROPS; C26.965; -. DR EnsemblBacteria; AAB98496; AAB98496; MJ_0506. DR KEGG; mja:MJ_0506; -. DR eggNOG; arCOG00089; Archaea. DR eggNOG; COG0118; LUCA. DR InParanoid; Q57929; -. DR KO; K02501; -. DR OMA; GMQMLLT; -. DR PhylomeDB; Q57929; -. DR UniPathway; UPA00031; UER00010. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0000107; F:imidazoleglycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00278; HisH; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010139; Imidazole-glycPsynth_HisH. DR Pfam; PF00117; GATase; 1. DR PIRSF; PIRSF000495; Amidotransf_hisH; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01855; IMP_synth_hisH; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Cytoplasm; KW Glutamine amidotransferase; Histidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 196 Imidazole glycerol phosphate synthase FT subunit HisH. FT /FTId=PRO_0000152458. FT DOMAIN 1 196 Glutamine amidotransferase type-1. FT ACT_SITE 76 76 Nucleophile. {ECO:0000250}. FT ACT_SITE 177 177 {ECO:0000250}. FT ACT_SITE 179 179 {ECO:0000250}. SQ SEQUENCE 196 AA; 22101 MW; 4D4E20DDE0AA2F5F CRC64; MIGIIDYNAG NLRSIQKAVE LYDKVIITNN SEELLACDKI ILPGVGNFGS AMENLAPLKE TIYKIVDDRV PFLGICLGMQ ILFEESEEKR GIKGLGIIKG NVIKFKDVEK LPHMGWNSVK IVKDCPLFEG IKNNSYFYFV HSYHVNPDED CIVGKTEYGR EFPSVINKDN VFATQFHPEK SGKIGLKIIE NFVELL // ID HJA4_METJA Reviewed; 67 AA. AC Q60264; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 81. DE RecName: Full=Probable archaeal histone 4; GN OrderedLocusNames=MJECL29; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds and compact DNA (95 to 150 base pairs) to form CC nucleosome-like structures that contain positive DNA supercoils. CC Increases the resistance of DNA to thermal denaturation (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37073.1; -; Genomic_DNA. DR PIR; D64513; D64513. DR ProteinModelPortal; Q60264; -. DR SMR; Q60264; 3-66. DR EnsemblBacteria; AAC37073; AAC37073; MJ_ECL29. DR KEGG; mja:MJECL29; -. DR HOGENOM; HOG000222925; -. DR InParanoid; Q60264; -. DR OMA; KENDKTF; -. DR PhylomeDB; Q60264; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR004823; TAF_TATA-bd. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 3: Inferred from homology; KW Chromosome; Complete proteome; Cytoplasm; DNA-binding; Plasmid; KW Reference proteome. FT CHAIN 1 67 Probable archaeal histone 4. FT /FTId=PRO_0000154990. SQ SEQUENCE 67 AA; 7476 MW; 1022FDE19747FB5C CRC64; MTELPVAPFE RILKKVGAER VSRAAAEYLA EAFEEIALEI AKEAVDLAKH AKRKTVKVED IKLALKK // ID HMD_METJA Reviewed; 358 AA. AC Q58194; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=5,10-methenyltetrahydromethanopterin hydrogenase; DE EC=1.12.98.2; DE AltName: Full=H(2)-dependent methylene-H(4)MPT dehydrogenase; DE AltName: Full=H(2)-forming N(5),N(10)-methylenetetrahydromethanopterin dehydrogenase; DE AltName: Full=N(5),N(10)-methenyltetrahydromethanopterin hydrogenase; GN Name=hmd; OrderedLocusNames=MJ0784; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible reduction of methenyl- CC H(4)MPT(+) to methylene-H(4)MPT. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: H(2) + 5,10-methenyltetrahydromethanopterin = CC H(+) + 5,10-methylenetetrahydromethanopterin. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl- CC 5,6,7,8-tetrahydromethanopterin (hydrogen route): step 1/1. CC -!- SIMILARITY: Belongs to the HMD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98781.1; -; Genomic_DNA. DR PIR; H64397; H64397. DR PDB; 2B0J; X-ray; 1.75 A; A=1-358. DR PDB; 3DAF; X-ray; 1.75 A; A=1-358. DR PDB; 3DAG; X-ray; 1.75 A; A=1-358. DR PDB; 3F46; X-ray; 1.95 A; A=1-358. DR PDB; 3F47; X-ray; 1.75 A; A=1-358. DR PDB; 3H65; X-ray; 2.15 A; A=1-358. DR PDBsum; 2B0J; -. DR PDBsum; 3DAF; -. DR PDBsum; 3DAG; -. DR PDBsum; 3F46; -. DR PDBsum; 3F47; -. DR PDBsum; 3H65; -. DR ProteinModelPortal; Q58194; -. DR SMR; Q58194; 1-344. DR STRING; 243232.MJ_0784; -. DR PRIDE; Q58194; -. DR EnsemblBacteria; AAB98781; AAB98781; MJ_0784. DR KEGG; mja:MJ_0784; -. DR eggNOG; arCOG03196; Archaea. DR eggNOG; COG4074; LUCA. DR KO; K13942; -. DR OMA; THACTIP; -. DR PhylomeDB; Q58194; -. DR BRENDA; 1.12.98.2; 3260. DR UniPathway; UPA00640; UER00696. DR EvolutionaryTrace; Q58194; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IEA:InterPro. DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_01090; HMD; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR010062; HMD_. DR InterPro; IPR004889; HMD_C. DR InterPro; IPR024190; METHMP_Hmd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF03201; HMD; 1. DR PIRSF; PIRSF016158; HMD; 1. DR PIRSF; PIRSF500165; HMDI; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01723; hmd_TIGR; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methanogenesis; KW One-carbon metabolism; Oxidoreductase; Reference proteome. FT CHAIN 1 358 5,10-methenyltetrahydromethanopterin FT hydrogenase. FT /FTId=PRO_0000218508. FT STRAND 2 6 {ECO:0000244|PDB:2B0J}. FT HELIX 12 17 {ECO:0000244|PDB:2B0J}. FT HELIX 23 32 {ECO:0000244|PDB:2B0J}. FT HELIX 35 39 {ECO:0000244|PDB:2B0J}. FT HELIX 42 53 {ECO:0000244|PDB:2B0J}. FT STRAND 59 63 {ECO:0000244|PDB:2B0J}. FT HELIX 65 68 {ECO:0000244|PDB:2B0J}. FT STRAND 69 75 {ECO:0000244|PDB:2B0J}. FT HELIX 81 89 {ECO:0000244|PDB:2B0J}. FT HELIX 93 95 {ECO:0000244|PDB:2B0J}. FT HELIX 97 109 {ECO:0000244|PDB:2B0J}. FT TURN 114 116 {ECO:0000244|PDB:2B0J}. FT STRAND 117 122 {ECO:0000244|PDB:2B0J}. FT HELIX 124 127 {ECO:0000244|PDB:2B0J}. FT STRAND 130 133 {ECO:0000244|PDB:2B0J}. FT HELIX 135 139 {ECO:0000244|PDB:2B0J}. FT STRAND 143 147 {ECO:0000244|PDB:2B0J}. FT STRAND 151 154 {ECO:0000244|PDB:3DAF}. FT HELIX 155 162 {ECO:0000244|PDB:2B0J}. FT HELIX 163 165 {ECO:0000244|PDB:2B0J}. FT STRAND 171 174 {ECO:0000244|PDB:2B0J}. FT STRAND 176 178 {ECO:0000244|PDB:2B0J}. FT HELIX 180 189 {ECO:0000244|PDB:2B0J}. FT STRAND 195 199 {ECO:0000244|PDB:2B0J}. FT TURN 206 208 {ECO:0000244|PDB:2B0J}. FT STRAND 212 219 {ECO:0000244|PDB:2B0J}. FT HELIX 221 235 {ECO:0000244|PDB:2B0J}. FT STRAND 238 242 {ECO:0000244|PDB:2B0J}. FT HELIX 243 245 {ECO:0000244|PDB:2B0J}. FT HELIX 246 250 {ECO:0000244|PDB:2B0J}. FT HELIX 254 272 {ECO:0000244|PDB:2B0J}. FT HELIX 279 300 {ECO:0000244|PDB:2B0J}. FT HELIX 302 304 {ECO:0000244|PDB:2B0J}. FT HELIX 305 308 {ECO:0000244|PDB:2B0J}. FT HELIX 311 316 {ECO:0000244|PDB:2B0J}. FT HELIX 318 321 {ECO:0000244|PDB:2B0J}. FT HELIX 324 326 {ECO:0000244|PDB:2B0J}. FT HELIX 329 339 {ECO:0000244|PDB:2B0J}. SQ SEQUENCE 358 AA; 38689 MW; 9D8E789759BCF43A CRC64; MKIAILGAGC YRTHAAAGIT NFMRACEVAK EVGKPEIALT HSSITYGAEL LHLVPDVKEV IVSDPCFAEE PGLVVIDEFD PKEVMEAHLS GNPESIMPKI REVVKAKAKE LPKPPKACIH LVHPEDVGLK VTSDDREAVE GADIVITWLP KGNKQPDIIK KFADAIPEGA IVTHACTIPT TKFAKIFKDL GREDLNITSY HPGCVPEMKG QVYIAEGYAS EEAVNKLYEI GKIARGKAFK MPANLIGPVC DMCSAVTATV YAGLLAYRDA VTKILGAPAD FAQMMADEAL TQIHNLMKEK GIANMEEALD PAALLGTADS MCFGPLAEIL PTALKVLEKH KVVEEEGKTK CEIMSQKE // ID HJA1_METJA Reviewed; 67 AA. AC Q57632; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Probable archaeal histone 1; GN OrderedLocusNames=MJ0168; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds and compact DNA (95 to 150 base pairs) to form CC nucleosome-like structures that contain positive DNA supercoils. CC Increases the resistance of DNA to thermal denaturation (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98153.1; -; Genomic_DNA. DR PIR; A64321; A64321. DR ProteinModelPortal; Q57632; -. DR SMR; Q57632; 2-66. DR STRING; 243232.MJ_0168; -. DR EnsemblBacteria; AAB98153; AAB98153; MJ_0168. DR KEGG; mja:MJ_0168; -. DR eggNOG; arCOG02144; Archaea. DR eggNOG; COG2036; LUCA. DR InParanoid; Q57632; -. DR OMA; CKHAGRK; -. DR PhylomeDB; Q57632; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR009072; Histone-fold. DR InterPro; IPR004823; TAF_TATA-bd. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR SMART; SM00803; TAF; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 3: Inferred from homology; KW Chromosome; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 67 Probable archaeal histone 1. FT /FTId=PRO_0000154987. SQ SEQUENCE 67 AA; 7384 MW; 103E8B391D9C927C CRC64; MAELPVAPFE RILKKAGAER VSRAAAEYLA EAVEEIALEI AKEAVELAKH AKRKTVKVED IKLALKK // ID HMDY_METJA Reviewed; 353 AA. AC Q58734; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein MJ1338; GN OrderedLocusNames=MJ1338; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HMD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99348.1; -; Genomic_DNA. DR PIR; A64467; A64467. DR PDB; 4YT2; X-ray; 1.65 A; A/B=8-353. DR PDB; 4YT4; X-ray; 2.20 A; A=1-353. DR PDB; 4YT5; X-ray; 1.90 A; A/B=1-353. DR PDB; 4YT8; X-ray; 1.90 A; A/B=1-353. DR PDBsum; 4YT2; -. DR PDBsum; 4YT4; -. DR PDBsum; 4YT5; -. DR PDBsum; 4YT8; -. DR ProteinModelPortal; Q58734; -. DR STRING; 243232.MJ_1338; -. DR EnsemblBacteria; AAB99348; AAB99348; MJ_1338. DR KEGG; mja:MJ_1338; -. DR eggNOG; arCOG03195; Archaea. DR eggNOG; COG4007; LUCA. DR OMA; IMTLQTM; -. DR PhylomeDB; Q58734; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IEA:InterPro. DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR010063; HMD-rel. DR InterPro; IPR004889; HMD_C. DR InterPro; IPR024190; METHMP_Hmd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF03201; HMD; 1. DR PIRSF; PIRSF016158; HMD; 1. DR PIRSF; PIRSF500166; HMDII_III; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01724; hmd_rel; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 353 H(2)-forming FT methylenetetrahydromethanopterin FT dehydrogenase-related protein MJ1338. FT /FTId=PRO_0000218518. FT STRAND 13 17 {ECO:0000244|PDB:4YT2}. FT HELIX 22 26 {ECO:0000244|PDB:4YT2}. FT HELIX 31 34 {ECO:0000244|PDB:4YT2}. FT HELIX 43 52 {ECO:0000244|PDB:4YT2}. FT STRAND 56 60 {ECO:0000244|PDB:4YT2}. FT HELIX 64 66 {ECO:0000244|PDB:4YT2}. FT HELIX 69 77 {ECO:0000244|PDB:4YT2}. FT STRAND 81 84 {ECO:0000244|PDB:4YT2}. FT HELIX 86 92 {ECO:0000244|PDB:4YT2}. FT STRAND 94 98 {ECO:0000244|PDB:4YT2}. FT TURN 102 104 {ECO:0000244|PDB:4YT2}. FT HELIX 105 114 {ECO:0000244|PDB:4YT2}. FT STRAND 122 125 {ECO:0000244|PDB:4YT2}. FT STRAND 127 129 {ECO:0000244|PDB:4YT2}. FT HELIX 131 142 {ECO:0000244|PDB:4YT2}. FT TURN 143 148 {ECO:0000244|PDB:4YT2}. FT STRAND 150 153 {ECO:0000244|PDB:4YT2}. FT STRAND 167 173 {ECO:0000244|PDB:4YT2}. FT HELIX 183 195 {ECO:0000244|PDB:4YT2}. FT STRAND 199 204 {ECO:0000244|PDB:4YT2}. FT TURN 205 207 {ECO:0000244|PDB:4YT2}. FT HELIX 208 212 {ECO:0000244|PDB:4YT2}. FT HELIX 216 235 {ECO:0000244|PDB:4YT2}. FT HELIX 241 271 {ECO:0000244|PDB:4YT2}. FT HELIX 273 281 {ECO:0000244|PDB:4YT2}. FT HELIX 290 300 {ECO:0000244|PDB:4YT2}. FT HELIX 304 312 {ECO:0000244|PDB:4YT2}. FT HELIX 323 334 {ECO:0000244|PDB:4YT2}. FT HELIX 336 351 {ECO:0000244|PDB:4YT2}. SQ SEQUENCE 353 AA; 38212 MW; 2AFF9FD87675F6A6 CRC64; MRNIRKIKVD NMKVSVYGAG NQNLYINKLN LPEKFGGEPP YGGSRMAIEF AEAGHDVVLA EPNKNIMSDD LWKKVEDAGV KVVSDDVEAA KHGEIHVLFT PFGKATFRIA KTIIEHVPEN AVICNTCTVS PVVLYYSLEP ILRTKRKDVG ISSMHPAAVP GTPQHGHYVI GGKTTDGKEL ATEEQIKKAV ELAKSAGKEA YVVPADVSSV VADMGSLVTA VALSGVLDYY TVGRKIINAP KKMIEQQVIM TLQTMASLVE TSGIEGMVKA LNPELLIRSA SSMKLLDRQK DLDAALEILQ NLDETLKAEV EKAEIKPTTL VAAQSLVKEI KTLIGGAAAE GAIKRSARKL FEH // ID HMVA_METJA Reviewed; 96 AA. AC Q59041; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=DNA-binding protein HmvA; GN Name=hmvA; OrderedLocusNames=MJ1647; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SUBUNIT. RX PubMed=10741836; DOI=10.1007/s007920050006; RA Li W.-T., Sandman K., Pereira S.L., Reeve J.N.; RT "MJ1647, an open reading frame in the genome of the hyperthermophile RT Methanococcus jannaschii, encodes a very thermostable archaeal histone RT with a C-terminal extension."; RL Extremophiles 4:43-51(2000). CC -!- FUNCTION: Binds and compacts DNA to form nucleosome-like CC structures that contain positive DNA supercoils. Increases the CC resistance of DNA to thermal denaturation (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10741836}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. Chromosome CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the archaeal histone HMF family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99668.1; -; Genomic_DNA. DR PIR; E64505; E64505. DR ProteinModelPortal; Q59041; -. DR STRING; 243232.MJ_1647; -. DR EnsemblBacteria; AAB99668; AAB99668; MJ_1647. DR KEGG; mja:MJ_1647; -. DR eggNOG; arCOG02145; Archaea. DR eggNOG; COG2036; LUCA. DR OMA; MKENTDM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR003958; CBFA_NFYB_domain. DR InterPro; IPR009072; Histone-fold. DR Pfam; PF00808; CBFD_NFYB_HMF; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 1: Evidence at protein level; KW Chromosome; Complete proteome; Cytoplasm; DNA-binding; KW Reference proteome. FT CHAIN 1 96 DNA-binding protein HmvA. FT /FTId=PRO_0000155005. SQ SEQUENCE 96 AA; 11201 MW; D64F2C5841855C42 CRC64; MLPKATVKRI MKQHTDFNIS AEAVDELCNM LEEIIKITTE VAEQNARKEG RKTIKARDIK QCDDERLKRK IMELSERTDK MPILIKEMLN VITSEL // ID HSPS_METJA Reviewed; 147 AA. AC Q57733; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Small heat shock protein HSP16.5; GN OrderedLocusNames=MJ0285; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9689045; DOI=10.1073/pnas.95.16.9129; RA Kim R., Kim K.K., Yokota H., Kim S.-H.; RT "Small heat shock protein of Methanococcus jannaschii, a RT hyperthermophile."; RL Proc. Natl. Acad. Sci. U.S.A. 95:9129-9133(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9707123; DOI=10.1038/29106; RA Kim K.K., Kim R., Kim S.-H.; RT "Crystal structure of a small heat-shock protein."; RL Nature 394:595-599(1998). CC -!- FUNCTION: Chaperone that confers thermal protection to other CC proteins. CC -!- SUBUNIT: Homooligomer of 24 subunits. Forms a spherical shape. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the small heat shock protein (HSP20) CC family. {ECO:0000255|PROSITE-ProRule:PRU00285}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98273.1; -; Genomic_DNA. DR PIR; F64335; F64335. DR PDB; 1SHS; X-ray; 2.90 A; A/B/C/D/E/F/G/H=1-147. DR PDB; 4ELD; X-ray; 2.70 A; A/B=1-147. DR PDB; 4I88; X-ray; 2.85 A; A/B/C/D/E/F/G/H=1-147. DR PDBsum; 1SHS; -. DR PDBsum; 4ELD; -. DR PDBsum; 4I88; -. DR DisProt; DP00067; -. DR ProteinModelPortal; Q57733; -. DR SMR; Q57733; 33-147. DR DIP; DIP-48450N; -. DR STRING; 243232.MJ_0285; -. DR EnsemblBacteria; AAB98273; AAB98273; MJ_0285. DR KEGG; mja:MJ_0285; -. DR eggNOG; arCOG01832; Archaea. DR eggNOG; COG0071; LUCA. DR InParanoid; Q57733; -. DR KO; K13993; -. DR OMA; SGKGFMP; -. DR PhylomeDB; Q57733; -. DR EvolutionaryTrace; Q57733; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR Gene3D; 2.60.40.790; -; 1. DR InterPro; IPR002068; A-crystallin/Hsp20_dom. DR InterPro; IPR031107; HSP20. DR InterPro; IPR008978; HSP20-like_chaperone. DR PANTHER; PTHR11527; PTHR11527; 1. DR Pfam; PF00011; HSP20; 1. DR SUPFAM; SSF49764; SSF49764; 1. DR PROSITE; PS01031; HSP20; 1. PE 1: Evidence at protein level; KW 3D-structure; Chaperone; Complete proteome; Cytoplasm; KW Reference proteome; Stress response. FT CHAIN 1 147 Small heat shock protein HSP16.5. FT /FTId=PRO_0000126060. FT STRAND 36 41 {ECO:0000244|PDB:4ELD}. FT STRAND 45 49 {ECO:0000244|PDB:4ELD}. FT STRAND 51 59 {ECO:0000244|PDB:4ELD}. FT HELIX 65 67 {ECO:0000244|PDB:4ELD}. FT STRAND 68 73 {ECO:0000244|PDB:4ELD}. FT STRAND 76 82 {ECO:0000244|PDB:4ELD}. FT STRAND 93 97 {ECO:0000244|PDB:4ELD}. FT STRAND 104 110 {ECO:0000244|PDB:4ELD}. FT HELIX 117 119 {ECO:0000244|PDB:4ELD}. FT STRAND 121 125 {ECO:0000244|PDB:4ELD}. FT STRAND 128 135 {ECO:0000244|PDB:4ELD}. FT HELIX 137 139 {ECO:0000244|PDB:4ELD}. SQ SEQUENCE 147 AA; 16452 MW; 0A53C6981CFD4266 CRC64; MFGRDPFDSL FERMFKEFFA TPMTGTTMIQ SSTGIQISGK GFMPISIIEG DQHIKVIAWL PGVNKEDIIL NAVGDTLEIR AKRSPLMITE SERIIYSEIP EEEEIYRTIK LPATVKEENA SAKFENGVLS VILPKAESSI KKGINIE // ID HISX_METJA Reviewed; 429 AA. AC Q58851; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Histidinol dehydrogenase; DE Short=HDH; DE EC=1.1.1.23; GN Name=hisD; OrderedLocusNames=MJ1456; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the sequential NAD-dependent oxidations of L- CC histidinol to L-histidinaldehyde and then to L-histidine. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-histidinol + H(2)O + 2 NAD(+) = L-histidine CC + 2 NADH. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-histidine biosynthesis; L- CC histidine from 5-phospho-alpha-D-ribose 1-diphosphate: step 9/9. CC -!- SIMILARITY: Belongs to the histidinol dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99465.1; -; Genomic_DNA. DR PIR; G64481; G64481. DR ProteinModelPortal; Q58851; -. DR STRING; 243232.MJ_1456; -. DR EnsemblBacteria; AAB99465; AAB99465; MJ_1456. DR KEGG; mja:MJ_1456; -. DR eggNOG; arCOG04352; Archaea. DR eggNOG; COG0141; LUCA. DR InParanoid; Q58851; -. DR KO; K00013; -. DR OMA; TEIYRVG; -. DR PhylomeDB; Q58851; -. DR UniPathway; UPA00031; UER00014. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004399; F:histidinol dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01024; HisD; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR001692; Histidinol_DH_CS. DR InterPro; IPR022695; Histidinol_DH_monofunct. DR InterPro; IPR012131; Hstdl_DH. DR Pfam; PF00815; Histidinol_dh; 1. DR PIRSF; PIRSF000099; Histidinol_dh; 1. DR PRINTS; PR00083; HOLDHDRGNASE. DR SUPFAM; SSF53720; SSF53720; 1. DR TIGRFAMs; TIGR00069; hisD; 1. DR PROSITE; PS00611; HISOL_DEHYDROGENASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Histidine biosynthesis; KW Metal-binding; NAD; Oxidoreductase; Reference proteome; Zinc. FT CHAIN 1 429 Histidinol dehydrogenase. FT /FTId=PRO_0000135894. FT ACT_SITE 327 327 Proton acceptor. {ECO:0000250}. FT ACT_SITE 328 328 Proton acceptor. {ECO:0000250}. FT METAL 261 261 Zinc. {ECO:0000250}. FT METAL 264 264 Zinc. {ECO:0000250}. FT METAL 361 361 Zinc. {ECO:0000250}. FT METAL 420 420 Zinc. {ECO:0000250}. FT BINDING 131 131 NAD. {ECO:0000250}. FT BINDING 193 193 NAD. {ECO:0000250}. FT BINDING 216 216 NAD. {ECO:0000250}. FT BINDING 239 239 Substrate. {ECO:0000250}. FT BINDING 261 261 Substrate. {ECO:0000250}. FT BINDING 264 264 Substrate. {ECO:0000250}. FT BINDING 328 328 Substrate. {ECO:0000250}. FT BINDING 361 361 Substrate. {ECO:0000250}. FT BINDING 415 415 Substrate. {ECO:0000250}. FT BINDING 420 420 Substrate. {ECO:0000250}. SQ SEQUENCE 429 AA; 47433 MW; 5E4DF4B17699EDB8 CRC64; MVTGMIIKKI KELTKEEEEK IINRNKANFE EILPTVMEIL KDVKEKGDEA LKYYTKKFDG VEIEDFKVTD EEIEEAYNSV DYKVVEAIER AKENIYFFHK KQMEQIKDLN VENNGIILGQ VVRAIEKVGC YVPGGRAFYP STVLMTTIPA KVAGCEEIYI TSPPTKDGKG NPATLIAGDI VGVSAIYKVG GVQAIGALAY GTETIPKVDI IVGPGNIYVT TAKKMVYGEV AIDFLAGPSE VLIIADETAN AEFVALDFIA QAEHDPNASC VITTTSEKKA EEIKNKIFEE IEKAERKEII LKALENSAIL IGDLEECIEF SNKYAPEHLE ILTKNPEEVL NKIKHAGSVF LGEYSPVPVG DYASGTNHVL PTSQFARMSS GLNVETFLKK ITYQKLDKES LKNIADIVIT LAEAEGLFGH AEAVRRRLK // ID HMDX_METJA Reviewed; 338 AA. AC Q58125; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=H(2)-forming methylenetetrahydromethanopterin dehydrogenase-related protein MJ0715; GN OrderedLocusNames=MJ0715; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HMD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98710.1; -; Genomic_DNA. DR PIR; C64389; C64389. DR PDB; 4YTE; X-ray; 2.15 A; A=1-194. DR PDBsum; 4YTE; -. DR ProteinModelPortal; Q58125; -. DR STRING; 243232.MJ_0715; -. DR PRIDE; Q58125; -. DR EnsemblBacteria; AAB98710; AAB98710; MJ_0715. DR KEGG; mja:MJ_0715; -. DR eggNOG; arCOG03195; Archaea. DR eggNOG; COG4007; LUCA. DR OMA; INAPKDM; -. DR PhylomeDB; Q58125; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IEA:InterPro. DR GO; GO:0047068; F:N5,N10-methenyltetrahydromethanopterin hydrogenase activity; IEA:InterPro. DR GO; GO:0015948; P:methanogenesis; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR010063; HMD-rel. DR InterPro; IPR004889; HMD_C. DR InterPro; IPR024190; METHMP_Hmd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR Pfam; PF03201; HMD; 1. DR PIRSF; PIRSF016158; HMD; 1. DR PIRSF; PIRSF500166; HMDII_III; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01724; hmd_rel; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 338 H(2)-forming FT methylenetetrahydromethanopterin FT dehydrogenase-related protein MJ0715. FT /FTId=PRO_0000218517. SQ SEQUENCE 338 AA; 36854 MW; 339B264EA44B013B CRC64; MKISIYGAGN QRLYLEQLKV PEKFGGEPPY GGAGMAIEFA KAGHDVVLSE PNRDVMSDDL WKKVEDAGVK VVSDDIEAAK HGEIHVLFTP FGRITLNIAN TIIEHVPENA IICNTCTIPT PVLYRSLEGI LRLKRRDVGI SSMHPTGVPG TPSQKYYTIA GKALEGKEYA TEDQINKLVE LVKSVGKIPY VTPADVVPAV ADMGALVTAV ALVGVLDYYR VGTQIINAPK DMIEKQILIS LQTIASIIET SGMEGLMKVF NKDALLSSAK NMLIDERQED LNLALKIIEE FDKSTIGEKD ISQTYLVAPQ ALIKEAVSLI GKSAVEGMIR RSSNKLFK // ID HPRT_METJA Reviewed; 183 AA. AC Q59049; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Hypoxanthine/guanine phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01467}; DE Short=HGPRTase {ECO:0000255|HAMAP-Rule:MF_01467}; DE EC=2.4.2.8 {ECO:0000255|HAMAP-Rule:MF_01467}; GN Name=hpt {ECO:0000255|HAMAP-Rule:MF_01467}; OrderedLocusNames=MJ1655; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes a salvage reaction resulting in the formation CC of IMP that is energically less costly than de novo synthesis. CC {ECO:0000255|HAMAP-Rule:MF_01467}. CC -!- CATALYTIC ACTIVITY: IMP + diphosphate = hypoxanthine + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01467}. CC -!- CATALYTIC ACTIVITY: GMP + diphosphate = guanine + 5-phospho-alpha- CC D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_01467}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; CC IMP from hypoxanthine: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01467}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01467}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. Archaeal HPRT subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01467}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99676.1; -; Genomic_DNA. DR PIR; E64506; E64506. DR ProteinModelPortal; Q59049; -. DR STRING; 243232.MJ_1655; -. DR EnsemblBacteria; AAB99676; AAB99676; MJ_1655. DR KEGG; mja:MJ_1655; -. DR eggNOG; arCOG00030; Archaea. DR eggNOG; COG0503; LUCA. DR InParanoid; Q59049; -. DR KO; K00759; -. DR OMA; IATDIPY; -. DR PhylomeDB; Q59049; -. DR UniPathway; UPA00591; UER00648. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052657; F:guanine phosphoribosyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0004422; F:hypoxanthine phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0043103; P:hypoxanthine salvage; IEA:UniProtKB-HAMAP. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01467; Hypx_phosphoribosyltr; 1. DR InterPro; IPR026597; HGPRTase-like. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 183 Hypoxanthine/guanine FT phosphoribosyltransferase. FT /FTId=PRO_0000149496. SQ SEQUENCE 183 AA; 20218 MW; A20172DC74A941FB CRC64; MLLEETLKSC PIVKRGEYHY FIHPISDGVP VVEPKLLREV ATRIIKIGDF EGATKLVTAE AMGIPLVTTL SLYTDIPYVI MRKREYKLPG EIPVFQSTGY SKGQLYLNGI EKGDKVVIID DVISTGGTMI AIIDALKRAG AEIKDIICVI ERGEGKKIVE EKTGYKIKTL VKIDVVDGKV VIL // ID HYPA_METJA Reviewed; 124 AA. AC Q57667; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Probable hydrogenase nickel incorporation protein HypA; GN Name=hypA; OrderedLocusNames=MJ0214; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably plays a role in a hydrogenase nickel cofactor CC insertion step. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HypA/HybF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98198.1; -; Genomic_DNA. DR PIR; G64326; G64326. DR ProteinModelPortal; Q57667; -. DR STRING; 243232.MJ_0214; -. DR EnsemblBacteria; AAB98198; AAB98198; MJ_0214. DR KEGG; mja:MJ_0214; -. DR eggNOG; arCOG04426; Archaea. DR eggNOG; COG0375; LUCA. DR InParanoid; Q57667; -. DR KO; K04651; -. DR OMA; QLKFAFE; -. DR PhylomeDB; Q57667; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006464; P:cellular protein modification process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00213; HypA; 1. DR InterPro; IPR000688; Hydgase_Ni_incorp_HypA/HybF. DR InterPro; IPR020538; Hydgase_Ni_incorp_HypA/HybF_CS. DR Pfam; PF01155; HypA; 1. DR PIRSF; PIRSF004761; Hydrgn_mat_HypA; 1. DR TIGRFAMs; TIGR00100; hypA; 1. DR PROSITE; PS01249; HYPA; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Nickel; Reference proteome. FT CHAIN 1 124 Probable hydrogenase nickel incorporation FT protein HypA. FT /FTId=PRO_0000129077. FT METAL 2 2 Nickel. {ECO:0000255}. FT METAL 78 78 Nickel. {ECO:0000255}. FT METAL 81 81 Nickel. {ECO:0000255}. FT METAL 97 97 Nickel. {ECO:0000255}. FT METAL 100 100 Nickel. {ECO:0000255}. SQ SEQUENCE 124 AA; 14058 MW; 1769B05D496957AD CRC64; MHELSYANAM LEAILNSIKK EEEKGKKIKK VTEINLEVGE LTFINVEQLK FAFEVIAEGT VCEGAKINVE FIKPKCKCLD CGYEGEPEIL DEFEVYCPKC KSIRLKLSGG KEFNIKNATV EYED // ID IDI2_METJA Reviewed; 359 AA. AC Q58272; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Isopentenyl-diphosphate delta-isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE Short=IPP isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE EC=5.3.3.2 {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Isopentenyl diphosphate:dimethylallyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Isopentenyl pyrophosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE AltName: Full=Type 2 isopentenyl diphosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00354}; DE Short=IDI-2 {ECO:0000255|HAMAP-Rule:MF_00354}; GN Name=fni {ECO:0000255|HAMAP-Rule:MF_00354}; OrderedLocusNames=MJ0862; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME RP REGULATION, AND COFACTOR. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=16793276; DOI=10.1016/j.bmc.2006.06.011; RA Hoshino T., Tamegai H., Kakinuma K., Eguchi T.; RT "Inhibition of type 2 isopentenyl diphosphate isomerase from RT Methanocaldococcus jannaschii by a mechanism-based inhibitor of type 1 RT isopentenyl diphosphate isomerase."; RL Bioorg. Med. Chem. 14:6555-6559(2006). RN [3] RP CRYSTALLIZATION. RX PubMed=21206036; DOI=10.1107/S1744309110046944; RA Hoshino T., Nango E., Baba S., Eguchi T., Kumasaka T.; RT "Crystallization and preliminary X-ray analysis of isopentenyl RT diphosphate isomerase from Methanocaldococcus jannaschii."; RL Acta Crystallogr. F 67:101-103(2011). CC -!- FUNCTION: Involved in the biosynthesis of isoprenoids. Catalyzes CC the 1,3-allylic rearrangement of the homoallylic substrate CC isopentenyl (IPP) to its allylic isomer, dimethylallyl diphosphate CC (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00354, CC ECO:0000269|PubMed:16793276}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate = dimethylallyl CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_00354, CC ECO:0000269|PubMed:16793276}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354, CC ECO:0000269|PubMed:16793276}; CC -!- COFACTOR: CC Name=NADPH; Xref=ChEBI:CHEBI:57783; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354, CC ECO:0000269|PubMed:16793276}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00354}; CC -!- ENZYME REGULATION: Inhibited by 3,4-epoxy-3-methylbutyl CC diphosphate (EIPP). {ECO:0000269|PubMed:16793276}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15.3 mM for IPP {ECO:0000269|PubMed:16793276}; CC Note=Kcat is 191 sec (-1) for isomerase activity with IPP.; CC pH dependence: CC Optimum pH is between 7 and 7.2. {ECO:0000269|PubMed:16793276}; CC Temperature dependence: CC Optimum temperature is between 85 and 95 degrees Celsius. CC {ECO:0000269|PubMed:16793276}; CC -!- SUBUNIT: Homooctamer. Dimer of tetramers. {ECO:0000255|HAMAP- CC Rule:MF_00354}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00354}. CC -!- SIMILARITY: Belongs to the IPP isomerase type 2 family. CC {ECO:0000255|HAMAP-Rule:MF_00354}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98867.1; -; Genomic_DNA. DR PIR; F64407; F64407. DR ProteinModelPortal; Q58272; -. DR STRING; 243232.MJ_0862; -. DR EnsemblBacteria; AAB98867; AAB98867; MJ_0862. DR KEGG; mja:MJ_0862; -. DR eggNOG; arCOG00613; Archaea. DR eggNOG; COG1304; LUCA. DR InParanoid; Q58272; -. DR KO; K01823; -. DR OMA; GSQRVML; -. DR PhylomeDB; Q58272; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0010181; F:FMN binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004452; F:isopentenyl-diphosphate delta-isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070402; F:NADPH binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00354; Idi_2; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000262; FMN-dep_DH. DR InterPro; IPR011179; IPdP_isomerase. DR PANTHER; PTHR10578:SF3; PTHR10578:SF3; 2. DR Pfam; PF01070; FMN_dh; 1. DR PIRSF; PIRSF003314; IPP_isomerase; 1. DR TIGRFAMs; TIGR02151; IPP_isom_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Flavoprotein; FMN; Isomerase; KW Isoprene biosynthesis; Magnesium; Metal-binding; NADP; KW Reference proteome. FT CHAIN 1 359 Isopentenyl-diphosphate delta-isomerase. FT /FTId=PRO_0000134444. FT NP_BIND 69 71 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT NP_BIND 278 280 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT NP_BIND 299 300 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT REGION 11 12 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00354}. FT REGION 99 101 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00354}. FT METAL 164 164 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00354}. FT BINDING 68 68 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT BINDING 99 99 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00354}. FT BINDING 127 127 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT BINDING 163 163 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00354}. FT BINDING 199 199 FMN. {ECO:0000255|HAMAP-Rule:MF_00354}. FT BINDING 229 229 FMN; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00354}. SQ SEQUENCE 359 AA; 39875 MW; 46BDD320262772EA CRC64; MVNNRNEIEV RKLEHIFLCS YCNVEYEKTT LLEDIELIHK GTCGINFNDI ETEIELFGKK LSAPIIVSGM TGGHSKAKEI NKNIAKAVEE LGLGMGVGSQ RAAIVNDELI DTYSIVRDYT NNLVIGNLGA VNFIVDDWDE EIIDKAIEMI DADAIAIHFN PLQEIIQPEG DLNFKNLYKL KEIISNYKKS YKNIPFIAKQ VGEGFSKEDA LILKDIGFDA IDVQGSGGTS WAKVEIYRVK EEEIKRLAEK FANWGIPTAA SIFEVKSVYD GIVIGSGGIR GGLDIAKCIA IGCDCCSVAL PILKASLKGW EEVVKVLESY IKELKIAMFL VGAENIEELK KTSYIVKGTL KEWISQRLK // ID HTPX_METJA Reviewed; 284 AA. AC Q59076; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 109. DE RecName: Full=Protease HtpX homolog {ECO:0000255|HAMAP-Rule:MF_00188}; DE EC=3.4.24.- {ECO:0000255|HAMAP-Rule:MF_00188}; GN Name=htpX {ECO:0000255|HAMAP-Rule:MF_00188}; OrderedLocusNames=MJ1682; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00188}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00188}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_00188}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_00188}. CC -!- SIMILARITY: Belongs to the peptidase M48B family. CC {ECO:0000255|HAMAP-Rule:MF_00188}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99703.1; -; Genomic_DNA. DR PIR; H64509; H64509. DR ProteinModelPortal; Q59076; -. DR STRING; 243232.MJ_1682; -. DR MEROPS; M48.004; -. DR EnsemblBacteria; AAB99703; AAB99703; MJ_1682. DR KEGG; mja:MJ_1682; -. DR eggNOG; arCOG01331; Archaea. DR eggNOG; COG0501; LUCA. DR InParanoid; Q59076; -. DR KO; K03799; -. DR OMA; EEAPWLH; -. DR PhylomeDB; Q59076; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00188; Pept_M48_protease_HtpX; 1. DR InterPro; IPR022919; Pept_M48_protease_HtpX. DR InterPro; IPR001915; Peptidase_M48. DR Pfam; PF01435; Peptidase_M48; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1 284 Protease HtpX homolog. FT /FTId=PRO_0000138917. FT TRANSMEM 7 26 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 33 47 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 148 168 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT TRANSMEM 180 200 Helical. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT ACT_SITE 130 130 {ECO:0000255|HAMAP-Rule:MF_00188}. FT METAL 129 129 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 133 133 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. FT METAL 205 205 Zinc; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_00188}. SQ SEQUENCE 284 AA; 31972 MW; 86B51795599F560A CRC64; MINQIKTYLL MALLVGLIYA ICMMLHIHPL IAIILALIPN VIAYYMSDKL VLMSYNARIL EEHEMPWLHQ MVERVARKAG LPKPKVAIVP TETPNAFATG RNPENAVVAV TEGILKLLSP EELEGVIGHE ISHIKHRDIL ISTIVATLAG AIVMIAEWML YWGGIFFVSE EEESNPLELI GTILLLILAP IAATIIQFAI SRQREFYADE EGAKLTHPLW LANALAKLER GVELYPLERG NPATAHMFII NPFRKDFIAK LFSTHPPTEE RIERLLEMCK RIGK // ID HYPB_METJA Reviewed; 221 AA. AC Q57884; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Probable hydrogenase nickel incorporation protein HypB; GN Name=hypB; OrderedLocusNames=MJ0442; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Could be involved in nickel binding and accumulation. CC -!- SIMILARITY: Belongs to the SIMIBI class G3E GTPase family. CC HypB/HupM subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98429.1; -; Genomic_DNA. DR PIR; B64355; B64355. DR PDB; 2HF8; X-ray; 2.10 A; A/B=1-221. DR PDB; 2HF9; X-ray; 1.90 A; A/B=1-221. DR PDBsum; 2HF8; -. DR PDBsum; 2HF9; -. DR ProteinModelPortal; Q57884; -. DR SMR; Q57884; 11-221. DR STRING; 243232.MJ_0442; -. DR EnsemblBacteria; AAB98429; AAB98429; MJ_0442. DR KEGG; mja:MJ_0442; -. DR eggNOG; arCOG01231; Archaea. DR eggNOG; COG0378; LUCA. DR InParanoid; Q57884; -. DR KO; K04652; -. DR OMA; GRSCHLD; -. DR PhylomeDB; Q57884; -. DR EvolutionaryTrace; Q57884; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0016151; F:nickel cation binding; IBA:GO_Central. DR GO; GO:0006461; P:protein complex assembly; IEA:InterPro. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR004392; Hyd_acc_HypB. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02492; cobW; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00073; hypB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Nickel; KW Reference proteome. FT CHAIN 1 221 Probable hydrogenase nickel incorporation FT protein HypB. FT /FTId=PRO_0000201445. FT HELIX 13 30 {ECO:0000244|PDB:2HF9}. FT STRAND 34 41 {ECO:0000244|PDB:2HF9}. FT HELIX 46 57 {ECO:0000244|PDB:2HF9}. FT TURN 58 60 {ECO:0000244|PDB:2HF9}. FT STRAND 63 69 {ECO:0000244|PDB:2HF9}. FT TURN 70 72 {ECO:0000244|PDB:2HF9}. FT HELIX 73 80 {ECO:0000244|PDB:2HF9}. FT TURN 81 83 {ECO:0000244|PDB:2HF9}. FT STRAND 85 90 {ECO:0000244|PDB:2HF9}. FT HELIX 99 106 {ECO:0000244|PDB:2HF9}. FT HELIX 111 113 {ECO:0000244|PDB:2HF9}. FT STRAND 115 120 {ECO:0000244|PDB:2HF9}. FT HELIX 127 130 {ECO:0000244|PDB:2HF9}. FT STRAND 136 143 {ECO:0000244|PDB:2HF9}. FT HELIX 144 146 {ECO:0000244|PDB:2HF9}. FT TURN 148 153 {ECO:0000244|PDB:2HF9}. FT HELIX 155 158 {ECO:0000244|PDB:2HF9}. FT STRAND 162 167 {ECO:0000244|PDB:2HF9}. FT HELIX 169 171 {ECO:0000244|PDB:2HF9}. FT HELIX 172 175 {ECO:0000244|PDB:2HF9}. FT HELIX 179 189 {ECO:0000244|PDB:2HF9}. FT STRAND 193 197 {ECO:0000244|PDB:2HF9}. FT TURN 200 202 {ECO:0000244|PDB:2HF9}. FT HELIX 206 219 {ECO:0000244|PDB:2HF9}. SQ SEQUENCE 221 AA; 24340 MW; 0BB5415386A81138 CRC64; MHLVGVLDIA KDILKANKRL ADKNRKLLNK HGVVAFDFMG AIGSGKTLLI EKLIDNLKDK YKIACIAGDV IAKFDAERME KHGAKVVPLN TGKECHLDAH LVGHALEDLN LDEIDLLFIE NVGNLICPAD FDLGTHKRIV VISTTEGDDT IEKHPGIMKT ADLIVINKID LADAVGADIK KMENDAKRIN PDAEVVLLSL KTMEGFDKVL EFIEKSVKEV K // ID HYPF_METJA Reviewed; 766 AA. AC Q58123; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=Probable carbamoyltransferase HypF; DE EC=2.1.3.-; DE AltName: Full=Carbamoyl phosphate-converting enzyme HypF; DE AltName: Full=[NiFe]-hydrogenase maturation factor HypF; DE Short=Hydrogenase maturation protein HypF; GN Name=hypF; OrderedLocusNames=MJ0713; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Along with HypE, it catalyzes the synthesis of the CN CC ligands of the active site iron of [NiFe]-hydrogenases using CC carbamoylphosphate as a substrate. It functions as a carbamoyl CC transferase using carbamoylphosphate as a substrate and CC transferring the carboxamido moiety in an ATP-dependent reaction CC to the thiolate of the C-terminal cysteine of HypE yielding a CC protein-S-carboxamide (By similarity). {ECO:0000250}. CC -!- PATHWAY: Protein modification; [NiFe] hydrogenase maturation. CC -!- SIMILARITY: Belongs to the carbamoyltransferase HypF family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98708.1; -; Genomic_DNA. DR PIR; A64389; A64389. DR ProteinModelPortal; Q58123; -. DR STRING; 243232.MJ_0713; -. DR EnsemblBacteria; AAB98708; AAB98708; MJ_0713. DR KEGG; mja:MJ_0713; -. DR eggNOG; arCOG01187; Archaea. DR eggNOG; COG0068; LUCA. DR InParanoid; Q58123; -. DR KO; K04656; -. DR OMA; YVMTSAN; -. DR PhylomeDB; Q58123; -. DR UniPathway; UPA00335; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0046944; P:protein carbamoylation; IEA:InterPro. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR InterPro; IPR017968; Acylphosphatase_CS. DR InterPro; IPR004421; Carbamoyltransferase_HypF. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR006070; YrdC-like_dom. DR InterPro; IPR011125; Znf_HypF. DR Pfam; PF00708; Acylphosphatase; 1. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR Pfam; PF07503; zf-HYPF; 2. DR PIRSF; PIRSF006256; CMPcnvr_hdrg_mat; 1. DR SUPFAM; SSF54975; SSF54975; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00143; hypF; 1. DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Transferase; KW Zinc; Zinc-finger. FT CHAIN 1 766 Probable carbamoyltransferase HypF. FT /FTId=PRO_0000071619. FT DOMAIN 11 98 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. FT DOMAIN 209 393 YrdC-like. {ECO:0000255|PROSITE- FT ProRule:PRU00518}. FT ZN_FING 117 142 C4-type. {ECO:0000255}. FT ZN_FING 167 192 C4-type. {ECO:0000255}. SQ SEQUENCE 766 AA; 87605 MW; 1B81EAB8D16CBFAD CRC64; MEILFFGVKM KVRIKVKGIV QGVGFRPFVY RIAKKNNLKG YVKNMGNYVE ILIEGKKEDI RNFINDLKNK KPPLSRIDKL DIEEIKGIEE FDDFYIIKSE NAKDEEEGTI PADVAICDDC LKEMLDKNDR RYRYPFIACT NCGPRFTIVE KLPYDRENTS MRDFPLCEKC LEEYKNPLDR RFHAQATCCP ICGPKVFLSD GKEIIAEKDE AIRETVKLLE EGHILAIKGI GGTHLACKVG EDDVVLELRK RLGRPTQPFA VMSKIEYTEL FAEFDEDEKN ALLSLRRPIV VLKKSQDYDK YFSKYVSNLD TIGVMFPYSG LHYLLFDKEI AYVMTSANLP GLPMVKDNDE ILKKLNGIAD YFLLHNRRIV NRCDDSVVKK VADRLVFLRR SRGFAPEPVK VNINNNKNIL CVGAELNSTA CIVKRDKFYL TQYIGNTSKY ETFCYLRDAI NNILRLTNTN KIDAIVCDLH PQFNSTKLAE ELSEKFGAEI FRVQHHFAHA YSLLGDNNYF DDAIILSLDG VGYGLDGNIW GGEVLLFKDG KMERVGHLEE QYQLGGDLAT KYPLRMLLSI LYKAIGEEAF DFIKRYNFFS EKELRLLKFQ LEKKLNCPIT TSTGRVLDAV SALLGICFEK TYDGEPSIRL EPVANRFKGD INIEPKIKNN ILNTTELIYK SYEMLLNNEN KEKIAHFAHI YIADGLFEIA KKISNKFGIN TIGITGGVSY NKIITERIMN NAKREGFNFI YHQRVPNGDG GISFGQGVAY ILKNGY // ID IF2B_METJA Reviewed; 143 AA. AC Q57562; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 106. DE RecName: Full=Translation initiation factor 2 subunit beta; DE AltName: Full=aIF2-beta; DE AltName: Full=eIF-2-beta; GN Name=eif2b; OrderedLocusNames=MJ0097; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis CC by forming a ternary complex with GTP and initiator tRNA. CC {ECO:0000250}. CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma CC chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eIF-2-beta/eIF-5 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98077.1; -; Genomic_DNA. DR PIR; A64312; A64312. DR PDB; 1K81; NMR; -; A=108-143. DR PDB; 1K8B; NMR; -; A=39-90. DR PDBsum; 1K81; -. DR PDBsum; 1K8B; -. DR ProteinModelPortal; Q57562; -. DR SMR; Q57562; 7-143. DR STRING; 243232.MJ_0097; -. DR EnsemblBacteria; AAB98077; AAB98077; MJ_0097. DR KEGG; mja:MJ_0097; -. DR eggNOG; arCOG01640; Archaea. DR eggNOG; COG1601; LUCA. DR InParanoid; Q57562; -. DR KO; K03238; -. DR OMA; PDHLMKY; -. DR PhylomeDB; Q57562; -. DR EvolutionaryTrace; Q57562; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.30.50; -; 1. DR HAMAP; MF_00232; eIF_2_beta; 1. DR InterPro; IPR004458; TIF2_bsu_arc. DR InterPro; IPR002735; Transl_init_fac_IF2/IF5. DR InterPro; IPR016189; Transl_init_fac_IF2/IF5_N. DR InterPro; IPR016190; Transl_init_fac_IF2/IF5_Zn-bd. DR Pfam; PF01873; eIF-5_eIF-2B; 1. DR SMART; SM00653; eIF2B_5; 1. DR SUPFAM; SSF100966; SSF100966; 1. DR SUPFAM; SSF75689; SSF75689; 1. DR TIGRFAMs; TIGR00311; aIF-2beta; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Initiation factor; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 143 Translation initiation factor 2 subunit FT beta. FT /FTId=PRO_0000137421. FT STRAND 40 43 {ECO:0000244|PDB:1K8B}. FT STRAND 46 49 {ECO:0000244|PDB:1K8B}. FT HELIX 52 60 {ECO:0000244|PDB:1K8B}. FT HELIX 63 74 {ECO:0000244|PDB:1K8B}. FT STRAND 75 81 {ECO:0000244|PDB:1K8B}. FT STRAND 84 88 {ECO:0000244|PDB:1K8B}. FT STRAND 111 113 {ECO:0000244|PDB:1K81}. FT STRAND 117 123 {ECO:0000244|PDB:1K81}. FT STRAND 126 132 {ECO:0000244|PDB:1K81}. FT TURN 133 135 {ECO:0000244|PDB:1K81}. FT STRAND 136 140 {ECO:0000244|PDB:1K81}. SQ SEQUENCE 143 AA; 16797 MW; 1762C47A953FEB25 CRC64; MSDLENIDYY DYKALLKRAR SQIPDYVFQK DRFELPEIEI LIEGNRTIIR NFRELAKAVN RDEEFFAKYL LKETGSAGNL EGGRLILQRR ISPELLKSRI NDFLREYVIC RECGKPDTKI IKEGRVHLLK CMACGAIRPI RMI // ID IF2P_METJA Reviewed; 1155 AA. AC Q57710; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 118. DE RecName: Full=Probable translation initiation factor IF-2; DE Contains: DE RecName: Full=Mja infB intein; DE AltName: Full=Mja IF2 intein; GN Name=infB; OrderedLocusNames=MJ0262; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Function in general translation initiation by promoting CC the binding of the formylmethionine-tRNA to ribosomes. Seems to CC function along with eIF-2 (By similarity). {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- MISCELLANEOUS: The intein interrupts the GTP-binding site. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. IF-2 CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98248.1; -; Genomic_DNA. DR PIR; G64332; G64332. DR ProteinModelPortal; Q57710; -. DR STRING; 243232.MJ_0262; -. DR EnsemblBacteria; AAB98248; AAB98248; MJ_0262. DR KEGG; mja:MJ_0262; -. DR eggNOG; arCOG01560; Archaea. DR eggNOG; arCOG03157; Archaea. DR eggNOG; COG0532; LUCA. DR eggNOG; COG1372; LUCA. DR InParanoid; Q57710; -. DR KO; K03243; -. DR OMA; DHGKCLL; -. DR PhylomeDB; Q57710; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. DR Gene3D; 3.40.50.10050; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00100_A; IF_2_A; 1. DR InterPro; IPR029459; EFTU-type. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR004544; TIF_aIF-2_arc. DR InterPro; IPR023115; TIF_IF2_dom3. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR Pfam; PF14578; GTP_EFTU_D4; 1. DR Pfam; PF11987; IF-2; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF51294; SSF51294; 3. DR SUPFAM; SSF52156; SSF52156; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR00491; aIF-2; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; GTP-binding; KW Initiation factor; Nucleotide-binding; Protein biosynthesis; KW Protein splicing; Reference proteome. FT CHAIN 1 30 Probable translation initiation factor FT IF-2, 1st part. {ECO:0000255}. FT /FTId=PRO_0000014484. FT CHAIN 31 576 Mja infB intein. {ECO:0000255}. FT /FTId=PRO_0000014485. FT CHAIN 577 1155 Probable translation initiation factor FT IF-2, 2nd part. {ECO:0000255}. FT /FTId=PRO_0000014486. FT DOMAIN 237 367 DOD-type homing endonuclease. FT DOMAIN 561 781 tr-type G. FT NP_BIND 634 638 GTP. {ECO:0000250}. FT NP_BIND 688 691 GTP. {ECO:0000250}. SQ SEQUENCE 1155 AA; 132299 MW; 6653FA355E7EE0D3 CRC64; MAKKNTKKDN KNQNLRCPIV CVLGHVDHGK CLMPHEKVLT EYGEIKIEDL FKIGKEIVEK DELKEIRKLN IKVHTLNENG EIKIINAPYV WKLKHKGKMI KVKLKNWHSI TTTPEHPFLT NNGWIKAENI KKGMYVAIPR KIYGNEDFEK FIEFINSKIL TNELIVKVNE KDLKNVELPS TKIYKKQKNV FRSEDIIEHN LNIEKISFSP RIHRCGKPQH YIKLPKSLNE WKAIFYFAGV MFGDGCVDRI ANNDEEVFNK LKSLNNLGIE VERIKRKSSY EIIFKNGKNA LINLLKILFD YPSEKKSHNI KIPQILYIAP KELVAEFIKG YFDADGYVNL RQNRIEVISA SKEFIEGLSI LLLRFEITSK IYEIKKSYKE TKKKYYQLNI VGKRNLKNFK NIGFSIKYKE ENLNKIIEKS RKSEKYPINK DMKRLRILFG MTRNEVNVSY YAKYENGKEI PSYEIVKKFL NSLKPKNLDK KIKVLEGKER DVNYLKAFES DGLIENGRLT KLGREALNIW KNHEFGKENI DYMKSLIENI AFVEVEDVEI IDYDGYVYDL TTETHNFIAN GIVVHNTTLL DKIRKTRVAK REAGGITQHI GASEIPIDVI KRLCGDLLKM LKADLKIPGL LVIDTPGHEA FTSLRKRGGA LADIAILVVD INEGFKPQTV EAVNILRQCK TPFVVAANKI DLIPGWNSKE GPFILNFNEK NQHPNALTEF EIRLYENIIK PLNELGFDAD LYSRVQDVTK TVCIIPVSAV TGEGIPDLLM MVAGLAQKFL EDRLKLNVEG YAKGTILEVK EEKGLGTTID AIIYDGIAKR GDYLVVGLPD DVLVTRVKAL LKPKPLDEMR DPRDKFKPVN EVTAAAGVKI AAPELDKVIA GCPIRIVPKD KIEEAKEEVM KEVEEAKIEV DDEGILIKAD TLGSLEALAN ELRKAGVKIK KAEVGDVTKK DVIEVASYKQ SNPLHGAIVA FNVKILPEAQ KEIEKYDIKV FLDNIIYKLV EDFTEWIKKE EERIKYGEFE KLIKPAIIRI LPDCIFRQKD PAICGVEVLC GTLRVGAPLM REDGMQLGYV REIKDRGENV KEAKAGKAVS IAIDGRVVLK RHVDEGDYMY VAVPESHVRE LYHKYMDRLR NDEKEALLRY MELMQKLTNN IFWGR // ID ILVC_METJA Reviewed; 330 AA. AC Q58938; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 17-OCT-2006, sequence version 3. DT 11-NOV-2015, entry version 106. DE RecName: Full=Ketol-acid reductoisomerase; DE EC=1.1.1.86; DE AltName: Full=Acetohydroxy-acid isomeroreductase; DE AltName: Full=Alpha-keto-beta-hydroxylacyl reductoisomerase; GN Name=ilvC; OrderedLocusNames=MJ1543; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: (2R)-2,3-dihydroxy-3-methylbutanoate + NADP(+) CC = (2S)-2-hydroxy-2-methyl-3-oxobutanoate + NADPH. CC -!- CATALYTIC ACTIVITY: (2R,3R)-2,3-dihydroxy-3-methylpentanoate + CC NADP(+) = (S)-2-hydroxy-2-ethyl-3-oxobutanoate + NADPH. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 2/4. CC -!- SIMILARITY: Belongs to the ketol-acid reductoisomerase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99561.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99561.1; ALT_INIT; Genomic_DNA. DR PIR; F64492; F64492. DR ProteinModelPortal; Q58938; -. DR SMR; Q58938; 2-325. DR STRING; 243232.MJ_1543; -. DR EnsemblBacteria; AAB99561; AAB99561; MJ_1543. DR KEGG; mja:MJ_1543; -. DR eggNOG; arCOG04465; Archaea. DR eggNOG; COG0059; LUCA. DR InParanoid; Q58938; -. DR KO; K00053; -. DR OMA; FETCHEL; -. DR PhylomeDB; Q58938; -. DR UniPathway; UPA00047; UER00056. DR UniPathway; UPA00049; UER00060. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004455; F:ketol-acid reductoisomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1040.10; -; 1. DR HAMAP; MF_00435; IlvC; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR013328; 6PGD_dom_2. DR InterPro; IPR000506; AcH_isomrdctse_C. DR InterPro; IPR013116; IlvN. DR InterPro; IPR013023; Ketol-acid_reductoisomrdctse. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR21371; PTHR21371; 1. DR Pfam; PF01450; IlvC; 1. DR Pfam; PF07991; IlvN; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00465; ilvC; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 330 Ketol-acid reductoisomerase. FT /FTId=PRO_0000151391. FT ACT_SITE 108 108 {ECO:0000255}. SQ SEQUENCE 330 AA; 36827 MW; B3B3B0A3BC0E027B CRC64; MVKIFYDKDV TFDAVKDKTI AVIGYGSQGR AQALNMKDSG LNVIVGLRPN GASWNKAIKD GHKVMTIEEA AEKADIIHIL IPDEVQPAVY KKQIEPYLTE GKTISFSHGY NIHYGFIRPP ENVNITMVAP KSPGAMVRKT YEEGFGVPGL VAVERDYTGD ALQIALGMAK GIGLTKVGVI QTTFREETET DLFGEQVVLC GGVTELIKAA FETLVEAGYA PEMAYFETCH ELKLIVDLIY QKGLQGMWEN VSNTAEYGGL TRRARVINEE SRKAMKEILK EIQDGRFAKE WSLEREAGFP HLNALRRLEK EHLIEKVGKE LRKMCGLEKE // ID IDSA_METJA Reviewed; 327 AA. AC Q58270; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Short chain isoprenyl diphosphate synthase; DE EC=2.5.1.-; GN Name=idsA; OrderedLocusNames=MJ0860; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 3 Mg(2+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98865.1; -; Genomic_DNA. DR PIR; D64407; D64407. DR ProteinModelPortal; Q58270; -. DR STRING; 243232.MJ_0860; -. DR EnsemblBacteria; AAB98865; AAB98865; MJ_0860. DR KEGG; mja:MJ_0860; -. DR eggNOG; arCOG01726; Archaea. DR eggNOG; COG0142; LUCA. DR InParanoid; Q58270; -. DR KO; K13787; -. DR OMA; ILSKACV; -. DR PhylomeDB; Q58270; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.600.10; -; 1. DR InterPro; IPR008949; Isoprenoid_synthase_dom. DR InterPro; IPR000092; Polyprenyl_synt. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF00348; polyprenyl_synt; 1. DR SUPFAM; SSF48576; SSF48576; 1. DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1. DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Magnesium; Metal-binding; KW Reference proteome; Transferase. FT CHAIN 1 327 Short chain isoprenyl diphosphate FT synthase. FT /FTId=PRO_0000123970. FT METAL 87 87 Magnesium 1. {ECO:0000250}. FT METAL 87 87 Magnesium 2. {ECO:0000250}. FT METAL 91 91 Magnesium 1. {ECO:0000250}. FT METAL 91 91 Magnesium 2. {ECO:0000250}. FT METAL 217 217 Magnesium 3. {ECO:0000250}. FT BINDING 48 48 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 51 51 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 80 80 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 96 96 Allylic substrate. {ECO:0000250}. FT BINDING 97 97 Isopentenyl diphosphate. {ECO:0000250}. FT BINDING 176 176 Allylic substrate. {ECO:0000250}. FT BINDING 177 177 Allylic substrate. {ECO:0000250}. FT BINDING 214 214 Allylic substrate. {ECO:0000250}. FT BINDING 231 231 Allylic substrate. {ECO:0000250}. FT BINDING 241 241 Allylic substrate. {ECO:0000250}. SQ SEQUENCE 327 AA; 37569 MW; 07D68AC9BD657DAC CRC64; MKELFKRGGI MLFDKNILQK IDEELKTYVD KDDKLYNASK HLLFAGGKRI RPYLTVVTYM LKKDDIEEVL PAAAAVELIH NYTLIHDDIM DNDDERRGKP TVHVVYGEPM AILAGDLLYA KAFEAVSRIK DNKKAHEVLK ILSKACVEVC EGQAMDMEFE NYYPTMEEYL DMIRKKTGAL LEASVGIGAV MADCNEEERE ALKEYAKRIG LTFQIQDDVL DLIGDQKKLG KPVGSDIREG KKTIIVIHAL KTLDEDKKKR LLEILGNKNV KDEEIKEAIE ILKPSIEYAK ELMKQKTEEA KEYLKIFNKD RRKVLEDLAD FIMSRIY // ID IF1A_METJA Reviewed; 102 AA. AC Q57887; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Translation initiation factor 1A; DE Short=aIF-1A; GN Name=eIF1A; OrderedLocusNames=MJ0445; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP STRUCTURE BY NMR. RX PubMed=11714910; DOI=10.1110/ps.18201; RA Li W., Hoffman D.W.; RT "Structure and dynamics of translation initiation factor aIF-1A from RT the archaeon Methanococcus jannaschii determined by NMR RT spectroscopy."; RL Protein Sci. 10:2426-2438(2001). CC -!- FUNCTION: Seems to be required for maximal rate of protein CC biosynthesis. Enhances ribosome dissociation into subunits and CC stabilizes the binding of the initiator Met-tRNA(I) to 40 S CC ribosomal subunits (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eIF-1A family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S1-like domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98435.1; -; Genomic_DNA. DR PIR; E64355; E64355. DR PDB; 1JT8; NMR; -; A=1-102. DR PDBsum; 1JT8; -. DR ProteinModelPortal; Q57887; -. DR SMR; Q57887; 1-102. DR STRING; 243232.MJ_0445; -. DR EnsemblBacteria; AAB98435; AAB98435; MJ_0445. DR KEGG; mja:MJ_0445; -. DR eggNOG; arCOG01179; Archaea. DR eggNOG; COG0361; LUCA. DR InParanoid; Q57887; -. DR KO; K03236; -. DR OMA; WVREGDI; -. DR PhylomeDB; Q57887; -. DR EvolutionaryTrace; Q57887; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00216; aIF_1A; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR006196; RNA-binding_domain_S1_IF1. DR InterPro; IPR001253; TIF_eIF-1A. DR InterPro; IPR018104; TIF_eIF-1A_CS. DR PANTHER; PTHR21668; PTHR21668; 1. DR Pfam; PF01176; eIF-1a; 1. DR ProDom; PD005579; TIF_eIF-1A; 1. DR SMART; SM00652; eIF1a; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00523; eIF-1A; 1. DR PROSITE; PS01262; IF1A; 1. DR PROSITE; PS50832; S1_IF1_TYPE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Initiation factor; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 102 Translation initiation factor 1A. FT /FTId=PRO_0000145121. FT DOMAIN 10 85 S1-like. FT STRAND 22 27 {ECO:0000244|PDB:1JT8}. FT STRAND 32 40 {ECO:0000244|PDB:1JT8}. FT STRAND 43 48 {ECO:0000244|PDB:1JT8}. FT HELIX 51 57 {ECO:0000244|PDB:1JT8}. FT STRAND 63 67 {ECO:0000244|PDB:1JT8}. FT STRAND 75 85 {ECO:0000244|PDB:1JT8}. FT HELIX 88 100 {ECO:0000244|PDB:1JT8}. SQ SEQUENCE 102 AA; 12184 MW; 8082FD686A103FC0 CRC64; MAEQQQEQQI RVRIPRKEEN EILGIIEQML GASRVRVRCL DGKTRLGRIP GRLKNRIWVR EGDVVIVKPW EVQGDQKCDI IWRYTKTQVE WLKRKGYLDE LL // ID IF2G_METJA Reviewed; 411 AA. AC Q58657; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 21-JUN-2005, sequence version 2. DT 17-FEB-2016, entry version 114. DE RecName: Full=Translation initiation factor 2 subunit gamma; DE AltName: Full=aIF2-gamma; DE AltName: Full=eIF-2-gamma; GN Name=eif2g; OrderedLocusNames=MJ1261; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 9-411. RX PubMed=14688270; DOI=10.1074/jbc.M310418200; RA Roll-Mecak A., Alone P., Cao C., Dever T.E., Burley S.K.; RT "X-ray structure of translation initiation factor eIF2gamma: RT implications for tRNA and eIF2alpha binding."; RL J. Biol. Chem. 279:10634-10642(2004). CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis CC by forming a ternary complex with GTP and initiator tRNA. CC {ECO:0000250}. CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma CC chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. EIF2G CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99264.1; -; Genomic_DNA. DR PIR; D64457; D64457. DR PDB; 1S0U; X-ray; 2.40 A; A=9-411. DR PDBsum; 1S0U; -. DR ProteinModelPortal; Q58657; -. DR SMR; Q58657; 9-411. DR STRING; 243232.MJ_1261; -. DR EnsemblBacteria; AAB99264; AAB99264; MJ_1261. DR KEGG; mja:MJ_1261; -. DR eggNOG; arCOG01563; Archaea. DR eggNOG; COG5257; LUCA. DR InParanoid; Q58657; -. DR KO; K03242; -. DR OMA; IAANEPC; -. DR PhylomeDB; Q58657; -. DR EvolutionaryTrace; Q58657; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central. DR GO; GO:0001731; P:formation of translation preinitiation complex; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00119; eIF_2_gamma; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR022424; TIF2_gsu. DR InterPro; IPR015256; TIF2_gsu_C. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF09173; eIF2_C; 1. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03680; eif2g_arch; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; GTP-binding; Initiation factor; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 411 Translation initiation factor 2 subunit FT gamma. FT /FTId=PRO_0000137454. FT DOMAIN 9 203 tr-type G. FT NP_BIND 18 25 GTP. {ECO:0000250}. FT NP_BIND 90 94 GTP. {ECO:0000250}. FT NP_BIND 146 149 GTP. {ECO:0000250}. FT REGION 18 25 G1. {ECO:0000250}. FT REGION 46 50 G2. {ECO:0000250}. FT REGION 90 93 G3. {ECO:0000250}. FT REGION 146 149 G4. {ECO:0000250}. FT REGION 181 183 G5. {ECO:0000250}. FT STRAND 12 18 {ECO:0000244|PDB:1S0U}. FT HELIX 24 32 {ECO:0000244|PDB:1S0U}. FT STRAND 52 60 {ECO:0000244|PDB:1S0U}. FT TURN 62 64 {ECO:0000244|PDB:1S0U}. FT STRAND 67 72 {ECO:0000244|PDB:1S0U}. FT STRAND 81 90 {ECO:0000244|PDB:1S0U}. FT HELIX 94 102 {ECO:0000244|PDB:1S0U}. FT STRAND 109 116 {ECO:0000244|PDB:1S0U}. FT HELIX 124 135 {ECO:0000244|PDB:1S0U}. FT STRAND 141 146 {ECO:0000244|PDB:1S0U}. FT TURN 153 158 {ECO:0000244|PDB:1S0U}. FT HELIX 159 167 {ECO:0000244|PDB:1S0U}. FT TURN 171 174 {ECO:0000244|PDB:1S0U}. FT STRAND 177 179 {ECO:0000244|PDB:1S0U}. FT HELIX 188 198 {ECO:0000244|PDB:1S0U}. FT STRAND 211 218 {ECO:0000244|PDB:1S0U}. FT HELIX 227 229 {ECO:0000244|PDB:1S0U}. FT STRAND 234 242 {ECO:0000244|PDB:1S0U}. FT STRAND 249 258 {ECO:0000244|PDB:1S0U}. FT STRAND 265 272 {ECO:0000244|PDB:1S0U}. FT STRAND 275 278 {ECO:0000244|PDB:1S0U}. FT STRAND 281 286 {ECO:0000244|PDB:1S0U}. FT STRAND 288 290 {ECO:0000244|PDB:1S0U}. FT STRAND 292 295 {ECO:0000244|PDB:1S0U}. FT HELIX 300 302 {ECO:0000244|PDB:1S0U}. FT HELIX 304 306 {ECO:0000244|PDB:1S0U}. FT TURN 307 310 {ECO:0000244|PDB:1S0U}. FT STRAND 312 315 {ECO:0000244|PDB:1S0U}. FT STRAND 322 332 {ECO:0000244|PDB:1S0U}. FT STRAND 353 358 {ECO:0000244|PDB:1S0U}. FT STRAND 361 371 {ECO:0000244|PDB:1S0U}. FT STRAND 374 384 {ECO:0000244|PDB:1S0U}. FT STRAND 390 396 {ECO:0000244|PDB:1S0U}. FT STRAND 398 411 {ECO:0000244|PDB:1S0U}. SQ SEQUENCE 411 AA; 44596 MW; 75D94AF71088008F CRC64; MAKKKQAKQA EVNIGMVGHV DHGKTSLTKA LTGVWTDRHS EELRRGISIR LGYADCEIRK CPQCGTYTTK PRCPNCLAET EFLRRVSFVD SPGHETLMAT MLSGASLMDG AILVIAANEP CPQPQTKEHL MALEILGIDK IIIVQNKIDL VDEKQAEENY EQIKEFVKGT IAENAPIIPI SAHHEANIDV LLKAIQDFIP TPKRDPDATP RMYVARSFDI NKPGTEIKDL KGGVLGGAII QGVFKVGDEI EIRPGIKVTE GNKTFWKPLT TKIVSLAAGN TILRKAHPGG LIGVGTTLDP YLTKSDALTG SVVGLPGTLP PIREKITIRA NLLDRVVGTK EELKIEPLRT GEVLMLNIGT ATTAGVITSA RGDIADIKLK LPICAEIGDR VAISRRVGSR WRLIGYGTIE G // ID ISF1_METJA Reviewed; 198 AA. AC Q58141; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 80. DE RecName: Full=Iron-sulfur flavoprotein MJ0731; DE Short=Isf-1; DE AltName: Full=MCJ-1; DE Short=Mj1; GN OrderedLocusNames=MJ0731; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN FAMILY. RX PubMed=10986231; DOI=10.1128/JB.182.19.5309-5316.2000; RA Leartsakulpanich U., Antonkine M.L., Ferry J.G.; RT "Site-specific mutational analysis of a novel cysteine motif proposed RT to ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the RT thermophilic methanoarchaeon Methanosarcina thermophila."; RL J. Bacteriol. 182:5309-5316(2000). CC -!- FUNCTION: Redox-active protein probably involved in electron CC transport. {ECO:0000250}. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the SsuE family. Isf subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98727.1; -; Genomic_DNA. DR PIR; C64391; C64391. DR ProteinModelPortal; Q58141; -. DR STRING; 243232.MJ_0731; -. DR EnsemblBacteria; AAB98727; AAB98727; MJ_0731. DR KEGG; mja:MJ_0731; -. DR eggNOG; arCOG02573; Archaea. DR eggNOG; COG0655; LUCA. DR InParanoid; Q58141; -. DR OMA; ANLGATF; -. DR PhylomeDB; Q58141; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR005025; FMN_Rdtase-like. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Flavoprotein; FMN; Iron; Iron-sulfur; KW Metal-binding; Reference proteome. FT CHAIN 1 198 Iron-sulfur flavoprotein MJ0731. FT /FTId=PRO_0000160599. FT METAL 46 46 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 49 49 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 52 52 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 59 59 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 198 AA; 22220 MW; FBED0E57A4C77017 CRC64; MKVFGISGSP RLQGTHFAVN YALNYLKEKG AEVRYFSVSR KKINFCLHCD YCIKKKEGCI HKDDMEEVYE NLIWADGVII GTPVYQGNVT GQLKTLMDRC RAILAKNPKV LRGRVGMAIA VGGDRNGGQE IALRTIHDFF IINEMIPVGG GSFGANLGAT FWSKDRGKKG VEEDEEGLRV LRKTLNRFYE VLKEKRGL // ID ISF2_METJA Reviewed; 193 AA. AC Q58483; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 86. DE RecName: Full=Iron-sulfur flavoprotein MJ1083; DE AltName: Full=Isf-2; DE AltName: Full=MCJ-2; DE Short=Mj2; GN OrderedLocusNames=MJ1083; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, COFACTOR, AND IRON-SULFUR CLUSTER. RX PubMed=11591665; DOI=10.1128/JB.183.21.6225-6233.2001; RA Zhao T., Cruz F., Ferry J.G.; RT "Iron-sulfur flavoprotein (Isf) from Methanosarcina thermophila is the RT prototype of a widely distributed family."; RL J. Bacteriol. 183:6225-6233(2001). RN [3] RP PROTEIN FAMILY. RX PubMed=10986231; DOI=10.1128/JB.182.19.5309-5316.2000; RA Leartsakulpanich U., Antonkine M.L., Ferry J.G.; RT "Site-specific mutational analysis of a novel cysteine motif proposed RT to ligate the 4Fe-4S cluster in the iron-sulfur flavoprotein of the RT thermophilic methanoarchaeon Methanosarcina thermophila."; RL J. Bacteriol. 182:5309-5316(2000). CC -!- FUNCTION: Redox-active protein probably involved in electron CC transport. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; CC Evidence={ECO:0000269|PubMed:11591665}; CC Note=Binds 1 FMN per subunit. {ECO:0000269|PubMed:11591665}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305|PubMed:11591665}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000305|PubMed:11591665}; CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Belongs to the SsuE family. Isf subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99085.1; -; Genomic_DNA. DR PIR; B64435; B64435. DR ProteinModelPortal; Q58483; -. DR STRING; 243232.MJ_1083; -. DR EnsemblBacteria; AAB99085; AAB99085; MJ_1083. DR KEGG; mja:MJ_1083; -. DR eggNOG; arCOG02573; Archaea. DR eggNOG; COG0655; LUCA. DR InParanoid; Q58483; -. DR OMA; CKNDDIG; -. DR PhylomeDB; Q58483; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR005025; FMN_Rdtase-like. DR Pfam; PF03358; FMN_red; 1. DR SUPFAM; SSF52218; SSF52218; 1. PE 1: Evidence at protein level; KW 4Fe-4S; Complete proteome; Direct protein sequencing; Flavoprotein; KW FMN; Iron; Iron-sulfur; Metal-binding; Reference proteome. FT CHAIN 1 193 Iron-sulfur flavoprotein MJ1083. FT /FTId=PRO_0000160600. FT METAL 47 47 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 50 50 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 53 53 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 59 59 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 193 AA; 20648 MW; EB58694A037D2F0B CRC64; MKVIGISGSP RPEGNTTLLV REALNAIAEE GIETEFISLA DKELNPCIGC NMCKEEGKCP IIDDVDEILK KMKEADGIIL GSPVYFGGVS AQLKMLMDRS RPLRIGFQLR NKVGGAVAVG ASRNGGQETT IQQIHNFFLI HSMIVVGDND PTAHYGGTGV GKAPGDCKND DIGLETARNL GKKVAEVVKL IKK // ID IF2A_METJA Reviewed; 266 AA. AC Q57581; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Translation initiation factor 2 subunit alpha; DE AltName: Full=aIF2-alpha; DE AltName: Full=eIF-2-alpha; GN Name=eif2a; OrderedLocusNames=MJ0117; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: eIF-2 functions in the early steps of protein synthesis CC by forming a ternary complex with GTP and initiator tRNA. CC {ECO:0000250}. CC -!- SUBUNIT: Heterotrimer composed of an alpha, a beta and a gamma CC chain. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eIF-2-alpha family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98098.1; -; Genomic_DNA. DR PIR; E64314; E64314. DR ProteinModelPortal; Q57581; -. DR SMR; Q57581; 6-265. DR STRING; 243232.MJ_0117; -. DR EnsemblBacteria; AAB98098; AAB98098; MJ_0117. DR KEGG; mja:MJ_0117; -. DR eggNOG; arCOG04107; Archaea. DR eggNOG; COG1093; LUCA. DR InParanoid; Q57581; -. DR KO; K03237; -. DR OMA; KDVNEHQ; -. DR PhylomeDB; Q57581; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0043022; F:ribosome binding; IBA:GO_Central. DR GO; GO:0003743; F:translation initiation factor activity; IBA:GO_Central. DR GO; GO:0006413; P:translational initiation; IBA:GO_Central. DR Gene3D; 1.10.150.190; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.70.1130; -; 1. DR HAMAP; MF_00231; eIF_2_alpha; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR InterPro; IPR022964; TIF2_asu_arc. DR InterPro; IPR024055; TIF2_asu_C. DR InterPro; IPR024054; TIF2_asu_middle. DR InterPro; IPR011488; TIF_2_asu. DR Pfam; PF07541; EIF_2_alpha; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF110993; SSF110993; 1. DR SUPFAM; SSF116742; SSF116742; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50126; S1; 1. PE 3: Inferred from homology; KW Complete proteome; Initiation factor; Protein biosynthesis; KW Reference proteome; RNA-binding. FT CHAIN 1 266 Translation initiation factor 2 subunit FT alpha. FT /FTId=PRO_0000137394. FT DOMAIN 12 83 S1 motif. SQ SEQUENCE 266 AA; 30485 MW; 31D2805A642D372A CRC64; MFIMRREFPE EGDIVIGTVK DVKPYGAFVE LLEYPGKEGM IHISEVTSGW VKNIRDHVKV GQRVVAKVLR VDERKGHIDL SLKRVTEQQK RAKVQEWKRF QRASKMLERA AEKLGKSLEE AWEEVGYLLE DEFGELYNAF ETMVIEGKEV LDDLEISEEW KNVLYEVAKE SIELTNVEVE GVIEMKSYAP DGIKQIKKAL TTALKANPYE DVEVKITYIG APKYRVVVIA PDYKSGEEVF KKVCEKAVAT IKKLGGEGTY YRESKK // ID IF6_METJA Reviewed; 228 AA. AC Q60357; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 104. DE RecName: Full=Translation initiation factor 6 {ECO:0000255|HAMAP-Rule:MF_00032}; DE Short=aIF-6 {ECO:0000255|HAMAP-Rule:MF_00032}; GN Name=eif6 {ECO:0000255|HAMAP-Rule:MF_00032}; OrderedLocusNames=MJ0048; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, MASS SPECTROMETRY, AND X-RAY CRYSTALLOGRAPHY (1.3 RP ANGSTROMS). RX PubMed=11101899; DOI=10.1038/82017; RA Groft C.M., Beckmann R., Sali A., Burley S.K.; RT "Crystal structures of ribosome anti-association factor IF6."; RL Nat. Struct. Biol. 7:1156-1164(2000). CC -!- FUNCTION: Binds to the 50S ribosomal subunit and prevents its CC association with the 30S ribosomal subunit to form the 70S CC initiation complex. {ECO:0000255|HAMAP-Rule:MF_00032, CC ECO:0000269|PubMed:11101899}. CC -!- MASS SPECTROMETRY: Mass=24948; Mass_error=6; Method=MALDI; CC Range=1-228; Evidence={ECO:0000269|PubMed:11101899}; CC -!- SIMILARITY: Belongs to the eIF-6 family. {ECO:0000255|HAMAP- CC Rule:MF_00032}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98029.1; -; Genomic_DNA. DR PIR; H64305; H64305. DR PDB; 1G61; X-ray; 1.30 A; A/B=1-228. DR PDBsum; 1G61; -. DR ProteinModelPortal; Q60357; -. DR SMR; Q60357; 3-227. DR STRING; 243232.MJ_0048; -. DR EnsemblBacteria; AAB98029; AAB98029; MJ_0048. DR KEGG; mja:MJ_0048; -. DR eggNOG; arCOG04176; Archaea. DR eggNOG; COG1976; LUCA. DR InParanoid; Q60357; -. DR KO; K03264; -. DR OMA; NDWCAFT; -. DR PhylomeDB; Q60357; -. DR EvolutionaryTrace; Q60357; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042256; P:mature ribosome assembly; IEA:InterPro. DR HAMAP; MF_00032; eIF_6; 1. DR InterPro; IPR002769; eIF6. DR PANTHER; PTHR10784; PTHR10784; 1. DR Pfam; PF01912; eIF-6; 1. DR PIRSF; PIRSF006413; IF-6; 1. DR SMART; SM00654; eIF6; 1. DR TIGRFAMs; TIGR00323; eIF-6; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Initiation factor; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 228 Translation initiation factor 6. FT /FTId=PRO_0000153746. FT STRAND 4 7 {ECO:0000244|PDB:1G61}. FT HELIX 15 18 {ECO:0000244|PDB:1G61}. FT STRAND 23 28 {ECO:0000244|PDB:1G61}. FT HELIX 34 44 {ECO:0000244|PDB:1G61}. FT STRAND 47 50 {ECO:0000244|PDB:1G61}. FT HELIX 59 62 {ECO:0000244|PDB:1G61}. FT STRAND 67 73 {ECO:0000244|PDB:1G61}. FT HELIX 78 90 {ECO:0000244|PDB:1G61}. FT STRAND 96 100 {ECO:0000244|PDB:1G61}. FT HELIX 107 110 {ECO:0000244|PDB:1G61}. FT STRAND 111 113 {ECO:0000244|PDB:1G61}. FT STRAND 115 120 {ECO:0000244|PDB:1G61}. FT HELIX 122 127 {ECO:0000244|PDB:1G61}. FT HELIX 128 135 {ECO:0000244|PDB:1G61}. FT STRAND 137 141 {ECO:0000244|PDB:1G61}. FT TURN 150 152 {ECO:0000244|PDB:1G61}. FT STRAND 153 156 {ECO:0000244|PDB:1G61}. FT STRAND 158 163 {ECO:0000244|PDB:1G61}. FT HELIX 169 179 {ECO:0000244|PDB:1G61}. FT STRAND 182 186 {ECO:0000244|PDB:1G61}. FT TURN 190 192 {ECO:0000244|PDB:1G61}. FT HELIX 196 198 {ECO:0000244|PDB:1G61}. FT STRAND 200 202 {ECO:0000244|PDB:1G61}. FT STRAND 207 210 {ECO:0000244|PDB:1G61}. FT HELIX 215 225 {ECO:0000244|PDB:1G61}. SQ SEQUENCE 228 AA; 24459 MW; 94DA7E11C10FCB47 CRC64; MTMIIRKYFS GIPTIGVLAL TTEEITLLPI FLDKDDVNEV SEVLETKCLQ TNIGGSSLVG SLSVANKYGL LLPKIVEDEE LDRIKNFLKE NNLDLNVEII KSKNTALGNL ILTNDKGALI SPELKDFKKD IEDSLNVEVE IGTIAELPTV GSNAVVTNKG CLTHPLVEDD ELEFLKSLFK VEYIGKGTAN KGTTSVGACI IANSKGAVVG GDTTGPELLI IEDALGLI // ID ILVB_METJA Reviewed; 591 AA. AC Q57725; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 109. DE RecName: Full=Probable acetolactate synthase large subunit; DE Short=AHAS; DE EC=2.2.1.6; DE AltName: Full=Acetohydroxy-acid synthase large subunit; DE Short=ALS; GN Name=ilvB; OrderedLocusNames=MJ0277; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. CC -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98265.1; -; Genomic_DNA. DR PIR; F64334; F64334. DR ProteinModelPortal; Q57725; -. DR STRING; 243232.MJ_0277; -. DR EnsemblBacteria; AAB98265; AAB98265; MJ_0277. DR KEGG; mja:MJ_0277; -. DR eggNOG; arCOG01998; Archaea. DR eggNOG; COG0028; LUCA. DR InParanoid; Q57725; -. DR KO; K01652; -. DR OMA; MVWPMVP; -. DR PhylomeDB; Q57725; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR012846; Acetolactate_synth_lsu. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR000399; TPP-bd_CS. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. DR TIGRFAMs; TIGR00118; acolac_lg; 1. DR PROSITE; PS00187; TPP_ENZYMES; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; FAD; Flavoprotein; Magnesium; Metal-binding; KW Reference proteome; Thiamine pyrophosphate; Transferase. FT CHAIN 1 591 Probable acetolactate synthase large FT subunit. FT /FTId=PRO_0000090808. FT NP_BIND 258 279 FAD. {ECO:0000250}. FT NP_BIND 301 320 FAD. {ECO:0000250}. FT REGION 396 476 Thiamine pyrophosphate binding. FT METAL 447 447 Magnesium. {ECO:0000250}. FT METAL 474 474 Magnesium. {ECO:0000250}. FT BINDING 47 47 Thiamine pyrophosphate. {ECO:0000250}. FT BINDING 149 149 FAD. {ECO:0000250}. SQ SEQUENCE 591 AA; 64493 MW; DB398C926D9B3A9D CRC64; MKGAEAIIKA LEAEGVKIIF GYPGGAMLPF YDALYDSDLV HILTRHEQAA AHAADGFARA SGEAGVCVST SGPGATNLVT GIATAYADSS PVIALTGQVP TKLIGNDAFQ EIDALGLFMP ITKHNFQIKK PEEIPETFRA AFEIATTGRP GPVHIDLPKD VQDGEIDIEK YPIPAKVDLP GYKPKTVGHP LQIKKAAKLI AESERPVILA GGGVIISGAS EELLRLAEFV KIPVCTTLMG KGCFPEDHPL ALGMVGMHGT KAANYAVTEC DVLIAIGCRF SDRVTGDIRY FAPEAKIIHI DIDPAEIGKN VRADIPIVGD AKNVLRDLLA ALIALEIKDK ETWLERIYEL KKLSIPMMDF DDKPIKPQRF VKDLMEVLNE IDSKLKNTII TTDVGQNQMW MAHFFKTKMP RSFLASGGLG TMGFGFPAAI GAKVAKPYAN VISITGDGGF LMNSQELATI SEYDIPVVIC IFDNRTLGMV YQWQNLYYGQ RQSEVHLGES PDFVKLAESY GVKADRIISP DEIKEKLKEA ILSNEPYLLD IVIDPAEALP MVPPGGRLTN IVQPIRVEPK IKKPQFDEIK KIRDMAAVKE F // ID ILVD_METJA Reviewed; 553 AA. AC Q58672; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 11-JUL-2002, sequence version 2. DT 17-FEB-2016, entry version 101. DE RecName: Full=Dihydroxy-acid dehydratase {ECO:0000255|HAMAP-Rule:MF_00012}; DE Short=DAD {ECO:0000255|HAMAP-Rule:MF_00012}; DE EC=4.2.1.9 {ECO:0000255|HAMAP-Rule:MF_00012}; GN Name=ilvD {ECO:0000255|HAMAP-Rule:MF_00012}; OrderedLocusNames=MJ1276; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2,3-dihydroxy-3-methylbutanoate = 3-methyl-2- CC oxobutanoate + H(2)O. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00012}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00012}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 3/4. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 3/4. {ECO:0000255|HAMAP-Rule:MF_00012}. CC -!- SIMILARITY: Belongs to the IlvD/Edd family. {ECO:0000255|HAMAP- CC Rule:MF_00012}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99282.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99282.1; ALT_INIT; Genomic_DNA. DR PIR; C64459; C64459. DR STRING; 243232.MJ_1276; -. DR EnsemblBacteria; AAB99282; AAB99282; MJ_1276. DR KEGG; mja:MJ_1276; -. DR eggNOG; arCOG04045; Archaea. DR eggNOG; COG0129; LUCA. DR InParanoid; Q58672; -. DR KO; K01687; -. DR OMA; GYEGNPC; -. DR PhylomeDB; Q58672; -. DR UniPathway; UPA00047; UER00057. DR UniPathway; UPA00049; UER00061. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004160; F:dihydroxy-acid dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016836; F:hydro-lyase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009082; P:branched-chain amino acid biosynthetic process; IBA:GO_Central. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00012; IlvD; 1. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR004404; DihydroxyA_deHydtase. DR InterPro; IPR000581; DiOHA_6PGluconate_deHydtase. DR InterPro; IPR020558; DiOHA_6PGluconate_deHydtase_CS. DR PANTHER; PTHR21000; PTHR21000; 1. DR Pfam; PF00920; ILVD_EDD; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR00110; ilvD; 1. DR PROSITE; PS00886; ILVD_EDD_1; 1. DR PROSITE; PS00887; ILVD_EDD_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Lyase; Metal-binding; Reference proteome. FT CHAIN 1 553 Dihydroxy-acid dehydratase. FT /FTId=PRO_0000103541. FT METAL 119 119 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. FT METAL 191 191 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00012}. SQ SEQUENCE 553 AA; 59198 MW; 9FF5127928919E60 CRC64; MISDRVKKGL KRAPNRSLLK ACGYTDEELE RPFIGVVNSF TEVVPGHIHL RDIAEAVKKG IYANGGTAFE FNTMAICDGI AMGHEGMKYS LPSREIIADT VESMAKAHGF DGLVLIPSCD KIVPGMIMGA IRTGLPFIVV TGGPMFPGEL RGKKYDLISV FEGVGACAAG KITEEELKEI EDIACPGAGS CAGLFTANTM ACLTEAMGLS LPYCATSHAT TAEKIRIAKR SGMRIVDLVR NNITPDKILT KEAFENAILV DLALGGSTNT TLHIPAIANE VKPKFITLDD FDRLSGEVPH IASLRPGGEH FIIDLHRAGG IPAVLKVLEE KIRKECLTVS GKTIGEIIKE VKYIDYSVIR PVDNPVHETA GLRILKGSLA PNGAVVKIGA VNPKMYKHEG PARVFDSEEE AVDAILGGDI ERGDVVVIRY EGPAGGPGMR EMLAPTSAIC GMGLDDSVAL ITDGRFSGGS RGPCIGHVSP EAMAGGPIAI VEDGDIIKID MINKKLDLAL DEEEIKERLA KWKKPEPKVK KGYLARYAKL VSSADEGAVL RYD // ID ILVE_METJA Reviewed; 288 AA. AC Q58414; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Putative branched-chain-amino-acid aminotransferase; DE Short=BCAT; DE EC=2.6.1.42; DE AltName: Full=Transaminase B; GN Name=ilvE; OrderedLocusNames=MJ1008; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Acts on leucine, isoleucine and valine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-leucine + 2-oxoglutarate = 4-methyl-2- CC oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-isoleucine + 2-oxoglutarate = (S)-3-methyl- CC 2-oxopentanoate + L-glutamate. CC -!- CATALYTIC ACTIVITY: L-valine + 2-oxoglutarate = 3-methyl-2- CC oxobutanoate + L-glutamate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 4/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 4/4. CC -!- SIMILARITY: Belongs to the class-IV pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99010.1; -; Genomic_DNA. DR PIR; G64425; G64425. DR ProteinModelPortal; Q58414; -. DR STRING; 243232.MJ_1008; -. DR EnsemblBacteria; AAB99010; AAB99010; MJ_1008. DR KEGG; mja:MJ_1008; -. DR eggNOG; arCOG02297; Archaea. DR eggNOG; COG0115; LUCA. DR InParanoid; Q58414; -. DR KO; K00826; -. DR OMA; IFEGIRI; -. DR PhylomeDB; Q58414; -. DR UniPathway; UPA00047; UER00058. DR UniPathway; UPA00048; UER00073. DR UniPathway; UPA00049; UER00062. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0052656; F:L-isoleucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052654; F:L-leucine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0052655; F:L-valine transaminase activity; IEA:UniProtKB-EC. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR001544; Aminotrans_IV. DR InterPro; IPR018300; Aminotrans_IV_CS. DR InterPro; IPR005785; B_amino_transI. DR PANTHER; PTHR11825; PTHR11825; 1. DR Pfam; PF01063; Aminotran_4; 1. DR SUPFAM; SSF56752; SSF56752; 1. DR TIGRFAMs; TIGR01122; ilvE_I; 1. DR PROSITE; PS00770; AA_TRANSFER_CLASS_4; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aminotransferase; KW Branched-chain amino acid biosynthesis; Complete proteome; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 288 Putative branched-chain-amino-acid FT aminotransferase. FT /FTId=PRO_0000103290. FT MOD_RES 146 146 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255}. SQ SEQUENCE 288 AA; 32096 MW; 033DB417DFD89CBC CRC64; MKIYLNGKFV DEKDAKVSVF DHGLLYGDGV FEGIRAYDGV VFMLKEHIDR LYDSAKSLCI DIPLTKEEMI DVVLETLRVN NLRDAYIRLV VTRGVGDLGL DPRKCGKPTI FCIAIPMPPL LGEDGIRAIT VSVRRLPVDV LNPAVKSLNY LNSVLAKIQA NYAGVDEAFL LDDKGFVVEG TGDNIFIVKN GVLKTPPVYQ SILKGITRDV VIKLAKEEGI EVVEEPLTLH DLYTADELFI TGTAAEIVPV FEIDGRVINN KQVGEITKKL KEKFKDIRTK WGIKVYDE // ID IF5A_METJA Reviewed; 132 AA. AC Q58625; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 119. DE RecName: Full=Translation initiation factor 5A; DE AltName: Full=Hypusine-containing protein; DE AltName: Full=eIF-5A; GN Name=eif5a; OrderedLocusNames=MJ1228; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9419357; DOI=10.1073/pnas.95.1.224; RA Kyrpides N.C., Woese C.R.; RT "Universally conserved translation initiation factors."; RL Proc. Natl. Acad. Sci. U.S.A. 95:224-228(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS), AND HYPUSINE AT LYS-37. RX PubMed=9724718; DOI=10.1073/pnas.95.18.10419; RA Kim K.K., Hung L.W., Yokota H., Kim R., Kim S.H.; RT "Crystal structures of eukaryotic translation initiation factor 5A RT from Methanococcus jannaschii at 1.8-A resolution."; RL Proc. Natl. Acad. Sci. U.S.A. 95:10419-10424(1998). CC -!- FUNCTION: Functions by promoting the formation of the first CC peptide bond. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the eIF-5A family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99231.1; -; Genomic_DNA. DR PDB; 1EIF; X-ray; 1.90 A; A=1-132. DR PDB; 2EIF; X-ray; 1.80 A; A=1-132. DR PDBsum; 1EIF; -. DR PDBsum; 2EIF; -. DR ProteinModelPortal; Q58625; -. DR SMR; Q58625; 1-129. DR STRING; 243232.MJ_1228; -. DR EnsemblBacteria; AAB99231; AAB99231; MJ_1228. DR KEGG; mja:MJ_1228; -. DR eggNOG; arCOG04277; Archaea. DR eggNOG; COG0231; LUCA. DR InParanoid; Q58625; -. DR KO; K03263; -. DR OMA; ETYETIT; -. DR PhylomeDB; Q58625; -. DR EvolutionaryTrace; Q58625; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043022; F:ribosome binding; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro. DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045901; P:positive regulation of translational elongation; IEA:InterPro. DR GO; GO:0045905; P:positive regulation of translational termination; IEA:InterPro. DR GO; GO:0006452; P:translational frameshifting; IEA:InterPro. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00085; eIF_5A; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR019769; Trans_elong_IF5A_hypusine_site. DR InterPro; IPR001884; Transl_elong_IF5A. DR InterPro; IPR022847; Transl_elong_IF5A_arc. DR InterPro; IPR020189; Transl_elong_IF5A_C. DR InterPro; IPR013185; Transl_elong_KOW-like. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR11673; PTHR11673; 1. DR Pfam; PF08207; EFP_N; 1. DR Pfam; PF01287; eIF-5a; 1. DR PIRSF; PIRSF003025; eIF5A; 1. DR SMART; SM01376; eIF-5a; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00037; eIF_5A; 1. DR PROSITE; PS00302; IF5A_HYPUSINE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hypusine; KW Initiation factor; Protein biosynthesis; Reference proteome. FT CHAIN 1 132 Translation initiation factor 5A. FT /FTId=PRO_0000142493. FT MOD_RES 37 37 Hypusine. {ECO:0000269|PubMed:9724718}. FT STRAND 2 8 {ECO:0000244|PDB:2EIF}. FT HELIX 9 11 {ECO:0000244|PDB:2EIF}. FT STRAND 16 20 {ECO:0000244|PDB:2EIF}. FT STRAND 23 32 {ECO:0000244|PDB:2EIF}. FT STRAND 37 39 {ECO:0000244|PDB:2EIF}. FT STRAND 42 52 {ECO:0000244|PDB:2EIF}. FT STRAND 55 61 {ECO:0000244|PDB:2EIF}. FT STRAND 64 69 {ECO:0000244|PDB:2EIF}. FT STRAND 71 82 {ECO:0000244|PDB:2EIF}. FT STRAND 85 90 {ECO:0000244|PDB:2EIF}. FT TURN 91 93 {ECO:0000244|PDB:2EIF}. FT STRAND 96 100 {ECO:0000244|PDB:2EIF}. FT STRAND 113 119 {ECO:0000244|PDB:2EIF}. FT STRAND 122 128 {ECO:0000244|PDB:2EIF}. SQ SEQUENCE 132 AA; 14180 MW; 5B0F48905B0DCF69 CRC64; MPGTKQVNVG SLKVGQYVMI DGVPCEIVDI SVSKPGKHGG AKARVVGIGI FEKVKKEFVA PTSSKVEVPI IDRRKGQVLA IMGDMVQIMD LQTYETLELP IPEGIEGLEP GGEVEYIEAV GQYKITRVIG GK // ID IPK_METJA Reviewed; 260 AA. AC Q60352; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 78. DE RecName: Full=Isopentenyl phosphate kinase; DE Short=IPK; DE EC=2.7.4.26; GN OrderedLocusNames=MJ0044; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND CATALYTIC RP ACTIVITY. RX PubMed=16621811; DOI=10.1128/JB.188.9.3192-3198.2006; RA Grochowski L.L., Xu H., White R.H.; RT "Methanocaldococcus jannaschii uses a modified mevalonate pathway for RT biosynthesis of isopentenyl diphosphate."; RL J. Bacteriol. 188:3192-3198(2006). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEXES WITH ISOPENTENYL RP PHOSPHATE; ISOPENTENYL DIPHOSPHATE AND SULFATE, CATALYTIC ACTIVITY, RP FUNCTION, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP HIS-60; PHE-83; ILE-86 AND ILE-156. RX PubMed=20392112; DOI=10.1021/cb1000313; RA Dellas N., Noel J.P.; RT "Mutation of archaeal isopentenyl phosphate kinase highlights RT mechanism and guides phosphorylation of additional isoprenoid RT monophosphates."; RL ACS Chem. Biol. 5:589-601(2010). CC -!- FUNCTION: Catalyzes the formation of isopentenyl diphosphate CC (IPP), the building block of all isoprenoids. Has no activity with CC farnesyl phosphate. {ECO:0000269|PubMed:16621811, CC ECO:0000269|PubMed:20392112}. CC -!- CATALYTIC ACTIVITY: ATP + isopentenyl phosphate = ADP + CC isopentenyl diphosphate. {ECO:0000269|PubMed:16621811, CC ECO:0000269|PubMed:20392112}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.3 uM for isopentenyl phosphate CC {ECO:0000269|PubMed:16621811, ECO:0000269|PubMed:20392112}; CC KM=198 uM for ATP {ECO:0000269|PubMed:16621811, CC ECO:0000269|PubMed:20392112}; CC pH dependence: CC Optimum pH is 7-9. {ECO:0000269|PubMed:16621811, CC ECO:0000269|PubMed:20392112}; CC Temperature dependence: CC Retains 38% activity when incubated at 100 degrees Celsius for CC 10 minutes. {ECO:0000269|PubMed:16621811, CC ECO:0000269|PubMed:20392112}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20392112}. CC -!- SIMILARITY: Belongs to the isopentenyl phosphate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98024.1; -; Genomic_DNA. DR PIR; D64305; D64305. DR PDB; 3K4O; X-ray; 2.05 A; A/B=1-260. DR PDB; 3K4Y; X-ray; 2.54 A; A/B=1-260. DR PDB; 3K52; X-ray; 2.70 A; A/B=1-260. DR PDB; 3K56; X-ray; 2.34 A; A/B=1-260. DR PDBsum; 3K4O; -. DR PDBsum; 3K4Y; -. DR PDBsum; 3K52; -. DR PDBsum; 3K56; -. DR ProteinModelPortal; Q60352; -. DR STRING; 243232.MJ_0044; -. DR EnsemblBacteria; AAB98024; AAB98024; MJ_0044. DR KEGG; mja:MJ_0044; -. DR eggNOG; arCOG00860; Archaea. DR eggNOG; COG1608; LUCA. DR InParanoid; Q60352; -. DR KO; K06981; -. DR OMA; KVMECYN; -. DR PhylomeDB; Q60352; -. DR BioCyc; MetaCyc:MONOMER-14619; -. DR BRENDA; 2.7.4.26; 3260. DR EvolutionaryTrace; Q60352; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004349; F:glutamate 5-kinase activity; IBA:GO_Central. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0006561; P:proline biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR024192; Fosfomycin_R_FomA-type. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF016496; Kin_FomA; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Isoprene biosynthesis; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 260 Isopentenyl phosphate kinase. FT /FTId=PRO_0000106666. FT NP_BIND 6 10 ATP. {ECO:0000305}. FT BINDING 55 55 Substrate; via amide nitrogen. FT BINDING 56 56 ATP; via amide nitrogen. {ECO:0000250}. FT BINDING 60 60 Substrate. FT BINDING 159 159 Substrate; via amide nitrogen. FT BINDING 180 180 ATP. {ECO:0000250}. FT BINDING 217 217 ATP; via carbonyl oxygen. {ECO:0000250}. FT BINDING 221 221 ATP. {ECO:0000305}. FT SITE 15 15 Transition state stabilizer. FT {ECO:0000250}. FT MUTAGEN 60 60 H->A,N: Abolishes enzyme activity. FT {ECO:0000269|PubMed:20392112}. FT MUTAGEN 60 60 H->Q: Nearly abolishes enzyme activity. FT {ECO:0000269|PubMed:20392112}. FT MUTAGEN 83 83 F->A: Confers activity with farnesyl FT phosphate; when associated with A-86 and FT A-156. Confers low activity with farnesyl FT phosphate. {ECO:0000269|PubMed:20392112}. FT MUTAGEN 86 86 I->A: Confers activity with farnesyl FT phosphate; when associated with A-83 and FT A-156. {ECO:0000269|PubMed:20392112}. FT MUTAGEN 86 86 I->G: Confers low activity with farnesyl FT phosphate. {ECO:0000269|PubMed:20392112}. FT MUTAGEN 156 156 I->A: Confers activity with farnesyl FT phosphate; when associated with A-83 and FT A-86. {ECO:0000269|PubMed:20392112}. FT MUTAGEN 156 156 I->G: Confers low activity with farnesyl FT phosphate. {ECO:0000269|PubMed:20392112}. FT STRAND 2 7 {ECO:0000244|PDB:3K4O}. FT HELIX 9 12 {ECO:0000244|PDB:3K56}. FT HELIX 23 42 {ECO:0000244|PDB:3K4O}. FT STRAND 48 53 {ECO:0000244|PDB:3K4O}. FT HELIX 56 63 {ECO:0000244|PDB:3K4O}. FT HELIX 64 66 {ECO:0000244|PDB:3K4O}. FT STRAND 67 69 {ECO:0000244|PDB:3K4O}. FT STRAND 71 76 {ECO:0000244|PDB:3K4O}. FT HELIX 79 102 {ECO:0000244|PDB:3K4O}. FT TURN 103 105 {ECO:0000244|PDB:3K4O}. FT STRAND 108 111 {ECO:0000244|PDB:3K4O}. FT HELIX 113 115 {ECO:0000244|PDB:3K4O}. FT STRAND 118 122 {ECO:0000244|PDB:3K4O}. FT HELIX 128 135 {ECO:0000244|PDB:3K4O}. FT STRAND 139 143 {ECO:0000244|PDB:3K4O}. FT STRAND 145 152 {ECO:0000244|PDB:3K4O}. FT STRAND 154 157 {ECO:0000244|PDB:3K4O}. FT HELIX 159 170 {ECO:0000244|PDB:3K4O}. FT STRAND 173 190 {ECO:0000244|PDB:3K4O}. FT STRAND 192 194 {ECO:0000244|PDB:3K4O}. FT TURN 196 198 {ECO:0000244|PDB:3K4O}. FT HELIX 199 207 {ECO:0000244|PDB:3K4O}. FT STRAND 208 210 {ECO:0000244|PDB:3K4Y}. FT HELIX 217 227 {ECO:0000244|PDB:3K4O}. FT STRAND 231 236 {ECO:0000244|PDB:3K4O}. FT HELIX 242 247 {ECO:0000244|PDB:3K4O}. FT STRAND 253 257 {ECO:0000244|PDB:3K4O}. SQ SEQUENCE 260 AA; 29472 MW; 833C2BFF020E3F07 CRC64; MLTILKLGGS ILSDKNVPYS IKWDNLERIA MEIKNALDYY KNQNKEIKLI LVHGGGAFGH PVAKKYLKIE DGKKIFINME KGFWEIQRAM RRFNNIIIDT LQSYDIPAVS IQPSSFVVFG DKLIFDTSAI KEMLKRNLVP VIHGDIVIDD KNGYRIISGD DIVPYLANEL KADLILYATD VDGVLIDNKP IKRIDKNNIY KILNYLSGSN SIDVTGGMKY KIDMIRKNKC RGFVFNGNKA NNIYKALLGE VEGTEIDFSE // ID ILVH_METJA Reviewed; 172 AA. AC Q57625; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Probable acetolactate synthase small subunit; DE EC=2.2.1.6; DE AltName: Full=Acetohydroxy-acid synthase small subunit; DE Short=AHAS; DE Short=ALS; GN Name=ilvH; Synonyms=ilvN; OrderedLocusNames=MJ0161; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 pyruvate = 2-acetolactate + CO(2). CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; L- CC isoleucine from 2-oxobutanoate: step 1/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-valine biosynthesis; L-valine CC from pyruvate: step 1/4. CC -!- SUBUNIT: Dimer of large and small chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the acetolactate synthase small subunit CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98145.1; -; Genomic_DNA. DR PIR; B64320; B64320. DR ProteinModelPortal; Q57625; -. DR STRING; 243232.MJ_0161; -. DR EnsemblBacteria; AAB98145; AAB98145; MJ_0161. DR KEGG; mja:MJ_0161; -. DR eggNOG; arCOG04445; Archaea. DR eggNOG; COG0440; LUCA. DR InParanoid; Q57625; -. DR KO; K01653; -. DR OMA; PYGIREI; -. DR PhylomeDB; Q57625; -. DR UniPathway; UPA00047; UER00055. DR UniPathway; UPA00049; UER00059. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003984; F:acetolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009099; P:valine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR004789; Acetalactate_synth_ssu. DR InterPro; IPR019455; Acetolactate_synth_ssu_C. DR InterPro; IPR002912; ACT_dom. DR Pfam; PF10369; ALS_ss_C; 1. DR TIGRFAMs; TIGR00119; acolac_sm; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 172 Probable acetolactate synthase small FT subunit. FT /FTId=PRO_0000151423. FT DOMAIN 10 84 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 172 AA; 19057 MW; 8C00191BD2B18303 CRC64; MVNIMEHRHV ISALVLNKPG VLQRISGLFT RRGFNISSIT VGITENPQIS RVTIVVNGDD KILEQVIKQL NKLIDVIKVS ELEEKKSVQR ELCLIKIYAP TESAKSQVIQ YTSIFRGNVV DLSPESLIVE ITGSEDKINA FIDLVKPLGI KEMARTGITA LARGPKILKP KS // ID KAD6_METJA Reviewed; 177 AA. AC Q58450; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative adenylate kinase {ECO:0000255|HAMAP-Rule:MF_00039}; DE Short=AK {ECO:0000255|HAMAP-Rule:MF_00039}; DE EC=2.7.4.3 {ECO:0000255|HAMAP-Rule:MF_00039}; DE AltName: Full=ATP-AMP transphosphorylase {ECO:0000255|HAMAP-Rule:MF_00039}; GN OrderedLocusNames=MJ1050; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase CC that catalyzes the reversible transfer of the terminal phosphate CC group between nucleoside triphosphates and monophosphates. CC {ECO:0000255|HAMAP-Rule:MF_00039}. CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. {ECO:0000255|HAMAP- CC Rule:MF_00039}. CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00039}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99053.1; -; Genomic_DNA. DR PIR; A64431; A64431. DR ProteinModelPortal; Q58450; -. DR STRING; 243232.MJ_1050; -. DR EnsemblBacteria; AAB99053; AAB99053; MJ_1050. DR KEGG; mja:MJ_1050; -. DR eggNOG; arCOG01038; Archaea. DR eggNOG; COG1936; LUCA. DR InParanoid; Q58450; -. DR KO; K18532; -. DR OMA; VDWSEVY; -. DR PhylomeDB; Q58450; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1. DR InterPro; IPR020618; Adenyl_kinase_AK6. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 177 Putative adenylate kinase. FT /FTId=PRO_0000153906. FT NP_BIND 10 15 ATP. {ECO:0000255|HAMAP-Rule:MF_00039}. FT REGION 30 53 NMPbind. {ECO:0000255|HAMAP- FT Rule:MF_00039}. FT REGION 103 113 LID. {ECO:0000255|HAMAP-Rule:MF_00039}. FT BINDING 100 100 ATP. {ECO:0000255|HAMAP-Rule:MF_00039}. FT BINDING 104 104 ATP. {ECO:0000255|HAMAP-Rule:MF_00039}. SQ SEQUENCE 177 AA; 20690 MW; F209572AA79CD2F9 CRC64; MRIAITGTPG VGKTTISKVL RDRLGIKVID ITEAVKKYKL YTEKDEDMDS YVIDFEKLEK FIDEIEEKEK TIILDGHVSH LLNPDYIIVL RCNPEIIKER LEKRGYKPKK VLENIQAEIL DVCLCESKGK VYEIDTTNRD VENIVDEIIE AIKHKKERKG VVDWTEKYFD YLTLEIK // ID IMDH_METJA Reviewed; 496 AA. AC Q59011; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 118. DE RecName: Full=Inosine-5'-monophosphate dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMP dehydrogenase {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPD {ECO:0000255|HAMAP-Rule:MF_01964}; DE Short=IMPDH {ECO:0000255|HAMAP-Rule:MF_01964}; DE EC=1.1.1.205 {ECO:0000255|HAMAP-Rule:MF_01964}; GN Name=guaB {ECO:0000255|HAMAP-Rule:MF_01964}; OrderedLocusNames=MJ1616; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of inosine 5'-phosphate (IMP) CC to xanthosine 5'-phosphate (XMP), the first committed and rate- CC limiting step in the de novo synthesis of guanine nucleotides, and CC therefore plays an important role in the regulation of cell CC growth. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- CATALYTIC ACTIVITY: Inosine 5'-phosphate + NAD(+) + H(2)O = CC xanthosine 5'-phosphate + NADH. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01964}; CC -!- ENZYME REGULATION: Mycophenolic acid (MPA) is a non-competitive CC inhibitor that prevents formation of the closed enzyme CC conformation by binding to the same site as the amobile flap. In CC contrast, mizoribine monophosphate (MZP) is a competitive CC inhibitor that induces the closed conformation. MPA is a potent CC inhibitor of mammalian IMPDHs but a poor inhibitor of the CC bacterial enzymes. MZP is a more potent inhibitor of bacterial CC IMPDH. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- PATHWAY: Purine metabolism; XMP biosynthesis via de novo pathway; CC XMP from IMP: step 1/1. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_01964}. CC -!- SIMILARITY: Belongs to the IMPDH/GMPR family. {ECO:0000255|HAMAP- CC Rule:MF_01964}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|HAMAP- CC Rule:MF_01964}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99638.1; -; Genomic_DNA. DR PIR; G64501; G64501. DR ProteinModelPortal; Q59011; -. DR SMR; Q59011; 2-493. DR STRING; 243232.MJ_1616; -. DR PRIDE; Q59011; -. DR EnsemblBacteria; AAB99638; AAB99638; MJ_1616. DR KEGG; mja:MJ_1616; -. DR eggNOG; arCOG00612; Archaea. DR eggNOG; ENOG4102TCX; Archaea. DR eggNOG; COG0516; LUCA. DR InParanoid; Q59011; -. DR KO; K00088; -. DR OMA; SSMGYCG; -. DR PhylomeDB; Q59011; -. DR UniPathway; UPA00601; UER00295. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003938; F:IMP dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006177; P:GMP biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01964; IMPDH; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR005990; IMP_DH. DR InterPro; IPR015875; IMP_DH/GMP_Rdtase_CS. DR InterPro; IPR001093; IMP_DH_GMPRt. DR PANTHER; PTHR11911:SF6; PTHR11911:SF6; 2. DR Pfam; PF00571; CBS; 2. DR Pfam; PF00478; IMPDH; 1. DR PIRSF; PIRSF000130; IMPDH; 1. DR SMART; SM00116; CBS; 2. DR TIGRFAMs; TIGR01302; IMP_dehydrog; 1. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00487; IMP_DH_GMP_RED; 1. PE 3: Inferred from homology; KW CBS domain; Complete proteome; GMP biosynthesis; Metal-binding; NAD; KW Oxidoreductase; Potassium; Purine biosynthesis; Reference proteome; KW Repeat. FT CHAIN 1 496 Inosine-5'-monophosphate dehydrogenase. FT /FTId=PRO_0000093719. FT DOMAIN 96 152 CBS 1. {ECO:0000255|HAMAP-Rule:MF_01964}. FT DOMAIN 156 212 CBS 2. {ECO:0000255|HAMAP-Rule:MF_01964}. FT NP_BIND 299 301 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}. FT REGION 339 341 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT REGION 362 363 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT REGION 386 390 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT ACT_SITE 306 306 Thioimidate intermediate. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT ACT_SITE 405 405 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01964}. FT METAL 301 301 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 303 303 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 306 306 Potassium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 477 477 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 478 478 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT METAL 479 479 Potassium; via carbonyl oxygen; shared FT with tetrameric partner. FT {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 247 247 NAD. {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 304 304 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}. FT BINDING 423 423 IMP. {ECO:0000255|HAMAP-Rule:MF_01964}. SQ SEQUENCE 496 AA; 53317 MW; C3E03FDDF3898396 CRC64; MFLKKLIEAK KAYTFDDVLL VPNASWVEPK DTDVSTDLAG LKLNIPIVSA AMDTVTEKEM AIALARLGGL GVIHRNMSIE EQVHQVQAVK KADEVVIKDV ITVSPDDTVG EAINVMETYS ISGLPVVDNE DKLVGIITHR DVKAIEDKTK KVKDVMTKDV VCAKEDVEEE EALELMYANR VERLPIVDDE NRLIGIITLR DILKRRKYPQ AARDKKGRLL VAAACGPHDF ERAKALIEAE VDAIAIDCAH AHNMRVVENV KKFKEMLEGT DIKLIVGNIA TKEAAEDLIK AGADVLKVGI GPGSICTTRV VAGVGVPQLT AVAEVADVAK EHNVPIIADG GIRYSGDIAK AIAAGADAVM LGSLLAGTDE APGQLMVING RKYKQYRGMG SLGAMTGGVG AGADRYFQAP AKSHMKHVKL VPEGVEGAVP YKGPVSEVVF QLIGGLRASM GYCGAKNLKE MQEKARFVII TPSGQVESHP HDIIITNEAP NYPLGK // ID KAE1B_METJA Reviewed; 535 AA. AC Q58530; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 127. DE RecName: Full=Probable bifunctional tRNA threonylcarbamoyladenosine biosynthesis protein {ECO:0000255|HAMAP-Rule:MF_01447}; DE Includes: DE RecName: Full=tRNA N6-adenosine threonylcarbamoyltransferase {ECO:0000255|HAMAP-Rule:MF_01447}; DE EC=2.3.1.234 {ECO:0000255|HAMAP-Rule:MF_01447}; DE AltName: Full=N6-L-threonylcarbamoyladenine synthase; DE Short=t(6)A synthase; DE AltName: Full=t(6)A37 threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01447}; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein Kae1 {ECO:0000255|HAMAP-Rule:MF_01447}; DE Includes: DE RecName: Full=Serine/threonine-protein kinase Bud32 {ECO:0000255|HAMAP-Rule:MF_01447}; DE EC=2.7.11.1 {ECO:0000255|HAMAP-Rule:MF_01447}; GN OrderedLocusNames=MJ1130; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.05 ANGSTROMS) IN COMPLEX WITH AN ATP ANALOG. RX PubMed=19172740; DOI=10.1038/emboj.2008.157; RA Hecker A., Lopreiato R., Graille M., Collinet B., Forterre P., RA Libri D., van Tilbeurgh H.; RT "Structure of the archaeal Kae1/Bud32 fusion protein MJ1130: a model RT for the eukaryotic EKC/KEOPS subcomplex."; RL EMBO J. 27:2340-2351(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.67 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM AND RP CGI121, FUNCTION, SUBUNIT, AND ENZYME REGULATION. RX PubMed=18951093; DOI=10.1016/j.molcel.2008.10.002; RA Mao D.Y., Neculai D., Downey M., Orlicky S., Haffani Y.Z., RA Ceccarelli D.F., Ho J.S., Szilard R.K., Zhang W., Ho C.S., Wan L., RA Fares C., Rumpel S., Kurinov I., Arrowsmith C.H., Durocher D., RA Sicheri F.; RT "Atomic structure of the KEOPS complex: an ancient protein kinase- RT containing molecular machine."; RL Mol. Cell 32:259-275(2008). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Is a component of the KEOPS complex that CC is probably involved in the transfer of the threonylcarbamoyl CC moiety of threonylcarbamoyl-AMP (TC-AMP) to the N6 group of A37. CC The Kae1 domain likely plays a direct catalytic role in this CC reaction (By similarity). The Bud32 domain probably displays CC kinase activity that regulates Kae1 function. In vitro, exhibits CC low ATPase activity, but does not bind DNA and does not have CC endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01447, CC ECO:0000269|PubMed:18951093}. CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC {ECO:0000255|HAMAP-Rule:MF_01447}. CC -!- CATALYTIC ACTIVITY: L-threonylcarbamoyladenylate + adenine(37) in CC tRNA = AMP + N(6)-L-threonylcarbamoyladenine(37) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01447}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01447}; CC Note=Binds 1 Fe(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01447}; CC -!- ENZYME REGULATION: Activity provided by the Kae1 region seems to CC be regulated via phosphorylation by the protein kinase Bud32, CC which is itself activated by Cgi121. CC {ECO:0000269|PubMed:18951093}. CC -!- SUBUNIT: Component of the KEOPS complex that consists of Kae1, CC Bud32, Cgi121 and Pcc1; the whole complex dimerizes. CC {ECO:0000255|HAMAP-Rule:MF_01447, ECO:0000269|PubMed:18951093, CC ECO:0000269|PubMed:19172740}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01447}. CC -!- SIMILARITY: In the N-terminal section; belongs to the KAE1 / TsaD CC family. {ECO:0000255|HAMAP-Rule:MF_01447}. CC -!- SIMILARITY: In the C-terminal section; belongs to the protein CC kinase superfamily. Tyr protein kinase family. BUD32 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01447}. CC -!- SIMILARITY: Contains 1 protein kinase domain. {ECO:0000255|HAMAP- CC Rule:MF_01447}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99132.1; -; Genomic_DNA. DR PDB; 2VWB; X-ray; 3.05 A; A/B=1-535. DR PDB; 3EN9; X-ray; 2.67 A; A/B=1-535. DR PDB; 3ENH; X-ray; 3.60 A; A/B=1-535. DR PDBsum; 2VWB; -. DR PDBsum; 3EN9; -. DR PDBsum; 3ENH; -. DR ProteinModelPortal; Q58530; -. DR STRING; 243232.MJ_1130; -. DR EnsemblBacteria; AAB99132; AAB99132; MJ_1130. DR KEGG; mja:MJ_1130; -. DR eggNOG; arCOG01183; Archaea. DR eggNOG; arCOG01185; Archaea. DR eggNOG; COG0533; LUCA. DR eggNOG; COG3642; LUCA. DR InParanoid; Q58530; -. DR KO; K15904; -. DR OMA; GETMDTG; -. DR PhylomeDB; Q58530; -. DR EvolutionaryTrace; Q58530; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR GO; GO:0061711; F:N(6)-L-threonylcarbamoyladenine synthase; IEA:UniProtKB-EC. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR GO; GO:0004712; F:protein serine/threonine/tyrosine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR HAMAP; MF_01446; Kae1_arch; 1. DR HAMAP; MF_01447; Kae1_Bud32_arch; 1. DR InterPro; IPR022495; Bud32. DR InterPro; IPR000905; Gcp-like_dom. DR InterPro; IPR022449; Kae1. DR InterPro; IPR017861; KAE1/TsaD. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR017860; Peptidase_M22_CS. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR009220; tRNA_threonyl_synthase/kinase. DR InterPro; IPR008266; Tyr_kinase_AS. DR Pfam; PF00814; Peptidase_M22; 1. DR PIRSF; PIRSF036401; Gcp_STYKS; 1. DR PRINTS; PR00789; OSIALOPTASE. DR SUPFAM; SSF56112; SSF56112; 1. DR TIGRFAMs; TIGR03724; arch_bud32; 1. DR TIGRFAMs; TIGR03722; arch_KAE1; 1. DR TIGRFAMs; TIGR00329; gcp_kae1; 1. DR PROSITE; PS01016; GLYCOPROTEASE; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS00109; PROTEIN_KINASE_TYR; 1. PE 1: Evidence at protein level; KW 3D-structure; Acyltransferase; ATP-binding; Complete proteome; KW Cytoplasm; Iron; Kinase; Metal-binding; Multifunctional enzyme; KW Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase; tRNA processing. FT CHAIN 1 535 Probable bifunctional tRNA FT threonylcarbamoyladenosine biosynthesis FT protein. FT /FTId=PRO_0000096979. FT DOMAIN 333 535 Protein kinase. {ECO:0000255|HAMAP- FT Rule:MF_01447}. FT NP_BIND 339 347 ATP. {ECO:0000255|HAMAP-Rule:MF_01447}. FT REGION 1 323 Kae1. FT REGION 127 131 Threonylcarbamoyl-AMP binding. FT {ECO:0000305}. FT ACT_SITE 451 451 Proton acceptor; for kinase activity. FT {ECO:0000255|HAMAP-Rule:MF_01447}. FT METAL 106 106 Iron. {ECO:0000305}. FT METAL 110 110 Iron. {ECO:0000305}. FT METAL 127 127 Iron. {ECO:0000305}. FT METAL 284 284 Iron. {ECO:0000305}. FT BINDING 159 159 Threonylcarbamoyl-AMP. {ECO:0000305}. FT BINDING 172 172 Threonylcarbamoyl-AMP; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01447}. FT BINDING 176 176 Threonylcarbamoyl-AMP. {ECO:0000305}. FT BINDING 256 256 Threonylcarbamoyl-AMP. {ECO:0000305}. FT BINDING 360 360 ATP. {ECO:0000255|HAMAP-Rule:MF_01447}. FT STRAND 2 7 {ECO:0000244|PDB:3EN9}. FT STRAND 9 19 {ECO:0000244|PDB:3EN9}. FT STRAND 24 31 {ECO:0000244|PDB:3EN9}. FT STRAND 37 40 {ECO:0000244|PDB:3EN9}. FT HELIX 44 62 {ECO:0000244|PDB:3EN9}. FT HELIX 65 67 {ECO:0000244|PDB:3EN9}. FT STRAND 70 78 {ECO:0000244|PDB:3EN9}. FT HELIX 80 97 {ECO:0000244|PDB:3EN9}. FT STRAND 101 105 {ECO:0000244|PDB:3EN9}. FT HELIX 106 117 {ECO:0000244|PDB:3EN9}. FT STRAND 124 128 {ECO:0000244|PDB:3EN9}. FT STRAND 133 139 {ECO:0000244|PDB:3EN9}. FT STRAND 142 152 {ECO:0000244|PDB:3EN9}. FT HELIX 154 164 {ECO:0000244|PDB:3EN9}. FT HELIX 172 180 {ECO:0000244|PDB:3EN9}. FT HELIX 200 211 {ECO:0000244|PDB:3EN9}. FT HELIX 216 242 {ECO:0000244|PDB:3EN9}. FT STRAND 245 251 {ECO:0000244|PDB:3EN9}. FT HELIX 252 255 {ECO:0000244|PDB:3EN9}. FT HELIX 257 269 {ECO:0000244|PDB:3EN9}. FT STRAND 273 275 {ECO:0000244|PDB:3EN9}. FT HELIX 279 282 {ECO:0000244|PDB:3EN9}. FT HELIX 286 298 {ECO:0000244|PDB:3EN9}. FT HELIX 305 307 {ECO:0000244|PDB:3EN9}. FT STRAND 345 351 {ECO:0000244|PDB:3EN9}. FT STRAND 356 362 {ECO:0000244|PDB:3EN9}. FT HELIX 370 390 {ECO:0000244|PDB:3EN9}. FT HELIX 391 394 {ECO:0000244|PDB:3EN9}. FT STRAND 401 405 {ECO:0000244|PDB:3EN9}. FT TURN 406 409 {ECO:0000244|PDB:3EN9}. FT STRAND 410 414 {ECO:0000244|PDB:3EN9}. FT STRAND 418 420 {ECO:0000244|PDB:3EN9}. FT HELIX 421 424 {ECO:0000244|PDB:3EN9}. FT HELIX 430 444 {ECO:0000244|PDB:3EN9}. FT STRAND 456 465 {ECO:0000244|PDB:3EN9}. FT HELIX 477 494 {ECO:0000244|PDB:3EN9}. FT HELIX 496 498 {ECO:0000244|PDB:3EN9}. FT HELIX 499 513 {ECO:0000244|PDB:3EN9}. FT HELIX 517 528 {ECO:0000244|PDB:3EN9}. SQ SEQUENCE 535 AA; 60570 MW; B18EEFACE8E5A99F CRC64; MICLGLEGTA EKTGVGIVTS DGEVLFNKTI MYKPPKQGIN PREAADHHAE TFPKLIKEAF EVVDKNEIDL IAFSQGPGLG PSLRVTATVA RTLSLTLKKP IIGVNHCIAH IEIGKLTTEA EDPLTLYVSG GNTQVIAYVS KKYRVFGETL DIAVGNCLDQ FARYVNLPHP GGPYIEELAR KGKKLVDLPY TVKGMDIAFS GLLTAAMRAY DAGERLEDIC YSLQEYAFSM LTEITERALA HTNKGEVMLV GGVAANNRLR EMLKAMCEGQ NVDFYVPPKE FCGDNGAMIA WLGLLMHKNG RWMSLDETKI IPNYRTDMVE VNWIKEIKGK KRKIPEHLIG KGAEADIKRD SYLDFDVIIK ERVKKGYRDE RLDENIRKSR TAREARYLAL VKDFGIPAPY IFDVDLDNKR IMMSYINGKL AKDVIEDNLD IAYKIGEIVG KLHKNDVIHN DLTTSNFIFD KDLYIIDFGL GKISNLDEDK AVDLIVFKKA VLSTHHEKFD EIWERFLEGY KSVYDRWEII LELMKDVERR ARYVE // ID KADA_METJA Reviewed; 192 AA. AC P43409; DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 2. DT 11-NOV-2015, entry version 89. DE RecName: Full=Adenylate kinase; DE Short=AK; DE EC=2.7.4.3; DE AltName: Full=ATP-AMP transphosphorylase; GN Name=adkA; Synonyms=adk; OrderedLocusNames=MJ0479; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9055821; DOI=10.1016/S0378-1119(96)00651-8; RA Ferber D.M., Haney P.J., Berk H., Lynn D., Konisky J.; RT "The adenylate kinase genes of M. voltae, M. thermolithotrophicus, M. RT jannaschii, and M. igneus define a new family of adenylate kinases."; RL Gene 185:239-244(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [3] RP PROTEIN SEQUENCE OF 1-30. RX PubMed=7768791; RA Rusnak P., Haney P., Konisky J.; RT "The adenylate kinases from a mesophilic and three thermophilic RT methanogenic members of the Archaea."; RL J. Bacteriol. 177:2977-2981(1995). CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Active from 70 to 90 degrees Celsius.; CC -!- SUBUNIT: Monomer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the archaeal adenylate kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98470.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U39882; AAC44863.1; -; Genomic_DNA. DR EMBL; L77117; AAB98470.1; ALT_INIT; Genomic_DNA. DR PIR; G64359; G64359. DR ProteinModelPortal; P43409; -. DR SMR; P43409; 2-192. DR STRING; 243232.MJ_0479; -. DR EnsemblBacteria; AAB98470; AAB98470; MJ_0479. DR KEGG; mja:MJ_0479; -. DR eggNOG; arCOG01039; Archaea. DR eggNOG; COG2019; LUCA. DR InParanoid; P43409; -. DR KO; K00939; -. DR OMA; HRDEMRK; -. DR PhylomeDB; P43409; -. DR BRENDA; 2.7.4.3; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004017; F:adenylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00234; Adenylate_kinase_AdkA; 1. DR InterPro; IPR023477; Adenylate_kinase_AdkA. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; KW Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 192 Adenylate kinase. FT /FTId=PRO_0000131814. FT NP_BIND 10 18 ATP. {ECO:0000250}. FT CONFLICT 16 16 S -> G (in Ref. 3; AA sequence). FT {ECO:0000305}. SQ SEQUENCE 192 AA; 21772 MW; ECD533AD4C85D99E CRC64; MKNKVVVIVG VPGVGSTTVT NKAIEELKKE GIEYKIVNFG TVMFEIAKEE GLVEHRDQLR KLPPEEQKRI QKLAGKKIAE MAKEFNIVVD THSTIKTPKG YLPGLPAWVL EELNPDIIVL VEAENDEILM RRLKDETRQR DFESTEDIGE HIFMNRCAAM TYAVLTGATV KIIKNRDFLL DKAVQELIEV LK // ID KCY_METJA Reviewed; 178 AA. AC Q58071; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Cytidylate kinase; DE Short=CK; DE EC=2.7.4.25; DE AltName: Full=Cytidine monophosphate kinase; DE Short=CMP kinase; GN Name=cmk; OrderedLocusNames=MJ0656; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + (d)CMP = ADP + (d)CDP. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the cytidylate kinase family. Type 2 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98651.1; -; Genomic_DNA. DR PIR; H64381; H64381. DR ProteinModelPortal; Q58071; -. DR STRING; 243232.MJ_0656; -. DR EnsemblBacteria; AAB98651; AAB98651; MJ_0656. DR KEGG; mja:MJ_0656; -. DR eggNOG; arCOG01037; Archaea. DR eggNOG; COG1102; LUCA. DR InParanoid; Q58071; -. DR KO; K00945; -. DR OMA; YTPLEFN; -. DR PhylomeDB; Q58071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004127; F:cytidylate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006220; P:pyrimidine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00239; Cytidyl_kinase_type2; 1. DR InterPro; IPR026865; Cmk2-like. DR InterPro; IPR011892; Cyt_kin_arch. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13189; Cytidylate_kin2; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02173; cyt_kin_arch; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 178 Cytidylate kinase. FT /FTId=PRO_0000132013. FT NP_BIND 7 15 ATP. {ECO:0000250}. SQ SEQUENCE 178 AA; 20495 MW; FEC3D475FD8CB7DD CRC64; MIITIGGLPG TGTTTIAKMI AEKYNLRHVC AGFIFREMAK EMGMDLQEFS KYAEQHKEID EEIDRRQVEI AKQGNVVLEG RLAAWMLLKN GIKPDLTIWF KAPLEVRAER ISKRENIDKD VALKKMIERE ASEKKRYKEI YNIDLDDLSI YDLVIDTSKW DVEGVFNIVS SAIDNLKK // ID K6PF_METJA Reviewed; 462 AA. AC Q58999; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Bifunctional ADP-specific glucokinase/phosphofructokinase; DE EC=2.7.1.146; DE EC=2.7.1.147; DE AltName: Full=ADP-GK; DE AltName: Full=ADP-GK/PFK; DE AltName: Full=ADP-Pfk; DE AltName: Full=ADP-dependent glucokinase; DE AltName: Full=ADP-dependent phosphofructokinase; GN Name=pfkC; Synonyms=glkA; OrderedLocusNames=MJ1604; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=11717273; DOI=10.1128/JB.183.24.7145-7153.2001; RA Verhees C.H., Tuininga J.E., Kengen S.W.M., Stams A.J.M., RA van der Oost J., de Vos W.M.; RT "ADP-dependent phosphofructokinases in mesophilic and thermophilic RT methanogenic archaea."; RL J. Bacteriol. 183:7145-7153(2001). RN [3] RP CHARACTERIZATION, AND ENZYME KINETICS. RX PubMed=11856730; DOI=10.1074/jbc.C200059200; RA Sakuraba H., Yoshioka I., Koga S., Takahashi M., Kitahama Y., RA Satomura T., Kawakami R., Ohshima T.; RT "ADP-dependent glucokinase/phosphofructokinase, a novel bifunctional RT enzyme from the hyperthermophilic archaeon Methanococcus jannaschii."; RL J. Biol. Chem. 277:12495-12498(2002). CC -!- FUNCTION: Catalyzes the phosphorylation of fructose 6-phosphate CC and D-glucose to fructose 1,6-bisphosphate and D-glucose 6- CC phosphate, respectively, using ADP as the phosphate donor. CC -!- CATALYTIC ACTIVITY: ADP + D-glucose = AMP + D-glucose 6-phosphate. CC -!- CATALYTIC ACTIVITY: ADP + D-fructose 6-phosphate = AMP + D- CC fructose 1,6-bisphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.6 mM for D-glucose; CC KM=0.032 mM for ADP with D-glucose as phosphoryl group acceptor; CC KM=9.6 uM for fructose 6-phosphate; CC KM=0.49 mM for ADP with D-fructose 6-phosphate as phosphoryl CC group acceptor; CC Vmax=11.2 umol/min/mg enzyme toward fructose 6-phosphate; CC Vmax=9.59 umol/min/mg enzyme toward ADP; CC pH dependence: CC Optimum pH is 6.5.; CC -!- PATHWAY: Carbohydrate degradation; glycolysis. CC -!- SUBUNIT: Monomer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkC family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ADPK (ADP-dependent kinase) domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99627.1; -; Genomic_DNA. DR PIR; C64500; C64500. DR ProteinModelPortal; Q58999; -. DR STRING; 243232.MJ_1604; -. DR EnsemblBacteria; AAB99627; AAB99627; MJ_1604. DR KEGG; mja:MJ_1604; -. DR eggNOG; arCOG03371; Archaea. DR eggNOG; COG4809; LUCA. DR InParanoid; Q58999; -. DR KO; K00918; -. DR OMA; HLEFASI; -. DR PhylomeDB; Q58999; -. DR BRENDA; 2.7.1.146; 3260. DR UniPathway; UPA00109; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC. DR GO; GO:0043844; F:ADP-specific phosphofructokinase activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008443; F:phosphofructokinase activity; IEA:InterPro. DR GO; GO:0006000; P:fructose metabolic process; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1190.20; -; 1. DR HAMAP; MF_00561; ADP_PFKinase; 1. DR InterPro; IPR007666; ADP_PFK/GK. DR InterPro; IPR015990; ADP_PFK/GK_arc. DR InterPro; IPR011790; ADP_PFK_arc. DR InterPro; IPR029056; Ribokinase-like. DR PANTHER; PTHR21208; PTHR21208; 2. DR Pfam; PF04587; ADP_PFK_GK; 1. DR PIRSF; PIRSF015883; ADP-Pfk_glckin; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR TIGRFAMs; TIGR02045; P_fruct_ADP; 1. DR PROSITE; PS51255; ADPK; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Glycolysis; Kinase; Magnesium; KW Metal-binding; Multifunctional enzyme; Reference proteome; KW Transferase. FT CHAIN 1 462 Bifunctional ADP-specific FT glucokinase/phosphofructokinase. FT /FTId=PRO_0000184764. FT DOMAIN 1 458 ADPK. FT ACT_SITE 442 442 Proton acceptor. {ECO:0000250}. FT METAL 272 272 Magnesium. {ECO:0000250}. FT METAL 302 302 Magnesium. {ECO:0000250}. FT METAL 442 442 Magnesium. {ECO:0000250}. SQ SEQUENCE 462 AA; 53362 MW; D91088B60DBAB104 CRC64; MCDIMEIKKF IETIKGTKLF TAYNTNVDAI KYLKDEDVQK LVDEFNHKDI IERMEEYPRI IEEPLDFVAR LVHSIKTGKP AEVPIKDDKK LHEWFDRIKY DEERMGGQAG IVSNLMATLQ IDKIIVYTPF LSKKQAEMFV DYDNLLYPLV ENGNLVLKKV REAYRDDPIK INRIFEFKKG LKFKLNGEEI TAKQSTRFIV ASRPEALRIE IKDDVRKFLP KIGEAVDCAF LSGYQAIKEE YRDGKTAKYY FERAEEDIKL LKKNKNIKTH LEFASISNIE IRKMVVDYIL SNVESVGMDE TEIANVLHIL GYDELSNNIL KDSFIEDVIE GAKILLDKFK NLEVVQVHTI YYILFVCRAD NPLSKEELEE CLEFSTILAS TKAKLGNIRA IDDLHEGLKI PHNKYGDLLK EIAEKFNDNN YKIALSPSRY VEKPKSTVGL GDTISSGAFV YYVSLLNKKR MS // ID KPRS_METJA Reviewed; 284 AA. AC Q58761; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 25-OCT-2002, sequence version 2. DT 11-NOV-2015, entry version 99. DE RecName: Full=Ribose-phosphate pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921}; DE Short=RPPK {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921}; DE EC=2.7.6.1 {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000269|PubMed:16288921}; DE AltName: Full=5-phospho-D-ribosyl alpha-1-diphosphate {ECO:0000255|HAMAP-Rule:MF_00583}; DE AltName: Full=Phosphoribosyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921}; DE AltName: Full=Phosphoribosyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921}; DE Short=P-Rib-PP synthase {ECO:0000255|HAMAP-Rule:MF_00583}; DE Short=PRPP synthase {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000303|PubMed:16288921}; DE Short=PRPPase {ECO:0000255|HAMAP-Rule:MF_00583}; GN Name=prs {ECO:0000255|HAMAP-Rule:MF_00583, GN ECO:0000303|PubMed:16288921}; OrderedLocusNames=MJ1366; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH SUBSTRATES, RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, RP SUBSTRATE SPECIFICITY, ENZYME REGULATION, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=16288921; DOI=10.1016/j.jmb.2005.10.001; RA Kadziola A., Jepsen C.H., Johansson E., McGuire J., Larsen S., RA Hove-Jensen B.; RT "Novel class III phosphoribosyl diphosphate synthase: structure and RT properties of the tetrameric, phosphate-activated, non-allosterically RT inhibited enzyme from Methanocaldococcus jannaschii."; RL J. Mol. Biol. 354:815-828(2005). CC -!- FUNCTION: Involved in the biosynthesis of ribose 1,5-bisphosphate. CC Catalyzes the transfer of pyrophosphoryl group from ATP to ribose- CC 5-phosphate to yield phosphoribosyl diphosphate (PRPP) and AMP. It CC can also use dATP as diphosphoryl donor. {ECO:0000255|HAMAP- CC Rule:MF_00583, ECO:0000269|PubMed:16288921}. CC -!- CATALYTIC ACTIVITY: ATP + D-ribose 5-phosphate = AMP + 5-phospho- CC alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP-Rule:MF_00583, CC ECO:0000269|PubMed:16288921}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00583, CC ECO:0000269|PubMed:16288921}; CC Note=Binds 1 Mg(2+) ion per subunit. Mn(2+) is also accepted, but CC the activity is less than 15% of that obtained with Mg(2+), when CC assayed at pH 9.5. {ECO:0000255|HAMAP-Rule:MF_00583, CC ECO:0000269|PubMed:16288921}; CC -!- ENZYME REGULATION: Activated by phosphate ion. Maximal activity is CC obtained at 190 mM, with a fairly flat activity profile around CC this concentration. Further increase in phosphate ion CC concentration inhibited the activity of the enzyme. Thus, at 250 CC mM the activity is 80% of maximal activity. Inhibited by CC alpha,beta-methylene ATP and ADP. {ECO:0000269|PubMed:16288921}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=2.6 mM for ATP (at pH 9 and 85 degrees Celsius) CC {ECO:0000269|PubMed:16288921}; CC KM=2.8 mM for ribose 5-phosphate (at pH 9 and 85 degrees CC Celsius) {ECO:0000269|PubMed:16288921}; CC Vmax=2.2 mmol/min/mg enzyme (at pH 9 and 85 degrees Celsius) CC {ECO:0000269|PubMed:16288921}; CC pH dependence: CC Optimum pH is 9.5. The activity declines strongly above pH 10. CC {ECO:0000269|PubMed:16288921}; CC Temperature dependence: CC Optimum temperature is 85 degrees Celsius. 70% of maximal CC activity at 72 and 95 degrees Celsius. CC {ECO:0000269|PubMed:16288921}; CC -!- PATHWAY: Metabolic intermediate biosynthesis; 5-phospho-alpha-D- CC ribose 1-diphosphate biosynthesis; 5-phospho-alpha-D-ribose 1- CC diphosphate from D-ribose 5-phosphate (route I): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00583, ECO:0000305|PubMed:16288921}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16288921}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- MISCELLANEOUS: M.jannaschii PRPP synthase is more compact than the CC PRPP synthase in the B. subtilis subunit. This is mainly due to CC truncations of eight residues at the N terminus, 14 residues at CC the C terminus and to a seven-residue shorter loop. CC {ECO:0000305|PubMed:16288921}. CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase CC family. {ECO:0000255|HAMAP-Rule:MF_00583}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99374.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99374.1; ALT_INIT; Genomic_DNA. DR PIR; E64470; E64470. DR PDB; 1U9Y; X-ray; 2.65 A; A/B/C/D=1-284. DR PDB; 1U9Z; X-ray; 2.80 A; A/B/C/D=1-284. DR PDBsum; 1U9Y; -. DR PDBsum; 1U9Z; -. DR ProteinModelPortal; Q58761; -. DR SMR; Q58761; 1-284. DR STRING; 243232.MJ_1366; -. DR EnsemblBacteria; AAB99374; AAB99374; MJ_1366. DR KEGG; mja:MJ_1366; -. DR eggNOG; arCOG00067; Archaea. DR eggNOG; COG0462; LUCA. DR InParanoid; Q58761; -. DR KO; K00948; -. DR OMA; GHPVSAR; -. DR PhylomeDB; Q58761; -. DR BRENDA; 2.7.6.1; 3260. DR UniPathway; UPA00087; UER00172. DR EvolutionaryTrace; Q58761; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006015; P:5-phosphoribose 1-diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.2020; -; 2. DR HAMAP; MF_00583_A; RibP_PPkinase_A; 1. DR InterPro; IPR029099; Pribosyltran_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005946; Rib-P_diPkinase. DR Pfam; PF00156; Pribosyltran; 1. DR Pfam; PF13793; Pribosyltran_N; 1. DR SUPFAM; SSF53271; SSF53271; 2. DR TIGRFAMs; TIGR01251; ribP_PPkin; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Kinase; KW Magnesium; Manganese; Metal-binding; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 284 Ribose-phosphate pyrophosphokinase. FT /FTId=PRO_0000141238. FT NP_BIND 34 36 ATP. {ECO:0000255|HAMAP-Rule:MF_00583, FT ECO:0000269|PubMed:16288921}. FT NP_BIND 92 95 ATP. {ECO:0000269|PubMed:16288921}. FT REGION 186 188 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583}. FT REGION 212 220 Ribose-5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00583, FT ECO:0000269|PubMed:16288921}. FT METAL 123 123 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT METAL 125 125 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00583}. FT BINDING 93 93 ATP. {ECO:0000255|HAMAP-Rule:MF_00583, FT ECO:0000269|PubMed:16288921}. FT BINDING 125 125 ATP. {ECO:0000255|HAMAP-Rule:MF_00583, FT ECO:0000269|PubMed:16288921}. FT BINDING 163 163 Ribose-5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_00583, FT ECO:0000269|PubMed:16288921}. FT STRAND 2 5 {ECO:0000244|PDB:1U9Y}. FT HELIX 7 9 {ECO:0000244|PDB:1U9Z}. FT HELIX 10 19 {ECO:0000244|PDB:1U9Y}. FT STRAND 27 31 {ECO:0000244|PDB:1U9Y}. FT STRAND 37 41 {ECO:0000244|PDB:1U9Y}. FT STRAND 47 53 {ECO:0000244|PDB:1U9Y}. FT HELIX 59 74 {ECO:0000244|PDB:1U9Y}. FT TURN 75 77 {ECO:0000244|PDB:1U9Y}. FT STRAND 80 84 {ECO:0000244|PDB:1U9Y}. FT TURN 89 92 {ECO:0000244|PDB:1U9Z}. FT HELIX 104 115 {ECO:0000244|PDB:1U9Y}. FT STRAND 117 123 {ECO:0000244|PDB:1U9Y}. FT HELIX 127 132 {ECO:0000244|PDB:1U9Y}. FT STRAND 137 140 {ECO:0000244|PDB:1U9Y}. FT HELIX 143 150 {ECO:0000244|PDB:1U9Y}. FT TURN 151 153 {ECO:0000244|PDB:1U9Y}. FT STRAND 158 163 {ECO:0000244|PDB:1U9Y}. FT HELIX 164 166 {ECO:0000244|PDB:1U9Y}. FT HELIX 167 177 {ECO:0000244|PDB:1U9Y}. FT STRAND 181 184 {ECO:0000244|PDB:1U9Y}. FT STRAND 198 200 {ECO:0000244|PDB:1U9Y}. FT STRAND 208 214 {ECO:0000244|PDB:1U9Y}. FT STRAND 216 218 {ECO:0000244|PDB:1U9Y}. FT HELIX 219 230 {ECO:0000244|PDB:1U9Y}. FT STRAND 235 242 {ECO:0000244|PDB:1U9Y}. FT HELIX 249 256 {ECO:0000244|PDB:1U9Y}. FT STRAND 259 264 {ECO:0000244|PDB:1U9Y}. FT STRAND 272 274 {ECO:0000244|PDB:1U9Y}. FT HELIX 277 281 {ECO:0000244|PDB:1U9Y}. SQ SEQUENCE 284 AA; 31395 MW; 9EAE9805785B1127 CRC64; MIVVSGSQSQ NLAFKVAKLL NTKLTRVEYK RFPDNEIYVR IVDEINDDEA VIINTQKNQN DAIVETILLC DALRDEGVKK ITLVAPYLAY ARQDKKFNPG EAISIRALAK IYSNIVDKLI TINPHETHIK DFFTIPFIYG DAVPKLAEYV KDKLNDPIVL APDKGALEFA KTASKILNAE YDYLEKTRLS PTEIQIAPKT LDAKDRDVFI VDDIISTGGT MATAVKLLKE QGAKKIIAAC VHPVLIGDAL NKLYSAGVEE VVGTDTYLSE VSKVSVAEVI VDLL // ID KHSE_METJA Reviewed; 296 AA. AC Q58504; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-NOV-2015, entry version 117. DE RecName: Full=Homoserine kinase; DE Short=HK; DE Short=HSK; DE EC=2.7.1.39; GN Name=thrB; OrderedLocusNames=MJ1104; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS). RX PubMed=11188689; DOI=10.1016/S0969-2126(00)00533-5; RA Zhou T., Daugherty M., Grishin N.V., Osterman A.L., Zhang H.; RT "Structure and mechanism of homoserine kinase: prototype for the GHMP RT kinase superfamily."; RL Structure 8:1247-1257(2000). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of L- CC homoserine to L-homoserine phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + L-homoserine = ADP + O-phospho-L- CC homoserine. CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 4/5. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Homoserine kinase CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99107.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99107.1; ALT_INIT; Genomic_DNA. DR PIR; G64437; G64437. DR PDB; 1FWK; X-ray; 2.10 A; A/B/C/D=1-296. DR PDB; 1FWL; X-ray; 2.25 A; A/B/C/D=1-296. DR PDB; 1H72; X-ray; 1.80 A; C=1-296. DR PDB; 1H73; X-ray; 2.00 A; A=1-296. DR PDB; 1H74; X-ray; 1.90 A; A/B/C/D=1-296. DR PDBsum; 1FWK; -. DR PDBsum; 1FWL; -. DR PDBsum; 1H72; -. DR PDBsum; 1H73; -. DR PDBsum; 1H74; -. DR ProteinModelPortal; Q58504; -. DR SMR; Q58504; 1-296. DR STRING; 243232.MJ_1104; -. DR EnsemblBacteria; AAB99107; AAB99107; MJ_1104. DR KEGG; mja:MJ_1104; -. DR eggNOG; arCOG01027; Archaea. DR eggNOG; COG0083; LUCA. DR InParanoid; Q58504; -. DR KO; K00872; -. DR OMA; VVEPCRA; -. DR PhylomeDB; Q58504; -. DR BioCyc; MetaCyc:MONOMER-14633; -. DR BRENDA; 2.7.1.39; 3260. DR SABIO-RK; Q58504; -. DR UniPathway; UPA00050; UER00064. DR EvolutionaryTrace; Q58504; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004413; F:homoserine kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00384; Homoser_kinase; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR000870; Homoserine_kinase. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF000676; Homoser_kin; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00191; thrB; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; ATP-binding; Complete proteome; KW Cytoplasm; Kinase; Nucleotide-binding; Reference proteome; KW Threonine biosynthesis; Transferase. FT CHAIN 1 296 Homoserine kinase. FT /FTId=PRO_0000156641. FT NP_BIND 86 96 ATP. {ECO:0000255}. FT STRAND 2 12 {ECO:0000244|PDB:1H72}. FT HELIX 15 17 {ECO:0000244|PDB:1H72}. FT TURN 18 20 {ECO:0000244|PDB:1H72}. FT STRAND 21 47 {ECO:0000244|PDB:1H72}. FT TURN 55 57 {ECO:0000244|PDB:1H72}. FT HELIX 59 70 {ECO:0000244|PDB:1H72}. FT STRAND 76 82 {ECO:0000244|PDB:1H72}. FT STRAND 89 91 {ECO:0000244|PDB:1H72}. FT HELIX 93 108 {ECO:0000244|PDB:1H72}. FT HELIX 115 130 {ECO:0000244|PDB:1H72}. FT HELIX 138 143 {ECO:0000244|PDB:1H72}. FT STRAND 145 151 {ECO:0000244|PDB:1H72}. FT TURN 152 155 {ECO:0000244|PDB:1H72}. FT STRAND 156 160 {ECO:0000244|PDB:1H72}. FT STRAND 168 171 {ECO:0000244|PDB:1H72}. FT HELIX 179 184 {ECO:0000244|PDB:1H72}. FT STRAND 188 191 {ECO:0000244|PDB:1H74}. FT HELIX 192 210 {ECO:0000244|PDB:1H72}. FT HELIX 214 221 {ECO:0000244|PDB:1H72}. FT HELIX 228 232 {ECO:0000244|PDB:1H72}. FT HELIX 238 245 {ECO:0000244|PDB:1H72}. FT HELIX 246 248 {ECO:0000244|PDB:1H72}. FT STRAND 249 254 {ECO:0000244|PDB:1H72}. FT STRAND 261 265 {ECO:0000244|PDB:1H72}. FT HELIX 267 269 {ECO:0000244|PDB:1H72}. FT HELIX 270 280 {ECO:0000244|PDB:1H72}. FT STRAND 284 287 {ECO:0000244|PDB:1H72}. FT STRAND 293 295 {ECO:0000244|PDB:1H74}. SQ SEQUENCE 296 AA; 32259 MW; 49919E68F3834C78 CRC64; MKVRVKAPCT SANLGVGFDV FGLCLKEPYD VIEVEAIDDK EIIIEVDDKN IPTDPDKNVA GIVAKKMIDD FNIGKGVKIT IKKGVKAGSG LGSSAASSAG TAYAINELFK LNLDKLKLVD YASYGELASS GAKHADNVAP AIFGGFTMVT NYEPLEVLHI PIDFKLDILI AIPNISINTK EAREILPKAV GLKDLVNNVG KACGMVYALY NKDKSLFGRY MMSDKVIEPV RGKLIPNYFK IKEEVKDKVY GITISGSGPS IIAFPKEEFI DEVENILRDY YENTIRTEVG KGVEVV // ID KORB_METJA Reviewed; 270 AA. AC Q57957; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=2-oxoglutarate synthase subunit KorB; DE EC=1.2.7.3; DE AltName: Full=2-ketoglutarate oxidoreductase beta chain; DE Short=KOR; DE AltName: Full=2-oxoglutarate-ferredoxin oxidoreductase subunit beta; GN Name=korB; OrderedLocusNames=MJ0537; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = CC succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of the KorA, KorB, KorC and KorD subunits. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98531.1; -; Genomic_DNA. DR PIR; A64367; A64367. DR ProteinModelPortal; Q57957; -. DR STRING; 243232.MJ_0537; -. DR EnsemblBacteria; AAB98531; AAB98531; MJ_0537. DR KEGG; mja:MJ_0537; -. DR eggNOG; arCOG01599; Archaea. DR eggNOG; COG1013; LUCA. DR InParanoid; Q57957; -. DR KO; K00175; -. DR OMA; FNNNIYG; -. DR PhylomeDB; Q57957; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. PE 4: Predicted; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 270 2-oxoglutarate synthase subunit KorB. FT /FTId=PRO_0000099942. SQ SEQUENCE 270 AA; 29895 MW; 4F7331CF37216554 CRC64; MHPALKYMRQ DRLPHIFCSG CGNGIVMNCF LKAIEELNIK PEDYIAVSGI GCSSRVPGYL YCDSLHTTHG RPIAFATGIK IARPDKHVVV FTGDGDLAAI GGNHFIHGCR RNIDLTVICI NNNIYGMTGG QVSPTTPYGK KATTAPYGSI ENTMDLCKMA IAAGATYVAR WTTAHPIQLV RSIKKGIQKK GFAFIEVVSQ CPTYYGRFNI SRKPADMIKF LKENSIHLNK AKDMSEEELN GKIVVGEFLD IEKPEFVEEL HKLIEKLKSE // ID KPYK_METJA Reviewed; 447 AA. AC Q57572; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Pyruvate kinase; DE Short=PK; DE EC=2.7.1.40; GN OrderedLocusNames=MJ0108; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + pyruvate = ADP + phosphoenolpyruvate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 5/5. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the pyruvate kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98090.1; -; Genomic_DNA. DR PIR; D64313; D64313. DR ProteinModelPortal; Q57572; -. DR STRING; 243232.MJ_0108; -. DR PRIDE; Q57572; -. DR EnsemblBacteria; AAB98090; AAB98090; MJ_0108. DR KEGG; mja:MJ_0108; -. DR eggNOG; arCOG04120; Archaea. DR eggNOG; COG0469; LUCA. DR InParanoid; Q57572; -. DR KO; K00873; -. DR OMA; GHFILIN; -. DR PhylomeDB; Q57572; -. DR UniPathway; UPA00109; UER00188. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:UniProtKB-EC. DR Gene3D; 2.40.33.10; -; 1. DR Gene3D; 3.20.20.60; -; 2. DR Gene3D; 3.40.1380.20; -; 1. DR InterPro; IPR001697; Pyr_Knase. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR InterPro; IPR011037; Pyrv_Knase-like_insert_dom. DR InterPro; IPR015794; Pyrv_Knase_a/b. DR InterPro; IPR018209; Pyrv_Knase_AS. DR InterPro; IPR015793; Pyrv_Knase_brl. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR015806; Pyrv_Knase_insert_dom. DR PANTHER; PTHR11817; PTHR11817; 1. DR Pfam; PF00224; PK; 1. DR Pfam; PF02887; PK_C; 1. DR PRINTS; PR01050; PYRUVTKNASE. DR SUPFAM; SSF50800; SSF50800; 1. DR SUPFAM; SSF51621; SSF51621; 2. DR SUPFAM; SSF52935; SSF52935; 1. DR TIGRFAMs; TIGR01064; pyruv_kin; 1. DR PROSITE; PS00110; PYRUVATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glycolysis; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Potassium; Pyruvate; KW Reference proteome; Transferase. FT CHAIN 1 447 Pyruvate kinase. FT /FTId=PRO_0000112128. FT METAL 35 35 Potassium. {ECO:0000250}. FT METAL 37 37 Potassium. {ECO:0000250}. FT METAL 61 61 Potassium. {ECO:0000250}. FT METAL 203 203 Magnesium. {ECO:0000250}. FT METAL 227 227 Magnesium. {ECO:0000250}. FT BINDING 33 33 Substrate. {ECO:0000250}. FT BINDING 226 226 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 227 227 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 259 259 Substrate. {ECO:0000250}. FT SITE 201 201 Transition state stabilizer. FT {ECO:0000250}. SQ SEQUENCE 447 AA; 50490 MW; EA6C4DC031B8C1A4 CRC64; MVGMMRKTKI LVTLGPSLEN KLDKAINLID GVRFNMSHAT TDYCEKFLNI LEKNNIAKVM DLKGIKIRIK EVKLKNKILK MGEKVVIGED IKLNYNIDTI EEGHFILIND GKIKLRVVEK TDKIIAVVEV GGEIKEGMGV NLPDTRIELP IIDETDLKNI KFAVEKDFEY IALSFVRNKE DVKELKDIIS EYKGDCEVIS KIETKEGLKN IKEIARESDG VMVARGDLGV EVPIENIPIE QKNILRIANR YGILSITATQ ILDSMINNPF PTRAEVTDIA NAIYDGTDCL MLSNETTIGK YPIEAIKVLN KVAKVADEHY EEFGDRVCLE VESIDEGLVY AVYELYKKLN TKLVITPTYS GRTAKLISKL RINSKIIAPT PNIRTLKRLR LVWGVESCLM EEFDDMEKII NTCREMAKKE IGKGIYLITL GHPIGQKKTN TIKVESI // ID KORC_METJA Reviewed; 187 AA. AC Q57956; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=2-oxoglutarate synthase subunit KorC; DE EC=1.2.7.3; DE AltName: Full=2-ketoglutarate oxidoreductase gamma chain; DE Short=KOR; DE AltName: Full=2-oxoglutarate-ferredoxin oxidoreductase subunit gamma; GN Name=korC; OrderedLocusNames=MJ0536; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = CC succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of the KorA, KorB, KorC and KorD subunits. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98530.1; -; Genomic_DNA. DR PIR; H64366; H64366. DR ProteinModelPortal; Q57956; -. DR STRING; 243232.MJ_0536; -. DR EnsemblBacteria; AAB98530; AAB98530; MJ_0536. DR KEGG; mja:MJ_0536; -. DR eggNOG; arCOG01602; Archaea. DR eggNOG; COG1014; LUCA. DR InParanoid; Q57956; -. DR KO; K00177; -. DR OMA; IDYPKVQ; -. DR PhylomeDB; Q57956; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.920.10; -; 1. DR InterPro; IPR011894; PorC_KorC. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat. DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen. DR Pfam; PF01558; POR; 1. DR SUPFAM; SSF53323; SSF53323; 1. DR TIGRFAMs; TIGR02175; PorC_KorC; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 187 2-oxoglutarate synthase subunit KorC. FT /FTId=PRO_0000099946. SQ SEQUENCE 187 AA; 20548 MW; 4B0687CBDE6B0536 CRC64; MNKRRVKMRK EIRLSGFGGQ GIILAGVILG RAAALYDNKE AVQTQSYGPE ARGGASKSEV VISDEPIDFP KVIKPDILVC LSQQAYDKYK DDIKEGGVVL VDEDLVSTDK MPEVDVTMYK IPFTRIASEE IKLPIVANIV MLGALTRLTN IVSKESMEKA ILDSVPKGTE EKNLLAFSKG YEVAKEL // ID KORA_METJA Reviewed; 366 AA. AC Q57724; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=2-oxoglutarate synthase subunit KorA; DE EC=1.2.7.3; DE AltName: Full=2-ketoglutarate oxidoreductase alpha chain; DE Short=KOR; DE AltName: Full=2-oxoglutarate-ferredoxin oxidoreductase subunit alpha; GN Name=korA; OrderedLocusNames=MJ0276; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2-oxoglutarate + CoA + 2 oxidized ferredoxin = CC succinyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of the KorA, KorB, KorC and KorD subunits. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98264.1; -; Genomic_DNA. DR PIR; E64334; E64334. DR ProteinModelPortal; Q57724; -. DR STRING; 243232.MJ_0276; -. DR EnsemblBacteria; AAB98264; AAB98264; MJ_0276. DR KEGG; mja:MJ_0276; -. DR eggNOG; arCOG01607; Archaea. DR eggNOG; COG0674; LUCA. DR InParanoid; Q57724; -. DR KO; K00174; -. DR OMA; QEMYDFT; -. DR PhylomeDB; Q57724; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047553; F:2-oxoglutarate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 366 2-oxoglutarate synthase subunit KorA. FT /FTId=PRO_0000099938. SQ SEQUENCE 366 AA; 41060 MW; 7C5E41EAD9EB6E78 CRC64; MKVEFMQGNQ ACAKGAIKAG CRFFAGYPIT PSTEIAEAMA RELPKVGGYY IQMEDEIGSI AAVIGASWGG LKAMTATSGP GFSLMQENIG FAYMTETPCV VVDIQRGGPS TGQPTMASQG DMMQCRWGSH GDYEVIALAP SSVQEMYDFT IMAFNYAEKY RIPVFVMADE IVGHMREKVI LHDNIEIINR KKPEEKPCKK PYPFDKLIPE MPVFGEGYNV HITGLTHDER GYPDVSPETH DKLVRRIVNK IRKNKDEIIK WEGENLDAEI VFVCYGSPSR TVKHAVRNLR EKGLDVGYIR LITVYPFPDD LLKKLKAKKV VVPEMNLGQI YYEVERVCKK AEEVILVDKI GGELHRPEEL ERAVLG // ID LADH_METJA Reviewed; 463 AA. AC Q58806; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 97. DE RecName: Full=Lactaldehyde dehydrogenase; DE EC=1.2.1.22; GN OrderedLocusNames=MJ1411; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION IN F420 BIOSYNTHESIS, CATALYTIC ACTIVITY, SUBUNIT, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16585745; DOI=10.1128/JB.188.8.2836-2844.2006; RA Grochowski L.L., Xu H., White R.H.; RT "Identification of lactaldehyde dehydrogenase in Methanocaldococcus RT jannaschii and its involvement in production of lactate for F420 RT biosynthesis."; RL J. Bacteriol. 188:2836-2844(2006). CC -!- FUNCTION: Involved in F420 biosynthesis through the oxidation of CC lactaldehyde to lactate. The substrate preference order is CC propionaldehyde > DL-lactaldehyde, DL-glyceraldehyde > CC crotonaldehyde > glycolaldehyde > acetaldehyde, acrolein > CC formaldehyde. No activity was observed towards methylglyoxal or CC glyceraldehyde-3-phosphate. Has a preference for NAD over NADP. CC {ECO:0000269|PubMed:16585745}. CC -!- CATALYTIC ACTIVITY: (S)-lactaldehyde + NAD(+) + H(2)O = (S)- CC lactate + NADH. {ECO:0000269|PubMed:16585745}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=284 uM for propionaldehyde (at pH 7.5) CC {ECO:0000269|PubMed:16585745}; CC KM=302 uM for DL-lactaldehyde (at pH 7.5) CC {ECO:0000269|PubMed:16585745}; CC Vmax=1.12 umol/min/mg enzyme with propionaldehyde as substrate CC (at pH 7.5) {ECO:0000269|PubMed:16585745}; CC Vmax=0.6 umol/min/mg enzyme with DL-lactaldehyde as substrate CC (at pH 7.5) {ECO:0000269|PubMed:16585745}; CC Note=As the lactaldehyde used was a mixture of D and L isomers, CC the kinetic parameters do not reflect the possible CC stereospecificity of the enzyme.; CC pH dependence: CC Optimum pH is 9. The activity remained constant to pH 10.0. CC Below pH 9, the activity gradually declined, and the enzyme was CC inactive at pH 6 or below. {ECO:0000269|PubMed:16585745}; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme F420 biosynthesis. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16585745}. CC -!- SIMILARITY: Belongs to the aldehyde dehydrogenase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99418.1; -; Genomic_DNA. DR PIR; B64476; B64476. DR PDB; 3PQA; X-ray; 1.50 A; A/B/C/D=1-463. DR PDB; 3RHD; X-ray; 2.20 A; A/B/C/D=1-463. DR PDBsum; 3PQA; -. DR PDBsum; 3RHD; -. DR ProteinModelPortal; Q58806; -. DR STRING; 243232.MJ_1411; -. DR EnsemblBacteria; AAB99418; AAB99418; MJ_1411. DR KEGG; mja:MJ_1411; -. DR eggNOG; arCOG01252; Archaea. DR eggNOG; COG1012; LUCA. DR InParanoid; Q58806; -. DR KO; K19266; -. DR OMA; KVNMISF; -. DR PhylomeDB; Q58806; -. DR BioCyc; MetaCyc:MONOMER-12177; -. DR BRENDA; 1.2.1.22; 3260. DR SABIO-RK; Q58806; -. DR UniPathway; UPA00071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008911; F:lactaldehyde dehydrogenase activity; IDA:MENGO. DR Gene3D; 3.40.309.10; -; 1. DR Gene3D; 3.40.605.10; -; 1. DR InterPro; IPR016161; Ald_DH/histidinol_DH. DR InterPro; IPR016163; Ald_DH_C. DR InterPro; IPR016162; Ald_DH_N. DR InterPro; IPR015590; Aldehyde_DH_dom. DR Pfam; PF00171; Aldedh; 1. DR SUPFAM; SSF53720; SSF53720; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; NAD; Oxidoreductase; KW Reference proteome. FT CHAIN 1 463 Lactaldehyde dehydrogenase. FT /FTId=PRO_0000056600. FT NP_BIND 220 225 NAD. {ECO:0000250}. FT ACT_SITE 240 240 {ECO:0000250}. FT ACT_SITE 274 274 {ECO:0000250}. FT STRAND 13 16 {ECO:0000244|PDB:3PQA}. FT TURN 18 20 {ECO:0000244|PDB:3PQA}. FT STRAND 23 27 {ECO:0000244|PDB:3PQA}. FT HELIX 32 44 {ECO:0000244|PDB:3PQA}. FT HELIX 46 50 {ECO:0000244|PDB:3PQA}. FT HELIX 54 70 {ECO:0000244|PDB:3PQA}. FT HELIX 72 83 {ECO:0000244|PDB:3PQA}. FT HELIX 87 110 {ECO:0000244|PDB:3PQA}. FT STRAND 113 116 {ECO:0000244|PDB:3PQA}. FT STRAND 121 129 {ECO:0000244|PDB:3PQA}. FT STRAND 131 137 {ECO:0000244|PDB:3PQA}. FT STRAND 139 141 {ECO:0000244|PDB:3PQA}. FT HELIX 142 155 {ECO:0000244|PDB:3PQA}. FT STRAND 159 164 {ECO:0000244|PDB:3PQA}. FT HELIX 170 185 {ECO:0000244|PDB:3PQA}. FT HELIX 190 192 {ECO:0000244|PDB:3PQA}. FT STRAND 193 195 {ECO:0000244|PDB:3PQA}. FT TURN 200 202 {ECO:0000244|PDB:3PQA}. FT HELIX 203 209 {ECO:0000244|PDB:3PQA}. FT STRAND 215 220 {ECO:0000244|PDB:3PQA}. FT HELIX 222 231 {ECO:0000244|PDB:3PQA}. FT STRAND 234 240 {ECO:0000244|PDB:3PQA}. FT STRAND 245 249 {ECO:0000244|PDB:3PQA}. FT HELIX 255 267 {ECO:0000244|PDB:3PQA}. FT HELIX 268 271 {ECO:0000244|PDB:3PQA}. FT STRAND 276 283 {ECO:0000244|PDB:3PQA}. FT HELIX 284 286 {ECO:0000244|PDB:3PQA}. FT HELIX 287 299 {ECO:0000244|PDB:3PQA}. FT HELIX 319 334 {ECO:0000244|PDB:3PQA}. FT STRAND 338 341 {ECO:0000244|PDB:3PQA}. FT STRAND 353 356 {ECO:0000244|PDB:3PQA}. FT HELIX 362 364 {ECO:0000244|PDB:3PQA}. FT STRAND 370 378 {ECO:0000244|PDB:3PQA}. FT HELIX 380 387 {ECO:0000244|PDB:3PQA}. FT STRAND 394 399 {ECO:0000244|PDB:3PQA}. FT HELIX 403 412 {ECO:0000244|PDB:3PQA}. FT STRAND 415 422 {ECO:0000244|PDB:3PQA}. FT HELIX 437 439 {ECO:0000244|PDB:3PQA}. FT STRAND 440 442 {ECO:0000244|PDB:3PQA}. FT HELIX 446 452 {ECO:0000244|PDB:3PQA}. FT STRAND 454 462 {ECO:0000244|PDB:3PQA}. SQ SEQUENCE 463 AA; 51136 MW; 46F265686595B6A5 CRC64; MFIDGKWINR EDMDVINPYS LEVIKKIPAL SREEAKEAID TAEKYKEVMK NLPITKRYNI LMNIAKQIKE KKEELAKILA IDAGKPIKQA RVEVERSIGT FKLAAFYVKE HRDEVIPSDD RLIFTRREPV GIVGAITPFN FPLNLSAHKI APAIATGNVI VHHPSSKAPL VCIELAKIIE NALKKYNVPL GVYNLLTGAG EVVGDEIVVN EKVNMISFTG SSKVGELITK KAGFKKIALE LGGVNPNIVL KDADLNKAVN ALIKGSFIYA GQVCISVGMI LVDESIADKF IEMFVNKAKV LNVGNPLDEK TDVGPLISVE HAEWVEKVVE KAIDEGGKLL LGGKRDKALF YPTILEVDRD NILCKTETFA PVIPIIRTNE EEMIDIANST EYGLHSAIFT NDINKSLKFA ENLEFGGVVI NDSSLFRQDN MPFGGVKKSG LGREGVKYAM EEMSNIKTII ISK // ID LEUC_METJA Reviewed; 424 AA. AC P81291; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Isopropylmalate/citramalate isomerase large subunit; DE EC=4.2.1.33 {ECO:0000255|HAMAP-Rule:MF_01027}; DE EC=4.2.1.35; DE AltName: Full=(R)-2-methylmalate dehydratase; DE AltName: Full=(R)-citramalate dehydratase; DE AltName: Full=3-isopropylmalate dehydratase; DE AltName: Full=Alpha-isopropylmalate dehydratase; DE AltName: Full=Citraconate hydratase; DE AltName: Full=Isopropylmalate isomerase {ECO:0000255|HAMAP-Rule:MF_01027}; DE Short=IPMI {ECO:0000255|HAMAP-Rule:MF_01027}; DE AltName: Full=Maleate hydratase; DE Short=Malease; DE EC=4.2.1.31; GN Name=leuC {ECO:0000255|HAMAP-Rule:MF_01027}; OrderedLocusNames=MJ0499; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17449626; DOI=10.1128/JB.00166-07; RA Drevland R.M., Waheed A., Graham D.E.; RT "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in RT Methanocaldococcus jannaschii."; RL J. Bacteriol. 189:4391-4400(2007). CC -!- FUNCTION: Enzyme with broad specificity that catalyzes reversible CC hydroxyacid isomerizations via dehydration/hydration reactions. CC Catalyzes the isomerization between 2-isopropylmalate and 3- CC isopropylmalate, via the formation of 2-isopropylmaleate, a step CC involved in leucine biosynthesis. Catalyzes the isomerization CC between 2-methylmalate and 3-methylmalate, via the formation of 2- CC methylmaleate (citraconate), a step involved in isoleucine CC biosynthesis. Also displays malease activity, i.e. catalyzes the CC hydration of maleate to form (R)-malate. CC {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000255|HAMAP-Rule:MF_01027, CC ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (R)-2-methylmalate = 2-methylmaleate + H(2)O. CC {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: 2-methylmaleate + H(2)O = (2R,3S)-3- CC methylmalate. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (R)-malate = maleate + H(2)O. CC {ECO:0000269|PubMed:17449626}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01027, CC ECO:0000269|PubMed:17449626}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01027, ECO:0000269|PubMed:17449626}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=80 uM for 2-methylmaleate {ECO:0000269|PubMed:17449626}; CC KM=810 uM for (R)-2-methylmalate {ECO:0000269|PubMed:17449626}; CC KM=1900 uM for racemic 2-isopropylmalate CC {ECO:0000269|PubMed:17449626}; CC KM=39 uM for racemic 3-isopropylmalate CC {ECO:0000269|PubMed:17449626}; CC KM=400 uM for maleate {ECO:0000269|PubMed:17449626}; CC Vmax=15 umol/min/mg enzyme for 2-methylmaleate hydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=1.5 umol/min/mg enzyme for (R)-2-methylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=4.2 umol/min/mg enzyme for 2-isopropylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=1.8 umol/min/mg enzyme for 3-isopropylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=34 umol/min/mg enzyme for maleate hydration reaction CC {ECO:0000269|PubMed:17449626}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:17449626}; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:17449626}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC {ECO:0000255|HAMAP-Rule:MF_01027}. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 2/3. CC -!- SUBUNIT: Heterotetramer of 2 LeuC and 2 LeuD. Can not form a CC complex with HacB. {ECO:0000269|PubMed:17449626}. CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family. LeuC CC type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01027}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98487.1; -; Genomic_DNA. DR PIR; C64362; C64362. DR PDB; 4KP1; X-ray; 1.80 A; A=1-424. DR PDB; 4NQY; X-ray; 2.60 A; A/B=1-424. DR PDBsum; 4KP1; -. DR PDBsum; 4NQY; -. DR ProteinModelPortal; P81291; -. DR STRING; 243232.MJ_0499; -. DR DNASU; 1451361; -. DR EnsemblBacteria; AAB98487; AAB98487; MJ_0499. DR KEGG; mja:MJ_0499; -. DR eggNOG; arCOG01698; Archaea. DR eggNOG; COG0065; LUCA. DR InParanoid; P81291; -. DR KO; K01703; -. DR OMA; KIEPQVA; -. DR PhylomeDB; P81291; -. DR BioCyc; MetaCyc:MONOMER-13647; -. DR BRENDA; 4.2.1.33; 3260. DR SABIO-RK; P81291; -. DR UniPathway; UPA00047; UER00067. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047508; F:(R)-2-methylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0050075; F:maleate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.499.10; -; 2. DR Gene3D; 3.40.1060.10; -; 1. DR HAMAP; MF_01027; LeuC_type2; 1. DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba. DR InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2. DR InterPro; IPR018136; Aconitase_4Fe-4S_BS. DR InterPro; IPR011826; HAcnase/IPMdehydase_lsu_prok. DR InterPro; IPR006251; Homoacnase/IPMdehydase_lsu. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00330; Aconitase; 1. DR PRINTS; PR00415; ACONITASE. DR SUPFAM; SSF53732; SSF53732; 1. DR TIGRFAMs; TIGR01343; hacA_fam; 1. DR TIGRFAMs; TIGR02086; IPMI_arch; 1. DR PROSITE; PS00450; ACONITASE_1; 1. DR PROSITE; PS01244; ACONITASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; Iron; KW Iron-sulfur; Isoleucine biosynthesis; Leucine biosynthesis; Lyase; KW Metal-binding; Reference proteome. FT CHAIN 1 424 Isopropylmalate/citramalate isomerase FT large subunit. FT /FTId=PRO_0000076869. FT METAL 304 304 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 365 365 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT METAL 368 368 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01027}. FT HELIX 5 14 {ECO:0000244|PDB:4KP1}. FT STRAND 24 28 {ECO:0000244|PDB:4KP1}. FT STRAND 30 35 {ECO:0000244|PDB:4KP1}. FT HELIX 38 48 {ECO:0000244|PDB:4KP1}. FT STRAND 59 63 {ECO:0000244|PDB:4KP1}. FT HELIX 73 89 {ECO:0000244|PDB:4KP1}. FT STRAND 93 95 {ECO:0000244|PDB:4KP1}. FT HELIX 97 99 {ECO:0000244|PDB:4NQY}. FT HELIX 102 108 {ECO:0000244|PDB:4KP1}. FT STRAND 117 122 {ECO:0000244|PDB:4KP1}. FT HELIX 125 131 {ECO:0000244|PDB:4KP1}. FT STRAND 134 137 {ECO:0000244|PDB:4KP1}. FT HELIX 140 149 {ECO:0000244|PDB:4KP1}. FT STRAND 150 155 {ECO:0000244|PDB:4KP1}. FT STRAND 159 166 {ECO:0000244|PDB:4KP1}. FT HELIX 174 185 {ECO:0000244|PDB:4KP1}. FT TURN 187 190 {ECO:0000244|PDB:4KP1}. FT STRAND 194 199 {ECO:0000244|PDB:4KP1}. FT HELIX 200 204 {ECO:0000244|PDB:4KP1}. FT HELIX 207 215 {ECO:0000244|PDB:4KP1}. FT HELIX 216 220 {ECO:0000244|PDB:4KP1}. FT STRAND 222 226 {ECO:0000244|PDB:4KP1}. FT HELIX 231 244 {ECO:0000244|PDB:4KP1}. FT STRAND 262 268 {ECO:0000244|PDB:4KP1}. FT HELIX 269 271 {ECO:0000244|PDB:4KP1}. FT STRAND 275 277 {ECO:0000244|PDB:4KP1}. FT STRAND 285 287 {ECO:0000244|PDB:4KP1}. FT HELIX 288 291 {ECO:0000244|PDB:4KP1}. FT STRAND 297 302 {ECO:0000244|PDB:4KP1}. FT STRAND 304 306 {ECO:0000244|PDB:4NQY}. FT HELIX 309 321 {ECO:0000244|PDB:4KP1}. FT STRAND 330 333 {ECO:0000244|PDB:4KP1}. FT HELIX 338 346 {ECO:0000244|PDB:4KP1}. FT HELIX 349 355 {ECO:0000244|PDB:4KP1}. FT HELIX 365 369 {ECO:0000244|PDB:4KP1}. FT STRAND 381 384 {ECO:0000244|PDB:4KP1}. FT STRAND 393 395 {ECO:0000244|PDB:4NQY}. FT STRAND 396 398 {ECO:0000244|PDB:4KP1}. FT STRAND 400 403 {ECO:0000244|PDB:4KP1}. FT HELIX 406 415 {ECO:0000244|PDB:4KP1}. FT HELIX 421 423 {ECO:0000244|PDB:4KP1}. SQ SEQUENCE 424 AA; 46107 MW; B4D106AE165C524C CRC64; MGMTIVEKIL AKASGKKEVS PGDIVMANID VAMVHDITGP LTVNTLKEYG IEKVWNPEKI VILFDHQVPA DSIKAAENHI LMRKFVKEQG IKYFYDIREG VCHQVLPEKG HVAPGEVVVG ADSHTCTHGA FGAFATGIGS TDMAHVFATG KLWFKVPETI YFNITGDLQP YVTSKDVILS IIGEVGVDGA TYKACQFGGE TVKKMSIASR MTMTNMAIEM GGKTGIIEPD EKTIQYVKEA MKKHGTERPF EVIKGDEDAE FAEVYEIEAD KIEPVFACPH NVDNVKQARE VAGKPIDQVF IGSCTNGRLE DLRMAIKIIE KHGGIADDVR VVVTPASREE YLKALKEGII EKFLKYGCVV TNPSCSACMG SLYGVLGPGE VCVSTSNRNF RGRQGSLEAE IYLASPITAA ACAVKGELVD PRDL // ID KTHY_METJA Reviewed; 188 AA. AC Q57741; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Probable thymidylate kinase; DE EC=2.7.4.9; DE AltName: Full=dTMP kinase; GN Name=tmk; OrderedLocusNames=MJ0293; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + dTMP = ADP + dTDP. CC -!- SIMILARITY: Belongs to the thymidylate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98278.1; -; Genomic_DNA. DR PIR; F64336; F64336. DR ProteinModelPortal; Q57741; -. DR STRING; 243232.MJ_0293; -. DR EnsemblBacteria; AAB98278; AAB98278; MJ_0293. DR KEGG; mja:MJ_0293; -. DR eggNOG; arCOG01891; Archaea. DR eggNOG; COG0125; LUCA. DR InParanoid; Q57741; -. DR KO; K00943; -. DR OMA; YVYSSIV; -. DR PhylomeDB; Q57741; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004798; F:thymidylate kinase activity; IBA:GO_Central. DR GO; GO:0009041; F:uridylate kinase activity; IBA:GO_Central. DR GO; GO:0006233; P:dTDP biosynthetic process; IBA:GO_Central. DR GO; GO:0006235; P:dTTP biosynthetic process; IBA:GO_Central. DR GO; GO:0006227; P:dUDP biosynthetic process; IBA:GO_Central. DR GO; GO:0046939; P:nucleotide phosphorylation; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00165; Thymidylate_kinase; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR018095; Thymidylate_kin_CS. DR InterPro; IPR018094; Thymidylate_kinase. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00041; DTMP_kinase; 1. DR PROSITE; PS01331; THYMIDYLATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 188 Probable thymidylate kinase. FT /FTId=PRO_0000155386. FT NP_BIND 11 18 ATP. {ECO:0000255}. SQ SEQUENCE 188 AA; 21687 MW; A7EC8A9B17F08585 CRC64; MVDNMFIVFE GIDGSGKTTQ SKLLAKKMDA FWTYEPSNSL VGKIIREILS GKTEVDNKTL ALLFAADRIE HTKLIKEELK KRDVVCDRYL YSSIAYQSVA GVDENFIKSI NRYALKPDIV FLLIVDIETA LKRVKTKDIF EKKDFLKKVQ DKYLELAEEY NFIVIDTTKK SVEEVHNEII GYLKNIPH // ID LEU3_METJA Reviewed; 333 AA. AC Q58130; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 112. DE RecName: Full=3-isopropylmalate/3-methylmalate dehydrogenase; DE EC=1.1.1.85; DE EC=1.1.1.n5; DE AltName: Full=3-isopropylmalate dehydrogenase; DE Short=3-IPM-DH; DE Short=IMDH; DE Short=IPMDH; DE AltName: Full=Beta-IPM dehydrogenase; DE AltName: Full=D-malate dehydrogenase [decarboxylating]; DE EC=1.1.1.83; GN Name=leuB; OrderedLocusNames=MJ0720; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=10940051; DOI=10.1128/JB.182.17.5013-5016.2000; RA Howell D.M., Graupner M., Xu H., White R.H.; RT "Identification of enzymes homologous to isocitrate dehydrogenase that RT are involved in coenzyme B and leucine biosynthesis in RT methanoarchaea."; RL J. Bacteriol. 182:5013-5016(2000). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, KINETIC RP PARAMETERS, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17449626; DOI=10.1128/JB.00166-07; RA Drevland R.M., Waheed A., Graham D.E.; RT "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in RT Methanocaldococcus jannaschii."; RL J. Bacteriol. 189:4391-4400(2007). CC -!- FUNCTION: Catalyzes the oxidation of 3-carboxy-2-hydroxy-4- CC methylpentanoate (3-isopropylmalate) to 3-carboxy-4-methyl-2- CC oxopentanoate, which decarboxylates to 4-methyl-2-oxopentanoate CC (2-oxoisocaproate). Also catalyzes the oxidative decarboxylation CC of 3-methylmalate to 2-oxobutyrate, and that of D-malate to CC pyruvate. Can not use NADP(+) instead of NAD(+). Can not catalyze CC the oxidation of L-malate, L-tartrate, D-tartrate, DL-isocitrate, CC or DL-lactate. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate + NAD(+) = 4-methyl- CC 2-oxopentanoate + CO(2) + NADH. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-methylmalate + NAD(+) = 2- CC oxobutanoate + CO(2) + NADH. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (R)-malate + NAD(+) = pyruvate + CO(2) + NADH. CC {ECO:0000269|PubMed:17449626}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=24 uM for 3-isopropylmalate {ECO:0000269|PubMed:17449626}; CC KM=410 uM for D-malate {ECO:0000269|PubMed:17449626}; CC Temperature dependence: CC Loses 50% of its activity after heating at 80 degrees Celsius CC for 10 min.; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 3/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 3/3. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:17449626}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the isocitrate and isopropylmalate CC dehydrogenases family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98716.1; -; Genomic_DNA. DR ProteinModelPortal; Q58130; -. DR SMR; Q58130; 2-332. DR STRING; 243232.MJ_0720; -. DR EnsemblBacteria; AAB98716; AAB98716; MJ_0720. DR KEGG; mja:MJ_0720; -. DR eggNOG; arCOG01163; Archaea. DR eggNOG; COG0473; LUCA. DR InParanoid; Q58130; -. DR KO; K00052; -. DR OMA; LGARRWH; -. DR PhylomeDB; Q58130; -. DR BioCyc; MetaCyc:MONOMER-13649; -. DR SABIO-RK; Q58130; -. DR UniPathway; UPA00047; UER00069. DR UniPathway; UPA00048; UER00072. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003862; F:3-isopropylmalate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046553; F:D-malate dehydrogenase (decarboxylating) activity; IEA:UniProtKB-EC. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0019298; P:coenzyme B biosynthetic process; IDA:MENGO. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.718.10; -; 1. DR InterPro; IPR019818; IsoCit/isopropylmalate_DH_CS. DR InterPro; IPR001804; Isocitrate/isopropylmalate_DH. DR InterPro; IPR024084; IsoPropMal-DH-like_dom. DR InterPro; IPR011828; LEU3_arc. DR PANTHER; PTHR11835; PTHR11835; 1. DR Pfam; PF00180; Iso_dh; 1. DR SMART; SM01329; Iso_dh; 1. DR TIGRFAMs; TIGR02088; LEU3_arch; 1. DR PROSITE; PS00470; IDH_IMDH; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Cytoplasm; Isoleucine biosynthesis; KW Leucine biosynthesis; Magnesium; Manganese; Metal-binding; NAD; KW Oxidoreductase; Reference proteome. FT CHAIN 1 333 3-isopropylmalate/3-methylmalate FT dehydrogenase. FT /FTId=PRO_0000083809. FT NP_BIND 260 272 NAD. {ECO:0000250}. FT METAL 203 203 Magnesium or manganese. {ECO:0000250}. FT METAL 227 227 Magnesium or manganese. {ECO:0000250}. FT METAL 231 231 Magnesium or manganese. {ECO:0000250}. FT BINDING 81 81 Substrate. {ECO:0000250}. FT BINDING 91 91 Substrate. {ECO:0000250}. FT BINDING 112 112 Substrate. {ECO:0000250}. FT BINDING 203 203 Substrate. {ECO:0000250}. FT SITE 119 119 Important for catalysis. {ECO:0000250}. FT SITE 170 170 Important for catalysis. {ECO:0000250}. SQ SEQUENCE 333 AA; 36330 MW; 0618F119A4E682F0 CRC64; MHKICVIEGD GIGKEVVPAT IQVLEATGLP FEFVYAEAGD EVYKRTGKAL PEETIETALD CDAVLFGAAG ETAADVIVKL RHILDTYANI RPVKAYKGVK CLRPDIDYVI VRENTEGLYK GIEAEIDEGI TIATRVITEK ACERIFRFAF NLARERKKMG KEGKVTCAHK ANVLKLTDGL FKKIFYKVAE EYDDIKAEDY YIDAMNMYII TKPQVFDVVV TSNLFGDILS DGAAGTVGGL GLAPSANIGD EHGLFEPVHG SAPDIAGKKI ANPTATILSA VLMLRYLGEY EAADKVEKAL EEVLALGLTT PDLGGNLNTF EMAEEVAKRV REE // ID LIVM_METJA Reviewed; 345 AA. AC Q58666; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Probable branched-chain amino acid transport permease protein LivM; GN Name=livM; OrderedLocusNames=MJ1270; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for branched-chain amino acids. Probably responsible for the CC translocation of the substrates across the membrane (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. LivHM subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99276.1; -; Genomic_DNA. DR PIR; E64458; E64458. DR ProteinModelPortal; Q58666; -. DR STRING; 243232.MJ_1270; -. DR EnsemblBacteria; AAB99276; AAB99276; MJ_1270. DR KEGG; mja:MJ_1270; -. DR eggNOG; arCOG01273; Archaea. DR eggNOG; COG4177; LUCA. DR InParanoid; Q58666; -. DR KO; K01998; -. DR OMA; WTFFPFL; -. DR PhylomeDB; Q58666; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IBA:GOC. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 345 Probable branched-chain amino acid FT transport permease protein LivM. FT /FTId=PRO_0000060065. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 222 242 Helical. {ECO:0000255}. FT TRANSMEM 269 289 Helical. {ECO:0000255}. FT TRANSMEM 297 317 Helical. {ECO:0000255}. SQ SEQUENCE 345 AA; 37937 MW; 7771476C39F6FB51 CRC64; MSIDLISMIL LWFGLYYIVS LSLNMEFGYA GIPNFGKALS VLVGAIAVGG ILDRLLMLYF GIGGDFITGT TYATSAINNL IASNPIVGIG ILILAIILAS ILGFVVGAIF ILPSAKLKED YLGITLLAIS EAVLLICTYN LNIIGGYYGI STPDILAFVS GEYRGWVFAW IVLFIAFLVY LFFERLLNTP FGRVLRAMRE NENTVKAFGR DIMKLRIKTM AIGSAIGAIA GVLYSLYTVN IIANAFTRVD WTFFPFLMVL LGGKGNNKGV ALGVLCYVIV KVLLDIYKYN IKYALGIPFE PVWLSYMLFG VLMLLILYYK PSGLIPEKPI ITPPMKKKIM EISGK // ID LEMA_METJA Reviewed; 189 AA. AC Q58971; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Protein LemA; GN Name=lemA; OrderedLocusNames=MJ1576; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the LemA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99598.1; -; Genomic_DNA. DR PIR; G64496; G64496. DR ProteinModelPortal; Q58971; -. DR STRING; 243232.MJ_1576; -. DR EnsemblBacteria; AAB99598; AAB99598; MJ_1576. DR KEGG; mja:MJ_1576; -. DR eggNOG; arCOG04574; Archaea. DR eggNOG; COG1704; LUCA. DR InParanoid; Q58971; -. DR KO; K03744; -. DR OMA; HRYTYNN; -. DR PhylomeDB; Q58971; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 1.20.1440.20; -; 1. DR InterPro; IPR007156; LemA. DR InterPro; IPR023353; LemA-like_dom. DR Pfam; PF04011; LemA; 1. DR SUPFAM; SSF140478; SSF140478; 1. PE 3: Inferred from homology; KW Cell membrane; Coiled coil; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 189 Protein LemA. FT /FTId=PRO_0000107422. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT COILED 87 150 {ECO:0000255}. SQ SEQUENCE 189 AA; 21824 MW; C937C05CE0DBAC9D CRC64; MLMLLLIIVG LILALIVLGI VIYIVSIYNR FQTLKNGAEA TLGQIRVALK KRLDMINQLV EAVKSYASFE KETLTKITEL RSSVLKANTA EEIQNIERES RNILGNILVA VENYPELKTS ETVKELMDAI KEIEDEIARH RYTYNNIVQE FNTKIDTFPS NIVANLFGFR KMDYLQFEEE IYERPKISF // ID LEU1_METJA Reviewed; 518 AA. AC Q58595; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=2-isopropylmalate synthase; DE EC=2.3.3.13; DE AltName: Full=Alpha-IPM synthase; DE AltName: Full=Alpha-isopropylmalate synthase; GN Name=leuA; OrderedLocusNames=MJ1195; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=9665716; DOI=10.1021/bi980662p; RA Howell D.M., Harich K., Xu H., White R.H.; RT "Alpha-keto acid chain elongation reactions involved in the RT biosynthesis of coenzyme B (7-mercaptoheptanoyl threonine phosphate) RT in methanogenic Archaea."; RL Biochemistry 37:10108-10117(1998). CC -!- FUNCTION: Catalyzes the condensation of the acetyl group of CC acetyl-CoA with 3-methyl-2-oxobutanoate (2-oxoisovalerate) to form CC 3-carboxy-3-hydroxy-4-methylpentanoate (2-isopropylmalate). CC {ECO:0000269|PubMed:9665716}. CC -!- CATALYTIC ACTIVITY: Acetyl-CoA + 3-methyl-2-oxobutanoate + H(2)O = CC (2S)-2-isopropylmalate + CoA. {ECO:0000269|PubMed:9665716}. CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 1/4. CC {ECO:0000269|PubMed:9665716}. CC -!- SIMILARITY: Belongs to the alpha-IPM synthase/homocitrate synthase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99199.1; -; Genomic_DNA. DR PIR; B64449; B64449. DR ProteinModelPortal; Q58595; -. DR STRING; 243232.MJ_1195; -. DR EnsemblBacteria; AAB99199; AAB99199; MJ_1195. DR KEGG; mja:MJ_1195; -. DR eggNOG; arCOG02092; Archaea. DR eggNOG; COG0119; LUCA. DR InParanoid; Q58595; -. DR KO; K01649; -. DR OMA; MAIKTRQ; -. DR PhylomeDB; Q58595; -. DR BRENDA; 2.3.3.13; 3260. DR UniPathway; UPA00048; UER00070. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003852; F:2-isopropylmalate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013709; 2-isopropylmalate_synth_dimer. DR InterPro; IPR002034; AIPM/Hcit_synth_CS. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011830; LEU1_arch. DR InterPro; IPR000891; PYR_CT. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF08502; LeuA_dimer; 1. DR SMART; SM00917; LeuA_dimer; 1. DR SUPFAM; SSF110921; SSF110921; 1. DR TIGRFAMs; TIGR02090; LEU1_arch; 1. DR PROSITE; PS00815; AIPM_HOMOCIT_SYNTH_1; 1. DR PROSITE; PS00816; AIPM_HOMOCIT_SYNTH_2; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Branched-chain amino acid biosynthesis; KW Complete proteome; Leucine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 518 2-isopropylmalate synthase. FT /FTId=PRO_0000140411. SQ SEQUENCE 518 AA; 56620 MW; 604AB61B41E607A4 CRC64; MIIYREENEI IKKALENLNI PDRVYIFDTT LRDGEQTPGV SLTPEEKIDI AIKLDDLGVD VIEAGFPVSS LGEQEAIKKI CSLNLDAEIC GLARAVKKDI DVAIDCGVDR IHTFIATSPL HRKYKLKKSK EEIIDIAVDA IEYIKEHGIR VEFSAEDATR TEIDYLIEVY KKAVDAGADI INVPDTVGVM IPRAMYYLIN ELKKEIKVPI SVHCHNDFGL AVANSLAAVE AGAEQVHCTI NGLGERGGNA ALEEVVMSLM SIYGVKTNIK TQKLYEISQL VSKYTEIKVQ PNKAIVGENA FAHESGIHAH GVLAHALTYE PIPPELVGQK RKIILGKHTG THAIEAKLKE LGIEVGKDIN KDQFDEIVKR IKALGDKGKR VTDRDVEAIV EDVVGKLAKK DRVVELEQIA VMTGNRVIPT ASVALKIEEE IKKSSAIGVG PVDAAVKAIQ KAIGEKIKLK EYHINAITGG TDALAEVIVT LEGYGREITT KAASEDIVRA SVEAVIDGIN KILAKREK // ID LEUD_METJA Reviewed; 168 AA. AC Q58673; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Isopropylmalate/citramalate isomerase small subunit; DE EC=4.2.1.33; DE EC=4.2.1.35; DE AltName: Full=(R)-2-methylmalate dehydratase; DE AltName: Full=(R)-citramalate dehydratase; DE AltName: Full=3-isopropylmalate dehydratase; DE AltName: Full=Alpha-isopropylmalate dehydratase; DE AltName: Full=Citraconate hydratase; DE AltName: Full=Isopropylmalate isomerase; DE Short=IPMI; DE AltName: Full=Maleate hydratase; DE Short=Malease; DE EC=4.2.1.31; GN Name=leuD; OrderedLocusNames=MJ1277; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=17449626; DOI=10.1128/JB.00166-07; RA Drevland R.M., Waheed A., Graham D.E.; RT "Enzymology and evolution of the pyruvate pathway to 2-oxobutyrate in RT Methanocaldococcus jannaschii."; RL J. Bacteriol. 189:4391-4400(2007). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=22326391; DOI=10.1016/j.bbrc.2012.01.125; RA Lee E.H., Cho Y.W., Hwang K.Y.; RT "Crystal structure of LeuD from Methanococcus jannaschii."; RL Biochem. Biophys. Res. Commun. 419:160-164(2012). CC -!- FUNCTION: Enzyme with broad specificity that catalyzes reversible CC hydroxyacid isomerizations via dehydration/hydration reactions. CC Catalyzes the isomerization between 2-isopropylmalate and 3- CC isopropylmalate, via the formation of 2-isopropylmaleate, a step CC involved in leucine biosynthesis. Catalyzes the isomerization CC between 2-methylmalate and 3-methylmalate, via the formation of 2- CC methylmaleate (citraconate), a step involved in isoleucine CC biosynthesis. Also displays malease activity, i.e. catalyzes the CC hydration of maleate to form (R)-malate. CC {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (2R,3S)-3-isopropylmalate = (2S)-2- CC isopropylmalate. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (R)-2-methylmalate = 2-methylmaleate + H(2)O. CC {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: 2-methylmaleate + H(2)O = (2R,3S)-3- CC methylmalate. {ECO:0000269|PubMed:17449626}. CC -!- CATALYTIC ACTIVITY: (R)-malate = maleate + H(2)O. CC {ECO:0000269|PubMed:17449626}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=80 uM for 2-methylmaleate {ECO:0000269|PubMed:17449626}; CC KM=810 uM for (R)-2-methylmalate {ECO:0000269|PubMed:17449626}; CC KM=1900 uM for racemic 2-isopropylmalate CC {ECO:0000269|PubMed:17449626}; CC KM=39 uM for racemic 3-isopropylmalate CC {ECO:0000269|PubMed:17449626}; CC KM=400 uM for maleate {ECO:0000269|PubMed:17449626}; CC Vmax=15 umol/min/mg enzyme for 2-methylmaleate hydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=1.5 umol/min/mg enzyme for (R)-2-methylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=4.2 umol/min/mg enzyme for 2-isopropylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=1.8 umol/min/mg enzyme for 3-isopropylmalate dehydration CC reaction {ECO:0000269|PubMed:17449626}; CC Vmax=34 umol/min/mg enzyme for maleate hydration reaction CC {ECO:0000269|PubMed:17449626}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:17449626}; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:17449626}; CC -!- PATHWAY: Amino-acid biosynthesis; L-leucine biosynthesis; L- CC leucine from 3-methyl-2-oxobutanoate: step 2/4. CC -!- PATHWAY: Amino-acid biosynthesis; L-isoleucine biosynthesis; 2- CC oxobutanoate from pyruvate: step 2/3. CC -!- SUBUNIT: Heterotetramer of 2 LeuC and 2 LeuD. The heterotetramer CC that can be formed in vitro between HacA and LeuD is inactive. CC {ECO:0000269|PubMed:17449626}. CC -!- SIMILARITY: Belongs to the LeuD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99283.1; -; Genomic_DNA. DR PIR; D64459; D64459. DR PDB; 3VBA; X-ray; 2.00 A; A/B/C/D/E/F=1-168. DR PDBsum; 3VBA; -. DR ProteinModelPortal; Q58673; -. DR SMR; Q58673; 4-167. DR STRING; 243232.MJ_1277; -. DR EnsemblBacteria; AAB99283; AAB99283; MJ_1277. DR KEGG; mja:MJ_1277; -. DR eggNOG; arCOG02230; Archaea. DR eggNOG; COG0066; LUCA. DR InParanoid; Q58673; -. DR KO; K01704; -. DR OMA; PFLRFNS; -. DR PhylomeDB; Q58673; -. DR BioCyc; MetaCyc:MONOMER-13648; -. DR SABIO-RK; Q58673; -. DR UniPathway; UPA00047; UER00067. DR UniPathway; UPA00048; UER00071. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0047508; F:(R)-2-methylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0003861; F:3-isopropylmalate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0050075; F:maleate hydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009097; P:isoleucine biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0009098; P:leucine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.19.10; -; 1. DR HAMAP; MF_01032; LeuD_type2; 1. DR InterPro; IPR015937; Acoase/IPM_deHydtase. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl. DR InterPro; IPR011827; LeuD_type2/HacB/DmdB. DR PANTHER; PTHR11670; PTHR11670; 1. DR Pfam; PF00694; Aconitase_C; 1. DR SUPFAM; SSF52016; SSF52016; 1. DR TIGRFAMs; TIGR02087; LEUD_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; KW Branched-chain amino acid biosynthesis; Complete proteome; KW Isoleucine biosynthesis; Leucine biosynthesis; Lyase; KW Reference proteome. FT CHAIN 1 168 Isopropylmalate/citramalate isomerase FT small subunit. FT /FTId=PRO_0000141937. FT STRAND 3 11 {ECO:0000244|PDB:3VBA}. FT HELIX 18 21 {ECO:0000244|PDB:3VBA}. FT HELIX 24 26 {ECO:0000244|PDB:3VBA}. FT HELIX 32 35 {ECO:0000244|PDB:3VBA}. FT HELIX 36 38 {ECO:0000244|PDB:3VBA}. FT TURN 39 43 {ECO:0000244|PDB:3VBA}. FT HELIX 47 50 {ECO:0000244|PDB:3VBA}. FT STRAND 56 59 {ECO:0000244|PDB:3VBA}. FT STRAND 65 67 {ECO:0000244|PDB:3VBA}. FT HELIX 71 78 {ECO:0000244|PDB:3VBA}. FT STRAND 83 87 {ECO:0000244|PDB:3VBA}. FT HELIX 91 99 {ECO:0000244|PDB:3VBA}. FT STRAND 104 106 {ECO:0000244|PDB:3VBA}. FT HELIX 110 113 {ECO:0000244|PDB:3VBA}. FT STRAND 119 123 {ECO:0000244|PDB:3VBA}. FT TURN 124 126 {ECO:0000244|PDB:3VBA}. FT STRAND 128 131 {ECO:0000244|PDB:3VBA}. FT TURN 132 134 {ECO:0000244|PDB:3VBA}. FT STRAND 137 139 {ECO:0000244|PDB:3VBA}. FT HELIX 145 153 {ECO:0000244|PDB:3VBA}. FT HELIX 156 165 {ECO:0000244|PDB:3VBA}. SQ SEQUENCE 168 AA; 18377 MW; A53C2CA883B6CCD7 CRC64; MRSIIKGRVW KFGNNVDTDA ILPARYLVYT KPEELAQFVM TGADPDFPKK VKPGDIIVGG KNFGCGSSRE HAPLGLKGAG ISCVIAESFA RIFYRNAINV GLPLIECKGI SEKVNEGDEL EVNLETGEIK NLTTGEVLKG QKLPEFMMEI LEAGGLMPYL KKKMAESQ // ID LIVG_METJA Reviewed; 257 AA. AC Q58663; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 107. DE RecName: Full=Probable branched-chain amino acid transport ATP-binding protein LivG; GN Name=livG; OrderedLocusNames=MJ1267; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS). RX PubMed=11470432; DOI=10.1016/S0969-2126(01)00617-7; RA Karpowich N., Martsinkevich O., Millen L., Yuan Y.-R., Dai P.L., RA MacVey K., Thomas P.J., Hunt J.F.; RT "Crystal structures of the MJ1267 ATP binding cassette reveal an RT induced-fit effect at the ATPase active site of an ABC transporter."; RL Structure 9:571-586(2001). CC -!- FUNCTION: Probable component of a branched-chain amino-acid CC transport system. CC -!- SUBUNIT: Monomer. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99273.1; -; Genomic_DNA. DR PIR; B64458; B64458. DR PDB; 1G6H; X-ray; 1.60 A; A=1-257. DR PDB; 1G9X; X-ray; 2.60 A; A/B/C=1-257. DR PDB; 1GAJ; X-ray; 2.50 A; A=1-257. DR PDBsum; 1G6H; -. DR PDBsum; 1G9X; -. DR PDBsum; 1GAJ; -. DR ProteinModelPortal; Q58663; -. DR SMR; Q58663; 4-257. DR STRING; 243232.MJ_1267; -. DR EnsemblBacteria; AAB99273; AAB99273; MJ_1267. DR KEGG; mja:MJ_1267; -. DR eggNOG; arCOG00925; Archaea. DR eggNOG; COG0411; LUCA. DR InParanoid; Q58663; -. DR KO; K01995; -. DR OMA; FRTPGFK; -. DR PhylomeDB; Q58663; -. DR EvolutionaryTrace; Q58663; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid transport; ATP-binding; Complete proteome; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 257 Probable branched-chain amino acid FT transport ATP-binding protein LivG. FT /FTId=PRO_0000092412. FT DOMAIN 8 253 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 40 47 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT STRAND 6 17 {ECO:0000244|PDB:1G6H}. FT STRAND 20 26 {ECO:0000244|PDB:1G6H}. FT STRAND 29 31 {ECO:0000244|PDB:1G6H}. FT STRAND 35 39 {ECO:0000244|PDB:1G6H}. FT HELIX 46 53 {ECO:0000244|PDB:1G6H}. FT STRAND 60 66 {ECO:0000244|PDB:1G6H}. FT HELIX 76 82 {ECO:0000244|PDB:1G6H}. FT STRAND 84 86 {ECO:0000244|PDB:1G6H}. FT HELIX 92 96 {ECO:0000244|PDB:1G6H}. FT HELIX 99 104 {ECO:0000244|PDB:1G6H}. FT HELIX 105 107 {ECO:0000244|PDB:1G6H}. FT HELIX 114 120 {ECO:0000244|PDB:1G6H}. FT HELIX 128 140 {ECO:0000244|PDB:1G6H}. FT HELIX 144 146 {ECO:0000244|PDB:1G6H}. FT HELIX 151 153 {ECO:0000244|PDB:1G6H}. FT HELIX 156 169 {ECO:0000244|PDB:1G6H}. FT STRAND 173 179 {ECO:0000244|PDB:1G6H}. FT TURN 180 183 {ECO:0000244|PDB:1G6H}. FT HELIX 186 201 {ECO:0000244|PDB:1G6H}. FT STRAND 205 209 {ECO:0000244|PDB:1G6H}. FT HELIX 213 216 {ECO:0000244|PDB:1GAJ}. FT HELIX 217 219 {ECO:0000244|PDB:1G6H}. FT STRAND 221 227 {ECO:0000244|PDB:1G6H}. FT STRAND 230 237 {ECO:0000244|PDB:1G6H}. FT HELIX 238 246 {ECO:0000244|PDB:1G6H}. FT HELIX 248 252 {ECO:0000244|PDB:1G6H}. FT TURN 253 256 {ECO:0000244|PDB:1G6H}. SQ SEQUENCE 257 AA; 28995 MW; B3347C3277D09C12 CRC64; MRDTMEILRT ENIVKYFGEF KALDGVSISV NKGDVTLIIG PNGSGKSTLI NVITGFLKAD EGRVYFENKD ITNKEPAELY HYGIVRTFQT PQPLKEMTVL ENLLIGEINP GESPLNSLFY KKWIPKEEEM VEKAFKILEF LKLSHLYDRK AGELSGGQMK LVEIGRALMT NPKMIVMDEP IAGVAPGLAH DIFNHVLELK AKGITFLIIE HRLDIVLNYI DHLYVMFNGQ IIAEGRGEEE IKNVLSDPKV VEIYIGE // ID LIVH_METJA Reviewed; 315 AA. AC Q58665; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Probable branched-chain amino acid transport permease protein LivH; GN Name=livH; OrderedLocusNames=MJ1269; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for branched-chain amino acids. Probably responsible for the CC translocation of the substrates across the membrane (By CC similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. LivHM subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99275.1; -; Genomic_DNA. DR PIR; D64458; D64458. DR ProteinModelPortal; Q58665; -. DR STRING; 243232.MJ_1269; -. DR EnsemblBacteria; AAB99275; AAB99275; MJ_1269. DR KEGG; mja:MJ_1269; -. DR eggNOG; arCOG01269; Archaea. DR eggNOG; COG0559; LUCA. DR InParanoid; Q58665; -. DR KO; K01997; -. DR OMA; NFAQGSY; -. DR PhylomeDB; Q58665; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR InterPro; IPR001851; ABC_transp_permease. DR Pfam; PF02653; BPD_transp_2; 1. PE 3: Inferred from homology; KW Amino-acid transport; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 315 Probable branched-chain amino acid FT transport permease protein LivH. FT /FTId=PRO_0000060064. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 283 303 Helical. {ECO:0000255}. SQ SEQUENCE 315 AA; 33655 MW; 9AA352698413760A CRC64; MVKLLLKDLG EKMILEGAII YSNLLVLLAL GLTLTYITTN VPNFAQGSYA IVGSYVALTL LKLFGICPYL SLPVLFVVGA IVGLITYLAL KPLIKRNASV EILMIATLAI DLILLGVIGA YSEILSQIVG STQAKFVFAN LDFSLFGFKG ILFVSTFVVI LLLIGLYLLL YKTKFGIALR ASMENPSLAQ TMGIDVEKTR LFSWILSGAL AGVAGGLLPF MQEIVPATGD LIIISIFAAS IVGGLRHISG ALIGGYIIGI SESLITYYLA SAFGTGFLVY GKVISLIIMI ATLLIAPYGI TGVDWKKLKR LLSTS // ID LONB_METJA Reviewed; 649 AA. AC Q58812; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 119. DE RecName: Full=Archaeal Lon protease; DE EC=3.4.21.-; DE AltName: Full=ATP-dependent protease La homolog; GN OrderedLocusNames=MJ1417; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 456-640, AND ACTIVE SITE. RX PubMed=15456757; DOI=10.1074/jbc.M410437200; RA Im Y.J., Na Y., Kang G.B., Rho S.H., Kim M.K., Lee J.H., Chung C.H., RA Eom S.H.; RT "The active site of a lon protease from Methanococcus jannaschii RT distinctly differs from the canonical catalytic Dyad of Lon RT proteases."; RL J. Biol. Chem. 279:53451-53457(2004). CC -!- FUNCTION: ATP-dependent serine protease that mediates the CC selective degradation of mutant and abnormal proteins as well as CC certain short-lived regulatory proteins. Degrades polypeptides CC processively (By similarity). {ECO:0000250}. CC -!- SUBUNIT: Homohexamer. Organized in a ring with a central cavity CC (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. Archaeal LonB CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99427.1; -; Genomic_DNA. DR PIR; H64476; H64476. DR PDB; 1XHK; X-ray; 1.90 A; A/B=456-640. DR PDBsum; 1XHK; -. DR ProteinModelPortal; Q58812; -. DR SMR; Q58812; 456-640. DR STRING; 243232.MJ_1417; -. DR MEROPS; S16.008; -. DR EnsemblBacteria; AAB99427; AAB99427; MJ_1417. DR KEGG; mja:MJ_1417; -. DR eggNOG; arCOG02160; Archaea. DR eggNOG; COG1067; LUCA. DR InParanoid; Q58812; -. DR KO; K04076; -. DR OMA; DVHIQFV; -. DR PhylomeDB; Q58812; -. DR EvolutionaryTrace; Q58812; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004663; Lon_arc. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR000523; Mg_chelatse_chII_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 2. DR Pfam; PF05362; Lon_C; 1. DR Pfam; PF01078; Mg_chelatase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00764; lon_rel; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Cell membrane; Complete proteome; KW Hydrolase; Membrane; Nucleotide-binding; Protease; Reference proteome; KW Serine protease; Transmembrane; Transmembrane helix. FT CHAIN 1 649 Archaeal Lon protease. FT /FTId=PRO_0000076150. FT TOPO_DOM 1 114 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TOPO_DOM 136 138 Extracellular. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TOPO_DOM 160 649 Cytoplasmic. {ECO:0000255}. FT DOMAIN 456 639 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT NP_BIND 47 54 ATP. {ECO:0000255}. FT ACT_SITE 550 550 {ECO:0000269|PubMed:15456757}. FT ACT_SITE 593 593 {ECO:0000269|PubMed:15456757}. FT STRAND 461 466 {ECO:0000244|PDB:1XHK}. FT STRAND 469 472 {ECO:0000244|PDB:1XHK}. FT STRAND 475 485 {ECO:0000244|PDB:1XHK}. FT STRAND 490 496 {ECO:0000244|PDB:1XHK}. FT HELIX 498 517 {ECO:0000244|PDB:1XHK}. FT STRAND 533 541 {ECO:0000244|PDB:1XHK}. FT TURN 545 547 {ECO:0000244|PDB:1XHK}. FT HELIX 548 551 {ECO:0000244|PDB:1XHK}. FT HELIX 552 564 {ECO:0000244|PDB:1XHK}. FT STRAND 570 574 {ECO:0000244|PDB:1XHK}. FT STRAND 583 585 {ECO:0000244|PDB:1XHK}. FT HELIX 590 599 {ECO:0000244|PDB:1XHK}. FT STRAND 603 608 {ECO:0000244|PDB:1XHK}. FT HELIX 609 614 {ECO:0000244|PDB:1XHK}. FT STRAND 620 628 {ECO:0000244|PDB:1XHK}. FT HELIX 629 636 {ECO:0000244|PDB:1XHK}. SQ SEQUENCE 649 AA; 71918 MW; 2419207160114DBB CRC64; MFSIKFKTTE ELPEPSPRLI DQVIGQEEAV KIVLSAVKNK RNVILLGDPG VGKSMIVKAV GEILSDFGEF TPYYVIAKPN LKNMERPIVE VIDGEYKEDS KDMPKLDFKA PSSTTLLLIM IGAILLSEYL LKYLPQNYLL AAVTITALIV LIFGFVIILT SIMGASRASM PNNLNPMDLK PVLLYECKKR PLVRASAYNV TRLLGDIKHC PLGGRPPLGT PPHKRIILGA IHEAHRGILY VDEIKTMPLE VQDYILTALQ DKQLPISGRN PNSSGATVET NPIPCDFILI MSGNMDDVYN LRAPLLDRID YKIVLKNKMD NTLENRDKLL QFIVQEIKNN NLNPMTYDGC CEVVRIAQYL AGSKDKLTLR LRLLANIIKM ANDVAMGKDV EELLGNFDDK GEYHPETQKD KSNKVYITAE HVRKVFDTGI YSMEKQVALN YIKNFKRYKH IVPNDEPKVG VIYGLAVLGA GGIGDVTKII VQILESKNPG THLLNISGDI AKHSITLASA LSKKLVAEKK LPLPKKDIDL NNKEIYIQFS QSYSKIDGDS ATAAVCLAII SALLDIPLKQ DFAITGSLDL SGNVLAIGGV NEKIEAAKRY GFKRVIIPEA NMIDVIETEG IEIIPVKTLD EIVPLVFDLD NRGGAERFN // ID LIVF_METJA Reviewed; 237 AA. AC Q58664; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2001, sequence version 2. DT 11-NOV-2015, entry version 92. DE RecName: Full=Probable branched-chain amino acid transport ATP-binding protein LivF; GN Name=livF; OrderedLocusNames=MJ1268; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probable component of a branched-chain amino-acid CC transport system. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99274.1; Type=Frameshift; Positions=27; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99274.1; ALT_FRAME; Genomic_DNA. DR PIR; C64458; C64458. DR ProteinModelPortal; Q58664; -. DR STRING; 243232.MJ_1268; -. DR EnsemblBacteria; AAB99274; AAB99274; MJ_1268. DR KEGG; mja:MJ_1268; -. DR eggNOG; arCOG00924; Archaea. DR eggNOG; COG0410; LUCA. DR InParanoid; Q58664; -. DR KO; K01996; -. DR OMA; HHAKEGN; -. DR PhylomeDB; Q58664; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW Amino-acid transport; ATP-binding; Complete proteome; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 237 Probable branched-chain amino acid FT transport ATP-binding protein LivF. FT /FTId=PRO_0000092405. FT DOMAIN 2 234 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 34 41 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 237 AA; 26353 MW; 5631954537C1E4F1 CRC64; MIKVKNLNAG YGKLQILFDV NAKIEKGKIT TVVGPNGSGK STFLKTLFGL TKIYSGEIIF KDKDIAKVPP HQKARMKIAY LPQTNNVFAN LTVEENLKIA GYVLDKDKVK ERIEIALSVF PELKDILKRK AGTLSGGQRQ FLAMGMALVR DAEVLMLDEP TAQLSPKLAE VIFEKIIEMR DNFGLTILLV EQNAKRALEI SDNGYMFVSG RVAFEGTAEE LLNHEKFKEY SLGITAV // ID M556_METJA Reviewed; 174 AA. AC Q57976; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 78. DE RecName: Full=Methylated protein MJ0556; GN OrderedLocusNames=MJ0556; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION BY MASS SPECTROMETRY, AND METHYLATION. RX PubMed=14976258; DOI=10.1073/pnas.0306575101; RA Forbes A.J., Patrie S.M., Taylor G.K., Kim Y.-B., Jiang L., RA Kelleher N.L.; RT "Targeted analysis and discovery of posttranslational modifications in RT proteins from methanogenic archaea by top-down MS."; RL Proc. Natl. Acad. Sci. U.S.A. 101:2678-2683(2004). CC -!- PTM: Methylated at an undetermined residue between Ser-2 and Asp- CC 26. {ECO:0000269|PubMed:14976258}. CC -!- MASS SPECTROMETRY: Mass=20207; Method=Electrospray; Range=2-174; CC Evidence={ECO:0000269|PubMed:14976258}; CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98550.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98550.1; ALT_INIT; Genomic_DNA. DR PIR; D64369; D64369. DR ProteinModelPortal; Q57976; -. DR STRING; 243232.MJ_0556; -. DR EnsemblBacteria; AAB98550; AAB98550; MJ_0556. DR KEGG; mja:MJ_0556; -. DR eggNOG; ENOG4102TWA; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q57976; -. DR OMA; IIFMEDI; -. DR PhylomeDB; Q57976; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW CBS domain; Complete proteome; Methylation; Reference proteome; KW Repeat. FT INIT_MET 1 1 Removed. {ECO:0000305}. FT CHAIN 2 174 Methylated protein MJ0556. FT /FTId=PRO_0000106929. FT DOMAIN 28 87 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 91 156 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 174 AA; 20352 MW; 984DEF1163F322ED CRC64; MSKFVKLHLV RTLNKYKELQ KIRVKDVMIS GDVIITTPEK TIKEIFDEMI KHNISGMPVV DDRGVMIGFI TLREIRKYMT SHPYLNVGEV MLKNPPYTTA DEDIITAFEK MIESNKKLDQ LPVINTKYPE KILGKLEGII FMEDIIKLLY ENIIKELKTL VSFYNHNTEI KIKY // ID MANB_METJA Reviewed; 449 AA. AC Q57842; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Phosphomannomutase; DE Short=PMM; DE EC=5.4.2.8; DE AltName: Full=Phosphoglucomutase; GN Name=manB; OrderedLocusNames=MJ0399; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A PHOSPHOMANNOMUTASE, AND SUBSTRATE SPECIFICITY. RX PubMed=17014089; DOI=10.1021/bi061018a; RA White R.H., Xu H.; RT "Methylglyoxal is an intermediate in the biosynthesis of 6-deoxy-5- RT ketofructose-1-phosphate: a precursor for aromatic amino acid RT biosynthesis in Methanocaldococcus jannaschii."; RL Biochemistry 45:12366-12379(2006). CC -!- FUNCTION: Catalyzes the formation of mannose-1-P from mannose-6-P. CC Can also use glucose-1-P. {ECO:0000269|PubMed:17014089}. CC -!- CATALYTIC ACTIVITY: Alpha-D-mannose 1-phosphate = D-mannose 6- CC phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98388.1; -; Genomic_DNA. DR PIR; G64349; G64349. DR ProteinModelPortal; Q57842; -. DR STRING; 243232.MJ_0399; -. DR EnsemblBacteria; AAB98388; AAB98388; MJ_0399. DR KEGG; mja:MJ_0399; -. DR eggNOG; arCOG00767; Archaea. DR eggNOG; COG1109; LUCA. DR InParanoid; Q57842; -. DR KO; K01840; -. DR OMA; RNKGAQI; -. DR PhylomeDB; Q57842; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004615; F:phosphomannomutase activity; IDA:UniProtKB. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.30.310.50; -; 1. DR Gene3D; 3.40.120.10; -; 3. DR InterPro; IPR005844; A-D-PHexomutase_a/b/a-I. DR InterPro; IPR016055; A-D-PHexomutase_a/b/a-I/II/III. DR InterPro; IPR005845; A-D-PHexomutase_a/b/a-II. DR InterPro; IPR005846; A-D-PHexomutase_a/b/a-III. DR InterPro; IPR005843; A-D-PHexomutase_C. DR InterPro; IPR016066; A-D-PHexomutase_CS. DR InterPro; IPR005841; Alpha-D-phosphohexomutase_SF. DR Pfam; PF02878; PGM_PMM_I; 1. DR Pfam; PF02879; PGM_PMM_II; 1. DR Pfam; PF02880; PGM_PMM_III; 1. DR Pfam; PF00408; PGM_PMM_IV; 1. DR PRINTS; PR00509; PGMPMM. DR SUPFAM; SSF53738; SSF53738; 3. DR SUPFAM; SSF55957; SSF55957; 1. DR PROSITE; PS00710; PGM_PMM; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Magnesium; Metal-binding; KW Phosphoprotein; Reference proteome. FT CHAIN 1 449 Phosphomannomutase. FT /FTId=PRO_0000147831. FT ACT_SITE 97 97 Phosphoserine intermediate. FT {ECO:0000250}. FT METAL 97 97 Magnesium; via phosphate group. FT {ECO:0000250}. FT METAL 237 237 Magnesium. {ECO:0000250}. FT METAL 239 239 Magnesium. {ECO:0000250}. FT METAL 241 241 Magnesium. {ECO:0000250}. SQ SEQUENCE 449 AA; 51474 MW; 1EB07EEAB409BA00 CRC64; MFGDLMVFKA YDIRGIYGRE LDENFAYSLG KCIGKKFENK KILVGNDVRI GSKELLPYFI VGLKEYADVF YAGTISTPLM YFGTKGKYDL GVILTASHNP PEYTGFKMCD KEAIPLSPIE EIKPIFKKYE LTESIKEEAK NLNLDDLKVN IIEEYKKFFL KRCKASDKKI AVDFANGATT IAEKEILNEL FDNAVFINDY PDGNFPAHQP DTLKMECLKD IIRAVKKNNC ELGLIFDGDG DRLGIVDENG NVLRGDILTA IIAKEILKEK SNAKIVYDLR CSKIVPEIIE KYGGIAIKSR VGHYFIKKLM HEIDAEFAGE LSNHFYFKEI GYFESPLLAL NYILKAMDEE NKSLSELNKE FSKYPHSGEI NFRVKDQKYI MEKIKEHFKD CKLEELDGIS IYCKNFWFNL RPSNTEPLLR LNLEADDEKT MKEKVEEIKN LIAKLDASL // ID MCRD_METJA Reviewed; 164 AA. AC Q58253; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Methyl-coenzyme M reductase I operon protein D; GN Name=mcrD; OrderedLocusNames=MJ0843; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: MCR is composed of three subunits: alpha, beta, and CC gamma. The function of proteins C and D is not known (By CC similarity). {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98848.1; -; Genomic_DNA. DR PIR; C64405; C64405. DR ProteinModelPortal; Q58253; -. DR STRING; 243232.MJ_0843; -. DR EnsemblBacteria; AAB98848; AAB98848; MJ_0843. DR KEGG; mja:MJ_0843; -. DR eggNOG; arCOG04859; Archaea. DR eggNOG; COG4055; LUCA. DR InParanoid; Q58253; -. DR KO; K03422; -. DR OMA; MAGRFWI; -. DR PhylomeDB; Q58253; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR003901; Me_CoM_Rdtase_D. DR Pfam; PF02505; MCR_D; 1. DR PIRSF; PIRSF005636; McrD; 1. DR ProDom; PD005228; Me_CoM_Rdtase_D; 1. DR TIGRFAMs; TIGR03260; met_CoM_red_D; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome. FT CHAIN 1 164 Methyl-coenzyme M reductase I operon FT protein D. FT /FTId=PRO_0000147494. SQ SEQUENCE 164 AA; 19048 MW; CC68B5A87ADDB174 CRC64; MFMIEVEIFP HRYLKASTTE KFLNKIYDLK TVERVVIHGQ PLPKVITYGP ARGLPVNHTE RKIIHVKGVP VELTVMAGRF WITLSDDSEL DKLDEICKEM FPFGYNLRVG KFLKDRPTVT DYIKYGEDGV FLINEMDRRL IGMVDPRSRM ANSVTVVEKE EKEE // ID MCRG_METJA Reviewed; 260 AA. AC Q58255; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Methyl-coenzyme M reductase I subunit gamma; DE Short=MCR I gamma; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma; GN Name=mcrG; OrderedLocusNames=MJ0845; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98850.1; -; Genomic_DNA. DR PIR; E64405; E64405. DR ProteinModelPortal; Q58255; -. DR SMR; Q58255; 6-250. DR STRING; 243232.MJ_0845; -. DR EnsemblBacteria; AAB98850; AAB98850; MJ_0845. DR KEGG; mja:MJ_0845; -. DR eggNOG; arCOG04858; Archaea. DR eggNOG; COG4057; LUCA. DR InParanoid; Q58255; -. DR KO; K00402; -. DR OMA; HRQPGED; -. DR PhylomeDB; Q58255; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.90.320.20; -; 1. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR InterPro; IPR003178; Me_CoM_Rdtase_gsu. DR Pfam; PF02240; MCR_gamma; 1. DR PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1. DR ProDom; PD005845; Me_CoM_Rdtase_gsu; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03259; met_CoM_red_gam; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome; Transferase. FT CHAIN 1 260 Methyl-coenzyme M reductase I subunit FT gamma. FT /FTId=PRO_0000147476. SQ SEQUENCE 260 AA; 30174 MW; 34413840D8EADACE CRC64; MAYKPQFYPG QTKIAQNRRD HMNPDVQLEK LRDIPDDDVV KIMGHRQPGE DYKTVHPPLE EMDLPEDYVR DLVEPLNGAK EGHRIRYIQF TDSMYFAPAQ PYDRARTYMW RFRGVDTGTL SGRQVIEMRE SDLEALSKNF LIDTAFFDPA RIGIRGATVH GHSLRLDENG LMFDALQRYV YDEKTGHVLY VKDQVGRPLD EPVDVGEPLP EEKLKEITTI YRIDGVPMRE DEELLTVVKR IHRARTLGGF LPVEDVFEKL // ID MCRX_METJA Reviewed; 552 AA. AC Q60391; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Methyl-coenzyme M reductase II subunit alpha; DE Short=MCR II alpha; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha; GN Name=mrtA; Synonyms=mtrA; OrderedLocusNames=MJ0083; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000250}; CC Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme CC F430 is a yellow nickel porphinoid. {ECO:0000250}; CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98063.1; -; Genomic_DNA. DR PIR; C64310; C64310. DR ProteinModelPortal; Q60391; -. DR SMR; Q60391; 7-551. DR STRING; 243232.MJ_0083; -. DR EnsemblBacteria; AAB98063; AAB98063; MJ_0083. DR KEGG; mja:MJ_0083; -. DR eggNOG; arCOG04857; Archaea. DR eggNOG; COG4058; LUCA. DR InParanoid; Q60391; -. DR KO; K00399; -. DR OMA; QRKLMAY; -. DR PhylomeDB; Q60391; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.20.840.10; -; 1. DR Gene3D; 3.30.70.470; -; 1. DR Gene3D; 3.90.390.10; -; 1. DR InterPro; IPR022681; MCR_a/b_chain_a-bundle. DR InterPro; IPR016212; Me_CoM_Rdtase_asu. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C. DR InterPro; IPR003183; Me_CoM_Rdtase_asu_N. DR InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR Pfam; PF02249; MCR_alpha; 1. DR Pfam; PF02745; MCR_alpha_N; 1. DR PIRSF; PIRSF000262; MCR_alpha; 1. DR SUPFAM; SSF48081; SSF48081; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03256; met_CoM_red_alp; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Methanogenesis; Methylation; Nickel; KW Reference proteome; Transferase. FT CHAIN 1 552 Methyl-coenzyme M reductase II subunit FT alpha. FT /FTId=PRO_0000147453. FT METAL 150 150 Nickel. {ECO:0000250}. FT MOD_RES 260 260 Pros-methylhistidine. {ECO:0000250}. FT MOD_RES 274 274 5-methylarginine. {ECO:0000250}. SQ SEQUENCE 552 AA; 61241 MW; DB66781796B987CE CRC64; MDVEKKLFLK ALKEKFEEDP KEKYTKFYIF GGWRQSARKR EFVEFAQKLI EKRGGIPFYN PDIGVPLGQR KLMTYKISGT DAFVEGDDLH FCNNAAIQQL VDDIKRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPGL VWDCYAKIFT GNDELADEID KRFLIDINKE FPEEQAEQIK KYIGNRTYQV SRVPTIVVRC CDGGTVSRWS AMQIGMSFIT AYKLCAGEAA IADFSYAAKH ADVIQMGMIL PARRARGPNE PGGVPFGIFA DIIQTSRVSD DPAQVTLEVI GAAATFYDQV WLGSYMSGGV GFTQYASATY TDDILDDFVY YGMDYVEKKY GLCGVKPSME VVKDIATEVT LYGLEQYDEY PALLEDHFGG SQRAGVTAAA AGCSVAFATG NSNAGINGWY LSQILHKEYH SRLGFYGYDL QDQCGAANSL SIRSDEGLLH ECRGPNYPNY AMNVGHQPEY AGIAQAPHAA RGDAFCLNPI IKVAFADDNL IFDFKWPRKC IAKGALREFE PAGERDLIIP AA // ID MCRZ_METJA Reviewed; 266 AA. AC Q60387; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Methyl-coenzyme M reductase II subunit gamma; DE Short=MCR II gamma; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase gamma; GN Name=mrtG; Synonyms=mtrG; OrderedLocusNames=MJ0082; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98062.1; -; Genomic_DNA. DR PIR; B64310; B64310. DR ProteinModelPortal; Q60387; -. DR SMR; Q60387; 6-252. DR STRING; 243232.MJ_0082; -. DR EnsemblBacteria; AAB98062; AAB98062; MJ_0082. DR KEGG; mja:MJ_0082; -. DR eggNOG; arCOG04858; Archaea. DR eggNOG; COG4057; LUCA. DR InParanoid; Q60387; -. DR KO; K00402; -. DR OMA; HRNPGES; -. DR PhylomeDB; Q60387; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 3.90.320.20; -; 1. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR InterPro; IPR003178; Me_CoM_Rdtase_gsu. DR Pfam; PF02240; MCR_gamma; 1. DR PIRSF; PIRSF000264; Meth_CoM_rd_gama; 1. DR ProDom; PD005845; Me_CoM_Rdtase_gsu; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03259; met_CoM_red_gam; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome; Transferase. FT CHAIN 1 266 Methyl-coenzyme M reductase II subunit FT gamma. FT /FTId=PRO_0000147477. SQ SEQUENCE 266 AA; 30764 MW; 51E7B3C7F984157A CRC64; MAYKPQFYPG NTLIAENRRK HMNPEVELKK LRDIPDDEIV KILGHRNPGE SYKTVHPPLE EMDFEEDPIK DIVEPIQGAK EGVRVRYIQF ADSMYNAPAQ PYDRARTYMW RFRGIDTGTL SGRQVIEMRE LDLEKISKNF LIDTEFFDPA TCGIRGATVH GHSLRLDENG LMFDGLQRYI YDEKTGHVLY VKDQVGRPLD EPVDVGEPLP HDYLAKITTI YRKDNIGMRE DKEALEVVQI IHEARTKGGF GLEVFKKDLK KRLGEE // ID MAP2_METJA Reviewed; 294 AA. AC Q58725; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 110. DE RecName: Full=Methionine aminopeptidase {ECO:0000255|HAMAP-Rule:MF_01975}; DE Short=MAP {ECO:0000255|HAMAP-Rule:MF_01975}; DE Short=MetAP {ECO:0000255|HAMAP-Rule:MF_01975}; DE EC=3.4.11.18 {ECO:0000255|HAMAP-Rule:MF_01975}; DE AltName: Full=Peptidase M {ECO:0000255|HAMAP-Rule:MF_01975}; GN Name=map {ECO:0000255|HAMAP-Rule:MF_01975}; OrderedLocusNames=MJ1329; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Removes the N-terminal methionine from nascent proteins. CC The N-terminal methionine is often cleaved when the second residue CC in the primary sequence is small and uncharged (Met-Ala-, Cys, CC Gly, Pro, Ser, Thr, or Val). {ECO:0000255|HAMAP-Rule:MF_01975}. CC -!- CATALYTIC ACTIVITY: Release of N-terminal amino acids, CC preferentially methionine, from peptides and arylamides. CC {ECO:0000255|HAMAP-Rule:MF_01975}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01975}; CC Note=Binds 2 divalent metal cations per subunit. Has a high- CC affinity and a low affinity metal-binding site. The true nature of CC the physiological cofactor is under debate. The enzyme is active CC with cobalt, zinc, manganese or divalent iron ions. Most likely, CC methionine aminopeptidases function as mononuclear Fe(2+)- CC metalloproteases under physiological conditions, and the CC catalytically relevant metal-binding site has been assigned to the CC histidine-containing high-affinity site. {ECO:0000255|HAMAP- CC Rule:MF_01975}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01975}. CC -!- SIMILARITY: Belongs to the peptidase M24A family. Methionine CC aminopeptidase archaeal type 2 subfamily. {ECO:0000255|HAMAP- CC Rule:MF_01975}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99338.1; -; Genomic_DNA. DR PIR; H64465; H64465. DR ProteinModelPortal; Q58725; -. DR STRING; 243232.MJ_1329; -. DR MEROPS; M24.035; -. DR EnsemblBacteria; AAB99338; AAB99338; MJ_1329. DR KEGG; mja:MJ_1329; -. DR eggNOG; arCOG01001; Archaea. DR eggNOG; COG0024; LUCA. DR InParanoid; Q58725; -. DR KO; K01265; -. DR OMA; IRASCIY; -. DR PhylomeDB; Q58725; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070006; F:metalloaminopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0070084; P:protein initiator methionine removal; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.90.230.10; -; 2. DR HAMAP; MF_01975; MetAP_2_arc; 1. DR InterPro; IPR028595; MetAP_archaeal. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR002468; Pept_M24A_MAP2. DR InterPro; IPR018349; Pept_M24A_MAP2_BS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR10804:SF9; PTHR10804:SF9; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF55920; SSF55920; 2. DR TIGRFAMs; TIGR00501; met_pdase_II; 1. DR PROSITE; PS01202; MAP_2; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; Protease; KW Reference proteome. FT CHAIN 1 294 Methionine aminopeptidase. FT /FTId=PRO_0000148975. FT METAL 85 85 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT METAL 96 96 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT METAL 96 96 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT METAL 156 156 Divalent metal cation 2; catalytic; via FT tele nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01975}. FT METAL 189 189 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT METAL 279 279 Divalent metal cation 1. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT METAL 279 279 Divalent metal cation 2; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01975}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01975}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01975}. SQ SEQUENCE 294 AA; 32950 MW; AA28D37E2BF34186 CRC64; MEIEGYEKII EAGKIASKVR EEAVKLIXPG VKLLEVAEFV ENRIRELGGE PAFPCNISIN EIAAHYTPKL NDNLEFKDDD VVKLDLGAHV DGYIADTAIT VDLSNSYKDL VKASEDALYT VIKEINPPMN IGEMGKIIQE VIESYGYKPI SNLSGHVMHR YELHTGISIP NVYERTNQYI DVGDLVAIEP FATDGFGMVK DGNLGNIYKF LAKRPIRLPQ ARKLLDVISK NYPYLPFAER WVLKNESERL ALNSLIRASC IYGYPILKER ENGIVGQAEH TILITENGVE ITTK // ID MCRW_METJA Reviewed; 167 AA. AC Q57582; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Methyl-coenzyme M reductase II operon protein D; GN Name=mrtD; Synonyms=mtrD; OrderedLocusNames=MJ0118; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: MCR is composed of three subunits: alpha, beta, and CC gamma. The function of protein D is not known (By similarity). CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98099.1; -; Genomic_DNA. DR PIR; F64314; F64314. DR ProteinModelPortal; Q57582; -. DR STRING; 243232.MJ_0118; -. DR EnsemblBacteria; AAB98099; AAB98099; MJ_0118. DR KEGG; mja:MJ_0118; -. DR eggNOG; arCOG04859; Archaea. DR eggNOG; COG4055; LUCA. DR InParanoid; Q57582; -. DR KO; K03422; -. DR OMA; IVRVIVH; -. DR PhylomeDB; Q57582; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR003901; Me_CoM_Rdtase_D. DR Pfam; PF02505; MCR_D; 1. DR PIRSF; PIRSF005636; McrD; 1. DR ProDom; PD005228; Me_CoM_Rdtase_D; 1. DR TIGRFAMs; TIGR03260; met_CoM_red_D; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome. FT CHAIN 1 167 Methyl-coenzyme M reductase II operon FT protein D. FT /FTId=PRO_0000147495. SQ SEQUENCE 167 AA; 19007 MW; 87B67CFC6B19AF1F CRC64; MKNEVKFMSE VIKVVDVKIF PHRYLKAETT EKVLNEIYDL DGIVRVIVHG QPLPKTVPFG PARGLPVNHQ DRKVIKVKGE EMELRVKVGE IIITVEGEKL EKIMDGIEEI CKRNFPFGYD IYVGAFTKIK PTVTDYMKYG DISSIDPRLI GMVDASARLK DSVKMIK // ID MCRA_METJA Reviewed; 553 AA. AC Q58256; Q977G8; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 112. DE RecName: Full=Methyl-coenzyme M reductase I subunit alpha; DE Short=MCR I alpha; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase alpha; GN Name=mcrA; OrderedLocusNames=MJ0846; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 340-478. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12427943; RA Luton P.E., Wayne J.M., Sharp R.J., Riley P.W.; RT "The mcrA gene as an alternative to 16S rRNA in the phylogenetic RT analysis of methanogen populations in landfill."; RL Microbiology 148:3521-3530(2002). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- COFACTOR: CC Name=coenzyme F430; Xref=ChEBI:CHEBI:60540; CC Evidence={ECO:0000250}; CC Note=Binds 1 coenzyme F430 noncovalently per subunit. Coenzyme CC F430 is a yellow nickel porphinoid. {ECO:0000250}; CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98851.1; -; Genomic_DNA. DR EMBL; AF414040; AAL29289.1; -; Genomic_DNA. DR ProteinModelPortal; Q58256; -. DR SMR; Q58256; 7-552. DR STRING; 243232.MJ_0846; -. DR EnsemblBacteria; AAB98851; AAB98851; MJ_0846. DR KEGG; mja:MJ_0846; -. DR eggNOG; arCOG04857; Archaea. DR eggNOG; COG4058; LUCA. DR InParanoid; Q58256; -. DR KO; K00399; -. DR OMA; INKLFPE; -. DR PhylomeDB; Q58256; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.20.840.10; -; 1. DR Gene3D; 3.30.70.470; -; 1. DR Gene3D; 3.90.390.10; -; 1. DR InterPro; IPR022681; MCR_a/b_chain_a-bundle. DR InterPro; IPR016212; Me_CoM_Rdtase_asu. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR009047; Me_CoM_Rdtase_asu_C. DR InterPro; IPR003183; Me_CoM_Rdtase_asu_N. DR InterPro; IPR015811; Me_CoM_Rdtase_asu_N_sub1. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR Pfam; PF02249; MCR_alpha; 1. DR Pfam; PF02745; MCR_alpha_N; 1. DR PIRSF; PIRSF000262; MCR_alpha; 1. DR SUPFAM; SSF48081; SSF48081; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03256; met_CoM_red_alp; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Methanogenesis; Methylation; Nickel; KW Reference proteome; Transferase. FT CHAIN 1 553 Methyl-coenzyme M reductase I subunit FT alpha. FT /FTId=PRO_0000147452. FT METAL 150 150 Nickel. {ECO:0000250}. FT MOD_RES 260 260 Pros-methylhistidine. {ECO:0000250}. FT MOD_RES 274 274 5-methylarginine. {ECO:0000250}. FT CONFLICT 424 424 N -> F (in Ref. 2; AAL29289). FT {ECO:0000305}. SQ SEQUENCE 553 AA; 61266 MW; CC3AB9AC4F745A24 CRC64; MDAEKRLFLK ALKEKFEEDP REKYTKFYVF GGWRQSARKR EFVEAAQKLI EKRGGIPFYN PDIGVPLGQR KLMPYKVSNT DAIVEGDDLH FMNNAAMQQF WDDIRRTVIV GMDTAHAVLE KRLGVEVTPE TINEYMETIN HALPGGAVVQ EHMVEVHPAL VWDCYAKIFT GDDELADEID KRFLIDINKL FPEEQAEQIK KAIGKRTYQV SRVPTLVGRV CDGGTIARWS AMQIGMSFIT AYKLCAGEAA IADFSYAAKH ADVIQMASFL PARRARGPNE PGGIFFGVLA DIVQTSRVSD DPVEQSLEVV AAGAMLYDQI WLGGYMSGGV GFTQYATATY TDDILDDFSY YGYDYITKKY GGCNSVKPTM DVVEDIATEV TLYGLEQYDT FPALLEDHFG GSQRAGVTAA AAGITTALAT GNSNAGVNGW YLSQILHKEY HSRLGFYGYD LQDQCGAANS LSFRNDEGSP LELRGPNYPN YAMNVGHQGE YAGITQAAHS ARGDAFALNP LIKVAFADPS LVFDFTHPRK EFARGALREF EPAGERDPII PAH // ID MCRB_METJA Reviewed; 447 AA. AC Q58252; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 101. DE RecName: Full=Methyl-coenzyme M reductase I subunit beta; DE Short=MCR I beta; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta; GN Name=mcrB; OrderedLocusNames=MJ0842; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98847.1; -; Genomic_DNA. DR ProteinModelPortal; Q58252; -. DR SMR; Q58252; 6-447. DR STRING; 243232.MJ_0842; -. DR EnsemblBacteria; AAB98847; AAB98847; MJ_0842. DR KEGG; mja:MJ_0842; -. DR eggNOG; arCOG04860; Archaea. DR eggNOG; COG4054; LUCA. DR InParanoid; Q58252; -. DR KO; K00401; -. DR OMA; GKQMAVQ; -. DR PhylomeDB; Q58252; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.20.840.10; -; 2. DR Gene3D; 3.30.70.470; -; 1. DR InterPro; IPR022681; MCR_a/b_chain_a-bundle. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR003179; Me_CoM_Rdtase_bsu. DR InterPro; IPR022679; Me_CoM_Rdtase_bsu_C. DR InterPro; IPR022680; Me_CoM_Rdtase_bsu_N. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1. DR SUPFAM; SSF48081; SSF48081; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03257; met_CoM_red_bet; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome; Transferase. FT CHAIN 1 447 Methyl-coenzyme M reductase I subunit FT beta. FT /FTId=PRO_0000147465. SQ SEQUENCE 447 AA; 47789 MW; 52C76BB2C4C425E7 CRC64; MIPMVKYKDT INLYDEKGKL VEENVPLEAI SPLHNPTIQK LVKDVKRTVA VNLAGIENAL RTGQVGGKGC MIKGRELDLP IVENAETIAE YVEKVVRVSE DDDTSIKLIN DGKQMAVQIP SKRLDVAAEY SVSVLVTAQA LKEAIIRTFD VDIFDAPMVH AAVLGGYPHE VTMKGSNIAA LLGSPLSLEG PGYALRNIMA NHFVACTKKN VMNAVAFAAI MEQTAMFEMG DAVGLFERLH LLGLAYQGLN ADNLVIDLVK ANGKNGTVGT VVASVVERAL EDGVIKEDKT LPSGFKLYKP VDVAKWNAYA AAGLVAAAIV NCGAARAAQN IASTILYYND ILEYETGLPG VDFGRAEGTA VGFSFFSHSI YGGGGPGIFN GNHIVTRHSK GFAIPPVAAA MCLDAGTQMF SPERTSALVG TVFSAIDEFR EPLKYVIKGA LEVKDKI // ID MCRC_METJA Reviewed; 200 AA. AC Q58254; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Methyl-coenzyme M reductase I operon protein C; GN Name=mcrC; OrderedLocusNames=MJ0844; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: MCR is composed of three subunits: alpha, beta, and CC gamma. The function of proteins C and D is not known (By CC similarity). {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98849.1; -; Genomic_DNA. DR PIR; D64405; D64405. DR ProteinModelPortal; Q58254; -. DR STRING; 243232.MJ_0844; -. DR EnsemblBacteria; AAB98849; AAB98849; MJ_0844. DR KEGG; mja:MJ_0844; -. DR eggNOG; arCOG03225; Archaea. DR eggNOG; COG4056; LUCA. DR InParanoid; Q58254; -. DR KO; K03421; -. DR OMA; TQVVDCR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR InterPro; IPR007687; Me_CoM_Rdtase_prot-C. DR InterPro; IPR026327; Me_CoM_Rdtase_prot-C-like. DR Pfam; PF04609; MCR_C; 1. DR PIRSF; PIRSF003137; McrC; 1. DR TIGRFAMs; TIGR03264; met_CoM_red_C; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome. FT CHAIN 1 200 Methyl-coenzyme M reductase I operon FT protein C. FT /FTId=PRO_0000147486. SQ SEQUENCE 200 AA; 21668 MW; B5DA112CA902F24C CRC64; MPVGRREQIV DCRSVMGLGE GGGLAQRGTF AEALKNDVVV VAMSPGRRHI TKPVCEITYG IREAGIQTSV LVLNAGSGIP HDAPRGALGS TFGIKPEEAE QINRHKLCVV HFGNVISHIV YKAGLLLKYV EIPTIIVCQA PVDMEDLAKY GIKTRDVMPL EPKTKGTVVD IVTGVIRGES CPQTKIDEVI RKIKLHLNLN // ID MCRY_METJA Reviewed; 447 AA. AC Q60390; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 103. DE RecName: Full=Methyl-coenzyme M reductase II subunit beta; DE Short=MCR II beta; DE EC=2.8.4.1; DE AltName: Full=Coenzyme-B sulfoethylthiotransferase beta; GN Name=mrtB; OrderedLocusNames=MJ0081; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reduction of methyl-coenzyme M (2-(methylthio) CC ethanesulfonic acid) with 7-mercaptoheptanoylthreonine phosphate CC to methane and a heterodisulfide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Methyl-CoM + CoB = CoM-S-S-CoB + methane. CC -!- PATHWAY: One-carbon metabolism; methyl-coenzyme M reduction; CC methane from methyl-coenzyme M: step 1/1. CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two gamma chains. CC {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98061.1; -; Genomic_DNA. DR ProteinModelPortal; Q60390; -. DR SMR; Q60390; 4-443. DR STRING; 243232.MJ_0081; -. DR EnsemblBacteria; AAB98061; AAB98061; MJ_0081. DR KEGG; mja:MJ_0081; -. DR eggNOG; arCOG04860; Archaea. DR eggNOG; COG4054; LUCA. DR InParanoid; Q60390; -. DR KO; K00401; -. DR OMA; VLYYNDI; -. DR PhylomeDB; Q60390; -. DR UniPathway; UPA00646; UER00699. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050524; F:coenzyme-B sulfoethylthiotransferase activity; IEA:UniProtKB-EC. DR GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW. DR Gene3D; 1.20.840.10; -; 2. DR Gene3D; 3.30.70.470; -; 1. DR InterPro; IPR022681; MCR_a/b_chain_a-bundle. DR InterPro; IPR008924; Me_CoM_Rdtase_asu/bsu_C. DR InterPro; IPR015823; Me_CoM_Rdtase_asu_N_sub2. DR InterPro; IPR003179; Me_CoM_Rdtase_bsu. DR InterPro; IPR022679; Me_CoM_Rdtase_bsu_C. DR InterPro; IPR022680; Me_CoM_Rdtase_bsu_N. DR InterPro; IPR009024; Me_CoM_Rdtase_Fd-like_fold. DR Pfam; PF02241; MCR_beta; 1. DR Pfam; PF02783; MCR_beta_N; 1. DR PIRSF; PIRSF000263; Meth_CoM_rd_beta; 1. DR SUPFAM; SSF48081; SSF48081; 1. DR SUPFAM; SSF55088; SSF55088; 1. DR TIGRFAMs; TIGR03257; met_CoM_red_bet; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Reference proteome; Transferase. FT CHAIN 1 447 Methyl-coenzyme M reductase II subunit FT beta. FT /FTId=PRO_0000147466. SQ SEQUENCE 447 AA; 47770 MW; B9CAE1066BE977BC CRC64; MLHYEDRIDL YDERGKLLEE NVPLEAISPL KNPTIEKIVN DIKRSVAINL AGIENALKTG AVGGKACFCP GRELDLPIVE NAEIIAEKIK RMVQIEEDDD TVVKLINGGK QLLLQLPSKR LRVAADYTVS ALIGGGATVQ AIVDAFDVDM FDAPVVKTAV MGRYPQTVDF HGANIATLLG PPVLLEGLGY GLRNIMANHI VAVTRKKTLN AVALASILEQ TAMFETGDAL GAFERLHLLG LAFQGLNANN LTYELVKENG KDGTVGTVVA SVVERALEDG VIRPLKTMPS GFTVYEPVDW ALWNAYAASG LVAAVIVNVG AARAAQGVAS TVLYYNDILE YETGLPSVDF GRAEGTAVGF SFFSHSIYGG GGPGTFHGNH VVTRHSKGFA IPCAAAAMCL DAGTQMFSVE RTSALVGTVY SAIDHLREPL KYVAEGAVEV KEKEKVI // ID MER_METJA Reviewed; 331 AA. AC Q58929; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 98. DE RecName: Full=5,10-methylenetetrahydromethanopterin reductase {ECO:0000255|HAMAP-Rule:MF_01091}; DE EC=1.5.98.2 {ECO:0000255|HAMAP-Rule:MF_01091}; DE AltName: Full=Coenzyme F420-dependent N(5),N(10)-methylenetetrahydromethanopterin reductase {ECO:0000255|HAMAP-Rule:MF_01091}; DE AltName: Full=Methylene-H(4)MPT reductase {ECO:0000255|HAMAP-Rule:MF_01091}; GN Name=mer {ECO:0000255|HAMAP-Rule:MF_01091}; OrderedLocusNames=MJ1534; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible reduction of methylene-H(4)MPT CC to methyl-H(4)MPT. {ECO:0000255|HAMAP-Rule:MF_01091}. CC -!- CATALYTIC ACTIVITY: 5-methyltetrahydromethanopterin + oxidized CC coenzyme F420 = 5,10-methylenetetrahydromethanopterin + reduced CC coenzyme F420. {ECO:0000255|HAMAP-Rule:MF_01091}. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 1/2. {ECO:0000255|HAMAP-Rule:MF_01091}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01091}. CC -!- SIMILARITY: Belongs to the mer family. {ECO:0000255|HAMAP- CC Rule:MF_01091}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99555.1; -; Genomic_DNA. DR ProteinModelPortal; Q58929; -. DR SMR; Q58929; 1-325. DR STRING; 243232.MJ_1534; -. DR EnsemblBacteria; AAB99555; AAB99555; MJ_1534. DR KEGG; mja:MJ_1534; -. DR eggNOG; arCOG02410; Archaea. DR eggNOG; COG2141; LUCA. DR InParanoid; Q58929; -. DR KO; K00320; -. DR OMA; FEYCWIT; -. DR PhylomeDB; Q58929; -. DR UniPathway; UPA00640; UER00697. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0018537; F:coenzyme F420-dependent N5,N10-methenyltetrahydromethanopterin reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.30; -; 1. DR HAMAP; MF_01091; F420_mer; 1. DR InterPro; IPR011251; Luciferase-like_dom. DR InterPro; IPR019946; MeH4methanopterin_reductase. DR Pfam; PF00296; Bac_luciferase; 1. DR SUPFAM; SSF51679; SSF51679; 1. DR TIGRFAMs; TIGR03555; F420_mer; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methanogenesis; One-carbon metabolism; KW Oxidoreductase; Reference proteome. FT CHAIN 1 331 5,10-methylenetetrahydromethanopterin FT reductase. FT /FTId=PRO_0000084807. SQ SEQUENCE 331 AA; 35353 MW; 367B5DFD1EB6EBBD CRC64; MKFGIEFVPN EPIQKLCYYV KLAEDNGFEY CWITDHYNNR NVYMALTAIA MNTNKIKLGP GVTNPYVRSP AITASAIATL DELSGGRAVL GIGPGDKATF DALGIEWVKP VTTLKESIEV IRKLLAGERV SYEGKVVKIA GAALAVKPIQ KAVPVYMGAQ GPKMLETAGM IADGVLINAS NPKDFEAAIP LIKKGAEAAG RSMDEIDVAA YACMSVDKNA DKAKQAAVPV VAFIAAGSPP VVLERHGIDM EKVEAIRNAL KSGNFPEAFK NVDDTMLEAF SIYGTPEDVV EKCKKLAEMG VTQIVAGSPI GPNKETAIKL IGKKVIPALK E // ID MFNE_METJA Reviewed; 216 AA. AC Q57900; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 81. DE RecName: Full=5-(aminomethyl)-3-furanmethanol phosphate kinase {ECO:0000305}; DE EC=2.7.4.- {ECO:0000269|PubMed:26100040}; GN Name=mfnE {ECO:0000303|PubMed:26100040}; GN Synonyms=adkB {ECO:0000303|PubMed:22002406}; OrderedLocusNames=MJ0458; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS AN ADENYLATE KINASE, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RX PubMed=22002406; DOI=10.1007/s00203-011-0759-9; RA Grochowski L.L., Censky K., Xu H., White R.H.; RT "A new class of adenylate kinase in methanogens is related to RT uridylate kinase."; RL Arch. Microbiol. 194:141-145(2012). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=26100040; DOI=10.1128/JB.00401-15; RA Wang Y., Xu H., Jones M.K., White R.H.; RT "Identification of the final two genes functioning in methanofuran RT biosynthesis in Methanocaldococcus jannaschii."; RL J. Bacteriol. 197:2850-2858(2015). RN [4] RP CRYSTALLIZATION. RX PubMed=24192367; DOI=10.1107/S1744309113026638; RA Wang X., Yuan Y., Teng M., Niu L., Gao Y.; RT "Crystallization and preliminary X-ray diffraction analysis of MJ0458, RT an adenylate kinase from Methanocaldococcus jannaschii."; RL Acta Crystallogr. F 69:1272-1274(2013). CC -!- FUNCTION: Catalyzes the formation of 5-(aminomethyl)-3- CC furanmethanol diphosphate (F1-PP) from 5-(aminomethyl)-3- CC furanmethanol phosphate (F1-P) and ATP (PubMed:26100040). In CC vitro, can also act as an adenylate kinase that catalyzes the CC transfer of a phosphoryl group from ATP to AMP, generating two CC molecules of ADP (PubMed:22002406). {ECO:0000269|PubMed:22002406, CC ECO:0000269|PubMed:26100040}. CC -!- CATALYTIC ACTIVITY: 5-(aminomethyl)-3-furanmethanol phosphate + CC ATP = 5-(aminomethyl)-3-furanmethanol diphosphate + ADP. CC {ECO:0000269|PubMed:26100040}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:26100040}; CC -!- ENZYME REGULATION: Inhibited by EDTA. CC {ECO:0000269|PubMed:26100040}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=10.2 uM for ATP {ECO:0000269|PubMed:22002406}; CC KM=26.2 uM for AMP {ECO:0000269|PubMed:22002406}; CC Vmax=3.1 umol/min/mg enzyme for the adenylate kinase reaction CC (at 37 degrees Celsius) {ECO:0000269|PubMed:22002406}; CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:26100040}; CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000305|PubMed:26100040}. CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:22002406}. CC -!- SIMILARITY: Belongs to the MfnE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98446.1; -; Genomic_DNA. DR PIR; B64357; B64357. DR ProteinModelPortal; Q57900; -. DR STRING; 243232.MJ_0458; -. DR EnsemblBacteria; AAB98446; AAB98446; MJ_0458. DR KEGG; mja:MJ_0458; -. DR eggNOG; arCOG00859; Archaea. DR eggNOG; COG2054; LUCA. DR InParanoid; Q57900; -. DR KO; K07144; -. DR OMA; YFSEISG; -. DR PhylomeDB; Q57900; -. DR BRENDA; 2.7.4.3; 3260. DR UniPathway; UPA00080; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.1160.10; -; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR011375; MfnE. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF004857; Kin_aa_kin; 1. DR SUPFAM; SSF53633; SSF53633; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 216 5-(aminomethyl)-3-furanmethanol phosphate FT kinase. FT /FTId=PRO_0000106886. FT NP_BIND 5 9 ATP. {ECO:0000250|UniProtKB:Q9HLX1}. FT NP_BIND 147 152 ATP. {ECO:0000250|UniProtKB:Q9HLX1}. FT BINDING 39 39 ATP; via amide nitrogen. FT {ECO:0000250|UniProtKB:Q9HLX1}. FT BINDING 142 142 ATP. {ECO:0000250|UniProtKB:Q9HLX1}. FT BINDING 166 166 ATP; via carbonyl oxygen. FT {ECO:0000250|UniProtKB:Q9HLX1}. SQ SEQUENCE 216 AA; 24080 MW; 37856E333F3D2A76 CRC64; MHIVKIGGSL TYDAKPLLKA LKNYAKENNK KIVIIPGGGE FANVVRKIDK ALNISNSLSH KLAIKCMDLI GEVYAEIGYI KAYDTLFDLK REIEKEKIAI LLPSKILLST DIAEHSWAIT SDSLSLYIGK LLDVREVIIA TDVDGIYDKF PGGKLLNIIN ANDIKGLTSV DETFPILLKQ FKMNAYVVNG RHPERVMDIL EGKHNIYTKI VGIDKI // ID MCH_METJA Reviewed; 323 AA. AC Q59030; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Methenyltetrahydromethanopterin cyclohydrolase; DE EC=3.5.4.27; DE AltName: Full=Methenyl-H4MPT cyclohydrolase; GN Name=mch; OrderedLocusNames=MJ1636; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible interconversion of 5-formyl- CC H(4)MPT to methenyl-H(4)MPT(+). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,10-methenyl-5,6,7,8-tetrahydromethanopterin CC + H(2)O = 5-formyl-5,6,7,8-tetrahydromethanopterin. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methenyl-5,6,7,8-tetrahydromethanopterin from CO(2): step 3/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MCH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99657.1; -; Genomic_DNA. DR PIR; B64504; B64504. DR ProteinModelPortal; Q59030; -. DR SMR; Q59030; 1-318. DR STRING; 243232.MJ_1636; -. DR EnsemblBacteria; AAB99657; AAB99657; MJ_1636. DR KEGG; mja:MJ_1636; -. DR eggNOG; arCOG02675; Archaea. DR eggNOG; COG3252; LUCA. DR InParanoid; Q59030; -. DR KO; K01499; -. DR OMA; YFAMGSG; -. DR PhylomeDB; Q59030; -. DR UniPathway; UPA00640; UER00694. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0018759; F:methenyltetrahydromethanopterin cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00486; McH; 1. DR InterPro; IPR003209; METHMP_CycHdrlase. DR Pfam; PF02289; MCH; 1. DR TIGRFAMs; TIGR03120; one_C_mch; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Methanogenesis; KW One-carbon metabolism; Reference proteome. FT CHAIN 1 323 Methenyltetrahydromethanopterin FT cyclohydrolase. FT /FTId=PRO_0000140881. SQ SEQUENCE 323 AA; 34900 MW; C793B6CF432BA31F CRC64; MLSVNKKALE IVNKMIENKE EINIDVIKLE NGATVLDCGV NVPGSWKAGK LFTKICLGGL AHVGISLSPC ECKGITLPYV KIKTSHPAIA TLGAQKAGWA VKVGKYFAMG SGPARALAKK PKKTYEEIGY EDDADVAVLC LEASKLPNEE VAEYVAKECG VEVENVYLLV APTASLVGSI QISGRVVENG TYKMLEVLEF DVNKVKYAAG LAPIAPIIGD DFAMMGATND MVLYGGITYY YIKSDENDDI ESLCKALPSC ASKDYGKPFM EVFKAADYDF YKIDKGMFAP AVVVINDMTT GKVYRAGKVN AEVLKKSLGW TEL // ID METE_METJA Reviewed; 308 AA. AC Q58868; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=Methionine synthase {ECO:0000255|HAMAP-Rule:MF_00288}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00288}; DE AltName: Full=Homocysteine methyltransferase; DE AltName: Full=Methylcobalamin:homocysteine methyltransferase; GN Name=metE {ECO:0000255|HAMAP-Rule:MF_00288}; OrderedLocusNames=MJ1473; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transfer of a methyl group to L- CC homocysteine resulting in methionine formation. Can use CC methylcobalamin and methylcobinamide as methyl donors, but CC methylcobalamin is not considered to be the physiological CC substrate (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00288}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00288}; CC -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de CC novo pathway. {ECO:0000255|HAMAP-Rule:MF_00288}. CC -!- SIMILARITY: Belongs to the archaeal MetE family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99479.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99479.1; ALT_INIT; Genomic_DNA. DR PIR; H64483; H64483. DR ProteinModelPortal; Q58868; -. DR STRING; 243232.MJ_1473; -. DR EnsemblBacteria; AAB99479; AAB99479; MJ_1473. DR KEGG; mja:MJ_1473; -. DR eggNOG; arCOG01876; Archaea. DR eggNOG; COG0620; LUCA. DR InParanoid; Q58868; -. DR KO; K00549; -. DR OMA; NIAHIID; -. DR PhylomeDB; Q58868; -. DR UniPathway; UPA00051; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005576; C:extracellular region; IBA:GO_Central. DR GO; GO:0003871; F:5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008705; F:methionine synthase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0050667; P:homocysteine metabolic process; IBA:GO_Central. DR HAMAP; MF_00288; MetE; 1. DR InterPro; IPR002629; Met_Synth_C/arc. DR InterPro; IPR022921; MetE_arc. DR Pfam; PF01717; Meth_synt_2; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Metal-binding; KW Methionine biosynthesis; Methyltransferase; Reference proteome; KW Transferase; Zinc. FT CHAIN 1 308 Methionine synthase. FT /FTId=PRO_0000098684. FT METAL 192 192 Zinc. {ECO:0000255|HAMAP-Rule:MF_00288}. FT METAL 194 194 Zinc. {ECO:0000255|HAMAP-Rule:MF_00288}. FT METAL 282 282 Zinc. {ECO:0000255|HAMAP-Rule:MF_00288}. SQ SEQUENCE 308 AA; 34724 MW; 6032FD5C97E2565D CRC64; MITTVVGSYP VVKKEETFLD KVKKVFGLYD EYKYAIERAV KDQVKAGVNI ISDGQVRGDM VEIFTNNMYG FDGKRVVGRV EFIKPITLKD ILYAKSIAKK LNPNVEIKGI ITGPCTIASS VRVESCYSDN RDENLIYDIA KALRKEVEAL KKHVPIIQID EPILSTGMYD FDVARKAIDI IVDGLNIKFA MHVCGNVYNI IDELNKFNVD ILDHEFASNK KNLVILESME KKVGFGCVNT KVKKVESVEE IKSLIEEGIE ILKNNEKLNK NLSDNILIDP DCGMRLLPID VAFNKLKNMV EATKLIKI // ID MDH_METJA Reviewed; 313 AA. AC Q60176; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 130. DE RecName: Full=L-2-hydroxycarboxylate dehydrogenase (NAD(P)(+)) {ECO:0000305}; DE EC=1.1.1.375 {ECO:0000269|PubMed:10850983, ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779}; DE AltName: Full=MdhII {ECO:0000303|PubMed:10850983}; GN Name=mdh; Synonyms=mdhB; OrderedLocusNames=MJ0490; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS MALATE/SULFOLACTATE DEHYDROGENASE, CATALYTIC ACTIVITY, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10850983; DOI=10.1128/JB.182.13.3688-3692.2000; RA Graupner M., Xu H., White R.H.; RT "Identification of an archaeal 2-hydroxy acid dehydrogenase catalyzing RT reactions involved in coenzyme biosynthesis in methanoarchaea."; RL J. Bacteriol. 182:3688-3692(2000). RN [3] RP FUNCTION AS A MALATE DEHYDROGENASE, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=10998181; DOI=10.1046/j.1365-2958.2000.02113.x; RA Madern D.; RT "The putative L-lactate dehydrogenase from Methanococcus jannaschii is RT an NADPH-dependent L-malate dehydrogenase."; RL Mol. Microbiol. 37:1515-1520(2000). RN [4] RP SUBUNIT. RX PubMed=11513609; DOI=10.1021/bi010168c; RA Madern D., Ebel C., Dale H.A., Lien T., Steen I.H., Birkeland N.-K., RA Zaccai G.; RT "Differences in the oligomeric states of the LDH-like L-MalDH from the RT hyperthermophilic archaea Methanococcus jannaschii and Archaeoglobus RT fulgidus."; RL Biochemistry 40:10310-10316(2001). RN [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=19555779; DOI=10.1016/j.bbapap.2009.06.014; RA Kawakami R., Sakuraba H., Goda S., Tsuge H., Ohshima T.; RT "Refolding, characterization and crystal structure of (S)-malate RT dehydrogenase from the hyperthermophilic archaeon Aeropyrum pernix."; RL Biochim. Biophys. Acta 1794:1496-1504(2009). RN [6] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEX WITH NADP, AND RP SUBUNIT. RX PubMed=11292347; DOI=10.1006/jmbi.2001.4532; RA Lee B.I., Chang C., Cho S.-J., Eom S.H., Kim K.K., Yu Y.G., Suh S.W.; RT "Crystal structure of the MJ0490 gene product of the hyperthermophilic RT archaebacterium Methanococcus jannaschii, a novel member of the RT lactate/malate family of dehydrogenases."; RL J. Mol. Biol. 307:1351-1362(2001). CC -!- FUNCTION: Catalyzes the reversible oxidation of (S)-malate and CC (S)-sulfolactate to oxaloacetate and sulfopyruvate, respectively. CC Can use both NADH and NADPH, although activity is higher with CC NADPH. Oxidation of (S)-sulfolactate is observed only in the CC presence of NADP(+). Can also oxidize tartrate. Can not reduce CC pyruvate, nor alpha-ketoglutarate. {ECO:0000269|PubMed:10850983, CC ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779}. CC -!- CATALYTIC ACTIVITY: A (2S)-2-hydroxycarboxylate + NAD(P)(+) = a 2- CC oxocarboxylate + NAD(P)H. {ECO:0000269|PubMed:10850983, CC ECO:0000269|PubMed:10998181, ECO:0000269|PubMed:19555779}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.15 mM for (S)-malate (in the presence of NAD(+)) CC {ECO:0000269|PubMed:10850983}; CC KM=0.41 mM for (S)-malate (in the presence of NAD(+)) CC {ECO:0000269|PubMed:19555779}; CC KM=0.025 mM for (S)-malate (in the presence of NADP(+)) CC {ECO:0000269|PubMed:10850983}; CC KM=0.084 mM for (S)-malate (in the presence of NADP(+)) CC {ECO:0000269|PubMed:19555779}; CC KM=4.6 mM for (S)-sulfolactate (in the presence of NADP(+)) CC {ECO:0000269|PubMed:10850983}; CC KM=11 mM for (2S,3S)-tartrate (in the presence of NAD(+)) CC {ECO:0000269|PubMed:19555779}; CC KM=5.1 mM for (2S,3S)-tartrate (in the presence of NADP(+)) CC {ECO:0000269|PubMed:19555779}; CC KM=0.25 mM for oxaloacetate (in the presence of NADH) CC {ECO:0000269|PubMed:10850983}; CC KM=0.30 mM for oxaloacetate (in the presence of NADPH) CC {ECO:0000269|PubMed:10850983}; CC KM=1.3 mM for sulfopyruvate (in the presence of NADH) CC {ECO:0000269|PubMed:10850983}; CC KM=0.19 mM for sulfopyruvate (in the presence of NADPH) CC {ECO:0000269|PubMed:10850983}; CC KM=0.14 mM for NADH {ECO:0000269|PubMed:10998181}; CC KM=0.02 mM for NADPH {ECO:0000269|PubMed:10998181}; CC Vmax=0.6 umol/min/mg enzyme toward (S)-malate (in the presence CC of NAD(+)) {ECO:0000269|PubMed:10850983}; CC Vmax=3 umol/min/mg enzyme toward (S)-malate (in the presence of CC NADP(+)) {ECO:0000269|PubMed:10850983}; CC Vmax=3 umol/min/mg enzyme toward (S)-sulfolactate (in the CC presence of NADP(+)) {ECO:0000269|PubMed:10850983}; CC Vmax=29 umol/min/mg enzyme toward oxaloacetate (in the presence CC of NADH) {ECO:0000269|PubMed:10850983}; CC Vmax=49 umol/min/mg enzyme toward oxaloacetate (in the presence CC of NADPH) {ECO:0000269|PubMed:10850983}; CC Vmax=43 umol/min/mg enzyme toward sulfopyruvate (in the presence CC of NADH) {ECO:0000269|PubMed:10850983}; CC Vmax=69 umol/min/mg enzyme toward sulfopyruvate (in the presence CC of NADPH) {ECO:0000269|PubMed:10850983}; CC Note=kcat is 0.33 sec(-1) for NAD-dependent malate oxidation. CC kcat is 0.069 sec(-1) for NADP-dependent malate oxidation. CC {ECO:0000269|PubMed:19555779}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:10998181, CC ECO:0000269|PubMed:11292347, ECO:0000269|PubMed:11513609}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the LDH/MDH superfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98481.1; -; Genomic_DNA. DR PIR; B64361; B64361. DR PDB; 1HYE; X-ray; 1.90 A; A=1-313. DR PDB; 1HYG; X-ray; 2.80 A; A/B=1-313. DR PDBsum; 1HYE; -. DR PDBsum; 1HYG; -. DR ProteinModelPortal; Q60176; -. DR SMR; Q60176; 1-313. DR STRING; 243232.MJ_0490; -. DR EnsemblBacteria; AAB98481; AAB98481; MJ_0490. DR KEGG; mja:MJ_0490; -. DR eggNOG; arCOG00246; Archaea. DR eggNOG; COG0039; LUCA. DR InParanoid; Q60176; -. DR KO; K00024; -. DR OMA; ILTCAAH; -. DR PhylomeDB; Q60176; -. DR BRENDA; 1.1.1.B46; 3260. DR SABIO-RK; Q60176; -. DR EvolutionaryTrace; Q60176; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004459; F:L-lactate dehydrogenase activity; IEA:InterPro. DR GO; GO:0030060; F:L-malate dehydrogenase activity; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006108; P:malate metabolic process; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.720; -; 1. DR Gene3D; 3.90.110.10; -; 1. DR InterPro; IPR001557; L-lactate/malate_DH. DR InterPro; IPR018177; L-lactate_DH_AS. DR InterPro; IPR022383; Lactate/malate_DH_C. DR InterPro; IPR001236; Lactate/malate_DH_N. DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C. DR InterPro; IPR011275; Malate_DH_type3. DR InterPro; IPR016040; NAD(P)-bd_dom. DR PANTHER; PTHR11540; PTHR11540; 1. DR Pfam; PF02866; Ldh_1_C; 1. DR Pfam; PF00056; Ldh_1_N; 1. DR PIRSF; PIRSF000102; Lac_mal_DH; 1. DR PRINTS; PR00086; LLDHDRGNASE. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF56327; SSF56327; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; NAD; NADP; Oxidoreductase; KW Reference proteome; Tricarboxylic acid cycle. FT CHAIN 1 313 L-2-hydroxycarboxylate dehydrogenase FT (NAD(P)(+)). FT /FTId=PRO_0000113485. FT NP_BIND 7 13 NADP. {ECO:0000269|PubMed:11292347}. FT NP_BIND 34 37 NADP. {ECO:0000269|PubMed:11292347}. FT NP_BIND 121 123 NADP. {ECO:0000269|PubMed:11292347}. FT ACT_SITE 178 178 Proton acceptor. FT {ECO:0000250|UniProtKB:P61889}. FT BINDING 86 86 Substrate. FT {ECO:0000250|UniProtKB:P61889}. FT BINDING 92 92 Substrate. FT {ECO:0000250|UniProtKB:P61889}. FT BINDING 99 99 NADP. {ECO:0000269|PubMed:11292347}. FT BINDING 123 123 Substrate. FT {ECO:0000250|UniProtKB:P61889}. FT BINDING 154 154 Substrate. FT {ECO:0000250|UniProtKB:P61889}. FT STRAND 2 6 {ECO:0000244|PDB:1HYE}. FT TURN 7 9 {ECO:0000244|PDB:1HYE}. FT HELIX 11 21 {ECO:0000244|PDB:1HYE}. FT STRAND 28 33 {ECO:0000244|PDB:1HYE}. FT HELIX 35 37 {ECO:0000244|PDB:1HYE}. FT HELIX 38 52 {ECO:0000244|PDB:1HYE}. FT STRAND 60 65 {ECO:0000244|PDB:1HYE}. FT HELIX 69 72 {ECO:0000244|PDB:1HYE}. FT STRAND 76 80 {ECO:0000244|PDB:1HYE}. FT HELIX 92 113 {ECO:0000244|PDB:1HYE}. FT STRAND 117 120 {ECO:0000244|PDB:1HYE}. FT STRAND 122 124 {ECO:0000244|PDB:1HYE}. FT HELIX 125 136 {ECO:0000244|PDB:1HYE}. FT STRAND 142 145 {ECO:0000244|PDB:1HYE}. FT HELIX 149 163 {ECO:0000244|PDB:1HYE}. FT HELIX 167 169 {ECO:0000244|PDB:1HYE}. FT STRAND 174 176 {ECO:0000244|PDB:1HYE}. FT STRAND 182 184 {ECO:0000244|PDB:1HYE}. FT HELIX 186 188 {ECO:0000244|PDB:1HYE}. FT HELIX 196 198 {ECO:0000244|PDB:1HYE}. FT HELIX 200 204 {ECO:0000244|PDB:1HYE}. FT HELIX 207 217 {ECO:0000244|PDB:1HYE}. FT HELIX 219 222 {ECO:0000244|PDB:1HYG}. FT STRAND 225 227 {ECO:0000244|PDB:1HYG}. FT HELIX 232 244 {ECO:0000244|PDB:1HYE}. FT STRAND 249 263 {ECO:0000244|PDB:1HYE}. FT STRAND 265 276 {ECO:0000244|PDB:1HYE}. FT STRAND 279 283 {ECO:0000244|PDB:1HYE}. FT HELIX 290 310 {ECO:0000244|PDB:1HYE}. SQ SEQUENCE 313 AA; 34609 MW; A7C0DB67C50151CC CRC64; MKVTIIGASG RVGSATALLL AKEPFMKDLV LIGREHSINK LEGLREDIYD ALAGTRSDAN IYVESDENLR IIDESDVVII TSGVPRKEGM SRMDLAKTNA KIVGKYAKKI AEICDTKIFV ITNPVDVMTY KALVDSKFER NQVFGLGTHL DSLRFKVAIA KFFGVHIDEV RTRIIGEHGD SMVPLLSATS IGGIPIQKFE RFKELPIDEI IEDVKTKGEQ IIRLKGGSEF GPAAAILNVV RCIVNNEKRL LTLSAYVDGE FDGIRDVCIG VPVKIGRDGI EEVVSIELDK DEIIAFRKSA EIIKKYCEEV KNL // ID METK_METJA Reviewed; 406 AA. AC Q58605; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=S-adenosylmethionine synthase; DE Short=AdoMet synthase; DE EC=2.5.1.6; DE AltName: Full=Methionine adenosyltransferase; GN Name=mat; OrderedLocusNames=MJ1208; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 3-43; 53-91; 132-178; 186-209; 213-225; 229-239; RP 250-269; 295-336 AND 347-379, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, RP PATHWAY, AND SUBUNIT. RX PubMed=10660563; DOI=10.1074/jbc.275.6.4055; RA Graham D.E., Bock C.L., Schalk-Hihi C., Lu Z.J., Markham G.D.; RT "Identification of a highly diverged class of S-adenosylmethionine RT synthetases in the archaea."; RL J. Biol. Chem. 275:4055-4059(2000). CC -!- FUNCTION: Catalyzes the formation of S-adenosylmethionine from CC methionine and ATP. {ECO:0000269|PubMed:10660563}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + H(2)O = phosphate + CC diphosphate + S-adenosyl-L-methionine. CC {ECO:0000269|PubMed:10660563}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10660563}; CC -!- PATHWAY: Amino-acid biosynthesis; S-adenosyl-L-methionine CC biosynthesis; S-adenosyl-L-methionine from L-methionine: step 1/1. CC {ECO:0000269|PubMed:10660563}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10660563}. CC -!- SIMILARITY: Belongs to the AdoMet synthase 2 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99212.1; -; Genomic_DNA. DR PIR; G64450; G64450. DR ProteinModelPortal; Q58605; -. DR STRING; 243232.MJ_1208; -. DR EnsemblBacteria; AAB99212; AAB99212; MJ_1208. DR KEGG; mja:MJ_1208; -. DR eggNOG; arCOG01678; Archaea. DR eggNOG; COG1812; LUCA. DR InParanoid; Q58605; -. DR KO; K00789; -. DR OMA; HNTDQVE; -. DR PhylomeDB; Q58605; -. DR BRENDA; 2.5.1.6; 3260. DR UniPathway; UPA00315; UER00080. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004478; F:methionine adenosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006556; P:S-adenosylmethionine biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00136; S_AdoMet_synth2; 1. DR InterPro; IPR027790; AdoMet_synthase_2_family. DR InterPro; IPR002795; S-AdoMet_synthetase_arc. DR Pfam; PF01941; AdoMet_Synthase; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Direct protein sequencing; Magnesium; KW Nucleotide-binding; One-carbon metabolism; Reference proteome; KW Transferase. FT CHAIN 1 406 S-adenosylmethionine synthase. FT /FTId=PRO_0000150028. FT NP_BIND 141 146 ATP. {ECO:0000255}. SQ SEQUENCE 406 AA; 45252 MW; 457B087EE1243404 CRC64; MRNIIVKKLD VEPIEERPTE IVERKGLGHP DSICDGIAES VSRALCKMYM EKFGTILHHN TDQVELVGGH AYPKFGGGVM VSPIYILLSG RATMEILDKE KNEVIKLPVG TTAVKAAKEY LKKVLRNVDV DKDVIIDCRI GQGSMDLVDV FERQKNEVPL ANDTSFGVGY APLSTTERLV LETERFLNSD ELKNEIPAVG EDIKVMGLRE GKKITLTIAM AVVDRYVKNI EEYKEVIEKV RKKVEDLAKK IADGYEVEIH INTADDYERE SVYLTVTGTS AEMGDDGSVG RGNRVNGLIT PFRPMSMEAA SGKNPVNHVG KIYNILANLI ANDIAKLEGV KECYVRILSQ IGKPINEPKA LDIEIITEDS YDIKDIEPKA KEIANKWLDN IMEVQKMIVE GKVTTF // ID MFNC_METJA Reviewed; 370 AA. AC Q58097; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 13-APR-2016, entry version 105. DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate transaminase {ECO:0000305}; DE EC=2.6.1.108 {ECO:0000269|PubMed:24977328}; DE AltName: Full=4-HFC-P:alanine aminotransferase {ECO:0000303|PubMed:24977328}; GN Name=mfnC {ECO:0000303|PubMed:24977328}; OrderedLocusNames=MJ0684; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=24977328; DOI=10.1021/bi500615p; RA Miller D., Wang Y., Xu H., Harich K., White R.H.; RT "Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of RT methanofuran."; RL Biochemistry 53:4635-4647(2014). RN [3] RP CRYSTALLIZATION, AND SUBUNIT. RX PubMed=12595727; DOI=10.1107/S0907444903000076; RA Yang J.K., Chang C., Cho S.J., Lee J.Y., Yu Y.G., Eom S.H., Suh S.W.; RT "Crystallization and preliminary X-ray analysis of the Mj0684 gene RT product, a putative aspartate aminotransferase, from Methanococcus RT jannaschii."; RL Acta Crystallogr. D 59:563-565(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH RP PYRIDOXAL-PHOSPHATE, COFACTOR, AND SUBUNIT. RX DOI=10.5012/bkcs.2008.29.1.173; RA Yang J.K.; RT "Crystal structure of MJ0684 from Methanococcus jannaschii, a novel RT archaeal homolog of kynurenine aminotransferase."; RL Bull. Korean Chem. Soc. 29:173-176(2008). CC -!- FUNCTION: Catalyzes the transamination reaction between 4- CC (hydroxymethyl)-2-furancarboxaldehyde phosphate (4-HFC-P) and CC alanine to produce pyruvate and 5-(aminomethyl)-3-furanmethanol CC phosphate (F1-P), the precursor for the furan moiety in CC methanofuran. {ECO:0000269|PubMed:24977328}. CC -!- CATALYTIC ACTIVITY: L-alanine + (5-formylfuran-3-yl)methyl CC phosphate = pyruvate + 5-(aminomethyl)-3-furanmethanol phosphate. CC {ECO:0000269|PubMed:24977328}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000269|Ref.4}; CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000269|PubMed:24977328}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12595727, CC ECO:0000269|Ref.4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98679.1; -; Genomic_DNA. DR PDB; 2Z61; X-ray; 2.20 A; A=1-370. DR PDBsum; 2Z61; -. DR ProteinModelPortal; Q58097; -. DR SMR; Q58097; 1-369. DR STRING; 243232.MJ_0684; -. DR EnsemblBacteria; AAB98679; AAB98679; MJ_0684. DR KEGG; mja:MJ_0684; -. DR eggNOG; arCOG01130; Archaea. DR eggNOG; COG0436; LUCA. DR InParanoid; Q58097; -. DR KO; K19793; -. DR OMA; FAYSLDT; -. DR PhylomeDB; Q58097; -. DR BioCyc; RETL1328306-WGS:GSTH-1926-MONOMER; -. DR UniPathway; UPA00080; -. DR EvolutionaryTrace; Q58097; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminotransferase; Complete proteome; Cytoplasm; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 370 (5-formylfuran-3-yl)methyl phosphate FT transaminase. FT /FTId=PRO_0000123859. FT MOD_RES 222 222 N6-(pyridoxal phosphate)lysine. FT {ECO:0000269|Ref.4}. FT HELIX 4 8 {ECO:0000244|PDB:2Z61}. FT HELIX 15 26 {ECO:0000244|PDB:2Z61}. FT HELIX 45 56 {ECO:0000244|PDB:2Z61}. FT HELIX 69 82 {ECO:0000244|PDB:2Z61}. FT HELIX 89 91 {ECO:0000244|PDB:2Z61}. FT STRAND 92 97 {ECO:0000244|PDB:2Z61}. FT HELIX 98 109 {ECO:0000244|PDB:2Z61}. FT STRAND 115 121 {ECO:0000244|PDB:2Z61}. FT HELIX 125 132 {ECO:0000244|PDB:2Z61}. FT STRAND 136 140 {ECO:0000244|PDB:2Z61}. FT HELIX 144 150 {ECO:0000244|PDB:2Z61}. FT STRAND 153 163 {ECO:0000244|PDB:2Z61}. FT TURN 165 167 {ECO:0000244|PDB:2Z61}. FT HELIX 173 182 {ECO:0000244|PDB:2Z61}. FT STRAND 184 189 {ECO:0000244|PDB:2Z61}. FT TURN 191 194 {ECO:0000244|PDB:2Z61}. FT STRAND 196 199 {ECO:0000244|PDB:2Z61}. FT HELIX 204 206 {ECO:0000244|PDB:2Z61}. FT STRAND 212 220 {ECO:0000244|PDB:2Z61}. FT TURN 221 225 {ECO:0000244|PDB:2Z61}. FT HELIX 227 229 {ECO:0000244|PDB:2Z61}. FT STRAND 232 235 {ECO:0000244|PDB:2Z61}. FT HELIX 238 251 {ECO:0000244|PDB:2Z61}. FT STRAND 253 255 {ECO:0000244|PDB:2Z61}. FT HELIX 257 263 {ECO:0000244|PDB:2Z61}. FT HELIX 264 267 {ECO:0000244|PDB:2Z61}. FT HELIX 269 295 {ECO:0000244|PDB:2Z61}. FT HELIX 317 328 {ECO:0000244|PDB:2Z61}. FT HELIX 335 338 {ECO:0000244|PDB:2Z61}. FT HELIX 340 342 {ECO:0000244|PDB:2Z61}. FT STRAND 343 349 {ECO:0000244|PDB:2Z61}. FT HELIX 354 368 {ECO:0000244|PDB:2Z61}. SQ SEQUENCE 370 AA; 42348 MW; 51C2EE6D50079940 CRC64; MLSKRLLNFE SFEVMDILAL AQKLESEGKK VIHLEIGEPD FNTPKPIVDE GIKSLKEGKT HYTDSRGILE LREKISELYK DKYKADIIPD NIIITGGSSL GLFFALSSII DDGDEVLIQN PCYPCYKNFI RFLGAKPVFC DFTVESLEEA LSDKTKAIII NSPSNPLGEV IDREIYEFAY ENIPYIISDE IYNGLVYEGK CYSAIEFDEN LEKTILINGF SKLYAMTGWR IGYVISNDEI IEAILKLQQN LFISAPTISQ YAALKAFEKE TEREINSMIK EFDRRRRLVL KYVKDFGWEV NNPIGAYYVF PNIGEDGREF AYKLLKEKFV ALTPGIGFGS KGKNYIRISY ANSYENIKEG LERIKEFLNK // ID MFND_METJA Reviewed; 308 AA. AC Q58225; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Tyramine--L-glutamate ligase; DE EC=6.3.4.24 {ECO:0000250|UniProtKB:C7P8V7}; GN Name=mfnD; OrderedLocusNames=MJ0815; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the formation of an amide bond between CC tyramine and the gamma carboxy group of L-glutamate. The enzyme CC also accepts phenylethylamine in vitro. CC {ECO:0000250|UniProtKB:C7P8V7}. CC -!- CATALYTIC ACTIVITY: ATP + tyramine + L-glutamate = ADP + phosphate CC + gamma-glutamyltyramine. {ECO:0000250|UniProtKB:C7P8V7}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:C7P8V7}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:C7P8V7}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000255|PROSITE-ProRule:PRU00409}; CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000250|UniProtKB:C7P8V7}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98814.1; -; Genomic_DNA. DR PIR; G64401; G64401. DR ProteinModelPortal; Q58225; -. DR STRING; 243232.MJ_0815; -. DR EnsemblBacteria; AAB98814; AAB98814; MJ_0815. DR KEGG; mja:MJ_0815; -. DR eggNOG; arCOG01592; Archaea. DR eggNOG; COG1821; LUCA. DR InParanoid; Q58225; -. DR KO; K06914; -. DR OMA; ENYIVQE; -. DR PhylomeDB; Q58225; -. DR UniPathway; UPA00080; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.470.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003806; ATP-grasp_DUF201-type. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR024710; MfnD. DR Pfam; PF02655; ATP-grasp_3; 1. DR PIRSF; PIRSF016766; UCP016766_ATPgrasp; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 308 Tyramine--L-glutamate ligase. FT /FTId=PRO_0000013998. FT DOMAIN 89 291 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 115 192 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT METAL 252 252 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 264 264 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 264 264 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 266 266 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. SQ SEQUENCE 308 AA; 35061 MW; 08C458E046749061 CRC64; MLLLQSILIT KIMVIQLILF FEYALASGFE DKNILKEGKM MFDTLLKQFL EIDKVISLLY KDFVDNYIDF KNLEIVKIKK ENEIENKLKS LLKSENIDYA LVVAPEDEDI LYNLTKIIES YPVKNLGCSS EAIKIAGNKY LTYLAIKDAV KTPKTFPPKK YVVKKIDSCG GKFNLFDENF LIQEFIDGEN LSVSLIVGKK IHPLSLNRQY IDKRGFVGGE VNINHKLKDK IFNEAIKAVK CINGLNGYVG VDVIVNNDGI YIIEINPRIT TTIYGLKTNP SLAELLIKNA NNEELKFKVK GEKFTIDK // ID MFNA_METJA Reviewed; 396 AA. AC Q60358; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-MAR-2016, entry version 100. DE RecName: Full=L-tyrosine/L-aspartate decarboxylase {ECO:0000305}; DE Short=TDC/ADC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000305}; DE EC=4.1.1.11 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24891443}; DE EC=4.1.1.25 {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:15715981}; GN Name=mfnA {ECO:0000255|HAMAP-Rule:MF_01610, GN ECO:0000303|PubMed:15715981}; OrderedLocusNames=MJ0050; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A TYROSINE DECARBOXYLASE, CATALYTIC ACTIVITY, COFACTOR, RP ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, PATHWAY, AND RP SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15715981; DOI=10.1016/j.bbagen.2004.12.003; RA Kezmarsky N.D., Xu H., Graham D.E., White R.H.; RT "Identification and characterization of a L-tyrosine decarboxylase in RT Methanocaldococcus jannaschii."; RL Biochim. Biophys. Acta 1722:175-182(2005). RN [3] RP FUNCTION AS AN ASPARTATE DECARBOXYLASE, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY. RX PubMed=24891443; DOI=10.1128/JB.01784-14; RA Wang Y., Xu H., White R.H.; RT "Beta-alanine biosynthesis in Methanocaldococcus jannaschii."; RL J. Bacteriol. 196:2869-2875(2014). RN [4] {ECO:0000244|PDB:3F9T} RP X-RAY CRYSTALLOGRAPHY (2.11 ANGSTROMS) IN COMPLEX WITH PYRIDOXAL RP PHOSPHATE. RG Joint Center for Structural Genomics (JCSG); RT "Crystal structure of L-tyrosine decarboxylase MfnA (EC 4.1.1.25) RT (NP_247014.1) from Methanococcus jannaschii at 2.11 A resolution."; RL Submitted (NOV-2008) to the PDB data bank. CC -!- FUNCTION: Catalyzes the decarboxylation of L-tyrosine to produce CC tyramine for methanofuran biosynthesis (PubMed:15715981). Can also CC catalyze the decarboxylation of L-aspartate to produce beta- CC alanine for coenzyme A (CoA) biosynthesis (PubMed:24891443). CC {ECO:0000269|PubMed:15715981, ECO:0000269|PubMed:24891443}. CC -!- CATALYTIC ACTIVITY: L-tyrosine = tyramine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:15715981}. CC -!- CATALYTIC ACTIVITY: L-aspartate = beta-alanine + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24891443}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01610, CC ECO:0000269|PubMed:15715981}; CC -!- ENZYME REGULATION: Inhibited by hydroxylamine and O- CC methylhydroxylamine. {ECO:0000269|PubMed:15715981}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.6 mM for L-tyrosine {ECO:0000269|PubMed:15715981}; CC KM=0.8 mM for L-aspartate {ECO:0000269|PubMed:24891443}; CC pH dependence: CC Optimum pH is 7.5-8.5 for tyrosine decarboxylase activity. CC {ECO:0000269|PubMed:15715981}; CC Temperature dependence: CC Thermostable. Retains full tyrosine decarboxylase activity after CC heating at 100 degrees Celsius for 10 minutes and 42% of its CC activity after 10 minutes at 110 degrees Celsius. Inactive after CC 10 minutes at 121 degrees Celsius. CC {ECO:0000269|PubMed:15715981}; CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:15715981}. CC -!- PATHWAY: Cofactor biosynthesis; coenzyme A biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01610, ECO:0000269|PubMed:24891443}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15715981}. CC -!- SIMILARITY: Belongs to the group II decarboxylase family. MfnA CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01610}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98031.1; -; Genomic_DNA. DR PIR; B64306; B64306. DR PDB; 3F9T; X-ray; 2.11 A; A/B=1-396. DR PDBsum; 3F9T; -. DR ProteinModelPortal; Q60358; -. DR STRING; 243232.MJ_0050; -. DR EnsemblBacteria; AAB98031; AAB98031; MJ_0050. DR KEGG; mja:MJ_0050; -. DR eggNOG; arCOG00027; Archaea. DR eggNOG; COG0076; LUCA. DR InParanoid; Q60358; -. DR KO; K18933; -. DR OMA; DNICELS; -. DR PhylomeDB; Q60358; -. DR BioCyc; MetaCyc:MONOMER-12228; -. DR BRENDA; 4.1.1.11; 3260. DR BRENDA; 4.1.1.25; 3260. DR UniPathway; UPA00080; -. DR UniPathway; UPA00241; -. DR EvolutionaryTrace; Q60358; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004068; F:aspartate 1-decarboxylase activity; IDA:UniProtKB. DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB. DR GO; GO:0004837; F:tyrosine decarboxylase activity; IDA:UniProtKB. DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro. DR GO; GO:0015937; P:coenzyme A biosynthetic process; TAS:UniProtKB. DR GO; GO:2001120; P:methanofuran biosynthetic process; TAS:UniProtKB. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR HAMAP; MF_01610; MfnA_decarbox; 1. DR InterPro; IPR020931; MfnA. DR InterPro; IPR002129; PyrdxlP-dep_de-COase. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00282; Pyridoxal_deC; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03812; tyr_de_CO2_Arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Decarboxylase; Lyase; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1 396 L-tyrosine/L-aspartate decarboxylase. FT /FTId=PRO_0000147023. FT MOD_RES 245 245 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255|HAMAP-Rule:MF_01610, FT ECO:0000269|Ref.4}. FT HELIX 11 22 {ECO:0000244|PDB:3F9T}. FT HELIX 28 30 {ECO:0000244|PDB:3F9T}. FT HELIX 44 52 {ECO:0000244|PDB:3F9T}. FT HELIX 60 62 {ECO:0000244|PDB:3F9T}. FT HELIX 64 80 {ECO:0000244|PDB:3F9T}. FT STRAND 87 92 {ECO:0000244|PDB:3F9T}. FT HELIX 94 114 {ECO:0000244|PDB:3F9T}. FT STRAND 124 128 {ECO:0000244|PDB:3F9T}. FT HELIX 134 142 {ECO:0000244|PDB:3F9T}. FT STRAND 145 149 {ECO:0000244|PDB:3F9T}. FT STRAND 155 157 {ECO:0000244|PDB:3F9T}. FT HELIX 159 168 {ECO:0000244|PDB:3F9T}. FT STRAND 173 179 {ECO:0000244|PDB:3F9T}. FT TURN 181 183 {ECO:0000244|PDB:3F9T}. FT HELIX 189 199 {ECO:0000244|PDB:3F9T}. FT STRAND 202 206 {ECO:0000244|PDB:3F9T}. FT HELIX 210 212 {ECO:0000244|PDB:3F9T}. FT HELIX 214 216 {ECO:0000244|PDB:3F9T}. FT HELIX 219 221 {ECO:0000244|PDB:3F9T}. FT HELIX 232 234 {ECO:0000244|PDB:3F9T}. FT STRAND 237 240 {ECO:0000244|PDB:3F9T}. FT TURN 243 247 {ECO:0000244|PDB:3F9T}. FT STRAND 254 260 {ECO:0000244|PDB:3F9T}. FT HELIX 261 266 {ECO:0000244|PDB:3F9T}. FT STRAND 274 279 {ECO:0000244|PDB:3F9T}. FT HELIX 289 326 {ECO:0000244|PDB:3F9T}. FT STRAND 331 333 {ECO:0000244|PDB:3F9T}. FT STRAND 336 343 {ECO:0000244|PDB:3F9T}. FT HELIX 347 356 {ECO:0000244|PDB:3F9T}. FT STRAND 365 373 {ECO:0000244|PDB:3F9T}. FT HELIX 380 393 {ECO:0000244|PDB:3F9T}. SQ SEQUENCE 396 AA; 45050 MW; 41CB8DEE45A8BBC0 CRC64; MRNMQEKGVS EKEILEELKK YRSLDLKYED GNIFGSMCSN VLPITRKIVD IFLETNLGDP GLFKGTKLLE EKAVALLGSL LNNKDAYGHI VSGGTEANLM ALRCIKNIWR EKRRKGLSKN EHPKIIVPIT AHFSFEKGRE MMDLEYIYAP IKEDYTIDEK FVKDAVEDYD VDGIIGIAGT TELGTIDNIE ELSKIAKENN IYIHVDAAFG GLVIPFLDDK YKKKGVNYKF DFSLGVDSIT IDPHKMGHCP IPSGGILFKD IGYKRYLDVD APYLTETRQA TILGTRVGFG GACTYAVLRY LGREGQRKIV NECMENTLYL YKKLKENNFK PVIEPILNIV AIEDEDYKEV CKKLRDRGIY VSVCNCVKAL RIVVMPHIKR EHIDNFIEIL NSIKRD // ID MJK2_METJA Reviewed; 343 AA. AC Q58752; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 99. DE RecName: Full=Probable potassium channel protein 2; DE AltName: Full=MjK2; GN OrderedLocusNames=MJ1357; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12860407; DOI=10.1016/S0014-5793(03)00706-3; RA Hellmer J., Zeilinger C.; RT "MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ RT sensitivity in E. coli."; RL FEBS Lett. 547:165-169(2003). CC -!- FUNCTION: Probable potassium channel protein. CC {ECO:0000269|PubMed:12860407}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 RCK C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99365.1; -; Genomic_DNA. DR PIR; D64469; D64469. DR ProteinModelPortal; Q58752; -. DR STRING; 243232.MJ_1357; -. DR EnsemblBacteria; AAB99365; AAB99365; MJ_1357. DR KEGG; mja:MJ_1357; -. DR eggNOG; arCOG01958; Archaea. DR eggNOG; COG1226; LUCA. DR InParanoid; Q58752; -. DR KO; K10716; -. DR OMA; GIHIAKG; -. DR PhylomeDB; Q58752; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR013099; K_chnl_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF07885; Ion_trans_2; 1. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Potassium; Potassium channel; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 343 Probable potassium channel protein 2. FT /FTId=PRO_0000054100. FT TOPO_DOM 1 7 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TOPO_DOM 29 61 Extracellular. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TOPO_DOM 83 343 Cytoplasmic. {ECO:0000255}. FT DOMAIN 109 234 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 253 338 RCK C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. FT MOTIF 46 51 Selectivity filter. {ECO:0000250}. SQ SEQUENCE 343 AA; 38884 MW; 61231B0C001B54C4 CRC64; METSKKLVIV AVLSITLILT YAYLISIIEG VDYFTALYFS VITITTTGYG DFTPKTFLGR TLTVVYLCVG VGIVMYLFSL IAEFIVEGKF EEFVRLKKMK NKIKTLKDHY IICGYGRLGK VVGEKFIEEN IPFIAIDINE DVLKEEYEKY PDKFLYIVGD AKKEEVLKKA KIDKAKGLIA TLPSDADNVF LTLTARELNP NILITAKADE KEAIRKLKIA GANRVVSPYL IGGLRMAEVS VRPGILDFLS TFIKIAKDEY EEDIELRKFV IEKDSELAYK SLKDANIRGK TGATILGIRR EKEFCINPYP EFILKPGDVI YAFGTEENLK YLENLVKKKK KKL // ID MOBA_METJA Reviewed; 204 AA. AC Q59057; DT 21-FEB-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Probable molybdenum cofactor guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE Short=MoCo guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE EC=2.7.7.77 {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=GTP:molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Mo-MPT guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin guanylyltransferase {ECO:0000255|HAMAP-Rule:MF_00316}; DE AltName: Full=Molybdopterin-guanine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_00316}; DE Short=MGD synthase {ECO:0000255|HAMAP-Rule:MF_00316}; GN Name=mobA {ECO:0000255|HAMAP-Rule:MF_00316}; OrderedLocusNames=MJ1663; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Transfers a GMP moiety from GTP to Mo-molybdopterin (Mo- CC MPT) cofactor (Moco or molybdenum cofactor) to form Mo- CC molybdopterin guanine dinucleotide (Mo-MGD) cofactor. CC {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- CATALYTIC ACTIVITY: GTP + molybdenum cofactor = diphosphate + CC guanylyl molybdenum cofactor. {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00316}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00316}. CC -!- DOMAIN: The N-terminal domain determines nucleotide recognition CC and specific binding, while the C-terminal domain determines the CC specific binding to the target protein. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC -!- SIMILARITY: Belongs to the MobA family. {ECO:0000255|HAMAP- CC Rule:MF_00316}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99681.1; -; Genomic_DNA. DR PIR; E64507; E64507. DR ProteinModelPortal; Q59057; -. DR STRING; 243232.MJ_1663; -. DR EnsemblBacteria; AAB99681; AAB99681; MJ_1663. DR KEGG; mja:MJ_1663; -. DR eggNOG; arCOG01872; Archaea. DR eggNOG; COG0746; LUCA. DR InParanoid; Q59057; -. DR KO; K03752; -. DR OMA; KHENGYI; -. DR PhylomeDB; Q59057; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0061603; F:molybdenum cofactor guanylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.550.10; -; 1. DR HAMAP; MF_00316; MobA; 1. DR InterPro; IPR025877; MobA-like_NTP_Trfase. DR InterPro; IPR013482; Molybde_CF_guanTrfase. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF12804; NTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Magnesium; Metal-binding; KW Molybdenum cofactor biosynthesis; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 204 Probable molybdenum cofactor FT guanylyltransferase. FT /FTId=PRO_0000134928. FT NP_BIND 10 12 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT METAL 104 104 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00316}. FT BINDING 22 22 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 75 75 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. FT BINDING 104 104 GTP. {ECO:0000255|HAMAP-Rule:MF_00316}. SQ SEQUENCE 204 AA; 23352 MW; BB5C5641ACEB7E84 CRC64; MVTIIAGIIL SGGKGERIGG KKPFRVFNGK YLINYPSDIL KSLNIPFVTV FAKNSIDLEM EKEYLTKYKC LISFDLIEGK GPLMGILCGM RVLNAKWFVV LPCDCPYINK EALKKLISNI SIAEKNNNLC IIPKHENGYI EPLFALYKRD ALSILNKIIM EDKNLSIRYF ISYLNPLYIK AEELDESKRI FKNINTIEEL MDNE // ID MFNB_METJA Reviewed; 235 AA. AC Q58499; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 87. DE RecName: Full=(5-formylfuran-3-yl)methyl phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000305}; DE EC=4.2.3.153 {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000269|PubMed:25905665}; DE AltName: Full=4-(hydroxymethyl)-2-furancarboxaldehyde-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000303|PubMed:25905665}; DE Short=4-HFC-P synthase {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000303|PubMed:24977328}; GN Name=mfnB {ECO:0000255|HAMAP-Rule:MF_00681, GN ECO:0000303|PubMed:24977328}; OrderedLocusNames=MJ1099; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND PATHWAY. RX PubMed=24977328; DOI=10.1021/bi500615p; RA Miller D., Wang Y., Xu H., Harich K., White R.H.; RT "Biosynthesis of the 5-(aminomethyl)-3-furanmethanol moiety of RT methanofuran."; RL Biochemistry 53:4635-4647(2014). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, REACTION RP MECHANISM, PATHWAY, ACTIVE SITE, AND MUTAGENESIS OF ASP-25; LYS-27; RP LYS-85; ASP-151 AND LYS-155. RX PubMed=25905665; DOI=10.1021/acs.biochem.5b00176; RA Wang Y., Jones M.K., Xu H., Ray W.K., White R.H.; RT "Mechanism of the enzymatic synthesis of 4-(hydroxymethyl)-2- RT furancarboxaldehyde-phosphate (4-HFC-P) from glyceraldehyde-3- RT phosphate catalyzed by 4-HFC-P synthase."; RL Biochemistry 54:2997-3008(2015). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS), AND SUBUNIT. RX PubMed=25372812; DOI=10.1107/S2053230X1402130X; RA Bobik T.A., Morales E.J., Shin A., Cascio D., Sawaya M.R., Arbing M., RA Yeates T.O., Rasche M.E.; RT "Structure of the methanofuran/methanopterin-biosynthetic enzyme RT MJ1099 from Methanocaldococcus jannaschii."; RL Acta Crystallogr. F 70:1472-1479(2014). CC -!- FUNCTION: Catalyzes the formation of 4-(hydroxymethyl)-2- CC furancarboxaldehyde phosphate (4-HFC-P) from two molecules of CC glyceraldehyde-3-P (GA-3-P). {ECO:0000255|HAMAP-Rule:MF_00681, CC ECO:0000269|PubMed:24977328, ECO:0000269|PubMed:25905665}. CC -!- CATALYTIC ACTIVITY: 2 D-glyceraldehyde 3-phosphate = (5- CC formylfuran-3-yl)methyl phosphate + phosphate + 2 H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000269|PubMed:25905665}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Note=kcat is 0.026 sec(-1). {ECO:0000269|PubMed:25905665}; CC pH dependence: CC Optimum pH is 7.0. {ECO:0000269|PubMed:25905665}; CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00681, ECO:0000269|PubMed:24977328, CC ECO:0000269|PubMed:25905665}. CC -!- SUBUNIT: Homohexamer. Trimer of dimers. CC {ECO:0000269|PubMed:25372812}. CC -!- SIMILARITY: Belongs to the MfnB family. {ECO:0000255|HAMAP- CC Rule:MF_00681}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99102.1; -; Genomic_DNA. DR PIR; B64437; B64437. DR PDB; 4RC1; X-ray; 2.40 A; A/B/C/D/E/F/G/H/I=1-235. DR PDB; 4U9P; X-ray; 1.70 A; A/B/C=1-235. DR PDBsum; 4RC1; -. DR PDBsum; 4U9P; -. DR ProteinModelPortal; Q58499; -. DR STRING; 243232.MJ_1099; -. DR DNASU; 1451996; -. DR EnsemblBacteria; AAB99102; AAB99102; MJ_1099. DR KEGG; mja:MJ_1099; -. DR eggNOG; arCOG04482; Archaea. DR eggNOG; COG1891; LUCA. DR InParanoid; Q58499; -. DR KO; K09733; -. DR OMA; YKPGTAS; -. DR PhylomeDB; Q58499; -. DR UniPathway; UPA00080; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:2001120; P:methanofuran biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00681; MfnB; 1. DR InterPro; IPR007565; 4-HFC-P_synthase. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF04476; DUF556; 1. DR PIRSF; PIRSF015957; UCP015957; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Reference proteome; KW Schiff base. FT CHAIN 1 235 (5-formylfuran-3-yl)methyl phosphate FT synthase. FT /FTId=PRO_0000134865. FT ACT_SITE 27 27 Schiff-base intermediate with substrate. FT {ECO:0000255|HAMAP-Rule:MF_00681, FT ECO:0000305|PubMed:25905665}. FT ACT_SITE 85 85 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00681, FT ECO:0000305|PubMed:25905665}. FT MUTAGEN 25 25 D->N: Lack of activity. FT {ECO:0000269|PubMed:25905665}. FT MUTAGEN 27 27 K->R: Lack of activity. FT {ECO:0000269|PubMed:25905665}. FT MUTAGEN 85 85 K->R: Lack of activity. FT {ECO:0000269|PubMed:25905665}. FT MUTAGEN 151 151 D->N: Lack of activity. FT {ECO:0000269|PubMed:25905665}. FT MUTAGEN 155 155 K->R: Almost no change in activity. FT {ECO:0000269|PubMed:25905665}. FT STRAND 2 5 {ECO:0000244|PDB:4U9P}. FT HELIX 10 19 {ECO:0000244|PDB:4U9P}. FT STRAND 22 26 {ECO:0000244|PDB:4U9P}. FT HELIX 29 31 {ECO:0000244|PDB:4U9P}. FT HELIX 39 48 {ECO:0000244|PDB:4U9P}. FT STRAND 53 62 {ECO:0000244|PDB:4U9P}. FT HELIX 66 78 {ECO:0000244|PDB:4U9P}. FT STRAND 82 88 {ECO:0000244|PDB:4U9P}. FT HELIX 94 111 {ECO:0000244|PDB:4U9P}. FT STRAND 115 122 {ECO:0000244|PDB:4U9P}. FT HELIX 125 127 {ECO:0000244|PDB:4U9P}. FT HELIX 133 135 {ECO:0000244|PDB:4U9P}. FT HELIX 136 143 {ECO:0000244|PDB:4U9P}. FT STRAND 146 151 {ECO:0000244|PDB:4U9P}. FT HELIX 160 163 {ECO:0000244|PDB:4U9P}. FT HELIX 166 178 {ECO:0000244|PDB:4U9P}. FT STRAND 182 185 {ECO:0000244|PDB:4U9P}. FT HELIX 191 193 {ECO:0000244|PDB:4U9P}. FT HELIX 194 199 {ECO:0000244|PDB:4U9P}. FT STRAND 203 208 {ECO:0000244|PDB:4U9P}. FT HELIX 209 211 {ECO:0000244|PDB:4U9P}. FT STRAND 212 214 {ECO:0000244|PDB:4RC1}. FT TURN 217 219 {ECO:0000244|PDB:4RC1}. FT HELIX 224 233 {ECO:0000244|PDB:4U9P}. SQ SEQUENCE 235 AA; 25099 MW; 9F425AC7C6096E85 CRC64; MILLVSPIDV EEAKEAIAGG ADIIDVKNPK EGSLGANFPW MIKAIREVTP KDLLVSATVG DVPYKPGTIS LAAVGAAISG ADYIKVGLYG VKNYYQAVEL MKNVVRAVKD IDENKIVVAA GYADAYRVGA VEPLIVPKIA RDAGCDVAML DTAIKDGKTL FDFQSKEILA EFVDEAHSYG LKCALAGSIK KEHIPILKEI GTDIVGVRGA ACKGGDRNNG RIDRELVKEL KELCK // ID MFNF_METJA Reviewed; 330 AA. AC Q58250; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=4-[[4-(2-aminoethyl)phenoxy]-methyl]-2-furanmethanamine-glutamate synthase {ECO:0000305}; DE Short=APMF-Glu synthase {ECO:0000305}; DE EC=6.1.-.- {ECO:0000269|PubMed:26100040}; GN Name=mfnF {ECO:0000303|PubMed:26100040}; OrderedLocusNames=MJ0840; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=26100040; DOI=10.1128/JB.00401-15; RA Wang Y., Xu H., Jones M.K., White R.H.; RT "Identification of the final two genes functioning in methanofuran RT biosynthesis in Methanocaldococcus jannaschii."; RL J. Bacteriol. 197:2850-2858(2015). CC -!- FUNCTION: Catalyzes the condensation between 5-(aminomethyl)-3- CC furanmethanol diphosphate (F1-PP) and gamma-glutamyltyramine to CC produce APMF-Glu. {ECO:0000269|PubMed:26100040}. CC -!- CATALYTIC ACTIVITY: gamma-glutamyltyramine + 5-(aminomethyl)-3- CC furanmethanol diphosphate = 4-[[4-(2-aminoethyl)phenoxy]-methyl]- CC 2-furanmethanamine-glutamate + diphosphate. CC {ECO:0000269|PubMed:26100040}. CC -!- PATHWAY: Cofactor biosynthesis; methanofuran biosynthesis. CC {ECO:0000305|PubMed:26100040}. CC -!- SIMILARITY: Belongs to the MfnF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98845.1; -; Genomic_DNA. DR PIR; H64404; H64404. DR ProteinModelPortal; Q58250; -. DR SMR; Q58250; 4-328. DR STRING; 243232.MJ_0840; -. DR EnsemblBacteria; AAB98845; AAB98845; MJ_0840. DR KEGG; mja:MJ_0840; -. DR eggNOG; arCOG04369; Archaea. DR eggNOG; COG1548; LUCA. DR InParanoid; Q58250; -. DR KO; K07072; -. DR OMA; GGANTKI; -. DR PhylomeDB; Q58250; -. DR UniPathway; UPA00080; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR InterPro; IPR002821; Hydantoinase_A. DR InterPro; IPR002756; MfnF. DR Pfam; PF01968; Hydantoinase_A; 1. DR TIGRFAMs; TIGR03123; one_C_unchar_1; 1. PE 1: Evidence at protein level; KW Complete proteome; Ligase; Reference proteome. FT CHAIN 1 330 4-[[4-(2-aminoethyl)phenoxy]-methyl]-2- FT furanmethanamine-glutamate synthase. FT /FTId=PRO_0000107076. SQ SEQUENCE 330 AA; 37377 MW; 5A3EAA6D2125D829 CRC64; MKIMILGIDI GGANTKITEI EGDNYKIHHI YFPMWKKKDE LEDLLKNYND NVDYVALVMT AELADCYKTK KEGVEDIIDK VEKAFNCPVY VFDVNGNFLT SEEAKKNYLD VSASNWNATA KFVAEFIKDS CILVDMGSTT TDIIPIKDKE VLAEKTDLDR LMNNQLVYVG TLRTPVSFLA NKIEFRGKLT NLSSEYFAIT ADISLILNKI TEEDYTCDTP DGAGKDFESC LTRLVRVLCA DREMVKDDEL IDFANKLYNK LLELIRENVD TIAKRYNLND VVITGLGEEI LKDALDEYNI ISIKETYGKD VSLATPSFAV AKLLQKQLDK // ID MPTD_METJA Reviewed; 121 AA. AC Q57851; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 86. DE RecName: Full=Dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:24982305}; DE Short=DHNA {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:22931285}; DE EC=4.1.2.25 {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000269|PubMed:22931285, ECO:0000269|PubMed:24982305}; DE AltName: Full=7,8-dihydroneopterin aldolase {ECO:0000255|HAMAP-Rule:MF_02130, ECO:0000303|PubMed:22931285}; GN Name=mptD {ECO:0000255|HAMAP-Rule:MF_02130}; OrderedLocusNames=MJ0408; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND PATHWAY. RX PubMed=22931285; DOI=10.1021/cb300342u; RA Crecy-Lagard V.D., Phillips G., Grochowski L.L., Yacoubi B.E., RA Jenney F., Adams M.W., Murzin A.G., White R.H.; RT "Comparative genomics guided discovery of two missing archaeal enzyme RT families involved in the biosynthesis of the pterin moiety of RT tetrahydromethanopterin and tetrahydrofolate."; RL ACS Chem. Biol. 7:1807-1816(2012). RN [3] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF RP GLU-25; HIS-35; GLN-61; TYR-78 AND TYR-111. RX PubMed=24982305; DOI=10.1128/JB.01812-14; RA Wang Y., Xu H., Grochowski L.L., White R.H.; RT "Biochemical characterization of a dihydroneopterin aldolase used for RT methanopterin biosynthesis in methanogens."; RL J. Bacteriol. 196:3191-3198(2014). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS) OF 2-121 IN COMPLEX WITH PTERIN RP ANALOG, AND SUBUNIT. RG New York structural genomix research consortium (NYSGXRC); RT "Crystal structure of hypothetical protein MJ0408 from Methanococcus RT jannaschii."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin (H2Neo) CC to 6-hydroxymethyl-7,8-dihydropterin (6-HMD). {ECO:0000255|HAMAP- CC Rule:MF_02130, ECO:0000269|PubMed:22931285}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin = 6-hydroxymethyl-7,8- CC dihydropterin + glycolaldehyde. {ECO:0000255|HAMAP-Rule:MF_02130, CC ECO:0000269|PubMed:22931285, ECO:0000269|PubMed:24982305}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=64.5 uM for 7,8-dihydroneopterin (at 25 degrees Celsius) CC {ECO:0000269|PubMed:24982305}; CC KM=9.9 uM for 7,8-dihydroneopterin (at 70 degrees Celsius) CC {ECO:0000269|PubMed:24982305}; CC Note=kcat is 0.07 sec(-1) at 25 degrees Celsius. kcat is 1.0 CC sec(-1) at 70 degrees Celsius. {ECO:0000269|PubMed:24982305}; CC pH dependence: CC Optimum pH is 8.3. {ECO:0000269|PubMed:24982305}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02130, CC ECO:0000269|PubMed:22931285}. CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_02130, CC ECO:0000269|Ref.4}. CC -!- SIMILARITY: Belongs to the archaeal dihydroneopterin aldolase CC family. {ECO:0000255|HAMAP-Rule:MF_02130}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98398.1; -; Genomic_DNA. DR PIR; H64350; H64350. DR PDB; 2OGF; X-ray; 1.89 A; A/B/C/D=2-121. DR PDBsum; 2OGF; -. DR ProteinModelPortal; Q57851; -. DR SMR; Q57851; 1-121. DR STRING; 243232.MJ_0408; -. DR EnsemblBacteria; AAB98398; AAB98398; MJ_0408. DR KEGG; mja:MJ_0408; -. DR eggNOG; arCOG04705; Archaea. DR eggNOG; COG2098; LUCA. DR InParanoid; Q57851; -. DR KO; K09739; -. DR OMA; MKNQPCV; -. DR PhylomeDB; Q57851; -. DR BioCyc; MetaCyc:MONOMER-17933; -. DR UniPathway; UPA00065; -. DR EvolutionaryTrace; Q57851; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004150; F:dihydroneopterin aldolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:2001118; P:tetrahydromethanopterin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1300.20; -; 1. DR HAMAP; MF_02130; DHNA_arch; 1. DR InterPro; IPR027508; DHN_aldolase_MptD. DR InterPro; IPR007181; MtpD_C. DR InterPro; IPR007179; MtpD_N. DR Pfam; PF04038; DHNA; 1. DR ProDom; PD027636; DUF372; 1. DR SUPFAM; SSF143560; SSF143560; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Reference proteome. FT CHAIN 1 121 Dihydroneopterin aldolase. FT /FTId=PRO_0000106857. FT BINDING 25 25 Substrate. {ECO:0000305|Ref.4}. FT BINDING 114 114 Substrate; via amide nitrogen and FT carbonyl oxygen. {ECO:0000305|Ref.4}. FT MUTAGEN 25 25 E->Q: Has 25-fold higher Km towards 7,8- FT dihydroneopterin than wild-type. FT {ECO:0000269|PubMed:24982305}. FT MUTAGEN 35 35 H->N: Has 20-fold lower kcat than wild- FT type. {ECO:0000269|PubMed:24982305}. FT MUTAGEN 61 61 Q->A: Has 20-fold lower kcat than wild- FT type. {ECO:0000269|PubMed:24982305}. FT MUTAGEN 78 78 Y->F: Has 20-fold lower kcat than wild- FT type. {ECO:0000269|PubMed:24982305}. FT MUTAGEN 111 111 Y->F: Has 2-fold lower kcat than wild- FT type. {ECO:0000269|PubMed:24982305}. FT HELIX 3 5 {ECO:0000244|PDB:2OGF}. FT HELIX 7 11 {ECO:0000244|PDB:2OGF}. FT TURN 12 15 {ECO:0000244|PDB:2OGF}. FT HELIX 18 37 {ECO:0000244|PDB:2OGF}. FT TURN 44 46 {ECO:0000244|PDB:2OGF}. FT HELIX 47 59 {ECO:0000244|PDB:2OGF}. FT STRAND 64 71 {ECO:0000244|PDB:2OGF}. FT HELIX 83 85 {ECO:0000244|PDB:2OGF}. FT STRAND 86 94 {ECO:0000244|PDB:2OGF}. FT STRAND 97 106 {ECO:0000244|PDB:2OGF}. FT HELIX 107 109 {ECO:0000244|PDB:2OGF}. FT STRAND 111 120 {ECO:0000244|PDB:2OGF}. SQ SEQUENCE 121 AA; 14182 MW; 281669A0B3616F73 CRC64; MRVEETEVFK KYFKNLTDRE RAVFEGGITL GALFHQFVGT PVSKYNKESL ERAIEEAMKN QPCVYDIKVK IRNVGEKYVS LDGKMLDVDL KIKINKTVAH LKLEYIPEID YPLMYVKKFE E // ID MPTN_METJA Reviewed; 291 AA. AC Q58037; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Tetrahydromethanopterin:alpha-L-glutamate ligase; DE EC=6.3.2.33; DE AltName: Full=H(4)MPT:alpha-L-glutamate ligase; GN Name=mptN; OrderedLocusNames=MJ0620; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12909715; DOI=10.1073/pnas.1733391100; RA Li H., Xu H., Graham D.E., White R.H.; RT "Glutathione synthetase homologs encode alpha-L-glutamate ligases for RT methanogenic coenzyme F420 and tetrahydrosarcinapterin biosyntheses."; RL Proc. Natl. Acad. Sci. U.S.A. 100:9785-9790(2003). CC -!- FUNCTION: Catalyzes the ATP or GTP-dependent addition of one L- CC glutamate molecule to tetrahydromethanopterin, producing CC tetrahydrosarcinapterin. {ECO:0000269|PubMed:12909715}. CC -!- CATALYTIC ACTIVITY: ATP + tetrahydromethanopterin + L-glutamate = CC ADP + phosphate + 5,6,7,8-tetrahydrosarcinapterin. CC {ECO:0000269|PubMed:12909715}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydrosarcinapterin CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12909715}. CC -!- SIMILARITY: Belongs to the RimK family. MptN subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98615.1; -; Genomic_DNA. DR PIR; D64377; D64377. DR ProteinModelPortal; Q58037; -. DR STRING; 243232.MJ_0620; -. DR EnsemblBacteria; AAB98615; AAB98615; MJ_0620. DR KEGG; mja:MJ_0620; -. DR eggNOG; arCOG01589; Archaea. DR eggNOG; COG0189; LUCA. DR InParanoid; Q58037; -. DR KO; K15740; -. DR OMA; NIELEVY; -. DR PhylomeDB; Q58037; -. DR BioCyc; MetaCyc:MONOMER-15293; -. DR BRENDA; 6.3.2.33; 3260. DR UniPathway; UPA00069; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006464; P:cellular protein modification process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013651; ATP-grasp_RimK-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR004666; RpS6_RimK/Lys_biosynth_LsyX. DR Pfam; PF08443; RimK; 1. DR TIGRFAMs; TIGR00768; rimK_fam; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; GTP-binding; Ligase; Magnesium; KW Manganese; Metal-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 291 Tetrahydromethanopterin:alpha-L-glutamate FT ligase. FT /FTId=PRO_0000205502. FT DOMAIN 101 286 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT NP_BIND 175 187 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT METAL 247 247 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 259 259 Magnesium or manganese 1. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 259 259 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT METAL 261 261 Magnesium or manganese 2. FT {ECO:0000255|PROSITE-ProRule:PRU00409}. FT BINDING 136 136 ATP. {ECO:0000250}. FT BINDING 203 203 ATP. {ECO:0000250}. SQ SEQUENCE 291 AA; 33277 MW; 2B6A3438290A3B0E CRC64; MKLGIITIER DAVVNDLIKS CEKYEVDYKV ITPSNIVAGF NLDFKLKYYK SFLDELDCCF VRNLGWDSFF RFDVLKYLNH YIPVINPPDG IDRASNKFLT SVFLELNNLP QPKTVVTESI NEAIVWIDKF EEAVLKPIFG CGGEGIVRVK KELPISTKLK ILNEFKEKYN TFYIQEFIKP VRNEHRDIRA FVVDDEVVAA MYRIGGENWK NNVSQGGRVE KCEITEEIEK LALKAKNALG LFYAGVDLIE SEDGLKVLEV NSTPSWIGLS KVSEVNIADK LLEKIIQYVK S // ID MSMJS_METJA Reviewed; 350 AA. AC Q57634; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Small-conductance mechanosensitive channel MscMJ; GN OrderedLocusNames=MJ0170; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A MECHANOSENSITIVE CHANNEL, AND SUBCELLULAR LOCATION. RX PubMed=11159397; DOI=10.1016/S0006-3495(01)76009-2; RA Kloda A., Martinac B.; RT "Molecular identification of a mechanosensitive channel in archaea."; RL Biophys. J. 80:229-240(2001). CC -!- FUNCTION: Small-conductance mechanosensitive channel that opens in CC response to stretch forces in the membrane lipid bilayer. Exhibits CC a sixfold preference for cations over anions. Non-rectifying. CC {ECO:0000269|PubMed:11159397}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11159397}; CC Multi-pass membrane protein {ECO:0000269|PubMed:11159397}. CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98155.1; -; Genomic_DNA. DR PIR; C64321; C64321. DR ProteinModelPortal; Q57634; -. DR STRING; 243232.MJ_0170; -. DR TCDB; 1.A.23.4.2; the small conductance mechanosensitive ion channel (mscs) family. DR EnsemblBacteria; AAB98155; AAB98155; MJ_0170. DR KEGG; mja:MJ_0170; -. DR eggNOG; arCOG01568; Archaea. DR eggNOG; COG0668; LUCA. DR InParanoid; Q57634; -. DR KO; K16052; -. DR OMA; DLRVEYF; -. DR PhylomeDB; Q57634; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR011066; MscC_channel_C. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR006686; MscS_channel_CS. DR InterPro; IPR011014; MscS_channel_TM-2. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82689; SSF82689; 1. DR SUPFAM; SSF82861; SSF82861; 1. DR PROSITE; PS01246; UPF0003; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 350 Small-conductance mechanosensitive FT channel MscMJ. FT /FTId=PRO_0000110253. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. SQ SEQUENCE 350 AA; 39953 MW; 4EA0E5025086E7DF CRC64; MNMEIFGNSI SNILIFVVIT LLGIFIGKIV DKIVRNYLKK IIDKTKTKFD DIILESIDLP IIVLVVTLFF YFGLRFLILP DYILKLIDEA VKVVVILSAT YFAVKFIDGI FEHYLIPLTE KTETELDEHI IKPLKKVVKI LTILLGILTA LSSVGYDITA LLAGLGVGGL ALALAMQDTI KNFIAGILIL IDKPFSLGHW VKVKGAEGIV EEIGIRSTRI RTFDYTLITI PNSELLDSAI ENLTVRDRRR VLMTIGLTYN TPVEKIKRAK EIIKEIVENH PATLPPYRVH FREYGDWSLN LRVEYFVRNM GFDYYLNAVD EINLKIKEEF EKEGIEMAFP TYTVYLEKDN // ID MJK1_METJA Reviewed; 333 AA. AC Q57604; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 107. DE RecName: Full=Potassium channel protein 1; DE AltName: Full=MjK1; GN OrderedLocusNames=MJ0138.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12860407; DOI=10.1016/S0014-5793(03)00706-3; RA Hellmer J., Zeilinger C.; RT "MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ RT sensitivity in E. coli."; RL FEBS Lett. 547:165-169(2003). CC -!- FUNCTION: Potassium channel protein. Seems to conduct potassium at CC low membrane potentials. {ECO:0000269|PubMed:12860407}. CC -!- SUBUNIT: Homotetramer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- MISCELLANEOUS: Inhibited by barium and cesium. CC -!- SIMILARITY: Contains 1 RCK C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98130.1; -; Genomic_DNA. DR PIR; D64317; D64317. DR ProteinModelPortal; Q57604; -. DR STRING; 243232.MJ_0138.1; -. DR TCDB; 1.A.1.13.8; the voltage-gated ion channel (vic) superfamily. DR EnsemblBacteria; AAB98130; AAB98130; MJ_0138.1. DR KEGG; mja:MJ_0138.1; -. DR eggNOG; arCOG01960; Archaea. DR eggNOG; COG1226; LUCA. DR InParanoid; Q57604; -. DR KO; K10716; -. DR OMA; IYAFGTK; -. DR PhylomeDB; Q57604; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005267; F:potassium channel activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR003280; 2pore_dom_K_chnl. DR InterPro; IPR013099; K_chnl_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF07885; Ion_trans_2; 1. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR PRINTS; PR01333; 2POREKCHANEL. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Potassium; Potassium channel; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 333 Potassium channel protein 1. FT /FTId=PRO_0000054099. FT TOPO_DOM 1 6 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TOPO_DOM 28 60 Extracellular. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TOPO_DOM 82 333 Cytoplasmic. {ECO:0000255}. FT DOMAIN 109 233 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 246 331 RCK C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. FT MOTIF 46 51 Selectivity filter. {ECO:0000250}. SQ SEQUENCE 333 AA; 37150 MW; 7CC082675F96B06A CRC64; METYEKIELG IIVIILLILI ESVILMTVEG WDFFTAFYTA VVTISTVGYG DYTPQTFLGK LSVIIYIFAG VGAVAYTMGN IASFFIEGHF RKYFRLRKMM DRIKKLNNHY IICGYGRLGK VIAEEFKKCN IPFVIIDSDE KLLEEALEKD PNLICIVGDA TSDDILKKAK IEKAKGLISV VSSDAENVFI TLSAKKLNPN IYIVAKAEKP STLDKLIKAG ADRAVCPYIV GGMEIARIAI NPDIVEFIHS LVATEEDMEV RRYIVKNKEL DNKLLKDSGI REKTGATILA VKKGDKTITS PPPDTVINIG DIIYAFGTKE QLEKLKRYVE GVE // ID MOBB_METJA Reviewed; 234 AA. AC Q58720; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Putative molybdopterin-guanine dinucleotide biosynthesis adapter protein; DE Short=MGD biosynthesis adapter protein; DE AltName: Full=Molybdenum cofactor biosynthesis adapter protein; DE Short=Moco biosynthesis adapter protein; GN Name=mobB; OrderedLocusNames=MJ1324; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: GTP-binding protein that is not required for the CC biosynthesis of Mo-molybdopterin guanine dinucleotide (Mo-MGD) CC cofactor, and not necessary for the formation of active CC molybdoenzymes using this form of molybdenum cofactor. May act as CC an adapter protein to achieve the efficient biosynthesis and CC utilization of MGD. Displays a weak intrinsic GTPase activity (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MobB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99333.1; -; Genomic_DNA. DR PIR; C64465; C64465. DR ProteinModelPortal; Q58720; -. DR STRING; 243232.MJ_1324; -. DR EnsemblBacteria; AAB99333; AAB99333; MJ_1324. DR KEGG; mja:MJ_1324; -. DR eggNOG; arCOG00532; Archaea. DR eggNOG; COG1763; LUCA. DR InParanoid; Q58720; -. DR KO; K03753; -. DR OMA; HCGYNCK; -. DR PhylomeDB; Q58720; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR007202; 4Fe-4S_dom. DR InterPro; IPR004435; MobB_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04060; FeS; 1. DR Pfam; PF03205; MobB; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00176; mobB; 1. DR PROSITE; PS51656; 4FE4S; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 234 Putative molybdopterin-guanine FT dinucleotide biosynthesis adapter FT protein. FT /FTId=PRO_0000107276. FT DOMAIN 134 196 4Fe-4S. FT NP_BIND 11 15 GTP. {ECO:0000250}. FT NP_BIND 42 45 GTP. {ECO:0000255}. FT NP_BIND 86 89 GTP. {ECO:0000255}. SQ SEQUENCE 234 AA; 26080 MW; F79BB9B1642A5E1B CRC64; MRVIGVIGYK DSGKTTLIEE ILKHSDKKIA VIKHTKEDVE VDKKGTDTYR LSNAGAKITV LATDSKTVFF TDRMDLENIL SVLSDYNIDF VIIEGFKEAL KRLNIPKIVM LKDKDGSDLI DDHTAMIIED YNYNIDDVLK VIYEKAVVPT MNLNCGHCGY NCRTFVKAVV KGEARWDDCV LAKGIKIIVD GKIIPAVPFV SKIVGSTIKA MIETLKGVDN PKTIKVEIDV SKLK // ID MPTA_METJA Reviewed; 313 AA. AC Q58185; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 11-NOV-2015, entry version 89. DE RecName: Full=GTP cyclohydrolase MptA; DE EC=3.5.4.39; DE AltName: Full=GTP cyclohydrolase IV; GN Name=mptA; OrderedLocusNames=MJ0775; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, COFACTOR, SUBSTRATE RP SPECIFICITY, ENZYME REGULATION, REACTION MECHANISM, MUTAGENESIS OF RP GLU-47; HIS-98; HIS-197; HIS-290 AND HIS-292, AND BIOPHYSICOCHEMICAL RP PROPERTIES. RX PubMed=17497938; DOI=10.1021/bi700052a; RA Grochowski L.L., Xu H., Leung K., White R.H.; RT "Characterization of an Fe(2+)-dependent archaeal-specific GTP RT cyclohydrolase, MptA, from Methanocaldococcus jannaschii."; RL Biochemistry 46:6658-6667(2007). CC -!- FUNCTION: Converts GTP to 7,8-dihydro-D-neopterin 2',3'-cyclic CC phosphate, the first intermediate in the biosynthesis of coenzyme CC methanopterin. It is also able to utilize a variety of GTP analogs CC as substrates, including GDP, beta,gamma-methylene-GTP and GTP- CC [gamma-thio]. {ECO:0000269|PubMed:17497938}. CC -!- CATALYTIC ACTIVITY: GTP + H(2)O = formate + 7,8-dihydro-D- CC neopterin 2',3'-cyclic phosphate + diphosphate. CC {ECO:0000269|PubMed:17497938}. CC -!- COFACTOR: CC Name=Cu(2+); Xref=ChEBI:CHEBI:29036; CC Evidence={ECO:0000269|PubMed:17497938}; CC Note=Binds 1 Fe(2+) ion per subunit. Mn(2+) and Zn(2+) can be used CC to a lesser extent, but not at a relevant physiological CC concentration. {ECO:0000269|PubMed:17497938}; CC -!- ENZYME REGULATION: Inhibited by GTP concentrations greater than CC 0.3 mM and by 2-amino-5-formylamino-6-ribofuranosylamino-4(3H)- CC pyrimidinone 5'-phosphate (fapyGMP). Partial inhibition is CC observed when 2 mM GMP, dGTP, or 7-methyl-GTP was included along CC with 2 mM GTP. {ECO:0000269|PubMed:17497938}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC Vmax=13 nmol/min/mg enzyme with GDP as substrate (at pH 7.2) CC {ECO:0000269|PubMed:17497938}; CC Vmax=30 nmol/min/mg enzyme with GTP as substrate (at pH 7.2) CC {ECO:0000269|PubMed:17497938}; CC Vmax=39 nmol/min/mg enzyme with GTP-[gamma-thio] as substrate CC (at pH 7.2) {ECO:0000269|PubMed:17497938}; CC Vmax=3 nmol/min/mg enzyme with beta,gamma-methylene-GTP as CC substrate (at pH 7.2) {ECO:0000269|PubMed:17497938}; CC Note=Other purine nucleotides including ATP, ITP, dGTP, GMP, and CC 7-methyl-GTP do not serve as substrates.; CC pH dependence: CC Optimum pH is 6.5. {ECO:0000269|PubMed:17497938}; CC Temperature dependence: CC MptA loses 27% activity when it incubates for 10 min at 80 CC degrees Celsius, 60% activity at 90 degrees Celsius, and 89% CC activity at 100 degrees Celsius. {ECO:0000269|PubMed:17497938}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17497938}. CC -!- MISCELLANEOUS: MptA is the archetype of a new class of GTP CC cyclohydrolases that catalyzes a series of reactions most similar CC to that seen with GTPCHI but unique in that the cyclic phosphate CC is the product. CC -!- SIMILARITY: Belongs to the GTP cyclohydrolase IV family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98765.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98765.1; ALT_INIT; Genomic_DNA. DR PIR; G64396; G64396. DR STRING; 243232.MJ_0775; -. DR DNASU; 1451652; -. DR EnsemblBacteria; AAB98765; AAB98765; MJ_0775. DR KEGG; mja:MJ_0775; -. DR eggNOG; arCOG04301; Archaea. DR eggNOG; COG1469; LUCA. DR InParanoid; Q58185; -. DR KO; K17488; -. DR OMA; PCSQGMS; -. DR PhylomeDB; Q58185; -. DR BioCyc; MetaCyc:MONOMER-14599; -. DR BRENDA; 3.5.4.39; 3260. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0044682; F:archaeal-specific GTP cyclohydrolase activity; IDA:MENGO. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01527_A; GTP_cyclohydrol_A; 1. DR InterPro; IPR003801; GTP_cyclohydrolase_FolE2/MptA. DR InterPro; IPR022840; GTP_cyclohydrolase_MptA. DR Pfam; PF02649; GCHY-1; 1. DR TIGRFAMs; TIGR00294; TIGR00294; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Iron; Manganese; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 313 GTP cyclohydrolase MptA. FT /FTId=PRO_0000147743. FT SITE 160 160 May be catalytically important. FT MUTAGEN 47 47 E->D: Unchanged. FT {ECO:0000269|PubMed:17497938}. FT MUTAGEN 98 98 H->N: Unchanged. FT {ECO:0000269|PubMed:17497938}. FT MUTAGEN 197 197 H->N: Strong decrease in specific FT activity. {ECO:0000269|PubMed:17497938}. FT MUTAGEN 290 290 H->N: Strong decrease in specific FT activity. {ECO:0000269|PubMed:17497938}. FT MUTAGEN 292 292 H->N: Strong decrease in specific FT activity. {ECO:0000269|PubMed:17497938}. SQ SEQUENCE 313 AA; 35873 MW; 4CCA67352C1773CF CRC64; MNWRCDVQNF EPDVKISLTR VGVTNLKKLV RLKRTNKRPI ILLSTFEVFV NLPSSQKGIH MSRNPEVIEG IIDEALELES YEMETICEEI VKRLFEKHEY ATEAEVFMVS DFMTKEKSPI SGKYSQEIHK IMGGAKGIKK DDEIELTKIV GAEVVGITAC PCAQNLIKEI CIKNLKEKGF SDEDIDKILD SVIFATHNQR GIGRIILEVP TGYDIEIMDI IEIIKKSMSA EIHGILKRAD EAYVVEQSHK NPKFVEDCVR EMAKRVVEKF KHLPDETKVL IRQINMESIH RHDAFAEKVA TLGELRRELL SYE // ID MPTB_METJA Reviewed; 249 AA. AC Q58247; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Dihydroneopterin 2',3'-cyclic phosphate phosphodiesterase; DE Short=H2N-cP phosphodiesterase; DE Short=H2Neo-cP phosphodiesterase; DE EC=3.1.4.56; DE AltName: Full=7,8-dihydro-D-neopterin 2',3'-cyclic phosphate phosphodiesterase; GN Name=mptB; OrderedLocusNames=MJ0837; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, GENE RP NAME, PATHWAY, PH DEPENDENCE, SUBUNIT, AND MUTAGENESIS OF HIS-61; RP HIS-96 AND ASP-167. RX PubMed=19746965; DOI=10.1021/bi9010336; RA Mashhadi Z., Xu H., White R.H.; RT "An Fe2+-dependent cyclic phosphodiesterase catalyzes the hydrolysis RT of 7,8-dihydro-D-neopterin 2',3'-cyclic phosphate in methanopterin RT biosynthesis."; RL Biochemistry 48:9384-9392(2009). CC -!- FUNCTION: Cyclic phosphodiesterase that hydrolyzes the cyclic CC phosphate of 7,8-dihydroneopterin 2',3'-cyclic phosphate (H2N-cP) CC and converts it to a mixture of 7,8-dihydroneopterin 2'-phosphate CC (H2N-2'P) and 7,8-dihydroneopterin 3'-phosphate (H2N-3'P). Is also CC able to utilize other phosphodiesters as substrates in vitro: CC hydrolysis of bis-pNPP and pNPPC produces nitrophenyl phosphate, CC and that of 2',3'-cAMP produces 3'-AMP. ATP, 3',5'-cAMP, GTP, CC 3',5'-cGMP, and 4',5'-cFMN can not serve as substrates. CC {ECO:0000269|PubMed:19746965}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 2',3'-cyclic phosphate + CC H(2)O = 7,8-dihydroneopterin 3'-phosphate. CC {ECO:0000269|PubMed:19746965}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 2',3'-cyclic phosphate + CC H(2)O = 7,8-dihydroneopterin 2'-phosphate. CC {ECO:0000269|PubMed:19746965}. CC -!- COFACTOR: CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; CC Evidence={ECO:0000269|PubMed:19746965}; CC Note=Binds 1 Fe(2+) ion per subunit. Since MptB requires Fe2(+) CC for activity, the Fe(2+) ion likely has a catalytic role. The CC enzyme is also active under high concentrations of Mn(2+) in CC vitro. {ECO:0000269|PubMed:19746965}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:19746965}; CC Note=Binds 1 Zn(2+) ion per subunit. The Zn(2+) ion is proposed to CC have a structural role. {ECO:0000269|PubMed:19746965}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5 with bis-pNPP as substrate. CC {ECO:0000269|PubMed:19746965}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000269|PubMed:19746965}. CC -!- SUBUNIT: Homododecamer. {ECO:0000269|PubMed:19746965}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98842.1; -; Genomic_DNA. DR PIR; E64404; E64404. DR ProteinModelPortal; Q58247; -. DR STRING; 243232.MJ_0837; -. DR EnsemblBacteria; AAB98842; AAB98842; MJ_0837. DR KEGG; mja:MJ_0837; -. DR eggNOG; arCOG01861; Archaea. DR eggNOG; COG3481; LUCA. DR KO; K17487; -. DR OMA; IRICQAR; -. DR PhylomeDB; Q58247; -. DR BioCyc; MetaCyc:MONOMER-16557; -. DR BRENDA; 3.1.4.56; 3260. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0044682; F:archaeal-specific GTP cyclohydrolase activity; IDA:MENGO. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Iron; Metal-binding; Reference proteome; KW Zinc. FT CHAIN 1 249 Dihydroneopterin 2',3'-cyclic phosphate FT phosphodiesterase. FT /FTId=PRO_0000107074. FT MUTAGEN 61 61 H->N: Large reduction in catalytic FT activity. {ECO:0000269|PubMed:19746965}. FT MUTAGEN 96 96 H->N: Slight reduction in catalytic FT activity with H2N-cP and 2',3'-cAMP as FT substrates, but 2-fold increase in FT activity with bis-pNPP. FT {ECO:0000269|PubMed:19746965}. FT MUTAGEN 167 167 D->N: Large reduction in catalytic FT activity. {ECO:0000269|PubMed:19746965}. SQ SEQUENCE 249 AA; 28523 MW; E8A59C478718E613 CRC64; MERLIKLAEQ IKDEELRKKV IEFLKNPKAT HPGIVDTGIS VEEAPASINW HHRYEGGLIE HTISVTKIAL KMADVLEEVY GVEVNRDYII AGALLHDIMK PYNYIRKEDG TFDHYDMFNL DHLTLAVAEL YKRDFPIEVI KIVASHHGDH SPTRPNSIEA YIVHYADEAD SKINDVAVRV CQARSRDLGI SEQEIYKAVN PLKVYEVRSR EGKLKTIEFL KDILKSIGII SEDEKKDENN ESLENKESN // ID MPTE_METJA Reviewed; 241 AA. AC Q59028; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=6-hydroxymethyl-7,8-dihydropterin pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131}; DE Short=HPPK {ECO:0000255|HAMAP-Rule:MF_02131}; DE EC=2.7.6.3 {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000269|PubMed:22931285}; DE AltName: Full=2-amino-4-hydroxy-6-hydroxymethyldihydropteridine pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131}; DE AltName: Full=6-hydroxymethyl-7,8-dihydropterin diphosphokinase {ECO:0000255|HAMAP-Rule:MF_02131}; DE Short=6-HMPDK {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000303|PubMed:22931285}; DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin diphosphokinase {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000303|PubMed:22931285}; DE AltName: Full=7,8-dihydro-6-hydroxymethylpterin pyrophosphokinase {ECO:0000255|HAMAP-Rule:MF_02131}; DE Short=PPPK {ECO:0000255|HAMAP-Rule:MF_02131}; GN Name=mptE {ECO:0000255|HAMAP-Rule:MF_02131, GN ECO:0000303|PubMed:22931285}; OrderedLocusNames=MJ1634; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, AND PATHWAY. RX PubMed=22931285; DOI=10.1021/cb300342u; RA Crecy-Lagard V.D., Phillips G., Grochowski L.L., Yacoubi B.E., RA Jenney F., Adams M.W., Murzin A.G., White R.H.; RT "Comparative genomics guided discovery of two missing archaeal enzyme RT families involved in the biosynthesis of the pterin moiety of RT tetrahydromethanopterin and tetrahydrofolate."; RL ACS Chem. Biol. 7:1807-1816(2012). CC -!- FUNCTION: Catalyzes the transfer of diphosphate from ATP to 6- CC hydroxymethyl-7,8-dihydropterin (6-HMD), leading to 6- CC hydroxymethyl-7,8-dihydropterin diphosphate (6-HMDP). CC {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000269|PubMed:22931285}. CC -!- CATALYTIC ACTIVITY: ATP + 6-hydroxymethyl-7,8-dihydropterin = AMP CC + 6-hydroxymethyl-7,8-dihydropterin diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_02131, ECO:0000269|PubMed:22931285}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02131}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_02131, CC ECO:0000269|PubMed:22931285}. CC -!- SIMILARITY: Belongs to the archaeal 6-HMPDK family. CC {ECO:0000255|HAMAP-Rule:MF_02131}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99656.1; -; Genomic_DNA. DR PIR; H64503; H64503. DR ProteinModelPortal; Q59028; -. DR STRING; 243232.MJ_1634; -. DR EnsemblBacteria; AAB99656; AAB99656; MJ_1634. DR KEGG; mja:MJ_1634; -. DR eggNOG; arCOG04303; Archaea. DR eggNOG; COG1634; LUCA. DR InParanoid; Q59028; -. DR KO; K07142; -. DR OMA; DGDRCCF; -. DR PhylomeDB; Q59028; -. DR BioCyc; MetaCyc:MONOMER-17934; -. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003848; F:2-amino-4-hydroxy-6-hydroxymethyldihydropteridine diphosphokinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004788; F:thiamine diphosphokinase activity; IEA:InterPro. DR GO; GO:2001118; P:tetrahydromethanopterin biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:InterPro. DR HAMAP; MF_02131; HMPDK_arch; 1. DR InterPro; IPR027510; HMPDK_MptE. DR InterPro; IPR002826; MptE-like. DR InterPro; IPR007371; TPK_catalytic. DR Pfam; PF01973; MAF_flag10; 1. DR SUPFAM; SSF63999; SSF63999; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 241 6-hydroxymethyl-7,8-dihydropterin FT pyrophosphokinase. FT /FTId=PRO_0000107449. SQ SEQUENCE 241 AA; 27581 MW; 7E7F2EBB4AC5DBAA CRC64; MDMKEWEIFY NKIMEDFGFD KDKDVESAVI LNNILENANT IPVDKLKDII EGREVFIFGA GPSIKKHINI LKELREINYK NPIIVADGAC KAFLEENIIP DIIVSDLDGD LEALFECNRK GSIIVVHAHG DNIEKIKKYV PKLKNVVGSC QIPNYKELNL RNVINFGGFT DGDRCCFLAY HFKAKKLILG GMDFGIYITK YSRPNIKEDI AIGDEIKIKK LEYAKTLINY LKDKIEIEFL K // ID MTM2_METJA Reviewed; 530 AA. AC Q58843; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Modification methylase MjaII; DE Short=M.MjaII; DE EC=2.1.1.113; DE AltName: Full=N-4 cytosine-specific methyltransferase MjaII; GN Name=mjaIIM; OrderedLocusNames=MJ1448; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GGNC, causes specific methylation on C-4 on both strands, and CC protects the DNA from cleavage by the MjaII endonuclease. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA cytosine = S- CC adenosyl-L-homocysteine + DNA N(4)-methylcytosine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC N(4) subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99457.1; -; Genomic_DNA. DR PIR; G64480; G64480. DR ProteinModelPortal; Q58843; -. DR STRING; 243232.MJ_1448; -. DR REBASE; 3896; M.MjaII. DR EnsemblBacteria; AAB99457; AAB99457; MJ_1448. DR KEGG; mja:MJ_1448; -. DR eggNOG; arCOG00890; Archaea. DR eggNOG; COG0863; LUCA. DR InParanoid; Q58843; -. DR OMA; EQHAYAY; -. DR PhylomeDB; Q58843; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 2. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 3. DR PROSITE; PS00093; N4_MTASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 530 Modification methylase MjaII. FT /FTId=PRO_0000087937. SQ SEQUENCE 530 AA; 63755 MW; FF6F29ADD080060C CRC64; MNLDAWLDIQ PAKKLYTIKE ASRILTKKFG KEIKEHNISY LVQYGRVNKY KIKNRVYVDI DEVENYYKKL FFEKRKEWEE KLGFKLDWDL AFDLLSEKER TKHVHGIHPY KGKFIPQLVE YFLKRHFNVG DIIIDPFMGS GTTLVQCMEM GINSIGIDIS PFNCLIAEVK LQKYDIQKLK KILLDMLNKT KEFSKNLGDD EFVKEMDKLI EKYNKKYFTL EYKRKLSKKE IDEDSYSEKI MEMFYLEYKK LKEKYCKNDD EFDDIFKDKP FLYKWYSPRI RAELNFYLNL IKDCRDETIK KVAMIILSRT ARSVRGTTHF DLATLKEPVF DPYYCYKHKK ICRPVQTILR HLEEYTNDVI SRIEEFSKIR KDAYYLIING DSRTVDIEEE LKKHPNFYEL YKNKKIDGIF TSPPYLGQID YHEQHAYAYE LFDIPRLDEL EIGPKFKGSS KKAQKEYIEG ISDVLINMKR FLNEDAKIFI VVNDKKNLYK EIFEKSGLIL VREFKRPVLN RTERDRNPYY ESIFELKMEE // ID MTNA_METJA Reviewed; 329 AA. AC Q57896; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative methylthioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; DE Short=M1Pi {ECO:0000255|HAMAP-Rule:MF_01678}; DE Short=MTR-1-P isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; DE EC=5.3.1.23 {ECO:0000255|HAMAP-Rule:MF_01678}; DE AltName: Full=MTNA-like protein {ECO:0000255|HAMAP-Rule:MF_01678}; DE Short=aMTNA {ECO:0000255|HAMAP-Rule:MF_01678}; DE AltName: Full=S-methyl-5-thioribose-1-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_01678}; GN OrderedLocusNames=MJ0454; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the interconversion of methylthioribose-1- CC phosphate (MTR-1-P) into methylthioribulose-1-phosphate (MTRu-1- CC P). {ECO:0000255|HAMAP-Rule:MF_01678}. CC -!- CATALYTIC ACTIVITY: S-methyl-5-thio-alpha-D-ribose 1-phosphate = CC S-methyl-5-thio-D-ribulose 1-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_01678}. CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits CC family. MtnA subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98443.1; -; Genomic_DNA. DR PIR; F64356; F64356. DR ProteinModelPortal; Q57896; -. DR SMR; Q57896; 4-328. DR STRING; 243232.MJ_0454; -. DR EnsemblBacteria; AAB98443; AAB98443; MJ_0454. DR KEGG; mja:MJ_0454; -. DR eggNOG; arCOG01123; Archaea. DR eggNOG; COG0182; LUCA. DR InParanoid; Q57896; -. DR KO; K08963; -. DR OMA; KVFNPAF; -. DR PhylomeDB; Q57896; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0046523; F:S-methyl-5-thioribose-1-phosphate isomerase activity; IBA:GO_Central. DR GO; GO:0019509; P:L-methionine biosynthetic process from methylthioadenosine; IBA:GO_Central. DR GO; GO:0019284; P:L-methionine biosynthetic process from S-adenosylmethionine; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.120.420; -; 1. DR HAMAP; MF_01678; Salvage_MtnA; 1. DR InterPro; IPR000649; IF-2B-related. DR InterPro; IPR005251; IF-M1Pi. DR InterPro; IPR011559; Initiation_fac_2B_a/b/d. DR InterPro; IPR027363; M1Pi_N. DR Pfam; PF01008; IF-2B; 1. DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1. DR TIGRFAMs; TIGR00512; salvage_mtnA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Isomerase; KW Methionine biosynthesis; Reference proteome. FT CHAIN 1 329 Putative methylthioribose-1-phosphate FT isomerase. FT /FTId=PRO_0000156086. FT REGION 50 52 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT REGION 233 234 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT ACT_SITE 223 223 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT BINDING 84 84 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT BINDING 182 182 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01678}. FT SITE 143 143 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01678}. SQ SEQUENCE 329 AA; 36803 MW; 3936298C574730C9 CRC64; MTKDLRPIIW DDDKKELILI DQRKLPNKLE YFICKTYEDV AYAIKDMVVR GAPAIGVSAA YGLALAEING DDIYKAYEVL KNTRPTAVNL FWALDRCLTA YKEGKSILDE AKKIHEEDIE TCKKIGMIGE KLIEDGDTIL THCNAGALAT SAYGTALSVI RFAFYNGKKI RVIADETRPR LQGAKLTAFE LNYEGIPVKV ITDNTAGFLM QKGEIDKIIV GADRILADGT VYNKIGTYSL AVLAKYHRIP FYVAAPLSTF DLRSSEEDVI IEERDEKEVA YIDGVRIVPE GVGCYNYAFD KTPPDLITAI ITEKGIVKPN RDEILKLFR // ID MOAA_METJA Reviewed; 298 AA. AC Q58234; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Probable cyclic pyranopterin monophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01225}; DE EC=4.1.99.18 {ECO:0000255|HAMAP-Rule:MF_01225}; DE AltName: Full=Molybdenum cofactor biosynthesis protein A {ECO:0000255|HAMAP-Rule:MF_01225}; GN Name=moaA {ECO:0000255|HAMAP-Rule:MF_01225}; OrderedLocusNames=MJ0824; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes, together with MoaC, the conversion of 5'-GTP CC to cyclic pyranopterin monophosphate (cPMP or molybdopterin CC precursor Z). {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- CATALYTIC ACTIVITY: GTP = cyclic pyranopterin phosphate + CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine and 1 [4Fe-4S] cluster coordinated with 3 cysteines and CC the GTP-derived substrate. {ECO:0000255|HAMAP-Rule:MF_01225}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01225}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000255|HAMAP-Rule:MF_01225}; CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01225}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. MoaA family. CC {ECO:0000255|HAMAP-Rule:MF_01225}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98823.1; -; Genomic_DNA. DR PIR; H64402; H64402. DR ProteinModelPortal; Q58234; -. DR STRING; 243232.MJ_0824; -. DR DNASU; 1451707; -. DR EnsemblBacteria; AAB98823; AAB98823; MJ_0824. DR KEGG; mja:MJ_0824; -. DR eggNOG; arCOG00930; Archaea. DR eggNOG; COG2896; LUCA. DR InParanoid; Q58234; -. DR KO; K03639; -. DR OMA; MHHRKKY; -. DR PhylomeDB; Q58234; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0019008; C:molybdopterin synthase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01225_A; MoaA_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR013485; MoaA_arc. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR010505; Mob_synth_C. DR InterPro; IPR007197; rSAM. DR Pfam; PF06463; Mob_synth_C; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR02668; moaA_archaeal; 1. DR PROSITE; PS01305; MOAA_NIFB_PQQE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; GTP-binding; Iron; Iron-sulfur; Lyase; KW Metal-binding; Molybdenum cofactor biosynthesis; Nucleotide-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 298 Probable cyclic pyranopterin FT monophosphate synthase. FT /FTId=PRO_0000153017. FT REGION 248 250 GTP binding. {ECO:0000255|HAMAP- FT Rule:MF_01225}. FT METAL 20 20 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 24 24 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 27 27 Iron-sulfur 1 (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 243 243 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 246 246 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT METAL 260 260 Iron-sulfur 2 (4Fe-4S-substrate). FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 13 13 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 26 26 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 61 61 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 65 65 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01225}. FT BINDING 91 91 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 115 115 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01225}. FT BINDING 152 152 GTP. {ECO:0000255|HAMAP-Rule:MF_01225}. SQ SEQUENCE 298 AA; 34652 MW; EA92B9A0A75BFD55 CRC64; MKDKFGREIR SLRISITNKC NLQCFYCHRE GHDSNNDRYM TPEEIGIIAK TSTKFGVKKI KISGGEPLLR KDVCEIIENI KDERIKDISL TTNGILLENL AEKLKDAGLN RVNVSLDTLN PELYKKITKF GDVERVINGI KKAIDVSLTP LKVNFLAMSI NIKDLPDIME FCRDIGAILQ IIEFIPLKEE LKGYYYNISP IENEIKEKAD KVITRNFMQN RKKYIVDGLE IEFVRPMDNS EFCMHCTRIR LTYDGYLKPC LLRDDNLVDV LTPLRKGENL EPYFIECINR REPYFKIK // ID MOAB_METJA Reviewed; 163 AA. AC Q57631; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Probable molybdopterin adenylyltransferase; DE Short=MPT adenylyltransferase; DE EC=2.7.7.75; GN Name=moaB; OrderedLocusNames=MJ0167; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the adenylation of molybdopterin as part of CC the biosynthesis of the molybdenum-cofactor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + molybdopterin = diphosphate + adenylyl- CC molybdopterin. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoaB/Mog family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98149.1; -; Genomic_DNA. DR PIR; H64320; H64320. DR ProteinModelPortal; Q57631; -. DR STRING; 243232.MJ_0167; -. DR EnsemblBacteria; AAB98149; AAB98149; MJ_0167. DR KEGG; mja:MJ_0167; -. DR eggNOG; arCOG00214; Archaea. DR eggNOG; COG0521; LUCA. DR InParanoid; Q57631; -. DR KO; K03638; -. DR OMA; PHILYII; -. DR PhylomeDB; Q57631; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0061598; F:molybdopterin adenylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR012245; MoaB. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR Pfam; PF00994; MoCF_biosynth; 1. DR PIRSF; PIRSF006443; MoaB; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR PROSITE; PS01078; MOCF_BIOSYNTHESIS_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Molybdenum cofactor biosynthesis; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 163 Probable molybdopterin FT adenylyltransferase. FT /FTId=PRO_0000170981. SQ SEQUENCE 163 AA; 18247 MW; 5B7FA49A5A223435 CRC64; MHKRIKNIKY AVVTVSDSRY NDLIKGKEVD DKSGKLLKKE LNAKVYTIIP DNKNMIKGIV EHIVEFFDVD CIVFTGGTGI AERDVTVEAL KEIIEKELDG FKIIFQKLSY EEVGFSAMLS RAMAGIYKGK IIYALPGSVN ACRTALKIIK EETGHILGHL REG // ID MOAC_METJA Reviewed; 152 AA. AC Q58535; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Probable cyclic pyranopterin monophosphate synthase accessory protein; DE AltName: Full=Molybdenum cofactor biosynthesis protein C; GN Name=moaC; OrderedLocusNames=MJ1135; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Together with MoaA, is involved in the conversion of 5'- CC GTP to cyclic pyranopterin monophosphate (cPMP or molybdopterin CC precursor Z). {ECO:0000250}. CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoaC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99137.1; -; Genomic_DNA. DR PIR; F64441; F64441. DR ProteinModelPortal; Q58535; -. DR SMR; Q58535; 9-151. DR STRING; 243232.MJ_1135; -. DR EnsemblBacteria; AAB99137; AAB99137; MJ_1135. DR KEGG; mja:MJ_1135; -. DR eggNOG; arCOG01530; Archaea. DR eggNOG; COG0315; LUCA. DR InParanoid; Q58535; -. DR KO; K03637; -. DR OMA; CEVRAYY; -. DR PhylomeDB; Q58535; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.640; -; 1. DR HAMAP; MF_01224_A; MoaC_A; 1. DR InterPro; IPR023045; Mo_CF_biosynth-C. DR InterPro; IPR023047; Mo_CF_biosynth-C_arc. DR InterPro; IPR002820; Mopterin_CF_biosynth-C_dom. DR Pfam; PF01967; MoaC; 1. DR SUPFAM; SSF55040; SSF55040; 1. DR TIGRFAMs; TIGR00581; moaC; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 152 Probable cyclic pyranopterin FT monophosphate synthase accessory protein. FT /FTId=PRO_0000097854. FT ACT_SITE 123 123 {ECO:0000255}. SQ SEQUENCE 152 AA; 17043 MW; D91AC8ED1D2852AF CRC64; MLTHVDDKGV KMVDISKKED VERICVAEGY IKLKPETIKL IKEQKIKKGN VLTTAQIAGI LAVKKTYELI PMCHPLPITS VNVDFEVFED KIKAICSVKT TYKTGIEMEA LTGVSIALLT IWDMVKSAEK DEDGQYKTAE IFGIRVVEKI KK // ID MSMJL_METJA Reviewed; 361 AA. AC Q58543; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Large-conductance mechanosensitive channel MscMJLR; GN OrderedLocusNames=MJ1143; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A MECHANOSENSITIVE CHANNEL, AND SUBCELLULAR LOCATION. RX PubMed=11296222; DOI=10.1093/emboj/20.8.1888; RA Kloda A., Martinac B.; RT "Structural and functional differences between two homologous RT mechanosensitive channels of Methanococcus jannaschii."; RL EMBO J. 20:1888-1896(2001). CC -!- FUNCTION: Large-conductance mechanosensitive channel that opens in CC response to stretch forces in the membrane lipid bilayer. CC Selective for cations. Rectifies with voltage. CC {ECO:0000269|PubMed:11296222}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:11296222}; CC Multi-pass membrane protein {ECO:0000269|PubMed:11296222}. CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99143.1; -; Genomic_DNA. DR PIR; F64442; F64442. DR ProteinModelPortal; Q58543; -. DR STRING; 243232.MJ_1143; -. DR TCDB; 1.A.23.4.1; the small conductance mechanosensitive ion channel (mscs) family. DR EnsemblBacteria; AAB99143; AAB99143; MJ_1143. DR KEGG; mja:MJ_1143; -. DR eggNOG; arCOG01568; Archaea. DR eggNOG; COG0668; LUCA. DR InParanoid; Q58543; -. DR KO; K16052; -. DR OMA; FFVYTFT; -. DR PhylomeDB; Q58543; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006811; P:ion transport; IEA:UniProtKB-KW. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR011066; MscC_channel_C. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR006686; MscS_channel_CS. DR InterPro; IPR011014; MscS_channel_TM-2. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82689; SSF82689; 1. DR SUPFAM; SSF82861; SSF82861; 1. DR PROSITE; PS01246; UPF0003; 1. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Reference proteome; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 361 Large-conductance mechanosensitive FT channel MscMJLR. FT /FTId=PRO_0000110254. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. SQ SEQUENCE 361 AA; 40683 MW; A6339C3C8AC4D68E CRC64; MTITQMISEI LMHNTVYNYI LSLISIILFI VIGKYANALI ERLADKLHKK SGIELDELLI RALSLPVAIA IILSGFYFGV NFLYLLPSLK TAVNEGILTA FILCVVVFFD RFLNELVERY LALTISKKTK KDVDDQIVVL TKKLVRLVVW VVGLLLILSN LGYDIKTLLA GLGIGGLAVA LASQNLVSNL IAGLIILTDK PFKIGNWITF SGGSGIVEDI GIRSTKIRAT DNSIIVVPNS KLIDEIIQNV PSKNKWKVST TIGVTYNTPV EKIRKAEEII KNILLEHPNV EDEPITVYFK EFGDWSLNIQ VVYYIKNSRY NGYQKYISTI NEVNLKIKEE FDRKGIEFAF PTYTLYLKRD D // ID MT51_METJA Reviewed; 310 AA. AC Q57983; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 96. DE RecName: Full=Probable modification methylase MJ0563; DE EC=2.1.1.37; DE AltName: Full=Cytosine-specific methyltransferase MJ0563; DE AltName: Full=M.MjaVIIIP; GN OrderedLocusNames=MJ0563; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98555.1; -; Genomic_DNA. DR PIR; C64370; C64370. DR ProteinModelPortal; Q57983; -. DR STRING; 243232.MJ_0563; -. DR REBASE; 3888; M.MjaORF563P. DR EnsemblBacteria; AAB98555; AAB98555; MJ_0563. DR KEGG; mja:MJ_0563; -. DR eggNOG; arCOG04157; Archaea. DR eggNOG; COG0270; LUCA. DR InParanoid; Q57983; -. DR KO; K00558; -. DR OMA; RARMFIS; -. DR PhylomeDB; Q57983; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 1. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 310 Probable modification methylase MJ0563. FT /FTId=PRO_0000087916. FT DOMAIN 1 310 SAM-dependent MTase C5-type. FT {ECO:0000255|PROSITE-ProRule:PRU01016}. FT ACT_SITE 77 77 {ECO:0000255|PROSITE-ProRule:PRU01016}. SQ SEQUENCE 310 AA; 36290 MW; 0F983B2193692D78 CRC64; MNVIDLFSGC GGFSKGFLDE NFRILGAIEN FKPVVKTYLY NIKAPVWMDD IKRIPPKAFD EFIKNEKVDV IIGSPPCEPF TKANKLIKDN PLDRLYKDKV GRLVLYYIDY VNYFTQRNDD LIFVMENVPQ IKEIKDELKK LFGDIGHKVY FNILRAEDYG NPSKRARMFI SNIKLKPKKV DKLVVVEEAL KDIPKDAKNH EIKKLSKEKV EMISKLKWGE ALYRYRGKKK LMFNWYKLHP KKLAPTVKGR SRFIHPYEDR LLTVREQARL MSYPDDFVFF GGRDVQYNQI GESVPPILGR AIAKEIKKQL // ID MTM4_METJA Reviewed; 298 AA. AC Q58724; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Putative modification methylase MjaIVP; DE Short=M.MjaIVP; DE EC=2.1.1.-; GN Name=mjaIVMP; OrderedLocusNames=MJ1328; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GTNNAC, causes specific methylation on ? on both strands, and CC protects the DNA from cleavage by the MjaIV endonuclease. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99337.1; -; Genomic_DNA. DR PIR; G64465; G64465. DR ProteinModelPortal; Q58724; -. DR STRING; 243232.MJ_1328; -. DR REBASE; 3895; M.MjaIV. DR EnsemblBacteria; AAB99337; AAB99337; MJ_1328. DR KEGG; mja:MJ_1328; -. DR eggNOG; arCOG03521; Archaea. DR eggNOG; COG1002; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; Transferase. FT CHAIN 1 298 Putative modification methylase MjaIVP. FT /FTId=PRO_0000088020. SQ SEQUENCE 298 AA; 35328 MW; 9BE52F35B001822B CRC64; MQKNQTIFLN TWKFLITLHQ KPWSTFFTKI PDFPHVLLKD IAKVGVGLVS GFDEAFLLNE DDISKLNEDE KQLIKNFVKA KNCKRFVVEG FVQYILIEDN LKDEEIFKTK YPNIYKKLLK FKDRMENRYL PKNKKWFNWQ ALRNYKFLIK NLNKKRIYVP TLDRKPYNRF SLGDDELLPS GDVIFIQPYN DDDIYFLLGY LNSSFFRNYY LANGGRRGGR VAFTQKLLEN AKIPTFSDEV KEKIKNIVKD IIYNLKNGKD IENLERQIDY IIVSAINNNQ FKGYQTTLKN LLKPKLKG // ID MTM6_METJA Reviewed; 194 AA. AC Q58606; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Modification methylase MjaVI; DE Short=M.MjaVI; DE EC=2.1.1.113; DE AltName: Full=N-4 cytosine-specific methyltransferase MjaVI; GN Name=mjaVIM; OrderedLocusNames=MJ1209; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC CCGG, causes specific methylation on C-? on both strands, and CC protects the DNA from cleavage by the MjaVI endonuclease. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA cytosine = S- CC adenosyl-L-homocysteine + DNA N(4)-methylcytosine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC N(4) subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99220.1; -; Genomic_DNA. DR ProteinModelPortal; Q58606; -. DR STRING; 243232.MJ_1209; -. DR REBASE; 3893; M.MjaVI. DR EnsemblBacteria; AAB99220; AAB99220; MJ_1209. DR KEGG; mja:MJ_1209; -. DR eggNOG; arCOG00115; Archaea. DR eggNOG; COG0863; LUCA. DR PhylomeDB; Q58606; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00093; N4_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 194 Modification methylase MjaVI. FT /FTId=PRO_0000087939. SQ SEQUENCE 194 AA; 22461 MW; 6DB2BAEEAEAEBC10 CRC64; MKVIIVKIWN KINGITLIND DFLNVDLPNE SIDLIVTSPP YNVGIDYNQH DDTIPYEEYL DWTKQWLKKA LTLLKKDGRL CLNIPLDKNK GGIKPVYADI VKIALDVGFK YQTTIIWNEQ NISRRTAWGS FMSASAPYVI APVETIVVLY KESWKKLSKG ESDITKEEFI EWTNGLWTFP GESKKELDIQ HHFR // ID MTM1_METJA Reviewed; 303 AA. AC Q58392; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Modification methylase MjaI; DE Short=M.MjaI; DE EC=2.1.1.113; DE AltName: Full=N-4 cytosine-specific methyltransferase MjaI; GN Name=mjaIM; OrderedLocusNames=MJ0985; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC CTAG, causes specific methylation on C-1 on both strands, and CC protects the DNA from cleavage by the MjaI endonuclease. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA cytosine = S- CC adenosyl-L-homocysteine + DNA N(4)-methylcytosine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC N(4) subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98988.1; -; Genomic_DNA. DR PIR; A64423; A64423. DR ProteinModelPortal; Q58392; -. DR STRING; 243232.MJ_0985; -. DR REBASE; 3889; M.MjaI. DR EnsemblBacteria; AAB98988; AAB98988; MJ_0985. DR KEGG; mja:MJ_0985; -. DR eggNOG; arCOG00115; Archaea. DR eggNOG; COG0863; LUCA. DR InParanoid; Q58392; -. DR KO; K00590; -. DR OMA; MWDDIFA; -. DR PhylomeDB; Q58392; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00093; N4_MTASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 303 Modification methylase MjaI. FT /FTId=PRO_0000087936. SQ SEQUENCE 303 AA; 35518 MW; 6D4DB9B36EA90E80 CRC64; MMSIDITTNH KIIFGDARKM DEIEDESVHL VVTSPPYPMI EMWDELFKML NLEINKRWME MENEEDEEKK EKLIMQIYNL MHQTLYPVWE EVYRVLVPGG IACINIGDAT RKINGVFRLF PNHSKIIENF EKIGFVTLPY ILWKKPSNKP NAFLGSGFLP PNAYVTLDVE YILIFRKGKP RKFKPKDPLR YASAYTKEER DRWFSQIWEI VGDKQTHPKI ERRTASFPEE IPRRLIRMFS IIGDTVLDPF LGTGTTVKAA IELKRNSIGY EIDKSLKPII EEKIGIKQKR IGMDFNVEFI NRG // ID MTRA_METJA Reviewed; 241 AA. AC Q58261; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 29-MAR-2005, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093}; DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01093}; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit A {ECO:0000255|HAMAP-Rule:MF_01093}; GN Name=mtrA {ECO:0000255|HAMAP-Rule:MF_01093}; OrderedLocusNames=MJ0851; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- COFACTOR: CC Name=5-hydroxybenzimidazolylcob(I)amide; Xref=ChEBI:CHEBI:60494; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01093}; CC Note=Binds 1 5-hydroxybenzimidazolylcobamide group. CC {ECO:0000255|HAMAP-Rule:MF_01093}; CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. {ECO:0000255|HAMAP-Rule:MF_01093}. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP- CC Rule:MF_01093}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01093}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01093}. CC -!- SIMILARITY: Belongs to the MtrA family. {ECO:0000255|HAMAP- CC Rule:MF_01093}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98856.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98856.1; ALT_INIT; Genomic_DNA. DR PIR; C64406; C64406. DR IntAct; Q58261; 2. DR MINT; MINT-8378586; -. DR STRING; 243232.MJ_0851; -. DR DNASU; 1451739; -. DR EnsemblBacteria; AAB98856; AAB98856; MJ_0851. DR KEGG; mja:MJ_0851; -. DR eggNOG; arCOG03221; Archaea. DR eggNOG; COG4063; LUCA. DR InParanoid; Q58261; -. DR KO; K00577; -. DR OMA; EVKGHIT; -. DR PhylomeDB; Q58261; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0050897; F:cobalt ion binding; IEA:InterPro. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR HAMAP; MF_01093; MtrA; 1. DR InterPro; IPR030688; MeTrfase_MtrA/MtxA. DR InterPro; IPR005778; MtrA. DR Pfam; PF04208; MtrA; 1. DR PIRSF; PIRSF500207; MtrA; 1. DR PIRSF; PIRSF009452; MtrA_MtxA; 1. DR TIGRFAMs; TIGR01111; mtrA; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalt; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 241 Tetrahydromethanopterin S- FT methyltransferase subunit A. FT /FTId=PRO_0000147503. FT TOPO_DOM 1 220 Cytoplasmic. {ECO:0000255|HAMAP- FT Rule:MF_01093}. FT TRANSMEM 221 241 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01093}. FT BINDING 85 85 5'-hydroxybenzimidazolyl-cobamide FT cofactor. {ECO:0000255|HAMAP- FT Rule:MF_01093}. SQ SEQUENCE 241 AA; 25880 MW; 155EAE6418E09B8D CRC64; MANKREPAPG WPIVSGEYVV GNPESCVGVV TLGSHGLEQA CIDAGAAIAG PCHTENLGIE KVVANYISNP NIRFMILCGS EVQGHITGQC FKALWENGIG DDGGIIGAKG AIPFLENVNK EAVERFRRQI VEVVDLIDCE DIGKITQAIK ECLSKDPGAI DEDPFIIELE GGKGGGEEEE GVIKPITPEM AIIESRMRLI GNEMCYNGLL AKWQAGYYNG KIQGIATGLF LMLLIMGILM F // ID MTRE_METJA Reviewed; 303 AA. AC Q58257; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit E; DE EC=2.1.1.86; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit E; GN Name=mtrE; OrderedLocusNames=MJ0847; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MtrE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98852.1; -; Genomic_DNA. DR PIR; G64405; G64405. DR ProteinModelPortal; Q58257; -. DR STRING; 243232.MJ_0847; -. DR EnsemblBacteria; AAB98852; AAB98852; MJ_0847. DR KEGG; mja:MJ_0847; -. DR eggNOG; arCOG04870; Archaea. DR eggNOG; COG4059; LUCA. DR InParanoid; Q58257; -. DR KO; K00581; -. DR OMA; VGSQSNP; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012506; C:vesicle membrane; IEA:InterPro. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR HAMAP; MF_01098; MtrE; 1. DR InterPro; IPR005780; MeTrfase_E. DR Pfam; PF04206; MtrE; 1. DR PIRSF; PIRSF016509; MtrE; 1. DR TIGRFAMs; TIGR01113; mtrE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 303 Tetrahydromethanopterin S- FT methyltransferase subunit E. FT /FTId=PRO_0000147539. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. SQ SEQUENCE 303 AA; 31635 MW; 46BA1BBD80FECCE2 CRC64; MDATLIALGA LALSGALATV AGCAEDLESD VGSQSNPNSQ VQLAPQMGNI HRYFNKAISG EPVSYGLYVA VAGTVAYAIM QMGLNPILAL ILGAGVAAFV HGAYAISAYL GRIVGQSKNF GQPVYWDVVM SHLGPIVGHG FIAVFCMVLM AYLANTILGN PFPLPLIALI FGITVGAIGS STGDVHYGAE REYQKYPFGG GVPVANHGDI DIKAEYGLRN GMDSSYFCSR LGGVLTGLCF GLIVFLDGWR GVLGDILKGG QGGSVITASI ISIVIGLIIV AILAIINRKV EVFARNKYGP YTK // ID MRE11_METJA Reviewed; 366 AA. AC Q58719; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=DNA double-strand break repair protein Mre11 {ECO:0000255|HAMAP-Rule:MF_02044}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_02044}; GN Name=mre11 {ECO:0000255|HAMAP-Rule:MF_02044}; GN OrderedLocusNames=MJ1323; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in CC the early steps of DNA double-strand break (DSB) repair. The CC complex may facilitate opening of the processed DNA ends to aid in CC the recruitment of HerA and NurA. Mre11 binds to DSB ends and has CC both double-stranded 3'-5' exonuclease activity and single- CC stranded endonuclease activity. {ECO:0000255|HAMAP-Rule:MF_02044}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02044}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_02044}; CC -!- ENZYME REGULATION: Nuclease activity is regulated by Rad50. CC {ECO:0000255|HAMAP-Rule:MF_02044}. CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11 CC subunits and two Rad50 subunits. {ECO:0000255|HAMAP- CC Rule:MF_02044}. CC -!- INTERACTION: CC Self; NbExp=3; IntAct=EBI-10107692, EBI-10107692; CC -!- SIMILARITY: Belongs to the MRE11/RAD32 family. {ECO:0000255|HAMAP- CC Rule:MF_02044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99332.1; -; Genomic_DNA. DR PIR; B64465; B64465. DR PDB; 3AUZ; X-ray; 3.21 A; A=1-313. DR PDB; 3AV0; X-ray; 3.10 A; A=1-366. DR PDB; 4TUG; X-ray; 3.55 A; A/B/C/D/E/F=1-333. DR PDB; 4TUI; X-ray; 3.59 A; A/B/C/D/E/F=1-333. DR PDB; 5DNY; X-ray; 3.11 A; A/C=1-366. DR PDB; 5F3W; X-ray; 3.11 A; A/C=1-366. DR PDBsum; 3AUZ; -. DR PDBsum; 3AV0; -. DR PDBsum; 4TUG; -. DR PDBsum; 4TUI; -. DR PDBsum; 5DNY; -. DR PDBsum; 5F3W; -. DR ProteinModelPortal; Q58719; -. DR STRING; 243232.MJ_1323; -. DR EnsemblBacteria; AAB99332; AAB99332; MJ_1323. DR KEGG; mja:MJ_1323; -. DR eggNOG; arCOG00397; Archaea. DR eggNOG; COG0420; LUCA. DR InParanoid; Q58719; -. DR OMA; IECREFV; -. DR PhylomeDB; Q58719; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.21.10; -; 1. DR HAMAP; MF_02044; Mre11; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR032885; Mre11_archaea-type. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Endonuclease; KW Exonuclease; Hydrolase; Manganese; Metal-binding; Nuclease; KW Reference proteome. FT CHAIN 1 366 DNA double-strand break repair protein FT Mre11. FT /FTId=PRO_0000138689. FT ACT_SITE 85 85 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_02044}. FT METAL 8 8 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_02044}. FT METAL 10 10 Manganese 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02044}. FT METAL 49 49 Manganese 1. {ECO:0000255|HAMAP- FT Rule:MF_02044}. FT METAL 49 49 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_02044}. FT METAL 84 84 Manganese 2. {ECO:0000255|HAMAP- FT Rule:MF_02044}. FT METAL 158 158 Manganese 2; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02044}. FT METAL 186 186 Manganese 2; via pros nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02044}. FT METAL 188 188 Manganese 1; via tele nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02044}. FT STRAND 2 6 {ECO:0000244|PDB:3AV0}. FT HELIX 15 17 {ECO:0000244|PDB:3AV0}. FT HELIX 19 37 {ECO:0000244|PDB:3AV0}. FT STRAND 42 46 {ECO:0000244|PDB:3AV0}. FT STRAND 50 55 {ECO:0000244|PDB:3AV0}. FT HELIX 58 73 {ECO:0000244|PDB:3AV0}. FT STRAND 77 80 {ECO:0000244|PDB:3AV0}. FT HELIX 84 86 {ECO:0000244|PDB:3AV0}. FT STRAND 89 93 {ECO:0000244|PDB:5DNY}. FT HELIX 96 100 {ECO:0000244|PDB:3AV0}. FT TURN 101 103 {ECO:0000244|PDB:3AV0}. FT STRAND 104 106 {ECO:0000244|PDB:5DNY}. FT STRAND 108 115 {ECO:0000244|PDB:3AV0}. FT STRAND 118 125 {ECO:0000244|PDB:3AV0}. FT HELIX 130 132 {ECO:0000244|PDB:5DNY}. FT HELIX 133 148 {ECO:0000244|PDB:3AV0}. FT STRAND 151 157 {ECO:0000244|PDB:3AV0}. FT TURN 162 164 {ECO:0000244|PDB:3AV0}. FT STRAND 165 168 {ECO:0000244|PDB:3AV0}. FT HELIX 173 175 {ECO:0000244|PDB:3AV0}. FT STRAND 180 184 {ECO:0000244|PDB:3AV0}. FT STRAND 191 194 {ECO:0000244|PDB:3AV0}. FT STRAND 196 202 {ECO:0000244|PDB:3AV0}. FT HELIX 211 213 {ECO:0000244|PDB:3AV0}. FT HELIX 215 220 {ECO:0000244|PDB:3AV0}. FT STRAND 222 228 {ECO:0000244|PDB:3AV0}. FT STRAND 231 233 {ECO:0000244|PDB:3AV0}. FT HELIX 236 238 {ECO:0000244|PDB:3AV0}. FT STRAND 239 243 {ECO:0000244|PDB:3AV0}. FT STRAND 249 254 {ECO:0000244|PDB:3AV0}. FT HELIX 257 267 {ECO:0000244|PDB:3AV0}. FT STRAND 269 272 {ECO:0000244|PDB:3AV0}. FT STRAND 275 281 {ECO:0000244|PDB:3AV0}. FT HELIX 282 284 {ECO:0000244|PDB:3AV0}. FT TURN 286 288 {ECO:0000244|PDB:3AV0}. FT HELIX 289 291 {ECO:0000244|PDB:3AV0}. FT TURN 292 294 {ECO:0000244|PDB:3AV0}. FT STRAND 296 303 {ECO:0000244|PDB:3AV0}. FT HELIX 321 332 {ECO:0000244|PDB:3AV0}. FT HELIX 336 347 {ECO:0000244|PDB:3AV0}. FT HELIX 352 362 {ECO:0000244|PDB:3AV0}. SQ SEQUENCE 366 AA; 43132 MW; EFF6ADAD43EB5AFC CRC64; MMFVHIADNH LGYRQYNLDD REKDIYDSFK LCIKKILEIK PDVVLHSGDL FNDLRPPVKA LRIAMQAFKK LHENNIKVYI VAGNHEMPRR LGEESPLALL KDYVKILDGK DVINVNGEEI FICGTYYHKK SKREEMLDKL KNFESEAKNY KKKILMLHQG INPYIPLDYE LEHFDLPKFS YYALGHIHKR ILERFNDGIL AYSGSTEIIY RNEYEDYKKE GKGFYLVDFS GNDLDISDIE KIDIECREFV EVNIKDKKSF NEAVNKIERC KNKPVVFGKI KREFKPWFDT LKDKILINKA IIVDDEFIDM PDNVDIESLN IKELLVDYAN RQGIDGDLVL SLYKALLNNE NWKELLDEYY NTKFRG // ID MTD_METJA Reviewed; 277 AA. AC Q58441; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=F420-dependent methylenetetrahydromethanopterin dehydrogenase; DE Short=MTD; DE EC=1.5.98.1; DE AltName: Full=Coenzyme F420-dependent N5,N10-methylenetetrahydromethanopterin dehydrogenase; GN Name=mtd; OrderedLocusNames=MJ1035; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible reduction of methenyl- CC H(4)MPT(+) to methylene-H(4)MPT. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5,10-methylenetetrahydromethanopterin + CC oxidized coenzyme F420 = 5,10-methenyltetrahydromethanopterin + CC reduced coenzyme F420. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); 5,10- CC methylene-5,6,7,8-tetrahydromethanopterin from 5,10-methenyl- CC 5,6,7,8-tetrahydromethanopterin (coenzyme F420 route): step 1/1. CC -!- SIMILARITY: Belongs to the MTD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99039.1; -; Genomic_DNA. DR PIR; B64429; B64429. DR ProteinModelPortal; Q58441; -. DR SMR; Q58441; 2-277. DR STRING; 243232.MJ_1035; -. DR EnsemblBacteria; AAB99039; AAB99039; MJ_1035. DR KEGG; mja:MJ_1035; -. DR eggNOG; arCOG04382; Archaea. DR eggNOG; COG1927; LUCA. DR InParanoid; Q58441; -. DR KO; K00319; -. DR OMA; KGCFMTK; -. DR UniPathway; UPA00640; UER00695. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0030268; F:methylenetetrahydromethanopterin dehydrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00058; MTD; 1. DR InterPro; IPR002844; Methylene_DH. DR Pfam; PF01993; MTD; 1. DR PIRSF; PIRSF005627; MTD; 1. DR ProDom; PD017604; Methylene_DH; 1. DR SUPFAM; SSF102324; SSF102324; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; One-carbon metabolism; KW Oxidoreductase; Reference proteome. FT CHAIN 1 277 F420-dependent FT methylenetetrahydromethanopterin FT dehydrogenase. FT /FTId=PRO_0000075038. SQ SEQUENCE 277 AA; 30306 MW; 93A1D2357CC85DDF CRC64; MVVKIGIIKC GNIGMSPVVD LALDERADRK DIAVRVLGSG AKMDPESVEE VTKKMVEEVK PDFIIYIGPN PAAPGPKKAR EILSQSGIPA VIIGDAPGLR VKDEMEQQGL GYIIIKCDPM IGARREFLDP VEMALFNADV IRVLAGTGAL RIVQEAIDKM IDAVKEGKEI ELPKIVITEQ KAVEAMEFTN PYAKAKAMAA FTIAEKVGDV DVKGCFMTKE AEKYIPIVAS AHEMIRYAAK LVDEARELEK AMDAVSRKPH HPEGKRLSKK ALMEKPE // ID MTRF_METJA Reviewed; 68 AA. AC Q58262; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit F; DE EC=2.1.1.86; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit F; GN Name=mtrF; OrderedLocusNames=MJ0852; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MtrF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98857.1; -; Genomic_DNA. DR PIR; D64406; D64406. DR STRING; 243232.MJ_0852; -. DR EnsemblBacteria; AAB98857; AAB98857; MJ_0852. DR KEGG; mja:MJ_0852; -. DR eggNOG; arCOG03381; Archaea. DR eggNOG; COG4218; LUCA. DR KO; K00582; -. DR OMA; YMEELEY; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01099; MtrF; 1. DR InterPro; IPR011307; MeTrfase_F. DR InterPro; IPR013347; MeTrfase_F_su. DR Pfam; PF09472; MtrF; 1. DR PIRSF; PIRSF006523; MtrF; 1. DR TIGRFAMs; TIGR02507; MtrF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 68 Tetrahydromethanopterin S- FT methyltransferase subunit F. FT /FTId=PRO_0000147548. FT TRANSMEM 46 66 Helical. {ECO:0000255}. SQ SEQUENCE 68 AA; 7259 MW; ADA19238B424D169 CRC64; MGVEVSNKPN VSSIQSYVED LEYKVGLITR NRGLESGTES AGTKGLIIGV VSAIVLMGIP LALYFLMK // ID MTM5_METJA Reviewed; 292 AA. AC Q58893; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Modification methylase MjaV; DE Short=M.MjaV; DE EC=2.1.1.113; DE AltName: Full=N-4 cytosine-specific methyltransferase MjaV; GN Name=mjaVM; OrderedLocusNames=MJ1498; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GTAC, causes specific methylation on C-4 on both strands, and CC protects the DNA from cleavage by the MjaV endonuclease. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA cytosine = S- CC adenosyl-L-homocysteine + DNA N(4)-methylcytosine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC N(4) subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99509.1; -; Genomic_DNA. DR PIR; A64487; A64487. DR ProteinModelPortal; Q58893; -. DR STRING; 243232.MJ_1498; -. DR REBASE; 3897; M.MjaV. DR EnsemblBacteria; AAB99509; AAB99509; MJ_1498. DR KEGG; mja:MJ_1498; -. DR eggNOG; arCOG00115; Archaea. DR eggNOG; COG0863; LUCA. DR InParanoid; Q58893; -. DR OMA; SIMHEYI; -. DR PhylomeDB; Q58893; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0015667; F:site-specific DNA-methyltransferase (cytosine-N4-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002941; DNA_methylase_N4/N6. DR InterPro; IPR017985; MeTrfase_CN4_CS. DR InterPro; IPR001091; RM_Methylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01555; N6_N4_Mtase; 1. DR PRINTS; PR00508; S21N4MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00093; N4_MTASE; 1. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 292 Modification methylase MjaV. FT /FTId=PRO_0000087938. SQ SEQUENCE 292 AA; 33877 MW; A5A46D7C8FBD3FE3 CRC64; MEINKIYCMD CLEGMKQLKD KTVDVVVTSP PYNIGIKYNK YSDNLSREDY LNWIEEVVKE IKRVLKDDGS FFINVGYTAK DPWIAFDVAN VIRKHFKLQN TIHWVKSIAI QKEDVGNYPN IIGDIAVGHY KPINSDRFLS IMHEYIFHFT KNGNVKLDKL AIGVPYQDKS NIKRFNRKGD LRDRGNTWFI PYETIQSKEK ERPHPATFPP KLPEMCIKLH GVKKTNLVLD PFMGIGSTAI ACIRLGIDYI GFEIDEYYCR VAEERIKKEL LKTDGKFDNV KNKNIITLDA FI // ID MTRC_METJA Reviewed; 265 AA. AC Q58259; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit C; DE EC=2.1.1.86; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit C; GN Name=mtrC; OrderedLocusNames=MJ0849; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MtrC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98854.1; -; Genomic_DNA. DR PIR; A64406; A64406. DR ProteinModelPortal; Q58259; -. DR STRING; 243232.MJ_0849; -. DR DNASU; 1451737; -. DR EnsemblBacteria; AAB98854; AAB98854; MJ_0849. DR KEGG; mja:MJ_0849; -. DR eggNOG; arCOG04868; Archaea. DR eggNOG; COG4061; LUCA. DR InParanoid; Q58259; -. DR KO; K00579; -. DR OMA; GMAILHP; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01096; MtrC; 1. DR InterPro; IPR005865; THM_MeTrfase_su_C. DR Pfam; PF04211; MtrC; 1. DR PIRSF; PIRSF006530; MtrC; 1. DR ProDom; PD013899; THM_MeTrfase_su_C; 1. DR TIGRFAMs; TIGR01148; mtrC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 265 Tetrahydromethanopterin S- FT methyltransferase subunit C. FT /FTId=PRO_0000147522. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 202 222 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. SQ SEQUENCE 265 AA; 27804 MW; 07FB20DA394A7FE0 CRC64; MSHGGGGHAA ELYPEEQIFA VGIALSLVGC YLANFLSPYG LGMLIGGLLA SAACVAGANT VRKVAAYGLG TGVPSIGMVS LGMGTLAAVA GVLIPDYFNL PYLVAPIITL IVSAVIGYIV GRLTVNPVGM KIPIMVRSMT FLSIAGAMAL LGFTVAYVGS LEPQKYIDYA LNNGMMALAF IAAGMAILHP FNACLGPNES HKRTLTLAVA CGFITWFVFS VVKLDIVSII VSIILWAIVY VKFVKMSFKD ACAVLHVPEI PKKEE // ID MVP_METJA Reviewed; 209 AA. AC Q57603; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Hyperpolarization-activated voltage-gated potassium channel; DE AltName: Full=MVP; GN Name=mvp; OrderedLocusNames=MJ0139; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CHARACTERIZATION. RX PubMed=12640457; DOI=10.1038/nn1028; RA Sesti F., Rajan S., Gonzalez-Colaso R., Nikolaeva N., RA Goldstein S.A.N.; RT "Hyperpolarization moves S4 sensors inward to open MVP, a RT methanococcal voltage-gated potassium channel."; RL Nat. Neurosci. 6:353-361(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [3] RP FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12860407; DOI=10.1016/S0014-5793(03)00706-3; RA Hellmer J., Zeilinger C.; RT "MjK1, a K+ channel from M. jannaschii, mediates K+ uptake and K+ RT sensitivity in E. coli."; RL FEBS Lett. 547:165-169(2003). CC -!- FUNCTION: Voltage-gated potassium-selective channel opened by CC hyperpolarization. {ECO:0000269|PubMed:12860407}. CC -!- SUBUNIT: Homotetramer. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- DOMAIN: The segment S4 is probably the voltage-sensor and is CC characterized by a series of positively charged amino acids. CC -!- MISCELLANEOUS: Inhibited by barium. CC -!- SIMILARITY: Belongs to the potassium channel family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY268105; AAP31055.1; -; mRNA. DR EMBL; L77117; AAB98122.1; -; Genomic_DNA. DR PIR; C64317; C64317. DR ProteinModelPortal; Q57603; -. DR STRING; 243232.MJ_0139; -. DR TCDB; 1.A.1.6.1; the voltage-gated ion channel (vic) superfamily. DR EnsemblBacteria; AAB98122; AAB98122; MJ_0139. DR KEGG; mja:MJ_0139; -. DR eggNOG; arCOG01964; Archaea. DR eggNOG; COG1226; LUCA. DR InParanoid; Q57603; -. DR KO; K10716; -. DR OMA; LSTYNPP; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0008076; C:voltage-gated potassium channel complex; IEA:InterPro. DR GO; GO:0005249; F:voltage-gated potassium channel activity; IBA:GO_Central. DR GO; GO:0071805; P:potassium ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR005821; Ion_trans_dom. DR InterPro; IPR028325; VG_K_chnl. DR PANTHER; PTHR11537; PTHR11537; 1. DR Pfam; PF00520; Ion_trans; 1. DR PRINTS; PR00169; KCHANNEL. PE 1: Evidence at protein level; KW Cell membrane; Complete proteome; Ion channel; Ion transport; KW Membrane; Potassium; Potassium channel; Potassium transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport; KW Voltage-gated channel. FT CHAIN 1 209 Hyperpolarization-activated voltage-gated FT potassium channel. FT /FTId=PRO_0000054098. FT TOPO_DOM 1 10 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 11 31 Helical; Name=Segment S1. {ECO:0000255}. FT TOPO_DOM 32 38 Extracellular. {ECO:0000255}. FT TRANSMEM 39 59 Helical; Name=Segment S2. {ECO:0000255}. FT TOPO_DOM 60 71 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 72 92 Helical; Name=Segment S3. {ECO:0000255}. FT TOPO_DOM 93 96 Extracellular. {ECO:0000255}. FT TRANSMEM 97 117 Helical; Voltage-sensor; Name=Segment S4. FT {ECO:0000255}. FT TOPO_DOM 118 125 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 126 146 Helical; Name=Segment S5. {ECO:0000255}. FT TOPO_DOM 147 181 Extracellular. {ECO:0000255}. FT TRANSMEM 182 202 Helical; Name=Segment S6. {ECO:0000255}. FT TOPO_DOM 203 209 Cytoplasmic. {ECO:0000255}. FT MOTIF 170 175 Selectivity filter. {ECO:0000250}. SQ SEQUENCE 209 AA; 24183 MW; FC91E7320F34D90F CRC64; MNLKDRRLKK IMEVLSLIFT FEIVASFILS TYNPPYQDLL IKLDYISIMF FTFEFIYNFY YVEDKAKFFK DIYNIVDAIV VIAFLLYSLQ VFYSKAFLGL RVINLLRILV LLRIIKLRKL EENQALINFL TLLTICFIAS CLIWIVESGV NPAINNFFDA FYFTTISITT VGYGDITPKT DAGKLIIIFS VLFFISGLIT SLQKALKGD // ID MT52_METJA Reviewed; 366 AA. AC Q58600; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Probable modification methylase MJ1200; DE EC=2.1.1.37; DE AltName: Full=Cytosine-specific methyltransferase MJ1200; DE AltName: Full=M.MjaVIIP; GN OrderedLocusNames=MJ1200; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA = S-adenosyl-L- CC homocysteine + DNA containing 5-methylcytosine. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. C5-methyltransferase family. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC -!- SIMILARITY: Contains 1 SAM-dependent MTase C5-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01016}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99203.1; -; Genomic_DNA. DR PIR; G64449; G64449. DR ProteinModelPortal; Q58600; -. DR STRING; 243232.MJ_1200; -. DR REBASE; 3906; M.MjaORF1200P. DR EnsemblBacteria; AAB99203; AAB99203; MJ_1200. DR KEGG; mja:MJ_1200; -. DR eggNOG; arCOG04157; Archaea. DR eggNOG; COG0270; LUCA. DR InParanoid; Q58600; -. DR KO; K00558; -. DR OMA; AIFIANR; -. DR PhylomeDB; Q58600; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003886; F:DNA (cytosine-5-)-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR001525; C5_MeTfrase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF00145; DNA_methylase; 2. DR PRINTS; PR00105; C5METTRFRASE. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS51679; SAM_MT_C5; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 366 Probable modification methylase MJ1200. FT /FTId=PRO_0000087917. FT DOMAIN 5 366 SAM-dependent MTase C5-type. FT {ECO:0000255|PROSITE-ProRule:PRU01016}. FT ACT_SITE 133 133 {ECO:0000255|PROSITE-ProRule:PRU01016}. SQ SEQUENCE 366 AA; 42269 MW; 9D5C60CA603FBCFE CRC64; MVIMLKFIDL FCGCGGFSRG FVEEGFEPLV AIELNEDAAF SYALNFNGQI YEKIRPGEFK LKELKGYVGI YPFKFPFEEE DIKWLKRLGT LNEKTKKLSP VVINDDIREI HAIEIEKFIK NKKVDVIIGG PPCEGYTGAN PKREKNPYDR LYKDETGRLV LEYIRIVGDL QPKIFVMENV PGIKEVRGAI IKEFREIGYE DVYFNTLRAE DYGNPSVRRR VFVSNIEINP EKTQPKTVIE AIGDLMYKGR DVPNHEFAAL PARFRKRVHK LGWGDAFIYF KGANRRLGNY IRLHPLKLAE TVMGKRFFIH PYEDRLLTPR EQARLMSYPD YHLFAGGIRS CYNQIGESVP VALSRAIARV IKENLK // ID MTRB_METJA Reviewed; 103 AA. AC Q58260; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit B; DE EC=2.1.1.86; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit B; GN Name=mtrB; OrderedLocusNames=MJ0850; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MtrB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98855.1; -; Genomic_DNA. DR PIR; B64406; B64406. DR IntAct; Q58260; 2. DR MINT; MINT-8378601; -. DR STRING; 243232.MJ_0850; -. DR EnsemblBacteria; AAB98855; AAB98855; MJ_0850. DR KEGG; mja:MJ_0850; -. DR eggNOG; arCOG04867; Archaea. DR eggNOG; COG4062; LUCA. DR InParanoid; Q58260; -. DR KO; K00578; -. DR OMA; FKSAFFG; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01094; MtrB; 1. DR InterPro; IPR008690; MtrB_MeTrfase. DR Pfam; PF05440; MtrB; 1. DR PIRSF; PIRSF005518; MtrB; 1. DR ProDom; PD012565; MtrB_MeTrfase; 1. DR TIGRFAMs; TIGR04166; methano_MtrB; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 103 Tetrahydromethanopterin S- FT methyltransferase subunit B. FT /FTId=PRO_0000147514. FT TRANSMEM 81 101 Helical. {ECO:0000255}. SQ SEQUENCE 103 AA; 11527 MW; 0797F2691A1CE10F CRC64; MATYVFIDQN IPLVYTVETG VITKGFGDLL FVDVSPIEEQ IKKLETLVDA YEHSLDPRYP PLNSFPNRDG VYAISGYFKS AFFGFWIGLG IMALLAIILG VKF // ID MTRG_METJA Reviewed; 84 AA. AC Q58263; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit G {ECO:0000255|HAMAP-Rule:MF_01500}; DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01500}; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit G {ECO:0000255|HAMAP-Rule:MF_01500}; GN Name=mtrG {ECO:0000255|HAMAP-Rule:MF_01500}; OrderedLocusNames=MJ0853; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step. {ECO:0000255|HAMAP-Rule:MF_01500}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. {ECO:0000255|HAMAP-Rule:MF_01500}. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. {ECO:0000255|HAMAP-Rule:MF_01500}. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP- CC Rule:MF_01500}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01500}; Single-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01500}. CC -!- SIMILARITY: Belongs to the MtrG family. {ECO:0000255|HAMAP- CC Rule:MF_01500}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98858.1; -; Genomic_DNA. DR PIR; E64406; E64406. DR STRING; 243232.MJ_0853; -. DR EnsemblBacteria; AAB98858; AAB98858; MJ_0853. DR KEGG; mja:MJ_0853; -. DR eggNOG; arCOG03380; Archaea. DR eggNOG; COG4064; LUCA. DR InParanoid; Q58263; -. DR KO; K00583; -. DR OMA; PQVIMDP; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01500; MtrG; 1. DR InterPro; IPR005866; THM_MeTrfase_su_G. DR Pfam; PF04210; MtrG; 1. DR PIRSF; PIRSF006500; MtrG; 1. DR ProDom; PD012265; THM_MeTrfase_su_G; 1. DR TIGRFAMs; TIGR01149; mtrG; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 84 Tetrahydromethanopterin S- FT methyltransferase subunit G. FT /FTId=PRO_0000147555. FT TRANSMEM 50 70 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01500}. SQ SEQUENCE 84 AA; 9449 MW; 4802F872BAD32A2E CRC64; MSEDEKLPQV IMDPADYEAL KKRLDELEKK VENTNAELFQ LAGKKVGRDI GILYGLVIGI ILSYILPALI KIIQILSLKV LVQQ // ID MTRH_METJA Reviewed; 319 AA. AC Q58264; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-2003, sequence version 2. DT 11-NOV-2015, entry version 100. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit H {ECO:0000255|HAMAP-Rule:MF_01501}; DE EC=2.1.1.86 {ECO:0000255|HAMAP-Rule:MF_01501}; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit H {ECO:0000255|HAMAP-Rule:MF_01501}; GN Name=mtrH {ECO:0000255|HAMAP-Rule:MF_01501}; OrderedLocusNames=MJ0854; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step. MtrH catalyzes the transfer of the CC methyl group from methyl-tetrahydromethanopterin to the corrinoid CC prosthetic group of MtrA. {ECO:0000255|HAMAP-Rule:MF_01501}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. {ECO:0000255|HAMAP-Rule:MF_01501}. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. {ECO:0000255|HAMAP-Rule:MF_01501}. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000255|HAMAP- CC Rule:MF_01501}. CC -!- SIMILARITY: Belongs to the MtrH family. {ECO:0000255|HAMAP- CC Rule:MF_01501}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98859.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98859.1; ALT_INIT; Genomic_DNA. DR PIR; F64406; F64406. DR ProteinModelPortal; Q58264; -. DR STRING; 243232.MJ_0854; -. DR EnsemblBacteria; AAB98859; AAB98859; MJ_0854. DR KEGG; mja:MJ_0854; -. DR eggNOG; arCOG04336; Archaea. DR eggNOG; COG1962; LUCA. DR InParanoid; Q58264; -. DR KO; K00584; -. DR OMA; YARHKIV; -. DR PhylomeDB; Q58264; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01501; MtrH; 1. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR023467; MeTrfase_MtrH/MtxH. DR InterPro; IPR028342; MtrH. DR Pfam; PF02007; MtrH; 1. DR PIRSF; PIRSF004960; MtrH_MtxH; 1. DR ProDom; PD009948; MtrH_MeTrfase; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR01114; mtrH; 1. PE 3: Inferred from homology; KW Complete proteome; Methanogenesis; Methyltransferase; KW One-carbon metabolism; Reference proteome; Transferase. FT CHAIN 1 319 Tetrahydromethanopterin S- FT methyltransferase subunit H. FT /FTId=PRO_0000147563. SQ SEQUENCE 319 AA; 34603 MW; 370E20B41F5CDA00 CRC64; MFKFDREQMV VEIAGRKIGG QPGEYPTALA GTIFYARHKI VEDERKGIFD KAAAEDLINK QAEMEDITGN PALVQVFGGT PEALVNYIDF VAEVWDGPML LDSTSGEARM AAAKRATEAG YAKQCIYNSI NVSIDEQEYQ VLVESDLEAS IVLCFDPMDP TVEGKINVLT NGGKTADKGM LELAEKAGIK YPLIDTAVTP LGNGAGAAVR ASFAVKALFG YPVGSGIHNI PSAWDWLREF RKQLREAGER EKAKDIHHVC DVGANLVQVM ASGDFVLYGP IDNAYMTFPA VAMVDAIIAE AAKELGIEPI DTHPFKKLV // ID NADA_METJA Reviewed; 307 AA. AC Q57850; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Quinolinate synthase A {ECO:0000255|HAMAP-Rule:MF_00568}; DE EC=2.5.1.72 {ECO:0000255|HAMAP-Rule:MF_00568}; GN Name=nadA {ECO:0000255|HAMAP-Rule:MF_00568}; OrderedLocusNames=MJ0407; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the condensation of iminoaspartate with CC dihydroxyacetone phosphate to form quinolinate. CC {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- CATALYTIC ACTIVITY: Glycerone phosphate + iminosuccinate = CC pyridine-2,3-dicarboxylate + 2 H(2)O + phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00568}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00568}; CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; quinolinate CC from iminoaspartate: step 1/1. {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00568}. CC -!- SIMILARITY: Belongs to the quinolinate synthase A family. Type 2 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00568}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98397.1; -; Genomic_DNA. DR PIR; G64350; G64350. DR ProteinModelPortal; Q57850; -. DR STRING; 243232.MJ_0407; -. DR EnsemblBacteria; AAB98397; AAB98397; MJ_0407. DR KEGG; mja:MJ_0407; -. DR eggNOG; arCOG04459; Archaea. DR eggNOG; COG0379; LUCA. DR InParanoid; Q57850; -. DR KO; K03517; -. DR OMA; IAHPECE; -. DR PhylomeDB; Q57850; -. DR UniPathway; UPA00253; UER00327. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008987; F:quinolinate synthetase A activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00568; NadA_type2; 1. DR InterPro; IPR003473; NadA. DR InterPro; IPR023066; Quinolinate_synth_type2. DR Pfam; PF02445; NadA; 1. DR TIGRFAMs; TIGR00550; nadA; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Metal-binding; Pyridine nucleotide biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 307 Quinolinate synthase A. FT /FTId=PRO_0000155803. FT BINDING 23 23 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 40 40 Iminoaspartate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00568}. FT BINDING 112 112 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 129 129 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 199 199 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. FT BINDING 216 216 Iminoaspartate. {ECO:0000255|HAMAP- FT Rule:MF_00568}. SQ SEQUENCE 307 AA; 34863 MW; C78611F2767C315C CRC64; MSMDIVERIN KLKEEKNAVI LAHNYQPKEI QKIADFLGDS LELCIKAKET DADIIVFCGV DFMGESAKIL NPEKKVLMPE IEGTQCPMAH QLPPEIIKKY RELYPEAPLV VYVNTTAETK ALADITCTSA NADRVVNSLD ADTVLFGPDN NLAYYVQKRT DKKVIAIPEG GGCYVHKKFT IDDLKRVKSK YPNAKVLIHP ECSPELQDNA DYIASTSGIL RIVLESDDEE FIIGTEVGMI NRLEIELEKL GKKKTLIPLR KDAICHEMKR ITLEKIEKCL LEERYEIKLE KEIIEKAQKA IERMLRI // ID MTIP_METJA Reviewed; 252 AA. AC Q60367; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=Probable S-methyl-5'-thioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE EC=2.4.2.44 {ECO:0000255|HAMAP-Rule:MF_01963}; DE AltName: Full=5'-methylthioinosine phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTI phosphorylase {ECO:0000255|HAMAP-Rule:MF_01963}; DE Short=MTIP {ECO:0000255|HAMAP-Rule:MF_01963}; GN OrderedLocusNames=MJ0060; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible phosphorylation of S-methyl-5'- CC thioinosine (MTI) to hypoxanthine and 5-methylthioribose-1- CC phosphate. Involved in the breakdown of S-methyl-5'-thioadenosine CC (MTA), a major by-product of polyamine biosynthesis. Catabolism of CC (MTA) occurs via deamination to MTI and phosphorolysis to CC hypoxanthine. {ECO:0000255|HAMAP-Rule:MF_01963}. CC -!- CATALYTIC ACTIVITY: S-methyl-5'-thioinosine + phosphate = CC hypoxanthine + S-methyl-5-thio-alpha-D-ribose 1-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_01963}. CC -!- PATHWAY: Purine metabolism; purine nucleoside salvage. CC {ECO:0000255|HAMAP-Rule:MF_01963}. CC -!- SUBUNIT: Homotrimer. {ECO:0000255|HAMAP-Rule:MF_01963}. CC -!- MISCELLANEOUS: Although this enzyme belongs to the family of MTA CC phosphorylases based on sequence homology, it has been shown that CC conserved amino acid substitutions in the substrate binding pocket CC convert the substrate specificity of this enzyme from 6- CC aminopurines to 6-oxopurines. {ECO:0000255|HAMAP-Rule:MF_01963}. CC -!- SIMILARITY: Belongs to the PNP/MTAP phosphorylase family. MTAP CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01963}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98042.1; -; Genomic_DNA. DR PIR; D64307; D64307. DR ProteinModelPortal; Q60367; -. DR STRING; 243232.MJ_0060; -. DR EnsemblBacteria; AAB98042; AAB98042; MJ_0060. DR KEGG; mja:MJ_0060; -. DR eggNOG; arCOG01327; Archaea. DR eggNOG; COG0005; LUCA. DR InParanoid; Q60367; -. DR KO; K00772; -. DR OMA; GCDIVGM; -. DR PhylomeDB; Q60367; -. DR UniPathway; UPA00606; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0017061; F:S-methyl-5-thioadenosine phosphorylase activity; IBA:GO_Central. DR GO; GO:0006166; P:purine ribonucleoside salvage; IEA:UniProtKB-KW. DR GO; GO:0043101; P:purine-containing compound salvage; IBA:GO_Central. DR Gene3D; 3.40.50.1580; -; 1. DR HAMAP; MF_01963; MTAP; 1. DR InterPro; IPR010044; MTAP. DR InterPro; IPR000845; Nucleoside_phosphorylase_d. DR InterPro; IPR001369; PNP/MTAP. DR InterPro; IPR018099; Purine_phosphorylase-2_CS. DR PANTHER; PTHR11904; PTHR11904; 1. DR Pfam; PF01048; PNP_UDP_1; 1. DR SUPFAM; SSF53167; SSF53167; 1. DR TIGRFAMs; TIGR01694; MTAP; 1. DR PROSITE; PS01240; PNP_MTAP_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Purine salvage; KW Reference proteome; Transferase. FT CHAIN 1 252 Probable S-methyl-5'-thioinosine FT phosphorylase. FT /FTId=PRO_0000184559. FT REGION 44 45 Phosphate binding. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT REGION 197 199 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT BINDING 8 8 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT BINDING 173 173 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01963}. FT BINDING 174 174 Phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01963}. FT SITE 156 156 Important for substrate specificity. FT {ECO:0000255|HAMAP-Rule:MF_01963}. FT SITE 209 209 Important for substrate specificity. FT {ECO:0000255|HAMAP-Rule:MF_01963}. SQ SEQUENCE 252 AA; 28664 MW; DFD7C01615774A79 CRC64; MIGIIGGTGI AEILKGDKEE IINTKYGKAR VIIDKENEVV LLFRHGVRHN IPPHKINYRA NIYALKKLGV ERILAINSVG SLKEDLKPGM FFVPNDFIEF TKKREETFYD EGKVVHIDMT DPYCPELRNI LKSILDKNNF SYGEGVYVCT EGPRFETKKE IAIYKNWGDV VGMTGYPEVV LARELEMCYV SLCNITNYAC GISKNILTVD EVLEKIKEME NKILKVVEDF INYGFGERKC ICKDALKHAV IG // ID MTM3_METJA Reviewed; 289 AA. AC Q58015; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Modification methylase MjaIII; DE Short=M.MjaIII; DE EC=2.1.1.72; DE AltName: Full=Adenine-specific methyltransferase MjaIII; GN Name=mjaIIIM; OrderedLocusNames=MJ0598; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This methylase recognizes the double-stranded sequence CC GATC, causes specific methylation on A-2 on both strands, and CC protects the DNA from cleavage by the MjaIII endonuclease. CC {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98590.1; -; Genomic_DNA. DR PIR; F64374; F64374. DR ProteinModelPortal; Q58015; -. DR STRING; 243232.MJ_0598; -. DR REBASE; 3890; M.MjaIII. DR PRIDE; Q58015; -. DR EnsemblBacteria; AAB98590; AAB98590; MJ_0598. DR KEGG; mja:MJ_0598; -. DR eggNOG; arCOG03416; Archaea. DR eggNOG; COG0338; LUCA. DR InParanoid; Q58015; -. DR KO; K06223; -. DR OMA; MNRHGFN; -. DR PhylomeDB; Q58015; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 1.10.1020.10; -; 1. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR023095; Ade_MeTrfase_dom_2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR012263; M_m6A_EcoRV. DR InterPro; IPR012327; MeTrfase_D12. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02086; MethyltransfD12; 1. DR PIRSF; PIRSF000398; M_m6A_EcoRV; 1. DR PRINTS; PR00505; D12N6MTFRASE. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00571; dam; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 289 Modification methylase MjaIII. FT /FTId=PRO_0000087976. FT BINDING 9 9 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 13 13 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. FT BINDING 63 63 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 199 199 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 289 AA; 34235 MW; CA95493C5CED8E78 CRC64; MEVKPFLKWA GGKTQILSQI EENLPKELKE GNIKKYIEPF VGGGAVLFYL LQKYEFKKVI ISDINEDLML CYKVVKNDVD RLIEELSSLR DEFLSLDEEK RKEFYYKVRD DFNKNKNDCD EVKRVAQFIF LNKTCYNGLY RVNKKGEFNV PYGRYKNPKI FDEQNLKNVS KLLKNVKILC GDFEIVDEYV DAESFVYFDP PYKPLNKTSS FTSYTKYDFN DDDQIRLAKF YRKLDKRGAK LMLSNSYNVD FFGKLYEGFN IKKVVAKRMI NCKGDKRKDG IYELLIMNY // ID MTRD_METJA Reviewed; 230 AA. AC Q58258; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Tetrahydromethanopterin S-methyltransferase subunit D; DE EC=2.1.1.86; DE AltName: Full=N5-methyltetrahydromethanopterin--coenzyme M methyltransferase subunit D; GN Name=mtrD; OrderedLocusNames=MJ0848; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a complex that catalyzes the formation of CC methyl-coenzyme M and tetrahydromethanopterin from coenzyme M and CC methyl-tetrahydromethanopterin. This is an energy-conserving, CC sodium-ion translocating step (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 5-methyl-5,6,7,8-tetrahydromethanopterin + 2- CC mercaptoethanesulfonate = 5,6,7,8-tetrahydromethanopterin + 2- CC (methylthio)ethanesulfonate. CC -!- PATHWAY: One-carbon metabolism; methanogenesis from CO(2); methyl- CC coenzyme M from 5,10-methylene-5,6,7,8-tetrahydromethanopterin: CC step 2/2. CC -!- SUBUNIT: The complex is composed of 8 subunits; MtrA, MtrB, MtrC, CC MtrD, MtrE, MtrF, MtrG and MtrH. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MtrD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98853.1; -; Genomic_DNA. DR PIR; H64405; H64405. DR ProteinModelPortal; Q58258; -. DR STRING; 243232.MJ_0848; -. DR EnsemblBacteria; AAB98853; AAB98853; MJ_0848. DR KEGG; mja:MJ_0848; -. DR eggNOG; arCOG04869; Archaea. DR eggNOG; COG4060; LUCA. DR InParanoid; Q58258; -. DR KO; K00580; -. DR OMA; GVHFVPV; -. DR UniPathway; UPA00640; UER00698. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0012506; C:vesicle membrane; IEA:InterPro. DR GO; GO:0030269; F:tetrahydromethanopterin S-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019386; P:methanogenesis, from carbon dioxide; IEA:UniProtKB-UniPathway. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR HAMAP; MF_01097; MtrD; 1. DR InterPro; IPR005779; MeTrfase_D. DR Pfam; PF04207; MtrD; 1. DR PIRSF; PIRSF016552; MtrD; 1. DR ProDom; PD013594; MeTrfase_D; 1. DR TIGRFAMs; TIGR01112; mtrD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Methanogenesis; KW Methyltransferase; One-carbon metabolism; Reference proteome; KW Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 230 Tetrahydromethanopterin S- FT methyltransferase subunit D. FT /FTId=PRO_0000147530. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. SQ SEQUENCE 230 AA; 22879 MW; B9D10D88DC6B64F3 CRC64; MDIVSAIVPL IEMTIAGAII NASVHFIPVG GAPAAMATST GVGTGTTQLA AGAGFTGLMG AAVMASNVGL SPIGMALIMI SGAVSSMIML GVTMLIGQLI YVFGVGVVPA ADKCEIDPIT KDPQKPYVTP GTTGHGVPTV CFVSGLIGAA LGGIGGALAY IALRKLGLDP GVAGMLAVGF FFINAVLASY NIGGTIEGFH DPKFKKMPNG VIASTVASLL FGIISVLMVL // ID MVK_METJA Reviewed; 312 AA. AC Q58487; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 120. DE RecName: Full=Mevalonate kinase {ECO:0000255|HAMAP-Rule:MF_00217}; DE Short=MK {ECO:0000255|HAMAP-Rule:MF_00217}; DE Short=MVK {ECO:0000255|HAMAP-Rule:MF_00217}; DE EC=2.7.1.36 {ECO:0000255|HAMAP-Rule:MF_00217}; GN Name=mvk {ECO:0000255|HAMAP-Rule:MF_00217}; OrderedLocusNames=MJ1087; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, RP ENZYME REGULATION, AND SUBUNIT. RX PubMed=10497066; DOI=10.1006/prep.1999.1106; RA Huang K.-X., Scott A.I., Bennett G.N.; RT "Overexpression, purification, and characterization of the RT thermostable mevalonate kinase from Methanococcus jannaschii."; RL Protein Expr. Purif. 17:33-40(1999). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, AND MUTAGENESIS OF RP ARG-196 AND LYS-272. RX PubMed=12880770; DOI=10.1016/S1046-5928(03)00101-3; RA Chu X., Liu X., Yau M., Leung Y.C., Li D.; RT "Expression and purification of Arg196 and Lys272 mutants of RT mevalonate kinase from Methanococcus jannaschii."; RL Protein Expr. Purif. 30:210-218(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS), ACTIVE SITE, AND REACTION RP MECHANISM. RX PubMed=11751891; DOI=10.1074/jbc.M110787200; RA Yang D., Shipman L.W., Roessner C.A., Scott A.I., Sacchettini J.C.; RT "Structure of the Methanococcus jannaschii mevalonate kinase, a member RT of the GHMP kinase superfamily."; RL J. Biol. Chem. 277:9462-9467(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.69 ANGSTROMS). RX PubMed=16021622; DOI=10.1002/prot.20541; RA Badger J., Sauder J.M., Adams J.M., Antonysamy S., Bain K., RA Bergseid M.G., Buchanan S.G., Buchanan M.D., Batiyenko Y., RA Christopher J.A., Emtage S., Eroshkina A., Feil I., Furlong E.B., RA Gajiwala K.S., Gao X., He D., Hendle J., Huber A., Hoda K., RA Kearins P., Kissinger C., Laubert B., Lewis H.A., Lin J., Loomis K., RA Lorimer D., Louie G., Maletic M., Marsh C.D., Miller I., Molinari J., RA Muller-Dieckmann H.J., Newman J.M., Noland B.W., Pagarigan B., RA Park F., Peat T.S., Post K.W., Radojicic S., Ramos A., Romero R., RA Rutter M.E., Sanderson W.E., Schwinn K.D., Tresser J., Winhoven J., RA Wright T.A., Wu L., Xu J., Harris T.J.R.; RT "Structural analysis of a set of proteins resulting from a bacterial RT genomics project."; RL Proteins 60:787-796(2005). CC -!- FUNCTION: Catalyzes the phosphorylation of (R)-mevalonate (MVA) to CC (R)-mevalonate 5-phosphate (MVAP). Functions in the mevalonate CC (MVA) pathway leading to isopentenyl diphosphate (IPP), a key CC precursor for the biosynthesis of isoprenoid compounds such as CC archaeal membrane lipids. {ECO:0000255|HAMAP-Rule:MF_00217, CC ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-mevalonate = ADP + (R)-5- CC phosphomevalonate. {ECO:0000255|HAMAP-Rule:MF_00217, CC ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00217, CC ECO:0000269|PubMed:10497066}; CC -!- ENZYME REGULATION: Farnesyl- and geranyl-pyrophosphates are CC competitive inhibitors. Slightly inhibited by high concentration CC of ATP. {ECO:0000269|PubMed:10497066}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=68.5 uM for (RS)-mevalonate (at 70 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC KM=106 uM for (RS)-mevalonate (at 34 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC KM=92 uM for ATP (at 70 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC KM=1180 uM for ATP (at 34 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC Vmax=387 umol/min/mg enzyme (at 70 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC Vmax=50.3 umol/min/mg enzyme (at 34 degrees Celsius) CC {ECO:0000269|PubMed:10497066, ECO:0000269|PubMed:12880770}; CC pH dependence: CC Optimum pH is 8.0-8.5. Exhibits at least 60% of its optimal CC activity over a rather broad pH range, from 5 to 7. CC {ECO:0000269|PubMed:10497066}; CC Temperature dependence: CC Optimum temperature is 70-75 degrees Celsius. Highly CC thermostable. Retains 100% of its activity after 24 hours of CC incubation at 70 degrees Celsius. At 90 and 100 degrees Celsius, CC the enzyme shows a half-life of 15 and 5 min, respectively. CC {ECO:0000269|PubMed:10497066}; CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via mevalonate pathway; isopentenyl diphosphate from CC (R)-mevalonate: step 1/3. {ECO:0000255|HAMAP-Rule:MF_00217}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00217, CC ECO:0000269|PubMed:10497066}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. Mevalonate kinase CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00217}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99088.1; -; Genomic_DNA. DR PIR; F64435; F64435. DR PDB; 1KKH; X-ray; 2.40 A; A=1-312. DR PDB; 1VIS; X-ray; 2.69 A; A=2-312. DR PDBsum; 1KKH; -. DR PDBsum; 1VIS; -. DR ProteinModelPortal; Q58487; -. DR SMR; Q58487; 1-312. DR STRING; 243232.MJ_1087; -. DR EnsemblBacteria; AAB99088; AAB99088; MJ_1087. DR KEGG; mja:MJ_1087; -. DR eggNOG; arCOG01028; Archaea. DR eggNOG; COG1577; LUCA. DR InParanoid; Q58487; -. DR KO; K00869; -. DR OMA; CMYALAP; -. DR PhylomeDB; Q58487; -. DR BioCyc; MetaCyc:MONOMER-14622; -. DR BRENDA; 2.7.1.36; 3260. DR SABIO-RK; Q58487; -. DR UniPathway; UPA00057; UER00098. DR EvolutionaryTrace; Q58487; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004496; F:mevalonate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019287; P:isopentenyl diphosphate biosynthetic process, mevalonate pathway; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.70.890; -; 1. DR HAMAP; MF_00217; Mevalonate_kinase; 1. DR InterPro; IPR013750; GHMP_kinase_C_dom. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR006203; GHMP_knse_ATP-bd_CS. DR InterPro; IPR006205; Mev_gal_kin. DR InterPro; IPR006206; Mevalonate/galactokinase. DR InterPro; IPR022937; Mevalonate_kinase_arc. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10457; PTHR10457; 1. DR Pfam; PF08544; GHMP_kinases_C; 1. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PRINTS; PR00959; MEVGALKINASE. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55060; SSF55060; 1. DR TIGRFAMs; TIGR00549; mevalon_kin; 1. DR PROSITE; PS00627; GHMP_KINASES_ATP; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Isoprene biosynthesis; Kinase; Lipid biosynthesis; Lipid metabolism; KW Magnesium; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 312 Mevalonate kinase. FT /FTId=PRO_0000156665. FT NP_BIND 104 114 ATP. {ECO:0000255|HAMAP-Rule:MF_00217}. FT ACT_SITE 155 155 Proton acceptor. FT {ECO:0000305|PubMed:11751891}. FT MUTAGEN 196 196 R->K: 13.5-fold decrease in affinity for FT mevalonate, whereas only little effect on FT affinity for ATP and on reaction rate. FT {ECO:0000269|PubMed:12880770}. FT MUTAGEN 196 196 R->Q: 1900-fold decrease in catalytic FT efficiency. FT {ECO:0000269|PubMed:12880770}. FT MUTAGEN 196 196 R->V: 63-fold decrease in catalytic FT efficiency. FT {ECO:0000269|PubMed:12880770}. FT MUTAGEN 272 272 K->R,A: 13- to 26-fold decrease in FT catalytic efficiency. Still thermostable. FT {ECO:0000269|PubMed:12880770}. FT STRAND 1 12 {ECO:0000244|PDB:1KKH}. FT HELIX 16 19 {ECO:0000244|PDB:1KKH}. FT STRAND 23 38 {ECO:0000244|PDB:1KKH}. FT STRAND 41 48 {ECO:0000244|PDB:1KKH}. FT TURN 49 51 {ECO:0000244|PDB:1KKH}. FT STRAND 54 58 {ECO:0000244|PDB:1KKH}. FT TURN 59 61 {ECO:0000244|PDB:1KKH}. FT HELIX 62 64 {ECO:0000244|PDB:1KKH}. FT HELIX 67 69 {ECO:0000244|PDB:1KKH}. FT HELIX 71 73 {ECO:0000244|PDB:1KKH}. FT HELIX 74 86 {ECO:0000244|PDB:1KKH}. FT STRAND 95 101 {ECO:0000244|PDB:1KKH}. FT STRAND 105 109 {ECO:0000244|PDB:1KKH}. FT HELIX 111 125 {ECO:0000244|PDB:1KKH}. FT TURN 126 128 {ECO:0000244|PDB:1KKH}. FT HELIX 133 147 {ECO:0000244|PDB:1KKH}. FT STRAND 148 150 {ECO:0000244|PDB:1KKH}. FT HELIX 154 161 {ECO:0000244|PDB:1KKH}. FT STRAND 163 170 {ECO:0000244|PDB:1KKH}. FT STRAND 172 175 {ECO:0000244|PDB:1KKH}. FT HELIX 177 184 {ECO:0000244|PDB:1KKH}. FT STRAND 188 194 {ECO:0000244|PDB:1KKH}. FT HELIX 200 208 {ECO:0000244|PDB:1KKH}. FT HELIX 213 229 {ECO:0000244|PDB:1KKH}. FT HELIX 233 248 {ECO:0000244|PDB:1KKH}. FT TURN 249 251 {ECO:0000244|PDB:1KKH}. FT HELIX 255 267 {ECO:0000244|PDB:1KKH}. FT STRAND 268 273 {ECO:0000244|PDB:1KKH}. FT STRAND 275 285 {ECO:0000244|PDB:1KKH}. FT HELIX 288 290 {ECO:0000244|PDB:1KKH}. FT HELIX 291 299 {ECO:0000244|PDB:1KKH}. FT STRAND 304 308 {ECO:0000244|PDB:1KKH}. SQ SEQUENCE 312 AA; 35177 MW; DFF9E5B869728298 CRC64; MIIETPSKVI LFGEHAVVYG YRAISMAIDL TSTIEIKETQ EDEIILNLND LNKSLGLNLN EIKNINPNNF GDFKYCLCAI KNTLDYLNIE PKTGFKINIS SKIPISCGLG SSASITIGTI KAVSGFYNKE LKDDEIAKLG YMVEKEIQGK ASITDTSTIT YKGILEIKNN KFRKIKGEFE EFLKNCKFLI VYAEKRKKKT AELVNEVAKI ENKDEIFKEI DKVIDEALKI KNKEDFGKLM TKNHELLKKL NISTPKLDRI VDIGNRFGFG AKLTGAGGGG CVIILVNEEK EKELLKELNK EDVRIFNCRM MN // ID NADM_METJA Reviewed; 168 AA. AC Q57961; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 112. DE RecName: Full=Nicotinamide-nucleotide adenylyltransferase; DE EC=2.7.7.1; DE AltName: Full=NAD(+) diphosphorylase; DE AltName: Full=NAD(+) pyrophosphorylase; DE AltName: Full=NMN adenylyltransferase; GN OrderedLocusNames=MJ0541; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 2-6, AND CHARACTERIZATION. RX PubMed=9401030; RA Raffaelli N., Pisani F.M., Lorenzi T., Emanuelli M., Amici A., RA Ruggieri S., Magni G.; RT "Characterization of nicotinamide mononucleotide adenylyltransferase RT from thermophilic archaea."; RL J. Bacteriol. 179:7718-7723(1997). RN [3] RP CHARACTERIZATION. RX PubMed=10331644; DOI=10.1023/A:1006968328186; RA Raffaelli N., Emanuelli M., Pisani F.M., Amici A., Lorenzi T., RA Ruggieri S., Magni G.; RT "Identification of the archaeal NMN adenylytransferase gene."; RL Mol. Cell. Biochem. 193:99-102(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2 ANGSTROMS). RX PubMed=10986466; DOI=10.1016/S0969-2126(00)00190-8; RA D'Angelo I., Raffaelli N., Dabusti V., Lorenzi T., Magni G., Rizzi M.; RT "Structure of nicotinamide mononucleotide adenylyltransferase: a key RT enzyme in NAD(+) biosynthesis."; RL Structure 8:993-1004(2000). CC -!- CATALYTIC ACTIVITY: ATP + nicotinamide ribonucleotide = CC diphosphate + NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC nicotinamide D-ribonucleotide: step 1/1. CC -!- SUBUNIT: Homohexamer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the archaeal NMN adenylyltransferase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98533.1; -; Genomic_DNA. DR PIR; E64367; E64367. DR PDB; 1F9A; X-ray; 2.00 A; A/B/C/D/E/F=2-168. DR PDBsum; 1F9A; -. DR ProteinModelPortal; Q57961; -. DR SMR; Q57961; 1-164. DR STRING; 243232.MJ_0541; -. DR EnsemblBacteria; AAB98533; AAB98533; MJ_0541. DR KEGG; mja:MJ_0541; -. DR eggNOG; arCOG00972; Archaea. DR eggNOG; COG1056; LUCA. DR InParanoid; Q57961; -. DR KO; K00952; -. DR OMA; NSVWVSH; -. DR PhylomeDB; Q57961; -. DR BRENDA; 2.7.7.1; 3260. DR UniPathway; UPA00253; UER00600. DR EvolutionaryTrace; Q57961; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0000309; F:nicotinamide-nucleotide adenylyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00243; NMN_adenylyltr; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR006418; NMN_Atrans_arc. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR01527; arch_NMN_Atrans; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Direct protein sequencing; NAD; Nucleotide-binding; KW Nucleotidyltransferase; Pyridine nucleotide biosynthesis; KW Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000305|PubMed:9401030}. FT CHAIN 2 168 Nicotinamide-nucleotide FT adenylyltransferase. FT /FTId=PRO_0000134992. FT STRAND 2 7 {ECO:0000244|PDB:1F9A}. FT HELIX 14 23 {ECO:0000244|PDB:1F9A}. FT TURN 24 26 {ECO:0000244|PDB:1F9A}. FT STRAND 28 34 {ECO:0000244|PDB:1F9A}. FT STRAND 41 44 {ECO:0000244|PDB:1F9A}. FT HELIX 49 60 {ECO:0000244|PDB:1F9A}. FT STRAND 66 71 {ECO:0000244|PDB:1F9A}. FT HELIX 78 80 {ECO:0000244|PDB:1F9A}. FT HELIX 81 88 {ECO:0000244|PDB:1F9A}. FT STRAND 93 96 {ECO:0000244|PDB:1F9A}. FT HELIX 100 108 {ECO:0000244|PDB:1F9A}. FT STRAND 112 114 {ECO:0000244|PDB:1F9A}. FT TURN 121 123 {ECO:0000244|PDB:1F9A}. FT HELIX 126 135 {ECO:0000244|PDB:1F9A}. FT HELIX 140 142 {ECO:0000244|PDB:1F9A}. FT HELIX 145 154 {ECO:0000244|PDB:1F9A}. FT HELIX 156 163 {ECO:0000244|PDB:1F9A}. SQ SEQUENCE 168 AA; 19610 MW; D82FF45E68E29834 CRC64; MRGFIIGRFQ PFHKGHLEVI KKIAEEVDEI IIGIGSAQKS HTLENPFTAG ERILMITQSL KDYDLTYYPI PIKDIEFNSI WVSYVESLTP PFDIVYSGNP LVRVLFEERG YEVKRPEMFN RKEYSGTEIR RRMLNGEKWE HLVPKAVVDV IKEIKGVERL RKLAQTDK // ID NADE_METJA Reviewed; 259 AA. AC Q58747; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Probable NH(3)-dependent NAD(+) synthetase; DE EC=6.3.1.5; GN Name=nadE; OrderedLocusNames=MJ1352; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + deamido-NAD(+) + NH(3) = AMP + CC diphosphate + NAD(+). CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; NAD(+) from CC deamido-NAD(+) (ammonia route): step 1/1. CC -!- SIMILARITY: Belongs to the NAD synthetase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99363.1; -; Genomic_DNA. DR PIR; G64468; G64468. DR ProteinModelPortal; Q58747; -. DR SMR; Q58747; 12-259. DR STRING; 243232.MJ_1352; -. DR EnsemblBacteria; AAB99363; AAB99363; MJ_1352. DR KEGG; mja:MJ_1352; -. DR eggNOG; arCOG00069; Archaea. DR eggNOG; COG0171; LUCA. DR InParanoid; Q58747; -. DR KO; K01916; -. DR OMA; MCILYYF; -. DR PhylomeDB; Q58747; -. DR BRENDA; 6.3.1.5; 3260. DR UniPathway; UPA00253; UER00333. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003952; F:NAD+ synthase (glutamine-hydrolyzing) activity; IEA:InterPro. DR GO; GO:0008795; F:NAD+ synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00193; NadE; 1. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR003694; NAD_synthase. DR InterPro; IPR022926; NH(3)-dep_NAD(+)_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 1. DR TIGRFAMs; TIGR00552; nadE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; NAD; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 259 Probable NH(3)-dependent NAD(+) FT synthetase. FT /FTId=PRO_0000152224. FT NP_BIND 33 40 ATP. {ECO:0000250}. FT ACT_SITE 35 35 {ECO:0000250}. SQ SEQUENCE 259 AA; 28982 MW; BAFD1B7ACAF951BF CRC64; MLWGESMEEI VNKITKFIRE KVEEANANGV VVGLSGGIDS SVTAYLCVKA LGKDKVLGLI MPEKNTNPKD VEHAKMVAEN LGIKYIISDI TDILKAFGAG GYVPTREFDK IADGNLKARI RMCILYYFAN KYNLLVAGTS NKSEIYVGYG TKHGDIACDI RPIGNLFKTE VKKLAKYIGV PKEIIEKPPS AGLWEGQTDE EELDIKYETL DTILKLYEKG KTPEEIHKET NIPLETINYV FDLIKKNEHK RTLPPTPEI // ID NAH2_METJA Reviewed; 422 AA. AC Q58916; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=Probable Na(+)/H(+) antiporter 2; DE AltName: Full=MjNhaP2; GN OrderedLocusNames=MJ1521; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY TO NA(+)/H(+) ANTIPORTERS. RX PubMed=12220668; DOI=10.1016/S0014-5793(02)03244-1; RA Hellmer J., Paetzold R., Zeilinger C.; RT "Identification of a pH regulated Na(+)/H(+) antiporter of RT Methanococcus jannaschii."; RL FEBS Lett. 527:245-249(2002). CC -!- FUNCTION: This is probably a Na(+)/H(+) antiporter. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 CC (CPA1) transporter (TC 2.A.36) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99540.1; -; Genomic_DNA. DR PIR; H64489; H64489. DR ProteinModelPortal; Q58916; -. DR STRING; 243232.MJ_1521; -. DR EnsemblBacteria; AAB99540; AAB99540; MJ_1521. DR KEGG; mja:MJ_1521; -. DR eggNOG; arCOG01961; Archaea. DR eggNOG; COG0025; LUCA. DR InParanoid; Q58916; -. DR OMA; ICALGSI; -. DR PhylomeDB; Q58916; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR006153; Cation/H_exchanger. DR Pfam; PF00999; Na_H_Exchanger; 1. PE 3: Inferred from homology; KW Antiport; Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 422 Probable Na(+)/H(+) antiporter 2. FT /FTId=PRO_0000052403. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 93 113 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 157 177 Helical. {ECO:0000255}. FT TRANSMEM 183 203 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. FT TRANSMEM 242 262 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TRANSMEM 307 327 Helical. {ECO:0000255}. FT TRANSMEM 341 361 Helical. {ECO:0000255}. FT TRANSMEM 384 404 Helical. {ECO:0000255}. SQ SEQUENCE 422 AA; 45810 MW; AF56570C0626D339 CRC64; MNIVLFLGYL SILFAGGAII AKIAKKIGIP DIPLLLIFGL ILSILNVIPK NIVESSFDFI GNFGLIILLF IGSFEMEWNI MKRVLDVIIK LDILALLIVW IISGIVFNFV FHLPILSLIG LLFGAIVSAT DPATLIPIFS SMDIDPEVAI TLEAESVFND PLGIVVTLIC LSALGLAKAE NPILEFFSLA VGGIILGVIA GKFYEIIISK IKFEDYIAPF TLGLAIAFWY FAEGIFPSIT GYEISGFMAV AIMGLYIGNV IVHKKEHKKD MEKVAVFMDE LSIFIRILIF VLLGASISIP LLEKYALPAF LCALGSILLA RPVGVLIATA IPPIRPLTER IYLALEGPRG VVPATLAAMV YTEIMKHPNI VPKNIASLMP PTELAGTILV ATFMTIIVSV VLEASWAKPL ANILLKRKTS TS // ID NAC_METJA Reviewed; 128 AA. AC Q57728; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Nascent polypeptide-associated complex protein {ECO:0000255|HAMAP-Rule:MF_00814}; GN Name=nac {ECO:0000255|HAMAP-Rule:MF_00814}; OrderedLocusNames=MJ0280; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Contacts the emerging nascent chain on the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_00814}. CC -!- SUBUNIT: Homodimer. Interacts with the ribosome. Binds ribosomal CC RNA. {ECO:0000255|HAMAP-Rule:MF_00814}. CC -!- SIMILARITY: Belongs to the NAC-alpha family. {ECO:0000255|HAMAP- CC Rule:MF_00814}. CC -!- SIMILARITY: Contains 1 NAC-A/B (NAC-alpha/beta) domain. CC {ECO:0000255|HAMAP-Rule:MF_00814}. CC -!- SIMILARITY: Contains 1 UBA domain. {ECO:0000255|HAMAP- CC Rule:MF_00814}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98268.1; -; Genomic_DNA. DR PIR; A64335; A64335. DR ProteinModelPortal; Q57728; -. DR STRING; 243232.MJ_0280; -. DR EnsemblBacteria; AAB98268; AAB98268; MJ_0280. DR KEGG; mja:MJ_0280; -. DR eggNOG; arCOG04061; Archaea. DR eggNOG; COG1308; LUCA. DR InParanoid; Q57728; -. DR KO; K03626; -. DR OMA; PRKMKQM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00814; NAC_arch; 1. DR InterPro; IPR005231; NAC_arc. DR InterPro; IPR002715; Nas_poly-pep-assoc_cplx_dom. DR InterPro; IPR009060; UBA-like. DR Pfam; PF01849; NAC; 1. DR SMART; SM01407; NAC; 1. DR SUPFAM; SSF46934; SSF46934; 1. DR TIGRFAMs; TIGR00264; TIGR00264; 1. DR PROSITE; PS51151; NAC_AB; 1. PE 3: Inferred from homology; KW Complete proteome; Protein transport; Reference proteome; RNA-binding; KW Transport. FT CHAIN 1 128 Nascent polypeptide-associated complex FT protein. FT /FTId=PRO_0000135601. FT DOMAIN 8 75 NAC-A/B. {ECO:0000255|HAMAP- FT Rule:MF_00814}. FT DOMAIN 84 122 UBA. {ECO:0000255|HAMAP-Rule:MF_00814}. SQ SEQUENCE 128 AA; 14958 MW; CE6B571273455E8D CRC64; MFPGKVNPRM LKKMQKMMKD FGMETEDLDV RKVIFVFDDE EWVFEEPKVQ VMDILGVKTY SITGKPKKIK KEKVEEEEEV KVEITEEDVE LVAKQCNVSK EEARKALEEC NGDIAEAILK LEEEKEEN // ID NADC_METJA Reviewed; 283 AA. AC Q57916; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable nicotinate-nucleotide pyrophosphorylase [carboxylating]; DE EC=2.4.2.19; DE AltName: Full=Quinolinate phosphoribosyltransferase [decarboxylating]; DE Short=QAPRTase; GN Name=nadC; OrderedLocusNames=MJ0493; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the catabolism of quinolinic acid (QA). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Beta-nicotinate D-ribonucleotide + diphosphate CC + CO(2) = pyridine-2,3-dicarboxylate + 5-phospho-alpha-D-ribose 1- CC diphosphate. CC -!- PATHWAY: Cofactor biosynthesis; NAD(+) biosynthesis; nicotinate D- CC ribonucleotide from quinolinate: step 1/1. CC -!- SUBUNIT: Hexamer formed by 3 homodimers. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NadC/ModD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98483.1; -; Genomic_DNA. DR PIR; E64361; E64361. DR ProteinModelPortal; Q57916; -. DR STRING; 243232.MJ_0493; -. DR EnsemblBacteria; AAB98483; AAB98483; MJ_0493. DR KEGG; mja:MJ_0493; -. DR eggNOG; arCOG01482; Archaea. DR eggNOG; COG0157; LUCA. DR InParanoid; Q57916; -. DR KO; K00767; -. DR OMA; FEPVKHV; -. DR PhylomeDB; Q57916; -. DR UniPathway; UPA00253; UER00331. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004514; F:nicotinate-nucleotide diphosphorylase (carboxylating) activity; IBA:GO_Central. DR GO; GO:0009435; P:NAD biosynthetic process; IBA:GO_Central. DR GO; GO:0034213; P:quinolinate catabolic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1170.20; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004393; NadC. DR InterPro; IPR027277; NadC/ModD. DR InterPro; IPR002638; Quinolinate_PRibosylTrfase_C. DR InterPro; IPR022412; Quinolinate_PRibosylTrfase_N. DR Pfam; PF01729; QRPTase_C; 1. DR Pfam; PF02749; QRPTase_N; 1. DR PIRSF; PIRSF006250; NadC_ModD; 1. DR SUPFAM; SSF51690; SSF51690; 1. DR TIGRFAMs; TIGR00078; nadC; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; KW Pyridine nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 283 Probable nicotinate-nucleotide FT pyrophosphorylase [carboxylating]. FT /FTId=PRO_0000155952. FT REGION 128 130 Substrate binding. {ECO:0000250}. FT REGION 242 244 Substrate binding. {ECO:0000250}. FT REGION 263 265 Substrate binding. {ECO:0000250}. FT BINDING 93 93 Substrate. {ECO:0000250}. FT BINDING 152 152 Substrate. {ECO:0000250}. FT BINDING 162 162 Substrate. {ECO:0000250}. FT BINDING 191 191 Substrate. {ECO:0000250}. FT BINDING 212 212 Substrate. {ECO:0000250}. SQ SEQUENCE 283 AA; 31970 MW; BDD118E9CE1401A8 CRC64; MLKDYALKIL KKSLEYDVGF GDITTNSIIP EGVKAKGVIK AKEKCIVCGI DFIVAFFEEY GIKCKKLFND GEEAYGNILE FEGDARTILM LERTALNLLM HLSGIATMTN RIVKKAKSVN KNVRVACTRK TLPLLSPLQK YAVYIGGGDT HRFRLDDCVL IKDNHIAIVG VKEAIRRAKE NVSFTKKIEV EVSNLKELRE ALEERADIIM LDNFKPEEIE EALKIIDEFE RKTNFKPIIE VSGGIKEDNI LEYAKYNVDV ISMGALTHSV KSVDMSLDIV RYQ // ID NAH1_METJA Reviewed; 426 AA. AC Q60362; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Na(+)/H(+) antiporter 1; DE AltName: Full=MjNhaP1; GN OrderedLocusNames=MJ0057; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=12220668; DOI=10.1016/S0014-5793(02)03244-1; RA Hellmer J., Paetzold R., Zeilinger C.; RT "Identification of a pH regulated Na(+)/H(+) antiporter of RT Methanococcus jannaschii."; RL FEBS Lett. 527:245-249(2002). RN [3] RP MUTAGENESIS OF ASP-93; ASP-132; GLU-156; ASP-161; HIS-211; HIS-215; RP ARG-320; HIS-333 AND ARG-347. RX PubMed=12729893; DOI=10.1016/S0014-5793(03)00332-6; RA Hellmer J., Teubner A., Zeilinger C.; RT "Conserved arginine and aspartate residues are critical for function RT of MjNhaP1, a Na+/H+ antiporter of M. jannaschii."; RL FEBS Lett. 542:32-36(2003). CC -!- FUNCTION: This is a Na(+)/H(+) antiporter. Can also transport CC lithium. {ECO:0000269|PubMed:12220668}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Active at pH 7.0 and below.; CC -!- INTERACTION: CC Self; NbExp=2; IntAct=EBI-8539024, EBI-8539024; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 CC (CPA1) transporter (TC 2.A.36) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98037.1; -; Genomic_DNA. DR PIR; A64307; A64307. DR PDB; 4CZB; X-ray; 3.50 A; A/B/C/D=1-426. DR PDB; 4D0A; EM; 6.00 A; B=1-426. DR PDBsum; 4CZB; -. DR PDBsum; 4D0A; -. DR ProteinModelPortal; Q60362; -. DR MINT; MINT-8099471; -. DR STRING; 243232.MJ_0057; -. DR TCDB; 2.A.36.6.6; the monovalent cation:proton antiporter-1 (cpa1) family. DR EnsemblBacteria; AAB98037; AAB98037; MJ_0057. DR KEGG; mja:MJ_0057; -. DR eggNOG; arCOG01961; Archaea. DR eggNOG; COG0025; LUCA. DR InParanoid; Q60362; -. DR OMA; FRADDID; -. DR PhylomeDB; Q60362; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0015299; F:solute:proton antiporter activity; IEA:InterPro. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR006153; Cation/H_exchanger. DR Pfam; PF00999; Na_H_Exchanger; 1. PE 1: Evidence at protein level; KW 3D-structure; Antiport; Cell membrane; Complete proteome; KW Ion transport; Membrane; Reference proteome; Sodium; Sodium transport; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 426 Na(+)/H(+) antiporter 1. FT /FTId=PRO_0000052402. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 184 204 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. FT TRANSMEM 309 329 Helical. {ECO:0000255}. FT TRANSMEM 382 402 Helical. {ECO:0000255}. FT MUTAGEN 93 93 D->A: Strong decrease in activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 132 132 D->A: Loss of activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 156 156 E->A: Almost no change in activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 161 161 D->A: Loss of activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 211 211 H->R: No change in activity; when FT associated with R-215. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 215 215 H->R: No change in activity; when FT associated with R-211. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 320 320 R->A,D: Loss of activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 320 320 R->H: Almost no change in activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 333 333 H->R: No change in activity. FT {ECO:0000269|PubMed:12729893}. FT MUTAGEN 347 347 R->A: Strong decrease in activity. FT {ECO:0000269|PubMed:12729893}. FT HELIX 2 26 {ECO:0000244|PDB:4CZB}. FT HELIX 32 42 {ECO:0000244|PDB:4CZB}. FT TURN 43 46 {ECO:0000244|PDB:4CZB}. FT HELIX 51 76 {ECO:0000244|PDB:4CZB}. FT HELIX 82 84 {ECO:0000244|PDB:4CZB}. FT HELIX 86 93 {ECO:0000244|PDB:4CZB}. FT HELIX 95 111 {ECO:0000244|PDB:4CZB}. FT HELIX 119 128 {ECO:0000244|PDB:4CZB}. FT TURN 133 136 {ECO:0000244|PDB:4CZB}. FT HELIX 137 140 {ECO:0000244|PDB:4CZB}. FT TURN 141 144 {ECO:0000244|PDB:4CZB}. FT HELIX 147 174 {ECO:0000244|PDB:4CZB}. FT STRAND 177 179 {ECO:0000244|PDB:4CZB}. FT HELIX 183 211 {ECO:0000244|PDB:4CZB}. FT HELIX 215 217 {ECO:0000244|PDB:4CZB}. FT HELIX 218 233 {ECO:0000244|PDB:4CZB}. FT HELIX 236 240 {ECO:0000244|PDB:4CZB}. FT HELIX 248 264 {ECO:0000244|PDB:4CZB}. FT HELIX 269 295 {ECO:0000244|PDB:4CZB}. FT HELIX 298 317 {ECO:0000244|PDB:4CZB}. FT HELIX 319 327 {ECO:0000244|PDB:4CZB}. FT HELIX 335 343 {ECO:0000244|PDB:4CZB}. FT HELIX 349 364 {ECO:0000244|PDB:4CZB}. FT STRAND 368 371 {ECO:0000244|PDB:4CZB}. FT TURN 372 376 {ECO:0000244|PDB:4CZB}. FT HELIX 379 410 {ECO:0000244|PDB:4CZB}. SQ SEQUENCE 426 AA; 45966 MW; 967F9A3E60949A1D CRC64; MELMMAIGYL GLALVLGSLV AKIAEKLKIP DIPLLLLLGL IIGPFLQIIP SDSAMEIFEY AGPIGLIFIL LGGAFTMRIS LLKRVIKTVV RLDTITFLIT LLISGFIFNM VLNLPYTSPV GYLFGAITAA TDPATLIPVF SRVRTNPEVA ITLEAESIFN DPLGIVSTSV ILGLFGLFSS SNPLIDLITL AGGAIVVGLL LAKIYEKIII HCDFHEYVAP LVLGGAMLLL YVGDDLLPSI CGYGFSGYMA VAIMGLYLGD ALFRADDIDY KYIVSFCDDL SLLARVFIFV FLGACIKLSM LENYFIPGLL VALGSIFLAR PLGVFLGLIG SKHSFKEKLY FALEGPRGVV PAALAVTVGI EILKNADKIP ASITKYITPT DIAGTIIIGT FMTILLSVIL EASWAGMLAL KLLGEYKPKY KEESHH // ID NAOX_METJA Reviewed; 448 AA. AC Q58065; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2005, sequence version 2. DT 11-NOV-2015, entry version 106. DE RecName: Full=Putative NADH oxidase; DE Short=NOXase; DE EC=1.6.99.3; GN OrderedLocusNames=MJ0649; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the four-electron reduction of molecular CC oxygen to water. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NADH + acceptor = NAD(+) + reduced acceptor. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC Note=Binds 1 FAD per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-III pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98641.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98641.1; ALT_INIT; Genomic_DNA. DR PIR; A64381; A64381. DR ProteinModelPortal; Q58065; -. DR STRING; 243232.MJ_0649; -. DR EnsemblBacteria; AAB98641; AAB98641; MJ_0649. DR KEGG; mja:MJ_0649; -. DR eggNOG; arCOG01069; Archaea. DR eggNOG; COG0446; LUCA. DR InParanoid; Q58065; -. DR KO; K17870; -. DR OMA; RVWGRIM; -. DR PhylomeDB; Q58065; -. DR BRENDA; 1.6.3.3; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005623; C:cell; IEA:GOC. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0003954; F:NADH dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0045454; P:cell redox homeostasis; IEA:InterPro. DR Gene3D; 3.30.390.30; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016156; FAD/NAD-linked_Rdtase_dimer. DR InterPro; IPR004099; Pyr_nucl-diS_OxRdtase_dimer. DR Pfam; PF07992; Pyr_redox_2; 1. DR Pfam; PF02852; Pyr_redox_dim; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF55424; SSF55424; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; NAD; Oxidation; Oxidoreductase; KW Redox-active center; Reference proteome. FT CHAIN 1 448 Putative NADH oxidase. FT /FTId=PRO_0000184704. FT NP_BIND 7 11 FAD. {ECO:0000250}. FT NP_BIND 110 113 FAD. {ECO:0000250}. FT NP_BIND 152 167 NAD. {ECO:0000250}. FT NP_BIND 271 281 FAD. {ECO:0000250}. FT ACT_SITE 42 42 Redox-active. FT BINDING 42 42 FAD. {ECO:0000250}. FT BINDING 132 132 FAD. {ECO:0000250}. FT BINDING 243 243 NAD; via amide nitrogen. {ECO:0000250}. FT MOD_RES 42 42 Cysteine sulfenic acid (-SOH). FT {ECO:0000250}. SQ SEQUENCE 448 AA; 48876 MW; 8790664DF98D9DCD CRC64; MRAIIIGSGA AGLTTASTIR KYNKDMEIVV ITKEKEIAYS PCAIPYVIEG AIKSFDDIIM HTPEDYKRER NIDILTETTV IDVDSKNNKI KCVDKDGNEF EMNYDYLVLA TGAEPFIPPI EGKDLDGVFK VRTIEDGRAI LKYIEENGCK KVAVVGAGAI GLEMAYGLKC RGLDVLVVEM APQVLPRFLD PDMAEIVQKY LEKEGIKVML SKPLEKIVGK EKVEAVYVDG KLYDVDMVIM ATGVRPNIEL AKKAGCKIGK FAIEVNEKMQ TSIPNIYAVG DCVEVIDFIT GEKTLSPFGT AAVRQGKVAG KNIAGVEAKF YPVLNSAVSK IGDLEIGGTG LTAFSANLKR IPIVIGRAKA LTRARYYPGG KEIEIKMIFN EDGKVVGCQI VGGERVAERI DAMSIAIFKK VSAEELANME FCYAPPVSMV HEPLSLAAED ALKKLSNK // ID NDK_METJA Reviewed; 140 AA. AC Q58661; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Nucleoside diphosphate kinase; DE Short=NDK; DE Short=NDP kinase; DE EC=2.7.4.6; DE AltName: Full=Nucleoside-2-P kinase; GN Name=ndk; OrderedLocusNames=MJ1265; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=11053861; DOI=10.1107/S0907444900011240; RA Min K., Song H.K., Chang C., Lee J.Y., Eom S.H., Kim K.K., Yu Y.G., RA Suh S.W.; RT "Nucleoside diphosphate kinase from the hyperthermophilic archaeon RT Methanococcus jannaschii: overexpression, crystallization and RT preliminary X-ray crystallographic analysis."; RL Acta Crystallogr. D 56:1485-1487(2000). CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates CC other than ATP. The ATP gamma phosphate is transferred to the NDP CC beta phosphate via a ping-pong mechanism, using a phosphorylated CC active-site intermediate. CC -!- CATALYTIC ACTIVITY: ATP + nucleoside diphosphate = ADP + CC nucleoside triphosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Homohexamer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the NDK family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99271.1; -; Genomic_DNA. DR PIR; H64457; H64457. DR ProteinModelPortal; Q58661; -. DR SMR; Q58661; 3-139. DR STRING; 243232.MJ_1265; -. DR EnsemblBacteria; AAB99271; AAB99271; MJ_1265. DR KEGG; mja:MJ_1265; -. DR eggNOG; arCOG04313; Archaea. DR eggNOG; COG0105; LUCA. DR InParanoid; Q58661; -. DR KO; K00940; -. DR OMA; AEHSERP; -. DR PhylomeDB; Q58661; -. DR BRENDA; 2.7.4.6; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IBA:GO_Central. DR GO; GO:0006241; P:CTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006183; P:GTP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006228; P:UTP biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00451; NDP_kinase; 1. DR InterPro; IPR001564; Nucleoside_diP_kinase. DR InterPro; IPR023005; Nucleoside_diP_kinase_AS. DR Pfam; PF00334; NDK; 1. DR PRINTS; PR01243; NUCDPKINASE. DR SMART; SM00562; NDK; 1. DR PROSITE; PS00469; NDP_KINASES; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Magnesium; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Phosphoprotein; Reference proteome; Transferase. FT CHAIN 1 140 Nucleoside diphosphate kinase. FT /FTId=PRO_0000137091. FT ACT_SITE 116 116 Pros-phosphohistidine intermediate. FT {ECO:0000250}. FT BINDING 10 10 ATP. {ECO:0000250}. FT BINDING 58 58 ATP. {ECO:0000250}. FT BINDING 86 86 ATP. {ECO:0000250}. FT BINDING 92 92 ATP. {ECO:0000250}. FT BINDING 103 103 ATP. {ECO:0000250}. FT BINDING 113 113 ATP. {ECO:0000250}. SQ SEQUENCE 140 AA; 16224 MW; B22C60A248BF21F7 CRC64; MKERTFVALK PDAVKRKLIG KIIERFENKG FEIVAMKMIK LDREMAEKYY EEHKGKEFYE RLINFMTSGR MIVMVVEGEN AISVVRKMIG KTNPAEAEPG TIRGDFALTT PDNIIHASDS KESAEREIKL FFKEDEIFDK // ID NAH3_METJA Reviewed; 388 AA. AC Q58671; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=Probable Na(+)/H(+) antiporter 3; DE AltName: Full=MjNapA; GN OrderedLocusNames=MJ1275; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY TO NA(+)/H(+) ANTIPORTERS. RX PubMed=12220668; DOI=10.1016/S0014-5793(02)03244-1; RA Hellmer J., Paetzold R., Zeilinger C.; RT "Identification of a pH regulated Na(+)/H(+) antiporter of RT Methanococcus jannaschii."; RL FEBS Lett. 527:245-249(2002). CC -!- FUNCTION: This is probably a Na(+)/H(+) antiporter. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the monovalent cation:proton antiporter 1 CC (CPA1) transporter (TC 2.A.36) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99281.1; -; Genomic_DNA. DR PIR; B64459; B64459. DR ProteinModelPortal; Q58671; -. DR STRING; 243232.MJ_1275; -. DR EnsemblBacteria; AAB99281; AAB99281; MJ_1275. DR KEGG; mja:MJ_1275; -. DR eggNOG; arCOG01953; Archaea. DR eggNOG; COG0475; LUCA. DR InParanoid; Q58671; -. DR OMA; VLGMETN; -. DR PhylomeDB; Q58671; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0012505; C:endomembrane system; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005451; F:monovalent cation:proton antiporter activity; IBA:GO_Central. DR GO; GO:1902600; P:hydrogen ion transmembrane transport; IBA:GOC. DR GO; GO:0006885; P:regulation of pH; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IEA:UniProtKB-KW. DR InterPro; IPR006153; Cation/H_exchanger. DR Pfam; PF00999; Na_H_Exchanger; 1. PE 3: Inferred from homology; KW Antiport; Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Sodium; Sodium transport; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 388 Probable Na(+)/H(+) antiporter 3. FT /FTId=PRO_0000052404. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 102 122 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 215 235 Helical. {ECO:0000255}. FT TRANSMEM 263 283 Helical. {ECO:0000255}. FT TRANSMEM 294 314 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. FT TRANSMEM 354 374 Helical. {ECO:0000255}. SQ SEQUENCE 388 AA; 42180 MW; FF07E8CAEBA4F0CC CRC64; MESYYYVFFI ILSIIFIVPN LLKKFNIPAI TSIMIAGIII GPYGLNILQV DETLKILADF GAIMLMFLAG LEVDNETLKQ EFKNSLILSL FSLLIPGVGG YLIGQYLGLG FIGSLLYAVI FASHSVAIVY AILEELKMVK TRLGTIILSA TIIVDLFTLL LLSVVIKLGI GGENVGTFLL ETVLYIGVLL LAIPSLSKNI LGVFEKLHAQ RIHYVLFIIF IAIIVGEVIG IHPIVGAFIC GVAVSEALTK EEHDELLNKN LNAIGYGFFI PIFFLVLGME TNIRVIFNLS NLELLLITLI SAVALKFISG FIALRILGFD RIKNTIGGLL TVPKISASLV AASIGRELGL IGNEIFVTIV ALSVITATIT PIVVKHIFVA KCNKKAKN // ID NCPP_METJA Reviewed; 179 AA. AC Q57709; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2003, sequence version 4. DT 11-NOV-2015, entry version 84. DE RecName: Full=Probable non-canonical purine NTP phosphatase {ECO:0000255|HAMAP-Rule:MF_00648}; DE EC=3.6.1.- {ECO:0000255|HAMAP-Rule:MF_00648}; GN OrderedLocusNames=MJ0261; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Phosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP to their respective diphosphate CC derivatives. Probably excludes non-canonical purines from DNA CC precursor pool, thus preventing their incorporation into DNA and CC avoiding chromosomal lesions. {ECO:0000255|HAMAP-Rule:MF_00648}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleoside diphosphate + monophosphate. {ECO:0000255|HAMAP- CC Rule:MF_00648}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00648}; CC Note=Binds 1 divalent metal cation per subunit; can use either CC Mg(2+) or Mn(2+). {ECO:0000255|HAMAP-Rule:MF_00648}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00648}. CC -!- SIMILARITY: Belongs to the YjjX NTPase family. {ECO:0000255|HAMAP- CC Rule:MF_00648}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98247.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98247.1; ALT_INIT; Genomic_DNA. DR PIR; F64332; F64332. DR ProteinModelPortal; Q57709; -. DR STRING; 243232.MJ_0261; -. DR EnsemblBacteria; AAB98247; AAB98247; MJ_0261. DR KEGG; mja:MJ_0261; -. DR eggNOG; arCOG01221; Archaea. DR eggNOG; COG1986; LUCA. DR InParanoid; Q57709; -. DR OMA; EDDMTFA; -. DR PhylomeDB; Q57709; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009117; P:nucleotide metabolic process; IEA:UniProtKB-KW. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_00648; Non_canon_purine_NTPase_YjjX; 1. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR002786; Non_canon_purine_NTPase. DR InterPro; IPR026533; NTPase/PRRC1. DR Pfam; PF01931; NTPase_I-T; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00258; TIGR00258; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Manganese; Metal-binding; KW Nucleotide metabolism; Nucleotide-binding; Reference proteome. FT CHAIN 1 179 Probable non-canonical purine NTP FT phosphatase. FT /FTId=PRO_0000156359. FT REGION 13 18 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00648}. FT METAL 70 70 Manganese or magnesium. FT {ECO:0000255|HAMAP-Rule:MF_00648}. SQ SEQUENCE 179 AA; 19374 MW; DFAF307795C3633F CRC64; MARHKLRIVA VGSTNPVKIE AVKEGFEKVL GAVEVIGVDV ISGVSSHPIG LEETYLGALN RAKNAFEKVQ CTYAVGIEAG LIKVGEHYID IHICVVFDGV NETVGLSQGF EYPKIVAEKV LEGIEGGKIA EEISGIKDIG KNIGLIGYLT DNNITRKDLC RESVIMALIP RMIKNAHLY // ID NEP1_METJA Reviewed; 205 AA. AC Q57977; DT 10-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Ribosomal RNA small subunit methyltransferase Nep1; DE EC=2.1.1.-; DE AltName: Full=16S rRNA (pseudouridine-N1-)-methyltransferase Nep1; DE AltName: Full=16S rRNA Psi914 methyltransferase; GN Name=nep1; OrderedLocusNames=MJ0557; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP NMR STUDIES. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=19779849; DOI=10.1007/s12104-009-9187-z; RA Wurm J.P., Duchardt E., Meyer B., Leal B.Z., Kotter P., Entian K.D., RA Wohnert J.; RT "Backbone resonance assignments of the 48 kDa dimeric putative 18S RT rRNA-methyltransferase Nep1 from Methanocaldococcus jannaschii."; RL Biomol. NMR. Assign. 3:251-254(2009). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, RNA-BINDING, AND RNA-BINDING SITES. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=20047967; DOI=10.1093/nar/gkp1189; RA Wurm J.P., Meyer B., Bahr U., Held M., Frolow O., Kotter P., RA Engels J.W., Heckel A., Karas M., Entian K.D., Wohnert J.; RT "The ribosome assembly factor Nep1 responsible for Bowen-Conradi RT syndrome is a pseudouridine-N1-specific methyltransferase."; RL Nucleic Acids Res. 38:2387-2398(2010). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF APOPROTEIN AND COMPLEXES RP WITH S-ADENOSYL-L-HOMOCYSTEINE AND SINEFUNGIN INHIBITOR, SUBUNIT, AND RP RNA-BINDING SITES. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18208838; DOI=10.1093/nar/gkm1172; RA Taylor A.B., Meyer B., Leal B.Z., Kotter P., Schirf V., Demeler B., RA Hart P.J., Entian K.D., Wohnert J.; RT "The crystal structure of Nep1 reveals an extended SPOUT-class RT methyltransferase fold and a pre-organized SAM-binding site."; RL Nucleic Acids Res. 36:1542-1554(2008). CC -!- FUNCTION: Methyltransferase involved in ribosomal biogenesis. CC Specifically catalyzes the N1-methylation of pseudouridine at CC position 914 (Psi914) in 16S rRNA. Is not able to methylate CC uridine at this position. {ECO:0000269|PubMed:20047967}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + pseudouridine(914) CC in 16S rRNA = S-adenosyl-L-homocysteine + N(1)- CC methylpseudouridine(914) in 16S rRNA. CC {ECO:0000269|PubMed:20047967}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18208838}. CC -!- SIMILARITY: Belongs to the NEP1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98551.1; -; Genomic_DNA. DR PIR; E64369; E64369. DR PDB; 3BBD; X-ray; 2.15 A; A/B=1-205. DR PDB; 3BBE; X-ray; 2.20 A; A/B=1-205. DR PDB; 3BBH; X-ray; 2.25 A; A/B=1-205. DR PDBsum; 3BBD; -. DR PDBsum; 3BBE; -. DR PDBsum; 3BBH; -. DR ProteinModelPortal; Q57977; -. DR SMR; Q57977; 2-205. DR STRING; 243232.MJ_0557; -. DR EnsemblBacteria; AAB98551; AAB98551; MJ_0557. DR KEGG; mja:MJ_0557; -. DR eggNOG; arCOG04122; Archaea. DR eggNOG; COG1756; LUCA. DR InParanoid; Q57977; -. DR KO; K14568; -. DR OMA; LMAWTVC; -. DR PhylomeDB; Q57977; -. DR BRENDA; 2.1.1.257; 3260. DR BRENDA; 2.1.1.260; 3260. DR EvolutionaryTrace; Q57977; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0070037; F:rRNA (pseudouridine) methyltransferase activity; IDA:UniProtKB. DR GO; GO:0019843; F:rRNA binding; IDA:UniProtKB. DR GO; GO:0070475; P:rRNA base methylation; IDA:SGD. DR HAMAP; MF_00554; NEP1; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR005304; Rbsml_bgen_MeTrfase_EMG1/NEP1. DR InterPro; IPR023503; Ribosome_NEP1_arc. DR PANTHER; PTHR12636; PTHR12636; 1. DR Pfam; PF03587; EMG1; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; Ribosome biogenesis; RNA-binding; rRNA processing; KW rRNA-binding; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 205 Ribosomal RNA small subunit FT methyltransferase Nep1. FT /FTId=PRO_0000158616. FT REGION 141 143 S-adenosyl-L-methionine binding. FT REGION 185 190 S-adenosyl-L-methionine binding. FT BINDING 162 162 S-adenosyl-L-methionine; via amide FT nitrogen. FT BINDING 167 167 S-adenosyl-L-methionine; via carbonyl FT oxygen. FT SITE 54 54 Interaction with substrate rRNA. FT SITE 56 56 Stabilizes Arg-54. FT SITE 95 95 Interaction with substrate rRNA. FT SITE 98 98 Interaction with substrate rRNA. FT SITE 102 102 Interaction with substrate rRNA. FT STRAND 3 11 {ECO:0000244|PDB:3BBD}. FT HELIX 17 22 {ECO:0000244|PDB:3BBD}. FT HELIX 36 39 {ECO:0000244|PDB:3BBD}. FT TURN 40 45 {ECO:0000244|PDB:3BBD}. FT HELIX 49 51 {ECO:0000244|PDB:3BBD}. FT HELIX 55 66 {ECO:0000244|PDB:3BBD}. FT HELIX 69 72 {ECO:0000244|PDB:3BBD}. FT STRAND 76 82 {ECO:0000244|PDB:3BBD}. FT STRAND 85 90 {ECO:0000244|PDB:3BBD}. FT HELIX 100 111 {ECO:0000244|PDB:3BBD}. FT STRAND 117 123 {ECO:0000244|PDB:3BBD}. FT HELIX 126 132 {ECO:0000244|PDB:3BBD}. FT STRAND 137 141 {ECO:0000244|PDB:3BBD}. FT STRAND 145 147 {ECO:0000244|PDB:3BBD}. FT HELIX 150 155 {ECO:0000244|PDB:3BBD}. FT STRAND 157 162 {ECO:0000244|PDB:3BBD}. FT STRAND 164 167 {ECO:0000244|PDB:3BBD}. FT HELIX 173 175 {ECO:0000244|PDB:3BBD}. FT STRAND 177 188 {ECO:0000244|PDB:3BBD}. FT HELIX 192 204 {ECO:0000244|PDB:3BBD}. SQ SEQUENCE 205 AA; 24082 MW; 8D3E8BFDCD502831 CRC64; MTYNIILAKS ALELIPEEIK NKIRKSRVYK YDILDSNYHY KAMEKLKDKE MRGRPDIIHI SLLNILDSPI NHEKKLNIYI HTYDDKVLKI NPETRLPRNY FRFLGVMEKV LKGERNHLIK MEEKTLEDLL NEINAKKIAI MTKTGKLTHP KLLKEYDTFI IGGFPYGKLK INKEKVFGDI KEISIYNKGL MAWTVCGIIC YSLSF // ID NPPNK_METJA Reviewed; 574 AA. AC Q58327; DT 04-MAY-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 20-JAN-2016, entry version 103. DE RecName: Full=Bifunctional NADP phosphatase/NAD kinase; DE Includes: DE RecName: Full=NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; DE EC=2.7.1.23 {ECO:0000255|HAMAP-Rule:MF_00361}; DE AltName: Full=ATP-dependent NAD kinase {ECO:0000255|HAMAP-Rule:MF_00361}; DE AltName: Full=Poly(P)-dependent NAD kinase; DE Short=PPNK; DE Includes: DE RecName: Full=NADP phosphatase; DE Short=NADPase; DE Short=pNPPase; DE EC=3.1.3.-; GN OrderedLocusNames=MJ0917; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-8, FUNCTION, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME RP REGULATION, AND SUBUNIT. RX PubMed=16192277; DOI=10.1074/jbc.M506426200; RA Kawai S., Fukuda C., Mukai T., Murata K.; RT "MJ0917 in archaeon Methanococcus jannaschii is a novel NADP RT phosphatase/NAD kinase."; RL J. Biol. Chem. 280:39200-39207(2005). CC -!- FUNCTION: Involved in the regulation of the intracellular balance CC between NAD(H) and NADP(H), and is a key enzyme in the CC biosynthesis of NADP. Catalyzes the phosphorylation and CC dephosphorylation of NAD and NADP, respectively. Although it shows CC conflicting dual activities and is able to supply NADP, it seems CC that its physiological role is to prevent excess accumulation of CC NADP. Kinase can use ATP and other nucleoside triphosphates (UTP, CC TTP, CTP, GTP) as well as inorganic polyphosphate (poly(P)) as CC phosphoryl donors, however poly(P) is not considered to be the CC physiological phosphoryl donor. NAD is the preferred substrate for CC the kinase, but NADH can also be used as phosphoryl acceptor. CC Phosphatase can use NADP or NADPH as phosphoryl donor, but NADP is CC the preferred substrate. Phosphatase also has an activity toward CC the terminal phosphate group at C-2 of adenosine in 2'-AMP and CC toward the phosphate group at C-1 of fructose 1,6-bisphosphate, CC but not toward inositol 1-phosphate. CC {ECO:0000269|PubMed:16192277}. CC -!- CATALYTIC ACTIVITY: ATP + NAD(+) = ADP + NADP(+). CC {ECO:0000255|HAMAP-Rule:MF_00361, ECO:0000269|PubMed:16192277}. CC -!- CATALYTIC ACTIVITY: NADP(+) + H(2)O = NAD(+) + phosphate. CC {ECO:0000269|PubMed:16192277}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:16192277}; CC Note=Mg(2+). NAD and pNPPase kinase show maximum activities at 50 CC and 20 mM magnesium, respectively. {ECO:0000269|PubMed:16192277}; CC -!- ENZYME REGULATION: Phosphatase activity is slightly inhibited by CC ADP, NADPH and ATP, and moderately inhibited by NAD and 5'-AMP. CC Kinase activity is slightly inhibited by ADP and NADP. CC {ECO:0000269|PubMed:16192277}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.35 mM for ATP (for kinase activity at pH 8.5 and at 85 CC degrees Celsius) {ECO:0000269|PubMed:16192277}; CC KM=3 mM for NAD (for kinase activity at pH 8.5 and at 85 degrees CC Celsius) {ECO:0000269|PubMed:16192277}; CC Vmax=93.4 umol/min/mg enzyme toward ATP (for kinase activity at CC pH 8.5 and at 85 degrees Celsius) {ECO:0000269|PubMed:16192277}; CC Vmax=99.2 umol/min/mg enzyme toward NAD (for kinase activity at CC pH 8.5 and at 85 degrees Celsius) {ECO:0000269|PubMed:16192277}; CC Vmax=212 umol/min/mg enzyme toward NADP (for phosphatase CC activity at pH 8.5 and at 85 degrees Celsius) CC {ECO:0000269|PubMed:16192277}; CC Vmax=212 umol/min/mg enzyme toward fructose 1,6-bisphosphate CC (for phosphatase activity at pH 8.5 and at 85 degrees Celsius) CC {ECO:0000269|PubMed:16192277}; CC Vmax=236 umol/min/mg enzyme toward NADPH (for phosphatase CC activity at pH 8.5 and at 85 degrees Celsius) CC {ECO:0000269|PubMed:16192277}; CC Note=Kcat is 399 sec(-1) for kinase activity with ATP as CC substrate. Kcat is 424 sec(-1) for kinase activity with NAD as CC substrate. Kcat is 906 sec(-1) for phosphatase activity with CC fructose 1,6-bisphosphate and NADP as substrates. Kcat is 1007 CC sec(-1) for phosphatase activity with NADPH as substrate.; CC Temperature dependence: CC Optimum temperature is 100 degrees Celsius for phosphatase and CC kinase activies. Both are inactive below 60 degrees Celsius. CC {ECO:0000269|PubMed:16192277}; CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:16192277}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00361}. CC -!- MISCELLANEOUS: The phosphatase is inert toward the substrates of CC NAD kinase (NAD, NADH, ATP, and poly(P)). This demonstrates that CC the phosphatase activity never interferes with the NAD kinase CC activity by degrading its substrates (PubMed:16192277). CC {ECO:0000305|PubMed:16192277}. CC -!- SIMILARITY: In the N-terminal section; belongs to the inositol CC monophosphatase family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NAD kinase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98922.1; -; Genomic_DNA. DR PIR; E64414; E64414. DR ProteinModelPortal; Q58327; -. DR STRING; 243232.MJ_0917; -. DR EnsemblBacteria; AAB98922; AAB98922; MJ_0917. DR KEGG; mja:MJ_0917; -. DR eggNOG; arCOG01348; Archaea. DR eggNOG; COG0061; LUCA. DR eggNOG; COG0483; LUCA. DR InParanoid; Q58327; -. DR KO; K00858; -. DR OMA; PLIGWEK; -. DR BRENDA; 2.7.1.23; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB. DR GO; GO:0003951; F:NAD+ kinase activity; IDA:UniProtKB. DR GO; GO:0019178; F:NADP phosphatase activity; IDA:UniProtKB. DR GO; GO:0016311; P:dephosphorylation; IDA:GOC. DR GO; GO:0006553; P:lysine metabolic process; IEA:InterPro. DR GO; GO:0019674; P:NAD metabolic process; IEA:InterPro. DR GO; GO:0006741; P:NADP biosynthetic process; IDA:UniProtKB. DR GO; GO:0046854; P:phosphatidylinositol phosphorylation; IEA:InterPro. DR Gene3D; 2.60.200.30; -; 1. DR Gene3D; 3.40.50.10330; -; 1. DR HAMAP; MF_00361; NAD_kinase; 1. DR InterPro; IPR017438; ATP-NAD_kinase_dom_1. DR InterPro; IPR017437; ATP-NAD_kinase_PpnK-typ_all-b. DR InterPro; IPR021175; Bifunctional_PpnK_predicted. DR InterPro; IPR020583; Inositol_monoP_metal-BS. DR InterPro; IPR000760; Inositol_monophosphatase. DR InterPro; IPR016064; NAD/diacylglycerol_kinase. DR InterPro; IPR002504; NADK. DR PANTHER; PTHR20275; PTHR20275; 2. DR Pfam; PF00459; Inositol_P; 2. DR Pfam; PF01513; NAD_kinase; 1. DR PIRSF; PIRSF036641; Bifunctional_PpnK_predicted; 1. DR PRINTS; PR00377; IMPHPHTASES. DR SUPFAM; SSF111331; SSF111331; 1. DR PROSITE; PS00629; IMP_1; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Cytoplasm; Direct protein sequencing; KW Hydrolase; Kinase; Magnesium; Metal-binding; Multifunctional enzyme; KW NAD; NADP; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 574 Bifunctional NADP phosphatase/NAD kinase. FT /FTId=PRO_0000120700. FT NP_BIND 362 363 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 436 437 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT NP_BIND 477 482 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT REGION 1 297 NADP phosphatase. FT REGION 302 574 NAD kinase. FT ACT_SITE 362 362 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00361}. FT METAL 69 69 Magnesium 1. {ECO:0000250}. FT METAL 87 87 Magnesium 1. {ECO:0000250}. FT METAL 87 87 Magnesium 2. {ECO:0000250}. FT METAL 90 90 Magnesium 2. {ECO:0000250}. FT METAL 243 243 Magnesium 2. {ECO:0000250}. FT BINDING 90 90 Substrate. {ECO:0000250}. FT BINDING 367 367 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 447 447 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 464 464 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 466 466 NAD. {ECO:0000255|HAMAP-Rule:MF_00361}. FT BINDING 474 474 NAD; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00361}. SQ SEQUENCE 574 AA; 64119 MW; 89A1AF944BD99DB1 CRC64; MVIMEGFKIA MKVIDEIDKK IKPLIGWEKA DEVVKIGADG TPTKRIDVIA ENMAINILEK FSGGILISEE IGLKVVGDEL EYIFILDPID GTYNALKSIP IYSTSIAVAK IKGEDKKLIR ENINNIDWIK SFIANKYTIN DLYVGIVKNL ATGDLYYAIK GEGSFLEKDG EKIKIETKNI KDLKEASVGL FVYGLSNDLL EFLKERKVRR VRLFGSMALE MCYVVSGALD AYINVNENSR LCDIAGAYVI CREGNAIVTN KNGKPLNMKL HLMERTSLIV SNKYLHKKLI ALFGNRWIIK PVKFGIVVRE DKEEAINLAI EICKYLKDKN IPFCVEDFLR ERVGGDKFDI SAISHIIAIG GDGTILRASR LVNGETIPII AVNMGKVGFL AEFCKDEVFE IIDKVIYGEY EIEKRSKLSC KIIKDNRVIK TPSALNEMVV ITKNPAKILE FDVYVNDTLV ENVRADGIIV STPTGSTAYS LSAGGPIVEP NVDCFIISPI CPFKLSSRPL VISASNRIKL KLKLEKPALL VIDGSVEYEI NKDDELIFEK SDSYAYFVKG QSFYNKLSRC LGIK // ID NOB1_METJA Reviewed; 197 AA. AC Q58869; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Endoribonuclease Nob1; DE Short=RNase Nob1; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Endonuclease VapC5; DE AltName: Full=Putative toxin VapC5 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=nob1; Synonyms=vapC5; OrderedLocusNames=MJ1474; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. CC Processes pre-16S-rRNA at its 3' end (the D-site) to yield the CC mature 3' end (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- DOMAIN: Has 2 structurally independent domains; the N-terminal CC PINc domain which binds Mn(2+), rRNA substrate and probably has CC endoribonuclease activity, and the C-terminal zinc ribbon domain CC which also binds rRNA substrate. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99480.1; -; Genomic_DNA. DR PIR; A64484; A64484. DR ProteinModelPortal; Q58869; -. DR STRING; 243232.MJ_1474; -. DR EnsemblBacteria; AAB99480; AAB99480; MJ_1474. DR KEGG; mja:MJ_1474; -. DR eggNOG; arCOG00721; Archaea. DR eggNOG; COG1439; LUCA. DR InParanoid; Q58869; -. DR KO; K07060; -. DR OMA; MQNVAEK; -. DR PhylomeDB; Q58869; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030688; C:preribosome, small subunit precursor; IBA:GO_Central. DR GO; GO:0004521; F:endoribonuclease activity; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0000469; P:cleavage involved in rRNA processing; IBA:GO_Central. DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR033411; Ribonuclease_PIN. DR InterPro; IPR022907; VapC_family. DR Pfam; PF17146; PIN_6; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Manganese; Metal-binding; KW Nuclease; Reference proteome; Ribosome biogenesis; RNA-binding; KW rRNA-binding; Toxin; Zinc. FT CHAIN 1 197 Endoribonuclease Nob1. FT /FTId=PRO_0000156045. FT DOMAIN 35 141 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT REGION 147 152 Flexible linker. {ECO:0000250}. FT REGION 153 188 Zinc ribbon. {ECO:0000250}. FT COMPBIAS 181 197 Lys-rich. FT METAL 37 37 Manganese. {ECO:0000255}. FT METAL 158 158 Zinc. {ECO:0000250}. FT METAL 161 161 Zinc. {ECO:0000250}. FT METAL 174 174 Zinc. {ECO:0000250}. FT METAL 177 177 Zinc. {ECO:0000250}. SQ SEQUENCE 197 AA; 22781 MW; 70075BB626934F58 CRC64; MLSLPPPEFY KLWIINKSPY QLFNIYRSGI MKVKVLDASA IIHGYNPIIE EGEHYTTPEV LEEIESKKII VEQALDFGKL KIMSPNREYI KKVEEVVKKT GDNLSQQDIG VLALALNLNA ILYTDDYGIQ NVAKKLNIEV RGIAFEPTNK DFIWRKICEG CKKLYPVDYE EDICEICGSP LKRKMVKSRL KKKRKKK // ID NIFH_METJA Reviewed; 279 AA. AC Q58289; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=Nitrogenase iron protein; DE EC=1.18.6.1; DE AltName: Full=Nitrogenase Fe protein; DE AltName: Full=Nitrogenase component II; DE AltName: Full=Nitrogenase reductase; GN Name=nifH; OrderedLocusNames=MJ0879; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are CC catalyzed by the nitrogenase complex, which has 2 components: the CC iron protein and the molybdenum-iron protein. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP CC + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 CC phosphate. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- PTM: The reversible ADP-ribosylation of Arg-97 inactivates the CC nitrogenase reductase and regulates nitrogenase activity. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98883.1; -; Genomic_DNA. DR PIR; G64409; G64409. DR ProteinModelPortal; Q58289; -. DR SMR; Q58289; 1-269. DR STRING; 243232.MJ_0879; -. DR EnsemblBacteria; AAB98883; AAB98883; MJ_0879. DR KEGG; mja:MJ_0879; -. DR eggNOG; arCOG00590; Archaea. DR eggNOG; COG1348; LUCA. DR InParanoid; Q58289; -. DR KO; K02588; -. DR OMA; FAMPLQK; -. DR PhylomeDB; Q58289; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00533; NifH; 1. DR InterPro; IPR030655; NifH/chlL_CS. DR InterPro; IPR000392; Nitogenase_NifH/Reductase_ChlL. DR InterPro; IPR005977; Nitrogenase_Fe_NifH. DR InterPro; IPR027417; P-loop_NTPase. DR PIRSF; PIRSF000363; Nitrogenase_iron; 1. DR PRINTS; PR00091; NITROGNASEII. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01287; nifH; 1. DR PROSITE; PS00746; NIFH_FRXC_1; 1. DR PROSITE; PS00692; NIFH_FRXC_2; 1. DR PROSITE; PS51026; NIFH_FRXC_3; 1. PE 3: Inferred from homology; KW 4Fe-4S; ADP-ribosylation; ATP-binding; Complete proteome; Iron; KW Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 279 Nitrogenase iron protein. FT /FTId=PRO_0000139539. FT NP_BIND 8 15 ATP. {ECO:0000255}. FT METAL 94 94 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000250}. FT METAL 130 130 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000250}. FT MOD_RES 97 97 ADP-ribosylarginine; by dinitrogenase FT reductase ADP-ribosyltransferase. FT {ECO:0000250}. SQ SEQUENCE 279 AA; 30167 MW; 56DC15F981A20C54 CRC64; MRKFCVYGKG GIGKSTTVSN IAAALAEDGK KVLVVGCDPK ADTTRNLVGR KIPTVLDVFR KKGAENMKLE DIVFEGFGGV YCVESGGPEP GVGCAGRGVI TAVDMLNRLG AFEELKPDVV IYDILGDVVC GGFAMPLQKH LADDVYIVTT CDPMAIYAAN NICKGIKRYA SRGKIALGGI IYNGRSVIDA PEIVKDFAKK IGTQVIGKIP MSNIITRAEI YKKTVIEYAP DSEIANTFRE IAKAIYENEN RVIPNPLSEE ELDEITEKID VLLKESVKG // ID NIKR_METJA Reviewed; 141 AA. AC Q57969; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Putative nickel-responsive regulator {ECO:0000255|HAMAP-Rule:MF_00476}; GN OrderedLocusNames=MJ0549; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Transcriptional regulator. {ECO:0000255|HAMAP- CC Rule:MF_00476}. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00476}; CC Note=Binds 1 nickel ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00476}; CC -!- SUBUNIT: Homotetramer. {ECO:0000255|HAMAP-Rule:MF_00476}. CC -!- SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR CC family. {ECO:0000255|HAMAP-Rule:MF_00476}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98541.1; -; Genomic_DNA. DR PIR; E64368; E64368. DR ProteinModelPortal; Q57969; -. DR SMR; Q57969; 3-132. DR STRING; 243232.MJ_0549; -. DR EnsemblBacteria; AAB98541; AAB98541; MJ_0549. DR KEGG; mja:MJ_0549; -. DR eggNOG; arCOG01008; Archaea. DR eggNOG; COG0864; LUCA. DR InParanoid; Q57969; -. DR KO; K07722; -. DR OMA; AHNCLET; -. DR PhylomeDB; Q57969; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016151; F:nickel cation binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0010045; P:response to nickel cation; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.1220.10; -; 1. DR HAMAP; MF_00476; NikR; 1. DR InterPro; IPR013321; Arc_rbn_hlx_hlx. DR InterPro; IPR002145; CopG. DR InterPro; IPR022988; Ni_resp_reg_NikR. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR014864; TF_NikR_Ni-bd_C. DR Pfam; PF08753; NikR_C; 1. DR Pfam; PF01402; RHH_1; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Metal-binding; Nickel; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 141 Putative nickel-responsive regulator. FT /FTId=PRO_0000139302. FT METAL 80 80 Nickel. {ECO:0000255|HAMAP- FT Rule:MF_00476}. FT METAL 91 91 Nickel. {ECO:0000255|HAMAP- FT Rule:MF_00476}. FT METAL 93 93 Nickel. {ECO:0000255|HAMAP- FT Rule:MF_00476}. FT METAL 99 99 Nickel. {ECO:0000255|HAMAP- FT Rule:MF_00476}. SQ SEQUENCE 141 AA; 16133 MW; 5BE0C5F09D38B5ED CRC64; MTEMDRISIS LPSKLLREFD EIIAERGYAS RSEAIRDAIR DYIIKHKWIH SLEGERAGSI SVIYNHHASD VMEKITEIQH NYTDIIVATL HLHLDHDHCL ETILVRGDAK RIRELTDRLT ALKGVKQVKL SVMVPGGQIP E // ID NTPTH_METJA Reviewed; 170 AA. AC Q58954; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 2. DT 11-NOV-2015, entry version 93. DE RecName: Full=Nucleoside-triphosphatase THEP1; DE Short=NTPase THEP1; DE EC=3.6.1.15; DE AltName: Full=Nucleoside triphosphate phosphohydrolase; GN OrderedLocusNames=MJ1559; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CC CTP, TTP and UTP. May hydrolyze nucleoside diphosphates with lower CC efficiency (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: NTP + H(2)O = NDP + phosphate. CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99578.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99578.1; ALT_INIT; Genomic_DNA. DR PIR; F64494; F64494. DR ProteinModelPortal; Q58954; -. DR STRING; 243232.MJ_1559; -. DR PRIDE; Q58954; -. DR EnsemblBacteria; AAB99578; AAB99578; MJ_1559. DR KEGG; mja:MJ_1559; -. DR eggNOG; arCOG01034; Archaea. DR eggNOG; COG1618; LUCA. DR InParanoid; Q58954; -. DR KO; K06928; -. DR OMA; IFITGMP; -. DR PhylomeDB; Q58954; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0098519; F:nucleotide phosphatase activity, acting on free nucleotides; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_00796; NTPase_1; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR004948; Nuc-triphosphatase_THEP1. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03266; NTPase_1; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Hydrolase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 170 Nucleoside-triphosphatase THEP1. FT /FTId=PRO_0000146696. FT NP_BIND 7 14 ATP. {ECO:0000250}. FT NP_BIND 98 105 ATP. {ECO:0000250}. SQ SEQUENCE 170 AA; 19088 MW; 48DBF7DA574109F6 CRC64; MRIFITGMPG VGKTTLALKI AEKLKELGYK VGGFITKEIR DGGKRVGFKI ITLDTNEETI LAYVGDGKIK VGKYAVFIEN LDNVGVEAIK RALKDADIII IDELGAMEFK SRKFSEVVDE VIKSDKPLLA TLHRNWVNKF KDKGELYTLT IENREKLFEE ILNKILAGLK // ID NNR_METJA Reviewed; 491 AA. AC Q58981; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Bifunctional NAD(P)H-hydrate repair enzyme Nnr; DE AltName: Full=Nicotinamide nucleotide repair protein; DE Includes: DE RecName: Full=ADP-dependent (S)-NAD(P)H-hydrate dehydratase; DE EC=4.2.1.136; DE AltName: Full=ADP-dependent NAD(P)HX dehydratase; DE Includes: DE RecName: Full=NAD(P)H-hydrate epimerase; DE EC=5.1.99.6; DE AltName: Full=NAD(P)HX epimerase; GN Name=nnr; OrderedLocusNames=MJ1586; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Bifunctional enzyme that catalyzes the epimerization of CC the S- and R-forms of NAD(P)HX and the dehydration of the S-form CC of NAD(P)HX at the expense of ADP, which is converted to AMP. This CC allows the repair of both epimers of NAD(P)HX, a damaged form of CC NAD(P)H that is a result of enzymatic or heat-dependent hydration CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide = AMP + phosphate + CC NADH. CC -!- CATALYTIC ACTIVITY: ADP + (6S)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide adenine-dinucleotide phosphate = AMP + CC phosphate + NADPH. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy- CC 1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. CC -!- CATALYTIC ACTIVITY: (6R)-6-beta-hydroxy-1,4,5,6- CC tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6- CC beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide CC phosphate. CC -!- COFACTOR: CC Name=K(+); Xref=ChEBI:CHEBI:29103; Evidence={ECO:0000250}; CC Note=Binds 1 potassium ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: In the N-terminal section; belongs to the NnrE/AIBP CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the NnrD/CARKD CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 YjeF C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 YjeF N-terminal domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99605.1; -; Genomic_DNA. DR PIR; A64498; A64498. DR ProteinModelPortal; Q58981; -. DR STRING; 243232.MJ_1586; -. DR EnsemblBacteria; AAB99605; AAB99605; MJ_1586. DR KEGG; mja:MJ_1586; -. DR eggNOG; arCOG00018; Archaea. DR eggNOG; ENOG4102TCZ; Archaea. DR eggNOG; COG0062; LUCA. DR eggNOG; COG0063; LUCA. DR InParanoid; Q58981; -. DR KO; K17758; -. DR KO; K17759; -. DR OMA; YGAPYLA; -. DR PhylomeDB; Q58981; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.50.10260; -; 1. DR HAMAP; MF_01965; NADHX_dehydratase; 1. DR HAMAP; MF_01966; NADHX_epimerase; 1. DR InterPro; IPR017953; Carbohydrate_kinase_pred_CS. DR InterPro; IPR000631; CARKD. DR InterPro; IPR030677; Nnr. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR004443; YjeF_N_dom. DR Pfam; PF01256; Carb_kinase; 1. DR Pfam; PF03853; YjeF_N; 1. DR PIRSF; PIRSF017184; Nnr; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR SUPFAM; SSF64153; SSF64153; 1. DR TIGRFAMs; TIGR00196; yjeF_cterm; 1. DR TIGRFAMs; TIGR00197; yjeF_nterm; 1. DR PROSITE; PS01049; YJEF_C_1; 1. DR PROSITE; PS01050; YJEF_C_2; 1. DR PROSITE; PS51383; YJEF_C_3; 1. DR PROSITE; PS51385; YJEF_N; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Isomerase; Lyase; Metal-binding; KW Multifunctional enzyme; NAD; NADP; Nucleotide-binding; Potassium; KW Reference proteome. FT CHAIN 1 491 Bifunctional NAD(P)H-hydrate repair FT enzyme Nnr. FT /FTId=PRO_0000119051. FT DOMAIN 35 230 YjeF N-terminal. FT DOMAIN 232 490 YjeF C-terminal. FT NP_BIND 404 408 ADP. {ECO:0000250}. FT NP_BIND 423 432 ADP. {ECO:0000250}. FT REGION 1 230 NAD(P)H-hydrate epimerase. {ECO:0000250}. FT REGION 80 84 NAD(P)HX (for epimerase activity). FT {ECO:0000250}. FT REGION 158 164 NAD(P)HX (for epimerase activity). FT {ECO:0000250}. FT REGION 232 491 ADP-dependent (S)-NAD(P)H-hydrate FT dehydratase. {ECO:0000250}. FT REGION 380 386 NAD(P)HX (for dehydratase activity). FT {ECO:0000250}. FT METAL 81 81 Potassium. {ECO:0000250}. FT METAL 154 154 Potassium. {ECO:0000250}. FT METAL 195 195 Potassium. {ECO:0000250}. FT BINDING 192 192 NAD(P)HX (for epimerase activity). FT {ECO:0000250}. FT BINDING 332 332 NAD(P)HX (for dehydratase activity); via FT amide nitrogen. {ECO:0000250}. FT BINDING 433 433 NAD(P)HX (for dehydratase activity). FT {ECO:0000250}. SQ SEQUENCE 491 AA; 54979 MW; 6F8994706685F6F2 CRC64; MRRDINNFLF GERMELFEIL KQKIKEKEVI TPKEMAIIDD NAEFLGIQKI LLMENAGKAV YEEIKDIDAE EFIIFCGTGN NGGDGFVVAR HLGKGDVILI GKESEIKTYE ARENFKILKN LAEFGNIRIR EIKWAEEVND IFERLKNKKA VIIDAMIGTG VKGELREPFK TIVDKINELK QINKNIFVIS VDVETGHLES DLTITFHKRK TINKDNAIVK KIGIPKEAEY IVGWGDLKAL RKRDSNSHKG QNGKVLIIGG SKDFYGAPIL AGLAALKIVD LVGILSVGKV IDKVNHPEFI MYRVEGDYLS SQHVDYTLEI AKKYDVVVLG NGLGANNRTK AFLNEFLAKY DGKVVIDADA IKVIDYNNFE FSENYIFTPH KREFEYMGID LDNIENIKST IVLKGKYDII FNANNLKINK TGNAGLTKGG TGDVLAGLIG ALFAVNEAFL SACCGAFING YAGDLLLKEK GYYYTPLDLI EKIPNVLKIF Q // ID NRPR_METJA Reviewed; 542 AA. AC Q57623; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 82. DE RecName: Full=Global nitrogen regulator NrpR {ECO:0000305}; DE AltName: Full=Nitrogen regulatory protein R {ECO:0000305}; GN Name=nrpR {ECO:0000303|PubMed:21070950}; GN OrderedLocusNames=MJ0159 {ECO:0000312|EMBL:AAB98143.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.50 ANGSTROMS) OF 306-542, DNA-BINDING, ENZYME RP REGULATION, AND SUBUNIT. RX PubMed=21070950; DOI=10.1016/j.str.2010.08.014; RA Wisedchaisri G., Dranow D.M., Lie T.J., Bonanno J.B., Patskovsky Y., RA Ozyurt S.A., Sauder J.M., Almo S.C., Wasserman S.R., Burley S.K., RA Leigh J.A., Gonen T.; RT "Structural underpinnings of nitrogen regulation by the prototypical RT nitrogen-responsive transcriptional factor NrpR."; RL Structure 18:1512-1521(2010). CC -!- FUNCTION: Transcriptional repressor of nitrogen fixation and CC assimilation genes. Binds to two tandem operators in the glnA and CC nif promoters, thereby blocking transcription of the genes. CC {ECO:0000250|UniProtKB:Q6LZL7}. CC -!- ENZYME REGULATION: Under nitrogen limitation, binding of the CC intracellular nitrogen metabolite 2-oxoglutarate to NrpR decreases CC the binding affinity of NrpR to DNA, leading to initiation of CC transcription. {ECO:0000269|PubMed:21070950}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21070950}. CC -!- MISCELLANEOUS: Adopts different quaternary structures in its CC active apo state compared with its inhibited 2-oxoglutarate-bound CC state. In the 2-oxoglutarate-bound state, NrpR is inhibited from CC binding to DNA because its DNA-binding domains are too far apart CC to recognize the operator DNA sequence. CC {ECO:0000269|PubMed:21070950}. CC -!- SIMILARITY: Belongs to the NrpR family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98143.1; -; Genomic_DNA. DR PIR; H64319; H64319. DR PDB; 3NEK; X-ray; 2.50 A; A/B=306-542. DR PDBsum; 3NEK; -. DR ProteinModelPortal; Q57623; -. DR SMR; Q57623; 318-539. DR DIP; DIP-59016N; -. DR STRING; 243232.MJ_0159; -. DR DNASU; 1451006; -. DR EnsemblBacteria; AAB98143; AAB98143; MJ_0159. DR KEGG; mja:MJ_0159; -. DR eggNOG; arCOG02710; Archaea. DR eggNOG; COG1693; LUCA. DR InParanoid; Q57623; -. DR KO; K09720; -. DR OMA; DPHEVFF; -. DR PhylomeDB; Q57623; -. DR EvolutionaryTrace; Q57623; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.1360; -; 2. DR InterPro; IPR002846; DUF128. DR InterPro; IPR013668; RNase_R_HTH_12. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01995; DUF128; 2. DR Pfam; PF08461; HTH_12; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome; KW Repeat; Repressor; Transcription; Transcription regulation. FT CHAIN 1 542 Global nitrogen regulator NrpR. FT /FTId=PRO_0000106723. FT REGION 12 77 Winged helix-turn-helix. {ECO:0000305}. FT REGION 85 320 NRD 1. {ECO:0000305|PubMed:21070950}. FT REGION 321 542 NRD 2. {ECO:0000305|PubMed:21070950}. FT HELIX 325 333 {ECO:0000244|PDB:3NEK}. FT TURN 340 343 {ECO:0000244|PDB:3NEK}. FT STRAND 346 355 {ECO:0000244|PDB:3NEK}. FT HELIX 356 358 {ECO:0000244|PDB:3NEK}. FT HELIX 359 371 {ECO:0000244|PDB:3NEK}. FT STRAND 375 384 {ECO:0000244|PDB:3NEK}. FT STRAND 386 394 {ECO:0000244|PDB:3NEK}. FT HELIX 397 405 {ECO:0000244|PDB:3NEK}. FT STRAND 410 420 {ECO:0000244|PDB:3NEK}. FT STRAND 425 433 {ECO:0000244|PDB:3NEK}. FT HELIX 440 443 {ECO:0000244|PDB:3NEK}. FT HELIX 445 447 {ECO:0000244|PDB:3NEK}. FT STRAND 450 462 {ECO:0000244|PDB:3NEK}. FT TURN 463 465 {ECO:0000244|PDB:3NEK}. FT HELIX 466 476 {ECO:0000244|PDB:3NEK}. FT STRAND 481 484 {ECO:0000244|PDB:3NEK}. FT STRAND 500 506 {ECO:0000244|PDB:3NEK}. FT HELIX 510 517 {ECO:0000244|PDB:3NEK}. FT STRAND 523 532 {ECO:0000244|PDB:3NEK}. FT HELIX 533 535 {ECO:0000244|PDB:3NEK}. FT STRAND 536 538 {ECO:0000244|PDB:3NEK}. SQ SEQUENCE 542 AA; 61195 MW; 5C7FC0734338AE0F CRC64; MIIMADLDRK LIEILDILSK SKEPVGAKII AKELNKRGYK IGERAVRYHL KLLDGMKLTK KVGYAGRVIT ERGLEELEKA NISYRLGSIY SNILEKTISA NYRFGYVVIN RCQVYADFND VLKIIKSVYE SGLAVGDRVG IIDREKFVEI NTLCSLNFDN ILLQNGIFPL HVCAGVVKYE DGKPVEFKEI IDYKSTSIDP LRAFIEKKET DVMGIIENGE GYLPANFRYF GVEFLERFET ILEIDELKCI ISYGTENVLG LDVGDDKVGV ALIGGLTPIA PFVENNYCVE ICPMSSIVRL ESLHKLKKNP RDIVTKKANI RIKTALSKMF NAMAKVTYDI DEADGDVIVN TAFIDKKYLD EAFDILKEAY KKGLGISDRF GIVEENDRIK IQTICAVTLD GIFLRNSVPL IPKYGGILEI TEDKERFIDI IGYDGSSLDP HEVFFNFVDC EKTFLAGFRE VHRVAREKLE EVLKKLNWNG IKAIGEPNNE LYGIGVNKDM CGVVTMGGIN PLVLLKENEI PIELKAMHEV VRFSDLKSYK EI // ID NTPA_METJA Reviewed; 185 AA. AC Q57679; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-JUN-2011, sequence version 2. DT 11-NOV-2015, entry version 110. DE RecName: Full=Non-canonical purine NTP pyrophosphatase; DE EC=3.6.1.19; DE AltName: Full=Non-standard purine NTP pyrophosphatase; DE AltName: Full=Nucleoside-triphosphate diphosphatase; DE AltName: Full=Nucleoside-triphosphate pyrophosphatase; DE Short=NTPase; GN OrderedLocusNames=MJ0226; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, RP SUBSTRATE SPECIFICITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND RP SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10404228; DOI=10.1038/10745; RA Hwang K.Y., Chung J.H., Kim S.-H., Han Y.S., Cho Y.; RT "Structure-based identification of a novel NTPase from Methanococcus RT jannaschii."; RL Nat. Struct. Biol. 6:691-696(1999). CC -!- FUNCTION: Pyrophosphatase that hydrolyzes non-canonical purine CC nucleotides such as XTP and ITP to their respective monophosphate CC derivatives. Probably excludes non-canonical purines from DNA CC precursor pool, thus preventing their incorporation into DNA and CC avoiding chromosomal lesions. {ECO:0000269|PubMed:10404228}. CC -!- CATALYTIC ACTIVITY: A nucleoside triphosphate + H(2)O = a CC nucleotide + diphosphate. {ECO:0000269|PubMed:10404228}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:10404228}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:10404228}; CC Note=Binds 1 divalent cation per subunit; can use either Mg(2+) or CC Mn(2+). {ECO:0000269|PubMed:10404228}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.10 mM for XTP {ECO:0000269|PubMed:10404228}; CC KM=0.15 mM for ITP {ECO:0000269|PubMed:10404228}; CC KM=1.11 mM for GTP {ECO:0000269|PubMed:10404228}; CC KM=1.13 mM for dGTP {ECO:0000269|PubMed:10404228}; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius. CC {ECO:0000269|PubMed:10404228}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10404228}. CC -!- MISCELLANEOUS: XTP is the best substrate, followed by ITP, GTP or CC dGTP, both of which are hydrolyzed 100-fold less efficiently than CC XTP, and finally ATP, CTP and TTP which are hydrolyzed the least CC well. XDP or GDP are not hydrolyzed to XMP or GMP, suggesting that CC Mj0226 is a pyrophosphate-releasing NTPase. CC -!- SIMILARITY: Belongs to the HAM1 NTPase family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98211.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98211.1; ALT_INIT; Genomic_DNA. DR PIR; C64328; C64328. DR PDB; 1B78; X-ray; 2.20 A; A/B=1-185. DR PDB; 2MJP; X-ray; 2.20 A; A/B=1-185. DR PDBsum; 1B78; -. DR PDBsum; 2MJP; -. DR STRING; 243232.MJ_0226; -. DR EnsemblBacteria; AAB98211; AAB98211; MJ_0226. DR KEGG; mja:MJ_0226; -. DR eggNOG; arCOG04184; Archaea. DR eggNOG; COG0127; LUCA. DR InParanoid; Q57679; -. DR KO; K02428; -. DR BRENDA; 3.6.1.66; 3260. DR BRENDA; 3.6.1.B14; 3260. DR EvolutionaryTrace; Q57679; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:InterPro. DR GO; GO:0047429; F:nucleoside-triphosphate diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0009143; P:nucleoside triphosphate catabolic process; IEA:InterPro. DR GO; GO:0006163; P:purine nucleotide metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.950.10; -; 1. DR HAMAP; MF_01405; Non_canon_purine_NTPase; 1. DR InterPro; IPR002637; Ham1p-like. DR InterPro; IPR029001; ITPase-like_fam. DR InterPro; IPR020922; NTPase. DR PANTHER; PTHR11067; PTHR11067; 1. DR Pfam; PF01725; Ham1p_like; 1. DR SUPFAM; SSF52972; SSF52972; 1. DR TIGRFAMs; TIGR00042; TIGR00042; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Magnesium; Manganese; KW Metal-binding; Nucleotide metabolism; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 185 Non-canonical purine NTP pyrophosphatase. FT /FTId=PRO_0000178274. FT REGION 7 12 Substrate binding. {ECO:0000250}. FT REGION 65 66 Substrate binding. {ECO:0000250}. FT METAL 37 37 Manganese or magnesium. {ECO:0000250}. FT METAL 65 65 Manganese or magnesium. {ECO:0000250}. FT BINDING 144 144 Substrate. {ECO:0000250}. FT BINDING 164 164 Substrate. {ECO:0000250}. FT BINDING 170 170 Substrate. {ECO:0000250}. FT STRAND 3 6 {ECO:0000244|PDB:1B78}. FT HELIX 10 19 {ECO:0000244|PDB:1B78}. FT TURN 20 22 {ECO:0000244|PDB:1B78}. FT STRAND 28 31 {ECO:0000244|PDB:1B78}. FT STRAND 38 40 {ECO:0000244|PDB:1B78}. FT HELIX 42 57 {ECO:0000244|PDB:1B78}. FT STRAND 61 70 {ECO:0000244|PDB:1B78}. FT HELIX 71 73 {ECO:0000244|PDB:1B78}. FT HELIX 81 87 {ECO:0000244|PDB:1B78}. FT HELIX 89 97 {ECO:0000244|PDB:1B78}. FT STRAND 104 115 {ECO:0000244|PDB:1B78}. FT STRAND 118 130 {ECO:0000244|PDB:1B78}. FT HELIX 142 145 {ECO:0000244|PDB:1B78}. FT STRAND 146 149 {ECO:0000244|PDB:1B78}. FT HELIX 156 158 {ECO:0000244|PDB:1B78}. FT HELIX 161 164 {ECO:0000244|PDB:1B78}. FT TURN 165 167 {ECO:0000244|PDB:1B78}. FT HELIX 169 182 {ECO:0000244|PDB:1B78}. SQ SEQUENCE 185 AA; 21273 MW; 97EC2DA5C0D21D67 CRC64; MKIYFATGNP NKIKEANIIL KDLKDVEIEQ IKISYPEIQG TLEEVAEFGA KWVYNILKKP VIVEDSGFFV EALNGFPGTY SKFVQETIGN EGILKLLEGK DNRNAYFKTV IGYCDENGVR LFKGIVKGRV SEEIRSKGYG FAYDSIFIPE EEERTFAEMT TEEKSQISHR KKAFEEFKKF LLDRI // ID NUCS_METJA Reviewed; 263 AA. AC Q57678; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Endonuclease NucS {ECO:0000255|HAMAP-Rule:MF_00722}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00722}; GN Name=nucS {ECO:0000255|HAMAP-Rule:MF_00722}; OrderedLocusNames=MJ0225; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Cleaves both 3' and 5' ssDNA extremities of branched DNA CC structures. {ECO:0000255|HAMAP-Rule:MF_00722}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00722}. CC -!- SIMILARITY: Belongs to the NucS endonuclease family. CC {ECO:0000255|HAMAP-Rule:MF_00722}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98210.1; -; Genomic_DNA. DR PIR; B64328; B64328. DR ProteinModelPortal; Q57678; -. DR STRING; 243232.MJ_0225; -. DR EnsemblBacteria; AAB98210; AAB98210; MJ_0225. DR KEGG; mja:MJ_0225; -. DR eggNOG; arCOG01304; Archaea. DR eggNOG; COG1637; LUCA. DR InParanoid; Q57678; -. DR KO; K07503; -. DR OMA; RCSVDYA; -. DR PhylomeDB; Q57678; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0000014; F:single-stranded DNA endodeoxyribonuclease activity; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00722; NucS; 1. DR InterPro; IPR002793; Endonuclease_NucS. DR Pfam; PF01939; DUF91; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; DNA-binding; Endonuclease; Hydrolase; KW Nuclease; Reference proteome. FT CHAIN 1 263 Endonuclease NucS. FT /FTId=PRO_0000155691. SQ SEQUENCE 263 AA; 30984 MW; 35F9F59D4C2D7A6E CRC64; MMRLEKVFYL TNPTTKDLEN FIDMYVFKYI LILLARCKVF YEGRAKSQLE EGDRVIIIKP DGAFLIHKDK KREPVNWQPS GSSIIWEVED NFFILKSIRR KPKEELKVVI SEVYHACAFN CEDYEEINLR GSESEMAEMI FRNPDLIEEG FKPISREYQI PTGIVDILGK DKENKWVILE LKRRRADLQA VSQLKRYVEY FKNKYGEDKV RGILVSPSLT TGAEKLLKEE NLEFKRLNPP KGSKRDLKHN IKTKKTTVLD EWL // ID NOP10_METJA Reviewed; 60 AA. AC P81303; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Ribosome biogenesis protein Nop10; GN Name=nop10; OrderedLocusNames=MJ0116.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in ribosome biogenesis; more specifically in CC 18S rRNA pseudouridylation and in cleavage of pre-rRNA. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the NOP10 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98109.1; -; Genomic_DNA. DR PDB; 2APO; X-ray; 1.95 A; B=1-60. DR PDB; 2AQC; NMR; -; A=1-60. DR PDBsum; 2APO; -. DR PDBsum; 2AQC; -. DR ProteinModelPortal; P81303; -. DR SMR; P81303; 1-60. DR DIP; DIP-60500N; -. DR STRING; 243232.MJ_0116.1; -. DR EnsemblBacteria; AAB98109; AAB98109; MJ_0116.1. DR KEGG; mja:MJ_0116.1; -. DR eggNOG; arCOG00906; Archaea. DR eggNOG; COG2260; LUCA. DR InParanoid; P81303; -. DR KO; K11130; -. DR OMA; FRIRKCP; -. DR PhylomeDB; P81303; -. DR EvolutionaryTrace; P81303; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030529; C:intracellular ribonucleoprotein complex; IEA:UniProtKB-KW. DR GO; GO:0030515; F:snoRNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00803; Nop10; 1. DR InterPro; IPR007264; H/ACA_rnp_Nop10. DR InterPro; IPR023532; Nop10_arc-typ. DR PANTHER; PTHR13305; PTHR13305; 1. DR Pfam; PF04135; Nop10p; 1. DR SUPFAM; SSF144210; SSF144210; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosome biogenesis; rRNA processing. FT CHAIN 1 60 Ribosome biogenesis protein Nop10. FT /FTId=PRO_0000149018. FT TURN 10 12 {ECO:0000244|PDB:2APO}. FT STRAND 15 20 {ECO:0000244|PDB:2APO}. FT STRAND 22 24 {ECO:0000244|PDB:2APO}. FT HELIX 43 54 {ECO:0000244|PDB:2APO}. SQ SEQUENCE 60 AA; 7130 MW; F803BDAF7F216DE7 CRC64; MVEMRMKKCP KCGLYTLKEI CPKCGEKTVI PKPPKFSLED RWGKYRRMLK RALKNKNKAE // ID OGT_METJA Reviewed; 167 AA. AC Q58924; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Methylated-DNA--protein-cysteine methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; DE EC=2.1.1.63 {ECO:0000255|HAMAP-Rule:MF_00772}; DE AltName: Full=6-O-methylguanine-DNA methyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; DE Short=MGMT {ECO:0000255|HAMAP-Rule:MF_00772}; DE AltName: Full=O-6-methylguanine-DNA-alkyltransferase {ECO:0000255|HAMAP-Rule:MF_00772}; GN Name=ogt {ECO:0000255|HAMAP-Rule:MF_00772}; OrderedLocusNames=MJ1529; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP STRUCTURE BY NMR, FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=16826543; DOI=10.1002/mrc.1823; RA Roberts A., Pelton J.G., Wemmer D.E.; RT "Structural studies of MJ1529, an O6-methylguanine-DNA RT methyltransferase."; RL Magn. Reson. Chem. 44:S71-S82(2006). CC -!- FUNCTION: Involved in the cellular defense against the biological CC effects of O6-methylguanine (O6-MeG) in DNA. Repairs alkylated CC guanine in DNA by stoichiometrically transferring the alkyl group CC at the O-6 position to a cysteine residue in the enzyme. This is a CC suicide reaction: the enzyme is irreversibly inactivated. CC {ECO:0000255|HAMAP-Rule:MF_00772, ECO:0000269|PubMed:16826543}. CC -!- CATALYTIC ACTIVITY: DNA (containing 6-O-methylguanine) + protein CC L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L- CC cysteine. {ECO:0000255|HAMAP-Rule:MF_00772, CC ECO:0000269|PubMed:16826543}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00772}. CC -!- MISCELLANEOUS: This enzyme catalyzes only one turnover and CC therefore is not strictly catalytic. According to one definition, CC an enzyme is a biocatalyst that acts repeatedly and over many CC reaction cycles. CC -!- SIMILARITY: Belongs to the MGMT family. {ECO:0000255|HAMAP- CC Rule:MF_00772}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99547.1; -; Genomic_DNA. DR PIR; H64490; H64490. DR PDB; 2G7H; NMR; -; A=1-167. DR PDBsum; 2G7H; -. DR ProteinModelPortal; Q58924; -. DR SMR; Q58924; 1-167. DR STRING; 243232.MJ_1529; -. DR EnsemblBacteria; AAB99547; AAB99547; MJ_1529. DR KEGG; mja:MJ_1529; -. DR eggNOG; arCOG02724; Archaea. DR eggNOG; COG0350; LUCA. DR InParanoid; Q58924; -. DR KO; K00567; -. DR OMA; ILKLYFA; -. DR PhylomeDB; Q58924; -. DR EvolutionaryTrace; Q58924; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central. DR GO; GO:0003908; F:methylated-DNA-[protein]-cysteine S-methyltransferase activity; IBA:GO_Central. DR GO; GO:0006307; P:DNA dealkylation involved in DNA repair; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00772; OGT; 1. DR InterPro; IPR001497; MethylDNA_cys_MeTrfase_AS. DR InterPro; IPR014048; MethylDNA_cys_MeTrfase_DNA-bd. DR InterPro; IPR023546; MGMT. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01035; DNA_binding_1; 1. DR SUPFAM; SSF46767; SSF46767; 1. DR TIGRFAMs; TIGR00589; ogt; 1. DR PROSITE; PS00374; MGMT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; DNA damage; DNA repair; KW Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 167 Methylated-DNA--protein-cysteine FT methyltransferase. FT /FTId=PRO_0000139377. FT ACT_SITE 128 128 Nucleophile; methyl group acceptor. FT {ECO:0000255|HAMAP-Rule:MF_00772}. FT STRAND 2 5 {ECO:0000244|PDB:2G7H}. FT STRAND 8 23 {ECO:0000244|PDB:2G7H}. FT HELIX 31 34 {ECO:0000244|PDB:2G7H}. FT TURN 44 47 {ECO:0000244|PDB:2G7H}. FT HELIX 48 58 {ECO:0000244|PDB:2G7H}. FT TURN 67 70 {ECO:0000244|PDB:2G7H}. FT HELIX 82 88 {ECO:0000244|PDB:2G7H}. FT HELIX 99 105 {ECO:0000244|PDB:2G7H}. FT HELIX 110 118 {ECO:0000244|PDB:2G7H}. FT TURN 123 125 {ECO:0000244|PDB:2G7H}. FT HELIX 127 130 {ECO:0000244|PDB:2G7H}. FT STRAND 134 136 {ECO:0000244|PDB:2G7H}. FT STRAND 140 142 {ECO:0000244|PDB:2G7H}. FT HELIX 145 155 {ECO:0000244|PDB:2G7H}. SQ SEQUENCE 167 AA; 19431 MW; 7FC44483D31F6EF2 CRC64; MIIQIEEYFI GMIFKGNQLV RNTIPLRREE IFNFMDGEVV SNPEDEHLKV AEIILKLYFA EIDDKKVREL ISYKLEVPEF TKKVLDIVKD IEFGKTLTYG DIAKKLNTSP RAVGMALKRN PLPLIIPCHR VVAKNSLGGY SYGLDKKKFI LERERLNMVS FKFNKVY // ID NUSA_METJA Reviewed; 183 AA. AC Q58447; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable transcription termination protein NusA {ECO:0000255|HAMAP-Rule:MF_00945}; GN Name=nusA {ECO:0000255|HAMAP-Rule:MF_00945}; OrderedLocusNames=MJ1045; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Participates in transcription termination. CC {ECO:0000255|HAMAP-Rule:MF_00945}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00945}. CC -!- SIMILARITY: Belongs to the NusA family. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|HAMAP- CC Rule:MF_00945}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99049.1; -; Genomic_DNA. DR PIR; D64430; D64430. DR ProteinModelPortal; Q58447; -. DR STRING; 243232.MJ_1045; -. DR EnsemblBacteria; AAB99049; AAB99049; MJ_1045. DR KEGG; mja:MJ_1045; -. DR eggNOG; arCOG01760; Archaea. DR eggNOG; COG0195; LUCA. DR InParanoid; Q58447; -. DR KO; K02600; -. DR OMA; QIKYIAL; -. DR PhylomeDB; Q58447; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006353; P:DNA-templated transcription, termination; IEA:UniProtKB-HAMAP. DR GO; GO:0031564; P:transcription antitermination; IBA:GO_Central. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_00945_A; NusA_A; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR025249; KH_dom_NusA-like. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR010212; NusA_arc. DR Pfam; PF13184; KH_5; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54814; SSF54814; 2. DR TIGRFAMs; TIGR01952; nusA_arch; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; RNA-binding; KW Transcription; Transcription regulation; Transcription termination. FT CHAIN 1 183 Probable transcription termination FT protein NusA. FT /FTId=PRO_0000181983. FT DOMAIN 32 98 KH. {ECO:0000255|HAMAP-Rule:MF_00945}. SQ SEQUENCE 183 AA; 21135 MW; 2845502CAD695783 CRC64; MAKVRLTTEE IMKIGFFEKI ANVPILDCVL NDERVAFIVK EGDVGAAIGK GGENVKTAEE KFGKKVDIIE YSDDWRKFIR NIFAPIQLDD VWVKRVGKDV VAFIKINPKV RRAVFGEKGK NLERALKILK RHTKITKIKV IVENQKFKRK RAKRPVVKDQ QQEQTETKQE TDVQQDVKET VKE // ID NURA_METJA Reviewed; 389 AA. AC Q58658; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Probable DNA double-strand break repair nuclease NurA {ECO:0000250|UniProtKB:Q8U1N8}; DE EC=3.1.-.- {ECO:0000250|UniProtKB:Q8U1N8}; GN Name=nurA {ECO:0000250|UniProtKB:Q8U1N8}; GN OrderedLocusNames=MJ1262 {ECO:0000312|EMBL:AAB99265.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in DNA double-strand break (DSB) repair (By CC similarity). Acts probably with HerA to stimulate resection of the CC 5' strand and produce the long 3' single-strand that is required CC for RadA loading (By similarity). {ECO:0000250|UniProtKB:Q8U1N8}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000250|UniProtKB:Q8U1N8}; CC -!- SIMILARITY: Belongs to the NurA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99265.1; -; Genomic_DNA. DR PIR; E64457; E64457. DR ProteinModelPortal; Q58658; -. DR STRING; 243232.MJ_1262; -. DR EnsemblBacteria; AAB99265; AAB99265; MJ_1262. DR KEGG; mja:MJ_1262; -. DR eggNOG; arCOG00367; Archaea. DR eggNOG; COG1630; LUCA. DR InParanoid; Q58658; -. DR OMA; YILKKSH; -. DR PhylomeDB; Q58658; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR InterPro; IPR018977; NurA_domain. DR Pfam; PF09376; NurA; 1. DR SMART; SM00933; NurA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA damage; DNA repair; Hydrolase; Manganese; KW Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 389 Probable DNA double-strand break repair FT nuclease NurA. FT /FTId=PRO_0000107244. FT METAL 74 74 Manganese. FT {ECO:0000250|UniProtKB:Q8U1N8}. FT METAL 151 151 Manganese. FT {ECO:0000250|UniProtKB:Q8U1N8}. SQ SEQUENCE 389 AA; 45314 MW; 28DBE8BEB9476404 CRC64; MFFKIFVENT VILPNPLILT KIEGLLMIEY LLKNREQIIK KMEKINDINR KEVEEKWILD NFENPKDMGF AGGDGSCNKL DYISFSFYGV GAVSFIHGRG EKVKKAKEEY IFDITHPLDI EDRIRRYMLT LELKTALYVL KNYNIDYYIF DGSLFSLLIF TKKGIEMYER ELEEIYNEYG KEFNKKIDEE TKSGEIGIIS KDLNLELNKK ILVEHVEYIL TLTKLINEFK DRIIGISKTS KINIYFDKNM PDIAIFTKYT DKSGYSEPID FVNKLGDEKK EKHKQLSSVV KGINFIKNKP FYAKIDTAYI QFVRLEDNCG VVGLTSFNKI DKEVLSSLKE ISINGYPYIL KKSHETVEIT TKKLEAIAKL LNIDDPIARH ILGKKKKKF // ID OTC_METJA Reviewed; 305 AA. AC Q58291; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Ornithine carbamoyltransferase; DE Short=OTCase; DE EC=2.1.3.3; GN Name=argF; OrderedLocusNames=MJ0881; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Reversibly catalyzes the transfer of the carbamoyl group CC from carbamoyl phosphate (CP) to the N(epsilon) atom of ornithine CC (ORN) to produce L-citrulline. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-ornithine = phosphate CC + L-citrulline. CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L- CC arginine from L-ornithine and carbamoyl phosphate: step 1/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98885.1; -; Genomic_DNA. DR PIR; A64410; A64410. DR ProteinModelPortal; Q58291; -. DR SMR; Q58291; 2-303. DR STRING; 243232.MJ_0881; -. DR EnsemblBacteria; AAB98885; AAB98885; MJ_0881. DR KEGG; mja:MJ_0881; -. DR eggNOG; arCOG00912; Archaea. DR eggNOG; COG0078; LUCA. DR InParanoid; Q58291; -. DR KO; K00611; -. DR OMA; GNNMAHS; -. DR PhylomeDB; Q58291; -. DR UniPathway; UPA00068; UER00112. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004585; F:ornithine carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central. DR GO; GO:0000050; P:urea cycle; IBA:GO_Central. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_01109; OTCase; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR InterPro; IPR002292; Orn/put_carbamltrans. DR InterPro; IPR024904; OTCase_ArgI. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00102; OTCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00658; orni_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Arginine biosynthesis; Complete proteome; KW Cytoplasm; Reference proteome; Transferase. FT CHAIN 1 305 Ornithine carbamoyltransferase. FT /FTId=PRO_0000113065. FT REGION 48 52 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 126 129 Carbamoyl phosphate binding. FT {ECO:0000250}. FT REGION 226 227 Ornithine binding. {ECO:0000250}. FT REGION 261 264 Carbamoyl phosphate binding. FT {ECO:0000250}. FT BINDING 4 4 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 99 99 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 157 157 Ornithine. {ECO:0000250}. FT BINDING 222 222 Ornithine. {ECO:0000250}. FT BINDING 272 272 Carbamoyl phosphate. {ECO:0000250}. FT BINDING 290 290 Carbamoyl phosphate. {ECO:0000250}. FT SITE 25 25 Important for structural integrity. FT {ECO:0000250}. FT SITE 139 139 Important for structural integrity. FT {ECO:0000250}. SQ SEQUENCE 305 AA; 34569 MW; 98F12CBA15BB319A CRC64; MHLLDLDVLS REDVLKIIEY GIYFKKNRRK HEKILEGKSV AILFEKPSTR TRMSFDIAVY ELGGHPLIMN QNEIHLGKKE SIKDTAKVMG RYVDTIVARV YKHRHLEEMA KYSSVPVINA LSDLAHPCQI LADLMTIKEY KGKFKGLKIA YLGDGNNVCN SLILGSALVG MDTYVGTPKG YEPNAKVVLK AKEIINNYGE GSLTLTNDPI EAAEDADVLY TDVWISMGDD KDKEEVLKIF PPFQINSKLL EYAKDDVIVM HCLPANRGYE ITDDVIDGEH SVVYDEAENR LHVQKGVFKF IFERK // ID P936_METJA Reviewed; 166 AA. AC Q58346; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Phosphodiesterase MJ0936; DE EC=3.1.4.-; GN OrderedLocusNames=MJ0936; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 1-165 OF NATIVE PROTEIN AND RP IN COMPLEXES WITH NICKEL AND MANGANESE, FUNCTION, COFACTOR, AND RP BIOPHYSICOCHEMICAL PROPERTIES. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15128743; DOI=10.1074/jbc.M401059200; RA Chen S., Yakunin A.F., Kuznetsova E., Busso D., Pufan R., RA Proudfoot M., Kim R., Kim S.-H.; RT "Structural and functional characterization of a novel RT phosphodiesterase from Methanococcus jannaschii."; RL J. Biol. Chem. 279:31854-31862(2004). CC -!- FUNCTION: Shows phosphodiesterase activity, hydrolyzing CC phosphodiesters bonds in the artificial chromogenic substrates CC bis-p-nitrophenyl phosphate (bis-pNPP), and less efficiently CC thymidine 5'-monophosphate p-nitrophenyl ester (pNP-TMP) and p- CC nitrophenylphosphorylcholine (pNPPC). No catalytic activity was CC found toward cAMP or cGMP, nucleotides or phospholipase substrates CC such as phosphatidylcholine. The physiological substrate is CC unknown. {ECO:0000269|PubMed:15128743}. CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; CC Evidence={ECO:0000269|PubMed:15128743}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15128743}; CC Note=Binds 2 divalent metal ions per subunit. Most effective are CC nickel and manganese. {ECO:0000269|PubMed:15128743}; CC -!- ENZYME REGULATION: Competitively inhibited by phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.15 mM for bis-pNPP (in the presence of Ni(2+)) CC {ECO:0000269|PubMed:15128743}; CC KM=0.035 mM for pNP-TMP (in the presence of Ni(2+)) CC {ECO:0000269|PubMed:15128743}; CC KM=3.33 mM for pNPPC (in the presence of Ni(2+)) CC {ECO:0000269|PubMed:15128743}; CC KM=1.53 mM for pNPPC (in the presence of Mn(2+)) CC {ECO:0000269|PubMed:15128743}; CC pH dependence: CC Optimum pH is 9.4-9.8. {ECO:0000269|PubMed:15128743}; CC -!- SUBUNIT: Monomer. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98941.1; -; Genomic_DNA. DR PIR; H64416; H64416. DR PDB; 1S3L; X-ray; 2.40 A; A/B=1-165. DR PDB; 1S3M; X-ray; 2.50 A; A/B=1-165. DR PDB; 1S3N; X-ray; 2.50 A; A/B=1-165. DR PDB; 2AHD; X-ray; 3.00 A; A/B/C/D=1-165. DR PDBsum; 1S3L; -. DR PDBsum; 1S3M; -. DR PDBsum; 1S3N; -. DR PDBsum; 2AHD; -. DR ProteinModelPortal; Q58346; -. DR SMR; Q58346; 1-165. DR STRING; 243232.MJ_0936; -. DR EnsemblBacteria; AAB98941; AAB98941; MJ_0936. DR KEGG; mja:MJ_0936; -. DR eggNOG; arCOG01141; Archaea. DR eggNOG; COG0622; LUCA. DR InParanoid; Q58346; -. DR KO; K07095; -. DR OMA; VIHCGDF; -. DR PhylomeDB; Q58346; -. DR BRENDA; 3.1.4.1; 3260. DR SABIO-RK; Q58346; -. DR EvolutionaryTrace; Q58346; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR020935; PdiEstase_YfcE_CS. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. DR PROSITE; PS01269; UPF0025; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Manganese; Metal-binding; KW Nickel; Reference proteome. FT CHAIN 1 166 Phosphodiesterase MJ0936. FT /FTId=PRO_0000155612. FT METAL 8 8 Nickel or manganese 1. FT METAL 10 10 Nickel or manganese 1. FT METAL 36 36 Nickel or manganese 1. FT METAL 36 36 Nickel or manganese 2. FT METAL 59 59 Nickel or manganese 2. FT METAL 97 97 Nickel or manganese 2. FT METAL 120 120 Nickel or manganese 2. FT METAL 122 122 Nickel or manganese 1. FT STRAND 2 6 {ECO:0000244|PDB:1S3L}. FT HELIX 13 25 {ECO:0000244|PDB:1S3L}. FT STRAND 29 33 {ECO:0000244|PDB:1S3L}. FT HELIX 41 45 {ECO:0000244|PDB:1S3L}. FT HELIX 46 48 {ECO:0000244|PDB:1S3L}. FT STRAND 50 56 {ECO:0000244|PDB:1S3L}. FT HELIX 64 74 {ECO:0000244|PDB:1S3L}. FT STRAND 79 88 {ECO:0000244|PDB:1S3L}. FT STRAND 91 98 {ECO:0000244|PDB:1S3L}. FT HELIX 101 110 {ECO:0000244|PDB:1S3L}. FT STRAND 114 119 {ECO:0000244|PDB:1S3L}. FT STRAND 125 129 {ECO:0000244|PDB:1S3L}. FT STRAND 132 136 {ECO:0000244|PDB:1S3L}. FT TURN 143 145 {ECO:0000244|PDB:1S3L}. FT STRAND 149 154 {ECO:0000244|PDB:1S3L}. FT TURN 155 158 {ECO:0000244|PDB:1S3L}. FT STRAND 159 164 {ECO:0000244|PDB:1S3L}. SQ SEQUENCE 166 AA; 19039 MW; 1F92D7A501EEA315 CRC64; MKIGIMSDTH DHLPNIRKAI EIFNDENVET VIHCGDFVSL FVIKEFENLN ANIIATYGNN DGERCKLKEW LKDINEENII DDFISVEIDD LKFFITHGHH QSVLEMAIKS GLYDVVIYGH THERVFEEVD DVLVINPGEC CGYLTGIPTI GILDTEKKEY REIVLE // ID OGG1_METJA Reviewed; 207 AA. AC Q58134; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=N-glycosylase/DNA lyase; DE Includes: DE RecName: Full=8-oxoguanine DNA glycosylase; DE EC=3.2.2.-; DE Includes: DE RecName: Full=DNA-(apurinic or apyrimidinic site) lyase; DE Short=AP lyase; DE EC=4.2.99.18; GN Name=ogg; OrderedLocusNames=MJ0724; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-129. RX PubMed=10521423; DOI=10.1074/jbc.274.43.30447; RA Gogos A., Clarke N.D.; RT "Characterization of an 8-oxoguanine DNA glycosylase from RT Methanococcus jannaschii."; RL J. Biol. Chem. 274:30447-30450(1999). CC -!- FUNCTION: Responsible for removing an oxidatively damaged form of CC guanine (7,8-dihydro-8-oxoguanine = 7-oxoG) from DNA. Also nicks CC DNA at apurinic/apyrimidinic sites (AP sites). Has little CC specificity for the base opposite oxoG. CC -!- CATALYTIC ACTIVITY: The C-O-P bond 3' to the apurinic or CC apyrimidinic site in DNA is broken by a beta-elimination reaction, CC leaving a 3'-terminal unsaturated sugar and a product with a CC terminal 5'-phosphate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5.; CC -!- SIMILARITY: Belongs to the type-2 OGG1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98720.1; -; Genomic_DNA. DR PIR; D64390; D64390. DR PDB; 3FHF; X-ray; 2.00 A; A=1-207. DR PDB; 3KNT; X-ray; 2.70 A; A/B/C/D=1-207. DR PDBsum; 3FHF; -. DR PDBsum; 3KNT; -. DR ProteinModelPortal; Q58134; -. DR STRING; 243232.MJ_0724; -. DR EnsemblBacteria; AAB98720; AAB98720; MJ_0724. DR KEGG; mja:MJ_0724; -. DR eggNOG; arCOG04357; Archaea. DR eggNOG; COG1059; LUCA. DR InParanoid; Q58134; -. DR KO; K03653; -. DR OMA; ELCFCIL; -. DR PhylomeDB; Q58134; -. DR BRENDA; 3.2.2.B5; 3260. DR BRENDA; 4.2.99.18; 3260. DR EvolutionaryTrace; Q58134; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IEA:UniProtKB-HAMAP. DR GO; GO:0006284; P:base-excision repair; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.340.30; -; 1. DR HAMAP; MF_00241; Ogg; 1. DR InterPro; IPR012092; DNA_glyclase/DNA_lyase_thermo. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003265; HhH-GPD_domain. DR PIRSF; PIRSF005954; Thrmst_ogg; 1. DR SMART; SM00478; ENDO3c; 1. DR SUPFAM; SSF48150; SSF48150; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; Glycosidase; KW Hydrolase; Lyase; Multifunctional enzyme; Nuclease; KW Reference proteome. FT CHAIN 1 207 N-glycosylase/DNA lyase. FT /FTId=PRO_0000159562. FT ACT_SITE 129 129 FT MUTAGEN 129 129 K->S: Loss of activity. FT {ECO:0000269|PubMed:10521423}. FT HELIX 1 11 {ECO:0000244|PDB:3FHF}. FT HELIX 15 27 {ECO:0000244|PDB:3FHF}. FT HELIX 28 31 {ECO:0000244|PDB:3FHF}. FT HELIX 34 47 {ECO:0000244|PDB:3FHF}. FT HELIX 52 62 {ECO:0000244|PDB:3FHF}. FT HELIX 65 68 {ECO:0000244|PDB:3FHF}. FT HELIX 71 80 {ECO:0000244|PDB:3FHF}. FT HELIX 86 96 {ECO:0000244|PDB:3FHF}. FT HELIX 97 99 {ECO:0000244|PDB:3FHF}. FT HELIX 102 108 {ECO:0000244|PDB:3FHF}. FT STRAND 109 111 {ECO:0000244|PDB:3FHF}. FT HELIX 112 122 {ECO:0000244|PDB:3FHF}. FT HELIX 128 137 {ECO:0000244|PDB:3FHF}. FT HELIX 148 156 {ECO:0000244|PDB:3FHF}. FT STRAND 159 162 {ECO:0000244|PDB:3FHF}. FT HELIX 169 185 {ECO:0000244|PDB:3FHF}. FT HELIX 190 202 {ECO:0000244|PDB:3FHF}. SQ SEQUENCE 207 AA; 24827 MW; D17747917BF10B45 CRC64; MMLIKKIEEL KNSEIKDIID KRIQEFKSFK NKSNEEWFKE LCFCILTANF TAEGGIRIQK EIGDGFLTLP REELEEKLKN LGHRFYRKRA EYIVLARRFK NIKDIVESFE NEKVAREFLV RNIKGIGYKE ASHFLRNVGY DDVAIIDRHI LRELYENNYI DEIPKTLSRR KYLEIENILR DIGEEVNLKL SELDLYIWYL RTGKVLK // ID PATS_METJA Reviewed; 273 AA. AC Q58378; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 3. DT 11-MAY-2016, entry version 107. DE RecName: Full=Soluble P-type ATPase-like phosphatase; DE EC=3.6.3.-; GN Name=patS; OrderedLocusNames=MJ0968; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=10760521; DOI=10.1016/S0014-5793(00)01374-0; RA Ogawa H., Haga T., Toyoshima C.; RT "Soluble P-type ATPase from an archaeon, Methanococcus jannaschii."; RL FEBS Lett. 471:99-102(2000). RN [3] RP CHARACTERIZATION. RX PubMed=12753900; DOI=10.1016/S0014-5793(03)00372-7; RA Bramkamp M., Gassel M., Herkenhoff-Hesselmann B., Bertrand J., RA Altendorf K.; RT "The Methanocaldococcus jannaschii protein Mj0968 is not a P-type RT ATPase."; RL FEBS Lett. 543:31-36(2003). CC -!- FUNCTION: Most probably acts as a phosphatase in the cytosol. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- ENZYME REGULATION: Inhibited by orthovanadate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 50 degrees Celsius.; CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IB subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98973.1; -; Genomic_DNA. DR PIR; H64420; H64420. DR ProteinModelPortal; Q58378; -. DR EnsemblBacteria; AAB98973; AAB98973; MJ_0968. DR KEGG; mja:MJ_0968; -. DR eggNOG; arCOG01579; Archaea. DR eggNOG; COG4087; LUCA. DR InParanoid; Q58378; -. DR KO; K17686; -. DR OMA; QTVDIVD; -. DR PhylomeDB; Q58378; -. DR SABIO-RK; Q58378; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1000; -; 2. DR InterPro; IPR023214; HAD-like_dom. DR SUPFAM; SSF56784; SSF56784; 2. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Hydrolase; Magnesium; Metal-binding; KW Nucleotide-binding; Phosphoprotein; Reference proteome. FT CHAIN 1 273 Soluble P-type ATPase-like phosphatase. FT /FTId=PRO_0000046397. FT ACT_SITE 8 8 4-aspartylphosphate intermediate. FT {ECO:0000305}. SQ SEQUENCE 273 AA; 30739 MW; FC6D56FD985E4381 CRC64; MKVAIVFDSA GTLVKIMRVI KDLKKNKFIC NSQTVDIVDK KKGRALVIIK EDPLKVVDKE NPEKLISDLL KEVEIGISYC NPPINREGIF KDRKTKVKEL QEPLNILKRY EVETGYGSAL IIDTYAGEVE YTIATAGCLF KEVKETIKQL KDLGVKVFIA SGDRKGFIKR LAEITGVDER YIMAEAHQEL KRDLIRNLKK EGYFTIMVGD GANDVPAMIE SDLAVVTLQN GNVSRRALET ADIKIYNIKE IVDICKKVIN GEIKGRMQIK ECS // ID PC2DH_METJA Reviewed; 206 AA. AC Q57605; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Putative precorrin-2 dehydrogenase; DE EC=1.3.1.76; GN OrderedLocusNames=MJ0140; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the archaeal biosynthesis of heme. Catalyzes CC the oxiation of precorrin-2 into sirohydroclorin (By similarity). CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin + CC NADH. CC -!- PATHWAY: Porphyrin-containing compound metabolism; siroheme CC biosynthesis; sirohydrochlorin from precorrin-2: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the precorrin-2 dehydrogenase / CC sirohydrochlorin ferrochelatase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98123.1; -; Genomic_DNA. DR PIR; E64317; E64317. DR ProteinModelPortal; Q57605; -. DR STRING; 243232.MJ_0140; -. DR EnsemblBacteria; AAB98123; AAB98123; MJ_0140. DR KEGG; mja:MJ_0140; -. DR eggNOG; arCOG01044; Archaea. DR eggNOG; COG1648; LUCA. DR InParanoid; Q57605; -. DR KO; K02304; -. DR OMA; IPACTEV; -. DR PhylomeDB; Q57605; -. DR UniPathway; UPA00262; UER00222. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; ISS:UniProtKB. DR GO; GO:0019354; P:siroheme biosynthetic process; ISS:UniProtKB. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006367; Sirohaem_synthase_N. DR Pfam; PF13241; NAD_binding_7; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01470; cysG_Nterm; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Porphyrin biosynthesis; KW Reference proteome. FT CHAIN 1 206 Putative precorrin-2 dehydrogenase. FT /FTId=PRO_0000106716. FT NP_BIND 20 21 NAD. {ECO:0000250}. FT NP_BIND 41 46 NAD. {ECO:0000250}. SQ SEQUENCE 206 AA; 23989 MW; 50C36E48EE4FBC44 CRC64; MLPILLSFEG KKVAVFGCGS VGKRRAKKIL KSGGIVDIYS KEFDEEIKKL KESNKNLNLI EIDINQLSDE ELKNIIMKYD FIVTAINDEI NKRIVKLAKE LNKFVNSSTK TEGVNFIIPA YTEVDEVIFS IYTKGKSPLI AKHIRIFVEN YLKSTDINMI AYIREFLKET IPKQKDREKI LKKIFENEKF REELKKLIEK WENGNH // ID PASYA_METJA Reviewed; 266 AA. AC Q57662; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Probable pantothenate synthetase; DE Short=PS; DE EC=6.3.2.44; DE AltName: Full=Pantoate--beta-alanine ligase; DE AltName: Full=Pantoate-activating enzyme; GN OrderedLocusNames=MJ0209; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the condensation of pantoate with beta-alanine CC in an ATP-dependent and ADP-producing reaction. CC {ECO:0000250|UniProtKB:Q8PUQ1}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate + beta-alanine = ADP + CC phosphate + (R)-pantothenate. CC -!- PATHWAY: Cofactor biosynthesis; (R)-pantothenate biosynthesis. CC -!- MISCELLANEOUS: Could also have phosphopantothenate synthetase CC activity, like the Pyrococcus kodakaraensis ortholog, which may be CC higher than the pantothenate synthetase activity. CC -!- SIMILARITY: Belongs to the archaeal CC phosphopantothenate/pantothenate synthetase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98192.1; -; Genomic_DNA. DR PIR; B64326; B64326. DR ProteinModelPortal; Q57662; -. DR STRING; 243232.MJ_0209; -. DR EnsemblBacteria; AAB98192; AAB98192; MJ_0209. DR KEGG; mja:MJ_0209; -. DR eggNOG; arCOG04262; Archaea. DR eggNOG; COG1701; LUCA. DR InParanoid; Q57662; -. DR KO; K09722; -. DR OMA; PKSHPRY; -. DR PhylomeDB; Q57662; -. DR UniPathway; UPA00028; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW. DR GO; GO:0015940; P:pantothenate biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR002855; PPS. DR Pfam; PF02006; DUF137; 1. DR PIRSF; PIRSF004853; UCP004853; 1. DR ProDom; PD016827; DUF137; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Nucleotide-binding; KW Pantothenate biosynthesis; Reference proteome. FT CHAIN 1 266 Probable pantothenate synthetase. FT /FTId=PRO_0000106742. FT COMPBIAS 66 69 Poly-Ala. SQ SEQUENCE 266 AA; 29853 MW; D3B064215551E6C5 CRC64; MLSVMRMQIP KTHPRYESLM KREKIIEALD KGILAKAGLI AHGRGETFDY LIGEKTAPIA LEAIKAAAAL LILAENPVIS VNGNTVALAI DEVVELAKEL NGKIEVNLFY RTKERELAIK RAFEEKFKDD IETGKIKILG IDDANKQIPN LDSLRGKVSE EGIFTADVVL VPLEDGDRAE ALVNMGKKVI AIDLNPLSRT ARKSTITIVD ELTRAMPLLI KYVKEFKNKD REELLKIVED FDNKKNLKDM IDYIAERLKN LSLDEL // ID PAN_METJA Reviewed; 430 AA. AC Q58576; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=Proteasome-activating nucleotidase {ECO:0000255|HAMAP-Rule:MF_00553}; DE Short=PAN {ECO:0000255|HAMAP-Rule:MF_00553}; DE AltName: Full=Proteasomal ATPase {ECO:0000255|HAMAP-Rule:MF_00553}; DE AltName: Full=Proteasome regulatory ATPase {ECO:0000255|HAMAP-Rule:MF_00553}; DE AltName: Full=Proteasome regulatory particle {ECO:0000255|HAMAP-Rule:MF_00553}; GN Name=pan {ECO:0000255|HAMAP-Rule:MF_00553}; OrderedLocusNames=MJ1176; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION AS AN ATPASE, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT, AND RP INTERACTION WITH THE PROTEASOME. RX PubMed=10692374; DOI=10.1128/JB.182.6.1680-1692.2000; RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.; RT "Biochemical and physical properties of the Methanococcus jannaschii RT 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the RT eucaryal 26S proteasome."; RL J. Bacteriol. 182:1680-1692(2000). RN [3] RP FUNCTION IN THE PROTEASOME DEGRADATION PATHWAY, ATPASE ACTIVITY, RP NUCLEOTIDE SPECIFICITY, AND ENZYME REGULATION. RX PubMed=10473546; DOI=10.1074/jbc.274.37.26008; RA Zwickl P., Ng D., Woo K.M., Klenk H.-P., Goldberg A.L.; RT "An archaebacterial ATPase, homologous to ATPases in the eukaryotic 26 RT S proteasome, activates protein breakdown by 20 S proteasomes."; RL J. Biol. Chem. 274:26008-26014(1999). RN [4] RP CHAPERONE ACTIVITY. RX PubMed=11056539; DOI=10.1038/35041081; RA Benaroudj N., Goldberg A.L.; RT "PAN, the proteasome-activating nucleotidase from archaebacteria, is a RT protein-unfolding molecular chaperone."; RL Nat. Cell Biol. 2:833-839(2000). RN [5] RP FUNCTION, INTERACTION WITH THE PROTEASOME, AND SUBUNIT. RX PubMed=16337593; DOI=10.1016/j.molcel.2005.10.019; RA Smith D.M., Kafri G., Cheng Y., Ng D., Walz T., Goldberg A.L.; RT "ATP binding to PAN or the 26S ATPases causes association with the 20S RT proteasome, gate opening, and translocation of unfolded proteins."; RL Mol. Cell 20:687-698(2005). RN [6] RP FUNCTION, ROLE OF C-TERMINUS IN GATE OPENING, AND MUTAGENESIS OF RP LEU-428; TYR-429 AND ARG-430. RX PubMed=17803938; DOI=10.1016/j.molcel.2007.06.033; RA Smith D.M., Chang S.C., Park S., Finley D., Cheng Y., Goldberg A.L.; RT "Docking of the proteasomal ATPases' carboxyl termini in the 20S RT proteasome's alpha ring opens the gate for substrate entry."; RL Mol. Cell 27:731-744(2007). RN [7] RP FUNCTION, UNFOLDING AND TRANSLOCATION MECHANISM, AND MUTAGENESIS OF RP GLY-113; ASP-153; ALA-156; LYS-157; PHE-244; ILE-245; GLY-246; RP 250-SER-LEU-251; GLU-271; GLY-285 AND GLY-286. RX PubMed=19481528; DOI=10.1016/j.molcel.2009.04.022; RA Zhang F., Wu Z., Zhang P., Tian G., Finley D., Shi Y.; RT "Mechanism of substrate unfolding and translocation by the regulatory RT particle of the proteasome from Methanocaldococcus jannaschii."; RL Mol. Cell 34:485-496(2009). RN [8] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 74-430 IN COMPLEX WITH ADP, RP AND DOMAIN. RX PubMed=19481527; DOI=10.1016/j.molcel.2009.04.021; RA Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.; RT "Structural insights into the regulatory particle of the proteasome RT from Methanocaldococcus jannaschii."; RL Mol. Cell 34:473-484(2009). RN [9] RP X-RAY CRYSTALLOGRAPHY (4.0 ANGSTROMS) OF 424-430 IN COMPLEX WITH THE RP PROTEASOME OF T.ACIDOPHILUM. RX PubMed=20019667; DOI=10.1038/emboj.2009.382; RA Yu Y., Smith D.M., Kim H.M., Rodriguez V., Goldberg A.L., Cheng Y.; RT "Interactions of PAN's C-termini with archaeal 20S proteasome and RT implications for the eukaryotic proteasome-ATPase interactions."; RL EMBO J. 29:692-702(2010). CC -!- FUNCTION: ATPase which is responsible for recognizing, binding, CC unfolding and translocation of substrate proteins into the CC archaeal 20S proteasome core particle. Is essential for opening CC the gate of the 20S proteasome via an interaction with its C- CC terminus, thereby allowing substrate entry and access to the site CC of proteolysis. Thus, the C-termini of the proteasomal ATPase CC function like a 'key in a lock' to induce gate opening and CC therefore regulate proteolysis. Unfolding activity requires energy CC from ATP hydrolysis, whereas ATP binding alone promotes ATPase-20S CC proteasome association which triggers gate opening, and supports CC translocation of unfolded substrates. In addition to ATP, is able CC to cleave other nucleotide triphosphates such as CTP, GTP and UTP, CC but hydrolysis of these other nucleotides is less effective in CC promoting proteolysis than ATP. Moreover, PAN by itself can CC function as a chaperone in vitro. {ECO:0000255|HAMAP- CC Rule:MF_00553, ECO:0000269|PubMed:10473546, CC ECO:0000269|PubMed:10692374, ECO:0000269|PubMed:16337593, CC ECO:0000269|PubMed:17803938, ECO:0000269|PubMed:19481528}. CC -!- ENZYME REGULATION: ATPase activity is inhibited by EDTA, N- CC ethylmaleimide (NEM) and p-chloromercuriphenyl-sulfonic acid CC (PCMS) in vitro. {ECO:0000269|PubMed:10473546, CC ECO:0000269|PubMed:10692374}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=497 uM for ATP {ECO:0000269|PubMed:10692374}; CC KM=307 uM for CTP {ECO:0000269|PubMed:10692374}; CC Vmax=3.5 umol/min/mg enzyme for ATPase activity CC {ECO:0000269|PubMed:10692374}; CC Vmax=5.8 umol/min/mg enzyme for CTPase activity CC {ECO:0000269|PubMed:10692374}; CC pH dependence: CC Optimum pH is 7-8 for ATPase activity. Is more active at pH 8 to CC 10 than at pH 5.5. {ECO:0000269|PubMed:10692374}; CC Temperature dependence: CC Optimum temperature is 80 degrees Celsius for ATPase activity. CC {ECO:0000269|PubMed:10692374}; CC -!- SUBUNIT: Homohexamer. The hexameric complex has a two-ring CC architecture resembling a top hat that caps the 20S proteasome CC core at one or both ends. Alone, can form a complex composed of CC two stacked hexameric rings in vitro. Upon ATP-binding, the C- CC terminus of PAN interacts with the alpha-rings of the proteasome CC core by binding to the intersubunit pockets. CC {ECO:0000269|PubMed:10692374, ECO:0000269|PubMed:16337593, CC ECO:0000269|PubMed:19481527, ECO:0000269|PubMed:20019667}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: Consists of three main regions, an N-terminal coiled-coil CC domain that may assist in substrate recognition, an interdomain CC involved in PAN hexamerization, and a C-terminal ATPase domain of CC the AAA type. {ECO:0000255|HAMAP-Rule:MF_00553, CC ECO:0000269|PubMed:19481527}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000255|HAMAP- CC Rule:MF_00553}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99179.1; -; Genomic_DNA. DR PIR; G64446; G64446. DR PDB; 3H43; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=74-150. DR PDB; 3H4M; X-ray; 3.11 A; A/B/C=155-430. DR PDB; 3IPM; X-ray; 4.00 A; O/P/Q/R/S/T/U=424-430. DR PDBsum; 3H43; -. DR PDBsum; 3H4M; -. DR PDBsum; 3IPM; -. DR ProteinModelPortal; Q58576; -. DR SMR; Q58576; 158-399. DR STRING; 243232.MJ_1176; -. DR PRIDE; Q58576; -. DR EnsemblBacteria; AAB99179; AAB99179; MJ_1176. DR KEGG; mja:MJ_1176; -. DR eggNOG; arCOG01306; Archaea. DR eggNOG; COG1222; LUCA. DR InParanoid; Q58576; -. DR KO; K03420; -. DR OMA; CVGAELK; -. DR PhylomeDB; Q58576; -. DR EvolutionaryTrace; Q58576; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central. DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central. DR GO; GO:0022623; C:proteasome-activating nucleotidase complex; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IDA:UniProtKB. DR GO; GO:0043273; F:CTPase activity; IDA:UniProtKB. DR GO; GO:0003924; F:GTPase activity; IDA:UniProtKB. DR GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central. DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central. DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IBA:GOC. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB. DR GO; GO:0043335; P:protein unfolding; IDA:UniProtKB. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00553; PAN; 1. DR InterPro; IPR005937; 26S_Psome_P45. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR023501; Nucleotidase_PAN. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01242; 26Sp45; 1. DR PROSITE; PS00674; AAA; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Chaperone; Coiled coil; Complete proteome; KW Cytoplasm; Direct protein sequencing; Nucleotide-binding; Proteasome; KW Reference proteome. FT CHAIN 1 430 Proteasome-activating nucleotidase. FT /FTId=PRO_0000084743. FT NP_BIND 214 219 ATP. FT REGION 428 430 Docks into pockets in the proteasome FT alpha-ring to cause gate opening. FT COILED 9 89 {ECO:0000255|HAMAP-Rule:MF_00553}. FT BINDING 353 353 ATP. FT MUTAGEN 113 113 G->W: 7% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 153 153 D->A: 2% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 156 156 A->D: 1.5% of wild-type unfolding FT activity. {ECO:0000269|PubMed:19481528}. FT MUTAGEN 157 157 K->G: 4% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 244 244 F->A: 1% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 245 245 I->A,W: 4% of wild-type unfolding FT activity. {ECO:0000269|PubMed:19481528}. FT MUTAGEN 246 246 G->A: 5% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 250 251 SL->AA: 4% of wild-type unfolding FT activity. {ECO:0000269|PubMed:19481528}. FT MUTAGEN 271 271 E->K: 9% of wild-type unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 285 285 G->W: 1.6% of wild-type unfolding FT activity. {ECO:0000269|PubMed:19481528}. FT MUTAGEN 286 286 G->A: No effect on unfolding activity. FT {ECO:0000269|PubMed:19481528}. FT MUTAGEN 286 286 G->L,W: 4% of wild-type unfolding FT activity. {ECO:0000269|PubMed:19481528}. FT MUTAGEN 428 428 L->A,V,F: Markedly decreased PAN's FT ability to stimulate gate opening. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 428 428 L->I,Y,W: Slightly decreased PAN's FT ability to stimulate gate opening. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 428 428 L->R,D,C,P: Loss of PAN's ability to FT stimulate gate opening. Fails to FT associate with the proteasome. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 429 429 Y->A,V,I,L,F,W,R,D: Loss of PAN's ability FT to stimulate gate opening. Fails to FT associate with the proteasome. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 R->A,W: No effect on PAN's ability to FT stimulate gate opening. Still associates FT with the proteasome. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 R->D: Loss of PAN's ability to stimulate FT gate opening. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 R->G: Slightly decreased PAN's ability to FT stimulate gate opening. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 R->L: Markedly decreased PAN's ability to FT stimulate gate opening. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 R->RA: Loss of PAN's ability to stimulate FT gate opening. Fails to associate with the FT proteasome. FT {ECO:0000269|PubMed:17803938}. FT MUTAGEN 430 430 Missing: Loss of PAN's ability to FT stimulate gate opening. Fails to FT associate with the proteasome. FT {ECO:0000269|PubMed:17803938}. FT HELIX 75 88 {ECO:0000244|PDB:3H43}. FT STRAND 92 102 {ECO:0000244|PDB:3H43}. FT STRAND 105 110 {ECO:0000244|PDB:3H43}. FT STRAND 113 120 {ECO:0000244|PDB:3H43}. FT HELIX 126 128 {ECO:0000244|PDB:3H43}. FT STRAND 134 137 {ECO:0000244|PDB:3H43}. FT TURN 139 141 {ECO:0000244|PDB:3H43}. FT STRAND 144 147 {ECO:0000244|PDB:3H43}. FT STRAND 159 164 {ECO:0000244|PDB:3H4M}. FT HELIX 169 171 {ECO:0000244|PDB:3H4M}. FT HELIX 176 185 {ECO:0000244|PDB:3H4M}. FT HELIX 187 191 {ECO:0000244|PDB:3H4M}. FT HELIX 193 199 {ECO:0000244|PDB:3H4M}. FT STRAND 205 216 {ECO:0000244|PDB:3H4M}. FT HELIX 217 227 {ECO:0000244|PDB:3H4M}. FT STRAND 231 236 {ECO:0000244|PDB:3H4M}. FT HELIX 237 240 {ECO:0000244|PDB:3H4M}. FT HELIX 247 261 {ECO:0000244|PDB:3H4M}. FT STRAND 264 270 {ECO:0000244|PDB:3H4M}. FT HELIX 273 276 {ECO:0000244|PDB:3H4M}. FT STRAND 280 282 {ECO:0000244|PDB:3H4M}. FT HELIX 285 288 {ECO:0000244|PDB:3H4M}. FT HELIX 289 302 {ECO:0000244|PDB:3H4M}. FT STRAND 306 315 {ECO:0000244|PDB:3H4M}. FT HELIX 319 321 {ECO:0000244|PDB:3H4M}. FT HELIX 324 327 {ECO:0000244|PDB:3H4M}. FT STRAND 331 337 {ECO:0000244|PDB:3H4M}. FT HELIX 343 354 {ECO:0000244|PDB:3H4M}. FT HELIX 365 371 {ECO:0000244|PDB:3H4M}. FT HELIX 377 393 {ECO:0000244|PDB:3H4M}. FT STRAND 397 399 {ECO:0000244|PDB:3H4M}. FT HELIX 401 415 {ECO:0000244|PDB:3H4M}. SQ SEQUENCE 430 AA; 48690 MW; 3FD2E94A68D483DD CRC64; MVFEEFISTE LKKEKKAFTE EFKEEKEIND NSNLKNDLLK EELQEKARIA ELESRILKLE LEKKELEREN LQLMKENEIL RRELDRMRVP PLIVGTVVDK VGERKVVVKS STGPSFLVNV SHFVNPDDLA PGKRVCLNQQ TLTVVDVLPE NKDYRAKAME VDERPNVRYE DIGGLEKQMQ EIREVVELPL KHPELFEKVG IEPPKGILLY GPPGTGKTLL AKAVATETNA TFIRVVGSEL VKKFIGEGAS LVKDIFKLAK EKAPSIIFID EIDAIAAKRT DALTGGDREV QRTLMQLLAE MDGFDARGDV KIIGATNRPD ILDPAILRPG RFDRIIEVPA PDEKGRLEIL KIHTRKMNLA EDVNLEEIAK MTEGCVGAEL KAICTEAGMN AIRELRDYVT MDDFRKAVEK IMEKKKVKVK EPAHLDVLYR // ID PDXS_METJA Reviewed; 330 AA. AC Q58090; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE Short=PLP synthase subunit PdxS {ECO:0000255|HAMAP-Rule:MF_01824}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01824}; DE AltName: Full=Pdx1 {ECO:0000255|HAMAP-Rule:MF_01824}; GN Name=pdxS {ECO:0000255|HAMAP-Rule:MF_01824}; OrderedLocusNames=MJ0677; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS). RA Manzoku M., Ebihara A., Chen L., Fu Z.-Q., Chrzas J., Wang B.-C., RA Yokoyama S., Kuramitsu S.; RT "Crystal structure of pyridoxine biosynthesis protein from RT Methanocaldococcus jannaschii."; RL Submitted (MAY-2007) to the PDB data bank. CC -!- FUNCTION: Catalyzes the formation of pyridoxal 5'-phosphate from CC ribose 5-phosphate (RBP), glyceraldehyde 3-phosphate (G3P) and CC ammonia. The ammonia is provided by the PdxT subunit. Can also use CC ribulose 5-phosphate and dihydroxyacetone phosphate as substrates, CC resulting from enzyme-catalyzed isomerization of RBP and G3P, CC respectively. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- SUBUNIT: In the presence of PdxT, forms a dodecamer of CC heterodimers. {ECO:0000255|HAMAP-Rule:MF_01824}. CC -!- SIMILARITY: Belongs to the PdxS/SNZ family. {ECO:0000255|HAMAP- CC Rule:MF_01824}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98672.1; -; Genomic_DNA. DR PIR; E64384; E64384. DR PDB; 2YZR; X-ray; 2.30 A; A/B/C=1-330. DR PDBsum; 2YZR; -. DR ProteinModelPortal; Q58090; -. DR SMR; Q58090; 15-313. DR STRING; 243232.MJ_0677; -. DR EnsemblBacteria; AAB98672; AAB98672; MJ_0677. DR KEGG; mja:MJ_0677; -. DR eggNOG; arCOG04075; Archaea. DR eggNOG; COG0214; LUCA. DR InParanoid; Q58090; -. DR KO; K06215; -. DR OMA; KVRIGHV; -. DR PhylomeDB; Q58090; -. DR UniPathway; UPA00245; -. DR EvolutionaryTrace; Q58090; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 2. DR HAMAP; MF_01824; PdxS; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001852; PdxS/SNZ. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF01680; SOR_SNZ; 1. DR PIRSF; PIRSF029271; Pdx1; 1. DR SUPFAM; SSF51366; SSF51366; 2. DR TIGRFAMs; TIGR00343; TIGR00343; 1. DR PROSITE; PS01235; PDXS_SNZ_1; 1. DR PROSITE; PS51129; PDXS_SNZ_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Lyase; Pyridoxal phosphate; KW Reference proteome; Schiff base. FT CHAIN 1 330 Pyridoxal 5'-phosphate synthase subunit FT PdxS. FT /FTId=PRO_0000109435. FT REGION 271 272 D-ribose 5-phosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT ACT_SITE 80 80 Schiff-base intermediate with D-ribose 5- FT phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824}. FT BINDING 23 23 D-ribose 5-phosphate. {ECO:0000255|HAMAP- FT Rule:MF_01824}. FT BINDING 152 152 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT BINDING 164 164 Glyceraldehyde 3-phosphate. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT BINDING 250 250 D-ribose 5-phosphate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01824}. FT HELIX 7 14 {ECO:0000244|PDB:2YZR}. FT TURN 15 18 {ECO:0000244|PDB:2YZR}. FT STRAND 19 26 {ECO:0000244|PDB:2YZR}. FT HELIX 27 36 {ECO:0000244|PDB:2YZR}. FT STRAND 39 43 {ECO:0000244|PDB:2YZR}. FT HELIX 48 51 {ECO:0000244|PDB:2YZR}. FT HELIX 63 72 {ECO:0000244|PDB:2YZR}. FT STRAND 77 82 {ECO:0000244|PDB:2YZR}. FT HELIX 86 94 {ECO:0000244|PDB:2YZR}. FT STRAND 98 103 {ECO:0000244|PDB:2YZR}. FT HELIX 117 119 {ECO:0000244|PDB:2YZR}. FT STRAND 124 127 {ECO:0000244|PDB:2YZR}. FT HELIX 131 140 {ECO:0000244|PDB:2YZR}. FT STRAND 143 147 {ECO:0000244|PDB:2YZR}. FT HELIX 157 173 {ECO:0000244|PDB:2YZR}. FT HELIX 178 189 {ECO:0000244|PDB:2YZR}. FT HELIX 190 193 {ECO:0000244|PDB:2YZR}. FT HELIX 194 202 {ECO:0000244|PDB:2YZR}. FT STRAND 213 216 {ECO:0000244|PDB:2YZR}. FT HELIX 221 238 {ECO:0000244|PDB:2YZR}. FT STRAND 242 247 {ECO:0000244|PDB:2YZR}. FT HELIX 254 262 {ECO:0000244|PDB:2YZR}. FT STRAND 268 271 {ECO:0000244|PDB:2YZR}. FT HELIX 272 275 {ECO:0000244|PDB:2YZR}. FT HELIX 280 292 {ECO:0000244|PDB:2YZR}. FT TURN 293 295 {ECO:0000244|PDB:2YZR}. FT HELIX 297 304 {ECO:0000244|PDB:2YZR}. SQ SEQUENCE 330 AA; 35856 MW; A4FCCE386CEF56AB CRC64; MKKGTDLLKK GFAKMVKHGV VMDVTNVEQA QIAEEAGAVA VMALERVPAD IRAAGGVARM SDPALIEEIM DAVSIPVMAK CRIGHTTEAL VLEAIGVDMI DESEVLTQAD PFFHIYKKKF NVPFVCGARN LGEAVRRIWE GAAMIRTKGE AGTGNIVEAV RHMRLMNEAI AQLQRMTDEE VYGVAKFYAN RYAELAKTVR EGMGLPATVL ENEPIYEGFT LAEIIDGLYE VLLEVKKLGR LPVVNFAAGG VATPADAALM MQLGSDGVFV GSGIFKSENP LERARAIVEA TYNYDKPDIV AEVSKNLGEA MKGIDITQIS EAEKMQYRGD // ID PFDB_METJA Reviewed; 113 AA. AC Q58394; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 17-FEB-2016, entry version 85. DE RecName: Full=Prefoldin subunit beta; DE AltName: Full=GimC subunit beta; GN Name=pfdB; OrderedLocusNames=MJ0987; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Molecular chaperone capable of stabilizing a range of CC proteins. Seems to fulfill an ATP-independent, HSP70-like function CC in archaeal de novo protein folding (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prefoldin subunit beta family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98989.1; -; Genomic_DNA. DR PIR; C64423; C64423. DR ProteinModelPortal; Q58394; -. DR PRIDE; Q58394; -. DR EnsemblBacteria; AAB98989; AAB98989; MJ_0987. DR KEGG; mja:MJ_0987; -. DR InParanoid; Q58394; -. DR KO; K04798; -. DR OMA; PPQVQAM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016272; C:prefoldin complex; IBA:GO_Central. DR GO; GO:0051087; F:chaperone binding; IBA:GO_Central. DR GO; GO:0051131; P:chaperone-mediated protein complex assembly; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR Gene3D; 1.10.287.370; -; 1. DR HAMAP; MF_00307; PfdB; 1. DR InterPro; IPR002777; PFD_beta-like. DR InterPro; IPR012713; PfdB. DR InterPro; IPR009053; Prefoldin. DR Pfam; PF01920; Prefoldin_2; 1. DR SUPFAM; SSF46579; SSF46579; 1. DR TIGRFAMs; TIGR02338; gimC_beta; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 113 Prefoldin subunit beta. FT /FTId=PRO_0000124860. FT COMPBIAS 6 29 Gln-rich. SQ SEQUENCE 113 AA; 13367 MW; 74982CA40FF4BEFB CRC64; MELPPQIQAQ LMQLQQLQQQ LQMILMQKQS VETELKECKK ALEELEKSSS DEVYKLVGGL FVKRKKEDVK KELEEKVETL ELRVKTLEKQ EEKLQSRLKE LQEKIQKMIP TAQ // ID PCNA_METJA Reviewed; 247 AA. AC Q57697; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=DNA polymerase sliding clamp {ECO:0000255|HAMAP-Rule:MF_00317}; DE AltName: Full=Proliferating cell nuclear antigen homolog {ECO:0000255|HAMAP-Rule:MF_00317}; DE Short=PCNA {ECO:0000255|HAMAP-Rule:MF_00317}; GN Name=pcn {ECO:0000255|HAMAP-Rule:MF_00317}; OrderedLocusNames=MJ0247; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Sliding clamp subunit that acts as a moving platform for CC DNA processing. Responsible for tethering the catalytic subunit of CC DNA polymerase and other proteins to DNA during high-speed CC replication. {ECO:0000255|HAMAP-Rule:MF_00317}. CC -!- SUBUNIT: Homotrimer. The subunits circularize to form a toroid; CC DNA passes through its center. Replication factor C (RFC) is CC required to load the toroid on the DNA. {ECO:0000255|HAMAP- CC Rule:MF_00317}. CC -!- SIMILARITY: Belongs to the PCNA family. {ECO:0000255|HAMAP- CC Rule:MF_00317}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98235.1; -; Genomic_DNA. DR PIR; H64330; H64330. DR ProteinModelPortal; Q57697; -. DR STRING; 243232.MJ_0247; -. DR EnsemblBacteria; AAB98235; AAB98235; MJ_0247. DR KEGG; mja:MJ_0247; -. DR eggNOG; arCOG00488; Archaea. DR eggNOG; COG0592; LUCA. DR InParanoid; Q57697; -. DR KO; K04802; -. DR OMA; ANVGMVD; -. DR PhylomeDB; Q57697; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043626; C:PCNA complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030337; F:DNA polymerase processivity factor activity; IBA:GO_Central. DR GO; GO:0006272; P:leading strand elongation; IBA:GO_Central. DR GO; GO:0006275; P:regulation of DNA replication; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00317; DNApol_clamp_arch; 1. DR InterPro; IPR000730; Pr_cel_nuc_antig. DR InterPro; IPR022649; Pr_cel_nuc_antig_C. DR InterPro; IPR022659; Pr_cel_nuc_antig_CS. DR InterPro; IPR022648; Pr_cel_nuc_antig_N. DR PANTHER; PTHR11352; PTHR11352; 1. DR Pfam; PF02747; PCNA_C; 1. DR Pfam; PF00705; PCNA_N; 1. DR PRINTS; PR00339; PCNACYCLIN. DR TIGRFAMs; TIGR00590; pcna; 1. DR PROSITE; PS01251; PCNA_1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA replication; DNA-binding; Reference proteome. FT CHAIN 1 247 DNA polymerase sliding clamp. FT /FTId=PRO_0000149196. SQ SEQUENCE 247 AA; 27638 MW; 28E8A363741931A5 CRC64; MFRGVMESAK EFKKVVDTIS TLLDEICFEV DEEGIKASAM DPSHVALVSL EIPRLAFEEY EADSHDIGID LEAFKKVMNR AKAKDRLILE LDEEKNKLNV IFENTGKRKF SLALLDISAS SVKVPEIEYP NVIMIKGDAF KEALKDADLF SDYVILKADE DKFVIHAKGD LNENEAIFEK DSSAIISLEV KEEAKSAFNL DYLMDMVKGV SSGDIIKIYL GNDMPLKLEY SIAGVNLTFL LAPRIEG // ID PGK2_METJA Reviewed; 309 AA. AC Q58877; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=2-phosphoglycerate kinase {ECO:0000255|HAMAP-Rule:MF_00769}; DE Short=2PGK {ECO:0000255|HAMAP-Rule:MF_00769}; DE EC=2.7.2.- {ECO:0000255|HAMAP-Rule:MF_00769}; GN Name=pgk2 {ECO:0000255|HAMAP-Rule:MF_00769}; OrderedLocusNames=MJ1482; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + 2-phospho-D-glycerate = ADP + 2-phospho- CC D-glyceroyl phosphate. {ECO:0000255|HAMAP-Rule:MF_00769}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00769}; CC -!- PATHWAY: Thermoadapter biosynthesis; cyclic 2,3-diphosphoglycerate CC biosynthesis; cyclic 2,3-diphosphoglycerate from 2-phospho-D- CC glycerate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00769}. CC -!- SIMILARITY: Belongs to the 2-phosphoglycerate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_00769}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|HAMAP- CC Rule:MF_00769}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99494.1; -; Genomic_DNA. DR PIR; A64485; A64485. DR ProteinModelPortal; Q58877; -. DR STRING; 243232.MJ_1482; -. DR EnsemblBacteria; AAB99494; AAB99494; MJ_1482. DR KEGG; mja:MJ_1482; -. DR eggNOG; arCOG01967; Archaea. DR eggNOG; COG2074; LUCA. DR InParanoid; Q58877; -. DR KO; K05715; -. DR OMA; YEMPFSK; -. DR PhylomeDB; Q58877; -. DR UniPathway; UPA00551; UER00609. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016774; F:phosphotransferase activity, carboxyl group as acceptor; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00769; 2PGK; 1. DR InterPro; IPR020872; 2-phosphoglycerate_kinase. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF03477; ATP-cone; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51161; ATP_CONE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 309 2-phosphoglycerate kinase. FT /FTId=PRO_0000156149. FT DOMAIN 5 92 ATP-cone. {ECO:0000255|HAMAP- FT Rule:MF_00769}. SQ SEQUENCE 309 AA; 35545 MW; 0F2528DB92E76278 CRC64; MDLQNDIIVR GKSYEMPFSK GILARSLTAA GLKPSIAYRI AWDIYEMLKK ENIRVIDKAD LRRRVYYYLI SKNYDEVAKK YLLWRMVLGR RPIVILIGGA SGVGTSTIAF EIASRLGIPS VIGTDSIREV MRKVISRDLI PTLYESSYTA WKVLRDDEGN KYIKGFERHS EAVLTGVEGV IDRCLVEGQS VIIEGTHLVP TLLKDKYLEN SHVVFIMLTI YNEELHKMRF YARGRVSSRP TERYLKYFKI IRMINDYMVE TAKKKGIPVV ENIKISETVD KCLNIITERL KTMIELEGLS EEDMLEEGL // ID PGK_METJA Reviewed; 417 AA. AC Q58058; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Phosphoglycerate kinase; DE EC=2.7.2.3; GN Name=pgk; OrderedLocusNames=MJ0641; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + 3-phospho-D-glycerate = ADP + 3-phospho- CC D-glyceroyl phosphate. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; pyruvate from D- CC glyceraldehyde 3-phosphate: step 2/5. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the phosphoglycerate kinase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98636.1; -; Genomic_DNA. DR PIR; A64380; A64380. DR ProteinModelPortal; Q58058; -. DR STRING; 243232.MJ_0641; -. DR EnsemblBacteria; AAB98636; AAB98636; MJ_0641. DR KEGG; mja:MJ_0641; -. DR eggNOG; arCOG00496; Archaea. DR eggNOG; COG0126; LUCA. DR InParanoid; Q58058; -. DR KO; K00927; -. DR OMA; AGHPVGK; -. DR PhylomeDB; Q58058; -. DR UniPathway; UPA00109; UER00185. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004618; F:phosphoglycerate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006096; P:glycolytic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1260; -; 1. DR Gene3D; 3.40.50.1270; -; 1. DR HAMAP; MF_00145; Phosphoglyc_kinase; 1. DR InterPro; IPR001576; Phosphoglycerate_kinase. DR InterPro; IPR015901; Phosphoglycerate_kinase_C. DR InterPro; IPR015911; Phosphoglycerate_kinase_CS. DR InterPro; IPR015824; Phosphoglycerate_kinase_N. DR PANTHER; PTHR11406; PTHR11406; 1. DR Pfam; PF00162; PGK; 1. DR PIRSF; PIRSF000724; Pgk; 1. DR PRINTS; PR00477; PHGLYCKINASE. DR SUPFAM; SSF53748; SSF53748; 1. DR PROSITE; PS00111; PGLYCERATE_KINASE; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glycolysis; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 417 Phosphoglycerate kinase. FT /FTId=PRO_0000146058. FT NP_BIND 366 369 ATP. {ECO:0000250}. FT REGION 22 24 Substrate binding. {ECO:0000250}. FT REGION 62 65 Substrate binding. {ECO:0000250}. FT BINDING 39 39 Substrate. {ECO:0000250}. FT BINDING 119 119 Substrate. {ECO:0000250}. FT BINDING 166 166 Substrate. {ECO:0000250}. FT BINDING 340 340 ATP. {ECO:0000250}. SQ SEQUENCE 417 AA; 46133 MW; C87589CCCE5835E0 CRC64; MIMFLTLDDF NFEDKRVVLR VDINCPIDPN TGEILDDKRI REIKSTITEL INKGAKVVIL AHQSRPGKKD FTTLKNHAKV LSDVIGKEVE YIDEVIGSTA REAIINMKCG DVILLENVRF YSEEVLSDWK KWENITPKKQ AETNLIKRLA PLFDYFVNDA FAAAHRAQPS LVGFSYYMPM IAGRLMEREV GVLSKVLENP EKPCVYVLGG AKADDSIRVM KNVLENGTAD KVLTSGIVAN IFLVAMGYDL GVNMDIIENL GLKSQIEIAK ELLNKFEDKI VVPVDVALNI NEERVEADLN KDEKVEHLIN DIGEKTIELY SEIINEAKTI VANGPAGVFE KEAFAKGTEE LLKAIANSKG FSVIGGGHLS AAAELFGIAD KIDHVSTGGG ATLDFLAGEK LPVIEMLKES YKKYKGQ // ID PHI_METJA Reviewed; 180 AA. AC Q58644; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=3-hexulose-6-phosphate isomerase; DE EC=5.3.1.27; DE AltName: Full=6-phospho-3-hexuloisomerase; DE Short=PHI; GN Name=phi; OrderedLocusNames=MJ1247; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PATHWAY. RX PubMed=16237021; DOI=10.1128/JB.187.21.7382-7389.2005; RA Grochowski L.L., Xu H., White R.H.; RT "Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii RT occurs in the absence of a pentose-phosphate pathway."; RL J. Bacteriol. 187:7382-7389(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH CITRIC ACID, RP FUNCTION, AND SUBUNIT. RX PubMed=11839305; DOI=10.1016/S0969-2126(02)00701-3; RA Martinez-Cruz L.A., Dreyer M.K., Boisvert D.C., Yokota H., RA Martinez-Chantar M.L., Kim R., Kim S.-H.; RT "Crystal structure of MJ1247 protein from M. jannaschii at 2.0 A RT resolution infers a molecular function of 3-hexulose-6-phosphate RT isomerase."; RL Structure 10:195-204(2002). CC -!- FUNCTION: Catalyzes the isomerization between 3-hexulose 6- CC phosphate and fructose 6-phosphate. {ECO:0000269|PubMed:11839305}. CC -!- CATALYTIC ACTIVITY: D-arabino-hex-3-ulose 6-phosphate = D-fructose CC 6-phosphate. CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate CC biosynthesis. {ECO:0000269|PubMed:16237021}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:11839305}. CC -!- SIMILARITY: Belongs to the SIS family. PHI subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 SIS domain. {ECO:0000255|PROSITE- CC ProRule:PRU00797}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99251.1; -; Genomic_DNA. DR PIR; F64455; F64455. DR PDB; 1JEO; X-ray; 2.00 A; A=1-180. DR PDBsum; 1JEO; -. DR ProteinModelPortal; Q58644; -. DR SMR; Q58644; 4-180. DR STRING; 243232.MJ_1247; -. DR EnsemblBacteria; AAB99251; AAB99251; MJ_1247. DR KEGG; mja:MJ_1247; -. DR eggNOG; arCOG00068; Archaea. DR eggNOG; COG0794; LUCA. DR InParanoid; Q58644; -. DR KO; K08094; -. DR OMA; FAMRLRH; -. DR PhylomeDB; Q58644; -. DR BRENDA; 5.3.1.27; 3260. DR UniPathway; UPA00293; -. DR EvolutionaryTrace; Q58644; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030246; F:carbohydrate binding; IEA:InterPro. DR GO; GO:0004360; F:glutamine-fructose-6-phosphate transaminase (isomerizing) activity; IBA:GO_Central. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0006002; P:fructose 6-phosphate metabolic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0006047; P:UDP-N-acetylglucosamine metabolic process; IBA:GO_Central. DR InterPro; IPR017552; PHI/rmpB. DR InterPro; IPR001347; SIS. DR Pfam; PF01380; SIS; 1. DR TIGRFAMs; TIGR03127; RuMP_HxlB; 1. DR PROSITE; PS51464; SIS; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 180 3-hexulose-6-phosphate isomerase. FT /FTId=PRO_0000136568. FT DOMAIN 33 167 SIS. {ECO:0000255|PROSITE- FT ProRule:PRU00797}. FT REGION 90 95 Substrate-binding. {ECO:0000305}. FT ACT_SITE 147 147 Proton acceptor. {ECO:0000305}. FT BINDING 51 51 Substrate. {ECO:0000305}. FT HELIX 5 15 {ECO:0000244|PDB:1JEO}. FT HELIX 16 18 {ECO:0000244|PDB:1JEO}. FT HELIX 19 22 {ECO:0000244|PDB:1JEO}. FT HELIX 24 39 {ECO:0000244|PDB:1JEO}. FT STRAND 41 46 {ECO:0000244|PDB:1JEO}. FT HELIX 49 64 {ECO:0000244|PDB:1JEO}. FT STRAND 69 71 {ECO:0000244|PDB:1JEO}. FT STRAND 85 93 {ECO:0000244|PDB:1JEO}. FT HELIX 96 106 {ECO:0000244|PDB:1JEO}. FT STRAND 112 118 {ECO:0000244|PDB:1JEO}. FT HELIX 121 125 {ECO:0000244|PDB:1JEO}. FT STRAND 127 131 {ECO:0000244|PDB:1JEO}. FT HELIX 144 164 {ECO:0000244|PDB:1JEO}. FT HELIX 169 175 {ECO:0000244|PDB:1JEO}. SQ SEQUENCE 180 AA; 20443 MW; 7C3D607BCBD4AA0A CRC64; MSKLEELDIV SNNILILKKF YTNDEWKNKL DSLIDRIIKA KKIFIFGVGR SGYIGRCFAM RLMHLGFKSY FVGETTTPSY EKDDLLILIS GSGRTESVLT VAKKAKNINN NIIAIVCECG NVVEFADLTI PLEVKKSKYL PMGTTFEETA LIFLDLVIAE IMKRLNLDES EIIKRHCNLL // ID PDAD_METJA Reviewed; 165 AA. AC Q57764; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 117. DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase; DE Short=PvlArgDC; DE EC=4.1.1.19; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit beta; DE Contains: DE RecName: Full=Pyruvoyl-dependent arginine decarboxylase subunit alpha; GN Name=pdaD; OrderedLocusNames=MJ0316; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION, AND MASS SPECTROMETRY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11980912; DOI=10.1074/jbc.M203467200; RA Graham D.E., Xu H., White R.H.; RT "Methanococcus jannaschii uses a pyruvoyl-dependent arginine RT decarboxylase in polyamine biosynthesis."; RL J. Biol. Chem. 277:23500-23507(2002). CC -!- CATALYTIC ACTIVITY: L-arginine = agmatine + CO(2). CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Note=Binds 1 pyruvoyl group covalently per subunit.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Thermostable.; CC -!- SUBUNIT: Trimer of an alpha-beta dimer. CC -!- MASS SPECTROMETRY: Mass=5436; Mass_error=11; Method=MALDI; CC Range=1-52; Evidence={ECO:0000269|PubMed:11980912}; CC -!- MASS SPECTROMETRY: Mass=12356; Mass_error=57; Method=MALDI; CC Range=53-165; Evidence={ECO:0000269|PubMed:11980912}; CC -!- SIMILARITY: Belongs to the PdaD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98302.1; -; Genomic_DNA. DR PIR; E64339; E64339. DR PDB; 1MT1; X-ray; 2.20 A; A/C/E/G/I/K=1-52, B/D/F/H/J/L=53-165. DR PDB; 1N13; X-ray; 1.40 A; A/C/E/G/I/K=1-52, B/D/F/H/J/L=53-165. DR PDB; 1N2M; X-ray; 1.90 A; A/B/C/D/E/F=1-165. DR PDB; 2QQC; X-ray; 2.00 A; A/C/E/G/I/K=1-52, B/D/F/H/J/L=54-165. DR PDB; 2QQD; X-ray; 2.00 A; A/D=1-52, B/E=54-165, C/F/G/H=1-165. DR PDBsum; 1MT1; -. DR PDBsum; 1N13; -. DR PDBsum; 1N2M; -. DR PDBsum; 2QQC; -. DR PDBsum; 2QQD; -. DR ProteinModelPortal; Q57764; -. DR SMR; Q57764; 3-165. DR STRING; 243232.MJ_0316; -. DR EnsemblBacteria; AAB98302; AAB98302; MJ_0316. DR KEGG; mja:MJ_0316; -. DR eggNOG; arCOG04490; Archaea. DR eggNOG; COG1945; LUCA. DR InParanoid; Q57764; -. DR KO; K02626; -. DR OMA; ISSIMPP; -. DR PhylomeDB; Q57764; -. DR BRENDA; 4.1.1.19; 3260. DR SABIO-RK; Q57764; -. DR EvolutionaryTrace; Q57764; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008792; F:arginine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006527; P:arginine catabolic process; IEA:InterPro. DR Gene3D; 3.50.20.10; -; 1. DR HAMAP; MF_01404; PvlArgDC; 1. DR InterPro; IPR016104; Pyr-dep_his/arg-deCO2ase. DR InterPro; IPR016105; Pyr-dep_his/arg-deCO2ase_sand. DR InterPro; IPR002724; Pyruvoyl-dep_arg_deCO2ase. DR Pfam; PF01862; PvlArgDC; 1. DR PIRSF; PIRSF005216; Pyruvoyl-dep_arg_deCO2ase; 1. DR ProDom; PD010449; Pyruvoyl-dep_arg_deCO2ase; 1. DR SUPFAM; SSF56271; SSF56271; 1. DR TIGRFAMs; TIGR00286; TIGR00286; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Decarboxylase; Lyase; Pyruvate; KW Reference proteome. FT CHAIN 1 52 Pyruvoyl-dependent arginine decarboxylase FT subunit beta. FT /FTId=PRO_0000023314. FT CHAIN 53 165 Pyruvoyl-dependent arginine decarboxylase FT subunit alpha. FT /FTId=PRO_0000023315. FT SITE 52 53 Cleavage (non-hydrolytic). FT MOD_RES 53 53 Pyruvic acid (Ser). FT HELIX 10 12 {ECO:0000244|PDB:2QQD}. FT STRAND 17 26 {ECO:0000244|PDB:1N13}. FT HELIX 30 41 {ECO:0000244|PDB:1N13}. FT STRAND 46 51 {ECO:0000244|PDB:1N13}. FT STRAND 53 55 {ECO:0000244|PDB:2QQD}. FT STRAND 72 82 {ECO:0000244|PDB:1N13}. FT STRAND 88 100 {ECO:0000244|PDB:1N13}. FT STRAND 105 114 {ECO:0000244|PDB:1N13}. FT HELIX 116 134 {ECO:0000244|PDB:1N13}. FT STRAND 138 149 {ECO:0000244|PDB:1N13}. FT STRAND 151 163 {ECO:0000244|PDB:1N13}. SQ SEQUENCE 165 AA; 17708 MW; 04C7F8AB3AEC2342 CRC64; MNAEINPLHA YFKLPNTVSL VAGSSEGETP LNAFDGALLN AGIGNVNLIR ISSIMPPEAE IVPLPKLPMG ALVPTAYGYI ISDVPGETIS AAISVAIPKD KSLCGLIMEY EGKCSKKEAE KTVREMAKIG FEMRGWELDR IESIAVEHTV EKLGCAFAAA ALWYK // ID PDXT_METJA Reviewed; 186 AA. AC Q59055; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Pyridoxal 5'-phosphate synthase subunit PdxT {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=4.3.3.6 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pdx2 {ECO:0000255|HAMAP-Rule:MF_01615}; DE AltName: Full=Pyridoxal 5'-phosphate synthase glutaminase subunit {ECO:0000255|HAMAP-Rule:MF_01615}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_01615}; GN Name=pdxT {ECO:0000255|HAMAP-Rule:MF_01615}; OrderedLocusNames=MJ1661; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS). RA Manzoku M., Ebihara A., Yokoyama S., Kuramitsu S.; RT "Crystal structure of uncharacterized conserved protein from RT Methanocaldococcus jannaschii."; RL Submitted (APR-2007) to the PDB data bank. CC -!- FUNCTION: Catalyzes the hydrolysis of glutamine to glutamate and CC ammonia as part of the biosynthesis of pyridoxal 5'-phosphate. The CC resulting ammonia molecule is channeled to the active site of CC PdxS. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate + D-glyceraldehyde 3- CC phosphate + L-glutamine = pyridoxal 5'-phosphate + L-glutamate + 3 CC H(2)O + phosphate. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- PATHWAY: Cofactor biosynthesis; pyridoxal 5'-phosphate CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SUBUNIT: In the presence of PdxS, forms a dodecamer of CC heterodimers. Only shows activity in the heterodimer. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC -!- SIMILARITY: Belongs to the glutaminase PdxT/SNO family. CC {ECO:0000255|HAMAP-Rule:MF_01615}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99679.1; -; Genomic_DNA. DR PIR; C64507; C64507. DR PDB; 2YWJ; X-ray; 1.90 A; A=1-186. DR PDBsum; 2YWJ; -. DR ProteinModelPortal; Q59055; -. DR SMR; Q59055; 1-185. DR STRING; 243232.MJ_1661; -. DR EnsemblBacteria; AAB99679; AAB99679; MJ_1661. DR KEGG; mja:MJ_1661; -. DR eggNOG; arCOG00034; Archaea. DR eggNOG; COG0311; LUCA. DR InParanoid; Q59055; -. DR KO; K08681; -. DR OMA; KINCIPK; -. DR PhylomeDB; Q59055; -. DR UniPathway; UPA00245; -. DR EvolutionaryTrace; Q59055; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0036381; F:pyridoxal 5'-phosphate synthase (glutamine hydrolysing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006543; P:glutamine catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01615; PdxT; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002161; PdxT/SNO. DR InterPro; IPR021196; PdxT/SNO_CS. DR Pfam; PF01174; SNO; 1. DR PIRSF; PIRSF005639; Glut_amidoT_SNO; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR03800; PLP_synth_Pdx2; 1. DR PROSITE; PS01236; PDXT_SNO_1; 1. DR PROSITE; PS51130; PDXT_SNO_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Glutamine amidotransferase; KW Hydrolase; Lyase; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 186 Pyridoxal 5'-phosphate synthase subunit FT PdxT. FT /FTId=PRO_0000135680. FT REGION 46 48 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT REGION 128 129 L-glutamine binding. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 75 75 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 165 165 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT ACT_SITE 167 167 Charge relay system. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT BINDING 101 101 L-glutamine. {ECO:0000255|HAMAP- FT Rule:MF_01615}. FT STRAND 2 6 {ECO:0000244|PDB:2YWJ}. FT STRAND 8 10 {ECO:0000244|PDB:2YWJ}. FT HELIX 13 21 {ECO:0000244|PDB:2YWJ}. FT STRAND 24 29 {ECO:0000244|PDB:2YWJ}. FT HELIX 32 35 {ECO:0000244|PDB:2YWJ}. FT STRAND 39 43 {ECO:0000244|PDB:2YWJ}. FT HELIX 48 57 {ECO:0000244|PDB:2YWJ}. FT HELIX 60 65 {ECO:0000244|PDB:2YWJ}. FT STRAND 71 74 {ECO:0000244|PDB:2YWJ}. FT HELIX 76 81 {ECO:0000244|PDB:2YWJ}. FT STRAND 95 100 {ECO:0000244|PDB:2YWJ}. FT TURN 101 104 {ECO:0000244|PDB:2YWJ}. FT STRAND 106 108 {ECO:0000244|PDB:2YWJ}. FT STRAND 111 117 {ECO:0000244|PDB:2YWJ}. FT TURN 118 120 {ECO:0000244|PDB:2YWJ}. FT STRAND 121 129 {ECO:0000244|PDB:2YWJ}. FT STRAND 132 136 {ECO:0000244|PDB:2YWJ}. FT STRAND 142 147 {ECO:0000244|PDB:2YWJ}. FT STRAND 150 156 {ECO:0000244|PDB:2YWJ}. FT STRAND 159 164 {ECO:0000244|PDB:2YWJ}. FT HELIX 166 168 {ECO:0000244|PDB:2YWJ}. FT HELIX 172 183 {ECO:0000244|PDB:2YWJ}. SQ SEQUENCE 186 AA; 20597 MW; FB1EB98EF5E982AA CRC64; MIIGVLAIQG DVEEHEEAIK KAGYEAKKVK RVEDLEGIDA LIIPGGESTA IGKLMKKYGL LEKIKNSNLP ILGTCAGMVL LSKGTGINQI LLELMDITVK RNAYGRQVDS FEKEIEFKDL GKVYGVFIRA PVVDKILSDD VEVIARDGDK IVGVKQGKYM ALSFHPELSE DGYKVYKYFV ENCVKK // ID PFDA2_METJA Reviewed; 147 AA. AC Q58064; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Prefoldin subunit alpha 2; DE AltName: Full=GimC subunit alpha 2; GN Name=pfdA2; OrderedLocusNames=MJ0648; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Molecular chaperone capable of stabilizing a range of CC proteins. Seems to fulfill an ATP-independent, HSP70-like function CC in archaeal de novo protein folding (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98646.1; -; Genomic_DNA. DR PIR; H64380; H64380. DR ProteinModelPortal; Q58064; -. DR STRING; 243232.MJ_0648; -. DR EnsemblBacteria; AAB98646; AAB98646; MJ_0648. DR KEGG; mja:MJ_0648; -. DR eggNOG; arCOG01341; Archaea. DR eggNOG; COG1730; LUCA. DR InParanoid; Q58064; -. DR KO; K04797; -. DR OMA; QVEMKVE; -. DR PhylomeDB; Q58064; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-HAMAP. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.370; -; 1. DR HAMAP; MF_00308; PfdA; 1. DR InterPro; IPR011599; PFD_alpha_archaea. DR InterPro; IPR009053; Prefoldin. DR InterPro; IPR004127; Prefoldin_subunit_alpha. DR Pfam; PF02996; Prefoldin; 1. DR SUPFAM; SSF46579; SSF46579; 1. DR TIGRFAMs; TIGR00293; TIGR00293; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 147 Prefoldin subunit alpha 2. FT /FTId=PRO_0000153675. FT COMPBIAS 133 147 Glu-rich. SQ SEQUENCE 147 AA; 16394 MW; 1731EAD91ED0AC9F CRC64; MVNEVIDINE AVRAYIAQIE GLRAEIGRLD ATIATLRQSL ATLKSLKTLG EGKTVLVPVG SIAQVEMKVE KMDKVVVSVG QNISAELEYE EALKYIEDEI KKLLTFRLVL EQAIAELYAK IEDLIAEAQQ TSEEEKAEEE ENEEKAE // ID PELO_METJA Reviewed; 347 AA. AC Q57638; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 95. DE RecName: Full=Protein pelota homolog {ECO:0000255|HAMAP-Rule:MF_01853}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01853}; GN Name=pelA {ECO:0000255|HAMAP-Rule:MF_01853}; OrderedLocusNames=MJ0174; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May function in recognizing stalled ribosomes, interact CC with stem-loop structures in stalled mRNA molecules, and effect CC endonucleolytic cleavage of the mRNA. May play a role in the CC release non-functional ribosomes and degradation of damaged mRNAs. CC Has endoribonuclease activity. {ECO:0000255|HAMAP-Rule:MF_01853}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01853}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01853}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01853}. CC -!- DOMAIN: The N-terminal domain has the RNA-binding Sm fold. It CC harbors the endoribonuclease activity. {ECO:0000255|HAMAP- CC Rule:MF_01853}. CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. CC Pelota subfamily. {ECO:0000255|HAMAP-Rule:MF_01853}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98159.1; -; Genomic_DNA. DR PIR; G64321; G64321. DR ProteinModelPortal; Q57638; -. DR STRING; 243232.MJ_0174; -. DR EnsemblBacteria; AAB98159; AAB98159; MJ_0174. DR KEGG; mja:MJ_0174; -. DR eggNOG; arCOG01741; Archaea. DR eggNOG; COG1537; LUCA. DR InParanoid; Q57638; -. DR KO; K06965; -. DR OMA; AFYGKKH; -. DR PhylomeDB; Q57638; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0070966; P:nuclear-transcribed mRNA catabolic process, no-go decay; IEA:InterPro. DR GO; GO:0070481; P:nuclear-transcribed mRNA catabolic process, non-stop decay; IEA:InterPro. DR GO; GO:0071025; P:RNA surveillance; IEA:InterPro. DR Gene3D; 3.30.1330.30; -; 2. DR HAMAP; MF_01853; PelO; 1. DR InterPro; IPR005140; eRF1_1_Pelota. DR InterPro; IPR005141; eRF1_2. DR InterPro; IPR005142; eRF1_3. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR023521; Pelota_arc. DR InterPro; IPR004405; Transl-rel_pelota. DR PANTHER; PTHR10853; PTHR10853; 1. DR Pfam; PF03463; eRF1_1; 1. DR Pfam; PF03464; eRF1_2; 1. DR Pfam; PF03465; eRF1_3; 1. DR SMART; SM01194; eRF1_1; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR TIGRFAMs; TIGR00111; pelota; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; KW Nuclease; Reference proteome. FT CHAIN 1 347 Protein pelota homolog. FT /FTId=PRO_0000143193. SQ SEQUENCE 347 AA; 39624 MW; 2F1FBCA439EB47A2 CRC64; MKIIEEIPQK NIIKLMPENL DDLWVLYNII EEGDKIFAVT ERRVQDKGDV IRADRGAKRK MFLGIEVKNV EFDENTKRVR ILGTIIHGPD DVPLGSHHTI EIKPFDELSI EKNWKKWQIE RIKEAIESSK RPKVLVVVMD DEEADIFEVR DYSIKEICSI KSHTSKKLDY KINEELKKEY YHEIAKVLSE YDVDNILVAG PGFAKNSFYN FISSQYPELK NKIVVESIST TSRAGLNEVI KRGIINRIYA ESRVAKETQL IEKLLEEIAK KGLAVYGIDE VKKALEYSAI DTLLVSDSLV RNHEIEKIID TTEEMGGKVV IVSSEHDAGK QLKALGGIAG LLRFPIE // ID PFDA1_METJA Reviewed; 142 AA. AC Q58362; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Prefoldin subunit alpha 1; DE AltName: Full=GimC subunit alpha 1; GN Name=pfdA1; Synonyms=pfdA; OrderedLocusNames=MJ0952; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Molecular chaperone capable of stabilizing a range of CC proteins. Seems to fulfill an ATP-independent, HSP70-like function CC in archaeal de novo protein folding (By similarity). CC {ECO:0000250}. CC -!- SUBUNIT: Heterohexamer of two alpha and four beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the prefoldin subunit alpha family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98957.1; -; Genomic_DNA. DR PIR; H64418; H64418. DR ProteinModelPortal; Q58362; -. DR STRING; 243232.MJ_0952; -. DR EnsemblBacteria; AAB98957; AAB98957; MJ_0952. DR KEGG; mja:MJ_0952; -. DR eggNOG; arCOG01341; Archaea. DR eggNOG; COG1730; LUCA. DR InParanoid; Q58362; -. DR KO; K04797; -. DR OMA; NQQLQMI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016272; C:prefoldin complex; IEA:UniProtKB-HAMAP. DR GO; GO:0006457; P:protein folding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.370; -; 1. DR HAMAP; MF_00308; PfdA; 1. DR InterPro; IPR011599; PFD_alpha_archaea. DR InterPro; IPR009053; Prefoldin. DR InterPro; IPR004127; Prefoldin_subunit_alpha. DR Pfam; PF02996; Prefoldin; 1. DR SUPFAM; SSF46579; SSF46579; 1. DR TIGRFAMs; TIGR00293; TIGR00293; 1. PE 3: Inferred from homology; KW Chaperone; Complete proteome; Cytoplasm; Reference proteome. FT CHAIN 1 142 Prefoldin subunit alpha 1. FT /FTId=PRO_0000153674. FT COMPBIAS 96 112 Lys-rich. FT COMPBIAS 128 142 Gln-rich. SQ SEQUENCE 142 AA; 16080 MW; 770B816F0A98517A CRC64; MENMAEDLRQ KAMALEIYNQ QLQMIQSEIT SIRALKSEIM NSIKTIENIK ADEETLIPVG PGVFLKAKIV DDKALIGVKS DIYVEKSFNE VIEDLKKSVE DLDKAEKEGM KKAEELAKAI TALRKELQTE IQKAQQAQDK KQ // ID PIMT_METJA Reviewed; 215 AA. AC Q57636; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Protein-L-isoaspartate O-methyltransferase; DE EC=2.1.1.77; DE AltName: Full=L-isoaspartyl protein carboxyl methyltransferase; DE AltName: Full=Protein L-isoaspartyl methyltransferase; DE AltName: Full=Protein-beta-aspartate methyltransferase; DE Short=PIMT; GN Name=pcm; OrderedLocusNames=MJ0172; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the methyl esterification of L-isoaspartyl CC residues in peptides and proteins that result from spontaneous CC decomposition of normal L-aspartyl and L-asparaginyl residues. It CC plays a role in the repair and/or degradation of damaged proteins CC (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + protein L- CC isoaspartate = S-adenosyl-L-homocysteine + protein L-isoaspartate CC alpha-methyl ester. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. L- CC isoaspartyl/D-aspartyl protein methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98157.1; -; Genomic_DNA. DR PIR; E64321; E64321. DR PDB; 2YXE; X-ray; 2.00 A; A/B=1-215. DR PDBsum; 2YXE; -. DR ProteinModelPortal; Q57636; -. DR SMR; Q57636; 2-215. DR STRING; 243232.MJ_0172; -. DR EnsemblBacteria; AAB98157; AAB98157; MJ_0172. DR KEGG; mja:MJ_0172; -. DR eggNOG; arCOG00976; Archaea. DR eggNOG; COG2518; LUCA. DR InParanoid; Q57636; -. DR KO; K00573; -. DR OMA; HNISTRH; -. DR PhylomeDB; Q57636; -. DR EvolutionaryTrace; Q57636; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004719; F:protein-L-isoaspartate (D-aspartate) O-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030091; P:protein repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00090; PIMT; 1. DR InterPro; IPR000682; PCMT. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11579; PTHR11579; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00080; pimt; 1. DR PROSITE; PS01279; PCMT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 215 Protein-L-isoaspartate O- FT methyltransferase. FT /FTId=PRO_0000111916. FT ACT_SITE 61 61 {ECO:0000250}. FT HELIX 3 16 {ECO:0000244|PDB:2YXE}. FT HELIX 23 31 {ECO:0000244|PDB:2YXE}. FT HELIX 34 37 {ECO:0000244|PDB:2YXE}. FT HELIX 40 45 {ECO:0000244|PDB:2YXE}. FT STRAND 52 55 {ECO:0000244|PDB:2YXE}. FT STRAND 58 60 {ECO:0000244|PDB:2YXE}. FT HELIX 63 72 {ECO:0000244|PDB:2YXE}. FT STRAND 80 84 {ECO:0000244|PDB:2YXE}. FT HELIX 90 99 {ECO:0000244|PDB:2YXE}. FT STRAND 103 110 {ECO:0000244|PDB:2YXE}. FT HELIX 112 125 {ECO:0000244|PDB:2YXE}. FT STRAND 130 135 {ECO:0000244|PDB:2YXE}. FT HELIX 137 139 {ECO:0000244|PDB:2YXE}. FT HELIX 142 144 {ECO:0000244|PDB:2YXE}. FT STRAND 147 158 {ECO:0000244|PDB:2YXE}. FT HELIX 161 165 {ECO:0000244|PDB:2YXE}. FT STRAND 167 190 {ECO:0000244|PDB:2YXE}. FT STRAND 193 202 {ECO:0000244|PDB:2YXE}. SQ SEQUENCE 215 AA; 23761 MW; E5A8634F2E2BAE8B CRC64; MDLEEQKKAV IEKLIREGYI KSKRVIDALL KVPREEFLPE HLKEYAYVDT PLEIGYGQTI SAIHMVGMMC ELLDLKPGMK VLEIGTGCGY HAAVTAEIVG EDGLVVSIER IPELAEKAER TLRKLGYDNV IVIVGDGTLG YEPLAPYDRI YTTAAGPKIP EPLIRQLKDG GKLLMPVGRY LQRLVLAEKR GDEIIIKDCG PVAFVPLVGK EGFQG // ID PHEA_METJA Reviewed; 272 AA. AC Q58054; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Prephenate dehydratase; DE Short=PDT; DE EC=4.2.1.51; DE AltName: Full=MjPDT; GN Name=pheA; OrderedLocusNames=MJ0637; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP BIOPHYSICAL CHARACTERIZATION, SUBUNIT, MASS SPECTROMETRY, AND RP INHIBITION. RX PubMed=17115705; DOI=10.1021/bi061274n; RA Kleeb A.C., Kast P., Hilvert D.; RT "A monofunctional and thermostable prephenate dehydratase from the RT archaeon Methanocaldococcus jannaschii."; RL Biochemistry 45:14101-14110(2006). CC -!- CATALYTIC ACTIVITY: Prephenate = phenylpyruvate + H(2)O + CO(2). CC -!- ENZYME REGULATION: Inhibited by L-phenylalanine but not by L- CC tyrosine or L-tryptophan. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=22 uM for prephenate; CC pH dependence: CC Optimum pH is 5-10.; CC Temperature dependence: CC Thermostable.; CC -!- PATHWAY: Amino-acid biosynthesis; L-phenylalanine biosynthesis; CC phenylpyruvate from prephenate: step 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17115705}. CC -!- MASS SPECTROMETRY: Mass=31413; Method=Electrospray; Range=1-272; CC Evidence={ECO:0000269|PubMed:17115705}; CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC -!- SIMILARITY: Contains 1 prephenate dehydratase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00517}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98631.1; -; Genomic_DNA. DR PIR; E64379; E64379. DR ProteinModelPortal; Q58054; -. DR STRING; 243232.MJ_0637; -. DR EnsemblBacteria; AAB98631; AAB98631; MJ_0637. DR KEGG; mja:MJ_0637; -. DR eggNOG; arCOG00255; Archaea. DR eggNOG; COG0077; LUCA. DR InParanoid; Q58054; -. DR KO; K04518; -. DR OMA; TKVYSHP; -. DR PhylomeDB; Q58054; -. DR SABIO-RK; Q58054; -. DR UniPathway; UPA00121; UER00345. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004664; F:prephenate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0009094; P:L-phenylalanine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR001086; Preph_deHydtase. DR InterPro; IPR018528; Preph_deHydtase_CS. DR Pfam; PF01842; ACT; 1. DR Pfam; PF00800; PDT; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00857; PREPHENATE_DEHYDR_1; 1. DR PROSITE; PS00858; PREPHENATE_DEHYDR_2; 1. DR PROSITE; PS51171; PREPHENATE_DEHYDR_3; 1. PE 1: Evidence at protein level; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Phenylalanine biosynthesis; KW Reference proteome. FT CHAIN 1 272 Prephenate dehydratase. FT /FTId=PRO_0000119180. FT DOMAIN 4 179 Prephenate dehydratase. FT {ECO:0000255|PROSITE-ProRule:PRU00517}. FT DOMAIN 194 269 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT SITE 172 172 Essential for activity. {ECO:0000250}. SQ SEQUENCE 272 AA; 31415 MW; 0A5FDCE74AB7C3AD CRC64; MNKAVIYTLP KGTYSEKATK KFLDYIDGDY KIDYCNSIYD VFERVDNNGL GVVPIENSIE GSVSLTQDLL LQFKDIKILG ELALDIHHNL IGYDKNKIKT VISHPQALAQ CRNYIKKHGW DVKAVESTAK AVKIVAESKD ETLGAIGSKE SAEHYNLKIL DENIEDYKNN KTRFILIGKK VKFKYHPKNY KVSIVFELKE DKPGALYHIL KEFAERNINL TRIESRPSKK RLGTYIFYID FENNKEKLEE ILKSLERHTT FINLLGKYPV FD // ID PHOU_METJA Reviewed; 236 AA. AC Q58415; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Phosphate-specific transport system accessory protein PhoU homolog; DE Short=Pst system accessory protein PhoU homolog; GN OrderedLocusNames=MJ1009; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Plays a role in the regulation of phosphate uptake. CC {ECO:0000250}. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PhoU family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99011.1; -; Genomic_DNA. DR PIR; H64425; H64425. DR ProteinModelPortal; Q58415; -. DR STRING; 243232.MJ_1009; -. DR EnsemblBacteria; AAB99011; AAB99011; MJ_1009. DR KEGG; mja:MJ_1009; -. DR eggNOG; arCOG00232; Archaea. DR eggNOG; COG0704; LUCA. DR InParanoid; Q58415; -. DR KO; K02039; -. DR OMA; ELATYMM; -. DR PhylomeDB; Q58415; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; ISS:UniProtKB. DR GO; GO:0030643; P:cellular phosphate ion homeostasis; IEA:InterPro. DR GO; GO:0045936; P:negative regulation of phosphate metabolic process; ISS:UniProtKB. DR GO; GO:2000186; P:negative regulation of phosphate transmembrane transport; ISS:UniProtKB. DR GO; GO:0006817; P:phosphate ion transport; IEA:UniProtKB-KW. DR InterPro; IPR028366; P_trasport_PhoU. DR InterPro; IPR026022; PhoU_dom. DR PANTHER; PTHR10010:SF14; PTHR10010:SF14; 1. DR Pfam; PF01895; PhoU; 2. DR PIRSF; PIRSF003107; PhoU; 1. DR TIGRFAMs; TIGR02135; phoU_full; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Phosphate transport; Reference proteome; KW Transport. FT CHAIN 1 236 Phosphate-specific transport system FT accessory protein PhoU homolog. FT /FTId=PRO_0000155188. SQ SEQUENCE 236 AA; 27426 MW; 900834E6BBE649D6 CRC64; MPKKFEEILK EVENDLIEMA ELCAEQTENA VKAFIESDRE LAKQVRKRDT TIDLMEMKIE EKCIKAIALY QPVSGDLREL MTAIKISSKL EKVGDNASKI CKILLKSDVE GNRKNELLIV MKDYLINMLK NAMIAFKTRD ESLARDVYNM DKRLDDLYEQ LYRSMISKII ENPKNLTLYT EIIFAGKYLE RSGNIVASIG DRIVYMITGE RIKEEEIEEE LKKEKDIEKN IDQIND // ID PORA_METJA Reviewed; 389 AA. AC Q57715; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Pyruvate synthase subunit PorA; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase alpha chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit alpha; GN Name=porA; OrderedLocusNames=MJ0267; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98254.1; -; Genomic_DNA. DR PIR; D64333; D64333. DR ProteinModelPortal; Q57715; -. DR STRING; 243232.MJ_0267; -. DR EnsemblBacteria; AAB98254; AAB98254; MJ_0267. DR KEGG; mja:MJ_0267; -. DR eggNOG; arCOG01608; Archaea. DR eggNOG; COG0674; LUCA. DR InParanoid; Q57715; -. DR KO; K00169; -. DR OMA; WHFEHKA; -. DR PhylomeDB; Q57715; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR033412; PFOR_II. DR InterPro; IPR002880; Pyrv_Fd/Flavodoxin_OxRdtase_N. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR Pfam; PF17147; PFOR_II; 1. DR Pfam; PF01855; POR_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 389 Pyruvate synthase subunit PorA. FT /FTId=PRO_0000099896. SQ SEQUENCE 389 AA; 42971 MW; 2CAA3DDE3EB0F5A9 CRC64; METMCEVKVI TGTSAAAEAA KLADVDVIAA YPITPQTTCV EKLAEFVANG ELDAEYIKVE SEHSAMSACI GAAATGARTF TATASQGLAL MHEMLFIASG MRLPIVMMVA NRALSAPINI WNDHQDSIAE RDSGWIQIYV EDNQETLDSI IQAYKIAENE DVLLPVMVCL DGFILTHTVE PVTIPKAERV REFLGVYEPK HAYLDPDRPI TQGPVGVPDC YMETRKQIEE AMERAKKVIR DVNEEFAEWF KRKYGNGLVE AYNLDNADTV LVAMGSVCGT IKYVIDELKK EGKNVGLLRI RAFRPFPKED VKELLKDANN IAVLDKNISL GFNKGALGIE MASILKNKKV CNYIVGLGGR DIKIDDIKTI INHVEKAEDD STLWVGLKE // ID PORB_METJA Reviewed; 298 AA. AC Q57714; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 3. DT 17-FEB-2016, entry version 87. DE RecName: Full=Pyruvate synthase subunit PorB; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase beta chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit beta; GN Name=porB; OrderedLocusNames=MJ0266; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P94692}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. CC {ECO:0000250|UniProtKB:P94692}; CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. {ECO:0000250}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98253.1; -; Genomic_DNA. DR PIR; C64333; C64333. DR ProteinModelPortal; Q57714; -. DR STRING; 243232.MJ_0266; -. DR EnsemblBacteria; AAB98253; AAB98253; MJ_0266. DR KEGG; mja:MJ_0266; -. DR eggNOG; arCOG01601; Archaea. DR eggNOG; COG1013; LUCA. DR InParanoid; Q57714; -. DR KO; K00170; -. DR OMA; TAWRVPW; -. DR PhylomeDB; Q57714; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR SUPFAM; SSF52518; SSF52518; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 298 Pyruvate synthase subunit PorB. FT /FTId=PRO_0000099903. FT METAL 19 19 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 22 22 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 47 47 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 218 218 Iron-sulfur (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. SQ SEQUENCE 298 AA; 33098 MW; D772C50EE8611A49 CRC64; MIVMQFPREE YFAPGHRGCA GCGAAIVARL LLKVAGKDTI ITNATGCLEV MTTPYPETSW RVPWIHTAFE NAAATASGIE AAVKALKRKR GKFADKKINV IAIGGDGGTA DIGFQALSGA MERGHDILYI MYDNEAYMNT GIQRSSSTPF MAATTTSPAG SKIRGEDRPK KDMTMIMAAH GIPYVATACI SYPEDFMRKV KKALSIEGPK FIQVLQPCTT GWGYPPEKTI EIGRLAVETG IFPLYEIENG EFRITYKPAK RKPVREYLKM QKRYRHLTDE DIERIQKYID EKCKLLGL // ID PPSA_METJA Reviewed; 1188 AA. AC Q57962; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 119. DE RecName: Full=Probable phosphoenolpyruvate synthase; DE Short=PEP synthase; DE EC=2.7.9.2; DE AltName: Full=Pyruvate, water dikinase; DE Contains: DE RecName: Full=Mja pep intein; DE AltName: Full=Mja pepA intein; GN Name=ppsA; OrderedLocusNames=MJ0542; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the phosphorylation of pyruvate to CC phosphoenolpyruvate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + H(2)O = AMP + CC phosphoenolpyruvate + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- DOMAIN: The N-terminal domain contains the ATP/Pi binding site, CC the central domain the pyrophosphate/phosphate carrier histidine, CC and the C-terminal domain the pyruvate binding site. CC {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- MISCELLANEOUS: The reaction takes place in three steps, mediated CC by a phosphocarrier histidine residue located on the surface of CC the central domain. The two first partial reactions are catalyzed CC at an active site located on the N-terminal domain, and the third CC partial reaction is catalyzed at an active site located on the C- CC terminal domain. For catalytic turnover, the central domain CC swivels from the concave surface of the N-terminal domain to that CC of the C-terminal domain (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PEP-utilizing enzyme family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98534.1; -; Genomic_DNA. DR PIR; F64367; F64367. DR ProteinModelPortal; Q57962; -. DR STRING; 243232.MJ_0542; -. DR EnsemblBacteria; AAB98534; AAB98534; MJ_0542. DR KEGG; mja:MJ_0542; -. DR eggNOG; arCOG01111; Archaea. DR eggNOG; COG0574; LUCA. DR eggNOG; COG1372; LUCA. DR InParanoid; Q57962; -. DR KO; K01007; -. DR OMA; PTMIVEA; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008986; F:pyruvate, water dikinase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 3.10.28.10; -; 1. DR Gene3D; 3.20.20.60; -; 1. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.50.30.10; -; 2. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR000121; PEP_util_C. DR InterPro; IPR023151; PEP_util_CS. DR InterPro; IPR002192; PPDK_PEP-bd. DR InterPro; IPR015813; Pyrv/PenolPyrv_Kinase-like_dom. DR Pfam; PF00391; PEP-utilizers; 2. DR Pfam; PF02896; PEP-utilizers_C; 1. DR Pfam; PF01326; PPDK_N; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF51621; SSF51621; 1. DR SUPFAM; SSF52009; SSF52009; 1. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS00742; PEP_ENZYMES_2; 1. PE 3: Inferred from homology; KW ATP-binding; Autocatalytic cleavage; Complete proteome; Kinase; KW Magnesium; Metal-binding; Nucleotide-binding; Phosphoprotein; KW Protein splicing; Reference proteome; Transferase. FT CHAIN 1 410 Probable phosphoenolpyruvate synthase, FT 1st part. {ECO:0000255}. FT /FTId=PRO_0000023556. FT CHAIN 411 822 Mja pep intein. {ECO:0000255}. FT /FTId=PRO_0000023557. FT CHAIN 823 1188 Probable phosphoenolpyruvate synthase, FT 2nd part. {ECO:0000255}. FT /FTId=PRO_0000023558. FT DOMAIN 536 670 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT ACT_SITE 824 824 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT ACT_SITE 1133 1133 Proton donor. {ECO:0000250}. FT METAL 1061 1061 Magnesium. {ECO:0000250}. FT METAL 1086 1086 Magnesium. {ECO:0000250}. FT BINDING 917 917 Substrate. {ECO:0000250}. FT BINDING 964 964 Substrate. {ECO:0000250}. FT BINDING 1061 1061 Substrate. {ECO:0000250}. FT BINDING 1083 1083 Substrate; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 1084 1084 Substrate; via amide nitrogen. FT {ECO:0000250}. FT BINDING 1085 1085 Substrate. {ECO:0000250}. FT BINDING 1086 1086 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 1188 AA; 134012 MW; 5547E2E2A8C46AEC CRC64; MLIIQNTKGD SMKFIAWLDE LSNKDVDIAG GKGASLGEMW NAGLPVPPAF VVTADAYRHF IKETGLMDKI REILSGLDVN DTDALTNASK KIRKLIEEAE MPEDLRLAII EAYNKLCEMC GEDEVTVAVR SSATAEDLPE ASFAGQQDTY LNIKGAENVV KYVQKCFSSL FTPRAIFYRE QQGFDHFKVA LAAVVQKLVN AEKAGVMFTV NPISENYDEL VIEAAWGLGE GVVSGSVSPD TYIVNKKTLE IVDKHIARKE TMFVKDEKGE TKVVEVPDDM KEKQVLSDDE IKELAKIGLN IEKHYGKPMD VEWAYEKGKF YMLQARPITT LKKGKKEKKA KEEDIEAKIL LKGIGASPGI ATGVVKIIHD VSEIDKVKEG DILVTEMTTP DMVPAMKKAA AIVTDEGGLT CIEGDAKILT DRGFLKMKEV YKLVKNGEKL KVLGLNAETL KTEWKEIIDA QKREARRYEI GVYRKNKNTK DTIKITPDHK FPVFVNGELS KVQLCDIIDN NLSVLSIDYI PMIEEKYESL AEVMYLGGAV LSDGHIVRRN GKPIRVRFTQ KDTEEKKDFI EKVKGDVKLI GGNFIEISNR NNVIEYQTSR KIPSEILGFI EVNINTIPLY ATKDEIADLI AGFVDGDGCL SGKRRVEIYQ NSSHIKKIEG LIVGLYRLGI IPRLRYKRSS TATIYFNNNL ETILQRTRRI KLDKLKEFKK PVEDKKLIDI SQILPELKEF DYKGYLYKTY KEKLFIGINK LEEYLSKIDK DGIERIKQKI KLLKESDIYS IRIKKVGEDY GEVYNITVKA ENEFNHNYVV WTKHYTPIVV FNCHAAIVSR ELGTPCVVGT KKATKVLKDG MIVTVDGEKG IVYEGEIKKV EEKEKKQEVV VQQAPIITAT EVKVNVSMPE VAERAAATGA DGVGLLRAEH MILGLGKHPR KILEEEGEEA LIEALMEGIR KVADAFYPRP VTYRTLDAPT DEFRGLEGGE NEPIEHNPML GWRGIRRDLD EVDILKCELK AIKRLREEGY KNIEIMIPLV THPDEVRRVK EIMREVGLEP CKDIPFGIMV ETPAAALIIE DFIKEGINFV SLGTNDLTQY TIAIDRNNEL VSKYYKEDHP AVLKLVEHVI KTCKKHGIKT SICGQAGSRP HIVEKLVEWG IDSVSANIDA VETIRRVVAR TEQKVILNYI RKSYVERE // ID PORD_METJA Reviewed; 86 AA. AC Q57716; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Pyruvate synthase subunit PorD; DE AltName: Full=Pyruvate oxidoreductase delta chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit delta; GN Name=porD; OrderedLocusNames=MJ0268; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P94692}; CC Note=Binds 2 [4Fe-4S] clusters. {ECO:0000250|UniProtKB:P94692}; CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98255.1; -; Genomic_DNA. DR PIR; E64333; E64333. DR ProteinModelPortal; Q57716; -. DR STRING; 243232.MJ_0268; -. DR EnsemblBacteria; AAB98255; AAB98255; MJ_0268. DR KEGG; mja:MJ_0268; -. DR eggNOG; arCOG01605; Archaea. DR eggNOG; COG1144; LUCA. DR InParanoid; Q57716; -. DR KO; K00171; -. DR OMA; CWIFCPD; -. DR PhylomeDB; Q57716; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR011898; PorD_KorD. DR TIGRFAMs; TIGR02179; PorD_KorD; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 86 Pyruvate synthase subunit PorD. FT /FTId=PRO_0000099918. FT DOMAIN 25 54 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 55 84 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 34 34 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 37 37 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 40 40 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 44 44 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 64 64 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 67 67 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 70 70 Iron-sulfur 2 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. FT METAL 74 74 Iron-sulfur 1 (4Fe-4S). FT {ECO:0000250|UniProtKB:P94692}. SQ SEQUENCE 86 AA; 9848 MW; 6F63454278C15091 CRC64; MVTIAAIIYE PGNSIKNKTG TWRTFRPILD NEKCVKCENC YIFCPEGAIQ EDENGNFKID YDYCKGCLIC MNECPVNAIT KVREEK // ID POK_METJA Reviewed; 270 AA. AC Q58379; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Putative pantoate kinase; DE Short=PoK; DE EC=2.7.1.169; GN OrderedLocusNames=MJ0969; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Phosphorylates (R)-pantoate to form (R)-4- CC phosphopantoate in the CoA biosynthesis pathway. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + (R)-pantoate = ADP + (R)-4- CC phosphopantoate. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the GHMP kinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98974.1; -; Genomic_DNA. DR PIR; A64421; A64421. DR ProteinModelPortal; Q58379; -. DR STRING; 243232.MJ_0969; -. DR EnsemblBacteria; AAB98974; AAB98974; MJ_0969. DR KEGG; mja:MJ_0969; -. DR eggNOG; arCOG04263; Archaea. DR eggNOG; COG1829; LUCA. DR InParanoid; Q58379; -. DR KO; K06982; -. DR OMA; MLGETVF; -. DR PhylomeDB; Q58379; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR012043; PoK. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF016896; GHMP_arc_MJ0969; 1. DR SUPFAM; SSF54211; SSF54211; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 270 Putative pantoate kinase. FT /FTId=PRO_0000107123. SQ SEQUENCE 270 AA; 30035 MW; F594A63020D4E66B CRC64; MFAPGHITGF FVICKSSNKL KTGSIGAGIT IDRGVNVELK EGNGSIFYNN KKVNICAVEK VIEHYKKFGY NDDYDIIFSS DFPLGSGLGM SGGCALILAK KLNEMLNLNE NYAEIAHISE VECGTGLGDV IAQYVKGFVI RKTPGFPINV EKIVVDDDYY IIIEIFGKKE TKEIITNDIW IKKINEYGER CLNELLKNPT LENFVNLSYE FAVNTGLINE KILSICEDLK FTVGASQSML GNTLFCISKK ETLEDALSIL KNPIVCNIYY // ID PORC_METJA Reviewed; 178 AA. AC Q57717; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Pyruvate synthase subunit PorC; DE EC=1.2.7.1; DE AltName: Full=Pyruvate oxidoreductase gamma chain; DE Short=POR; DE AltName: Full=Pyruvic-ferredoxin oxidoreductase subunit gamma; GN Name=porC; OrderedLocusNames=MJ0269; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Pyruvate + CoA + 2 oxidized ferredoxin = CC acetyl-CoA + CO(2) + 2 reduced ferredoxin + 2 H(+). CC -!- SUBUNIT: Heterotetramer of one alpha, one beta, one delta and one CC gamma chain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98256.1; -; Genomic_DNA. DR PIR; F64333; F64333. DR ProteinModelPortal; Q57717; -. DR STRING; 243232.MJ_0269; -. DR EnsemblBacteria; AAB98256; AAB98256; MJ_0269. DR KEGG; mja:MJ_0269; -. DR eggNOG; arCOG01603; Archaea. DR eggNOG; COG1014; LUCA. DR InParanoid; Q57717; -. DR KO; K00172; -. DR OMA; TTLMGAF; -. DR PhylomeDB; Q57717; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0019164; F:pyruvate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006979; P:response to oxidative stress; IBA:GO_Central. DR Gene3D; 3.40.920.10; -; 1. DR InterPro; IPR011894; PorC_KorC. DR InterPro; IPR019752; Pyrv/ketoisovalerate_OxRed_cat. DR InterPro; IPR002869; Pyrv_flavodox_OxRed_cen. DR Pfam; PF01558; POR; 1. DR SUPFAM; SSF53323; SSF53323; 1. DR TIGRFAMs; TIGR02175; PorC_KorC; 1. PE 4: Predicted; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 178 Pyruvate synthase subunit PorC. FT /FTId=PRO_0000099910. SQ SEQUENCE 178 AA; 19202 MW; 3758EE7EC70FAEE1 CRC64; MIEIRFHGRG GQGAVTAAQI LAKAAFYDGK FCQAFPFFGV ERRGAPVMAF TRIDDKKITL RCQIYEPDYV IVQDATLLES VNVVEGLKKD GAVVINTVKD DLDLGYKTYT IDATGIALDV LGVPIVNTAM VGAFAGVTGI VSIESVKKAI LDTFKGKLGE KNAKAAEVAY NEMLKKYG // ID PPAC_METJA Reviewed; 307 AA. AC Q58025; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Manganese-dependent inorganic pyrophosphatase; DE EC=3.6.1.1; DE AltName: Full=Pyrophosphate phospho-hydrolase; DE Short=PPase; GN Name=ppaC; OrderedLocusNames=MJ0608; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-5, CATALYTIC ACTIVITY, AND MASS SPECTROMETRY. RX PubMed=10898947; DOI=10.1006/abbi.2000.1860; RA Kuhn N.J., Wadeson A., Ward S., Young T.W.; RT "Methanococcus jannaschii ORF mj0608 codes for a class C inorganic RT pyrophosphatase protected by Co(2+) or Mn(2+) ions against fluoride RT inhibition."; RL Arch. Biochem. Biophys. 379:292-298(2000). CC -!- CATALYTIC ACTIVITY: Diphosphate + H(2)O = 2 phosphate. CC {ECO:0000269|PubMed:10898947}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- MASS SPECTROMETRY: Mass=34169; Method=Electrospray; Range=1-307; CC Evidence={ECO:0000269|PubMed:10898947}; CC -!- SIMILARITY: Belongs to the PPase class C family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98601.1; -; Genomic_DNA. DR PIR; H64375; H64375. DR PDB; 2EB0; X-ray; 2.20 A; A/B=1-307. DR PDBsum; 2EB0; -. DR ProteinModelPortal; Q58025; -. DR SMR; Q58025; 1-307. DR STRING; 243232.MJ_0608; -. DR EnsemblBacteria; AAB98601; AAB98601; MJ_0608. DR KEGG; mja:MJ_0608; -. DR eggNOG; arCOG01567; Archaea. DR eggNOG; COG1227; LUCA. DR InParanoid; Q58025; -. DR KO; K15986; -. DR OMA; MLCAILS; -. DR PhylomeDB; Q58025; -. DR EvolutionaryTrace; Q58025; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central. DR GO; GO:0004427; F:inorganic diphosphatase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central. DR HAMAP; MF_00207; PPase_C; 1. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR004097; DHHA2. DR InterPro; IPR022934; Mn-dep_inorganic_PyrPase. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02833; DHHA2; 1. DR SMART; SM01131; DHHA2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cobalt; Complete proteome; Cytoplasm; KW Direct protein sequencing; Hydrolase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 307 Manganese-dependent inorganic FT pyrophosphatase. FT /FTId=PRO_0000158599. FT METAL 7 7 Manganese 1. {ECO:0000250}. FT METAL 11 11 Manganese 1. {ECO:0000250}. FT METAL 13 13 Manganese 2. {ECO:0000250}. FT METAL 66 66 Manganese 1. {ECO:0000250}. FT METAL 66 66 Manganese 2. {ECO:0000250}. FT METAL 88 88 Manganese 2. {ECO:0000250}. FT METAL 147 147 Manganese 2. {ECO:0000250}. FT STRAND 2 5 {ECO:0000244|PDB:2EB0}. FT HELIX 12 25 {ECO:0000244|PDB:2EB0}. FT STRAND 27 33 {ECO:0000244|PDB:2EB0}. FT HELIX 37 46 {ECO:0000244|PDB:2EB0}. FT STRAND 61 66 {ECO:0000244|PDB:2EB0}. FT HELIX 70 72 {ECO:0000244|PDB:2EB0}. FT HELIX 77 79 {ECO:0000244|PDB:2EB0}. FT STRAND 80 89 {ECO:0000244|PDB:2EB0}. FT STRAND 100 103 {ECO:0000244|PDB:2EB0}. FT STRAND 105 107 {ECO:0000244|PDB:2EB0}. FT HELIX 109 118 {ECO:0000244|PDB:2EB0}. FT HELIX 122 125 {ECO:0000244|PDB:2EB0}. FT HELIX 134 148 {ECO:0000244|PDB:2EB0}. FT TURN 149 152 {ECO:0000244|PDB:2EB0}. FT HELIX 158 171 {ECO:0000244|PDB:2EB0}. FT HELIX 176 188 {ECO:0000244|PDB:2EB0}. FT HELIX 189 192 {ECO:0000244|PDB:2EB0}. FT HELIX 195 199 {ECO:0000244|PDB:2EB0}. FT STRAND 202 208 {ECO:0000244|PDB:2EB0}. FT STRAND 211 221 {ECO:0000244|PDB:2EB0}. FT HELIX 224 243 {ECO:0000244|PDB:2EB0}. FT STRAND 247 255 {ECO:0000244|PDB:2EB0}. FT TURN 256 259 {ECO:0000244|PDB:2EB0}. FT STRAND 260 267 {ECO:0000244|PDB:2EB0}. FT HELIX 269 275 {ECO:0000244|PDB:2EB0}. FT STRAND 282 287 {ECO:0000244|PDB:2EB0}. FT HELIX 293 296 {ECO:0000244|PDB:2EB0}. FT HELIX 298 305 {ECO:0000244|PDB:2EB0}. SQ SEQUENCE 307 AA; 34113 MW; EF7EDD1610668D9A CRC64; MRYVVGHKNP DTDSIASAIV LAYFLDCYPA RLGDINPETE FVLRKFGVME PELIESAKGK EIILVDHSEK SQSFDDLEEG KLIAIIDHHK VGLTTTEPIL YYAKPVGSTA TVIAELYFKD AIDLIGGKKK ELKPDLAGLL LSAIISDTVL FKSPTTTDLD KEMAKKLAEI AGISNIEEFG MEILKAKSVV GKLKPEEIIN MDFKNFDFNG KKVGIGQVEV IDVSEVESKK EDIYKLLEEK LKNEGYDLIV FLITDIMKEG SEALVVGNKE MFEKAFNVKV EGNSVFLEGV MSRKKQVVPP LERAYNG // ID PRIL_METJA Reviewed; 414 AA. AC Q58112; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=DNA primase large subunit PriL {ECO:0000255|HAMAP-Rule:MF_00701}; GN Name=priL {ECO:0000255|HAMAP-Rule:MF_00701}; OrderedLocusNames=MJ0701; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Regulatory subunit of DNA primase, an RNA polymerase CC that catalyzes the synthesis of short RNA molecules used as CC primers for DNA polymerase during DNA replication. Stabilizes and CC modulates the activity of the small subunit, increasing the rate CC of DNA synthesis, and conferring RNA synthesis capability. The DNA CC polymerase activity may enable DNA primase to also catalyze primer CC extension after primer synthesis. May also play a role in DNA CC repair. {ECO:0000255|HAMAP-Rule:MF_00701}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00701}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00701}; CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00701}. CC -!- SIMILARITY: Belongs to the eukaryotic-type primase large subunit CC family. {ECO:0000255|HAMAP-Rule:MF_00701}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98698.1; -; Genomic_DNA. DR PIR; E64387; E64387. DR ProteinModelPortal; Q58112; -. DR STRING; 243232.MJ_0701; -. DR EnsemblBacteria; AAB98698; AAB98698; MJ_0701. DR KEGG; mja:MJ_0701; -. DR eggNOG; arCOG03013; Archaea. DR eggNOG; COG2219; LUCA. DR InParanoid; Q58112; -. DR KO; K18882; -. DR OMA; HYARRSF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR HAMAP; MF_00701; DNA_primase_lrg_arc; 1. DR InterPro; IPR007238; DNA_primase_lsu_euk/arc. DR InterPro; IPR023642; DNA_primase_lsu_PriL. DR Pfam; PF04104; DNA_primase_lrg; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; DNA replication; KW DNA-directed RNA polymerase; Iron; Iron-sulfur; Metal-binding; KW Nucleotidyltransferase; Primosome; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 414 DNA primase large subunit PriL. FT /FTId=PRO_0000106995. FT METAL 251 251 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00701}. FT METAL 352 352 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00701}. FT METAL 370 370 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00701}. FT METAL 376 376 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00701}. SQ SEQUENCE 414 AA; 49101 MW; B53D6FEEB506CAF1 CRC64; MIIMLSEYLE EFKEYLERFK NIDINFSDVL KMSKKFIIWR LKQIFGDSST IFTNISSEIT IFDKIFQMID YDIDGEVEKR LPKDESRFMI GVRREKEIEI KKEIITNLLD FLLIILLSHT PYFNAFVRKY AEIKKIKVIK KLPNKISVWE FIKIASRSRI NDLHLERLDL ENGFVDITKI KEIFAKEIIR VELMKLGENI KKRKLPDDSV VKELLNEISD YLKDKVKYEQ ISGIKALNYK GNIPLEWHPP CIRGILNDIL SGGSPSHYAR RSFVVYWFCA KFNPNLRPLD KNGNLVNVSA TDIASEEEIE RFIDELIEML FKNVEDFDEK KTRYYIMHNI GYKVGHGRLT HCEYCKNWQD DGGKGLSYYC KPDELCKKKF IIHPLDYLCY NINKHLKKER FKKIKKEDKN GDNK // ID PRIS_METJA Reviewed; 350 AA. AC Q58249; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 94. DE RecName: Full=DNA primase small subunit PriS {ECO:0000255|HAMAP-Rule:MF_00700}; DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_00700}; GN Name=priS {ECO:0000255|HAMAP-Rule:MF_00700}; Synonyms=priA; GN OrderedLocusNames=MJ0839; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=10536154; DOI=10.1093/nar/27.22.4444; RA Desogus G., Onesti S., Brick P., Rossi M., Pisani F.; RT "Identification and characterization of a DNA primase from the RT hyperthermophilic archaeon Methanococcus jannaschii."; RL Nucleic Acids Res. 27:4444-4450(1999). CC -!- FUNCTION: Catalytic subunit of DNA primase, an RNA polymerase that CC catalyzes the synthesis of short RNA molecules used as primers for CC DNA polymerase during DNA replication. The small subunit contains CC the primase catalytic core and has DNA synthesis activity on its CC own. Binding to the large subunit stabilizes and modulates the CC activity, increasing the rate of DNA synthesis while decreasing CC the length of the DNA fragments, and conferring RNA synthesis CC capability. The DNA polymerase activity may enable DNA primase to CC also catalyze primer extension after primer synthesis. May also CC play a role in DNA repair. {ECO:0000255|HAMAP-Rule:MF_00700, CC ECO:0000269|PubMed:10536154}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700, CC ECO:0000269|PubMed:10536154}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00700, CC ECO:0000269|PubMed:10536154}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:10536154}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.06. {ECO:0000269|PubMed:10536154}; CC Temperature dependence: CC Optimum temperature is 60-70 degrees Celsius. CC {ECO:0000269|PubMed:10536154}; CC -!- SUBUNIT: Heterodimer of a small subunit (PriS) and a large subunit CC (PriL). {ECO:0000255|HAMAP-Rule:MF_00700}. CC -!- SIMILARITY: Belongs to the eukaryotic-type primase small subunit CC family. {ECO:0000255|HAMAP-Rule:MF_00700}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98844.1; -; Genomic_DNA. DR ProteinModelPortal; Q58249; -. DR STRING; 243232.MJ_0839; -. DR EnsemblBacteria; AAB98844; AAB98844; MJ_0839. DR KEGG; mja:MJ_0839; -. DR eggNOG; arCOG04110; Archaea. DR eggNOG; COG1467; LUCA. DR InParanoid; Q58249; -. DR KO; K02683; -. DR OMA; IDGDHLD; -. DR PhylomeDB; Q58249; -. DR BRENDA; 2.7.7.B16; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:1990077; C:primosome complex; IEA:UniProtKB-KW. DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR HAMAP; MF_00700; DNA_primase_sml_arc; 1. DR InterPro; IPR002755; DNA_primase_S. DR InterPro; IPR014052; DNA_primase_ssu_euk/arc. DR InterPro; IPR023639; DNA_primase_ssu_PriS. DR PANTHER; PTHR10536; PTHR10536; 1. DR Pfam; PF01896; DNA_primase_S; 1. DR TIGRFAMs; TIGR00335; primase_sml; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA replication; DNA-directed RNA polymerase; KW Magnesium; Manganese; Metal-binding; Nucleotidyltransferase; KW Primosome; Reference proteome; Transcription; Transferase; Zinc. FT CHAIN 1 350 DNA primase small subunit PriS. FT /FTId=PRO_0000046742. FT ACT_SITE 97 97 {ECO:0000255|HAMAP-Rule:MF_00700}. FT ACT_SITE 99 99 {ECO:0000255|HAMAP-Rule:MF_00700}. FT ACT_SITE 251 251 {ECO:0000255|HAMAP-Rule:MF_00700}. SQ SEQUENCE 350 AA; 41802 MW; D308EBA1FB23EEFD CRC64; MNTFAEVQKL YREYYNFAIK NNILEIPEGI EYREFGYGYL KKVDNRNLSF KNEREYKDWV LKNAPMHFYK SLAYMLYPNK SGGASKKGIF RRELAFDIDV HKTKKCKHED DWICKHCLEE AKNQAIYLIE EFLIPDFGLN EEDLKIVFSG NRGYHIYIKP RDEKIRDIIE SYSKEDRRFL MDYILGKNLN LNSVGSGWRR RLIKAIKERD KRISTKKLEN EKNWKKVIEN LKSKNKIYNI IEETKNKIEL DEKVMDDDIR LLRVINSLHG YTGFIVKPLS GLDELRRFNP LEDAIFKDFE NKVYEVNIFD DRKFEIEICG KKYNNKSKKI TASALLYLFG HNIKFELLKS // ID PSTB_METJA Reviewed; 252 AA. AC Q58418; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Phosphate import ATP-binding protein PstB {ECO:0000255|HAMAP-Rule:MF_01702}; DE EC=3.6.3.27 {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=ABC phosphate transporter {ECO:0000255|HAMAP-Rule:MF_01702}; DE AltName: Full=Phosphate-transporting ATPase {ECO:0000255|HAMAP-Rule:MF_01702}; GN Name=pstB {ECO:0000255|HAMAP-Rule:MF_01702}; OrderedLocusNames=MJ1012; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. Responsible for energy coupling to the transport CC system. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + phosphate(Out) = ADP + phosphate CC + phosphate(In). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PstB), two transmembrane proteins (PstC and PstA) and a solute- CC binding protein (PstS). {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01702}; Peripheral membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. Phosphate CC importer (TC 3.A.1.7) family. {ECO:0000255|HAMAP-Rule:MF_01702}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. {ECO:0000255|HAMAP- CC Rule:MF_01702}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99016.1; -; Genomic_DNA. DR PIR; C64426; C64426. DR ProteinModelPortal; Q58418; -. DR STRING; 243232.MJ_1012; -. DR EnsemblBacteria; AAB99016; AAB99016; MJ_1012. DR KEGG; mja:MJ_1012; -. DR eggNOG; arCOG00231; Archaea. DR eggNOG; COG1117; LUCA. DR InParanoid; Q58418; -. DR KO; K02036; -. DR OMA; MTVEPRS; -. DR PhylomeDB; Q58418; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR015850; ABC_transpr_PstB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005670; Phosp_transpt1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00972; 3a0107s01c2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. DR PROSITE; PS51238; PSTB; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Phosphate transport; Reference proteome; KW Transport. FT CHAIN 1 252 Phosphate import ATP-binding protein FT PstB. FT /FTId=PRO_0000092946. FT DOMAIN 6 247 ABC transporter. {ECO:0000255|HAMAP- FT Rule:MF_01702}. FT NP_BIND 38 45 ATP. {ECO:0000255|HAMAP-Rule:MF_01702}. SQ SEQUENCE 252 AA; 28688 MW; CA6F160C5BFEE65B CRC64; MTKVKMETKN LNLWYGEKQA LFDINLPIYE NKITALIGPS GCGKSTFLRC LNRLNDLIPN VRIEGEVLLD GKNIYDKDVD VYELRKRVGM VFQKPNPFAM SIYDNVAFGP RIHGIKDKKE LDKIVEWALK KAALWDEVKD ELHKNALSLS GGQQQRLCIA RAIAVKPEVL LMDEPTSALD PISTLKIEEL MVELAKDYTI VVVTHNMQQA SRVSDYTAFF LMGKLIEFGE TEQIFLNPQK KETDDYISGR FG // ID PSTC_METJA Reviewed; 315 AA. AC Q58420; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Probable phosphate transport system permease protein PstC; GN Name=pstC; OrderedLocusNames=MJ1014; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for phosphate; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99018.1; -; Genomic_DNA. DR PIR; E64426; E64426. DR ProteinModelPortal; Q58420; -. DR STRING; 243232.MJ_1014; -. DR EnsemblBacteria; AAB99018; AAB99018; MJ_1014. DR KEGG; mja:MJ_1014; -. DR eggNOG; arCOG00167; Archaea. DR eggNOG; COG0573; LUCA. DR InParanoid; Q58420; -. DR KO; K02037; -. DR OMA; TAIFITE; -. DR PhylomeDB; Q58420; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GOC. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR011864; Phosphate_PstC. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR02138; phosphate_pstC; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 315 Probable phosphate transport system FT permease protein PstC. FT /FTId=PRO_0000060220. FT TRANSMEM 18 38 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 80 100 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 119 139 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 167 187 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 227 247 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 283 303 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 76 302 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 315 AA; 35263 MW; 6003F4F6B8B68477 CRC64; MKTMEIKKLL RKIDEFKIIT LPAIFVVFIL FVLILGFYFF NALPAIERYG IDLFITNVWK AAEEPAKEVY GLAAPIWGSI YTATIAVLIA LPLSICYAIF VNDYAPKRLK YPLIVISDIM AGLPTIIYGI WGAFILVPLL RDHIMKFLYE HFSFIPLFDY PPLSGYCYLS AGILLGIMVT PFAAAIIREA YAMIPSVYKE GLVALGATRY ETTKVLIKYI RPAIISGLIL AFGRALGETV AVSLVIGNSF NLTYKLFAPG YTISSLIANQ FGNAVLYEYM TSVLYSAGLV LFVIGLVVNI IGIYYLKRWR EHVSH // ID PRNK_METJA Reviewed; 361 AA. AC Q58711; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=Polyribonucleotide 5'-hydroxyl-kinase MJ1315; DE EC=2.7.1.78; DE AltName: Full=Polynucleotide kinase MJ1315; GN OrderedLocusNames=MJ1315; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Polynucleotide kinase that can phosphorylate the 5'- CC hydroxyl groups of both single-stranded RNA (ssRNA) and single- CC stranded DNA (ssDNA). Exhibits a strong preference for ssRNA (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + 5'-dephospho-DNA = ADP + 5'-phospho-DNA. CC -!- CATALYTIC ACTIVITY: ATP + 5'-dephospho-RNA = ADP + 5'-phospho-RNA. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99322.1; -; Genomic_DNA. DR PIR; B64464; B64464. DR ProteinModelPortal; Q58711; -. DR STRING; 243232.MJ_1315; -. DR PRIDE; Q58711; -. DR DNASU; 1452217; -. DR EnsemblBacteria; AAB99322; AAB99322; MJ_1315. DR KEGG; mja:MJ_1315; -. DR eggNOG; arCOG04127; Archaea. DR eggNOG; COG1341; LUCA. DR InParanoid; Q58711; -. DR KO; K06947; -. DR OMA; RKIHREM; -. DR PhylomeDB; Q58711; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046404; F:ATP-dependent polydeoxyribonucleotide 5'-hydroxyl-kinase activity; IEA:UniProtKB-EC. DR GO; GO:0051731; F:polynucleotide 5'-hydroxyl-kinase activity; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR032319; CLP1_P. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF16575; CLP1_P; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Nucleotide-binding; KW Reference proteome; Transferase. FT CHAIN 1 361 Polyribonucleotide 5'-hydroxyl-kinase FT MJ1315. FT /FTId=PRO_0000107272. FT NP_BIND 39 46 ATP. {ECO:0000255}. SQ SEQUENCE 361 AA; 41352 MW; E2397969BE7E8870 CRC64; MVDNMISKAY YTTEIPEDRF EALSCIKDSQ KPLKIILLGG VDSGKTTLAT FLANELLNLG FKVAIVDSDV GQKSILPPAT ISLAFPETNF NNLYEIKPYK SYFVGSTAPI QFFGEMITGT KLLCDYAEDK ADIIIVDTTG LISGSGADLK RMKIEMIKPD IIIALEKRNE LKSILKPFEN KIRVFYLKVY ENAKSFSREE RKEIRAEKWK EYFKNSKIYN IGFNDVVIGG TKVFQGEKIL EDEKYLLESL FKWKILYGSK CDGRYTIVKR DLVNMPRQID KNILYYIEPE RFNNLIVGLI DEDSFCIGLG ILKTIDFENE TLEILTPISE EDIKNIREIR FGRIRVDENG EELGLLDRDS I // ID PRS2_METJA Reviewed; 371 AA. AC Q58889; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 84. DE RecName: Full=Putative 26S protease regulatory subunit homolog MJ1494; GN OrderedLocusNames=MJ1494; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: The 26S protease is involved in the ATP-dependent CC degradation of ubiquitinated proteins. The regulatory (or ATPase) CC complex confers ATP dependency and substrate specificity to the CC 26S complex (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AAA ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99505.1; -; Genomic_DNA. DR ProteinModelPortal; Q58889; -. DR STRING; 243232.MJ_1494; -. DR EnsemblBacteria; AAB99505; AAB99505; MJ_1494. DR KEGG; mja:MJ_1494; -. DR eggNOG; arCOG04163; Archaea. DR eggNOG; COG1223; LUCA. DR InParanoid; Q58889; -. DR KO; K07392; -. DR OMA; FGEWAPK; -. DR PhylomeDB; Q58889; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0031597; C:cytosolic proteasome complex; IBA:GO_Central. DR GO; GO:0008540; C:proteasome regulatory particle, base subcomplex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0036402; F:proteasome-activating ATPase activity; IBA:GO_Central. DR GO; GO:0017025; F:TBP-class protein binding; IBA:GO_Central. DR GO; GO:0030433; P:ER-associated ubiquitin-dependent protein catabolic process; IBA:GO_Central. DR GO; GO:1901800; P:positive regulation of proteasomal protein catabolic process; IBA:GOC. DR GO; GO:0045899; P:positive regulation of RNA polymerase II transcriptional preinitiation complex assembly; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00674; AAA; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; Proteasome; KW Reference proteome. FT CHAIN 1 371 Putative 26S protease regulatory subunit FT homolog MJ1494. FT /FTId=PRO_0000084754. FT NP_BIND 161 168 ATP. {ECO:0000255}. SQ SEQUENCE 371 AA; 42167 MW; 01903F231167E85E CRC64; MSKIGFNPIK IKSFSKIKTY DDTLPSLKYV VLEPAGFPIR VSSENVKVST DDPILFNIYA RDQWIGEIVK EGDYLFDNSI LPDYAFKVIS TYPKEGGMIT SETVFKLQTP KKVLRTQFKK AKFSEIIGQE EAKKKCRIIM KYLENPKLFG EWAPKNVLFY GPPGTGKTLM ARALATETNS SFILVKAPEL IGEHVGDASK MIRELYQRAS ESAPCIVFID ELDAIGLSRE YQSLRGDVSE VVNALLTELD GIKENEGVVT IAATNNPAML DPAIRSRFEE EIEFKLPNDE ERLKIMELYA KKMPLPVKAN LKEFVEKTKG FSGRDIKEKF LKPALHRAIL EDRDYVSKED LEWALKKILG NRREAPQHLY L // ID PSTA_METJA Reviewed; 281 AA. AC Q58419; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Probable phosphate transport system permease protein PstA; GN Name=pstA; OrderedLocusNames=MJ1013; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the binding-protein-dependent transport system CC for phosphate; probably responsible for the translocation of the CC substrate across the membrane. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99017.1; -; Genomic_DNA. DR PIR; D64426; D64426. DR ProteinModelPortal; Q58419; -. DR STRING; 243232.MJ_1013; -. DR EnsemblBacteria; AAB99017; AAB99017; MJ_1013. DR KEGG; mja:MJ_1013; -. DR eggNOG; arCOG00168; Archaea. DR eggNOG; COG0581; LUCA. DR InParanoid; Q58419; -. DR KO; K02038; -. DR OMA; TNPLEPV; -. DR PhylomeDB; Q58419; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IEA:InterPro. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR InterPro; IPR005672; Phosphate_PstA. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR TIGRFAMs; TIGR00974; 3a0107s02c; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 281 Probable phosphate transport system FT permease protein PstA. FT /FTId=PRO_0000060206. FT TRANSMEM 16 36 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 68 88 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 107 127 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 128 148 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 194 214 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 251 271 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 68 271 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 281 AA; 30249 MW; A807ECBD406DD45E CRC64; MSPIKHKTIR MIKDKIFLFI VGALTLLAIL PLFHIIISIV EKGLPIIMER GLTFITGTLS EGGIGPAIVG TLMLTFLATL IGLPLAFLAG AYAYEFPNSF IGRATKMLLQ IMLEFPTILV GTFVMGMLVV PMGTFSALAG ALALALILTP YVAVYTEEAM AEVPKIYKEG GYALGCTRAQ VIFKVITKMA KKGILTGILI GMAKVAGETA PLLFTAGGLY EVYPTNPLEP VGAIPLLIYT LVQSPSIEDH QMAWGAALVM LIIFLAIFVP IRYALKDDIK L // ID PSTK_METJA Reviewed; 248 AA. AC Q58933; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2007, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=L-seryl-tRNA(Sec) kinase; DE EC=2.7.1.164; DE AltName: Full=O-phosphoseryl-tRNA(Sec) kinase; DE Short=PSTK; GN Name=pstK; OrderedLocusNames=MJ1538; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=16201757; DOI=10.1021/bi051110r; RA Kaiser J.T., Gromadski K., Rother M., Engelhardt H., Rodnina M.V., RA Wahl M.C.; RT "Structural and functional investigation of a putative archaeal RT selenocysteine synthase."; RL Biochemistry 44:13315-13327(2005). CC -!- FUNCTION: Specifically phosphorylates seryl-tRNA(Sec) to O- CC phosphoseryl-tRNA(Sec), an activated intermediate for CC selenocysteine biosynthesis. {ECO:0000269|PubMed:16201757}. CC -!- CATALYTIC ACTIVITY: ATP + L-seryl-tRNA(Sec) = ADP + O-phospho-L- CC seryl-tRNA(Sec). CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) CC (archaeal/eukaryal route): step 1/2. CC -!- SIMILARITY: Belongs to the L-seryl-tRNA(Sec) kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99557.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99557.1; ALT_INIT; Genomic_DNA. DR PIR; A64492; A64492. DR PDB; 3A4L; X-ray; 1.80 A; A/B=1-248. DR PDB; 3A4M; X-ray; 1.79 A; A/B=1-248. DR PDB; 3A4N; X-ray; 2.50 A; A/B=1-248. DR PDB; 3ADB; X-ray; 2.80 A; A/B=1-248. DR PDB; 3ADC; X-ray; 2.90 A; A/B=1-248. DR PDB; 3ADD; X-ray; 2.40 A; A/B=1-248. DR PDB; 3AM1; X-ray; 2.40 A; A=1-248. DR PDBsum; 3A4L; -. DR PDBsum; 3A4M; -. DR PDBsum; 3A4N; -. DR PDBsum; 3ADB; -. DR PDBsum; 3ADC; -. DR PDBsum; 3ADD; -. DR PDBsum; 3AM1; -. DR ProteinModelPortal; Q58933; -. DR DIP; DIP-48971N; -. DR STRING; 243232.MJ_1538; -. DR EnsemblBacteria; AAB99557; AAB99557; MJ_1538. DR KEGG; mja:MJ_1538; -. DR eggNOG; arCOG01041; Archaea. DR eggNOG; COG4088; LUCA. DR InParanoid; Q58933; -. DR KO; K10837; -. DR OMA; YNSKRRD; -. DR BioCyc; MetaCyc:MONOMER-14956; -. DR BRENDA; 2.7.1.164; 3260. DR UniPathway; UPA00906; UER00897. DR EvolutionaryTrace; Q58933; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW. DR GO; GO:0016773; F:phosphotransferase activity, alcohol group as acceptor; IEA:InterPro. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR013641; KTI12/PSTK. DR InterPro; IPR020024; L-seryl-tRNA_Sec_kinase_arc. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF08433; KTI12; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03574; selen_PSTK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Kinase; KW Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 248 L-seryl-tRNA(Sec) kinase. FT /FTId=PRO_0000107396. FT NP_BIND 7 14 ATP. {ECO:0000255}. FT STRAND 1 6 {ECO:0000244|PDB:3A4M}. FT HELIX 13 26 {ECO:0000244|PDB:3A4M}. FT STRAND 31 34 {ECO:0000244|PDB:3A4M}. FT HELIX 37 40 {ECO:0000244|PDB:3A4M}. FT STRAND 43 45 {ECO:0000244|PDB:3A4M}. FT HELIX 48 50 {ECO:0000244|PDB:3A4M}. FT HELIX 51 66 {ECO:0000244|PDB:3A4M}. FT STRAND 69 73 {ECO:0000244|PDB:3A4M}. FT HELIX 80 92 {ECO:0000244|PDB:3A4M}. FT STRAND 96 103 {ECO:0000244|PDB:3A4M}. FT HELIX 106 115 {ECO:0000244|PDB:3A4M}. FT HELIX 122 131 {ECO:0000244|PDB:3A4M}. FT HELIX 140 142 {ECO:0000244|PDB:3A4M}. FT STRAND 145 149 {ECO:0000244|PDB:3A4M}. FT HELIX 156 167 {ECO:0000244|PDB:3A4M}. FT STRAND 172 174 {ECO:0000244|PDB:3ADD}. FT HELIX 186 205 {ECO:0000244|PDB:3A4M}. FT HELIX 209 227 {ECO:0000244|PDB:3A4M}. FT STRAND 229 231 {ECO:0000244|PDB:3ADC}. FT HELIX 234 247 {ECO:0000244|PDB:3A4M}. SQ SEQUENCE 248 AA; 29467 MW; 815EF9A453BEA450 CRC64; MLIILTGLPG VGKSTFSKNL AKILSKNNID VIVLGSDLIR ESFPVWKEKY EEFIKKSTYR LIDSALKNYW VIVDDTNYYN SMRRDLINIA KKYNKNYAII YLKASLDVLI RRNIERGEKI PNEVIKKMYE KFDEPGKKYK WDEPFLIIDT TKDIDFNEIA KKLIEKSKEI PKFYVLEENK NKNNNISDKI DKETRKIVSE YIKSKKLDKD KIKEVVELRK EFLKKIKKME EVDADRVLKE FKDLLNSY // ID PSA_METJA Reviewed; 261 AA. AC Q60177; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Proteasome subunit alpha {ECO:0000255|HAMAP-Rule:MF_00289}; DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_00289}; DE AltName: Full=20S proteasome alpha subunit {ECO:0000255|HAMAP-Rule:MF_00289}; DE AltName: Full=Proteasome core protein PsmA {ECO:0000255|HAMAP-Rule:MF_00289}; GN Name=psmA {ECO:0000255|HAMAP-Rule:MF_00289}; OrderedLocusNames=MJ0591; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH PAN. RX PubMed=10692374; DOI=10.1128/JB.182.6.1680-1692.2000; RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.; RT "Biochemical and physical properties of the Methanococcus jannaschii RT 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the RT eucaryal 26S proteasome."; RL J. Bacteriol. 182:1680-1692(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH BETA SUBUNIT, RP GATED STRUCTURE, AND SUBUNIT. RX PubMed=19481527; DOI=10.1016/j.molcel.2009.04.021; RA Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.; RT "Structural insights into the regulatory particle of the proteasome RT from Methanocaldococcus jannaschii."; RL Mol. Cell 34:473-484(2009). CC -!- FUNCTION: Component of the proteasome core, a large protease CC complex with broad specificity involved in protein degradation. CC The M.jannaschii proteasome is able to cleave oligopeptides after CC Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. CC Thus, displays caspase-like and chymotrypsin-like activities and CC low level of trypsin-like activity. {ECO:0000255|HAMAP- CC Rule:MF_00289, ECO:0000269|PubMed:10692374}. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000255|HAMAP-Rule:MF_00289, CC ECO:0000269|PubMed:10692374}. CC -!- ENZYME REGULATION: The formation of the proteasomal ATPase PAN-20S CC proteasome complex, via the docking of the C-termini of PAN into CC the intersubunit pockets in the alpha-rings, triggers opening of CC the gate for substrate entry. Interconversion between the open- CC gate and close-gate conformations leads to a dynamic regulation of CC the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP- CC Rule:MF_00289}. CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 CC beta subunits that assemble into four stacked heptameric rings, CC resulting in a barrel-shaped structure. The two inner rings, each CC composed of seven catalytic beta subunits, are sandwiched by two CC outer rings, each composed of seven alpha subunits. The catalytic CC chamber with the active sites is on the inside of the barrel. Has CC a gated structure, the ends of the cylinder being occluded by the CC N-termini of the alpha-subunits. Is capped at one or both ends by CC the proteasome regulatory ATPase, PAN. {ECO:0000255|HAMAP- CC Rule:MF_00289, ECO:0000269|PubMed:10692374, CC ECO:0000269|PubMed:19481527}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00289}. CC -!- SIMILARITY: Belongs to the peptidase T1A family. CC {ECO:0000255|HAMAP-Rule:MF_00289}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98581.1; -; Genomic_DNA. DR PIR; G64373; G64373. DR PDB; 3H4P; X-ray; 4.10 A; A/B/C/D/E/F/G/H/I/J/K/L/M/N=1-261. DR PDBsum; 3H4P; -. DR ProteinModelPortal; Q60177; -. DR SMR; Q60177; 5-247. DR STRING; 243232.MJ_0591; -. DR EnsemblBacteria; AAB98581; AAB98581; MJ_0591. DR KEGG; mja:MJ_0591; -. DR eggNOG; arCOG00971; Archaea. DR eggNOG; COG0638; LUCA. DR InParanoid; Q60177; -. DR KO; K03432; -. DR OMA; EKNYKYD; -. DR PhylomeDB; Q60177; -. DR EvolutionaryTrace; Q60177; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019773; C:proteasome core complex, alpha-subunit complex; IDA:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB. DR GO; GO:0006511; P:ubiquitin-dependent protein catabolic process; IEA:InterPro. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_00289_A; Proteasome_A_A; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR019982; Proteasome_asu_arc. DR InterPro; IPR000426; Proteasome_asu_N. DR InterPro; IPR023332; Proteasome_suA-type. DR InterPro; IPR001353; Proteasome_sua/b. DR Pfam; PF00227; Proteasome; 1. DR Pfam; PF10584; Proteasome_A_N; 1. DR SMART; SM00948; Proteasome_A_N; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03633; arc_protsome_A; 1. DR PROSITE; PS00388; PROTEASOME_ALPHA_1; 1. DR PROSITE; PS51475; PROTEASOME_ALPHA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Hydrolase; Protease; KW Proteasome; Reference proteome; Threonine protease. FT CHAIN 1 261 Proteasome subunit alpha. FT /FTId=PRO_0000124174. FT HELIX 23 33 FT STRAND 48 52 FT TURN 62 64 FT STRAND 68 72 FT STRAND 75 80 FT HELIX 84 90 FT HELIX 93 102 FT HELIX 110 123 FT STRAND 136 140 FT STRAND 149 152 FT STRAND 159 163 FT TURN 171 176 FT HELIX 177 180 FT HELIX 192 201 FT STRAND 202 204 FT STRAND 209 216 FT TURN 217 220 FT STRAND 221 224 FT TURN 227 230 FT HELIX 231 233 FT TURN 234 239 FT STRAND 240 242 SQ SEQUENCE 261 AA; 29321 MW; 93FC7DF277E01AD8 CRC64; MQMVPPSAYD RAITVFSPEG RLYQVEYARE AVRRGTTAIG IACKDGVVLA VDRRITSKLV KIRSIEKIFQ IDDHVAAATS GLVADARVLI DRARLEAQIY RLTYGEEISI EMLAKKICDI KQAYTQHGGV RPFGVSLLIA GIDKNEARLF ETDPSGALIE YKATAIGSGR PVVMELLEKE YRDDITLDEG LELAITALTK ANEDIKPENV DVCIITVKDA QFKKIPVEEI KKLIEKVKKK LNEENKKEEE NREETKEKQE E // ID PURA_METJA Reviewed; 345 AA. AC Q57981; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=Adenylosuccinate synthetase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AMPSase {ECO:0000255|HAMAP-Rule:MF_00011}; DE Short=AdSS {ECO:0000255|HAMAP-Rule:MF_00011}; DE EC=6.3.4.4 {ECO:0000255|HAMAP-Rule:MF_00011}; DE AltName: Full=IMP--aspartate ligase {ECO:0000255|HAMAP-Rule:MF_00011}; GN Name=purA {ECO:0000255|HAMAP-Rule:MF_00011}; OrderedLocusNames=MJ0561; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Plays an important role in the de novo pathway of purine CC nucleotide biosynthesis. Catalyzes the first committed step in the CC biosynthesis of AMP from IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- CATALYTIC ACTIVITY: GTP + IMP + L-aspartate = GDP + phosphate + CC N(6)-(1,2-dicarboxyethyl)-AMP. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00011}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00011}; CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00011}. CC -!- SIMILARITY: Belongs to the adenylosuccinate synthetase family. CC {ECO:0000255|HAMAP-Rule:MF_00011}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98554.1; -; Genomic_DNA. DR PIR; A64370; A64370. DR ProteinModelPortal; Q57981; -. DR SMR; Q57981; 11-343. DR STRING; 243232.MJ_0561; -. DR EnsemblBacteria; AAB98554; AAB98554; MJ_0561. DR KEGG; mja:MJ_0561; -. DR eggNOG; arCOG04387; Archaea. DR eggNOG; COG0104; LUCA. DR InParanoid; Q57981; -. DR KO; K01939; -. DR OMA; ILPLHRE; -. DR PhylomeDB; Q57981; -. DR BRENDA; 6.3.4.4; 3260. DR UniPathway; UPA00075; UER00335. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004019; F:adenylosuccinate synthase activity; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046040; P:IMP metabolic process; IBA:GO_Central. DR HAMAP; MF_00011; Adenylosucc_synth; 1. DR InterPro; IPR018220; Adenylosuccin_syn_GTP-bd. DR InterPro; IPR001114; Adenylosuccinate_synthetase. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11846; PTHR11846; 1. DR Pfam; PF00709; Adenylsucc_synt; 2. DR SMART; SM00788; Adenylsucc_synt; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS01266; ADENYLOSUCCIN_SYN_1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 345 Adenylosuccinate synthetase. FT /FTId=PRO_0000095271. FT NP_BIND 18 24 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 48 50 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 290 292 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT NP_BIND 330 332 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT REGION 19 22 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 46 49 IMP binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT REGION 258 264 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 19 19 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT ACT_SITE 49 49 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 19 19 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00011}. FT METAL 48 48 Magnesium; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 133 133 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 147 147 IMP; shared with dimeric partner. FT {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 185 185 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 200 200 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 262 262 IMP. {ECO:0000255|HAMAP-Rule:MF_00011}. FT BINDING 264 264 GTP. {ECO:0000255|HAMAP-Rule:MF_00011}. SQ SEQUENCE 345 AA; 37820 MW; 9974DBC30D1DEE72 CRC64; MKKVVLLTCT IIVGGQWGDE GKGKIISYIC DKDKPSIIAR GGVGPNAGHT VNIGGKSYGI RMIPTGFPYK EAKLAIGAGV LVDPEVLLKE VEMLKDFNVK ERLIVDYRCG IIEEKHKIMD RKDEHLAKEI GTTGSGCGPA NVDRVLRILK QAKDIEELKE FLGDVSEEVN NALDRGENVL IEGTQGTLLS LYYGTYPYVT SKDTTASSFA ADVGIGPTKV DEVIVVFKTF PTRVGAGPFP TEMSLEEAES LGIVEYGTVT GRRRRVGYFD FELARKACRL NGATQIALTG LDKYDKECYG VTEYNKLSEK AKEFINKIEE VTGVPVTIIS TGPEMHQTID LRNEL // ID PSLS_METJA Reviewed; 251 AA. AC Q57703; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Phosphosulfolactate synthase; DE EC=4.4.1.19; DE AltName: Full=(2R)-phospho-3-sulfolactate synthase; DE Short=PSL synthase; GN Name=comA; OrderedLocusNames=MJ0255; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION, AND MUTAGENESIS OF LYS-137. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11830598; DOI=10.1074/jbc.M201011200; RA Graham D.E., Xu H., White R.H.; RT "Identification of coenzyme M biosynthetic phosphosulfolactate RT synthase: a new family of sulfonate-biosynthesizing enzymes."; RL J. Biol. Chem. 277:13421-13429(2002). CC -!- FUNCTION: Catalyzes the addition of sulfite to phosphoenolpyruvate CC (PEP) to yield (2R)-phospho-3-sulfolactate (PSL). CC -!- CATALYTIC ACTIVITY: (2R)-2-O-phospho-3-sulfolactate = CC phosphoenolpyruvate + hydrogen sulfite. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5.; CC -!- PATHWAY: Cofactor biosynthesis; coenzyme M biosynthesis; CC sulfoacetaldehyde from phosphoenolpyruvate and sulfite: step 1/4. CC -!- SUBUNIT: Homotrimer. {ECO:0000305}. CC -!- MISCELLANEOUS: The enzyme is stereospecific. CC -!- SIMILARITY: Belongs to the phosphosulfolactate synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98242.1; -; Genomic_DNA. DR PIR; H64331; H64331. DR PDB; 1QWG; X-ray; 1.60 A; A=1-251. DR PDBsum; 1QWG; -. DR ProteinModelPortal; Q57703; -. DR SMR; Q57703; 1-251. DR STRING; 243232.MJ_0255; -. DR EnsemblBacteria; AAB98242; AAB98242; MJ_0255. DR KEGG; mja:MJ_0255; -. DR eggNOG; arCOG04896; Archaea. DR eggNOG; COG1809; LUCA. DR InParanoid; Q57703; -. DR KO; K08097; -. DR OMA; IIWEAPQ; -. DR BioCyc; MetaCyc:MONOMER-2262; -. DR SABIO-RK; Q57703; -. DR UniPathway; UPA00355; UER00469. DR EvolutionaryTrace; Q57703; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043817; F:phosphosulfolactate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0050545; F:sulfopyruvate decarboxylase activity; IDA:MENGO. DR GO; GO:0019295; P:coenzyme M biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR022370; Arch_ComA. DR InterPro; IPR003830; ComA_synth. DR Pfam; PF02679; ComA; 1. DR SUPFAM; SSF102110; SSF102110; 1. DR TIGRFAMs; TIGR03849; arch_ComA; 1. PE 1: Evidence at protein level; KW 3D-structure; Coenzyme M biosynthesis; Complete proteome; Lyase; KW Reference proteome. FT CHAIN 1 251 Phosphosulfolactate synthase. FT /FTId=PRO_0000080830. FT MUTAGEN 137 137 K->N: Loss of function. FT {ECO:0000269|PubMed:11830598}. FT HELIX 5 7 {ECO:0000244|PDB:1QWG}. FT STRAND 16 22 {ECO:0000244|PDB:1QWG}. FT HELIX 25 35 {ECO:0000244|PDB:1QWG}. FT HELIX 36 38 {ECO:0000244|PDB:1QWG}. FT STRAND 40 44 {ECO:0000244|PDB:1QWG}. FT HELIX 48 51 {ECO:0000244|PDB:1QWG}. FT HELIX 54 65 {ECO:0000244|PDB:1QWG}. FT TURN 66 68 {ECO:0000244|PDB:1QWG}. FT STRAND 70 73 {ECO:0000244|PDB:1QWG}. FT HELIX 75 83 {ECO:0000244|PDB:1QWG}. FT HELIX 87 97 {ECO:0000244|PDB:1QWG}. FT STRAND 101 104 {ECO:0000244|PDB:1QWG}. FT STRAND 107 109 {ECO:0000244|PDB:1QWG}. FT HELIX 113 125 {ECO:0000244|PDB:1QWG}. FT STRAND 129 134 {ECO:0000244|PDB:1QWG}. FT HELIX 139 142 {ECO:0000244|PDB:1QWG}. FT HELIX 147 160 {ECO:0000244|PDB:1QWG}. FT STRAND 163 167 {ECO:0000244|PDB:1QWG}. FT TURN 170 172 {ECO:0000244|PDB:1QWG}. FT HELIX 187 194 {ECO:0000244|PDB:1QWG}. FT HELIX 199 201 {ECO:0000244|PDB:1QWG}. FT STRAND 202 205 {ECO:0000244|PDB:1QWG}. FT HELIX 209 219 {ECO:0000244|PDB:1QWG}. FT STRAND 225 229 {ECO:0000244|PDB:1QWG}. FT HELIX 230 232 {ECO:0000244|PDB:1QWG}. FT HELIX 233 241 {ECO:0000244|PDB:1QWG}. FT HELIX 245 247 {ECO:0000244|PDB:1QWG}. FT TURN 248 250 {ECO:0000244|PDB:1QWG}. SQ SEQUENCE 251 AA; 28368 MW; 9B3F2CD349880E4C CRC64; MKAFEFLYED FQRGLTVVLD KGLPPKFVED YLKVCGDYID FVKFGWGTSA VIDRDVVKEK INYYKDWGIK VYPGGTLFEY AYSKGKFDEF LNECEKLGFE AVEISDGSSD ISLEERKNAI KRAKDNGFMV LTEVGKKMPD KDKQLTIDDR IKLINFDLDA GADYVIIEGR ESGKGIGLFD KEGKVKENEL DVLAKNVDIN KVIFEAPQKS QQVAFILKFG SSVNLANIAF DEVISLETLR RGLRGDTFGK V // ID PSTS_METJA Reviewed; 389 AA. AC Q58421; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Phosphate-binding protein PstS; DE Short=PBP; GN Name=pstS; OrderedLocusNames=MJ1015; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the ABC transporter complex PstSACB involved in CC phosphate import. {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (PstB), two transmembrane proteins (PstC and PstA) and a solute- CC binding protein (PstS). {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the PstS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99019.1; -; Genomic_DNA. DR PIR; F64426; F64426. DR ProteinModelPortal; Q58421; -. DR STRING; 243232.MJ_1015; -. DR EnsemblBacteria; AAB99019; AAB99019; MJ_1015. DR KEGG; mja:MJ_1015; -. DR eggNOG; arCOG00213; Archaea. DR eggNOG; COG0226; LUCA. DR InParanoid; Q58421; -. DR KO; K02040; -. DR OMA; KNAMAEW; -. DR PhylomeDB; Q58421; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042301; F:phosphate ion binding; IBA:GO_Central. DR GO; GO:0015415; F:phosphate ion transmembrane-transporting ATPase activity; IBA:GO_Central. DR GO; GO:0016036; P:cellular response to phosphate starvation; IBA:GO_Central. DR GO; GO:0006817; P:phosphate ion transport; IBA:GO_Central. DR InterPro; IPR005673; ABC_phos-bd_PstS. DR InterPro; IPR024370; PBP_domain. DR Pfam; PF12849; PBP_like_2; 1. DR PIRSF; PIRSF002756; PstS; 1. DR TIGRFAMs; TIGR00975; 3a0107s03; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 389 Phosphate-binding protein PstS. FT /FTId=PRO_0000062778. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT REGION 59 61 Phosphate binding. FT {ECO:0000250|UniProtKB:P9WGT7}. FT REGION 197 199 Phosphate binding. FT {ECO:0000250|UniProtKB:P9WGT7}. FT BINDING 89 89 Phosphate. FT {ECO:0000250|UniProtKB:P9WGT7}. FT BINDING 107 107 Phosphate. FT {ECO:0000250|UniProtKB:P9WGT7}. SQ SEQUENCE 389 AA; 42414 MW; 48B54C6A953ADAC9 CRC64; MNDTTQPTKG DAVKKILALI LGLCLIVPVI SIAGCVGGGN SQPSNNEKPS TIIIRTTGAT FPKYQIQKWI EDYQKTHPNV KIEYEGGGSG YGQEAFAKGL TDIGRTDPPV KESMWKKFLS TGDQPLQFPE IVGAVVVTYN IPEIGDKTLK LSRDVLADIF LGKIEYWDDE RIKKINPEIA DKLPHEKIIV VHRSDASGTT AIFTTYLSLI SKEWAEKVGA GKTVNWPTDN IGRGVAGKGN PGVVAIVKST PYTVAYTELS YAIEQKLPVA ALENKNGKFV KPTDETIKAA VSAVKASIPN PTEGYKEDLK QMLDAPGDNA YPIVAFTHLL VWENKNGKHY SPEKAKAIKD FLTWVLTEGQ KPEHLAPGYV GLPEDVAKIG LNAVNMIKE // ID PTH_METJA Reviewed; 115 AA. AC Q60363; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00628}; DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00628}; DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00628}; GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00628}; Synonyms=pth2; GN OrderedLocusNames=MJ0051; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PARTIAL PROTEIN SEQUENCE, FUNCTION, AND CHARACTERIZATION. RX PubMed=12475929; DOI=10.1073/pnas.222659199; RA Rosas-Sandoval G., Ambrogelly A., Rinehart J., Wei D., Cruz-Vera L.R., RA Graham D.E., Stetter K.O., Guarneros G., Soell D.; RT "Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA RT hydrolase are nonessential in yeast."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16707-16712(2002). CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl- CC tRNAs which drop off the ribosome during protein synthesis. CC {ECO:0000255|HAMAP-Rule:MF_00628, ECO:0000269|PubMed:12475929}. CC -!- CATALYTIC ACTIVITY: N-substituted aminoacyl-tRNA + H(2)O = N- CC substituted amino acid + tRNA. {ECO:0000255|HAMAP-Rule:MF_00628}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP- CC Rule:MF_00628}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98032.1; -; Genomic_DNA. DR PIR; C64306; C64306. DR PDB; 2ZV3; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I=1-115. DR PDBsum; 2ZV3; -. DR ProteinModelPortal; Q60363; -. DR STRING; 243232.MJ_0051; -. DR EnsemblBacteria; AAB98032; AAB98032; MJ_0051. DR KEGG; mja:MJ_0051; -. DR eggNOG; arCOG04228; Archaea. DR eggNOG; COG1990; LUCA. DR InParanoid; Q60363; -. DR KO; K04794; -. DR OMA; QVAHGAV; -. DR PhylomeDB; Q60363; -. DR EvolutionaryTrace; Q60363; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1490.10; -; 1. DR HAMAP; MF_00628; Pept_tRNA_hydro_arch; 1. DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom. DR InterPro; IPR002833; PTH2. DR Pfam; PF01981; PTH2; 1. DR SUPFAM; SSF102462; SSF102462; 1. DR TIGRFAMs; TIGR00283; arch_pth2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing; KW Hydrolase; Reference proteome. FT CHAIN 1 115 Peptidyl-tRNA hydrolase. FT /FTId=PRO_0000120292. FT STRAND 2 11 {ECO:0000244|PDB:2ZV3}. FT HELIX 15 36 {ECO:0000244|PDB:2ZV3}. FT HELIX 38 46 {ECO:0000244|PDB:2ZV3}. FT STRAND 51 58 {ECO:0000244|PDB:2ZV3}. FT HELIX 59 72 {ECO:0000244|PDB:2ZV3}. FT STRAND 76 81 {ECO:0000244|PDB:2ZV3}. FT STRAND 91 100 {ECO:0000244|PDB:2ZV3}. FT HELIX 102 109 {ECO:0000244|PDB:2ZV3}. SQ SEQUENCE 115 AA; 12670 MW; FFBC33D185B4A8A2 CRC64; MKMVVVIRND LGMGKGKMVA QGGHAIIEAF LDAKRKNPRA VDEWLREGQK KVVVKVNSEK ELIDIYNKAR SEGLPCSIIR DAGHTQLEPG TLTAVAIGPE KDEKIDKITG HLKLL // ID PUR1_METJA Reviewed; 471 AA. AC Q57657; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 11-NOV-2015, entry version 113. DE RecName: Full=Amidophosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=ATase {ECO:0000255|HAMAP-Rule:MF_01931}; DE EC=2.4.2.14 {ECO:0000255|HAMAP-Rule:MF_01931}; DE AltName: Full=Glutamine phosphoribosylpyrophosphate amidotransferase {ECO:0000255|HAMAP-Rule:MF_01931}; DE Short=GPATase {ECO:0000255|HAMAP-Rule:MF_01931}; GN Name=purF {ECO:0000255|HAMAP-Rule:MF_01931}; OrderedLocusNames=MJ0204; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the formation of phosphoribosylamine from CC phosphoribosylpyrophosphate (PRPP) and glutamine. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- CATALYTIC ACTIVITY: 5-phospho-beta-D-ribosylamine + diphosphate + CC L-glutamate = L-glutamine + 5-phospho-alpha-D-ribose 1-diphosphate CC + H(2)O. {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01931}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01931}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01931}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 1/2. {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: In the C-terminal section; belongs to the CC purine/pyrimidine phosphoribosyltransferase family. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|HAMAP-Rule:MF_01931}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98188.1; -; Genomic_DNA. DR PIR; E64325; E64325. DR ProteinModelPortal; Q57657; -. DR STRING; 243232.MJ_0204; -. DR MEROPS; C44.001; -. DR EnsemblBacteria; AAB98188; AAB98188; MJ_0204. DR KEGG; mja:MJ_0204; -. DR eggNOG; arCOG00093; Archaea. DR eggNOG; COG0034; LUCA. DR InParanoid; Q57657; -. DR KO; K00764; -. DR OMA; IRHFGVK; -. DR PhylomeDB; Q57657; -. DR UniPathway; UPA00074; UER00124. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004044; F:amidophosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_01931; PurF; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR005854; PurF. DR Pfam; PF13537; GATase_7; 1. DR Pfam; PF00156; Pribosyltran; 1. DR PIRSF; PIRSF000485; Amd_phspho_trans; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR01134; purF; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Glutamine amidotransferase; KW Glycosyltransferase; Iron; Iron-sulfur; Magnesium; Metal-binding; KW Purine biosynthesis; Reference proteome; Transferase. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 471 Amidophosphoribosyltransferase. FT /FTId=PRO_0000139644. FT DOMAIN 2 224 Glutamine amidotransferase type-2. FT {ECO:0000255|HAMAP-Rule:MF_01931}. FT ACT_SITE 2 2 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 255 255 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 302 302 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 364 364 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 365 365 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 401 401 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 450 450 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01931}. FT METAL 453 453 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_01931}. SQ SEQUENCE 471 AA; 52187 MW; 27E25B66A8D5120A CRC64; MCGIFGIYSY ERLNVAKKIY YGLFALQHRG QEGAGIATSD GKNIHYYKNI GLVTDVFKNE TLQNLFGYIG IGHVRYSTTG GKAVENCQPF VVKSSFGNIA IAHNGDLVNS DELRRELEMK GHIFTSSTDS EVIAQLLVRE LLKTSDKIEA IKNTLKKLVG AYSLLIMFND SLIAVRDPWG FKPLCIGRDE SNIYISSEDC ALTTLDAEFV KDIEPGEIIE IKDGEIISHK LDYGVSEYNP VNVDVPCIYR GAATCMFEYV YFARPDSTID GISVYKVRKR IGKILAKEHP VDADVVSPIP DSGVTFALGF SEESGIPYYE GLIKNRYVGR TFILPSQNER ELAVRLKLSP VKSVLEGKRV VLVDDSIVRG TTSRRIVNMV RKAGAKEVHL RIGCPKIISP CYYGIDMATK KELIASNKTE EEIGKAIGVD SIGYLSLEGL VKAIGRKDLC LACVTGKYPT EVNFEKILGR E // ID PUR7_METJA Reviewed; 242 AA. AC Q58987; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Phosphoribosylaminoimidazole-succinocarboxamide synthase; DE EC=6.3.2.6; DE AltName: Full=SAICAR synthetase; GN Name=purC; OrderedLocusNames=MJ1592; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxylate + L-aspartate = ADP + phosphate + CC (S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamido)succinate. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 1/2. CC -!- SIMILARITY: Belongs to the SAICAR synthetase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99610.1; -; Genomic_DNA. DR PIR; G64498; G64498. DR PDB; 2YZL; X-ray; 2.20 A; A=1-242. DR PDB; 2Z02; X-ray; 2.03 A; A/B=1-242. DR PDBsum; 2YZL; -. DR PDBsum; 2Z02; -. DR ProteinModelPortal; Q58987; -. DR SMR; Q58987; 1-242. DR STRING; 243232.MJ_1592; -. DR EnsemblBacteria; AAB99610; AAB99610; MJ_1592. DR KEGG; mja:MJ_1592; -. DR eggNOG; arCOG04421; Archaea. DR eggNOG; COG0152; LUCA. DR InParanoid; Q58987; -. DR KO; K01923; -. DR OMA; FNAQKRG; -. DR PhylomeDB; Q58987; -. DR BRENDA; 6.3.2.6; 3260. DR UniPathway; UPA00074; UER00131. DR EvolutionaryTrace; Q58987; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.470.20; -; 1. DR HAMAP; MF_00137; SAICAR_synth; 1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR028923; SAICAR_synt/ADE2_N. DR InterPro; IPR001636; SAICAR_synth. DR InterPro; IPR018236; SAICAR_synthetase_CS. DR Pfam; PF01259; SAICAR_synt; 1. DR TIGRFAMs; TIGR00081; purC; 1. DR PROSITE; PS01057; SAICAR_SYNTHETASE_1; 1. DR PROSITE; PS01058; SAICAR_SYNTHETASE_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 242 Phosphoribosylaminoimidazole- FT succinocarboxamide synthase. FT /FTId=PRO_0000100909. FT HELIX 5 8 {ECO:0000244|PDB:2Z02}. FT STRAND 14 16 {ECO:0000244|PDB:2Z02}. FT STRAND 18 24 {ECO:0000244|PDB:2Z02}. FT STRAND 26 34 {ECO:0000244|PDB:2Z02}. FT STRAND 36 40 {ECO:0000244|PDB:2Z02}. FT TURN 41 44 {ECO:0000244|PDB:2Z02}. FT STRAND 45 48 {ECO:0000244|PDB:2Z02}. FT HELIX 52 69 {ECO:0000244|PDB:2Z02}. FT STRAND 74 80 {ECO:0000244|PDB:2Z02}. FT TURN 81 83 {ECO:0000244|PDB:2Z02}. FT STRAND 84 88 {ECO:0000244|PDB:2Z02}. FT STRAND 90 92 {ECO:0000244|PDB:2Z02}. FT STRAND 94 102 {ECO:0000244|PDB:2Z02}. FT HELIX 106 110 {ECO:0000244|PDB:2Z02}. FT STRAND 118 128 {ECO:0000244|PDB:2Z02}. FT HELIX 131 133 {ECO:0000244|PDB:2Z02}. FT HELIX 140 145 {ECO:0000244|PDB:2Z02}. FT HELIX 151 174 {ECO:0000244|PDB:2Z02}. FT STRAND 177 184 {ECO:0000244|PDB:2Z02}. FT STRAND 186 189 {ECO:0000244|PDB:2Z02}. FT STRAND 194 196 {ECO:0000244|PDB:2Z02}. FT TURN 202 204 {ECO:0000244|PDB:2Z02}. FT STRAND 205 209 {ECO:0000244|PDB:2Z02}. FT TURN 210 212 {ECO:0000244|PDB:2Z02}. FT HELIX 219 222 {ECO:0000244|PDB:2Z02}. FT HELIX 228 238 {ECO:0000244|PDB:2Z02}. SQ SEQUENCE 242 AA; 27761 MW; E72A473335DA3E1E CRC64; MEIKLEEILK KQPLYSGKAK SIYEIDDDKV LIEFRDDITA GNGAKHDVKQ GKGYLNALIS SKLFEALEEN GVKTHYIKYI EPRYMIAKKV EIIPIEVIVR NIAAGSLCRR YPFEEGKELP FPIVQFDYKN DEYGDPMLNE DIAVALGLAT REELNKIKEI ALKVNEVLKK LFDEKGIILV DFKIEIGKDR EGNLLVADEI SPDTMRLWDK ETRDVLDKDV FRKDLGDVIA KYRIVAERLG LL // ID PSB_METJA Reviewed; 224 AA. AC Q58634; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Proteasome subunit beta {ECO:0000255|HAMAP-Rule:MF_02113}; DE EC=3.4.25.1 {ECO:0000255|HAMAP-Rule:MF_02113}; DE AltName: Full=20S proteasome beta subunit {ECO:0000255|HAMAP-Rule:MF_02113}; DE AltName: Full=Proteasome core protein PsmB {ECO:0000255|HAMAP-Rule:MF_02113}; DE Flags: Precursor; GN Name=psmB {ECO:0000255|HAMAP-Rule:MF_02113}; OrderedLocusNames=MJ1237; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND INTERACTION WITH PAN. RX PubMed=10692374; DOI=10.1128/JB.182.6.1680-1692.2000; RA Wilson H.L., Ou M.S., Aldrich H.C., Maupin-Furlow J.; RT "Biochemical and physical properties of the Methanococcus jannaschii RT 20S proteasome and PAN, a homolog of the ATPase (Rpt) subunits of the RT eucaryal 26S proteasome."; RL J. Bacteriol. 182:1680-1692(2000). RN [3] RP X-RAY CRYSTALLOGRAPHY (4.1 ANGSTROMS) IN COMPLEX WITH ALPHA SUBUNIT, RP GATED STRUCTURE, AND SUBUNIT. RX PubMed=19481527; DOI=10.1016/j.molcel.2009.04.021; RA Zhang F., Hu M., Tian G., Zhang P., Finley D., Jeffrey P.D., Shi Y.; RT "Structural insights into the regulatory particle of the proteasome RT from Methanocaldococcus jannaschii."; RL Mol. Cell 34:473-484(2009). CC -!- FUNCTION: Component of the proteasome core, a large protease CC complex with broad specificity involved in protein degradation. CC The M.jannaschii proteasome is able to cleave oligopeptides after CC Glu, Asp, Tyr, Phe, Trp, slightly after Arg, but not after Ala. CC Thus, displays caspase-like and chymotrypsin-like activities and CC low level of trypsin-like activity. {ECO:0000255|HAMAP- CC Rule:MF_02113, ECO:0000269|PubMed:10692374}. CC -!- CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad CC specificity. {ECO:0000255|HAMAP-Rule:MF_02113, CC ECO:0000269|PubMed:10692374}. CC -!- ENZYME REGULATION: The formation of the proteasomal ATPase PAN-20S CC proteasome complex, via the docking of the C-termini of PAN into CC the intersubunit pockets in the alpha-rings, triggers opening of CC the gate for substrate entry. Interconversion between the open- CC gate and close-gate conformations leads to a dynamic regulation of CC the 20S proteasome proteolysis activity. {ECO:0000255|HAMAP- CC Rule:MF_02113}. CC -!- SUBUNIT: The 20S proteasome core is composed of 14 alpha and 14 CC beta subunits that assemble into four stacked heptameric rings, CC resulting in a barrel-shaped structure. The two inner rings, each CC composed of seven catalytic beta subunits, are sandwiched by two CC outer rings, each composed of seven alpha subunits. The catalytic CC chamber with the active sites is on the inside of the barrel. Has CC a gated structure, the ends of the cylinder being occluded by the CC N-termini of the alpha-subunits. Is capped at one or both ends by CC the proteasome regulatory ATPase, PAN. {ECO:0000255|HAMAP- CC Rule:MF_02113, ECO:0000269|PubMed:10692374, CC ECO:0000269|PubMed:19481527}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02113}. CC -!- SIMILARITY: Belongs to the peptidase T1B family. CC {ECO:0000255|HAMAP-Rule:MF_02113}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99241.1; -; Genomic_DNA. DR PIR; D64454; D64454. DR PDB; 3H4P; X-ray; 4.10 A; a/b/c/d/e/f/g/h/i/j/k/l/m/n=7-224. DR PDBsum; 3H4P; -. DR ProteinModelPortal; Q58634; -. DR SMR; Q58634; 7-208. DR STRING; 243232.MJ_1237; -. DR MEROPS; T01.002; -. DR EnsemblBacteria; AAB99241; AAB99241; MJ_1237. DR KEGG; mja:MJ_1237; -. DR eggNOG; arCOG00970; Archaea. DR eggNOG; COG0638; LUCA. DR InParanoid; Q58634; -. DR KO; K03433; -. DR OMA; VESHFGK; -. DR PhylomeDB; Q58634; -. DR EvolutionaryTrace; Q58634; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0019774; C:proteasome core complex, beta-subunit complex; IDA:UniProtKB. DR GO; GO:0004175; F:endopeptidase activity; IDA:UniProtKB. DR GO; GO:0004298; F:threonine-type endopeptidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0010498; P:proteasomal protein catabolic process; IDA:UniProtKB. DR Gene3D; 3.60.20.10; -; 1. DR HAMAP; MF_02113_A; Proteasome_B_A; 1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR019983; Pept_T1A_Psome_bsu_arc. DR InterPro; IPR000243; Pept_T1A_subB. DR InterPro; IPR016050; Proteasome_bsu_CS. DR InterPro; IPR001353; Proteasome_sua/b. DR InterPro; IPR023333; Proteasome_suB-type. DR Pfam; PF00227; Proteasome; 1. DR PRINTS; PR00141; PROTEASOME. DR SUPFAM; SSF56235; SSF56235; 1. DR TIGRFAMs; TIGR03634; arc_protsome_B; 1. DR PROSITE; PS00854; PROTEASOME_BETA_1; 1. DR PROSITE; PS51476; PROTEASOME_BETA_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Autocatalytic cleavage; Complete proteome; Cytoplasm; KW Hydrolase; Protease; Proteasome; Reference proteome; KW Threonine protease; Zymogen. FT PROPEP 1 6 Removed in mature form; by autocatalysis. FT {ECO:0000255|HAMAP-Rule:MF_02113}. FT /FTId=PRO_0000026661. FT CHAIN 7 224 Proteasome subunit beta. FT /FTId=PRO_0000026662. FT ACT_SITE 7 7 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_02113}. FT STRAND 12 14 FT STRAND 17 21 FT STRAND 32 34 FT STRAND 40 44 FT STRAND 47 50 FT HELIX 58 75 FT HELIX 82 95 FT TURN 96 100 FT TURN 141 143 FT HELIX 162 172 FT STRAND 184 187 FT HELIX 197 206 SQ SEQUENCE 224 AA; 24285 MW; 45B2A0D1EAEF7A58 CRC64; MDVMKGTTTV GLICDDAVIL ATDKRASLGN LVADKEAKKL YKIDDYIAMT IAGSVGDAQA IVRLLIAEAK LYKMRTGRNI PPLACATLLS NILHSSRMFP FLTQIIIGGY DLLEGAKLFS LDPLGGMNEE KTFTATGSGS PIAYGVLEAG YDRDMSVEEG IKLALNALKS AMERDTFSGN GISLAVITKD GVKIFEDEEI EKILDSMKAK PKKKTTKRSR RKSK // ID PUR2_METJA Reviewed; 444 AA. AC Q58347; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Phosphoribosylamine--glycine ligase {ECO:0000255|HAMAP-Rule:MF_00138}; DE EC=6.3.4.13 {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=GARS {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Glycinamide ribonucleotide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; DE AltName: Full=Phosphoribosylglycinamide synthetase {ECO:0000255|HAMAP-Rule:MF_00138}; GN Name=purD {ECO:0000255|HAMAP-Rule:MF_00138}; OrderedLocusNames=MJ0937; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + 5-phospho-D-ribosylamine + glycine = ADP CC + phosphate + N(1)-(5-phospho-D-ribosyl)glycinamide. CC {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 magnesium or manganese ions per subunit. CC {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(1)-(5-phospho-D-ribosyl)glycinamide from 5-phospho-alpha-D- CC ribose 1-diphosphate: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00138}. CC -!- SIMILARITY: Belongs to the GARS family. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00138}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98942.1; -; Genomic_DNA. DR PIR; A64417; A64417. DR ProteinModelPortal; Q58347; -. DR STRING; 243232.MJ_0937; -. DR EnsemblBacteria; AAB98942; AAB98942; MJ_0937. DR KEGG; mja:MJ_0937; -. DR eggNOG; arCOG04415; Archaea. DR eggNOG; COG0151; LUCA. DR InParanoid; Q58347; -. DR KO; K01945; -. DR OMA; DEFGPPY; -. DR PhylomeDB; Q58347; -. DR UniPathway; UPA00074; UER00125. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004637; F:phosphoribosylamine-glycine ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009113; P:purine nucleobase biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR Gene3D; 3.90.600.10; -; 1. DR HAMAP; MF_00138; GARS; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR020561; PRibGlycinamid_synth_ATP-grasp. DR InterPro; IPR000115; PRibGlycinamide_synth. DR InterPro; IPR020560; PRibGlycinamide_synth_C-dom. DR InterPro; IPR020559; PRibGlycinamide_synth_CS. DR InterPro; IPR020562; PRibGlycinamide_synth_N. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF01071; GARS_A; 1. DR Pfam; PF02843; GARS_C; 1. DR Pfam; PF02844; GARS_N; 1. DR SMART; SM01210; GARS_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00877; purD; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS00184; GARS; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 444 Phosphoribosylamine--glycine ligase. FT /FTId=PRO_0000151510. FT DOMAIN 109 324 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00138}. FT NP_BIND 140 202 ATP. {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 282 282 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 294 294 Magnesium or manganese 1. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 294 294 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00138}. FT METAL 296 296 Magnesium or manganese 2. FT {ECO:0000255|HAMAP-Rule:MF_00138}. SQ SEQUENCE 444 AA; 49098 MW; 9AD115FBC8AB8BD1 CRC64; MKILLIGGGA RESAIAHALK KNEEVKLYTL MKNKNPGIAR LSEEIKLAKE TDLDAVKEFA EKVKPDLAVI GPEAPLGEGV VDLLEEMGIS AVGPKKLAAQ IETNKEFMRN LFKKYNIKGS LMYKAFEEYG EELESFIDEL TEKGIKAVVK PVGLTGGKGV KVVGEQLKDN EEAKKYAKEI FETGLGGGKV LIEEKLEGVE FTLHGFVDGD TIKFTPFVQD HPHALEGDEG SITGGMGSYS CPDHKLPFMT EEDVKLAKEI MEETVKALKE EVGGYKGILY GQFMLTKEGP KIIEYNARFG DPEAMNLLAI LKNDFLEVCE AIVNKKLKDI DVEFENKATV CKYVVPKGYP DNPVRGEPIT VDEEAIKKTG AILHYASVNE DNGSLYMTGS RAVAVVGVAD TIEEAERIAE EATKYIKGEV YHRSDIGKKE LIKKRIEKMN ELRR // ID PYRB_METJA Reviewed; 306 AA. AC Q58976; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Aspartate carbamoyltransferase; DE EC=2.1.3.2; DE AltName: Full=Aspartate transcarbamylase; DE Short=ATCase; GN Name=pyrB; OrderedLocusNames=MJ1581; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CATALYTIC ACTIVITY, PATHWAY, AND SUBUNIT. RX PubMed=10748118; DOI=10.1074/jbc.M909220199; RA Hack E.S., Vorobyova T., Sakash J.B., West J.M., Macol C.P., Herve G., RA Williams M.K., Kantrowitz E.R.; RT "Characterization of the aspartate transcarbamoylase from RT Methanococcus jannaschii."; RL J. Biol. Chem. 275:15820-15827(2000). RN [3] RP CRYSTALLIZATION. RX PubMed=10944354; DOI=10.1107/S0907444900008167; RA Vitali J., Vorobyova T., Webster G., Kantrowitz E.R.; RT "Crystallization and structure determination of the catalytic trimer RT of Methanococcus jannaschii aspartate transcarbamoylase."; RL Acta Crystallogr. D 56:1061-1063(2000). CC -!- CATALYTIC ACTIVITY: Carbamoyl phosphate + L-aspartate = phosphate CC + N-carbamoyl-L-aspartate. {ECO:0000269|PubMed:10748118}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 2/3. CC {ECO:0000269|PubMed:10748118}. CC -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains CC organized as two trimers (C3), and six regulatory PyrI chains CC organized as three dimers (R2). {ECO:0000269|PubMed:10748118}. CC -!- SIMILARITY: Belongs to the ATCase/OTCase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99601.1; -; Genomic_DNA. DR PIR; D64497; D64497. DR PDB; 2RGW; X-ray; 2.80 A; A/B/C/D/E/F=1-306. DR PDB; 3E2P; X-ray; 3.00 A; A/B/C/D/E/F/I/J/K/L/M/N=1-306. DR PDB; 4EKN; X-ray; 2.50 A; B=1-306. DR PDBsum; 2RGW; -. DR PDBsum; 3E2P; -. DR PDBsum; 4EKN; -. DR ProteinModelPortal; Q58976; -. DR SMR; Q58976; 2-300. DR STRING; 243232.MJ_1581; -. DR EnsemblBacteria; AAB99601; AAB99601; MJ_1581. DR KEGG; mja:MJ_1581; -. DR eggNOG; arCOG00911; Archaea. DR eggNOG; COG0540; LUCA. DR InParanoid; Q58976; -. DR KO; K00609; -. DR OMA; KQSFYGV; -. DR PhylomeDB; Q58976; -. DR BRENDA; 2.1.3.2; 3260. DR UniPathway; UPA00070; UER00116. DR EvolutionaryTrace; Q58976; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0004070; F:aspartate carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006520; P:cellular amino acid metabolic process; IEA:InterPro. DR GO; GO:0009220; P:pyrimidine ribonucleotide biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.1370; -; 2. DR HAMAP; MF_00001; Asp_carb_tr; 1. DR InterPro; IPR006132; Asp/Orn_carbamoyltranf_P-bd. DR InterPro; IPR006130; Asp/Orn_carbamoylTrfase. DR InterPro; IPR002082; Asp_carbamoyltransf. DR InterPro; IPR006131; Asp_carbamoyltransf_Asp/Orn-bd. DR Pfam; PF00185; OTCace; 1. DR Pfam; PF02729; OTCace_N; 1. DR PRINTS; PR00100; AOTCASE. DR PRINTS; PR00101; ATCASE. DR SUPFAM; SSF53671; SSF53671; 1. DR TIGRFAMs; TIGR00670; asp_carb_tr; 1. DR PROSITE; PS00097; CARBAMOYLTRANSFERASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Pyrimidine biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 306 Aspartate carbamoyltransferase. FT /FTId=PRO_0000113247. FT HELIX 7 9 {ECO:0000244|PDB:4EKN}. FT HELIX 12 30 {ECO:0000244|PDB:4EKN}. FT TURN 37 40 {ECO:0000244|PDB:4EKN}. FT STRAND 42 49 {ECO:0000244|PDB:4EKN}. FT HELIX 52 64 {ECO:0000244|PDB:4EKN}. FT STRAND 68 72 {ECO:0000244|PDB:4EKN}. FT TURN 76 79 {ECO:0000244|PDB:4EKN}. FT STRAND 80 83 {ECO:0000244|PDB:4EKN}. FT HELIX 86 96 {ECO:0000244|PDB:4EKN}. FT STRAND 98 103 {ECO:0000244|PDB:4EKN}. FT STRAND 105 108 {ECO:0000244|PDB:3E2P}. FT HELIX 109 116 {ECO:0000244|PDB:4EKN}. FT STRAND 121 124 {ECO:0000244|PDB:4EKN}. FT STRAND 126 129 {ECO:0000244|PDB:4EKN}. FT HELIX 132 146 {ECO:0000244|PDB:4EKN}. FT STRAND 149 151 {ECO:0000244|PDB:2RGW}. FT STRAND 153 158 {ECO:0000244|PDB:4EKN}. FT TURN 160 162 {ECO:0000244|PDB:4EKN}. FT HELIX 164 174 {ECO:0000244|PDB:4EKN}. FT STRAND 176 178 {ECO:0000244|PDB:4EKN}. FT STRAND 180 184 {ECO:0000244|PDB:4EKN}. FT HELIX 187 189 {ECO:0000244|PDB:4EKN}. FT HELIX 193 201 {ECO:0000244|PDB:4EKN}. FT STRAND 206 210 {ECO:0000244|PDB:4EKN}. FT HELIX 212 214 {ECO:0000244|PDB:4EKN}. FT STRAND 220 224 {ECO:0000244|PDB:4EKN}. FT HELIX 229 231 {ECO:0000244|PDB:4EKN}. FT HELIX 235 245 {ECO:0000244|PDB:4EKN}. FT HELIX 249 252 {ECO:0000244|PDB:4EKN}. FT STRAND 258 260 {ECO:0000244|PDB:4EKN}. FT STRAND 266 269 {ECO:0000244|PDB:4EKN}. FT HELIX 271 273 {ECO:0000244|PDB:4EKN}. FT HELIX 281 302 {ECO:0000244|PDB:4EKN}. SQ SEQUENCE 306 AA; 35160 MW; CBDC31FC450CEF6A CRC64; MKHLISMKDI GKEEILEILD EARKMEELLN TKRPLKLLEG KILATVFYEP STRTRLSFET AMKRLGGEVI TMTDLKSSSV AKGESLIDTI RVISGYADII VLRHPSEGAA RLASEYSQVP IINAGDGSNQ HPTQTLLDLY TIMREIGRID GIKIAFVGDL KYGRTVHSLV YALSLFENVE MYFVSPKELR LPKDIIEDLK AKNIKFYEKE SLDDLDDDID VLYVTRIQKE RFPDPNEYEK VKGSYKIKRE YVEGKKFIIM HPLPRVDEID YDVDDLPQAK YFKQSFYGIP VRMAILKKLI EDNEGE // ID PYRF_METJA Reviewed; 213 AA. AC Q57700; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2002, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=Orotidine 5'-phosphate decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE EC=4.1.1.23 {ECO:0000255|HAMAP-Rule:MF_01200}; DE AltName: Full=OMP decarboxylase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPDCase {ECO:0000255|HAMAP-Rule:MF_01200}; DE Short=OMPdecase {ECO:0000255|HAMAP-Rule:MF_01200}; GN Name=pyrF {ECO:0000255|HAMAP-Rule:MF_01200}; OrderedLocusNames=MJ0252; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the decarboxylation of orotidine 5'- CC monophosphate (OMP) to uridine 5'-monophosphate (UMP). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate = UMP + CO(2). CC {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 2/2. {ECO:0000255|HAMAP- CC Rule:MF_01200}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SIMILARITY: Belongs to the OMP decarboxylase family. Type 1 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01200}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98239.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98239.1; ALT_INIT; Genomic_DNA. DR PIR; E64331; E64331. DR PDB; 4LUI; X-ray; 1.60 A; A/B=1-213. DR PDB; 4LUJ; X-ray; 1.60 A; A/B=1-213. DR PDBsum; 4LUI; -. DR PDBsum; 4LUJ; -. DR ProteinModelPortal; Q57700; -. DR STRING; 243232.MJ_0252; -. DR PRIDE; Q57700; -. DR EnsemblBacteria; AAB98239; AAB98239; MJ_0252. DR KEGG; mja:MJ_0252; -. DR eggNOG; arCOG00081; Archaea. DR eggNOG; COG0284; LUCA. DR InParanoid; Q57700; -. DR KO; K01591; -. DR OMA; VTEMSHP; -. DR PhylomeDB; Q57700; -. DR UniPathway; UPA00070; UER00120. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004590; F:orotidine-5'-phosphate decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01200_A; OMPdecase_type1_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR014732; OMPdecase. DR InterPro; IPR018089; OMPdecase_AS. DR InterPro; IPR001754; OMPdeCOase_dom. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00215; OMPdecase; 1. DR SMART; SM00934; OMPdecase; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01740; pyrF; 1. DR PROSITE; PS00156; OMPDECASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Decarboxylase; Lyase; KW Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 213 Orotidine 5'-phosphate decarboxylase. FT /FTId=PRO_0000134610. FT REGION 59 68 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT REGION 166 176 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT ACT_SITE 61 61 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 9 9 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 31 31 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 115 115 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT BINDING 191 191 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01200}. FT BINDING 192 192 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01200}. FT STRAND 3 7 {ECO:0000244|PDB:4LUI}. FT HELIX 13 23 {ECO:0000244|PDB:4LUI}. FT TURN 24 26 {ECO:0000244|PDB:4LUI}. FT STRAND 28 33 {ECO:0000244|PDB:4LUI}. FT HELIX 34 38 {ECO:0000244|PDB:4LUI}. FT HELIX 43 52 {ECO:0000244|PDB:4LUI}. FT STRAND 54 62 {ECO:0000244|PDB:4LUI}. FT HELIX 66 76 {ECO:0000244|PDB:4LUI}. FT TURN 77 79 {ECO:0000244|PDB:4LUI}. FT STRAND 81 87 {ECO:0000244|PDB:4LUI}. FT HELIX 91 103 {ECO:0000244|PDB:4LUI}. FT STRAND 107 111 {ECO:0000244|PDB:4LUI}. FT HELIX 117 120 {ECO:0000244|PDB:4LUI}. FT TURN 121 123 {ECO:0000244|PDB:4LUI}. FT HELIX 124 126 {ECO:0000244|PDB:4LUI}. FT HELIX 127 137 {ECO:0000244|PDB:4LUI}. FT STRAND 140 143 {ECO:0000244|PDB:4LUI}. FT HELIX 149 159 {ECO:0000244|PDB:4LUI}. FT STRAND 163 166 {ECO:0000244|PDB:4LUI}. FT HELIX 175 177 {ECO:0000244|PDB:4LUJ}. FT HELIX 179 181 {ECO:0000244|PDB:4LUI}. FT STRAND 187 190 {ECO:0000244|PDB:4LUI}. FT HELIX 192 195 {ECO:0000244|PDB:4LUI}. FT HELIX 200 209 {ECO:0000244|PDB:4LUI}. SQ SEQUENCE 213 AA; 23592 MW; 0B073BE37D50C556 CRC64; MPKLMLALDV LDRDRALKIV EDVKDYVDAI KVGYPLVLST GTEIIKEIKK LCNKEVIADF KVADIPATNE KIAKITLKYA DGIIVHGFVG EDSVKAVQDV AKKLNKKVIM VTEMSHPGAV QFLQPIADKL SEMAKKLKVD AIVAPSTRPE RLKEIKEIAE LPVITPGVGA QGGKIEDILN ILDENDYVIV GRAIYQSQNP KEEAKKYKEM LNK // ID PSS_METJA Reviewed; 201 AA. AC Q58609; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=CDP-diacylglycerol--serine O-phosphatidyltransferase; DE EC=2.7.8.8; DE AltName: Full=Phosphatidylserine synthase; GN Name=pssA; OrderedLocusNames=MJ1212; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: CDP-diacylglycerol + L-serine = CMP + (3-sn- CC phosphatidyl)-L-serine. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase CC class-I family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99214.1; -; Genomic_DNA. DR PIR; C64451; C64451. DR ProteinModelPortal; Q58609; -. DR STRING; 243232.MJ_1212; -. DR DNASU; 1452108; -. DR EnsemblBacteria; AAB99214; AAB99214; MJ_1212. DR KEGG; mja:MJ_1212; -. DR eggNOG; arCOG00671; Archaea. DR eggNOG; COG1183; LUCA. DR InParanoid; Q58609; -. DR KO; K17103; -. DR OMA; RFNLMAF; -. DR PhylomeDB; Q58609; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003882; F:CDP-diacylglycerol-serine O-phosphatidyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0008654; P:phospholipid biosynthetic process; IBA:GO_Central. DR InterPro; IPR004533; CDP-diaglyc--ser_O-PTrfase. DR InterPro; IPR000462; CDP-OH_P_trans. DR Pfam; PF01066; CDP-OH_P_transf; 1. DR TIGRFAMs; TIGR00473; pssA; 1. DR PROSITE; PS00379; CDP_ALCOHOL_P_TRANSF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipid biosynthesis; KW Lipid metabolism; Membrane; Phospholipid biosynthesis; KW Phospholipid metabolism; Reference proteome; Transferase; KW Transmembrane; Transmembrane helix. FT CHAIN 1 201 CDP-diacylglycerol--serine O- FT phosphatidyltransferase. FT /FTId=PRO_0000056799. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. SQ SEQUENCE 201 AA; 22014 MW; D45D3201941615CA CRC64; MFSIRKIITI SDYVTMLNII TGLLAILLNS FSLIYLSIIF DSLDGYVARK TGTVSDFGAE LDSISDVVSF GVAPAYLLYN NFESNLALIS AIIFCLCGAL RLARFGILNV KGFIGLPIPA GALLLVGFCQ LINSYLINSI LAILIGLLMI SDIKYPKYPN KIFIYIFAVS LCLAIVGIPH FALMLCLIYA IYGIIKYIRG D // ID PURO_METJA Reviewed; 202 AA. AC Q58043; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 09-SEP-2003, sequence version 2. DT 11-NOV-2015, entry version 93. DE RecName: Full=IMP cyclohydrolase; DE EC=3.5.4.10; DE AltName: Full=IMP synthase; DE AltName: Full=Inosinicase; GN Name=purO; OrderedLocusNames=MJ0626; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=11844782; DOI=10.1128/JB.184.5.1471-1473.2002; RA Graupner M., Xu H., White R.H.; RT "New class of IMP cyclohydrolases in Methanococcus jannaschii."; RL J. Bacteriol. 184:1471-1473(2002). CC -!- FUNCTION: Catalyzes the cyclization of 5-formylamidoimidazole-4- CC carboxamide ribonucleotide to IMP. CC -!- CATALYTIC ACTIVITY: IMP + H(2)O = 5-formamido-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6-8.5.; CC Temperature dependence: CC Fully active at 80 degrees Celsius. Gradually loses some CC activity from 90 to 100 degrees Celsius.; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC IMP from 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxamide: step 1/1. CC -!- SIMILARITY: Belongs to the archaeal IMP cyclohydrolase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98620.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98620.1; ALT_INIT; Genomic_DNA. DR PIR; B64378; B64378. DR ProteinModelPortal; Q58043; -. DR STRING; 243232.MJ_0626; -. DR EnsemblBacteria; AAB98620; AAB98620; MJ_0626. DR KEGG; mja:MJ_0626; -. DR eggNOG; arCOG04727; Archaea. DR eggNOG; COG3363; LUCA. DR InParanoid; Q58043; -. DR KO; K11176; -. DR OMA; YIGRFLV; -. DR PhylomeDB; Q58043; -. DR BioCyc; MetaCyc:MONOMER-14617; -. DR BRENDA; 3.5.4.10; 3260. DR UniPathway; UPA00074; UER00135. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003937; F:IMP cyclohydrolase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.20.20; -; 1. DR HAMAP; MF_00705; IMP_cyclohydrol; 1. DR InterPro; IPR010191; IMP_cyclohydrolase. DR InterPro; IPR020600; IMP_cyclohydrolase-like. DR Pfam; PF07826; IMP_cyclohyd; 1. DR PIRSF; PIRSF004866; IMP_cclhdr_arch; 1. DR SUPFAM; SSF75569; SSF75569; 1. DR TIGRFAMs; TIGR01922; purO_arch; 1. PE 1: Evidence at protein level; KW Complete proteome; Hydrolase; Purine biosynthesis; Reference proteome. FT CHAIN 1 202 IMP cyclohydrolase. FT /FTId=PRO_0000145795. SQ SEQUENCE 202 AA; 22941 MW; 339DDF505D0733D9 CRC64; MYIGRFLVVG KTKEGKPFAA YRVSSRSFPN REAKKMDDNT VAIIPKDLNE MFKNPYITYN CIKVIDKTIV VSNGTHTDFI AEKLHFGKRD ALAYVLAVMD YEKDDYKTPR IAAILDENEC YMGYVAHDDI RVKKVELKDG KGYYLGVYNA CKIDENQIID IKGETAEEIA DYILNYEEFE HPVACAVAVI DKDGIKIATK GK // ID PURT_METJA Reviewed; 389 AA. AC Q58881; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 17-FEB-2016, entry version 106. DE RecName: Full=Phosphoribosylglycinamide formyltransferase 2 {ECO:0000255|HAMAP-Rule:MF_01643}; DE Short=GART 2 {ECO:0000255|HAMAP-Rule:MF_01643}; DE EC=2.1.2.- {ECO:0000255|HAMAP-Rule:MF_01643}; DE AltName: Full=5'-phosphoribosylglycinamide transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643}; DE AltName: Full=Formate-dependent GAR transformylase {ECO:0000255|HAMAP-Rule:MF_01643}; DE AltName: Full=GAR transformylase 2 {ECO:0000255|HAMAP-Rule:MF_01643}; GN Name=purT {ECO:0000255|HAMAP-Rule:MF_01643}; OrderedLocusNames=MJ1486; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes two reactions: the first one is the production CC of beta-formyl glycinamide ribonucleotide (GAR) from formate, ATP CC and beta GAR; the second, a side reaction, is the production of CC acetyl phosphate and ADP from acetate and ATP. {ECO:0000255|HAMAP- CC Rule:MF_01643}. CC -!- CATALYTIC ACTIVITY: Formate + ATP + 5'-phospho-ribosylglycinamide CC = 5'-phosphoribosyl-N-formylglycinamide + ADP + diphosphate. CC {ECO:0000255|HAMAP-Rule:MF_01643}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC N(2)-formyl-N(1)-(5-phospho-D-ribosyl)glycinamide from N(1)-(5- CC phospho-D-ribosyl)glycinamide (formate route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01643}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01643}. CC -!- SIMILARITY: Belongs to the PurK/PurT family. {ECO:0000255|HAMAP- CC Rule:MF_01643}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_01643}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99496.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99496.1; ALT_INIT; Genomic_DNA. DR PIR; E64485; E64485. DR ProteinModelPortal; Q58881; -. DR SMR; Q58881; 3-389. DR STRING; 243232.MJ_1486; -. DR EnsemblBacteria; AAB99496; AAB99496; MJ_1486. DR KEGG; mja:MJ_1486; -. DR eggNOG; arCOG01598; Archaea. DR eggNOG; COG0027; LUCA. DR InParanoid; Q58881; -. DR KO; K08289; -. DR OMA; IFGVEFF; -. DR PhylomeDB; Q58881; -. DR BioCyc; MetaCyc:MONOMER-14618; -. DR UniPathway; UPA00074; UER00127. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004638; F:phosphoribosylaminoimidazole carboxylase activity; IBA:GO_Central. DR GO; GO:0004639; F:phosphoribosylaminoimidazolesuccinocarboxamide synthase activity; IBA:GO_Central. DR GO; GO:0043815; F:phosphoribosylglycinamide formyltransferase 2 activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004644; F:phosphoribosylglycinamide formyltransferase activity; IEA:InterPro. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IBA:GO_Central. DR GO; GO:0046084; P:adenine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01643; PurT; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003135; ATP-grasp_carboxylate-amine. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR005862; PurT. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02222; ATP-grasp; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR01142; purT; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Magnesium; Metal-binding; KW Nucleotide-binding; Purine biosynthesis; Reference proteome; KW Transferase. FT CHAIN 1 389 Phosphoribosylglycinamide FT formyltransferase 2. FT /FTId=PRO_0000074959. FT DOMAIN 118 307 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_01643}. FT NP_BIND 159 164 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}. FT NP_BIND 194 197 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}. FT REGION 21 22 5'-phosphoribosylglycinamide binding. FT {ECO:0000255|HAMAP-Rule:MF_01643}. FT REGION 360 361 5'-phosphoribosylglycinamide binding. FT {ECO:0000255|HAMAP-Rule:MF_01643}. FT METAL 266 266 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01643}. FT METAL 278 278 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01643}. FT BINDING 81 81 5'-phosphoribosylglycinamide. FT {ECO:0000255|HAMAP-Rule:MF_01643}. FT BINDING 113 113 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}. FT BINDING 154 154 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}. FT BINDING 202 202 ATP. {ECO:0000255|HAMAP-Rule:MF_01643}. FT BINDING 285 285 5'-phosphoribosylglycinamide. FT {ECO:0000255|HAMAP-Rule:MF_01643}. FT BINDING 353 353 5'-phosphoribosylglycinamide. FT {ECO:0000255|HAMAP-Rule:MF_01643}. SQ SEQUENCE 389 AA; 43048 MW; 3887A7EC474BECE8 CRC64; MAIGTPLLKG SIKFLLLGSG ELGKEVVIEA QRLGIECIAV DRYQNAPAMQ VAHKSYVIDM KDYDALMAII EREEPDYIVP EIEAINTDAL IDAEKMGYTV IPTAEATKIT MNRELIRRLA AEKLGLKTAK YEFADSLEEL RDAVEKLGLP CVVKPIMSSS GKGQSVVRSE EDIEKAWKIA KEGARGIGNR VIVEEFINFD YEITLLTART AEGTKFCEPI GHVQIDGDYH ESWQPHNMSA ELKEQAQDIA KKVTDALGGY GIFGVELFVK GDEVIFSEVS PRPHDTGMVT MITQEMSEFE IHVRAILGLP VSTKLIHPGA SHVIKAEINK YAPKYHIEDA LKVPNTKLRL FGKPNAKVGR RMGVALAYAD SVEKARELAE KCAHAVRIE // ID PYRE_METJA Reviewed; 176 AA. AC Q58509; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Orotate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRT {ECO:0000255|HAMAP-Rule:MF_01208}; DE Short=OPRTase {ECO:0000255|HAMAP-Rule:MF_01208}; DE EC=2.4.2.10 {ECO:0000255|HAMAP-Rule:MF_01208}; GN Name=pyrE {ECO:0000255|HAMAP-Rule:MF_01208}; OrderedLocusNames=MJ1109; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transfer of a ribosyl phosphate group from CC 5-phosphoribose 1-diphosphate to orotate, leading to the formation CC of orotidine monophosphate (OMP). {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- CATALYTIC ACTIVITY: Orotidine 5'-phosphate + diphosphate = orotate CC + 5-phospho-alpha-D-ribose 1-diphosphate. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01208}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; UMP from orotate: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01208}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01208}. CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. PyrE subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99112.1; -; Genomic_DNA. DR PIR; D64438; D64438. DR ProteinModelPortal; Q58509; -. DR STRING; 243232.MJ_1109; -. DR EnsemblBacteria; AAB99112; AAB99112; MJ_1109. DR KEGG; mja:MJ_1109; -. DR eggNOG; arCOG00029; Archaea. DR eggNOG; COG0461; LUCA. DR InParanoid; Q58509; -. DR KO; K00762; -. DR OMA; TTNPKVL; -. DR PhylomeDB; Q58509; -. DR UniPathway; UPA00070; UER00119. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004588; F:orotate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01208; PyrE; 1. DR InterPro; IPR023031; OPRT. DR InterPro; IPR004467; Or_phspho_trans_dom. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR TIGRFAMs; TIGR00336; pyrE; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Magnesium; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 176 Orotate phosphoribosyltransferase. FT /FTId=PRO_0000110779. FT REGION 116 124 5-phosphoribose 1-diphosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 90 90 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 91 91 5-phosphoribose 1-diphosphate. FT {ECO:0000255|HAMAP-Rule:MF_01208}. FT BINDING 94 94 5-phosphoribose 1-diphosphate; shared FT with dimeric partner. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 120 120 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. FT BINDING 148 148 Orotate. {ECO:0000255|HAMAP- FT Rule:MF_01208}. SQ SEQUENCE 176 AA; 19284 MW; D208C1F49789E694 CRC64; MDKKSKLINL LKEVGCIRFG EFILASGKKS NYYIDIKKAT TNPEILKLVG EIIAEQIKDE DVKVAGVELG SVPIATAVSI IAQKPLLIVR KKPKDYGTKN KIEGELKEGD KVVIVEDVTT TGGSVLKAVK EIRENGGIVD KVFVVVDRLE GAKENLQKEN VELIPLVTVK ELQSTQ // ID PTR1_METJA Reviewed; 148 AA. AC Q57615; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=HTH-type transcriptional regulator Ptr1; GN Name=ptr1; OrderedLocusNames=MJ0151; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=11226165; DOI=10.1093/emboj/20.1.146; RA Ouhammouch M., Geiduschek E.P.; RT "A thermostable platform for transcriptional regulation: the DNA- RT binding properties of two Lrp homologs from the hyperthermophilic RT archaeon Methanococcus jannaschii."; RL EMBO J. 20:146-156(2001). CC -!- FUNCTION: Participates in positive as well as negative regulation CC of transcription. Binds to its own promoter. CC -!- SUBUNIT: Homodimer. CC -!- SIMILARITY: Contains 1 HTH asnC-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00319}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98133.1; -; Genomic_DNA. DR PIR; H64318; H64318. DR ProteinModelPortal; Q57615; -. DR STRING; 243232.MJ_0151; -. DR EnsemblBacteria; AAB98133; AAB98133; MJ_0151. DR KEGG; mja:MJ_0151; -. DR eggNOG; arCOG01580; Archaea. DR eggNOG; COG1522; LUCA. DR InParanoid; Q57615; -. DR KO; K03718; -. DR OMA; VHVRVKK; -. DR PhylomeDB; Q57615; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 1: Evidence at protein level; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 148 HTH-type transcriptional regulator Ptr1. FT /FTId=PRO_0000111752. FT DOMAIN 2 63 HTH asnC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. FT DNA_BIND 21 40 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. SQ SEQUENCE 148 AA; 16633 MW; B3AAAC4B34A39982 CRC64; MLDRIDLKIL RILNGNARKS FREIGRELGI SEGTVRNRVK RLTEKGIITG FHASINPKNL GFEVVAILGL YIKPSKVEET LNKLKELDEI VELYQTTGEY DAVCIAILKD IESLGKFLAE KIYPLVNVNG CKVTLVLRTF KDGSKMPI // ID PUR8_METJA Reviewed; 462 AA. AC Q58339; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 110. DE RecName: Full=Adenylosuccinate lyase; DE Short=ASL; DE EC=4.3.2.2; DE AltName: Full=Adenylosuccinase; DE Short=ASase; GN Name=purB; OrderedLocusNames=MJ0929; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: N(6)-(1,2-dicarboxyethyl)AMP = fumarate + AMP. CC -!- CATALYTIC ACTIVITY: (S)-2-(5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamido)succinate = fumarate + 5-amino-1- CC (5-phospho-D-ribosyl)imidazole-4-carboxamide. CC -!- PATHWAY: Purine metabolism; AMP biosynthesis via de novo pathway; CC AMP from IMP: step 2/2. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate: step 2/2. CC -!- SUBUNIT: Homotetramer. Residues from neighboring subunits CC contribute catalytic and substrate-binding residues to each active CC site (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the lyase 1 family. Adenylosuccinate lyase CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98931.1; -; Genomic_DNA. DR PIR; A64416; A64416. DR ProteinModelPortal; Q58339; -. DR STRING; 243232.MJ_0929; -. DR EnsemblBacteria; AAB98931; AAB98931; MJ_0929. DR KEGG; mja:MJ_0929; -. DR eggNOG; arCOG01747; Archaea. DR eggNOG; COG0015; LUCA. DR InParanoid; Q58339; -. DR KO; K01756; -. DR OMA; AVHPIDY; -. DR PhylomeDB; Q58339; -. DR UniPathway; UPA00074; UER00132. DR UniPathway; UPA00075; UER00336. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0070626; F:(S)-2-(5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamido)succinate AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0004018; F:N6-(1,2-dicarboxyethyl)AMP AMP-lyase (fumarate-forming) activity; IBA:GO_Central. DR GO; GO:0044208; P:'de novo' AMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0051262; P:protein tetramerization; IBA:GO_Central. DR GO; GO:0006163; P:purine nucleotide metabolic process; IBA:GO_Central. DR Gene3D; 1.10.275.10; -; 1. DR InterPro; IPR019468; AdenyloSucc_lyase_C. DR InterPro; IPR024083; Fumarase/histidase_N. DR InterPro; IPR020557; Fumarate_lyase_CS. DR InterPro; IPR000362; Fumarate_lyase_fam. DR InterPro; IPR022761; Fumarate_lyase_N. DR InterPro; IPR008948; L-Aspartase-like. DR InterPro; IPR004769; Pur_lyase. DR PANTHER; PTHR11444; PTHR11444; 1. DR Pfam; PF10397; ADSL_C; 1. DR Pfam; PF00206; Lyase_1; 1. DR PRINTS; PR00149; FUMRATELYASE. DR SMART; SM00998; ADSL_C; 1. DR SUPFAM; SSF48557; SSF48557; 1. DR TIGRFAMs; TIGR00928; purB; 1. DR PROSITE; PS00163; FUMARATE_LYASES; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Purine biosynthesis; Reference proteome. FT CHAIN 1 462 Adenylosuccinate lyase. FT /FTId=PRO_0000137888. FT REGION 21 22 Substrate binding. {ECO:0000250}. FT REGION 87 89 Substrate binding. {ECO:0000250}. FT ACT_SITE 162 162 Proton donor/acceptor. {ECO:0000250}. FT ACT_SITE 287 287 Proton donor/acceptor. {ECO:0000250}. FT BINDING 236 236 Substrate. {ECO:0000250}. FT BINDING 326 326 Substrate. {ECO:0000250}. FT BINDING 331 331 Substrate. {ECO:0000250}. FT BINDING 335 335 Substrate. {ECO:0000250}. SQ SEQUENCE 462 AA; 52592 MW; D0E89A0D2F0C1894 CRC64; MELNQIIKSG EKMAVHPIDY RYGTPEMRKV WEEENKLEKM LKVEAALAKA QAELGLIPKE AAEEINKKAS TKYVKLERVK EIEKQTKHDV VAMIRALAEV CEGNAGEYIH FGATSNDIVD TANSLLIKES IEIIEDKLKQ LRDILLDKAE EHKYTVCVGR THGQHAIPTT YGMRFALWAA EIDRHLERLK EAKKRICVSM ITGAVGTMAA MGEKGLEVHK RVAEILGLEP VLISNQVIQR DRHAEFVFLL ALIAQTLNKI GVTVRSMQRT EIGELEEEFD PTKQTGSSTM PHKRNPITFE QICGLSRVIK SLCIAEMDNI PLWEERDLTN SSAERCIFAE VCVLTDHILT LAIKGVKKLK VNKENVERNL ELTKGLIMAE RIMIELAKRG MGRQTAHEIV RQCAMKAYEE KRHLKDILLE NEEVMKYITK EELEELMNPK TYIGLAPQIV DEVIKTLKNK KY // ID PURE_METJA Reviewed; 157 AA. AC Q58033; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=N5-carboxyaminoimidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE Short=N5-CAIR mutase {ECO:0000255|HAMAP-Rule:MF_01929}; DE EC=5.4.99.18 {ECO:0000255|HAMAP-Rule:MF_01929}; DE AltName: Full=5-(carboxyamino)imidazole ribonucleotide mutase {ECO:0000255|HAMAP-Rule:MF_01929}; GN Name=purE {ECO:0000255|HAMAP-Rule:MF_01929}; OrderedLocusNames=MJ0616; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of N5-carboxyaminoimidazole CC ribonucleotide (N5-CAIR) to 4-carboxy-5-aminoimidazole CC ribonucleotide (CAIR). {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- CATALYTIC ACTIVITY: 5-carboxyamino-1-(5-phospho-D- CC ribosyl)imidazole = 5-amino-1-(5-phospho-D-ribosyl)imidazole-4- CC carboxylate. {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxylate from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole (N5-CAIR route): step 2/2. CC {ECO:0000255|HAMAP-Rule:MF_01929}. CC -!- SIMILARITY: Belongs to the AIR carboxylase family. Class I CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01929}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98611.1; -; Genomic_DNA. DR PIR; H64376; H64376. DR PDB; 2YWX; X-ray; 2.31 A; A=1-157. DR PDBsum; 2YWX; -. DR ProteinModelPortal; Q58033; -. DR SMR; Q58033; 1-157. DR STRING; 243232.MJ_0616; -. DR EnsemblBacteria; AAB98611; AAB98611; MJ_0616. DR KEGG; mja:MJ_0616; -. DR eggNOG; arCOG02464; Archaea. DR eggNOG; COG0041; LUCA. DR InParanoid; Q58033; -. DR KO; K01588; -. DR OMA; SDWATMR; -. DR PhylomeDB; Q58033; -. DR UniPathway; UPA00074; UER00943. DR EvolutionaryTrace; Q58033; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0034023; F:5-(carboxyamino)imidazole ribonucleotide mutase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.7700; -; 1. DR HAMAP; MF_01929; PurE_classI; 1. DR InterPro; IPR024694; N5-CAIR_mutase_PurE. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR PIRSF; PIRSF001338; AIR_carboxylase; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. DR TIGRFAMs; TIGR01162; purE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 157 N5-carboxyaminoimidazole ribonucleotide FT mutase. FT /FTId=PRO_0000074987. FT BINDING 8 8 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 11 11 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT BINDING 38 38 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01929}. FT STRAND 2 8 {ECO:0000244|PDB:2YWX}. FT HELIX 9 11 {ECO:0000244|PDB:2YWX}. FT HELIX 12 24 {ECO:0000244|PDB:2YWX}. FT STRAND 29 33 {ECO:0000244|PDB:2YWX}. FT TURN 36 38 {ECO:0000244|PDB:2YWX}. FT HELIX 40 49 {ECO:0000244|PDB:2YWX}. FT STRAND 53 62 {ECO:0000244|PDB:2YWX}. FT HELIX 65 70 {ECO:0000244|PDB:2YWX}. FT STRAND 77 82 {ECO:0000244|PDB:2YWX}. FT HELIX 86 88 {ECO:0000244|PDB:2YWX}. FT HELIX 89 96 {ECO:0000244|PDB:2YWX}. FT HELIX 112 123 {ECO:0000244|PDB:2YWX}. FT TURN 124 126 {ECO:0000244|PDB:2YWX}. FT HELIX 128 153 {ECO:0000244|PDB:2YWX}. SQ SEQUENCE 157 AA; 16951 MW; 398E2DDA35030078 CRC64; MICIIMGSES DLKIAEKAVN ILKEFGVEFE VRVASAHRTP ELVEEIVKNS KADVFIAIAG LAAHLPGVVA SLTTKPVIAV PVDAKLDGLD ALLSSVQMPP GIPVATVGID RGENAAILAL EILALKDENI AKKLIEYREK MKKKVYASDE KVKEMFK // ID PURP_METJA Reviewed; 361 AA. AC Q57600; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'-monophosphate synthetase {ECO:0000255|HAMAP-Rule:MF_01163}; DE EC=6.3.4.23 {ECO:0000255|HAMAP-Rule:MF_01163}; DE AltName: Full=5-aminoimidazole-4-carboxamide-1-beta-D-ribofuranosyl 5'-monophosphate--formate ligase {ECO:0000255|HAMAP-Rule:MF_01163}; GN Name=purP {ECO:0000255|HAMAP-Rule:MF_01163}; OrderedLocusNames=MJ0136; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES, AND ENZYME RP REGULATION. RX PubMed=15623504; DOI=10.1074/jbc.M413937200; RA Ownby K., Xu H., White R.H.; RT "A Methanocaldococcus jannaschii archaeal signature gene encodes for a RT 5-formaminoimidazole-4-carboxamide-1-(beta)-D-ribofuranosyl 5'- RT monophosphate synthetase: a new enzyme in purine biosynthesis."; RL J. Biol. Chem. 280:10881-10887(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) IN COMPLEXES WITH ATP AND RP SUBSTRATE, AND SUBUNIT. RX PubMed=18069798; DOI=10.1021/bi701406g; RA Zhang Y., White R.H., Ealick S.E.; RT "Crystal structure and function of 5-formaminoimidazole-4-carboxamide RT ribonucleotide synthetase from Methanocaldococcus jannaschii."; RL Biochemistry 47:205-217(2008). CC -!- FUNCTION: Catalyzes the ATP- and formate-dependent formylation of CC 5-aminoimidazole-4-carboxamide-1-beta-d-ribofuranosyl 5'- CC monophosphate (AICAR) to 5-formaminoimidazole-4-carboxamide-1- CC beta-d-ribofuranosyl 5'-monophosphate (FAICAR) in the absence of CC folates. {ECO:0000255|HAMAP-Rule:MF_01163, CC ECO:0000269|PubMed:15623504}. CC -!- CATALYTIC ACTIVITY: ATP + formate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole-4-carboxamide = ADP + phosphate + 5-formamido-1- CC (5-phospho-D-ribosyl)imidazole-4-carboxamide. {ECO:0000255|HAMAP- CC Rule:MF_01163}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:15623504}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:15623504}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. CC {ECO:0000269|PubMed:15623504}; CC -!- ENZYME REGULATION: Inhibited by ADP. CC {ECO:0000269|PubMed:15623504}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 6.25. {ECO:0000269|PubMed:15623504}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-formamido-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide from 5- CC amino-1-(5-phospho-D-ribosyl)imidazole-4-carboxamide (formate CC route): step 1/1. {ECO:0000255|HAMAP-Rule:MF_01163}. CC -!- SUBUNIT: Homohexamer. Dimer of trimers. CC {ECO:0000269|PubMed:18069798}. CC -!- SIMILARITY: Belongs to the phosphohexose mutase family. CC {ECO:0000255|HAMAP-Rule:MF_01163}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_01163}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98117.1; -; Genomic_DNA. DR PIR; H64316; H64316. DR PDB; 2R7K; X-ray; 2.10 A; A=1-361. DR PDB; 2R7L; X-ray; 2.10 A; A=1-361. DR PDB; 2R7M; X-ray; 2.30 A; A=1-361. DR PDB; 2R7N; X-ray; 2.40 A; A=1-361. DR PDBsum; 2R7K; -. DR PDBsum; 2R7L; -. DR PDBsum; 2R7M; -. DR PDBsum; 2R7N; -. DR ProteinModelPortal; Q57600; -. DR SMR; Q57600; 1-361. DR STRING; 243232.MJ_0136; -. DR EnsemblBacteria; AAB98117; AAB98117; MJ_0136. DR KEGG; mja:MJ_0136; -. DR eggNOG; arCOG04346; Archaea. DR eggNOG; COG1759; LUCA. DR InParanoid; Q57600; -. DR KO; K06863; -. DR OMA; CIHYFYS; -. DR PhylomeDB; Q57600; -. DR BioCyc; MetaCyc:MONOMER-14616; -. DR BRENDA; 6.3.4.23; 3260. DR UniPathway; UPA00074; UER00134. DR EvolutionaryTrace; Q57600; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 2. DR Gene3D; 3.40.50.20; -; 1. DR HAMAP; MF_01163; IMP_biosynth_PurP; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR023656; IMP_biosynth_PurP. DR InterPro; IPR009720; IMP_biosynth_PurP_C. DR InterPro; IPR010672; IMP_biosynth_PurP_N. DR InterPro; IPR016185; PreATP-grasp_dom. DR Pfam; PF06849; DUF1246; 1. DR Pfam; PF06973; DUF1297; 1. DR PIRSF; PIRSF004602; ATPgrasp_PurP; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; Magnesium; KW Manganese; Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 361 5-formaminoimidazole-4-carboxamide-1- FT (beta)-D-ribofuranosyl 5'-monophosphate FT synthetase. FT /FTId=PRO_0000148024. FT DOMAIN 116 348 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_01163}. FT NP_BIND 156 166 ATP. FT NP_BIND 199 202 ATP. FT METAL 297 297 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01163}. FT METAL 310 310 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_01163}. FT BINDING 27 27 Substrate. FT BINDING 94 94 Substrate. FT BINDING 230 230 ATP. FT BINDING 258 258 Substrate. FT HELIX 4 11 {ECO:0000244|PDB:2R7K}. FT STRAND 20 26 {ECO:0000244|PDB:2R7K}. FT HELIX 29 38 {ECO:0000244|PDB:2R7K}. FT STRAND 43 47 {ECO:0000244|PDB:2R7K}. FT TURN 49 51 {ECO:0000244|PDB:2R7N}. FT HELIX 53 57 {ECO:0000244|PDB:2R7K}. FT STRAND 62 66 {ECO:0000244|PDB:2R7K}. FT HELIX 70 74 {ECO:0000244|PDB:2R7K}. FT HELIX 76 84 {ECO:0000244|PDB:2R7K}. FT STRAND 87 89 {ECO:0000244|PDB:2R7K}. FT HELIX 93 99 {ECO:0000244|PDB:2R7K}. FT HELIX 101 106 {ECO:0000244|PDB:2R7K}. FT STRAND 112 114 {ECO:0000244|PDB:2R7K}. FT HELIX 116 120 {ECO:0000244|PDB:2R7K}. FT TURN 121 123 {ECO:0000244|PDB:2R7K}. FT HELIX 125 134 {ECO:0000244|PDB:2R7K}. FT STRAND 142 145 {ECO:0000244|PDB:2R7K}. FT HELIX 146 148 {ECO:0000244|PDB:2R7K}. FT STRAND 153 156 {ECO:0000244|PDB:2R7K}. FT STRAND 166 171 {ECO:0000244|PDB:2R7K}. FT HELIX 172 184 {ECO:0000244|PDB:2R7K}. FT STRAND 186 188 {ECO:0000244|PDB:2R7N}. FT HELIX 190 195 {ECO:0000244|PDB:2R7K}. FT STRAND 197 200 {ECO:0000244|PDB:2R7K}. FT STRAND 204 214 {ECO:0000244|PDB:2R7K}. FT TURN 215 218 {ECO:0000244|PDB:2R7K}. FT STRAND 219 232 {ECO:0000244|PDB:2R7K}. FT HELIX 233 236 {ECO:0000244|PDB:2R7K}. FT HELIX 241 245 {ECO:0000244|PDB:2R7K}. FT STRAND 253 260 {ECO:0000244|PDB:2R7K}. FT HELIX 265 267 {ECO:0000244|PDB:2R7K}. FT HELIX 268 285 {ECO:0000244|PDB:2R7K}. FT STRAND 292 300 {ECO:0000244|PDB:2R7K}. FT STRAND 306 315 {ECO:0000244|PDB:2R7K}. FT HELIX 317 322 {ECO:0000244|PDB:2R7K}. FT HELIX 329 331 {ECO:0000244|PDB:2R7K}. FT HELIX 339 353 {ECO:0000244|PDB:2R7K}. FT HELIX 356 358 {ECO:0000244|PDB:2R7K}. SQ SEQUENCE 361 AA; 40824 MW; 0B9928DDD41D4DB6 CRC64; MISKDEILEI FDKYNKDEIT IATLGSHTSL HILKGAKLEG FSTVCITMKG RDVPYKRFKV ADKFIYVDNF SDIKNEEIQE KLRELNSIVV PHGSFIAYCG LDNVENSFLV PMFGNRRILR WESERSLEGK LLREAGLRVP KKYESPEDID GTVIVKFPGA RGGRGYFIAS STEEFYKKAE DLKKRGILTD EDIANAHIEE YVVGTNFCIH YFYSPLKDEV ELLGMDKRYE SNIDGLVRIP AKDQLEMNIN PSYVITGNIP VVIRESLLPQ VFEMGDKLVA KAKELVPPGM IGPFCLQSLC NENLELVVFE MSARVDGGTN SFMNGGPYSF LYNGEPLSMG QRIAREIKMA LQLDMIDKII S // ID PYCA_METJA Reviewed; 501 AA. AC Q58626; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=Pyruvate carboxylase subunit A; DE EC=6.4.1.1; DE AltName: Full=Pyruvic carboxylase A; GN Name=pycA; OrderedLocusNames=MJ1229; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-12, FUNCTION, AND MASS SPECTROMETRY. RX PubMed=11195096; DOI=10.1007/s002030000225; RA Mukhopadhyay B., Patel V.J., Wolfe R.S.; RT "A stable archaeal pyruvate carboxylase from the hyperthermophile RT Methanococcus jannaschii."; RL Arch. Microbiol. 174:406-414(2000). CC -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, CC involving the ATP-dependent carboxylation of the covalently CC attached biotin in the first step and the transfer of the carboxyl CC group to pyruvate in the second. {ECO:0000269|PubMed:11195096}. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate + CC oxaloacetate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC -!- ENZYME REGULATION: Inhibited by magnesium, when its concentration CC exceeded the ATP one, and by high concentration of ATP and alpha- CC ketoglutarate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5.; CC Temperature dependence: CC Optimum temperature is 80-90 degrees Celsius.; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Heterooctamer of four A and four B subunits. CC -!- MASS SPECTROMETRY: Mass=55500; Method=MALDI; Range=1-501; CC Evidence={ECO:0000269|PubMed:11195096}; CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC -!- SIMILARITY: Contains 1 biotin carboxylation domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99232.1; -; Genomic_DNA. DR PIR; D64453; D64453. DR ProteinModelPortal; Q58626; -. DR SMR; Q58626; 1-445. DR STRING; 243232.MJ_1229; -. DR EnsemblBacteria; AAB99232; AAB99232; MJ_1229. DR KEGG; mja:MJ_1229; -. DR eggNOG; arCOG01590; Archaea. DR eggNOG; COG0439; LUCA. DR InParanoid; Q58626; -. DR KO; K01959; -. DR OMA; EAPSPIM; -. DR PhylomeDB; Q58626; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004075; F:biotin carboxylase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.20; -; 1. DR InterPro; IPR004549; Acetyl_CoA_COase_biotin_COase. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005481; BC-like_N. DR InterPro; IPR011764; Biotin_carboxylation_dom. DR InterPro; IPR005482; Biotin_COase_C. DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd. DR InterPro; IPR016185; PreATP-grasp_dom. DR InterPro; IPR011054; Rudment_hybrid_motif. DR Pfam; PF02785; Biotin_carb_C; 1. DR Pfam; PF00289; Biotin_carb_N; 1. DR Pfam; PF02786; CPSase_L_D2; 1. DR SMART; SM00878; Biotin_carb_C; 1. DR SUPFAM; SSF51246; SSF51246; 1. DR SUPFAM; SSF52440; SSF52440; 1. DR TIGRFAMs; TIGR00514; accC; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS50979; BC; 1. DR PROSITE; PS00866; CPSASE_1; 1. DR PROSITE; PS00867; CPSASE_2; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; Direct protein sequencing; KW Gluconeogenesis; Ligase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Pyruvate; KW Reference proteome. FT CHAIN 1 501 Pyruvate carboxylase subunit A. FT /FTId=PRO_0000146828. FT DOMAIN 1 445 Biotin carboxylation. FT DOMAIN 120 316 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. FT ACT_SITE 291 291 {ECO:0000255}. FT BINDING 116 116 ATP. {ECO:0000250}. FT BINDING 200 200 ATP. {ECO:0000250}. FT BINDING 235 235 ATP. {ECO:0000250}. SQ SEQUENCE 501 AA; 55403 MW; 04D2E401892F872F CRC64; MFNKVLIANR GEIAIRIIRA CWELGIKTVA VYSEADKRSL HATLADEAYC IGPAPAAKSY LNIDAILNVA EKAKVDAIHP GYGFLAENAE FARAVKKAGF EFIGPNPDAI EAMGSKINAK KIMKKAGVPL IPGSEGAIED IDEAIEIAEA IGFPVVVKAS AGGGGMGMSV AYSKEELKEV IESARNIAKS AFGDPTVFIE KYLENPRHIE IQLLGDKHGN IIHLGDRECS IQRRHQKLIE EAPSPIMTEE LRERMGEAAI KAGKAINYDS AGTVEFLYEN GNFYFLEMNT RIQVEHTVTE QVTGIDLVKA MIKIAAGEEL TLKQEDVKIR GHAIECRINA EDPLNDFVPC PGKIKLYRSP GGPGVRIDSG VYGGAEIPPY YDSMIAKLIT YGNSREEAIA RMKRALREYV IIGVKTNIPF HRAVLEEENF LKGNISTHYV EQNMHKLREK MVKYALESRD LYSVVSEKVF EKNKKIAAAV GGLTMYISQI MKENEVNNKE W // ID QUEC_METJA Reviewed; 232 AA. AC Q58742; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 25-JUL-2006, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=7-cyano-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE EC=6.3.4.20 {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=7-cyano-7-carbaguanine synthase {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=Archaeosine biosynthesis protein QueC {ECO:0000255|HAMAP-Rule:MF_01633}; DE AltName: Full=PreQ(0) synthase {ECO:0000255|HAMAP-Rule:MF_01633}; GN Name=queC {ECO:0000255|HAMAP-Rule:MF_01633}; OrderedLocusNames=MJ1347; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent conversion of 7-carboxy-7- CC deazaguanine (CDG) to 7-cyano-7-deazaguanine (preQ(0)). CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- CATALYTIC ACTIVITY: 7-carboxy-7-carbaguanine + NH(3) + ATP = 7- CC cyano-7-carbaguanine + ADP + phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01633}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01633}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01633}. CC -!- SIMILARITY: Belongs to the QueC family. {ECO:0000255|HAMAP- CC Rule:MF_01633}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99356.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99356.1; ALT_INIT; Genomic_DNA. DR PIR; B64468; B64468. DR ProteinModelPortal; Q58742; -. DR STRING; 243232.MJ_1347; -. DR DNASU; 1452250; -. DR EnsemblBacteria; AAB99356; AAB99356; MJ_1347. DR KEGG; mja:MJ_1347; -. DR eggNOG; arCOG00039; Archaea. DR eggNOG; COG0603; LUCA. DR InParanoid; Q58742; -. DR KO; K06920; -. DR OMA; EKTWSCY; -. DR PhylomeDB; Q58742; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008616; P:queuosine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_01633; QueC; 1. DR InterPro; IPR018317; QueC. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF06508; QueC; 1. DR PIRSF; PIRSF006293; ExsB; 1. DR TIGRFAMs; TIGR00364; TIGR00364; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Metal-binding; KW Nucleotide-binding; Reference proteome; Zinc. FT CHAIN 1 232 7-cyano-7-deazaguanine synthase. FT /FTId=PRO_0000107287. FT NP_BIND 7 17 ATP. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 195 195 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 206 206 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 209 209 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. FT METAL 212 212 Zinc. {ECO:0000255|HAMAP-Rule:MF_01633}. SQ SEQUENCE 232 AA; 26029 MW; CEB27A7BC62987D6 CRC64; MKAITVLSGG LDSTVVTLIA KDLGYEVTAI TFNYGQRAAK REINSAKKIC EILGIEHIVV DLPFVKQFGK SSLITEKEIP TLKMEELDSE KAYETMKAVW VPARNVIMFG IASGFAEALD AEKIFIGINK EEGVTFPDNT IEFVEAFNKV LEYGTLNKVK IEAPLYDKTK EEIVKLGAEL EKKLGVEVLK YSYSCYHDNG EDFLHCGKCE SCMRRKRAFL MAGVEDKTKY IE // ID QUED_METJA Reviewed; 163 AA. AC Q58668; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Putative 6-carboxy-5,6,7,8-tetrahydropterin synthase; DE Short=CPH4 synthase; DE EC=4.1.2.50; DE AltName: Full=Archaeosine biosynthesis protein QueD; GN Name=queD; OrderedLocusNames=MJ1272; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of 7,8-dihydroneopterin CC triphosphate (H2NTP) to 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) CC and acetaldehyde. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 7,8-dihydroneopterin 3'-triphosphate + H(2)O = CC 6-carboxy-5,6,7,8-tetrahydropterin + acetaldehyde + triphosphate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC -!- MISCELLANEOUS: The active site is at the interface between 2 CC subunits. The proton acceptor Cys is on one subunit, and the CC charge relay system is on the other subunit (By similarity). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the PTPS family. QueD subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99278.1; -; Genomic_DNA. DR PIR; G64458; G64458. DR ProteinModelPortal; Q58668; -. DR STRING; 243232.MJ_1272; -. DR EnsemblBacteria; AAB99278; AAB99278; MJ_1272. DR KEGG; mja:MJ_1272; -. DR eggNOG; arCOG02172; Archaea. DR eggNOG; COG0720; LUCA. DR InParanoid; Q58668; -. DR KO; K01737; -. DR OMA; IGQGACY; -. DR PhylomeDB; Q58668; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR007115; 6-PTP_synth/QueD. DR PANTHER; PTHR12589; PTHR12589; 2. DR Pfam; PF01242; PTPS; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 163 Putative 6-carboxy-5,6,7,8- FT tetrahydropterin synthase. FT /FTId=PRO_0000057931. FT ACT_SITE 26 26 Proton acceptor. {ECO:0000250}. FT ACT_SITE 70 70 Charge relay system. {ECO:0000250}. FT ACT_SITE 148 148 Charge relay system. {ECO:0000250}. FT METAL 18 18 Zinc. {ECO:0000250}. FT METAL 30 30 Zinc. {ECO:0000250}. FT METAL 32 32 Zinc. {ECO:0000250}. SQ SEQUENCE 163 AA; 18816 MW; 3CDF37E98EF9C8CC CRC64; MMLELNGLHA GLRFSSAHIV FGHPTCGVIH GHSYYVDVKL YGERAGDFKF VCDFKIIKKI VKEICDELDH KLILPKNHEH VYYELRDKTL YFKYENKEYS IPVEDVILLP IPSTTAEDLA IYFANEIADR LKNLGFSNIN WIEVSINEGI GQGACYRKYL EVK // ID PTR2_METJA Reviewed; 140 AA. AC Q58133; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 18-OCT-2001, sequence version 2. DT 11-MAY-2016, entry version 102. DE RecName: Full=HTH-type transcriptional regulator Ptr2; GN Name=ptr2; OrderedLocusNames=MJ0723; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=11226165; DOI=10.1093/emboj/20.1.146; RA Ouhammouch M., Geiduschek E.P.; RT "A thermostable platform for transcriptional regulation: the DNA- RT binding properties of two Lrp homologs from the hyperthermophilic RT archaeon Methanococcus jannaschii."; RL EMBO J. 20:146-156(2001). CC -!- FUNCTION: Participates in positive as well as negative regulation CC of transcription. Binds to its own promoter. CC -!- SUBUNIT: Homotetramer. CC -!- SIMILARITY: Contains 1 HTH asnC-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00319}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98719.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98719.1; ALT_INIT; Genomic_DNA. DR PIR; C64390; C64390. DR ProteinModelPortal; Q58133; -. DR SMR; Q58133; 1-140. DR STRING; 243232.MJ_0723; -. DR EnsemblBacteria; AAB98719; AAB98719; MJ_0723. DR KEGG; mja:MJ_0723; -. DR eggNOG; arCOG01580; Archaea. DR eggNOG; COG1522; LUCA. DR InParanoid; Q58133; -. DR KO; K03718; -. DR OMA; KKICPAI; -. DR PhylomeDB; Q58133; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.30.70.920; -; 1. DR InterPro; IPR000485; AsnC-type_HTH_dom. DR InterPro; IPR011008; Dimeric_a/b-barrel. DR InterPro; IPR019888; Tscrpt_reg_AsnC-typ. DR InterPro; IPR019887; Tscrpt_reg_AsnC/Lrp_C. DR InterPro; IPR019885; Tscrpt_reg_HTH_AsnC-type_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01037; AsnC_trans_reg; 1. DR Pfam; PF13404; HTH_AsnC-type; 1. DR PRINTS; PR00033; HTHASNC. DR SMART; SM00344; HTH_ASNC; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF54909; SSF54909; 1. DR PROSITE; PS00519; HTH_ASNC_1; 1. DR PROSITE; PS50956; HTH_ASNC_2; 1. PE 1: Evidence at protein level; KW Activator; Complete proteome; DNA-binding; Reference proteome; KW Repressor; Transcription; Transcription regulation. FT CHAIN 1 140 HTH-type transcriptional regulator Ptr2. FT /FTId=PRO_0000111753. FT DOMAIN 1 62 HTH asnC-type. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. FT DNA_BIND 20 39 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00319}. SQ SEQUENCE 140 AA; 15903 MW; B2135182FF834EC9 CRC64; MDEKDLKIIE ILMRDGRKSY TDIARELGTS ESSIRKRVKK LEEEGVIKGY TAIIDPSKIG YNVVALTGFD TEPDKFLNVA KELCKFPEVK KVFTSTGDHM IMTEIWAKDG KEFSDLIFNK IGKIEGIKKI CPAIILEQMK // ID PUR5_METJA Reviewed; 350 AA. AC Q57656; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Phosphoribosylformylglycinamidine cyclo-ligase; DE EC=6.3.3.1; DE AltName: Full=AIR synthase; DE AltName: Full=AIRS; DE AltName: Full=Phosphoribosyl-aminoimidazole synthetase; GN Name=purM; OrderedLocusNames=MJ0203; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + 2-(formamido)-N(1)-(5-phospho-D- CC ribosyl)acetamidine = ADP + phosphate + 5-amino-1-(5-phospho-D- CC ribosyl)imidazole. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 2/2. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the AIR synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98187.1; -; Genomic_DNA. DR PIR; D64325; D64325. DR ProteinModelPortal; Q57656; -. DR STRING; 243232.MJ_0203; -. DR EnsemblBacteria; AAB98187; AAB98187; MJ_0203. DR KEGG; mja:MJ_0203; -. DR eggNOG; arCOG00639; Archaea. DR eggNOG; COG0150; LUCA. DR InParanoid; Q57656; -. DR KO; K01933; -. DR OMA; NHCVNDI; -. DR PhylomeDB; Q57656; -. DR UniPathway; UPA00074; UER00129. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004641; F:phosphoribosylformylglycinamidine cyclo-ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00741; AIRS; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR004733; PurM_cligase. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00878; purM; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Purine biosynthesis; Reference proteome. FT CHAIN 1 350 Phosphoribosylformylglycinamidine cyclo- FT ligase. FT /FTId=PRO_0000148281. SQ SEQUENCE 350 AA; 38202 MW; C1F68B7884DFB293 CRC64; MVTYKDAGVD ISHEDKVIKA LVSQITFKRS DIKPAELGLH YAGAVEFGDY YLVLSTDGVG SKMIVAEMAN KFDTVGIDMI AMNVNDAICI GAEPIALVDY LAVGHITEEI AEQIGKGLNE GAKEANINIV GGETATLPDM IKGIDLAGTV LAIVKKDEII TGKDVKAGDV IVGLRSSGIH SNGLSLARKV FFDIAKLDIN DKLSYGKTVA EELLTPTRIY VKPVLEMIRD KDIEVKGLAH ITGGSFRKLK RLNDKVTYYI DNLPEPLPIF KEIQRLGNVP DEEMFRTFNM GIGFCVIVDE EDANKVIKIA NKYNIPAQVI GRVVDSLEVN GNKIVGKAVV KYNDKHIILE // ID PUS10_METJA Reviewed; 454 AA. AC Q60346; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=tRNA pseudouridine synthase Pus10; DE EC=5.4.99.-; DE AltName: Full=tRNA pseudouridine 54/55 synthase; DE Short=Psi54/55 synthase; GN Name=pus10; OrderedLocusNames=MJ0041; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=18952823; DOI=10.1261/rna.1276508; RA Gurha P., Gupta R.; RT "Archaeal Pus10 proteins can produce both pseudouridine 54 and 55 in RT tRNA."; RL RNA 14:2521-2527(2008). CC -!- FUNCTION: Responsible for synthesis of pseudouridine from uracil- CC 54 and uracil-55 in the psi GC loop of transfer RNAs. CC {ECO:0000269|PubMed:18952823}. CC -!- CATALYTIC ACTIVITY: tRNA uridine = tRNA pseudouridine. CC {ECO:0000269|PubMed:18952823}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98022.1; -; Genomic_DNA. DR PIR; A64305; A64305. DR ProteinModelPortal; Q60346; -. DR STRING; 243232.MJ_0041; -. DR EnsemblBacteria; AAB98022; AAB98022; MJ_0041. DR KEGG; mja:MJ_0041; -. DR eggNOG; arCOG01015; Archaea. DR eggNOG; COG1258; LUCA. DR InParanoid; Q60346; -. DR KO; K07583; -. DR OMA; PQTRWPC; -. DR PhylomeDB; Q60346; -. DR BRENDA; 5.4.99.25; 3260. DR BRENDA; 5.4.99.B25; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IDA:UniProtKB. DR HAMAP; MF_01893; Pus10_arch; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR005912; Pus10. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF02926; THUMP; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR01213; pseudo_Pus10arc; 1. DR PROSITE; PS51165; THUMP; 1. PE 1: Evidence at protein level; KW Complete proteome; Isomerase; Reference proteome; RNA-binding; KW tRNA processing. FT CHAIN 1 454 tRNA pseudouridine synthase Pus10. FT /FTId=PRO_0000106664. FT DOMAIN 100 206 THUMP. FT ACT_SITE 275 275 Nucleophile. {ECO:0000255}. FT BINDING 339 339 Substrate. {ECO:0000255}. FT BINDING 411 411 Substrate. {ECO:0000255}. SQ SEQUENCE 454 AA; 52927 MW; C91F61339D284209 CRC64; MASIINKQII SPTGRNMEII NYEILKKYPL CDRCFGRLYA KLLHTTNTER GRALKLYKAL ELEAKIKKAK EKGINYEEEL ELLKALAKSG VDEIRLEDIE IEKENCPWCR GIFNKQKMEK LLNKAIELLK EYDFDTFLIG THIPEEIKDL EKEIETEFME SIKQEFGREF GKMLAVRLDK APDKEYPDIV VHINPYTEEI YLQINPLFIK GRYRKLVRGI PQTRWPCRKC RGKGCELCNY TGKKYPISVE EIIAKPFLEA TKGVDAKFHG AGREDIDVRM LGDGRPFVLE IKEPKIRKID LNKIAEEINK DGRVEVLNLE FGVRKDKVIF KNTPHRKTYR ALVECSDKIT DEELKLLEKE LENRTIYQKT PKRVLHRRAD LERIRKVYKV KTSKVDDNHF EMIIYCDGGL YIKELISGDD GRTNPSVSSI LNKNCICKEL DVLKIHDNNL LEKG // ID PYRDB_METJA Reviewed; 306 AA. AC Q58070; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit; DE Short=DHOD B; DE Short=DHODase B; DE Short=DHOdehase B; DE EC=1.3.1.14; DE AltName: Full=Dihydroorotate oxidase B; DE AltName: Full=Orotate reductase (NADH); GN Name=pyrD; OrderedLocusNames=MJ0654; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of dihydroorotate to orotate CC with NAD(+) as electron acceptor. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + NAD(+) = orotate + NADH. CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000250}; CC Note=Binds 1 FMN per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the dihydroorotate dehydrogenase family. CC Type 1 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98649.1; -; Genomic_DNA. DR PIR; F64381; F64381. DR ProteinModelPortal; Q58070; -. DR STRING; 243232.MJ_0654; -. DR EnsemblBacteria; AAB98649; AAB98649; MJ_0654. DR KEGG; mja:MJ_0654; -. DR eggNOG; arCOG00603; Archaea. DR eggNOG; COG0167; LUCA. DR InParanoid; Q58070; -. DR KO; K17828; -. DR OMA; VYYRGYD; -. DR PhylomeDB; Q58070; -. DR UniPathway; UPA00070; UER00945. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004152; F:dihydroorotate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0004589; F:orotate reductase (NADH) activity; IEA:UniProtKB-EC. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IBA:GO_Central. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00224; DHO_dh_type1; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005720; Dihydroorotate_DH. DR InterPro; IPR024920; Dihydroorotate_DH_1. DR InterPro; IPR012135; Dihydroorotate_DH_1_2. DR InterPro; IPR001295; Dihydroorotate_DH_CS. DR Pfam; PF01180; DHO_dh; 1. DR PIRSF; PIRSF000164; DHO_oxidase; 1. DR TIGRFAMs; TIGR01037; pyrD_sub1_fam; 1. DR PROSITE; PS00911; DHODEHASE_1; 1. DR PROSITE; PS00912; DHODEHASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Flavoprotein; FMN; NAD; Oxidoreductase; KW Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 306 Dihydroorotate dehydrogenase B (NAD(+)), FT catalytic subunit. FT /FTId=PRO_0000148409. FT NP_BIND 47 48 FMN. {ECO:0000250}. FT NP_BIND 246 247 FMN. {ECO:0000250}. FT NP_BIND 268 269 FMN. {ECO:0000250}. FT REGION 71 75 Substrate binding. {ECO:0000250}. FT REGION 195 196 Substrate binding. {ECO:0000250}. FT ACT_SITE 133 133 Nucleophile. FT BINDING 23 23 FMN. {ECO:0000250}. FT BINDING 47 47 Substrate. {ECO:0000250}. FT BINDING 130 130 FMN. {ECO:0000250}. FT BINDING 130 130 Substrate. {ECO:0000250}. FT BINDING 168 168 FMN. {ECO:0000250}. FT BINDING 194 194 FMN; via carbonyl oxygen. {ECO:0000250}. FT BINDING 220 220 FMN; via amide nitrogen. {ECO:0000250}. SQ SEQUENCE 306 AA; 32940 MW; E3532389BA9FC7C3 CRC64; MGECMLKTNI CGIEFKNPVF LASGIMGETG SALKRIAKGG AGAVTTKSIG LNPNPGHKNP TIVEVYGGFL NAMGLPNPGV DEYLEEIEKV RDELNRMDVR IIGSIYGKDE EEFAEVAKKM ERYVDIIELN ISCPHAKGYG ATIGQNPDLS YDVCKAVKKA VKIPVFAKLT PNVTDIIEIA QAVVDAGVDG LVAINTVRGM AIDIRAKKPI LANKFGGLSG KAIKSIGIKV VWDLYENFDV PIIGVGGIMS GEDAIEYMMA GASAVQIGSG VYYRGYDIFK KVCDEIISFL KEENLTLEEI VGMAHE // ID PURL_METJA Reviewed; 733 AA. AC Q58660; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00420}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR amidotransferase II {ECO:0000255|HAMAP-Rule:MF_00420}; DE Short=FGAR-AT II {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Glutamine amidotransferase PurL {ECO:0000255|HAMAP-Rule:MF_00420}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit II {ECO:0000255|HAMAP-Rule:MF_00420}; GN Name=purL {ECO:0000255|HAMAP-Rule:MF_00420}; OrderedLocusNames=MJ1264; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC -!- SUBUNIT: Monomer. Part of the FGAM synthase complex composed of 1 CC PurL, 1 PurQ and 2 PurS subunits. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00420}. CC -!- SIMILARITY: Belongs to the FGAMS family. {ECO:0000255|HAMAP- CC Rule:MF_00420}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99270.1; -; Genomic_DNA. DR PIR; G64457; G64457. DR ProteinModelPortal; Q58660; -. DR STRING; 243232.MJ_1264; -. DR EnsemblBacteria; AAB99270; AAB99270; MJ_1264. DR KEGG; mja:MJ_1264; -. DR eggNOG; arCOG00641; Archaea. DR eggNOG; COG0046; LUCA. DR InParanoid; Q58660; -. DR KO; K01952; -. DR OMA; VMWQFAE; -. DR PhylomeDB; Q58660; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.1330.10; -; 2. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00420; PurL_2; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR010074; PRibForGlyAmidine_synth_PurL. DR InterPro; IPR016188; PurM-like_N. DR Pfam; PF00586; AIRS; 2. DR Pfam; PF02769; AIRS_C; 2. DR PIRSF; PIRSF001587; FGAM_synthase_II; 1. DR SUPFAM; SSF56042; SSF56042; 2. DR TIGRFAMs; TIGR01736; FGAM_synth_II; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Magnesium; KW Metal-binding; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 733 Phosphoribosylformylglycinamidine FT synthase subunit PurL. FT /FTId=PRO_0000100513. FT REGION 82 85 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT REGION 301 303 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT ACT_SITE 32 32 {ECO:0000255|HAMAP-Rule:MF_00420}. FT ACT_SITE 83 83 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT METAL 81 81 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT METAL 105 105 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT METAL 258 258 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT METAL 520 520 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT BINDING 35 35 ATP. {ECO:0000255|HAMAP-Rule:MF_00420}. FT BINDING 104 104 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT BINDING 230 230 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT BINDING 482 482 ATP. {ECO:0000255|HAMAP-Rule:MF_00420}. FT BINDING 519 519 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00420}. FT BINDING 522 522 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00420}. SQ SEQUENCE 733 AA; 80866 MW; E0923221CB37722D CRC64; MDENDLKYIE KVLGRKPNHI ELAMFENLWS EHCAYRTSKK LLRMFAKTVN EKTSKNIVVG IGDDAAVIRL KNDICLAIAM ESHNHPSYID PYNGAATGVG GIVRDVLSMG AKPIALLDPL RFGDIFGKEG DKVRWLIEGV VKGIGDYGNR IGVPTVGGEC EFDSSFDYNN LVNVVCVGLV KENEIITGKA KEPGLSLILI GSTGRDGIGG ASFASKDLTE ESEEERPSVQ VGDAFSEKCL IDAVLEAVKT GKVKAMKDLG AAGLSGASSE MCYGGGVGCE LYLENVVLRE PLTPYEIMVS ESQERMLLAV EPGSEEEIIE IFKKYELPAS VIGKTIPEKR IIAKYKGEVV VDLPLDLLCE APLYDREGKE DLKEKEDDKE KIKMPEDLNA VLLKLLESPN ICSKEWIYQQ YDHEVQIRTV VKPGKDAAVL RINEVYPMGI ALTTDCNSRY CKLNPYVGAV NAVAEAVRNL ATVGAEPIAM LDNLNFGNPE RPERFWQLAE CIKGLADAAE FFEIPVVGGN VSLYNETVIE GKEHPINPTP AIFVLGKVED VEKVPGVLDN KIKEGDILII TNETKDEMGG SEYYKVIHNT EEGRVPRVDL EKEKKIYEEV REVVKEGLVS EAVDCSRGGL AVALAKMAVL NNIGLEVDLT EYNKNNLRDD ILLFSETSGR IILAVRDENK DKVLSKLSSA YIIGKVGGSR LKIKINEKDV VNLDVEEMKK RYYEAFPKMM GEL // ID PURQ_METJA Reviewed; 230 AA. AC Q59042; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 120. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurQ {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_00421}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit I {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAR amidotransferase I {ECO:0000255|HAMAP-Rule:MF_00421}; DE Short=FGAR-AT I {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Glutaminase PurQ {ECO:0000255|HAMAP-Rule:MF_00421}; DE EC=3.5.1.2 {ECO:0000255|HAMAP-Rule:MF_00421}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit I {ECO:0000255|HAMAP-Rule:MF_00421}; GN Name=purQ {ECO:0000255|HAMAP-Rule:MF_00421}; OrderedLocusNames=MJ1648; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_00421}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- CATALYTIC ACTIVITY: L-glutamine + H(2)O = L-glutamate + NH(3). CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_00421}. CC -!- SUBUNIT: Part of the FGAM synthase complex composed of 1 PurL, 1 CC PurQ and 2 PurS subunits. {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00421}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|HAMAP-Rule:MF_00421}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99669.1; -; Genomic_DNA. DR PIR; F64505; F64505. DR ProteinModelPortal; Q59042; -. DR STRING; 243232.MJ_1648; -. DR EnsemblBacteria; AAB99669; AAB99669; MJ_1648. DR KEGG; mja:MJ_1648; -. DR eggNOG; arCOG00102; Archaea. DR eggNOG; COG0047; LUCA. DR InParanoid; Q59042; -. DR KO; K01952; -. DR OMA; HAEGRFY; -. DR PhylomeDB; Q59042; -. DR UniPathway; UPA00074; UER00128. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IBA:GO_Central. DR GO; GO:0004359; F:glutaminase activity; IEA:UniProtKB-EC. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IBA:GO_Central. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006541; P:glutamine metabolic process; IBA:GO_Central. DR GO; GO:0006164; P:purine nucleotide biosynthetic process; IBA:GO_Central. DR GO; GO:0009156; P:ribonucleoside monophosphate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_00421; PurQ; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR010075; PRibForGlyAmidine_synth_PurQ. DR PIRSF; PIRSF001586; FGAM_synth_I; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01737; FGAM_synth_I; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Glutamine amidotransferase; KW Hydrolase; Ligase; Nucleotide-binding; Purine biosynthesis; KW Reference proteome. FT CHAIN 1 230 Phosphoribosylformylglycinamidine FT synthase subunit PurQ. FT /FTId=PRO_0000100608. FT DOMAIN 2 230 Glutamine amidotransferase type-1. FT {ECO:0000255|HAMAP-Rule:MF_00421}. FT ACT_SITE 85 85 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00421}. FT ACT_SITE 202 202 {ECO:0000255|HAMAP-Rule:MF_00421}. FT ACT_SITE 204 204 {ECO:0000255|HAMAP-Rule:MF_00421}. SQ SEQUENCE 230 AA; 25417 MW; 978792753DE169E1 CRC64; MKIAVTKFLG TNCDLDVCHA VKLAGGEPEL VFFTQENLDS YKGAVIPGGF SYGDYLRAGA ISARTPIIKG LKKMVEEGKP VLGICNGAQI GLEAGFSKGT LTNNLNAKFI CKWVYIRVEN NKTPFTQYYK KGEVLKIPIA HAEGRFYADD ETLDYMYKNN MIVFKYCDET GEVTEEANPN GSIDNIAGVC NENQNCVLLM PHPERASEKI LGSDDGLKMF KGMIDYAKRI // ID PURS_METJA Reviewed; 83 AA. AC Q58988; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Phosphoribosylformylglycinamidine synthase subunit PurS {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAM synthase {ECO:0000255|HAMAP-Rule:MF_01926}; DE EC=6.3.5.3 {ECO:0000255|HAMAP-Rule:MF_01926}; DE AltName: Full=Formylglycinamide ribonucleotide amidotransferase subunit III {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAR amidotransferase III {ECO:0000255|HAMAP-Rule:MF_01926}; DE Short=FGAR-AT III {ECO:0000255|HAMAP-Rule:MF_01926}; DE AltName: Full=Phosphoribosylformylglycinamidine synthase subunit III {ECO:0000255|HAMAP-Rule:MF_01926}; GN Name=purS {ECO:0000255|HAMAP-Rule:MF_01926}; OrderedLocusNames=MJ1593; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RG RIKEN structural genomics initiative (RSGI); RT "Crystal structure of Methanocaldococcus jannaschII purs, one of the RT subunits of formylglycinamide ribonucleotide amidotransferase in the RT purine biosynthetic pathway."; RL Submitted (JUL-2011) to the PDB data bank. CC -!- FUNCTION: Part of the phosphoribosylformylglycinamidine synthase CC complex involved in the purines biosynthetic pathway. Catalyzes CC the ATP-dependent conversion of formylglycinamide ribonucleotide CC (FGAR) and glutamine to yield formylglycinamidine ribonucleotide CC (FGAM) and glutamate. The FGAM synthase complex is composed of CC three subunits. PurQ produces an ammonia molecule by converting CC glutamine to glutamate. PurL transfers the ammonia molecule to CC FGAR to form FGAM in an ATP-dependent manner. PurS interacts with CC PurQ and PurL and is thought to assist in the transfer of the CC ammonia molecule from PurQ to PurL. {ECO:0000255|HAMAP- CC Rule:MF_01926}. CC -!- CATALYTIC ACTIVITY: ATP + N(2)-formyl-N(1)-(5-phospho-D- CC ribosyl)glycinamide + L-glutamine + H(2)O = ADP + phosphate + 2- CC (formamido)-N(1)-(5-phospho-D-ribosyl)acetamidine + L-glutamate. CC {ECO:0000255|HAMAP-Rule:MF_01926}. CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via de novo pathway; CC 5-amino-1-(5-phospho-D-ribosyl)imidazole from N(2)-formyl-N(1)-(5- CC phospho-D-ribosyl)glycinamide: step 1/2. {ECO:0000255|HAMAP- CC Rule:MF_01926}. CC -!- SUBUNIT: Homodimer. Part of the FGAM synthase complex composed of CC 1 PurL, 1 PurQ and 2 PurS subunits (By similarity). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01926}. CC -!- SIMILARITY: Belongs to the PurS family. {ECO:0000255|HAMAP- CC Rule:MF_01926}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99611.1; -; Genomic_DNA. DR PIR; H64498; H64498. DR PDB; 2YX5; X-ray; 2.30 A; A=1-83. DR PDBsum; 2YX5; -. DR ProteinModelPortal; Q58988; -. DR SMR; Q58988; 1-83. DR STRING; 243232.MJ_1593; -. DR EnsemblBacteria; AAB99611; AAB99611; MJ_1593. DR KEGG; mja:MJ_1593; -. DR eggNOG; arCOG04462; Archaea. DR eggNOG; COG1828; LUCA. DR InParanoid; Q58988; -. DR KO; K01952; -. DR OMA; VIENYRF; -. DR PhylomeDB; Q58988; -. DR UniPathway; UPA00074; UER00128. DR EvolutionaryTrace; Q58988; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004642; F:phosphoribosylformylglycinamidine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1280.10; -; 1. DR HAMAP; MF_01926; PurS; 1. DR InterPro; IPR003850; PurS. DR Pfam; PF02700; PurS; 1. DR ProDom; PD010362; FGAM_PurS; 1. DR TIGRFAMs; TIGR00302; TIGR00302; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; Ligase; KW Nucleotide-binding; Purine biosynthesis; Reference proteome. FT CHAIN 1 83 Phosphoribosylformylglycinamidine FT synthase subunit PurS. FT /FTId=PRO_0000100399. FT STRAND 2 10 {ECO:0000244|PDB:2YX5}. FT HELIX 17 28 {ECO:0000244|PDB:2YX5}. FT STRAND 41 47 {ECO:0000244|PDB:2YX5}. FT HELIX 52 65 {ECO:0000244|PDB:2YX5}. FT TURN 70 72 {ECO:0000244|PDB:2YX5}. FT STRAND 73 81 {ECO:0000244|PDB:2YX5}. SQ SEQUENCE 83 AA; 9696 MW; 461F8DDB0DF0B808 CRC64; MYKATVIIKL KKGVLNPEGR TIQRALNFLG FNNVKEVQTY KMIDIIMEGE NEEKVKEEVE EMCKKLLANP VIHDYEIKVE KIE // ID PYRC_METJA Reviewed; 423 AA. AC Q58885; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Dihydroorotase; DE Short=DHOase; DE EC=3.5.2.3; GN Name=pyrC; OrderedLocusNames=MJ1490; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: (S)-dihydroorotate + H(2)O = N-carbamoyl-L- CC aspartate. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; (S)-dihydroorotate from bicarbonate: step 3/3. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the DHOase family. Type 2 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99503.1; -; Genomic_DNA. DR PIR; A64486; A64486. DR ProteinModelPortal; Q58885; -. DR STRING; 243232.MJ_1490; -. DR MEROPS; M38.972; -. DR DNASU; 1452397; -. DR EnsemblBacteria; AAB99503; AAB99503; MJ_1490. DR KEGG; mja:MJ_1490; -. DR eggNOG; arCOG00689; Archaea. DR eggNOG; COG0044; LUCA. DR InParanoid; Q58885; -. DR KO; K01465; -. DR OMA; CHVHFRE; -. DR PhylomeDB; Q58885; -. DR UniPathway; UPA00070; UER00117. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004151; F:dihydroorotase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.30.40.10; -; 1. DR HAMAP; MF_00220_A; PyrC_type2_A; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR004722; DHOase. DR InterPro; IPR002195; Dihydroorotase_CS. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51338; SSF51338; 2. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00857; pyrC_multi; 1. DR PROSITE; PS00482; DIHYDROOROTASE_1; 1. DR PROSITE; PS00483; DIHYDROOROTASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 423 Dihydroorotase. FT /FTId=PRO_0000147270. FT METAL 56 56 Zinc 1. {ECO:0000250}. FT METAL 58 58 Zinc 1. {ECO:0000250}. FT METAL 137 137 Zinc 1; via carbamate group. FT {ECO:0000250}. FT METAL 137 137 Zinc 2; via carbamate group. FT {ECO:0000250}. FT METAL 168 168 Zinc 2. {ECO:0000250}. FT METAL 227 227 Zinc 2. {ECO:0000250}. FT METAL 302 302 Zinc 1. {ECO:0000250}. FT MOD_RES 137 137 N6-carboxylysine. {ECO:0000250}. SQ SEQUENCE 423 AA; 48104 MW; 3C15A023B1E9750B CRC64; MLLKNCRIIK DNKIIEGDIL IDENGRIKKI AKDIKVDDEI IDIKNSLVIP GVIDAHVHFR WGEEKKEDFL SGSLAGINGG VCFAIDMPNN KPPITTKELF YKKLEDCKKD SKINVFLNFG VTENNYLGTV EDAKAYKIFM VKSVGDLFIE DYSKLKDILN QNKLFCIHAE HKDVINENLK KYQLNSWIDH CKIRDEKSEV EAVKEVIKNL KIIDRQSNKK PHVHFCHIST KEALYLIKKV RQELKNIKIT VEVTPHHIYL NKDMAEELKG FGKFNPPLRE KDDNIALIKG IVNKDVDIIA SDHAPHLLED KLKNVKNCPS GIPGIETIVP LTLNLVNKGL ISLFDAIRVL SKNPAKIFNI NNKIEEGNLA NLTIIDLKKE GKINAELFKS KAKFSPFDGW EVKGFPIYTV INGTLYEAYG CKC // ID PYREL_METJA Reviewed; 211 AA. AC Q59040; DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=PyrE-like protein; GN OrderedLocusNames=MJ1646; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the purine/pyrimidine CC phosphoribosyltransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99667.1; -; Genomic_DNA. DR PIR; D64505; D64505. DR ProteinModelPortal; Q59040; -. DR STRING; 243232.MJ_1646; -. DR EnsemblBacteria; AAB99667; AAB99667; MJ_1646. DR KEGG; mja:MJ_1646; -. DR eggNOG; arCOG00028; Archaea. DR eggNOG; COG0856; LUCA. DR InParanoid; Q59040; -. DR KO; K00762; -. DR OMA; DIHVDWS; -. DR PhylomeDB; Q59040; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR GO; GO:0009116; P:nucleoside metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.2020; -; 1. DR HAMAP; MF_01214; PyrE_like; 1. DR InterPro; IPR000836; PRibTrfase_dom. DR InterPro; IPR029057; PRTase-like. DR InterPro; IPR022854; PyrE-like. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR Pfam; PF00156; Pribosyltran; 1. DR SUPFAM; SSF53271; SSF53271; 1. DR SUPFAM; SSF88659; SSF88659; 1. DR PROSITE; PS00103; PUR_PYR_PR_TRANSFER; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 211 PyrE-like protein. FT /FTId=PRO_0000110810. SQ SEQUENCE 211 AA; 23306 MW; 61693F216CB2CEF1 CRC64; MREIMNKELL KKVIELKSNG LTIGEIAEEL NVSMETARYL VLNAEKLLKE EEKAIKLENV DIFIDWKNIG SSANRLKYIS SIIVDILKSR NIEFDTVVGV STSGVPIATL VASELGKELT IYIPKKHISE EGKKITGSIS QNFSAVNYKR AVIIDDVVTS GSTLKECIKQ LKEVCSPKLV VVLIDKSGLD EIEGVPLIPL IRIGAVNVEQ K // ID PYRH_METJA Reviewed; 226 AA. AC Q58656; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-AUG-2002, sequence version 2. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uridylate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UK {ECO:0000255|HAMAP-Rule:MF_01220}; DE EC=2.7.4.22 {ECO:0000255|HAMAP-Rule:MF_01220}; DE AltName: Full=Uridine monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMP kinase {ECO:0000255|HAMAP-Rule:MF_01220}; DE Short=UMPK {ECO:0000255|HAMAP-Rule:MF_01220}; GN Name=pyrH {ECO:0000255|HAMAP-Rule:MF_01220}; OrderedLocusNames=MJ1259; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible phosphorylation of UMP to UDP. CC {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- CATALYTIC ACTIVITY: ATP + UMP = ADP + UDP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- ENZYME REGULATION: Inhibited by UTP. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; UDP from UMP (UMPK route): step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- SUBUNIT: Homohexamer. {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01220}. CC -!- SIMILARITY: Belongs to the UMP kinase family. {ECO:0000255|HAMAP- CC Rule:MF_01220}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99262.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99262.1; ALT_INIT; Genomic_DNA. DR PIR; B64457; B64457. DR ProteinModelPortal; Q58656; -. DR SMR; Q58656; 1-225. DR STRING; 243232.MJ_1259; -. DR DNASU; 1452157; -. DR EnsemblBacteria; AAB99262; AAB99262; MJ_1259. DR KEGG; mja:MJ_1259; -. DR eggNOG; arCOG00858; Archaea. DR eggNOG; COG0528; LUCA. DR InParanoid; Q58656; -. DR KO; K09903; -. DR OMA; IMEYANI; -. DR PhylomeDB; Q58656; -. DR UniPathway; UPA00159; UER00275. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0033862; F:UMP kinase activity; IEA:UniProtKB-EC. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006561; P:proline biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1160.10; -; 1. DR HAMAP; MF_01220_A; PyrH_A; 1. DR InterPro; IPR001048; Asp/Glu/Uridylate_kinase. DR InterPro; IPR001057; Glu/AcGlu_kinase. DR InterPro; IPR011817; Uridylate_kinase. DR InterPro; IPR011818; Uridylate_kinase_arch/spir. DR PANTHER; PTHR21499:SF23; PTHR21499:SF23; 1. DR Pfam; PF00696; AA_kinase; 1. DR PIRSF; PIRSF005650; Uridylate_kin; 1. DR PRINTS; PR00474; GLU5KINASE. DR SUPFAM; SSF53633; SSF53633; 1. DR TIGRFAMs; TIGR02076; pyrH_arch; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Kinase; Nucleotide-binding; KW Pyrimidine biosynthesis; Reference proteome; Transferase. FT CHAIN 1 226 Uridylate kinase. FT /FTId=PRO_0000143917. FT NP_BIND 9 10 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT NP_BIND 116 122 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 46 46 UMP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 47 47 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 51 51 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 68 68 UMP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 142 142 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 143 143 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. FT BINDING 148 148 ATP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_01220}. FT BINDING 151 151 ATP. {ECO:0000255|HAMAP-Rule:MF_01220}. SQ SEQUENCE 226 AA; 24099 MW; 7052087EE2AE240D CRC64; MRIVFDLGGS VVMPKEGAKA EKIMEYANIF KKIKDEGHEV AIVVGGGKTA REYIEIGREL GASESFCDEL GIMATRMNAM ILITALGDYS IKKVPTSFEE AELILNLGKI PVMGGTHPGH TTDAVAASLA EFINADLLVI GTNVDGVYDK DPNKYEDAKK FDKMSAKELV DLAISSSLKA GSSSVVDLLA AKIIERAKLK VAVVKGTPEE LLNVSKGIIN GTIIEG // ID PYRK_METJA Reviewed; 257 AA. AC Q58841; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 119. DE RecName: Full=Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211}; DE AltName: Full=Dihydroorotate oxidase B, electron transfer subunit {ECO:0000255|HAMAP-Rule:MF_01211}; GN Name=pyrK {ECO:0000255|HAMAP-Rule:MF_01211}; OrderedLocusNames=MJ1446; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Responsible for channeling the electrons from the CC oxidation of dihydroorotate from the FMN redox center in the PyrD CC type B subunit to the ultimate electron acceptor NAD(+). CC {ECO:0000255|HAMAP-Rule:MF_01211}. CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211}; CC Note=Binds 1 [2Fe-2S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01211}; CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01211}; CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01211}; CC -!- PATHWAY: Pyrimidine metabolism; UMP biosynthesis via de novo CC pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_01211}. CC -!- SUBUNIT: Heterotetramer of 2 PyrK and 2 PyrD type B subunits. CC {ECO:0000255|HAMAP-Rule:MF_01211}. CC -!- SIMILARITY: Belongs to the PyrK family. {ECO:0000255|HAMAP- CC Rule:MF_01211}. CC -!- SIMILARITY: Contains 1 FAD-binding FR-type domain. CC {ECO:0000255|HAMAP-Rule:MF_01211}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99455.1; -; Genomic_DNA. DR PIR; E64480; E64480. DR ProteinModelPortal; Q58841; -. DR STRING; 243232.MJ_1446; -. DR DNASU; 1452350; -. DR EnsemblBacteria; AAB99455; AAB99455; MJ_1446. DR KEGG; mja:MJ_1446; -. DR eggNOG; arCOG02199; Archaea. DR eggNOG; COG0543; LUCA. DR InParanoid; Q58841; -. DR KO; K02823; -. DR OMA; MKCGIGV; -. DR PhylomeDB; Q58841; -. DR UniPathway; UPA00070; UER00945. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:UniProtKB-HAMAP. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0044205; P:'de novo' UMP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 2.10.240.10; -; 1. DR HAMAP; MF_01211; DHODB_Fe_S_bind; 1. DR InterPro; IPR012165; Cyt_c3_hydrogenase_gsu. DR InterPro; IPR019480; Dihydroorotate_DH_Fe-S-bd. DR InterPro; IPR023455; Dihydroorotate_DHASE_ETsu. DR InterPro; IPR017927; Fd_Rdtase_FAD-bd. DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd. DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl. DR Pfam; PF10418; DHODB_Fe-S_bind; 1. DR Pfam; PF00175; NAD_binding_1; 1. DR PIRSF; PIRSF006816; Cyc3_hyd_g; 1. DR SUPFAM; SSF63380; SSF63380; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51384; FAD_FR; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Electron transport; FAD; Flavoprotein; KW Iron; Iron-sulfur; Metal-binding; Pyrimidine biosynthesis; KW Reference proteome; Transport. FT CHAIN 1 257 Probable dihydroorotate dehydrogenase B FT (NAD(+)), electron transfer subunit. FT /FTId=PRO_0000148375. FT DOMAIN 2 89 FAD-binding FR-type. {ECO:0000255|HAMAP- FT Rule:MF_01211}. FT METAL 208 208 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_01211}. FT METAL 213 213 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_01211}. FT METAL 216 216 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_01211}. FT METAL 226 226 Iron-sulfur (2Fe-2S). {ECO:0000255|HAMAP- FT Rule:MF_01211}. SQ SEQUENCE 257 AA; 28908 MW; 08D463BFE1CD432D CRC64; MEKPVICRIK EIIEESPTVK TFVVDKDFDF KPGQFAMLWL PGVDEKPFGF SSKNSFSVAR VGEFTKKMHE LKEGDIIGVR GPYGTYFEPI GDKVLAVAGG IGAAPIITAV EEFSKQGIEI TTILGARTKE ELLFLDRFEK VSRLEICTDD GSFGFKGFTT EKMKEVLKEE KFDLIITCGP EIMMKKVVEI ANEYNIPVQV SMERYMKCGI GICGQCCVDD EGLCVCKDGP VFWGDKLKFI REFGKYKRDA SGKKIYY // ID PYCB_METJA Reviewed; 567 AA. AC Q58628; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=Pyruvate carboxylase subunit B; DE EC=6.4.1.1; DE AltName: Full=Pyruvic carboxylase B; GN Name=pycB; OrderedLocusNames=MJ1231; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 190-195; 260-270; 277-289; 277-289; 309-325; RP 328-358; 370-380; 386-409; 422-438; 491-506 AND 491-506, FUNCTION, AND RP MASS SPECTROMETRY. RX PubMed=11195096; DOI=10.1007/s002030000225; RA Mukhopadhyay B., Patel V.J., Wolfe R.S.; RT "A stable archaeal pyruvate carboxylase from the hyperthermophile RT Methanococcus jannaschii."; RL Arch. Microbiol. 174:406-414(2000). CC -!- FUNCTION: Pyruvate carboxylase catalyzes a 2-step reaction, CC involving the ATP-dependent carboxylation of the covalently CC attached biotin in the first step and the transfer of the carboxyl CC group to pyruvate in the second. {ECO:0000269|PubMed:11195096}. CC -!- CATALYTIC ACTIVITY: ATP + pyruvate + HCO(3)(-) = ADP + phosphate + CC oxaloacetate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC -!- ENZYME REGULATION: Inhibited by magnesium, when its concentration CC exceeded the ATP one, and by high concentration of ATP and alpha- CC ketoglutarate. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 8.5.; CC Temperature dependence: CC Optimum temperature is 80-90 degrees Celsius.; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC -!- SUBUNIT: Heterooctamer of four A and four B subunits. CC -!- MASS SPECTROMETRY: Mass=64160; Method=MALDI; Range=1-567; CC Evidence={ECO:0000269|PubMed:11195096}; CC -!- SIMILARITY: Contains 1 biotinyl-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU01066, ECO:0000305}. CC -!- SIMILARITY: Contains 1 carboxyltransferase domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99233.1; -; Genomic_DNA. DR PIR; F64453; F64453. DR ProteinModelPortal; Q58628; -. DR SMR; Q58628; 2-442. DR STRING; 243232.MJ_1231; -. DR EnsemblBacteria; AAB99233; AAB99233; MJ_1231. DR KEGG; mja:MJ_1231; -. DR eggNOG; arCOG02095; Archaea. DR eggNOG; COG0511; LUCA. DR eggNOG; COG5016; LUCA. DR InParanoid; Q58628; -. DR KO; K01960; -. DR OMA; TYALYPQ; -. DR PhylomeDB; Q58628; -. DR UniPathway; UPA00138; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008948; F:oxaloacetate decarboxylase activity; IEA:InterPro. DR GO; GO:0004736; F:pyruvate carboxylase activity; IEA:UniProtKB-EC. DR GO; GO:0006094; P:gluconeogenesis; IEA:UniProtKB-UniPathway. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001882; Biotin_BS. DR InterPro; IPR000089; Biotin_lipoyl. DR InterPro; IPR003379; Carboxylase_cons_dom. DR InterPro; IPR005776; OadA. DR InterPro; IPR000891; PYR_CT. DR InterPro; IPR011053; Single_hybrid_motif. DR Pfam; PF00364; Biotin_lipoyl; 1. DR Pfam; PF00682; HMGL-like; 1. DR Pfam; PF02436; PYC_OADA; 1. DR SUPFAM; SSF51230; SSF51230; 1. DR TIGRFAMs; TIGR01108; oadA; 1. DR PROSITE; PS00188; BIOTIN; 1. DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1. DR PROSITE; PS50991; PYR_CT; 1. PE 1: Evidence at protein level; KW ATP-binding; Biotin; Complete proteome; Direct protein sequencing; KW Gluconeogenesis; Ligase; Magnesium; Metal-binding; KW Multifunctional enzyme; Nucleotide-binding; Pyruvate; KW Reference proteome. FT CHAIN 1 567 Pyruvate carboxylase subunit B. FT /FTId=PRO_0000146830. FT DOMAIN 1 262 Carboxyltransferase. FT DOMAIN 492 567 Biotinyl-binding. {ECO:0000255|PROSITE- FT ProRule:PRU01066}. FT REGION 10 14 Substrate binding. {ECO:0000250}. FT METAL 11 11 Divalent metal cation. {ECO:0000250}. FT METAL 172 172 Divalent metal cation; via carbamate FT group. {ECO:0000250}. FT METAL 201 201 Divalent metal cation. {ECO:0000250}. FT METAL 203 203 Divalent metal cation. {ECO:0000250}. FT BINDING 81 81 Substrate. {ECO:0000250}. FT BINDING 337 337 Substrate. {ECO:0000250}. FT MOD_RES 172 172 N6-carboxylysine. {ECO:0000250}. FT MOD_RES 533 533 N6-biotinyllysine. {ECO:0000250, FT ECO:0000255|PROSITE-ProRule:PRU01066}. SQ SEQUENCE 567 AA; 63908 MW; 5E07800622545628 CRC64; MVKIVDTTFR DAQQSLIATR MRTEDMLPIA EKMDEVGFYS MEVWGGATFD ACIRYLNEDP WERLRALKKR IQNTPLQMLL RGQNLVGYRH YPDDIVEKFV IKAHENGIDI FRIFDALNDV RNMETAIKTA KKVGAEVQGA ICYTISPVHT IDQYVELAKK LEEMGCDSIC IKDMAGLLTP YEGYELVKRL KEEISLPIDV HSHCTSGLAP MTYLKVIEAG ADMVDCAISP FAMGTSQPPT ESIVVALKGT KYDTGLDLKL LNEIRDYFMK VREKYKMLFS PISQIVDARV LVYQVPGGML SNLVSQLKEQ GALDKFEEVL QEIPRVRKDL GYPPLVTPTS QIVGTQAVLN VLTEERYKII TNEVVNYVKG FYGKPPAPIN PELLKRVLDE GEKPITCRPA DLLPPEWEKV KKEAEEKGIV KKEEDILTYA LYPQIAVKFL RGELKAEPIP KEKDIGKILE IPTEYIVEVD GEKFEVKIEP KIGTELKRKK EVITAEMEGA VTSPFRGMVT KIKVKEGDKV KKGDVIVVLE AMKMEHPIES PVEGTVERIL IDEGDAVNVG DVIMIIK // ID PYRG_METJA Reviewed; 540 AA. AC Q58574; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=CTP synthase; DE EC=6.3.4.2; DE AltName: Full=CTP synthetase; DE AltName: Full=UTP--ammonia ligase; GN Name=pyrG; OrderedLocusNames=MJ1174; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent amination of UTP to CTP with CC either L-glutamine or ammonia as the source of nitrogen. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + UTP + L-glutamine = ADP + phosphate + CC CTP + L-glutamate. CC -!- ENZYME REGULATION: Allosterically activated by GTP, when glutamine CC is the substrate. Inhibited by CTP (By similarity). {ECO:0000250}. CC -!- PATHWAY: Pyrimidine metabolism; CTP biosynthesis via de novo CC pathway; CTP from UDP: step 2/2. CC -!- SIMILARITY: Belongs to the CTP synthase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99177.1; -; Genomic_DNA. DR PIR; E64446; E64446. DR ProteinModelPortal; Q58574; -. DR SMR; Q58574; 2-537. DR STRING; 243232.MJ_1174; -. DR EnsemblBacteria; AAB99177; AAB99177; MJ_1174. DR KEGG; mja:MJ_1174; -. DR eggNOG; arCOG00063; Archaea. DR eggNOG; COG0504; LUCA. DR InParanoid; Q58574; -. DR KO; K01937; -. DR OMA; FDHNITT; -. DR PhylomeDB; Q58574; -. DR UniPathway; UPA00159; UER00277. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003883; F:CTP synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0044210; P:'de novo' CTP biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR HAMAP; MF_01227; PyrG; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR004468; CTP_synthase. DR InterPro; IPR017456; CTP_synthase_N. DR InterPro; IPR017926; GATASE. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11550; PTHR11550; 1. DR Pfam; PF06418; CTP_synth_N; 1. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00337; PyrG; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Glutamine amidotransferase; Ligase; KW Nucleotide-binding; Pyrimidine biosynthesis; Reference proteome. FT CHAIN 1 540 CTP synthase. FT /FTId=PRO_0000138260. FT DOMAIN 292 540 Glutamine amidotransferase type-1. FT REGION 1 254 Aminator domain. FT ACT_SITE 387 387 Nucleophile. {ECO:0000250}. FT ACT_SITE 513 513 {ECO:0000250}. FT ACT_SITE 515 515 {ECO:0000250}. SQ SEQUENCE 540 AA; 61023 MW; 6DD879FC31DA8A01 CRC64; MKIMKFIFIT GGVISSLGKG ITAASLGRLL KARGFKVNMI KIDPYLQIDA GTMSPYEHGE VFVTEDGGES DLDLGHYERF IDENLTKNNN ITTGKIYWSV LTKERKGEYL GKTVQVIPHI TNEIKDWIKN LGEGYDITIV EIGGTVGDIE SLPFLEAIRQ FKKDVGKENV LYIHVSLLPY IRAAGELKTK PTQHSVKELR SIGIQPDILI CRTEMPISDK IREKLALFCD VDKEAVIEAR DARTIYEVPL NLEKEGLGKL VTKKLNLPDR EPDLDEWRKF VDRVINPLNE VTIGIVGKYV ELKDAYLSIT EALIHAGAKN DTKVNINWIH SERLESEEFE ELLDRYREDN QLDGILVPGG FGDRGVEGKI NAIKYAREND IPFLGICMGM QCAVIEFARN VCGLEGANST EFDENTKYPV VDLLPEQKEI DAKGGTMRLG AYPAILMEGT LAYKLYGRKE VYERHRHRYE VNPEYHEILE NHGLTISGKS PDGRLAEFIE ISKNRYFIAT QAHPEFKSRP NKPHPLFDGL VRASLGEKIK // ID R15PI_METJA Reviewed; 308 AA. AC Q57586; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=Ribose 1,5-bisphosphate isomerase; DE Short=R15P isomerase; DE Short=R15Pi; DE EC=5.3.1.29; DE AltName: Full=Ribulose 1,5-bisphosphate synthase; DE Short=RuBP synthase; GN OrderedLocusNames=MJ0122; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the isomerization of ribose 1,5-bisphosphate CC (R15P) to ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and CC substrate for RubisCO. Functions in an archaeal AMP degradation CC pathway, together with AMP phosphorylase and RubisCO (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1,5-bisphosphate = D-ribulose CC 1,5-bisphosphate. CC -!- SUBUNIT: Homohexamer; trimer of dimers. {ECO:0000250}. CC -!- MISCELLANEOUS: Reaction proceeds via a cis-phosphoenolate CC intermediate. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eIF-2B alpha/beta/delta subunits CC family. R15P isomerase subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98103.1; -; Genomic_DNA. DR PIR; B64315; B64315. DR ProteinModelPortal; Q57586; -. DR STRING; 243232.MJ_0122; -. DR EnsemblBacteria; AAB98103; AAB98103; MJ_0122. DR KEGG; mja:MJ_0122; -. DR eggNOG; arCOG01124; Archaea. DR eggNOG; COG1184; LUCA. DR InParanoid; Q57586; -. DR KO; K18237; -. DR OMA; DSAVRYF; -. DR PhylomeDB; Q57586; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005851; C:eukaryotic translation initiation factor 2B complex; IBA:GO_Central. DR GO; GO:0005085; F:guanyl-nucleotide exchange factor activity; IBA:GO_Central. DR GO; GO:0016853; F:isomerase activity; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0044249; P:cellular biosynthetic process; IEA:InterPro. DR GO; GO:0043547; P:positive regulation of GTPase activity; IBA:GOC. DR GO; GO:0006446; P:regulation of translational initiation; IBA:GO_Central. DR Gene3D; 1.20.120.420; -; 1. DR InterPro; IPR000649; IF-2B-related. DR InterPro; IPR011559; Initiation_fac_2B_a/b/d. DR InterPro; IPR027363; M1Pi_N. DR InterPro; IPR005250; Ribulose_e2b2. DR Pfam; PF01008; IF-2B; 1. DR TIGRFAMs; TIGR00524; eIF-2B_rel; 1. DR TIGRFAMs; TIGR00511; ribulose_e2b2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 308 Ribose 1,5-bisphosphate isomerase. FT /FTId=PRO_0000156103. FT REGION 24 27 Substrate binding. {ECO:0000250}. FT REGION 131 133 Substrate binding. {ECO:0000250}. FT REGION 208 209 Substrate binding. {ECO:0000250}. FT ACT_SITE 129 129 Proton acceptor. {ECO:0000250}. FT ACT_SITE 198 198 Proton donor. {ECO:0000250}. FT BINDING 67 67 Substrate. {ECO:0000250}. FT BINDING 234 234 Substrate. {ECO:0000250}. FT SITE 223 223 Plays a key role in hexamerization. FT {ECO:0000250}. SQ SEQUENCE 308 AA; 34518 MW; EC2BAE3E061E4FCE CRC64; MVFKMSEMDI IKETYEKIKN MEIRGAGRIG RAAAKALKEY ALKISHLNEE EFKNKMREAG NILISARPTA VSLPNVVKYV LKGLNEENPK ERVIERADEF INSSLKAIEN IGKFGANRIK DGDTILTHCN SEAAISVIKT AYDEGKDIKV FCTETRPRNQ GYLTAKTLYD YGIDVTLIVD SAVRYFIKEI DIVVVGADAI TANGCLVNKI GTSQIALIAN ESRVPFLTAA ETYKFHPKTI VGELIEIEER SPEEVAVFED KYKGIKIRNP AFDVTPAKYI DAIITEVGLI PPQGAWYIIE KYFGWLEK // ID QUEE_METJA Reviewed; 243 AA. AC Q59039; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=7-carboxy-7-deazaguanine synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE Short=CDG synthase {ECO:0000255|HAMAP-Rule:MF_00917}; DE EC=4.3.99.3 {ECO:0000255|HAMAP-Rule:MF_00917}; DE AltName: Full=Archaeosine biosynthesis protein QueE {ECO:0000255|HAMAP-Rule:MF_00917}; GN Name=queE {ECO:0000255|HAMAP-Rule:MF_00917}; OrderedLocusNames=MJ1645; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the complex heterocyclic radical-mediated CC conversion of 6-carboxy-5,6,7,8-tetrahydropterin (CPH4) to 7- CC carboxy-7-deazaguanine (CDG), a step common to the biosynthetic CC pathways of all 7-deazapurine-containing compounds. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- CATALYTIC ACTIVITY: 6-carboxy-5,6,7,8-tetrahydropterin = 7- CC carboxy-7-carbaguanine + NH(3). {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=S-adenosyl-L-methionine; Xref=ChEBI:CHEBI:59789; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC Note=Binds 1 S-adenosyl-L-methionine per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00917}; CC -!- PATHWAY: Purine metabolism; 7-cyano-7-deazaguanine biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00917}. CC -!- SIMILARITY: Belongs to the radical SAM superfamily. 7-carboxy-7- CC deazaguanine synthase family. {ECO:0000255|HAMAP-Rule:MF_00917}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99666.1; -; Genomic_DNA. DR PIR; C64505; C64505. DR ProteinModelPortal; Q59039; -. DR STRING; 243232.MJ_1645; -. DR EnsemblBacteria; AAB99666; AAB99666; MJ_1645. DR KEGG; mja:MJ_1645; -. DR eggNOG; arCOG02173; Archaea. DR eggNOG; COG0602; LUCA. DR InParanoid; Q59039; -. DR OMA; WRYEVEP; -. DR PhylomeDB; Q59039; -. DR UniPathway; UPA00391; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016840; F:carbon-nitrogen lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:1904047; F:S-adenosyl-L-methionine binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00917; QueE; 1. DR InterPro; IPR024924; 7-CO-7-deazaguanine_synth-like. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF000370; QueE; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Magnesium; KW Metal-binding; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 243 7-carboxy-7-deazaguanine synthase. FT /FTId=PRO_0000107457. FT REGION 9 11 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT METAL 28 28 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 32 32 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT METAL 35 35 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00917}. FT BINDING 24 24 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 84 84 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00917}. FT BINDING 86 86 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00917}. SQ SEQUENCE 243 AA; 28280 MW; E035C9BE4188BCA2 CRC64; MIREIFNSIM GEGKYIGRRF IFVRFAGCPL NCVYCDEESK GYFNRVEKIP GSGEFETLQK MEIEDIINAI DKLKTPDLFA VSFTGGEPLL YHKQIKEIAE ILKDKGYRTF LESNGMFPER IFYFDIASID IKLKEHFEYI KDEDYEKLYK NELKTIKKLY NLNSDIYAKV VIMEETNIED VKIIAKDLSD IGNITLCIQP VTPHGNIKSP SQRKLFEIME ACGEYLKDNV MLTIQMHKYL GML // ID RAD50_METJA Reviewed; 1005 AA. AC Q58718; DT 26-SEP-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 112. DE RecName: Full=DNA double-strand break repair Rad50 ATPase {ECO:0000255|HAMAP-Rule:MF_00449}; GN Name=rad50 {ECO:0000255|HAMAP-Rule:MF_00449}; GN OrderedLocusNames=MJ1322; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] {ECO:0000244|PDB:3AUX, ECO:0000244|PDB:3AUY, ECO:0000244|PDB:3AV0} RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS) IN COMPLEX WITH ADP. RA Lim H.S., Kim J.S., Park Y.B., Gwon G.H., Cho Y.; RT "Crystal structure of the Mre11-Rad50-ATP S complex: understanding the RT interplay between Mre11 and Rad50."; RL Submitted (FEB-2011) to the PDB data bank. CC -!- FUNCTION: Part of the Rad50/Mre11 complex, which is involved in CC the early steps of DNA double-strand break (DSB) repair. The CC complex may facilitate opening of the processed DNA ends to aid in CC the recruitment of HerA and NurA. Rad50 controls the balance CC between DNA end bridging and DNA resection via ATP-dependent CC structural rearrangements of the Rad50/Mre11 complex. CC {ECO:0000255|HAMAP-Rule:MF_00449}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00449}; CC Note=Binds 1 zinc ion per homodimer. {ECO:0000255|HAMAP- CC Rule:MF_00449}; CC -!- SUBUNIT: Homodimer. Forms a heterotetramer composed of two Mre11 CC subunits and two Rad50 subunits. {ECO:0000255|HAMAP- CC Rule:MF_00449}. CC -!- DOMAIN: The two conserved Cys that bind zinc constitute the zinc- CC hook, which separates the large intramolecular coiled coil CC regions. The 2 Cys residues coordinate one molecule of zinc with CC the help of the 2 Cys residues of the zinc-hook of another Rad50 CC molecule, thereby forming a V-shaped homodimer. CC {ECO:0000255|HAMAP-Rule:MF_00449}. CC -!- SIMILARITY: Belongs to the SMC family. RAD50 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00449}. CC -!- SIMILARITY: Contains 1 zinc-hook domain. {ECO:0000255|HAMAP- CC Rule:MF_00449}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99331.1; -; Genomic_DNA. DR PIR; A64465; A64465. DR PDB; 3AUX; X-ray; 2.80 A; A=1-1005. DR PDB; 3AUY; X-ray; 2.70 A; A/B=1-1005. DR PDB; 3AV0; X-ray; 3.10 A; B=1-1005. DR PDB; 5DNY; X-ray; 3.11 A; B/D=1-1005. DR PDB; 5F3W; X-ray; 3.11 A; B/D=1-190, B/D=825-1005. DR PDBsum; 3AUX; -. DR PDBsum; 3AUY; -. DR PDBsum; 3AV0; -. DR PDBsum; 5DNY; -. DR PDBsum; 5F3W; -. DR ProteinModelPortal; Q58718; -. DR STRING; 243232.MJ_1322; -. DR EnsemblBacteria; AAB99331; AAB99331; MJ_1322. DR KEGG; mja:MJ_1322; -. DR eggNOG; arCOG00368; Archaea. DR eggNOG; COG0419; LUCA. DR InParanoid; Q58718; -. DR KO; K03546; -. DR OMA; LCKTPID; -. DR PhylomeDB; Q58718; -. DR EvolutionaryTrace; Q58718; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016887; F:ATPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006302; P:double-strand break repair; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_00449; RAD50; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022982; Rad50_ATPase_archaeal. DR InterPro; IPR013134; Zn_hook_RAD50. DR Pfam; PF04423; Rad50_zn_hook; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS51131; ZN_HOOK; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Coiled coil; Complete proteome; DNA damage; KW DNA repair; Hydrolase; Metal-binding; Nucleotide-binding; KW Reference proteome; Zinc. FT CHAIN 1 1005 DNA double-strand break repair Rad50 FT ATPase. FT /FTId=PRO_0000138654. FT DOMAIN 457 554 Zinc-hook. {ECO:0000255|HAMAP- FT Rule:MF_00449}. FT NP_BIND 35 40 ATP. {ECO:0000244|PDB:3AUX, FT ECO:0000244|PDB:3AUY}. FT NP_BIND 62 64 ATP. {ECO:0000244|PDB:3AUX, FT ECO:0000244|PDB:3AUY}. FT COILED 189 230 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 292 321 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 346 379 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 404 498 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 523 600 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 656 692 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COILED 800 834 {ECO:0000255|HAMAP-Rule:MF_00449}. FT COMPBIAS 915 953 Ala/Asp-rich (DA-box). FT METAL 502 502 Zinc. {ECO:0000255|HAMAP-Rule:MF_00449}. FT METAL 505 505 Zinc. {ECO:0000255|HAMAP-Rule:MF_00449}. FT BINDING 14 14 ATP. {ECO:0000244|PDB:3AUY, FT ECO:0000255|HAMAP-Rule:MF_00449}. FT BINDING 134 134 ATP. {ECO:0000255|HAMAP-Rule:MF_00449}. FT STRAND 3 13 {ECO:0000244|PDB:3AUY}. FT STRAND 16 22 {ECO:0000244|PDB:3AUY}. FT STRAND 25 32 {ECO:0000244|PDB:3AUY}. FT HELIX 38 50 {ECO:0000244|PDB:3AUY}. FT STRAND 54 56 {ECO:0000244|PDB:5DNY}. FT TURN 58 61 {ECO:0000244|PDB:3AUY}. FT STRAND 67 77 {ECO:0000244|PDB:3AUY}. FT STRAND 80 89 {ECO:0000244|PDB:3AUY}. FT STRAND 92 99 {ECO:0000244|PDB:3AUY}. FT STRAND 102 105 {ECO:0000244|PDB:3AUY}. FT HELIX 108 119 {ECO:0000244|PDB:3AUY}. FT HELIX 123 130 {ECO:0000244|PDB:3AUY}. FT HELIX 136 142 {ECO:0000244|PDB:3AUY}. FT HELIX 145 156 {ECO:0000244|PDB:3AUY}. FT HELIX 158 185 {ECO:0000244|PDB:3AUY}. FT TURN 186 188 {ECO:0000244|PDB:3AV0}. FT HELIX 827 858 {ECO:0000244|PDB:3AUY}. FT TURN 860 862 {ECO:0000244|PDB:3AUY}. FT HELIX 863 885 {ECO:0000244|PDB:3AUY}. FT STRAND 893 895 {ECO:0000244|PDB:3AUY}. FT STRAND 901 905 {ECO:0000244|PDB:3AUY}. FT STRAND 908 910 {ECO:0000244|PDB:3AUY}. FT HELIX 912 914 {ECO:0000244|PDB:3AUY}. FT HELIX 917 936 {ECO:0000244|PDB:3AUY}. FT STRAND 941 947 {ECO:0000244|PDB:3AUY}. FT TURN 948 951 {ECO:0000244|PDB:3AUY}. FT HELIX 954 966 {ECO:0000244|PDB:3AUY}. FT STRAND 971 978 {ECO:0000244|PDB:3AUY}. FT HELIX 980 985 {ECO:0000244|PDB:3AUY}. FT STRAND 987 997 {ECO:0000244|PDB:3AUY}. FT STRAND 999 1004 {ECO:0000244|PDB:3AUY}. SQ SEQUENCE 1005 AA; 119388 MW; 9BBBB48173E788F3 CRC64; MSMILKEIRM NNFKSHVNSR IKFEKGIVAI IGENGSGKSS IFEAVFFALF GAGSNFNYDT IITKGKKSVY VELDFEVNGN NYKIIREYDS GRGGAKLYKN GKPYATTISA VNKAVNEILG VDRNMFLNSI YIKQGEIAKF LSLKPSEKLE TVAKLLGIDE FEKCYQKMGE IVKEYEKRLE RIEGELNYKE NYEKELKNKM SQLEEKNKKL MEINDKLNKI KKEFEDIEKL FNEWENKKLL YEKFINKLEE RKRALELKNQ ELKILEYDLN TVVEARETLN RHKDEYEKYK SLVDEIRKIE SRLRELKSHY EDYLKLTKQL EIIKGDIEKL KEFINKSKYR DDIDNLDTLL NKIKDEIERV ETIKDLLEEL KNLNEEIEKI EKYKRICEEC KEYYEKYLEL EEKAVEYNKL TLEYITLLQE KKSIEKNIND LETRINKLLE ETKNIDIESI ENSLKEIEEK KKVLENLQKE KIELNKKLGE INSEIKRLKK ILDELKEVEG KCPLCKTPID ENKKMELINQ HKTQLNNKYT ELEEINKKIR EIEKDIEKLK KEIDKEENLK TLKTLYLEKQ SQIEELELKL KNYKEQLDEI NKKISNYVIN GKPVDEILED IKSQLNKFKN FYNQYLSAVS YLNSVDEEGI RNRIKEIENI VSGWNKEKCR EELNKLREDE REINRLKDKL NELKNKEKEL IEIENRRSLK FDKYKEYLGL TEKLEELKNI KDGLEEIYNI CNSKILAIDN IKRKYNKEDI EIYLNNKILE VNKEINDIEE RISYINQKLD EINYNEEEHK KIKELYENKR QELDNVREQK TEIETGIEYL KKDVESLKAR LKEMSNLEKE KEKLTKFVEY LDKVRRIFGR NGFQAYLREK YVPLIQKYLN EAFSEFDLPY SFVELTKDFE VRVHAPNGVL TIDNLSGGEQ IAVALSLRLA IANALIGNRV ECIILDEPTV YLDENRRAKL AEIFRKVKSI PQMIIITHHR ELEDVADVII NVKKDGNVSK VKING // ID RADB_METJA Reviewed; 212 AA. AC Q57702; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=DNA repair and recombination protein RadB; GN Name=radB; OrderedLocusNames=MJ0254; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. CC May regulate the cleavage reactions of the branch-structured DNA. CC Has a very weak ATPase activity that is not stimulated by DNA. CC Binds DNA but does not promote DNA strands exchange (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family. CC RadB subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98241.1; -; Genomic_DNA. DR PIR; G64331; G64331. DR ProteinModelPortal; Q57702; -. DR STRING; 243232.MJ_0254; -. DR EnsemblBacteria; AAB98241; AAB98241; MJ_0254. DR KEGG; mja:MJ_0254; -. DR eggNOG; arCOG00417; Archaea. DR eggNOG; COG0468; LUCA. DR InParanoid; Q57702; -. DR KO; K04484; -. DR OMA; TQVYGPP; -. DR PhylomeDB; Q57702; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00350; RadB; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C. DR InterPro; IPR011939; DNA_repair_and_recomb_RadB. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR Pfam; PF08423; Rad51; 1. DR PIRSF; PIRSF003336; RadB; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02237; recomb_radB; 1. DR PROSITE; PS50162; RECA_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 212 DNA repair and recombination protein FT RadB. FT /FTId=PRO_0000150113. FT NP_BIND 20 27 ATP. {ECO:0000255}. SQ SEQUENCE 212 AA; 23842 MW; 0BD1C9D5D68579CB CRC64; MLKEILLGNA EKGIITQIYG PPGVGKTNIC IINSINAVNS GKVIYIDTEG GLSIERIKQI ASNNYKIVLE NMIIYNAFDF YEQDKIIQKE LPLITNNASL IVVDNITSLY RLELSDEANK NIMLNKMLGN QVKTLLKLAK TNNLAVIITN QVRETVNGFE ASGGRLLEYW SKCIVRLEKL NGDRLAILEK HLHAGEERVK FRIVERGIEI ID // ID PYRI_METJA Reviewed; 149 AA. AC Q58801; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Aspartate carbamoyltransferase regulatory chain; GN Name=pyrI; OrderedLocusNames=MJ1406; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=10748118; DOI=10.1074/jbc.M909220199; RA Hack E.S., Vorobyova T., Sakash J.B., West J.M., Macol C.P., Herve G., RA Williams M.K., Kantrowitz E.R.; RT "Characterization of the aspartate transcarbamoylase from RT Methanococcus jannaschii."; RL J. Biol. Chem. 275:15820-15827(2000). CC -!- FUNCTION: Involved in allosteric regulation of aspartate CC carbamoyltransferase. {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBUNIT: Heterododecamer (2C3:3R2) of six catalytic PyrB chains CC organized as two trimers (C3), and six regulatory PyrI chains CC organized as three dimers (R2). CC -!- SIMILARITY: Belongs to the PyrI family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99414.1; -; Genomic_DNA. DR PIR; E64475; E64475. DR PDB; 2YWW; X-ray; 2.00 A; A/B=1-149. DR PDBsum; 2YWW; -. DR ProteinModelPortal; Q58801; -. DR SMR; Q58801; 8-149. DR STRING; 243232.MJ_1406; -. DR EnsemblBacteria; AAB99414; AAB99414; MJ_1406. DR KEGG; mja:MJ_1406; -. DR eggNOG; arCOG04229; Archaea. DR eggNOG; COG1781; LUCA. DR InParanoid; Q58801; -. DR KO; K00610; -. DR OMA; MNVPSDR; -. DR PhylomeDB; Q58801; -. DR BRENDA; 2.1.3.2; 3260. DR EvolutionaryTrace; Q58801; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009347; C:aspartate carbamoyltransferase complex; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006207; P:'de novo' pyrimidine nucleobase biosynthetic process; IEA:InterPro. DR GO; GO:0006221; P:pyrimidine nucleotide biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.20; -; 1. DR Gene3D; 3.30.70.140; -; 1. DR HAMAP; MF_00002; Asp_carb_tr_reg; 1. DR InterPro; IPR020545; Asp_carbamoyltransf_reg_N. DR InterPro; IPR002801; Asp_carbamoylTrfase_reg. DR InterPro; IPR020542; Asp_carbamoyltrfase_reg_C. DR Pfam; PF01948; PyrI; 1. DR Pfam; PF02748; PyrI_C; 1. DR ProDom; PD006194; Asp_carbamoylTrfase_reg; 1. DR SUPFAM; SSF54893; SSF54893; 1. DR SUPFAM; SSF57825; SSF57825; 1. DR TIGRFAMs; TIGR00240; ATCase_reg; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; KW Pyrimidine biosynthesis; Reference proteome; Zinc. FT CHAIN 1 149 Aspartate carbamoyltransferase regulatory FT chain. FT /FTId=PRO_0000142331. FT METAL 108 108 Zinc. {ECO:0000250}. FT METAL 113 113 Zinc. {ECO:0000250}. FT METAL 136 136 Zinc. {ECO:0000250}. FT METAL 139 139 Zinc. {ECO:0000250}. FT STRAND 13 22 {ECO:0000244|PDB:2YWW}. FT HELIX 26 33 {ECO:0000244|PDB:2YWW}. FT STRAND 41 49 {ECO:0000244|PDB:2YWW}. FT TURN 50 52 {ECO:0000244|PDB:2YWW}. FT STRAND 53 61 {ECO:0000244|PDB:2YWW}. FT HELIX 67 76 {ECO:0000244|PDB:2YWW}. FT STRAND 81 86 {ECO:0000244|PDB:2YWW}. FT STRAND 89 94 {ECO:0000244|PDB:2YWW}. FT STRAND 100 106 {ECO:0000244|PDB:2YWW}. FT HELIX 114 116 {ECO:0000244|PDB:2YWW}. FT STRAND 123 128 {ECO:0000244|PDB:2YWW}. FT TURN 129 132 {ECO:0000244|PDB:2YWW}. FT STRAND 133 136 {ECO:0000244|PDB:2YWW}. FT TURN 137 139 {ECO:0000244|PDB:2YWW}. SQ SEQUENCE 149 AA; 16907 MW; 192B446466DF0ECE CRC64; MIPMEELKVK KITNGTVIDH IDAGKALMVF KVLNVPKETS VMIAINVPSK KKGKKDILKI EGIELKKEDV DKISLISPDV TINIIRNGKV VEKLKPQIPD EIEGTLKCTN PNCITNKEKV RGKFKIESKN PLKIRCYYCE KFLNEVIFE // ID RADA_METJA Reviewed; 352 AA. AC Q49593; Q58279; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 13-APR-2016, entry version 101. DE RecName: Full=DNA repair and recombination protein RadA; GN Name=radA; OrderedLocusNames=MJ0869; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=8668545; DOI=10.1093/nar/24.11.2125; RA Sandler S.J., Satin L.H., Samra H.S., Clark A.J.; RT "recA-like genes from three archaean species with putative protein RT products similar to Rad51 and Dmc1 proteins of the yeast Saccharomyces RT cerevisiae."; RL Nucleic Acids Res. 24:2125-2132(1996). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in DNA repair and in homologous recombination. CC Binds and assemble on single-stranded DNA to form a nucleoprotein CC filament. Hydrolyzes ATP in a ssDNA-dependent manner and promotes CC DNA strand exchange between homologous DNA molecules. CC -!- SIMILARITY: Belongs to the eukaryotic RecA-like protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U45312; AAC44122.1; -; Genomic_DNA. DR EMBL; L77117; AAB98875.1; -; Genomic_DNA. DR PIR; E64408; E64408. DR ProteinModelPortal; Q49593; -. DR SMR; Q49593; 36-352. DR STRING; 243232.MJ_0869; -. DR EnsemblBacteria; AAB98875; AAB98875; MJ_0869. DR KEGG; mja:MJ_0869; -. DR eggNOG; arCOG00415; Archaea. DR eggNOG; COG0468; LUCA. DR InParanoid; Q49593; -. DR KO; K04483; -. DR OMA; RAYNSDM; -. DR PhylomeDB; Q49593; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00348; RadA_arch; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR013632; DNA_recomb/repair_Rad51_C. DR InterPro; IPR011938; DNA_recomb/repair_RadA. DR InterPro; IPR016467; DNA_recomb/repair_RecA-like. DR InterPro; IPR010995; DNA_repair_Rad51/TF_NusA_a-hlx. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR020588; RecA_ATP-bd. DR InterPro; IPR020587; RecA_monomer-monomer_interface. DR Pfam; PF08423; Rad51; 1. DR PIRSF; PIRSF005856; Rad51; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF47794; SSF47794; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR02236; recomb_radA; 1. DR PROSITE; PS50162; RECA_2; 1. DR PROSITE; PS50163; RECA_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA damage; DNA recombination; KW DNA-binding; Nucleotide-binding; Reference proteome. FT CHAIN 1 352 DNA repair and recombination protein FT RadA. FT /FTId=PRO_0000150095. FT NP_BIND 136 143 ATP. {ECO:0000255}. SQ SEQUENCE 352 AA; 39084 MW; 861579C0C59AA29C CRC64; MITFIYFFGN IIYYLPIYSY INNYKFMLMV IIMDDLTQLP GVGPTTAEKL KEAGYTDFMK IATASIGELT EIDGISEKAA ARIIEAAREL CNLGFKSGTE VLSQRKNIWK LSTGSKNLDE ILGGGLESQS VTEFAGMFGS GKTQIAHQAC VNLQCPERIV ADDAIKDEIL NEPKAVYIDT EGTFRPERIV QMAEALGLDG NEVLNNIFVA RAYNSDMQML YAENVENLIR EGHNIKLVIV DSLTSTFRTE YIGRGKLAER QQKLGRHMAT LNKLADIYNC VVIVTNQVAA RPDALFGPSE QAIGGHIVGH AATFRIFLRK AKGDKRVAKL YDSPHLPDAE AMFRITEKGI HD // ID RBL_METJA Reviewed; 425 AA. AC Q58632; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 108. DE RecName: Full=Ribulose bisphosphate carboxylase {ECO:0000255|HAMAP-Rule:MF_01133}; DE Short=RuBisCO {ECO:0000255|HAMAP-Rule:MF_01133}; DE EC=4.1.1.39 {ECO:0000255|HAMAP-Rule:MF_01133}; GN Name=rbcL {ECO:0000255|HAMAP-Rule:MF_01133}; OrderedLocusNames=MJ1235; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CATALYTIC ACTIVITY, ENZYME REGULATION, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10049390; RA Watson G.M.F., Yu J.-P., Tabita F.R.; RT "Unusual ribulose 1,5-bisphosphate carboxylase/oxygenase of anoxic RT Archaea."; RL J. Bacteriol. 181:1569-1575(1999). RN [3] RP ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=12730164; DOI=10.1128/JB.185.10.3049-3059.2003; RA Finn M.W., Tabita F.R.; RT "Synthesis of catalytically active form III ribulose 1,5-bisphosphate RT carboxylase/oxygenase in archaea."; RL J. Bacteriol. 185:3049-3059(2003). CC -!- FUNCTION: Catalyzes the addition of molecular CO(2) and H(2)O to CC ribulose 1,5-bisphosphate (RuBP), generating two molecules of 3- CC phosphoglycerate (3-PGA). Functions in an archaeal AMP degradation CC pathway, together with AMP phosphorylase and R15P isomerase. CC {ECO:0000255|HAMAP-Rule:MF_01133}. CC -!- CATALYTIC ACTIVITY: 2 3-phospho-D-glycerate + 2 H(+) = D-ribulose CC 1,5-bisphosphate + CO(2) + H(2)O. {ECO:0000255|HAMAP- CC Rule:MF_01133, ECO:0000269|PubMed:10049390}. CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + 2-phosphoglycolate = CC D-ribulose 1,5-bisphosphate + O(2). {ECO:0000255|HAMAP- CC Rule:MF_01133, ECO:0000269|PubMed:10049390}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01133}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01133}; CC -!- ENZYME REGULATION: Reversibly inhibited by O(2). CC {ECO:0000269|PubMed:10049390, ECO:0000269|PubMed:12730164}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Optimum temperature is 65 degrees Celsius. Highly thermostable. CC {ECO:0000269|PubMed:12730164}; CC -!- SUBUNIT: Homodimer. In contrast to form I RuBisCO, the form III CC RuBisCO is composed solely of large subunits. CC {ECO:0000269|PubMed:10049390, ECO:0000269|PubMed:12730164}. CC -!- MISCELLANEOUS: Because the Archaea possessing a type III RuBisCO CC are all anaerobic, it is most likely that only the carboxylase CC activity of RuBisCO, and not the competitive oxygenase activity CC (by which RuBP reacts with O(2) to form one molecule of 3- CC phosphoglycerate and one molecule of 2-phosphoglycolate), is CC biologically relevant in these strains. {ECO:0000255|HAMAP- CC Rule:MF_01133}. CC -!- SIMILARITY: Belongs to the RuBisCO large chain family. Type III CC subfamily. {ECO:0000255|HAMAP-Rule:MF_01133}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99239.1; -; Genomic_DNA. DR ProteinModelPortal; Q58632; -. DR STRING; 243232.MJ_1235; -. DR EnsemblBacteria; AAB99239; AAB99239; MJ_1235. DR KEGG; mja:MJ_1235; -. DR eggNOG; arCOG04443; Archaea. DR eggNOG; COG1850; LUCA. DR InParanoid; Q58632; -. DR KO; K01601; -. DR OMA; FTQDWAS; -. DR PhylomeDB; Q58632; -. DR BRENDA; 4.1.1.39; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0016984; F:ribulose-bisphosphate carboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006196; P:AMP catabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0015977; P:carbon fixation; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.110; -; 1. DR Gene3D; 3.30.70.150; -; 1. DR HAMAP; MF_01133; RuBisCO_L_type3; 1. DR InterPro; IPR017712; RuBisCO_III. DR InterPro; IPR000685; RuBisCO_lsu_C. DR InterPro; IPR017443; RuBisCO_lsu_fd_N. DR Pfam; PF00016; RuBisCO_large; 1. DR Pfam; PF02788; RuBisCO_large_N; 1. DR SUPFAM; SSF51649; SSF51649; 1. DR SUPFAM; SSF54966; SSF54966; 1. DR TIGRFAMs; TIGR03326; rubisco_III; 1. PE 1: Evidence at protein level; KW Carbon dioxide fixation; Complete proteome; Lyase; Magnesium; KW Metal-binding; Oxidoreductase; Reference proteome. FT CHAIN 1 425 Ribulose bisphosphate carboxylase. FT /FTId=PRO_0000062673. FT REGION 353 355 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT REGION 375 378 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT ACT_SITE 153 153 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT ACT_SITE 269 269 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT METAL 179 179 Magnesium; via carbamate group. FT {ECO:0000255|HAMAP-Rule:MF_01133}. FT METAL 181 181 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT METAL 182 182 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT BINDING 155 155 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT BINDING 270 270 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT BINDING 302 302 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01133}. FT SITE 309 309 Transition state stabilizer. FT {ECO:0000255|HAMAP-Rule:MF_01133}. FT MOD_RES 179 179 N6-carboxylysine. {ECO:0000255|HAMAP- FT Rule:MF_01133}. SQ SEQUENCE 425 AA; 47859 MW; C6F9F1653BA76039 CRC64; MDYINLNYRP NEGDLLSCMV IKGENLEKLA NEIAGESSIG TWTKVQTMKS DIYEKLRPKV YEIKEIGEEN GYKVGLIKIA YPLYDFEINN MPGVLAGIAG NIFGMKIAKG LRILDFRFPA EFVKAYKGPR FGIEGVRETL KIKERPLLGT IVKPKVGLKT EEHAKVAYEA WVGGVDLVKD DENLTSQEFN KFEDRIYKTL EMRDKAEEET GERKAYMPNI TAPYREMIRR AEIAEDAGSE YVMIDVVVCG FSAVQSFREE DFKFIIHAHR AMHAAMTRSR DFGISMLALA KIYRLLGVDQ LHIGTVVGKM EGGEKEVKAI RDEIVYDKVE ADNENKFFNQ DWFDIKPVFP VSSGGVHPRL VPKIVEILGR DLIIQAGGGV HGHPDGTRAG AKAMRAAIEA IIEGKSLEEK AEEVAELKKA LEYWK // ID RELE1_METJA Reviewed; 90 AA. AC Q60374; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Putative toxin RelE1; GN Name=relE1; OrderedLocusNames=MJ0071; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Its CC cognate antitoxin is RelB1 (Potential). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98049.1; -; Genomic_DNA. DR PIR; G64308; G64308. DR ProteinModelPortal; Q60374; -. DR STRING; 243232.MJ_0071; -. DR EnsemblBacteria; AAB98049; AAB98049; MJ_0071. DR KEGG; mja:MJ_0071; -. DR eggNOG; arCOG01665; Archaea. DR eggNOG; COG2026; LUCA. DR InParanoid; Q60374; -. DR OMA; YRVRIGK; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007712; RelE/ParE_toxin. DR Pfam; PF05016; ParE_toxin; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Toxin. FT CHAIN 1 90 Putative toxin RelE1. FT /FTId=PRO_0000106679. SQ SEQUENCE 90 AA; 10851 MW; 78902F645671F70A CRC64; MKFNVEIHKR VLKDLKDLPP SNLKKFKELI ETLKTNPIPK EKFDIKRLKG SDEVYRVRIG KFRVQYVVLW DDRIIIIRKI SRREGAYKNP // ID RELE3_METJA Reviewed; 88 AA. AC Q58503; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Toxin RelE3; DE EC=3.1.-.-; DE AltName: Full=MjRelE; DE AltName: Full=Putative endoribonuclease RelE; GN Name=relE3; Synonyms=relE; OrderedLocusNames=MJ1103; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) IN COMPLEX WITH RELB, SUBUNIT, RP AND MUTAGENESIS OF ARG-62. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=19712680; DOI=10.1016/j.jmb.2009.08.048; RA Francuski D., Saenger W.; RT "Crystal structure of the antitoxin-toxin protein complex RelB-RelE RT from Methanococcus jannaschii."; RL J. Mol. Biol. 393:898-908(2009). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Has CC RNase activity (By similarity). Is very toxic upon expression in CC E.coli. Its toxic activity is probably neutralized by the cognate CC antitoxin RelB3. {ECO:0000250}. CC -!- SUBUNIT: Forms heterodimers with RelB3 and possibly a CC heterotetramer RelE3-RelB3(2)-RelE3 from 2 heterodimers. The CC heterotetramer is probably not very stable in solution. CC {ECO:0000269|PubMed:19712680}. CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99106.1; -; Genomic_DNA. DR PIR; F64437; F64437. DR PDB; 3BPQ; X-ray; 2.20 A; B/D=1-88. DR PDBsum; 3BPQ; -. DR ProteinModelPortal; Q58503; -. DR STRING; 243232.MJ_1103; -. DR EnsemblBacteria; AAB99106; AAB99106; MJ_1103. DR KEGG; mja:MJ_1103; -. DR eggNOG; arCOG01665; Archaea. DR eggNOG; COG2026; LUCA. DR OMA; MKVLFAK; -. DR EvolutionaryTrace; Q58503; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR InterPro; IPR007712; RelE/ParE_toxin. DR Pfam; PF05016; ParE_toxin; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 88 Toxin RelE3. FT /FTId=PRO_0000107168. FT MUTAGEN 62 62 R->K,S: Inactivates toxin. FT {ECO:0000269|PubMed:19712680}. FT STRAND 4 6 {ECO:0000244|PDB:3BPQ}. FT HELIX 7 13 {ECO:0000244|PDB:3BPQ}. FT HELIX 18 34 {ECO:0000244|PDB:3BPQ}. FT STRAND 44 46 {ECO:0000244|PDB:3BPQ}. FT STRAND 50 58 {ECO:0000244|PDB:3BPQ}. FT STRAND 61 68 {ECO:0000244|PDB:3BPQ}. FT STRAND 71 79 {ECO:0000244|PDB:3BPQ}. FT HELIX 80 83 {ECO:0000244|PDB:3BPQ}. FT HELIX 84 86 {ECO:0000244|PDB:3BPQ}. SQ SEQUENCE 88 AA; 10562 MW; DD58E41BCBE59F5D CRC64; MKVLFAKTFV KDLKHVPGHI RKRIKLIIEE CQNSNSLNDL KLDIKKIKGY HNYYRIRVGN YRIGIEVNGD TIIFRRVLHR KSIYDYFP // ID RF1_METJA Reviewed; 421 AA. AC Q58239; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 11-MAY-2016, entry version 91. DE RecName: Full=Peptide chain release factor subunit 1; DE AltName: Full=Translation termination factor aRF1; GN Name=prf1; OrderedLocusNames=MJ0829; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=10788613; DOI=10.1016/S0014-5793(00)01466-6; RA Dontsova M., Frolova L., Vassilieva J., Piendl W., Kisselev L., RA Garber M.; RT "Translation termination factor aRF1 from the archaeon Methanococcus RT jannaschii is active with eukaryotic ribosomes."; RL FEBS Lett. 472:213-216(2000). CC -!- FUNCTION: Directs the termination of nascent peptide synthesis CC (translation) in response to the termination codons UAA, UAG and CC UGA. {ECO:0000269|PubMed:10788613}. CC -!- SUBUNIT: Heterodimer of two subunits, one of which binds GTP. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the eukaryotic release factor 1 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98828.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98828.1; ALT_INIT; Genomic_DNA. DR PIR; E64403; E64403. DR ProteinModelPortal; Q58239; -. DR STRING; 243232.MJ_0829; -. DR EnsemblBacteria; AAB98828; AAB98828; MJ_0829. DR KEGG; mja:MJ_0829; -. DR eggNOG; arCOG01742; Archaea. DR eggNOG; COG1503; LUCA. DR InParanoid; Q58239; -. DR KO; K03265; -. DR OMA; YRCDSEF; -. DR PhylomeDB; Q58239; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016149; F:translation release factor activity, codon specific; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.30; -; 1. DR Gene3D; 3.30.960.10; -; 1. DR HAMAP; MF_00424; Rel_fact_arch_1; 1. DR InterPro; IPR005140; eRF1_1_Pelota. DR InterPro; IPR005141; eRF1_2. DR InterPro; IPR005142; eRF1_3. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR020918; Peptide_chain-rel_aRF1. DR InterPro; IPR004403; Peptide_chain-rel_eRF1/aRF1. DR InterPro; IPR024049; Release_factor_eRF1/aRF1_N. DR PANTHER; PTHR10113; PTHR10113; 1. DR Pfam; PF03463; eRF1_1; 1. DR Pfam; PF03464; eRF1_2; 1. DR Pfam; PF03465; eRF1_3; 1. DR SMART; SM01194; eRF1_1; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR SUPFAM; SSF55481; SSF55481; 1. DR TIGRFAMs; TIGR03676; aRF1/eRF1; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 421 Peptide chain release factor subunit 1. FT /FTId=PRO_0000143174. SQ SEQUENCE 421 AA; 47508 MW; 6F3C642D466A8D5B CRC64; MASTDSKQLY LFKKMLKELK SKKGKGTELI SLYIPAGRRI SDVAQHLREE MSQASNIKSK STRKNVQSAI EAILQRLKLL KEPLEKGVVI FAGMVPRSGP GTEKMETYVI EPPEPIKTYI YRCDSEFYLE PLEEFLEDKD AYGVILVDRN EATIALVKGR NINILKKLTS GVPGKFKAGG QSARRLERLI DLAAHEFLQR VGQKANEQFL PLLQEKKLRG ILVGGPGHTK NEFVEGDYLH HELKKIVLDT FDLCYTEEFG IRELLEKAAP LLKDVELMKE REAVQRFLKE LIKEDGGLAC YGEKEVLEAL MMGAVDTLIV SEELEKYKVK IACNNCDYLE EKTVNKLELI KLEEELKNAQ CPKCGGALSI VEEKDYIEYL SELCEQSGAK LVTVSSETEE GAMILNAFKG IAAILRYKIH Q // ID RELB3_METJA Reviewed; 53 AA. AC P0CL56; DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 1. DT 04-MAR-2015, entry version 12. DE RecName: Full=Antitoxin RelB3; GN Name=relB3; Synonyms=relB; OrderedLocusNames=MJ1103.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, AND POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-52, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=19712680; DOI=10.1016/j.jmb.2009.08.048; RA Francuski D., Saenger W.; RT "Crystal structure of the antitoxin-toxin protein complex RelB-RelE RT from Methanococcus jannaschii."; RL J. Mol. Biol. 393:898-908(2009). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Probably neutralizes the toxic activity of cognate toxin RelE (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: Forms heterodimers with RelE and possibly a CC heterotetramer RelE3-RelB3(2)-RelE3 from 2 heterodimers. The CC heterotetramer is probably not very stable in solution. CC {ECO:0000269|PubMed:19712680}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 3BPQ; X-ray; 2.20 A; A/C=1-52. DR PDBsum; 3BPQ; -. DR EvolutionaryTrace; P0CL56; -. DR Proteomes; UP000000805; Chromosome. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 53 Antitoxin RelB3. FT /FTId=PRO_0000406203. FT HELIX 14 33 {ECO:0000244|PDB:3BPQ}. FT TURN 34 37 {ECO:0000244|PDB:3BPQ}. FT HELIX 43 47 {ECO:0000244|PDB:3BPQ}. SQ SEQUENCE 53 AA; 6440 MW; 6F309BD5CBD5CF5F CRC64; MRLKKRFKKF FISRKEYEKI EEILDIGLAK AMEETKDDEL LTYDEIKELL GDK // ID RGYR_METJA Reviewed; 1613 AA. AC Q58907; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 120. DE RecName: Full=Reverse gyrase; DE Includes: DE RecName: Full=Helicase; DE EC=3.6.4.12; DE Includes: DE RecName: Full=Topoisomerase; DE EC=5.99.1.3; DE Contains: DE RecName: Full=Mja r-Gyr intein; GN Name=rgy; OrderedLocusNames=MJ1512; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Modifies the topological state of DNA by introducing CC positive supercoils in an ATP-dependent process. It cleaves CC transiently a single DNA strand and remains covalently bound to CC the 5' DNA end through a tyrosine residue. May be involved in CC rewinding the DNA strands in the regions of the chromosome that CC have opened up to allow transcription or replication (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- DOMAIN: Both the DNA unwinding and positive supercoiling CC activities require the cooperation of both domains. The CC cooperative action between the helicase-like and the topoisomerase CC domains is specific. The helicase-like domain probably does not CC directly unwind DNA but acts more likely by driving ATP-dependent CC conformational changes within the whole enzyme, functioning more CC like a protein motor. The "latch" region of the N-terminal domain CC plays a regulatory role in the enzyme, repressing topoisomerase CC activity in the absence of ATP and therefore preventing the enzyme CC from acting as an ATP-independent relaxing enzyme; it also helps CC to coordinate nucleotide hydrolysis by the ATPase domain with the CC supercoiling activity of the topoisomerase domain (By similarity). CC {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- MISCELLANEOUS: This enzyme is the only unique feature of CC hyperthermophilic bacteria/archaea discovered so far. It appears CC to be essential for adaptation to life at high temperatures. CC -!- SIMILARITY: In the N-terminal section; belongs to the DEAD box CC helicase family. DDVD subfamily. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic CC type I/III topoisomerase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99531.1; -; Genomic_DNA. DR PIR; G64488; G64488. DR ProteinModelPortal; Q58907; -. DR STRING; 243232.MJ_1512; -. DR PRIDE; Q58907; -. DR EnsemblBacteria; AAB99531; AAB99531; MJ_1512. DR KEGG; mja:MJ_1512; -. DR eggNOG; arCOG01526; Archaea. DR eggNOG; arCOG03145; Archaea. DR eggNOG; COG1110; LUCA. DR InParanoid; Q58907; -. DR KO; K03170; -. DR OMA; GWVSAKN; -. DR PhylomeDB; Q58907; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:InterPro. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 1.10.290.10; -; 2. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. DR Gene3D; 3.40.50.140; -; 1. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01125; Reverse_gyrase; 1. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005736; Reverse_gyrase. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 3. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF01131; Topoisom_bac; 2. DR Pfam; PF01751; Toprim; 1. DR PRINTS; PR00379; INTEIN. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF51294; SSF51294; 3. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF55608; SSF55608; 1. DR SUPFAM; SSF56712; SSF56712; 2. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR01054; rgy; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW ATP-binding; Autocatalytic cleavage; Complete proteome; DNA-binding; KW Helicase; Hydrolase; Isomerase; Magnesium; Metal-binding; KW Nucleotide-binding; Protein splicing; Reference proteome; KW Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 866 Reverse gyrase, 1st part. {ECO:0000255}. FT /FTId=PRO_0000030353. FT CHAIN 867 1360 Mja r-Gyr intein. {ECO:0000255}. FT /FTId=PRO_0000030354. FT CHAIN 1361 1613 Reverse gyrase, 2nd part. {ECO:0000255}. FT /FTId=PRO_0000030355. FT DOMAIN 87 291 Helicase ATP-binding. FT DOMAIN 310 525 Helicase C-terminal. FT DOMAIN 550 712 Toprim. FT DOMAIN 1070 1199 DOD-type homing endonuclease. FT ZN_FING 10 30 C4-type. {ECO:0000250}. FT NP_BIND 100 107 ATP. {ECO:0000250}. FT REGION 556 1613 Topoisomerase I. FT MOTIF 203 206 DEAD box. FT ACT_SITE 1363 1363 For DNA cleavage activity. {ECO:0000250}. FT METAL 556 556 Magnesium 1; catalytic. {ECO:0000250}. FT METAL 681 681 Magnesium 1; catalytic. {ECO:0000250}. FT METAL 681 681 Magnesium 2. {ECO:0000250}. FT METAL 683 683 Magnesium 2. {ECO:0000250}. FT BINDING 83 83 ATP. {ECO:0000250}. SQ SEQUENCE 1613 AA; 188257 MW; 7170C4E120237AE3 CRC64; MIPMIYKEMC PNCNGEITSE RLAIGVCEKC LKEENVFEKL KLCEKLREEK TLKNLKDYCI IWNEFKEFEE FVKDLGFELL SIQKMWAKRV LKNKSFSIVV PTGVGKSFFG ILMSLFLAKK GKRCYIILPT TLLVKQTYEK ISSLTEKNNL NIRVVAYHSE LSTKEKKEVK ERIENNDYDV LITTSNYLTK NMPKCKFDFV FVDDVDALLK ASKNIDRTLK LLGFDEEIIN EAYKIIYLIK IGKIEDAMKK REILKKKISK IKHGCLIIAS ATGKSYGDRV KLYRELLDFE IGFGMNKLRD VVDIYDEEFS KEKILEYIKL FGSGGIVFVS IDYGVEKAQE IEKYLLENNI KAKLIHSKDK KGFDDFREGK IDVLIGVASY YGVLVRGLDM PERVRYAIFY GIPKFKIRLK EYINSLKEKG ELKEDINIEG KTEEEIRQII TEKLKIKNFS LRKEDDEYLL LIPDVKTYIQ ASGRTSRMTE FGLTKGASIV LVDEKEIFEA LKKYMLFMYE SEFKRIDEVN LEELIKKIDE DREKIKVGRA KGKVPDLLKS VLMVVESPNK ARTIANFFGK PSVRKINNRN VYEVCIGDLN LIITASGGHV FDLVTKEGFY GVKIENNLYI PIYTSIKKVN GEQFTDQKDL EELIKQLMEK GERVNAMDAK ENIEIIREIA DEVDAIFIAT DIDTEGEKIG YDIAINALPF NRNIYRVGFN EITKRAILKA VESFKKGEEL SLDENKVKGQ VVRRIEDRWI GFRLSQKLWE VFNKNYLSAG RVQTPVLGWI IERYNEHKIK VPYLSLKLEN DIYIGKIWED EFDKDEVEVE VKVYEKEIPP LPPFTTDTLL EEATKRFGLS TDEIMSIAQE LFELGLCLTP DTYVVLGDGR IETIEDIVNA KERNVLSLDL DNLSIKIDTA IKFWKLRYNG NLSKITLSNN YELKATPDHC LLVLRDNQLK WIPAKDIKEN DYIAMPFNYK VERKPISLLN LLKYLDITDV LIEFDENSTI FEKIAEYIRN NIKTSTKYKY LRNRRVPLKY LIEWNFDLDE IEKEAKYIYK SVAGTKKIPL FKLDERFWYF AGLVLGDGSI QDSKIRIAQT PLKDVKSILD ETFPFLHNWI SGNQVIISNP IIAEILEKLG MRNGKLNGII FSLPESYINA LIAGYFDTDG CFSLLYDKKA KKHNLRMVLT SKRRDVLEKI GIYLNSIGIL NTLHKSREVY SLIISNKSLE TFKEKIAKYL KIRKEAFING YKTYKKEHEE RFECDLLPVK EVFKKLTFEK GRKEILKDSK IHIENWYKEK TNNIPREKLK TVLRYANNSE HKEFLEKIVN GDISFVRVKK VENIPYDGYV YDLSIKHNQN FISNGVISHN CTYHRTSSTR VSLDGMRVAR EYLKLNNLED YLKNREYFME GAHECIRPTK PMNTDELIEF LKENNIKLTK NHIKVYDLIF RRFIASQMKE AVVEYEEIYI KDLDEKVEGY VDIKFDGWSR IYNLKLKKLP RIEKSSLKVL DKKLRKIPKV PLYDEGEVVK LMKERGIGRP STYAQIIKKL LDRGYVVKSK DKNKLIPTKL GIEVYNYLIN NYPHLISEER TRELEEIMDK IENGEVDYIE VLKALHEEIL SIR // ID RIBL_METJA Reviewed; 149 AA. AC Q58579; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 88. DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115}; DE EC=2.7.7.2 {ECO:0000269|PubMed:20822113}; DE AltName: Full=FMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_02115}; DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_02115}; GN Name=ribL; OrderedLocusNames=MJ1179; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC RP PARAMETERS, ENZYME REGULATION, GENE NAME, PATHWAY, SUBUNIT, AND RP MUTAGENESIS OF CYS-126 AND CYS-143. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=20822113; DOI=10.1021/bi100817q; RA Mashhadi Z., Xu H., Grochowski L.L., White R.H.; RT "Archaeal RibL: a new FAD synthetase that is air sensitive."; RL Biochemistry 49:8748-8755(2010). CC -!- FUNCTION: Catalyzes the transfer of the AMP portion of ATP to CC flavin mononucleotide (FMN) to produce flavin adenine dinucleotide CC (FAD) coenzyme. To a lesser extent, is also able to utilize other CC nucleotides such as CTP and GTP as substrates, producing the CC modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin CC guanine dinucleotide (FGD), respectively. Does not catalyze the CC reverse reaction to produce FMN and ATP from FAD and PPi. Does not CC function as a glycerol-3-phosphate cytidylyltransferase, as CC previously annotated in the complete genome. CC {ECO:0000269|PubMed:20822113}. CC -!- CATALYTIC ACTIVITY: ATP + FMN = diphosphate + FAD. CC {ECO:0000269|PubMed:20822113}. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; CC Evidence={ECO:0000269|PubMed:20822113}; CC Note=Divalent metal cations. The best activity is observed with CC Co(2+), where the activity is 4 and 2.5 times greater than that CC with Mg(2+) and Mn(2+), respectively. CC {ECO:0000269|PubMed:20822113}; CC -!- ENZYME REGULATION: Is inhibited by the product PPi. CC {ECO:0000269|PubMed:20822113}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=25 uM for ATP {ECO:0000269|PubMed:20822113}; CC KM=63 uM for FMN {ECO:0000269|PubMed:20822113}; CC KM=480 uM for CTP {ECO:0000269|PubMed:20822113}; CC Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates CC {ECO:0000269|PubMed:20822113}; CC Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates CC {ECO:0000269|PubMed:20822113}; CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: CC step 1/1. {ECO:0000269|PubMed:20822113}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20822113}. CC -!- MISCELLANEOUS: Alkylation of both Cys-126 and Cys-143 results in CC complete loss of enzymatic activity. CC {ECO:0000269|PubMed:20822113}. CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99182.1; -; Genomic_DNA. DR PIR; B64447; B64447. DR ProteinModelPortal; Q58579; -. DR STRING; 243232.MJ_1179; -. DR EnsemblBacteria; AAB99182; AAB99182; MJ_1179. DR KEGG; mja:MJ_1179; -. DR eggNOG; arCOG01222; Archaea. DR eggNOG; COG0615; LUCA. DR InParanoid; Q58579; -. DR KO; K14656; -. DR OMA; FAKKHAD; -. DR PhylomeDB; Q58579; -. DR BioCyc; MetaCyc:MONOMER-16487; -. DR BRENDA; 2.7.7.2; 3260. DR UniPathway; UPA00277; UER00407. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB. DR GO; GO:0002135; F:CTP binding; IDA:UniProtKB. DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:UniProtKB. DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB. DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB. DR GO; GO:0006747; P:FAD biosynthetic process; IDA:UniProtKB. DR GO; GO:0046444; P:FMN metabolic process; IDA:UniProtKB. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_02115; FAD_synth_arch; 1. DR InterPro; IPR004821; Cyt_trans-like. DR InterPro; IPR024902; FAD_synth_RibL. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01467; CTP_transf_like; 1. DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; FAD; Flavoprotein; FMN; KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 149 FAD synthase. FT /FTId=PRO_0000107202. FT NP_BIND 10 11 ATP. {ECO:0000255|HAMAP-Rule:MF_02115}. FT NP_BIND 15 18 ATP. {ECO:0000255|HAMAP-Rule:MF_02115}. FT BINDING 95 95 ATP. {ECO:0000255|HAMAP-Rule:MF_02115}. FT BINDING 123 123 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_02115}. FT MUTAGEN 126 126 C->S: 2-fold increase in activity with FT Mg(2+) but loss of activity with Co(2+) FT as cofactor. FT {ECO:0000269|PubMed:20822113}. FT MUTAGEN 143 143 C->S: Nearly no change in activity with FT Mg(2+) but loss of activity with Co(2+) FT as cofactor. FT {ECO:0000269|PubMed:20822113}. SQ SEQUENCE 149 AA; 17288 MW; 55FD11671ED94594 CRC64; MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP IIPEEQRREM VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD EETLKKELAK YNLYPEIVRF RGYKKCPFHS SFDIVKEIIR RFCNKEIKI // ID RIFK_METJA Reviewed; 132 AA. AC Q60365; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 05-APR-2011, sequence version 2. DT 11-NOV-2015, entry version 84. DE RecName: Full=Riboflavin kinase; DE Short=RFK; DE EC=2.7.1.161; DE AltName: Full=CTP-dependent riboflavin kinase; DE AltName: Full=CTP:riboflavin 5'-phosphotransferase; DE AltName: Full=Flavokinase; GN Name=ribK; OrderedLocusNames=MJ0056; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS, SUBSTRATE RP SPECIFICITY, GENE NAME, MASS SPECTROMETRY, AND SUBUNIT. RX PubMed=18245297; DOI=10.1128/JB.01900-07; RA Mashhadi Z., Zhang H., Xu H., White R.H.; RT "Identification and characterization of an archaeon-specific RT riboflavin kinase."; RL J. Bacteriol. 190:2615-2618(2008). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEX WITH CDP. RG New York structural genomics research consortium (NYSGRC); RT "Crystal structure of hypothetical protein from Methanococcus RT jannaschii bound to CDP."; RL Submitted (MAR-2007) to the PDB data bank. RN [4] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH RP REACTION PRODUCTS AND MAGNESIUM, STRUCTURE BY NMR, FUNCTION, CATALYTIC RP ACTIVITY, CHARACTERIZATION, SUBSTRATE SPECIFICITY, AND SUBUNIT. RX PubMed=18073108; DOI=10.1016/j.str.2007.09.027; RA Ammelburg M., Hartmann M.D., Djuranovic S., Alva V., Koretke K.K., RA Martin J., Sauer G., Truffault V., Zeth K., Lupas A.N., Coles M.; RT "A CTP-dependent archaeal riboflavin kinase forms a bridge in the RT evolution of cradle-loop barrels."; RL Structure 15:1577-1590(2007). CC -!- FUNCTION: Catalyzes the CTP-dependent phosphorylation of CC riboflavin (vitamin B2) to form flavin mononucleotide (FMN). Can CC also utilize UTP as the phosphate donor, although less CC efficiently, and it is unclear if ATP and GTP can also serve as CC substrates (PubMed:18245297) or not (PubMed:18073108). CC {ECO:0000269|PubMed:18073108, ECO:0000269|PubMed:18245297}. CC -!- CATALYTIC ACTIVITY: CTP + riboflavin = CDP + FMN. CC {ECO:0000269|PubMed:18073108, ECO:0000269|PubMed:18245297}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 1 magnesium ion per subunit. This ion is coordinated by CC a threonine and an asparagine, and by the alpha- and beta- CC phosphates of CDP.; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=159 uM for riboflavin {ECO:0000269|PubMed:18245297}; CC KM=1.8 mM for CTP {ECO:0000269|PubMed:18245297}; CC Vmax=1.3 umol/min/mg enzyme {ECO:0000269|PubMed:18245297}; CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from CC riboflavin (CTP route): step 1/1. CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:18073108, CC ECO:0000269|PubMed:18245297, ECO:0000269|Ref.3}. CC -!- MASS SPECTROMETRY: Mass=15218.1; Mass_error=10; CC Method=Electrospray; Range=1-132; CC Evidence={ECO:0000269|PubMed:18245297}; CC -!- SIMILARITY: Belongs to the archaeal riboflavin kinase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98036.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98036.1; ALT_INIT; Genomic_DNA. DR PIR; H64306; H64306. DR PDB; 2OYN; X-ray; 1.85 A; A=1-132. DR PDB; 2P3M; NMR; -; A=1-132. DR PDB; 2VBS; X-ray; 3.00 A; A=1-132. DR PDB; 2VBT; X-ray; 2.70 A; A=1-132. DR PDB; 2VBU; X-ray; 1.70 A; A=1-132. DR PDB; 2VBV; X-ray; 2.40 A; A/B=1-132. DR PDBsum; 2OYN; -. DR PDBsum; 2P3M; -. DR PDBsum; 2VBS; -. DR PDBsum; 2VBT; -. DR PDBsum; 2VBU; -. DR PDBsum; 2VBV; -. DR STRING; 243232.MJ_0056; -. DR EnsemblBacteria; AAB98036; AAB98036; MJ_0056. DR KEGG; mja:MJ_0056; -. DR eggNOG; arCOG01904; Archaea. DR eggNOG; COG1339; LUCA. DR InParanoid; Q60365; -. DR KO; K07732; -. DR BioCyc; MetaCyc:MONOMER-13864; -. DR BRENDA; 2.7.1.161; 3260. DR UniPathway; UPA00276; UER00929. DR EvolutionaryTrace; Q60365; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-HAMAP. DR GO; GO:0008531; F:riboflavin kinase activity; IEA:InterPro. DR GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro. DR Gene3D; 2.40.30.30; -; 1. DR HAMAP; MF_01285; Riboflavin_kinase; 1. DR InterPro; IPR023470; Riboflavin_kinase_archaeal. DR InterPro; IPR015865; Riboflavin_kinase_bac/euk. DR InterPro; IPR023602; Riboflavin_kinase_CTP-dep. DR InterPro; IPR023465; Riboflavin_kinase_domain. DR Pfam; PF01982; CTP-dep_RFKase; 1. DR SUPFAM; SSF82114; SSF82114; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Flavoprotein; FMN; Kinase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1 132 Riboflavin kinase. FT /FTId=PRO_0000106673. FT NP_BIND 10 15 CDP. {ECO:0000269|Ref.3}. FT NP_BIND 108 111 CDP. {ECO:0000269|Ref.3}. FT METAL 39 39 Magnesium. {ECO:0000269|PubMed:18073108}. FT METAL 41 41 Magnesium. {ECO:0000269|PubMed:18073108}. FT BINDING 95 95 FMN. FT BINDING 96 96 FMN. FT BINDING 103 103 FMN. FT STRAND 1 8 {ECO:0000244|PDB:2VBU}. FT HELIX 13 18 {ECO:0000244|PDB:2VBU}. FT HELIX 21 31 {ECO:0000244|PDB:2VBU}. FT STRAND 40 48 {ECO:0000244|PDB:2VBU}. FT HELIX 50 52 {ECO:0000244|PDB:2VBU}. FT STRAND 56 58 {ECO:0000244|PDB:2P3M}. FT STRAND 61 63 {ECO:0000244|PDB:2VBU}. FT STRAND 66 68 {ECO:0000244|PDB:2VBU}. FT STRAND 71 80 {ECO:0000244|PDB:2VBU}. FT STRAND 83 93 {ECO:0000244|PDB:2VBU}. FT STRAND 99 105 {ECO:0000244|PDB:2VBU}. FT HELIX 110 113 {ECO:0000244|PDB:2VBU}. FT STRAND 121 127 {ECO:0000244|PDB:2VBU}. SQ SEQUENCE 132 AA; 15214 MW; 12B9AF1567F7D8B8 CRC64; MIIEGEVVSG LGEGRYFLSL PPYKEIFKKI LGFEPYEGTL NLKLDREFDI NKFKYIETED FEFNGKRFFG VKVLPIKILI GNKKIDGAIV VPKKTYHSSE IIEIIAPMKL REQFNLKDGD VIKILIKGDK DE // ID RELE4_METJA Reviewed; 94 AA. AC Q58573; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative toxin RelE4; GN Name=relE4; OrderedLocusNames=MJ1173; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Its CC cognate antitoxin is RelB4 (Potential). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99176.1; -; Genomic_DNA. DR PIR; D64446; D64446. DR ProteinModelPortal; Q58573; -. DR STRING; 243232.MJ_1173; -. DR EnsemblBacteria; AAB99176; AAB99176; MJ_1173. DR KEGG; mja:MJ_1173; -. DR eggNOG; arCOG02414; Archaea. DR eggNOG; COG2026; LUCA. DR InParanoid; Q58573; -. DR OMA; HIDSHFV; -. DR PhylomeDB; Q58573; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007712; RelE/ParE_toxin. DR InterPro; IPR004386; Toxin_YafQ-like. DR Pfam; PF05016; ParE_toxin; 1. DR TIGRFAMs; TIGR02385; RelE_StbE; 1. DR TIGRFAMs; TIGR00053; TIGR00053; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Toxin. FT CHAIN 1 94 Putative toxin RelE4. FT /FTId=PRO_0000107200. SQ SEQUENCE 94 AA; 11450 MW; 85FDCBCD4A8E4A05 CRC64; MYEIEIMPSL DKILQKLSKR DKKKLKAILK KMEEITQNPH HYKNLRHPLN DFKRVHIDKS FVLVFTVDEN NKTVIFVDFD HHDNIYKKKK LFKD // ID RFCS_METJA Reviewed; 1847 AA. AC Q58817; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Replication factor C small subunit; DE Short=RFC small subunit; DE AltName: Full=Clamp loader small subunit; DE Contains: DE RecName: Full=Mja RFC-1 intein; DE Contains: DE RecName: Full=Mja RFC-2 intein; DE Contains: DE RecName: Full=Mja RFC-3 intein; GN Name=rfcS; OrderedLocusNames=MJ1422; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the CC PCNA sliding clamp onto DNA. {ECO:0000250}. CC -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and CC large subunits (RfcL). {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- MISCELLANEOUS: The intein interrupts the potential ATP-binding CC site. CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcS CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 3 DOD-type homing endonuclease domains. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99433.1; -; Genomic_DNA. DR PIR; E64477; E64477. DR ProteinModelPortal; Q58817; -. DR SMR; Q58817; 2-53, 1058-1125, 1667-1847. DR STRING; 243232.MJ_1422; -. DR EnsemblBacteria; AAB99433; AAB99433; MJ_1422. DR KEGG; mja:MJ_1422; -. DR eggNOG; arCOG00469; Archaea. DR eggNOG; arCOG03145; Archaea. DR eggNOG; arCOG03154; Archaea. DR eggNOG; arCOG03158; Archaea. DR eggNOG; COG0470; LUCA. DR InParanoid; Q58817; -. DR KO; K04801; -. DR OMA; TNDENEM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0009378; F:four-way junction helicase activity; IEA:InterPro. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006261; P:DNA-dependent DNA replication; IBA:GO_Central. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR Gene3D; 2.170.16.10; -; 7. DR Gene3D; 3.10.28.10; -; 5. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013748; Rep_factorC_C. DR InterPro; IPR008824; RuvB_N. DR Pfam; PF01381; HTH_3; 1. DR Pfam; PF14528; LAGLIDADG_3; 3. DR Pfam; PF08542; Rep_fac_C; 1. DR Pfam; PF05496; RuvB_N; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 3. DR SMART; SM00306; HintN; 3. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR SUPFAM; SSF48019; SSF48019; 1. DR SUPFAM; SSF51294; SSF51294; 7. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF55608; SSF55608; 3. DR TIGRFAMs; TIGR01443; intein_Cterm; 3. DR TIGRFAMs; TIGR01445; intein_Nterm; 3. DR PROSITE; PS50818; INTEIN_C_TER; 3. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 3. DR PROSITE; PS50817; INTEIN_N_TER; 3. PE 3: Inferred from homology; KW ATP-binding; Autocatalytic cleavage; Complete proteome; KW DNA replication; Nucleotide-binding; Protein splicing; KW Reference proteome; Repeat. FT CHAIN 1 53 Replication factor C small subunit, 1st FT part. {ECO:0000255}. FT /FTId=PRO_0000030361. FT CHAIN 54 601 Mja RFC-1 intein. {ECO:0000255}. FT /FTId=PRO_0000030362. FT CHAIN 602 626 Replication factor C small subunit, 2nd FT part. {ECO:0000255}. FT /FTId=PRO_0000030363. FT CHAIN 627 1062 Mja RFC-2 intein. {ECO:0000255}. FT /FTId=PRO_0000030364. FT CHAIN 1063 1124 Replication factor C small subunit, 3rd FT part. {ECO:0000255}. FT /FTId=PRO_0000030365. FT CHAIN 1125 1667 Mja RFC-3 intein. {ECO:0000255}. FT /FTId=PRO_0000030366. FT CHAIN 1668 1847 Replication factor C small subunit, 4th FT part. {ECO:0000255}. FT /FTId=PRO_0000030367. FT DOMAIN 179 311 DOD-type homing endonuclease 1. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT DOMAIN 780 927 DOD-type homing endonuclease 2. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT DOMAIN 1348 1508 DOD-type homing endonuclease 3. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 1847 AA; 214097 MW; 44EADB5B4D6DE64A CRC64; MVIIMEKPWV EKYRPKTLDD IVGQDEIVKR LKKYVEKKSM PHLLFSGPPG VGKCLTGDTK VIVNGEIREI GEVIEEISNG KFGVTLTNNL KVLGIDEDGK IREFDVQYVY KDKTNTLIKI KTKMGRELKV TTYHPLLINH KNGEIKWEKA ENLKVGDKLA TPRYILFNES DYNEELAEWL GYFIGDGHAD KESNKITFTN GDEKLRKRFA ELTEKLFKDA KIKERIHKDR TPDIYVNSKE AVEFIDKLGL RGKKADKVRI PKEIMRSDAL RAFLRAYFDC DGGIEKHSIV LSTASKEMAE DLVYALLRFG IIAKLREKVN KNNNKVYYHI VISNSSNLRT FLDNIGFSQE RKLKKLLEII KDENPNLDVI TIDKEKIRYI RDRLKVKLTR DIEKDNWSYN KCRKITQELL KEIYYRLEEL KEIEKALEEN ILIDWDEVAE RRKEIAEKTG IRSDRILEYI RGKRKPSLKN YIKIANTLGK NIEKIIDAMR IFAKKYSSYA EIGKMLNMWN SSIKIYLESN TQEIEKLEEI RKTELKLVKE ILNDEKLIDS IGYVLFLASN EIYWDEIVEI EQLNGEFTIY DLHVPRYHNF IGGNLPTILH NTTAALCLAR DLFGENWRDN FLELNASVSK DTPILVKIDG KVKRTTFEEL DKIYFETNDE NEMYKKVDNL EVLTVDENFR VRWRKVSTII RHKVDKILRI KFEGGYIELT GNHSIMMLDE NGLVAKKASD IKVGDCFLSF VANIEGEKDR LDLKEFEPKD ITSRVKIIND FDIDEDTAWM LGLYVAEGAV GFKGKTSGQV IYTLGSHEHD LINKLNDIVD KKGFSKYENF TGSGFDRKRL SAKQIRILNT QLARFVEENF YDGNGRRARN KRIPDIIFEL KENLRVEFLK GLADGDSSGN WREVVRISSK SDNLLIDTVW LARISGIESS IFENEARLIW KGGMKWKKSN LLPAEPIIKM IKKLENKING NWRYILRHQL YEGKKRVSKD KIKQILEMVN VEKLSDKEKE VYDLLKKLSK TELYALVVKE IEIIDYNDFV YDVSVPNNEM FFAGNVPILL HNSDERGIDV IRTKVKDFAR TKPIGDVPFK IIFLDESDAL TADAQNALRR TMEKYSDVCR FILSCLTGDA KITLPDEREI KIEDFIKMFE ERKLKHVLNR NGEDLVLAGV KFNSKIVNHK VYRLVLESGR EIEATGDHKF LTRDGWKEVY ELKEDDEVLV YPALEGVGFE VDERRIIGLN EFYEFLTNYE IKLGYKPLGK AKSYKELITR DKEKILSRVL ELSDKYSKSE IRRKIEEEFG IKISLTTIKN LINGKIDGFA LKYVRKIKEL GWDEITYDDE KAGIFARLLG FIIGDGHLSK SKEGRILITA TINELEGIKK DLEKLGIKAS NIIEKDIEHK LDGREIKGKT SFIYINNKAF YLLLNFWGVE IGNKTINGYN IPKWIKYGNK FVKREFLRGL FGADGTKPYI KKYNINGIKL GIRVENISKD KTLEFFEEVK KMLEEFEVES YIKVSKIDNK NLTELIVKAN NKNYLKYLSR ISYAYEKDNF ARLVGEYLRI KEAYKDIILK EIAENALKEA DGEKSLRELA RKYNVPVDFI INQLKGKDIG LPRNFMTFEE FLKEKVVDGK YVSERIIKKE CIGYRDVYDI TCHKDPSFIA NGFVSHNCNY PSKIIPPIQS RCAVFRFSPL KKEDIAKKLK EIAEKEGLNL TESGLEAIIY VSEGDMRKAI NVLQTAAALS DVIDDEIVYK VSSRARPEEV KKMMELALDG KFMEARDLLY KLMVEWGMSG EDILNQMFRE INSLDIDERK KVELADAIGE TDFRIVEGAN ERIQLSALLA KMALMGR // ID RIB7_METJA Reviewed; 224 AA. AC Q58085; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=2,5-diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase; DE Short=DAROPP reductase; DE Short=DARP reductase; DE EC=1.1.1.302; DE AltName: Full=2,5-diamino-6-(5-phospho-D-ribosylamino)pyrimidin-4(3H)-one reductase; DE AltName: Full=2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthase; DE Short=DARIPP synthase; DE AltName: Full=MjaRED; GN Name=arfC; OrderedLocusNames=MJ0671; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY. RX PubMed=11889103; DOI=10.1128/JB.184.7.1952-1957.2002; RA Graupner M., Xu H., White R.H.; RT "The pyrimidine nucleotide reductase step in riboflavin and F(420) RT biosynthesis in archaea proceeds by the eukaryotic route to RT riboflavin."; RL J. Bacteriol. 184:1952-1957(2002). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION STEREOSPECIFICITY. RX PubMed=18671734; DOI=10.1111/j.1742-4658.2008.06586.x; RA Romisch-Margl W., Eisenreich W., Haase I., Bacher A., Fischer M.; RT "2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate synthases RT of fungi and archaea."; RL FEBS J. 275:4403-4414(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 6-224 IN COMPLEX WITH NADP, RP PROTEIN SEQUENCE OF 2-11, CATALYTIC ACTIVITY, MASS SPECTROMETRY, RP SUBUNIT, AND REACTION MECHANISM. RX PubMed=16730025; DOI=10.1016/j.jmb.2006.04.045; RA Chatwell L., Krojer T., Fidler A., Romisch W., Eisenreich W., RA Bacher A., Huber R., Fischer M.; RT "Biosynthesis of riboflavin: structure and properties of 2,5-diamino- RT 6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate reductase of RT Methanocaldococcus jannaschii."; RL J. Mol. Biol. 359:1334-1351(2006). CC -!- FUNCTION: Catalyzes an early step in riboflavin biosynthesis, the CC NAD(P)H-dependent reduction of the ribose side chain of 2,5- CC diamino-6-ribosylamino-4(3H)-pyrimidinone 5'-phosphate, yielding CC 2,5-diamino-6-ribitylamino-4(3H)-pyrimidinone 5'-phosphate. The CC beta anomer is the authentic substrate, and the alpha anomer can CC serve as substrate subsequent to spontaneous anomerization. NADPH CC and NADH function equally well as the reductants. Does not CC catalyze the reduction of 5-amino-6-(5-phospho-D- CC ribosylamino)uracil to 5-amino-6-(5-phospho-D-ribitylamino)uracil. CC {ECO:0000269|PubMed:11889103, ECO:0000269|PubMed:18671734}. CC -!- CATALYTIC ACTIVITY: 2,5-diamino-6-(5-phospho-D- CC ribitylamino)pyrimidin-4(3H)-one + NAD(P)(+) = 2,5-diamino-6-(5- CC phospho-D-ribosylamino)pyrimidin-4(3H)-one + NAD(P)H. CC {ECO:0000269|PubMed:11889103, ECO:0000269|PubMed:16730025, CC ECO:0000269|PubMed:18671734}. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16730025}. CC -!- MASS SPECTROMETRY: Mass=24906; Method=Electrospray; Range=2-224; CC Evidence={ECO:0000269|PubMed:16730025}; CC -!- MISCELLANEOUS: The protein sequence in PubMed:16730025 comes from CC protein expressed and processed in E.coli. CC -!- MISCELLANEOUS: Using chirally deuterated NADPH, the enzyme was CC shown to be A-type reductase catalyzing the transfer of deuterium CC from the 4(R) position of NADPH to the 1' (S) position of the CC substrate. CC -!- SIMILARITY: Belongs to the HTP reductase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98665.1; -; Genomic_DNA. DR PIR; G64383; G64383. DR PDB; 2AZN; X-ray; 2.70 A; A/B/C/D/E/F=6-224. DR PDBsum; 2AZN; -. DR ProteinModelPortal; Q58085; -. DR SMR; Q58085; 6-224. DR STRING; 243232.MJ_0671; -. DR EnsemblBacteria; AAB98665; AAB98665; MJ_0671. DR KEGG; mja:MJ_0671; -. DR eggNOG; arCOG01484; Archaea. DR eggNOG; COG1985; LUCA. DR InParanoid; Q58085; -. DR KO; K14654; -. DR OMA; KPYVISN; -. DR PhylomeDB; Q58085; -. DR BioCyc; MetaCyc:MONOMER-14596; -. DR BRENDA; 1.1.1.302; 3260. DR UniPathway; UPA00275; -. DR EvolutionaryTrace; Q58085; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051287; F:NAD binding; IDA:UniProtKB. DR GO; GO:0050661; F:NADP binding; IDA:UniProtKB. DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IDA:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; IDA:UniProtKB. DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB. DR Gene3D; 3.40.430.10; -; 1. DR InterPro; IPR024072; DHFR-like_dom. DR InterPro; IPR006401; Rib_reduct_arc. DR InterPro; IPR011549; RibD_C. DR InterPro; IPR002734; RibDG_C. DR Pfam; PF01872; RibD_C; 1. DR SUPFAM; SSF53597; SSF53597; 1. DR TIGRFAMs; TIGR01508; rib_reduct_arch; 1. DR TIGRFAMs; TIGR00227; ribD_Cterm; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; NAD; NADP; KW Oxidoreductase; Reference proteome; Riboflavin biosynthesis. FT INIT_MET 1 1 Removed. {ECO:0000305|PubMed:16730025}. FT CHAIN 2 224 2,5-diamino-6-ribosylamino-4(3H)- FT pyrimidinone 5'-phosphate reductase. FT /FTId=PRO_0000135944. FT NP_BIND 83 86 NADP. {ECO:0000269|PubMed:16730025}. FT NP_BIND 156 159 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 16 16 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:16730025}. FT BINDING 57 57 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 61 61 NADP. {ECO:0000269|PubMed:16730025}. FT BINDING 134 134 NADP; via amide nitrogen and carbonyl FT oxygen. {ECO:0000269|PubMed:16730025}. FT STRAND 10 18 {ECO:0000244|PDB:2AZN}. FT STRAND 22 24 {ECO:0000244|PDB:2AZN}. FT HELIX 35 46 {ECO:0000244|PDB:2AZN}. FT STRAND 48 54 {ECO:0000244|PDB:2AZN}. FT HELIX 55 61 {ECO:0000244|PDB:2AZN}. FT STRAND 77 81 {ECO:0000244|PDB:2AZN}. FT HELIX 92 94 {ECO:0000244|PDB:2AZN}. FT STRAND 100 104 {ECO:0000244|PDB:2AZN}. FT HELIX 110 121 {ECO:0000244|PDB:2AZN}. FT STRAND 125 128 {ECO:0000244|PDB:2AZN}. FT STRAND 131 133 {ECO:0000244|PDB:2AZN}. FT HELIX 136 145 {ECO:0000244|PDB:2AZN}. FT STRAND 150 155 {ECO:0000244|PDB:2AZN}. FT HELIX 157 165 {ECO:0000244|PDB:2AZN}. FT STRAND 171 178 {ECO:0000244|PDB:2AZN}. FT STRAND 188 190 {ECO:0000244|PDB:2AZN}. FT HELIX 198 200 {ECO:0000244|PDB:2AZN}. FT STRAND 204 212 {ECO:0000244|PDB:2AZN}. FT STRAND 215 222 {ECO:0000244|PDB:2AZN}. SQ SEQUENCE 224 AA; 25037 MW; 4D8C15CE291E89D8 CRC64; MVMVMEKKPY IISNVGMTLD GKLATINNDS RISCEEDLIR VHKIRANVDG IMVGIGTVLK DDPRLTVHKI KSDRNPVRIV VDSKLRVPLN ARVLNKDAKT IIATTEDTNE EKEKKIKILE DMGVEVVKCG RGKVDLKKLM DILYDKGIKS ILLEGGGTLN WGMFKEGLVD EVSVYIAPKI FGGKEAPTYV DGEGFKTVDE CVKLELKNFY RLGEGIVLEF KVKK // ID RELB1_METJA Reviewed; 82 AA. AC Q60373; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Putative antitoxin RelB1; GN Name=relB1; OrderedLocusNames=MJ0070; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Its cognate toxin is RelE1 (Potential). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98053.1; -; Genomic_DNA. DR PIR; F64308; F64308. DR STRING; 243232.MJ_0070; -. DR EnsemblBacteria; AAB98053; AAB98053; MJ_0070. DR KEGG; mja:MJ_0070; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 82 Putative antitoxin RelB1. FT /FTId=PRO_0000106678. FT COMPBIAS 46 58 Glu-rich. SQ SEQUENCE 82 AA; 9607 MW; 298230477B2C550B CRC64; MLNINKEIAQ IETELNELKK LRDEISERIE KLEIKLLKLK ALAIPEEEFE EDYEEIIEDV KKSLDKKETV PAEEALKELG LL // ID RELB2_METJA Reviewed; 61 AA. AC P0CW76; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 6. DE RecName: Full=Putative antitoxin RelB2; GN Name=relB2; OrderedLocusNames=MJ0909.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, AND POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Its cognate toxin is RelE2 (Potential). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 61 Putative antitoxin RelB2. FT /FTId=PRO_0000408468. SQ SEQUENCE 61 AA; 7093 MW; 3144BE941C838D43 CRC64; MSIVQSYITD EKGNIKGVIL DYKTFKKIEE LLLDYGLLKA MEEVENEEEI DLETAKKLLE Q // ID RELB4_METJA Reviewed; 84 AA. AC Q58572; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Putative antitoxin RelB4; GN Name=relB4; OrderedLocusNames=MJ1172; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Antitoxin component of a toxin-antitoxin (TA) module. CC Its cognate toxin is RelE4 (Potential). {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99187.1; -; Genomic_DNA. DR PIR; C64446; C64446. DR STRING; 243232.MJ_1172; -. DR EnsemblBacteria; AAB99187; AAB99187; MJ_1172. DR KEGG; mja:MJ_1172; -. DR eggNOG; arCOG05071; Archaea. DR eggNOG; ENOG4112D5V; LUCA. DR InParanoid; Q58572; -. DR OMA; INIDDHT; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020271; Uncharacterised_MJ1172. DR Pfam; PF10884; DUF2683; 1. DR ProDom; PD060824; Uncharacterised_MJ1172; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 84 Putative antitoxin RelB4. FT /FTId=PRO_0000107199. SQ SEQUENCE 84 AA; 9986 MW; 4B7837421CBADAE4 CRC64; MILMVKAIVD ITDENNRIIN IVKAKYNLRD KSQAINKIIE EYAEFLLEDE LKPEYIEKIR NIMKNEKPIY IGSIENLKKR YLGE // ID RFAPS_METJA Reviewed; 328 AA. AC Q58822; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 87. DE RecName: Full=Beta-ribofuranosylaminobenzene 5'-phosphate synthase; DE Short=Beta-RFA-P synthase; DE EC=2.4.2.54 {ECO:0000269|PubMed:15262968}; GN OrderedLocusNames=MJ1427; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, ENZYME MECHANISM, BIOPHYSICOCHEMICAL RP PROPERTIES, PATHWAY, AND SUBUNIT. RX PubMed=15262968; DOI=10.1074/jbc.M406442200; RA Dumitru R.V., Ragsdale S.W.; RT "Mechanism of 4-(beta-D-ribofuranosyl)aminobenzene 5'-phosphate RT synthase, a key enzyme in the methanopterin biosynthetic pathway."; RL J. Biol. Chem. 279:39389-39395(2004). CC -!- FUNCTION: Catalyzes the condensation of 4-aminobenzoate (pABA) CC with 5-phospho-alpha-D-ribose 1-diphosphate (PRPP) to produce CC beta-ribofuranosylaminobenzene 5'-phosphate (beta-RFA-P). CC {ECO:0000269|PubMed:15262968}. CC -!- CATALYTIC ACTIVITY: 5-phospho-alpha-D-ribose 1-diphosphate + 4- CC hydroxybenzoate = 4-(beta-D-ribofuranosyl)phenol 5'-phosphate + CC CO(2) + diphosphate. {ECO:0000269|PubMed:15262968}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.5 mM for PRPP {ECO:0000269|PubMed:15262968}; CC KM=0.15 mM for pABA {ECO:0000269|PubMed:15262968}; CC Vmax=180 nmol/min/mg enzyme {ECO:0000269|PubMed:15262968}; CC Note=kcat is 0.23 sec(-1).; CC pH dependence: CC Optimum pH is 4.9. {ECO:0000269|PubMed:15262968}; CC -!- PATHWAY: Cofactor biosynthesis; 5,6,7,8-tetrahydromethanopterin CC biosynthesis. {ECO:0000269|PubMed:15262968}. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:15262968}. CC -!- MISCELLANEOUS: Lacks any chromogenic cofactor, and the presence of CC pyridoxal phosphate and the mechanistically related pyruvoyl CC cofactors has been strictly excluded. CC {ECO:0000305|PubMed:15262968}. CC -!- SIMILARITY: Belongs to the beta-RFA-P synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99449.1; -; Genomic_DNA. DR PIR; B64478; B64478. DR ProteinModelPortal; Q58822; -. DR STRING; 243232.MJ_1427; -. DR EnsemblBacteria; AAB99449; AAB99449; MJ_1427. DR KEGG; mja:MJ_1427; -. DR eggNOG; arCOG01026; Archaea. DR eggNOG; COG1907; LUCA. DR InParanoid; Q58822; -. DR KO; K06984; -. DR OMA; AEICRIV; -. DR PhylomeDB; Q58822; -. DR BioCyc; MetaCyc:MONOMER-14546; -. DR BRENDA; 2.4.2.54; 3260. DR UniPathway; UPA00065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR004422; GHMP_kin. DR InterPro; IPR006204; GHMP_kinase_N_dom. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR Pfam; PF00288; GHMP_kinases_N; 1. DR PIRSF; PIRSF004884; Sugar_kin_arch; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR00144; beta_RFAP_syn; 1. PE 1: Evidence at protein level; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 328 Beta-ribofuranosylaminobenzene 5'- FT phosphate synthase. FT /FTId=PRO_0000107320. SQ SEQUENCE 328 AA; 36198 MW; 67F166A355C41FA1 CRC64; MIIQTPSRIH MGLIDLNGSI GRVDGGIGLA LEEPNIKIEG KESDDISIEF DKKLIEKYGE DYIKSVRDRV YNTAIKVLDV IGGEGVDLKI LSLFPAHSGL GSGTQLSLAV GKLISKIYNK EMNAYNIAKI TGRGGTSGIG IGAFEYGGFL IDGGHSFGKG KDKEDFRPSS ASKGVKPAPI IFRHDFDWET ILIIPKGEHV YGKKEVDIFK KYCPVPLNEV EKICHLVLMK MMPAVVEKNL DDFGEVINKL QYLGFKKVEL SLQSDIVKDL INELHKDVYA GLSSFGPTIY AFGDKKLIVE KANDIFDKYG VYGEIIITKA NNVGHKIW // ID RECJ_METJA Reviewed; 469 AA. AC Q58387; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=Single-stranded-DNA-specific exonuclease RecJ; DE EC=3.1.-.-; GN Name=recJ; OrderedLocusNames=MJ0977; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=10633092; DOI=10.1128/JB.182.3.607-612.2000; RA Rajman L.A., Lovett S.T.; RT "A thermostable single-strand DNase from Methanococcus jannaschii RT related to the RecJ recombination and repair exonuclease from RT Escherichia coli."; RL J. Bacteriol. 182:607-612(2000). CC -!- FUNCTION: Single-stranded-DNA-specific exonuclease. CC {ECO:0000269|PubMed:10633092}. CC -!- SIMILARITY: Belongs to the RecJ family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98980.1; -; Genomic_DNA. DR PIR; A64422; A64422. DR ProteinModelPortal; Q58387; -. DR STRING; 243232.MJ_0977; -. DR EnsemblBacteria; AAB98980; AAB98980; MJ_0977. DR KEGG; mja:MJ_0977; -. DR eggNOG; arCOG00427; Archaea. DR eggNOG; COG0608; LUCA. DR InParanoid; Q58387; -. DR KO; K07463; -. DR OMA; YKVSARC; -. DR PhylomeDB; Q58387; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. PE 3: Inferred from homology; KW Complete proteome; Exonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 469 Single-stranded-DNA-specific exonuclease FT RecJ. FT /FTId=PRO_0000097231. SQ SEQUENCE 469 AA; 53847 MW; 037110C6D53B7554 CRC64; MENWVELKKG AKVLQNNKNN KILIVTHIDT DGLTSRAILQ KLAERLNLDA DFMFLKQITI ETINDIPFKD YDLIIFADLG SGQLKMIKEK LDELNLSDKR DKIIILDHHQ PEEIKIPKTI IHINPLTIAK SGAEICGAGV SYLFAKAINN DWIDLAKYAV LGAVGDIQNI EGKLIGLNRK ILCDAIMNGD VKVKTDLQMY GRQTRPLFVS MRYWADVRTD LLNNDSKIIK YIQSINKKYD IEINPTMRLA EIPFEHKRII GNELLIKCLN YVPNHWTPYI PKVIFGEVYE FRGEEFGSPL RDLEEFSTCI NACSRYGDYE TALNVLMGDR DKYYRKMLSN LRKHRNNLRE ALEHVKNDVE IIQKDRFQYF ETDKIMSNIV GIVAGMSYSI EEVDWMKPIF AITEDENGYK VSARCPKLLC FAEDVNLAKA IKYASEKVNG SGGGHKFACG AYIPDNKREF IKYLEIALR // ID RELE2_METJA Reviewed; 91 AA. AC Q58319; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Putative toxin RelE2; GN Name=relE2; OrderedLocusNames=MJ0909; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. Its CC cognate antitoxin is RelB2 (Potential). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RelE toxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98911.1; -; Genomic_DNA. DR PIR; E64413; E64413. DR ProteinModelPortal; Q58319; -. DR STRING; 243232.MJ_0909; -. DR EnsemblBacteria; AAB98911; AAB98911; MJ_0909. DR KEGG; mja:MJ_0909; -. DR eggNOG; arCOG01663; Archaea. DR eggNOG; COG2026; LUCA. DR OMA; ADSYYRI; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007712; RelE/ParE_toxin. DR Pfam; PF05016; ParE_toxin; 1. DR TIGRFAMs; TIGR02385; RelE_StbE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Toxin. FT CHAIN 1 91 Putative toxin RelE2. FT /FTId=PRO_0000107099. SQ SEQUENCE 91 AA; 11146 MW; 4E42600B3466CD72 CRC64; MKQWKYLLKK SFIKDLKELP KNIQEKIKKL VFEEIPNKNN PPEIPNVKKL KGADSYYRIR VGDYRIGFKY ENGKIVFYRV LHRKQIYKRF P // ID RFCL_METJA Reviewed; 516 AA. AC Q58294; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Replication factor C large subunit; DE Short=RFC large subunit; DE AltName: Full=Clamp loader large subunit; GN Name=rfcL; OrderedLocusNames=MJ0884; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CRYSTALLIZATION. RX PubMed=11856841; DOI=10.1107/S090744490102159X; RA Lee I., Lokanath N.K., Min K., Ha S.C., Kim D.Y., Kim K.K.; RT "Cloning, purification, crystallization and preliminary X-ray studies RT of RFC boxes II-VIII of replication factor C from Methanococcus RT jannaschii."; RL Acta Crystallogr. D 58:519-521(2002). CC -!- FUNCTION: Part of the RFC clamp loader complex which loads the CC PCNA sliding clamp onto DNA. {ECO:0000250}. CC -!- SUBUNIT: Heteromultimer composed of small subunits (RfcS) and CC large subunits (RfcL). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the activator 1 small subunits family. RfcL CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98888.1; -; Genomic_DNA. DR PIR; D64410; D64410. DR ProteinModelPortal; Q58294; -. DR STRING; 243232.MJ_0884; -. DR EnsemblBacteria; AAB98888; AAB98888; MJ_0884. DR KEGG; mja:MJ_0884; -. DR eggNOG; arCOG00470; Archaea. DR eggNOG; COG0470; LUCA. DR InParanoid; Q58294; -. DR KO; K04800; -. DR OMA; GGWTRYG; -. DR PhylomeDB; Q58294; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003689; F:DNA clamp loader activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.300; -; 2. DR HAMAP; MF_01508; RfcL; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR023935; Rep_factor-C_lsu. DR Pfam; PF00004; AAA; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW ATP-binding; Complete proteome; DNA replication; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 516 Replication factor C large subunit. FT /FTId=PRO_0000135952. FT NP_BIND 46 53 ATP. {ECO:0000255}. SQ SEQUENCE 516 AA; 58770 MW; 800BF6A70560859E CRC64; MLSWVEKYRP KSLKDVAGHE KVKEKLKTWI ESYLKGETPK PILLVGPPGC GKTTLAYALA NDYGFEVIEL NASDKRNSSA IKKVVGHAAT SSSIFGKKFL IVLDEVDGIS GKEDAGGVSE LIKVIKKAKN PIILTANDAY APSIRSLLPY VEVIQLNPVH TNSVYKVLKK IAEKEGLDVD DKTLKMIAQH SAGDLRSAIN DLEALALSGD LSYEAAQKLP DRKREANIFD ALRVILKTTH YGIATTALMN VDETPDVVIE WIAENVPKEY EKPEEVARAF EYLSKADRYL GRVMRRQNYS FWKYATTLMT AGVALSKDEK YRKWTPYSYP KIFRLLTKTK AEREILNKIL KKIGEKTHTS SKRARFDLQM LKLLAKENPS VAADLVDYFE IKEDELKVLV GDKLASEILK ILKEKKKLER KKKKEKEKLE KEKKKEEKAK EKQSNLIIQP KEIKEEVKAE VEKKEEVKEK IVEKPKAEEV KEKSKTEEKE TKKDKKKGKK KKEDKGKQLT LDAFFK // ID RIBB_METJA Reviewed; 227 AA. AC Q60364; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=3,4-dihydroxy-2-butanone 4-phosphate synthase; DE Short=DHBP synthase; DE EC=4.1.99.12; GN Name=ribB; OrderedLocusNames=MJ0055; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-15, FUNCTION, MASS SPECTROMETRY, RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, COFACTOR, AND MUTAGENESIS OF RP ASP-21; ARG-25; GLU-26; GLU-28; ASP-30; CYS-55; THR-112; ARG-119; RP ARG-161; HIS-164; THR-165; GLU-166 AND GLU-185. RX PubMed=12200440; DOI=10.1074/jbc.M206863200; RA Fischer M., Roemisch W., Schiffmann S., Kelly M., Oschkinat H., RA Steinbacher S., Huber R., Eisenreich W., Richter G., Bacher A.; RT "Biosynthesis of riboflavin in archaea studies on the mechanism of RT 3,4-dihydroxy-2-butanone-4-phosphate synthase of Methanococcus RT jannaschii."; RL J. Biol. Chem. 277:41410-41416(2002). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF MUTANT SER-147 IN COMPLEX RP WITH DIVALENT METAL CATIONS AND SUBSTRATE, AND SUBUNIT. RX PubMed=12904291; DOI=10.1074/jbc.M307301200; RA Steinbacher S., Schiffmann S., Richter G., Huber R., Bacher A., RA Fischer M.; RT "Structure of 3,4-dihydroxy-2-butanone 4-phosphate synthase from RT Methanococcus jannaschii in complex with divalent metal ions and the RT substrate ribulose 5-phosphate: implications for the catalytic RT mechanism."; RL J. Biol. Chem. 278:42256-42265(2003). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF MUTANT SER-147 IN COMPLEX RP WITH DIVALENT METAL CATIONS AND SUBSTRATE, AND SUBUNIT. RX PubMed=15213409; DOI=10.1107/S0907444904009862; RA Steinbacher S., Schiffmann S., Bacher A., Fischer M.; RT "Metal sites in 3,4-dihydroxy-2-butanone 4-phosphate synthase from RT Methanococcus jannaschii in complex with the substrate ribulose 5- RT phosphate."; RL Acta Crystallogr. D 60:1338-1340(2004). CC -!- FUNCTION: Catalyzes the conversion of D-ribulose 5-phosphate to CC formate and 3,4-dihydroxy-2-butanone 4-phosphate. CC {ECO:0000269|PubMed:12200440}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = formate + L-3,4- CC dihydroxybutan-2-one 4-phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12200440}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000269|PubMed:12200440}; CC Note=Binds 2 divalent metal cations per subunit. Magnesium or CC manganese. {ECO:0000269|PubMed:12200440}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=140 uM for ribulose-5-phosphate CC {ECO:0000269|PubMed:12200440}; CC Vmax=148 nmol/min/mg enzyme {ECO:0000269|PubMed:12200440}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; 2- CC hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step CC 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:12200440, CC ECO:0000269|PubMed:12904291, ECO:0000269|PubMed:15213409}. CC -!- MASS SPECTROMETRY: Mass=25799; Method=Electrospray; Range=1-227; CC Evidence={ECO:0000269|PubMed:12200440}; CC -!- SIMILARITY: Belongs to the DHBP synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98035.1; -; Genomic_DNA. DR PIR; G64306; G64306. DR PDB; 1PVW; X-ray; 2.45 A; A/B/C=1-227. DR PDB; 1PVY; X-ray; 1.70 A; A/B=1-227. DR PDB; 1SNN; X-ray; 1.55 A; A/B=1-227. DR PDBsum; 1PVW; -. DR PDBsum; 1PVY; -. DR PDBsum; 1SNN; -. DR ProteinModelPortal; Q60364; -. DR SMR; Q60364; 2-220. DR STRING; 243232.MJ_0055; -. DR EnsemblBacteria; AAB98035; AAB98035; MJ_0055. DR KEGG; mja:MJ_0055; -. DR eggNOG; arCOG01320; Archaea. DR eggNOG; COG0108; LUCA. DR InParanoid; Q60364; -. DR KO; K02858; -. DR OMA; QMAKLIR; -. DR PhylomeDB; Q60364; -. DR BioCyc; MetaCyc:MONOMER-14603; -. DR BRENDA; 4.1.99.12; 3260. DR UniPathway; UPA00275; UER00399. DR EvolutionaryTrace; Q60364; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008686; F:3,4-dihydroxy-2-butanone-4-phosphate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.870.10; -; 1. DR HAMAP; MF_00180; RibB; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR000422; DHBP_synthase_RibB. DR Pfam; PF00926; DHBP_synthase; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00506; ribB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Direct protein sequencing; Lyase; KW Magnesium; Manganese; Metal-binding; Reference proteome; KW Riboflavin biosynthesis. FT CHAIN 1 227 3,4-dihydroxy-2-butanone 4-phosphate FT synthase. FT /FTId=PRO_0000151825. FT REGION 25 26 Substrate binding. FT REGION 161 165 Substrate binding. FT METAL 26 26 Magnesium or manganese 1. FT METAL 26 26 Magnesium or manganese 2. FT METAL 164 164 Magnesium or manganese 2. FT BINDING 30 30 Substrate. {ECO:0000269|PubMed:12904291, FT ECO:0000269|PubMed:15213409}. FT BINDING 185 185 Substrate. {ECO:0000269|PubMed:12904291, FT ECO:0000269|PubMed:15213409}. FT SITE 147 147 Essential for catalytic activity. FT SITE 185 185 Essential for catalytic activity. FT MUTAGEN 21 21 D->E,N: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 21 21 D->S: Reduces activity 70-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 25 25 R->E,K: Reduces activity 50-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 26 26 E->D,Q,S: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 28 28 E->D,S: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 28 28 E->Q: Reduces activity 23-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 30 30 D->E,N: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 30 30 D->S: Reduces activity 30-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 55 55 C->G: Reduces activity 70-fold. Increases FT Km for ribulose-5-phosphate 7-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 55 55 C->S: Reduces activity 30-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 112 112 T->A: Reduces activity 50-fold. Increases FT Km for ribulose-5-phosphate 10-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 119 119 R->S: Reduces activity 8-fold. Increases FT Km for ribulose-5-phosphate 8-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 147 147 H->S: Reduces activity 10-fold. FT MUTAGEN 161 161 R->S: Reduces activity 10-fold. Increases FT Km for ribulose-5-phosphate 7-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 164 164 H->N,S: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 165 165 T->A: Reduces activity by 2-fold. FT Increases Km for ribulose-5-phosphate 8- FT fold. {ECO:0000269|PubMed:12200440}. FT MUTAGEN 165 165 T->S: Reduces activity by 3-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 166 166 E->S: Increases Km for ribulose-5- FT phosphate 8-fold. FT {ECO:0000269|PubMed:12200440}. FT MUTAGEN 185 185 E->D,Q,S: Loss of activity. FT {ECO:0000269|PubMed:12200440}. FT HELIX 3 12 {ECO:0000244|PDB:1SNN}. FT STRAND 17 20 {ECO:0000244|PDB:1SNN}. FT TURN 23 26 {ECO:0000244|PDB:1SNN}. FT STRAND 29 34 {ECO:0000244|PDB:1SNN}. FT HELIX 35 37 {ECO:0000244|PDB:1SNN}. FT HELIX 40 49 {ECO:0000244|PDB:1SNN}. FT STRAND 51 58 {ECO:0000244|PDB:1SNN}. FT HELIX 60 66 {ECO:0000244|PDB:1SNN}. FT HELIX 71 78 {ECO:0000244|PDB:1SNN}. FT TURN 79 81 {ECO:0000244|PDB:1SNN}. FT HELIX 83 87 {ECO:0000244|PDB:1SNN}. FT STRAND 96 98 {ECO:0000244|PDB:1SNN}. FT STRAND 101 107 {ECO:0000244|PDB:1SNN}. FT STRAND 111 113 {ECO:0000244|PDB:1SNN}. FT HELIX 116 131 {ECO:0000244|PDB:1SNN}. FT HELIX 135 137 {ECO:0000244|PDB:1SNN}. FT HELIX 138 141 {ECO:0000244|PDB:1SNN}. FT STRAND 142 152 {ECO:0000244|PDB:1SNN}. FT HELIX 157 159 {ECO:0000244|PDB:1SNN}. FT HELIX 164 174 {ECO:0000244|PDB:1SNN}. FT STRAND 179 187 {ECO:0000244|PDB:1SNN}. FT STRAND 191 193 {ECO:0000244|PDB:1SNN}. FT HELIX 196 206 {ECO:0000244|PDB:1SNN}. FT STRAND 210 212 {ECO:0000244|PDB:1SNN}. FT HELIX 213 219 {ECO:0000244|PDB:1SNN}. SQ SEQUENCE 227 AA; 25797 MW; 0718EE5B4247995D CRC64; MNNVEKAIEA LKKGEIILVY DSDEREGETD MVVASQFITP EHIRIMRKDA GGLICTALHP DICNKLGIPF MVDILEFASQ KFKVLRELYP NDIPYDEKSS FSITINHRKT FTGITDNDRA FTIKKLAELV KEGRFNDFGK EFRSPGHVTL LRAAEGLVKN RQGHTEMTVA LAELANLVPI TTICEMMGDD GNAMSKNETK RYAEKHNLIY LSGEEIINYY LDKYLKD // ID RISB_METJA Reviewed; 141 AA. AC Q57751; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase; DE Short=DMRL synthase; DE Short=LS; DE Short=Lumazine synthase; DE EC=2.5.1.78; GN Name=ribH; OrderedLocusNames=MJ0303; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, KINETIC RP PARAMETERS, SUBUNIT, MASS SPECTROMETRY, AND PATHWAY. RX PubMed=12603336; DOI=10.1046/j.1432-1033.2003.03478.x; RA Haase I., Mortl S., Kohler P., Bacher A., Fischer M.; RT "Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine RT synthase of Methanococcus jannaschii."; RL Eur. J. Biochem. 270:1025-1032(2003). CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8- CC ribityllumazine by condensation of 5-amino-6-(D- CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. CC This is the penultimate step in the biosynthesis of riboflavin. CC {ECO:0000269|PubMed:12603336}. CC -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5- CC amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D- CC ribityl)lumazine + 2 H(2)O + phosphate. CC {ECO:0000269|PubMed:12603336}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=12.5 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees CC Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; CC KM=52 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees CC Celsius and pH 7.0) {ECO:0000269|PubMed:12603336}; CC Vmax=11 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0) CC {ECO:0000269|PubMed:12603336}; CC Vmax=90 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0) CC {ECO:0000269|PubMed:12603336}; CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 1/2. {ECO:0000269|PubMed:12603336}. CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, CC arranged as a dodecamer of pentamers. CC {ECO:0000305|PubMed:12603336}. CC -!- MASS SPECTROMETRY: Mass=15645; Method=Electrospray; Range=1-141; CC Evidence={ECO:0000269|PubMed:12603336}; CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98290.1; -; Genomic_DNA. DR PIR; H64337; H64337. DR ProteinModelPortal; Q57751; -. DR STRING; 243232.MJ_0303; -. DR EnsemblBacteria; AAB98290; AAB98290; MJ_0303. DR KEGG; mja:MJ_0303; -. DR eggNOG; arCOG01323; Archaea. DR eggNOG; COG0054; LUCA. DR InParanoid; Q57751; -. DR KO; K00794; -. DR OMA; QHAARKI; -. DR PhylomeDB; Q57751; -. DR BioCyc; MetaCyc:MONOMER-14604; -. DR BRENDA; 2.5.1.78; 3260. DR UniPathway; UPA00275; UER00404. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.960; -; 1. DR HAMAP; MF_00178; Lumazine_synth; 1. DR InterPro; IPR002180; DMRL_synthase. DR PANTHER; PTHR21058; PTHR21058; 1. DR Pfam; PF00885; DMRL_synthase; 1. DR SUPFAM; SSF52121; SSF52121; 1. DR TIGRFAMs; TIGR00114; lumazine-synth; 1. PE 1: Evidence at protein level; KW Complete proteome; Direct protein sequencing; Reference proteome; KW Riboflavin biosynthesis; Transferase. FT CHAIN 1 141 6,7-dimethyl-8-ribityllumazine synthase. FT /FTId=PRO_0000134843. FT REGION 46 48 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000250}. FT REGION 70 72 5-amino-6-(D-ribitylamino)uracil binding. FT {ECO:0000250}. FT REGION 75 76 1-deoxy-L-glycero-tetrulose 4-phosphate FT binding. {ECO:0000250}. FT ACT_SITE 78 78 Proton donor. {ECO:0000255}. FT BINDING 14 14 5-amino-6-(D-ribitylamino)uracil. FT {ECO:0000250}. FT BINDING 103 103 5-amino-6-(D-ribitylamino)uracil; via FT amide nitrogen and carbonyl oxygen. FT {ECO:0000250}. FT BINDING 118 118 1-deoxy-L-glycero-tetrulose 4-phosphate. FT {ECO:0000250}. SQ SEQUENCE 141 AA; 15645 MW; 646C2C494E27F371 CRC64; MVLMVNLGFV IAEFNRDITY MMEKVAEEHA EFLGATVKYK IVVPGVFDMP LAVKKLLEKD DVDAVVTIGC VIEGETEHDE IVVHNAARKI ADLALQYDKP VTLGISGPGM TRLQAQERVD YGKRAVEAAV KMVKRLKALE E // ID RL11_METJA Reviewed; 161 AA. AC P54030; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=50S ribosomal protein L11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN Name=rpl11 {ECO:0000255|HAMAP-Rule:MF_00736}; GN OrderedLocusNames=MJ0373; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Forms part of the ribosomal stalk which helps the CC ribosome interact with GTP-bound translation factors. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- SUBUNIT: Part of the ribosomal stalk of the 50S ribosomal subunit. CC Interacts with L10 and the large rRNA to form the base of the CC stalk. L10 forms an elongated spine to which L12 dimers bind in a CC sequential fashion forming a multimeric L10(L12)X complex. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC -!- SIMILARITY: Belongs to the ribosomal protein L11P family. CC {ECO:0000255|HAMAP-Rule:MF_00736}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98362.1; -; Genomic_DNA. DR PIR; E64346; E64346. DR ProteinModelPortal; P54030; -. DR STRING; 243232.MJ_0373; -. DR EnsemblBacteria; AAB98362; AAB98362; MJ_0373. DR KEGG; mja:MJ_0373; -. DR eggNOG; arCOG04372; Archaea. DR eggNOG; COG0080; LUCA. DR InParanoid; P54030; -. DR KO; K02867; -. DR OMA; STCKAMG; -. DR PhylomeDB; P54030; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.10.250; -; 1. DR Gene3D; 3.30.1550.10; -; 1. DR HAMAP; MF_00736; Ribosomal_L11; 1. DR InterPro; IPR000911; Ribosomal_L11/L12. DR InterPro; IPR020783; Ribosomal_L11_C. DR InterPro; IPR020785; Ribosomal_L11_CS. DR InterPro; IPR020784; Ribosomal_L11_N. DR PANTHER; PTHR11661; PTHR11661; 1. DR Pfam; PF00298; Ribosomal_L11; 1. DR Pfam; PF03946; Ribosomal_L11_N; 1. DR SMART; SM00649; RL11; 1. DR SUPFAM; SSF46906; SSF46906; 1. DR SUPFAM; SSF54747; SSF54747; 1. DR PROSITE; PS00359; RIBOSOMAL_L11; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 161 50S ribosomal protein L11. FT /FTId=PRO_0000104435. SQ SEQUENCE 161 AA; 17490 MW; 2B3B00332D110A81 CRC64; MAKEVVEVLV TGGRATAGPP LGPAIGPLGV NVMQVVKEIN EKTKDYEGMQ VPVKVIVDTE TRKFEIEVGI PPTTALIKKE LGIETAAHEP RHEVVGNLTL EQVIKIAKMK KDAMLSYTLK NAVKEVLGTC GSMGVTVEGK DPKEVQKEID AGVYDEYFKE E // ID RIO1_METJA Reviewed; 290 AA. AC Q57886; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=RIO-type serine/threonine-protein kinase Rio1; DE EC=2.7.11.1; GN Name=rio1; OrderedLocusNames=MJ0444; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type CC Ser/Thr kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98431.1; -; Genomic_DNA. DR PIR; D64355; D64355. DR ProteinModelPortal; Q57886; -. DR STRING; 243232.MJ_0444; -. DR EnsemblBacteria; AAB98431; AAB98431; MJ_0444. DR KEGG; mja:MJ_0444; -. DR eggNOG; arCOG01180; Archaea. DR eggNOG; COG1718; LUCA. DR InParanoid; Q57886; -. DR KO; K07178; -. DR OMA; GDPRFHL; -. DR PhylomeDB; Q57886; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR000687; RIO_kinase. DR InterPro; IPR018935; RIO_kinase_CS. DR InterPro; IPR017407; Ser/Thr_kinase_Rio1. DR InterPro; IPR008266; Tyr_kinase_AS. DR PANTHER; PTHR10593:SF23; PTHR10593:SF23; 1. DR SMART; SM00090; RIO; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS01245; RIO1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 290 RIO-type serine/threonine-protein kinase FT Rio1. FT /FTId=PRO_0000213534. FT DOMAIN 76 290 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 82 90 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 214 214 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT METAL 219 219 Magnesium. {ECO:0000250}. FT METAL 231 231 Magnesium. {ECO:0000250}. FT BINDING 103 103 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 219 219 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 231 231 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. SQ SEQUENCE 290 AA; 34469 MW; 52A8045266B2ACAB CRC64; MSCYKVMPIA KNIDDELYEL NKLLSEKEEF QLDREYQKEI LEKERKFLED LKTANEVFDK RTLMTLFSLL AGKHLTEYIG IVNSGKEAVV FKARKGKFYR AVKVYRVATC DFKTMSKYIQ GDPRFHLRKS SRRQIIHAWV EKEFRNLRRA SEIINAPKAR LRRENVLVMD FVGYRGIPAP KLKDMQDLDW EKYFKIIKES MKKLYEEGEL VHGDLSEYNI LVKDDEPVFI DFSQSVITQH PLAHPLLIRD CINICNFFRR KRVDCNYKDL YKYITGKEID PIDEAMIKQL // ID RIO2_METJA Reviewed; 270 AA. AC Q58473; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 100. DE RecName: Full=RIO-type serine/threonine-protein kinase Rio2; DE EC=2.7.11.1; GN Name=rio2; OrderedLocusNames=MJ1073; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + a protein = ADP + a phosphoprotein. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the protein kinase superfamily. RIO-type CC Ser/Thr kinase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 protein kinase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00159}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99073.1; -; Genomic_DNA. DR PIR; H64433; H64433. DR ProteinModelPortal; Q58473; -. DR STRING; 243232.MJ_1073; -. DR EnsemblBacteria; AAB99073; AAB99073; MJ_1073. DR KEGG; mja:MJ_1073; -. DR eggNOG; arCOG01181; Archaea. DR eggNOG; COG0478; LUCA. DR InParanoid; Q58473; -. DR KO; K07179; -. DR OMA; HREGYTN; -. DR PhylomeDB; Q58473; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011009; Kinase-like_dom. DR InterPro; IPR000719; Prot_kinase_dom. DR InterPro; IPR030484; Rio2. DR InterPro; IPR015285; RIO2_wHTH_N. DR InterPro; IPR000687; RIO_kinase. DR InterPro; IPR018935; RIO_kinase_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR10593:SF36; PTHR10593:SF36; 1. DR Pfam; PF09202; Rio2_N; 1. DR SMART; SM00090; RIO; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF56112; SSF56112; 1. DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1. DR PROSITE; PS01245; RIO1; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; KW Serine/threonine-protein kinase; Transferase. FT CHAIN 1 270 RIO-type serine/threonine-protein kinase FT Rio2. FT /FTId=PRO_0000213535. FT DOMAIN 65 270 Protein kinase. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 72 77 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 158 164 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT NP_BIND 206 207 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT ACT_SITE 202 202 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT METAL 76 76 Magnesium 1. {ECO:0000250}. FT METAL 207 207 Magnesium 2. {ECO:0000250}. FT METAL 220 220 Magnesium 1. {ECO:0000250}. FT METAL 220 220 Magnesium 2. {ECO:0000250}. FT BINDING 93 93 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. FT BINDING 220 220 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00159}. SQ SEQUENCE 270 AA; 31881 MW; 837BCE317A8A5CDF CRC64; MRHHEWVPLD EIVRKAKMPE KDVLYRLKRL NKFGFVVRST YGYAVSMGGY DALAINAFVK KGILKAIGNK LGVGKEGDVY TVLLSDGREA VLKFHKHGRT CFTRGKRYRG YLADKHHISW LYVSRLTAER EFEILNELFP IVKVPEPIEW NRHAIIMGKV VGEELKRLDL SEFMSKEEIK DLFWKIIEEV KKAYEIGYIH GDLSEFNILL DENGDFVIID WPQAVPKYHP DAEFYLKRDI WNVIRYFKKY KIDKEDEKID VDKIFEYITK // ID RL10E_METJA Reviewed; 174 AA. AC Q57963; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=50S ribosomal protein L10e {ECO:0000255|HAMAP-Rule:MF_00448}; GN Name=rpl10e {ECO:0000255|HAMAP-Rule:MF_00448}; GN OrderedLocusNames=MJ0543; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L10e family. CC {ECO:0000255|HAMAP-Rule:MF_00448}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98535.1; -; Genomic_DNA. DR PIR; G64367; G64367. DR ProteinModelPortal; Q57963; -. DR STRING; 243232.MJ_0543; -. DR EnsemblBacteria; AAB98535; AAB98535; MJ_0543. DR KEGG; mja:MJ_0543; -. DR eggNOG; arCOG04113; Archaea. DR eggNOG; COG0197; LUCA. DR InParanoid; Q57963; -. DR KO; K02866; -. DR OMA; EHKMATG; -. DR PhylomeDB; Q57963; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.90.1170.10; -; 1. DR HAMAP; MF_00448; Ribosomal_L10e; 1. DR InterPro; IPR001197; Ribosomal_L10e. DR InterPro; IPR016180; Ribosomal_L10e/L16. DR InterPro; IPR022981; Ribosomal_L10e_arc. DR InterPro; IPR018255; Ribosomal_L10e_CS. DR Pfam; PF00252; Ribosomal_L16; 1. DR PIRSF; PIRSF005590; Ribosomal_L10; 1. DR SUPFAM; SSF54686; SSF54686; 1. DR TIGRFAMs; TIGR00279; uL16_euk_arch; 1. DR PROSITE; PS01257; RIBOSOMAL_L10E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 174 50S ribosomal protein L10e. FT /FTId=PRO_0000147135. SQ SEQUENCE 174 AA; 19576 MW; CB9BB339DA713968 CRC64; MASLRPNRCY RDVDKPPYTR KEYVKGVPQP KVVHFIMGNL SAEFPVKVNL VATRPIQIRH NALEAARVAA NKYLTKMCGR MGYKFQIRVY PHQILREHKM ATGAGADRIS DGMRLAFGKP IGTAARVKEG QAILTVWVNP DKFPAAKEAL RRAAMKLPVP CRIVIEQGKE LLKL // ID RL18_METJA Reviewed; 195 AA. AC P54044; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=50S ribosomal protein L18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN Name=rpl18 {ECO:0000255|HAMAP-Rule:MF_01337}; GN OrderedLocusNames=MJ0474; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This is one of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts the 5S and CC 23S rRNAs. {ECO:0000255|HAMAP-Rule:MF_01337}. CC -!- SIMILARITY: Belongs to the ribosomal protein L18P family. CC {ECO:0000255|HAMAP-Rule:MF_01337}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98463.1; -; Genomic_DNA. DR PIR; B64359; B64359. DR ProteinModelPortal; P54044; -. DR STRING; 243232.MJ_0474; -. DR EnsemblBacteria; AAB98463; AAB98463; MJ_0474. DR KEGG; mja:MJ_0474; -. DR eggNOG; arCOG04088; Archaea. DR eggNOG; COG0256; LUCA. DR InParanoid; P54044; -. DR KO; K02881; -. DR OMA; GNTPSAY; -. DR PhylomeDB; P54044; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0008097; F:5S rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_01337_A; Ribosomal_L18_A; 1. DR InterPro; IPR005485; Rbsml_L5_euk/L18_arc. DR InterPro; IPR025607; Rbsml_L5e/L18P_C. DR PANTHER; PTHR23410; PTHR23410; 1. DR Pfam; PF14204; Ribosomal_L18_c; 1. DR Pfam; PF17144; Ribosomal_L5e; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 195 50S ribosomal protein L18. FT /FTId=PRO_0000131405. SQ SEQUENCE 195 AA; 22354 MW; E2637368BAADECDF CRC64; MATGPTYRVK FRRRREAKTD YRKRLKLLLS RKPRLVARRT LNHCIAQIVL YDEKGDKTVV SAHSRELIKL GYKGHTGNLP SAYLTGYLLG KKALAKGYTE AVLDIGLHRA TKGNAIFAIL KGALDAGMEI PHGEEILPSE ERIRGEHIKA YAEMLKEQDE ERYKKQFSKY LEKGLEPEKL PEHFEEIKAK IDSMF // ID RISC_METJA Reviewed; 156 AA. AC Q58584; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Riboflavin synthase; DE EC=2.5.1.9; GN Name=ribC; OrderedLocusNames=MJ1184; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 2 6,7-dimethyl-8-(1-D-ribityl)lumazine = CC riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D- CC ribitylamino)uracil: step 2/2. CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99185.1; -; Genomic_DNA. DR PIR; G64447; G64447. DR PDB; 2B98; X-ray; 2.30 A; A/B/C/D/E=1-156. DR PDB; 2B99; X-ray; 2.22 A; A/B/C/D/E=1-156. DR PDB; 4Y7J; X-ray; 4.10 A; A/B/C/D/E=1-156. DR PDB; 4Y7K; X-ray; 3.50 A; A/B/C/D/E=2-156. DR PDBsum; 2B98; -. DR PDBsum; 2B99; -. DR PDBsum; 4Y7J; -. DR PDBsum; 4Y7K; -. DR ProteinModelPortal; Q58584; -. DR SMR; Q58584; 2-153. DR STRING; 243232.MJ_1184; -. DR EnsemblBacteria; AAB99185; AAB99185; MJ_1184. DR KEGG; mja:MJ_1184; -. DR eggNOG; arCOG01322; Archaea. DR eggNOG; COG1731; LUCA. DR InParanoid; Q58584; -. DR KO; K00793; -. DR OMA; GIVDTTF; -. DR PhylomeDB; Q58584; -. DR BioCyc; MetaCyc:MONOMER-14602; -. DR BRENDA; 2.5.1.9; 3260. DR UniPathway; UPA00275; UER00405. DR EvolutionaryTrace; Q58584; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro. DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC. DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.960; -; 1. DR InterPro; IPR002180; DMRL_synthase. DR InterPro; IPR006399; Ribfl_synth_arc. DR Pfam; PF00885; DMRL_synthase; 1. DR PIRSF; PIRSF015750; Ribfl_synth_arc; 1. DR SUPFAM; SSF52121; SSF52121; 1. DR TIGRFAMs; TIGR01506; ribC_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Riboflavin biosynthesis; Transferase. FT CHAIN 1 156 Riboflavin synthase. FT /FTId=PRO_0000134860. FT STRAND 4 12 {ECO:0000244|PDB:2B99}. FT HELIX 18 28 {ECO:0000244|PDB:2B99}. FT STRAND 33 41 {ECO:0000244|PDB:2B99}. FT HELIX 42 44 {ECO:0000244|PDB:2B99}. FT HELIX 45 55 {ECO:0000244|PDB:2B99}. FT STRAND 59 65 {ECO:0000244|PDB:2B99}. FT HELIX 71 91 {ECO:0000244|PDB:2B99}. FT STRAND 95 99 {ECO:0000244|PDB:2B99}. FT HELIX 102 104 {ECO:0000244|PDB:2B99}. FT STRAND 105 107 {ECO:0000244|PDB:2B99}. FT HELIX 108 131 {ECO:0000244|PDB:2B99}. FT HELIX 133 138 {ECO:0000244|PDB:2B99}. FT TURN 139 141 {ECO:0000244|PDB:2B99}. FT STRAND 146 148 {ECO:0000244|PDB:2B98}. SQ SEQUENCE 156 AA; 17495 MW; 6D65112C6B1320F5 CRC64; MTKKVGIVDT TFARVDMASI AIKKLKELSP NIKIIRKTVP GIKDLPVACK KLLEEEGCDI VMALGMPGKA EKDKVCAHEA SLGLMLAQLM TNKHIIEVFV HEDEAKDDKE LDWLAKRRAE EHAENVYYLL FKPEYLTRMA GKGLRQGFED AGPARE // ID RL19E_METJA Reviewed; 151 AA. AC P54043; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=50S ribosomal protein L19e {ECO:0000255|HAMAP-Rule:MF_01475}; GN Name=rpl19e {ECO:0000255|HAMAP-Rule:MF_01475}; GN OrderedLocusNames=MJ0473; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01475}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01475}. CC -!- SIMILARITY: Belongs to the ribosomal protein L19e family. CC {ECO:0000255|HAMAP-Rule:MF_01475}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98462.1; -; Genomic_DNA. DR PIR; A64359; A64359. DR ProteinModelPortal; P54043; -. DR STRING; 243232.MJ_0473; -. DR EnsemblBacteria; AAB98462; AAB98462; MJ_0473. DR KEGG; mja:MJ_0473; -. DR eggNOG; arCOG04089; Archaea. DR eggNOG; COG2147; LUCA. DR InParanoid; P54043; -. DR KO; K02885; -. DR OMA; LKCGENR; -. DR PhylomeDB; P54043; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.1200.60; -; 1. DR Gene3D; 1.10.1650.10; -; 1. DR Gene3D; 1.20.5.560; -; 1. DR HAMAP; MF_01475; Ribosomal_L19e; 1. DR InterPro; IPR027547; Ribosomal_L19/L19e. DR InterPro; IPR023638; Ribosomal_L19/L19e_CS. DR InterPro; IPR000196; Ribosomal_L19/L19e_dom. DR InterPro; IPR015972; Ribosomal_L19/L19e_dom1. DR InterPro; IPR015973; Ribosomal_L19/L19e_dom2. DR InterPro; IPR015974; Ribosomal_L19/L19e_dom3. DR Pfam; PF01280; Ribosomal_L19e; 1. DR SMART; SM01416; Ribosomal_L19e; 1. DR SUPFAM; SSF48140; SSF48140; 1. DR PROSITE; PS00526; RIBOSOMAL_L19E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 151 50S ribosomal protein L19e. FT /FTId=PRO_0000131189. SQ SEQUENCE 151 AA; 17630 MW; BFB46E99A0520FF0 CRC64; MIIMDVSVQR RMAAEILKCG IERVWIDPTQ LDRVKMAMSK DDIRALIKEG VIKKKQKKGI SSARVKKLKE QRKKGRRRGP GSRRGAAGAR TPPKERWMAT IRALRKTLKQ LRDSGKIDRK VYRKLYRMAK GGAFRSRSHL FLYMREHELL K // ID RL22_METJA Reviewed; 156 AA. AC P54033; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=50S ribosomal protein L22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN Name=rpl22 {ECO:0000255|HAMAP-Rule:MF_01331}; GN OrderedLocusNames=MJ0460; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This protein binds specifically to 23S rRNA. It makes CC multiple contacts with different domains of the 23S rRNA in the CC assembled 50S subunit and ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- FUNCTION: The globular domain of the protein is located near the CC polypeptide exit tunnel on the outside of the subunit, while an CC extended beta-hairpin is found that lines the wall of the exit CC tunnel in the center of the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01331}. CC -!- SIMILARITY: Belongs to the ribosomal protein L22P family. CC {ECO:0000255|HAMAP-Rule:MF_01331}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98449.1; -; Genomic_DNA. DR PIR; D64357; D64357. DR ProteinModelPortal; P54033; -. DR STRING; 243232.MJ_0460; -. DR EnsemblBacteria; AAB98449; AAB98449; MJ_0460. DR KEGG; mja:MJ_0460; -. DR eggNOG; arCOG04098; Archaea. DR eggNOG; COG0091; LUCA. DR InParanoid; P54033; -. DR KO; K02890; -. DR OMA; VHIQVIL; -. DR PhylomeDB; P54033; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.470.10; -; 1. DR HAMAP; MF_01331_A; Ribosomal_L22_A; 1. DR InterPro; IPR001063; Ribosomal_L22. DR InterPro; IPR018260; Ribosomal_L22/L17_CS. DR InterPro; IPR005721; Ribosomal_L22/L17_euk/arc. DR PANTHER; PTHR11593; PTHR11593; 1. DR Pfam; PF00237; Ribosomal_L22; 1. DR SUPFAM; SSF54843; SSF54843; 1. DR TIGRFAMs; TIGR01038; uL22_arch_euk; 1. DR PROSITE; PS00464; RIBOSOMAL_L22; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 156 50S ribosomal protein L22. FT /FTId=PRO_0000125275. SQ SEQUENCE 156 AA; 18039 MW; 58745761B5472C4E CRC64; MIMMGKLKYK IQVNPEKTAR AMGRNIPISR KHAREICKSI NGMKLDEAIK FLEDVIAMRR PVLFRRHCKK VGHRKGKLGW PAGRYPVKAA KAILKILQHA KANAEYKGLN TEKLRIKHIS TNKGITIKRY MPRAFGRATP KFQETVHIQV ILEEYH // ID RL13_METJA Reviewed; 137 AA. AC P54023; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 94. DE RecName: Full=50S ribosomal protein L13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN Name=rpl13 {ECO:0000255|HAMAP-Rule:MF_01366}; GN OrderedLocusNames=MJ0194; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This protein is one of the early assembly proteins of CC the 50S ribosomal subunit, although it is not seen to bind rRNA by CC itself. It is important during the early stages of 50S assembly. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01366}. CC -!- SIMILARITY: Belongs to the ribosomal protein L13P family. CC {ECO:0000255|HAMAP-Rule:MF_01366}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98174.1; -; Genomic_DNA. DR ProteinModelPortal; P54023; -. DR STRING; 243232.MJ_0194; -. DR EnsemblBacteria; AAB98174; AAB98174; MJ_0194. DR KEGG; mja:MJ_0194; -. DR eggNOG; arCOG04242; Archaea. DR eggNOG; COG0102; LUCA. DR InParanoid; P54023; -. DR KO; K02871; -. DR OMA; TYQEERE; -. DR PhylomeDB; P54023; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.90.1180.10; -; 1. DR HAMAP; MF_01366; Ribosomal_L13; 1. DR InterPro; IPR005822; Ribosomal_L13. DR InterPro; IPR023563; Ribosomal_L13_CS. DR InterPro; IPR023564; Ribosomal_L13_dom. DR InterPro; IPR005755; Ribosomal_L13_euk/arc. DR PANTHER; PTHR11545; PTHR11545; 1. DR Pfam; PF00572; Ribosomal_L13; 1. DR PIRSF; PIRSF002181; Ribosomal_L13; 1. DR SUPFAM; SSF52161; SSF52161; 1. DR TIGRFAMs; TIGR01077; L13_A_E; 1. DR PROSITE; PS00783; RIBOSOMAL_L13; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 137 50S ribosomal protein L13. FT /FTId=PRO_0000133760. SQ SEQUENCE 137 AA; 15786 MW; F92D686B0D9D0E29 CRC64; MTVIDAEGAI LGRLASEVAK RVLRGEEIVI VNAEMVVITG NKDWIIKTYQ EEREKKNVAN PRRFGPKFPR RPDDILRRTI RKMLPYKKPK GREAFKRVKV YVGNPKNLTV DEKISHKLNT TKYITLAELS KHLGAKF // ID RL14_METJA Reviewed; 132 AA. AC P54037; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=50S ribosomal protein L14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN Name=rpl14 {ECO:0000255|HAMAP-Rule:MF_01367}; GN OrderedLocusNames=MJ0466; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to 23S rRNA. Forms part of two intersubunit CC bridges in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L24e, part of which may contact the 16S rRNA in 2 CC intersubunit bridges. {ECO:0000255|HAMAP-Rule:MF_01367}. CC -!- SIMILARITY: Belongs to the ribosomal protein L14P family. CC {ECO:0000255|HAMAP-Rule:MF_01367}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98455.1; -; Genomic_DNA. DR PIR; B64358; B64358. DR ProteinModelPortal; P54037; -. DR SMR; P54037; 11-131. DR STRING; 243232.MJ_0466; -. DR EnsemblBacteria; AAB98455; AAB98455; MJ_0466. DR KEGG; mja:MJ_0466; -. DR eggNOG; arCOG04095; Archaea. DR eggNOG; COG0093; LUCA. DR InParanoid; P54037; -. DR KO; K02874; -. DR OMA; ELRKKTM; -. DR PhylomeDB; P54037; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.150.20; -; 1. DR HAMAP; MF_01367; Ribosomal_L14; 1. DR InterPro; IPR000218; Ribosomal_L14P. DR InterPro; IPR019971; Ribosomal_L14P_arc. DR InterPro; IPR019972; Ribosomal_L14P_CS. DR PANTHER; PTHR11761; PTHR11761; 1. DR Pfam; PF00238; Ribosomal_L14; 1. DR SMART; SM01374; Ribosomal_L14; 1. DR SUPFAM; SSF50193; SSF50193; 1. DR TIGRFAMs; TIGR03673; uL14_arch; 1. DR PROSITE; PS00049; RIBOSOMAL_L14; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 132 50S ribosomal protein L14. FT /FTId=PRO_0000128573. SQ SEQUENCE 132 AA; 14271 MW; C02B0EE98C742F3D CRC64; MKAIGSKPVR ALPVGARCIC ADNTGAKEVE IIAVRNYKGV ARRLPTARVG DMVIVTVKKG TPEMRKQVLP AVVIRQRKEI RRPDGTRVKF ADNAVVIVTP DGNPKGSDIK GPVAKEAAER WPGIARIAKI II // ID RL15_METJA Reviewed; 143 AA. AC P54047; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=50S ribosomal protein L15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN Name=rpl15 {ECO:0000255|HAMAP-Rule:MF_01341}; GN OrderedLocusNames=MJ0477; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01341}. CC -!- SIMILARITY: Belongs to the ribosomal protein L15P family. CC {ECO:0000255|HAMAP-Rule:MF_01341}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98466.1; -; Genomic_DNA. DR PIR; E64359; E64359. DR ProteinModelPortal; P54047; -. DR STRING; 243232.MJ_0477; -. DR EnsemblBacteria; AAB98466; AAB98466; MJ_0477. DR KEGG; mja:MJ_0477; -. DR eggNOG; arCOG00779; Archaea. DR eggNOG; COG0200; LUCA. DR InParanoid; P54047; -. DR KO; K02876; -. DR OMA; SHTHGWG; -. DR PhylomeDB; P54047; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.990.10; -; 1. DR HAMAP; MF_01341; Ribosomal_L15; 1. DR InterPro; IPR027386; 50S_Rbsml_prot_L15P_N. DR InterPro; IPR030878; Ribosomal_L15. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR Pfam; PF00828; Ribosomal_L27A; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR PROSITE; PS00475; RIBOSOMAL_L15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 143 50S ribosomal protein L15. FT /FTId=PRO_0000104863. SQ SEQUENCE 143 AA; 16107 MW; 2A78A8ABA578FF87 CRC64; MIRKKKKVKK IRGSRTCGGG SHKKRRGAGN KGGRGMAGGH KHKWTWIIKY CPDYFGKYGF KRHPSLVKRL ETINVGELEE IVLKNPDKFE KEDDKFVVDV IELGYEKVLG KGKVTIPMIV KAVEVSEKAR EKIEAVGGEV VEL // ID RL14E_METJA Reviewed; 80 AA. AC P54054; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=50S ribosomal protein L14e {ECO:0000255|HAMAP-Rule:MF_00721}; GN Name=rpl14e {ECO:0000255|HAMAP-Rule:MF_00721}; GN OrderedLocusNames=MJ0657; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L14e family. CC {ECO:0000255|HAMAP-Rule:MF_00721}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98652.1; -; Genomic_DNA. DR PIR; A64382; A64382. DR ProteinModelPortal; P54054; -. DR SMR; P54054; 1-76. DR STRING; 243232.MJ_0657; -. DR EnsemblBacteria; AAB98652; AAB98652; MJ_0657. DR KEGG; mja:MJ_0657; -. DR eggNOG; arCOG04167; Archaea. DR eggNOG; COG2163; LUCA. DR InParanoid; P54054; -. DR KO; K02875; -. DR OMA; YVVITGP; -. DR PhylomeDB; P54054; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_00721; Ribosomal_L14e; 1. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR023651; Ribosomal_L14e. DR InterPro; IPR008991; Translation_prot_SH3-like. DR SUPFAM; SSF50104; SSF50104; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 80 50S ribosomal protein L14e. FT /FTId=PRO_0000132046. SQ SEQUENCE 80 AA; 8739 MW; F3B78C1E42629C93 CRC64; MPAIEVGRVC IKTAGREAGK VCVIVDILDK NFVIVDGLVK RRRCNIKHLE PTEKKVDIPK GASTEEVKLA LDAAGLLKEE // ID RL1_METJA Reviewed; 219 AA. AC P54050; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-NOV-2015, entry version 102. DE RecName: Full=50S ribosomal protein L1 {ECO:0000255|HAMAP-Rule:MF_01318}; GN Name=rpl1 {ECO:0000255|HAMAP-Rule:MF_01318}; OrderedLocusNames=MJ0510; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP BINDING TO ENDOGENOUS 23S RRNA, AND BINDING TO METHANOCOCCUS VANNIELII RP L1 MRNA. RX PubMed=9746351; DOI=10.1046/j.1432-1327.1998.2560097.x; RA Koehrer C., Mayer C., Neumair O., Groebner P., Piendl W.; RT "Interaction of ribosomal L1 proteins from mesophilic and thermophilic RT Archaea and Bacteria with specific L1-binding sites on 23S rRNA and RT mRNA."; RL Eur. J. Biochem. 256:97-105(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS). RX PubMed=10801481; DOI=10.1016/S0969-2126(00)00116-7; RA Nevskaya N., Tischenko S., Fedorov R., Al-Karadaghi S., Liljas A., RA Kraft A., Piendl W., Garber M.B., Nikonov S.; RT "Archaeal ribosomal protein L1: the structure provides new insights RT into RNA binding of the L1 protein family."; RL Structure 8:363-371(2000). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS). RX PubMed=12037305; DOI=10.1107/S0907444902006157; RA Nevskaya N., Tishchenko S., Paveliev M., Smolinskaya Y., Fedorov R., RA Piendl W., Nakamura Y., Toyoda T., Garber M.B., Nikonov S.; RT "Structure of ribosomal protein L1 from Methanococcus RT thermolithotrophicus. Functionally important structural invariants on RT the L1 surface."; RL Acta Crystallogr. D 58:1023-1029(2002). RN [5] RP X-RAY CRYSTALLOGRAPHY (3.4 ANGSTROMS) IN COMPLEX WITH AN ENDOGENOUS L1 RP MRNA FRAGMENT. RX PubMed=15659579; DOI=10.1093/nar/gki194; RA Nevskaya N., Tishchenko S., Gabdoulkhakov A., Nikonova E., Nikonov O., RA Nikulin A., Platonova O., Garber M.B., Nikonov S., Piendl W.; RT "Ribosomal protein L1 recognizes the same specific structural motif in RT its target sites on the autoregulatory mRNA and 23S rRNA."; RL Nucleic Acids Res. 33:478-485(2005). CC -!- FUNCTION: Probably involved in E site tRNA release (By CC similarity). Binds directly to 23S rRNA. {ECO:0000250}. CC -!- FUNCTION: Protein L1 is also a translational repressor protein, it CC controls the translation of its operon by binding to its mRNA. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01318, ECO:0000269|PubMed:15659579}. CC -!- SIMILARITY: Belongs to the ribosomal protein L1P family. CC {ECO:0000255|HAMAP-Rule:MF_01318}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98500.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98500.1; ALT_INIT; Genomic_DNA. DR PIR; F64363; F64363. DR PDB; 1CJS; X-ray; 2.30 A; A=1-219. DR PDB; 1I2A; X-ray; 1.85 A; A=1-219. DR PDB; 1U63; X-ray; 3.40 A; A/C=1-219. DR PDB; 4LQ4; X-ray; 1.75 A; A=1-211. DR PDBsum; 1CJS; -. DR PDBsum; 1I2A; -. DR PDBsum; 1U63; -. DR PDBsum; 4LQ4; -. DR ProteinModelPortal; P54050; -. DR SMR; P54050; 1-214. DR STRING; 243232.MJ_0510; -. DR EnsemblBacteria; AAB98500; AAB98500; MJ_0510. DR KEGG; mja:MJ_0510; -. DR eggNOG; arCOG04289; Archaea. DR eggNOG; COG0081; LUCA. DR InParanoid; P54050; -. DR KO; K02863; -. DR OMA; DFFIAQA; -. DR PhylomeDB; P54050; -. DR EvolutionaryTrace; P54050; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015934; C:large ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-KW. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.190.20; -; 2. DR Gene3D; 3.40.50.790; -; 1. DR HAMAP; MF_01318_A; Ribosomal_L1_A; 1. DR InterPro; IPR002143; Ribosomal_L1. DR InterPro; IPR023674; Ribosomal_L1-like. DR InterPro; IPR028364; Ribosomal_L1/biogenesis. DR InterPro; IPR016094; Ribosomal_L1_2-a/b-sand. DR InterPro; IPR016095; Ribosomal_L1_3-a/b-sand. DR InterPro; IPR023669; Ribosomal_L1_arc. DR InterPro; IPR023673; Ribosomal_L1_CS. DR Pfam; PF00687; Ribosomal_L1; 1. DR PIRSF; PIRSF002155; Ribosomal_L1; 1. DR SUPFAM; SSF56808; SSF56808; 1. DR PROSITE; PS01199; RIBOSOMAL_L1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Repressor; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW Translation regulation; tRNA-binding. FT CHAIN 1 219 50S ribosomal protein L1. FT /FTId=PRO_0000125798. FT HELIX 3 16 {ECO:0000244|PDB:4LQ4}. FT STRAND 25 34 {ECO:0000244|PDB:4LQ4}. FT HELIX 40 42 {ECO:0000244|PDB:4LQ4}. FT STRAND 45 49 {ECO:0000244|PDB:4LQ4}. FT STRAND 60 63 {ECO:0000244|PDB:4LQ4}. FT HELIX 66 74 {ECO:0000244|PDB:4LQ4}. FT STRAND 78 80 {ECO:0000244|PDB:4LQ4}. FT HELIX 82 90 {ECO:0000244|PDB:4LQ4}. FT HELIX 92 101 {ECO:0000244|PDB:4LQ4}. FT STRAND 103 108 {ECO:0000244|PDB:4LQ4}. FT HELIX 109 111 {ECO:0000244|PDB:4LQ4}. FT HELIX 112 118 {ECO:0000244|PDB:4LQ4}. FT HELIX 120 123 {ECO:0000244|PDB:4LQ4}. FT HELIX 124 126 {ECO:0000244|PDB:4LQ4}. FT STRAND 131 133 {ECO:0000244|PDB:4LQ4}. FT HELIX 140 146 {ECO:0000244|PDB:4LQ4}. FT STRAND 149 153 {ECO:0000244|PDB:4LQ4}. FT STRAND 157 166 {ECO:0000244|PDB:4LQ4}. FT HELIX 171 188 {ECO:0000244|PDB:4LQ4}. FT HELIX 192 195 {ECO:0000244|PDB:4LQ4}. FT STRAND 196 203 {ECO:0000244|PDB:4LQ4}. SQ SEQUENCE 219 AA; 24793 MW; BEFF3E31B693F9EA CRC64; MDREALLQAV KEARELAKPR NFTQSFEFIA TLKEIDMRKP ENRIKTEVVL PHGRGKEAKI AVIGTGDLAK QAEELGLTVI RKEEIEELGK NKRKLRKIAK AHDFFIAQAD LMPLIGRYMG VILGPRGKMP KPVPANANIK PLVERLKKTV VINTRDKPYF QVLVGNEKMT DEQIVDNIEA VLNVVAKKYE KGLYHIKDAY VKLTMGPAVK VKKEKAKKK // ID RL29_METJA Reviewed; 70 AA. AC P54035; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=50S ribosomal protein L29P; GN Name=rpl29p; OrderedLocusNames=MJ0462; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L29P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98451.1; -; Genomic_DNA. DR PIR; F64357; F64357. DR ProteinModelPortal; P54035; -. DR STRING; 243232.MJ_0462; -. DR EnsemblBacteria; AAB98451; AAB98451; MJ_0462. DR KEGG; mja:MJ_0462; -. DR eggNOG; arCOG00785; Archaea. DR eggNOG; COG0255; LUCA. DR InParanoid; P54035; -. DR KO; K02904; -. DR OMA; IQREEGD; -. DR PhylomeDB; P54035; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.287.310; -; 1. DR HAMAP; MF_00374; Ribosomal_L29; 1. DR InterPro; IPR001854; Ribosomal_L29. DR InterPro; IPR018254; Ribosomal_L29_CS. DR Pfam; PF00831; Ribosomal_L29; 1. DR SUPFAM; SSF46561; SSF46561; 1. DR TIGRFAMs; TIGR00012; L29; 1. DR PROSITE; PS00579; RIBOSOMAL_L29; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 70 50S ribosomal protein L29P. FT /FTId=PRO_0000130511. SQ SEQUENCE 70 AA; 8082 MW; 95FC2D0736AF500A CRC64; MAILRADELR GMSMEELKEK LVELKRELLK ERASKAVAGA PSNPGRMREI RRTIARILTI MNEKKRMTSQ // ID RL2_METJA Reviewed; 242 AA. AC P54017; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-MAY-2016, entry version 93. DE RecName: Full=50S ribosomal protein L2 {ECO:0000255|HAMAP-Rule:MF_01320}; GN Name=rpl2 {ECO:0000255|HAMAP-Rule:MF_01320}; OrderedLocusNames=MJ0179; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins. Required for CC association of the 30S and 50S subunits to form the 70S ribosome, CC for tRNA binding and peptide bond formation. It has been suggested CC to have peptidyltransferase activity; this is somewhat CC controversial. Makes several contacts with the 16S rRNA in the 70S CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01320}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a bridge to the CC 30S subunit in the 70S ribosome. {ECO:0000255|HAMAP- CC Rule:MF_01320}. CC -!- SIMILARITY: Belongs to the ribosomal protein L2P family. CC {ECO:0000255|HAMAP-Rule:MF_01320}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98164.1; -; Genomic_DNA. DR ProteinModelPortal; P54017; -. DR STRING; 243232.MJ_0179; -. DR EnsemblBacteria; AAB98164; AAB98164; MJ_0179. DR KEGG; mja:MJ_0179; -. DR eggNOG; arCOG04067; Archaea. DR eggNOG; COG0090; LUCA. DR InParanoid; P54017; -. DR KO; K02886; -. DR OMA; HFRDPYK; -. DR PhylomeDB; P54017; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 4.10.950.10; -; 1. DR HAMAP; MF_01320_A; Ribosomal_L2_A; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022666; Rbsml_prot_L2_RNA-bd_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR002171; Ribosomal_L2. DR InterPro; IPR023672; Ribosomal_L2_arc. DR InterPro; IPR022669; Ribosomal_L2_C. DR InterPro; IPR022671; Ribosomal_L2_CS. DR InterPro; IPR014726; Ribosomal_L2_dom3. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR13691; PTHR13691; 1. DR Pfam; PF00181; Ribosomal_L2; 1. DR Pfam; PF03947; Ribosomal_L2_C; 1. DR PIRSF; PIRSF002158; Ribosomal_L2; 1. DR SMART; SM01383; Ribosomal_L2; 1. DR SMART; SM01382; Ribosomal_L2_C; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00467; RIBOSOMAL_L2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 242 50S ribosomal protein L2. FT /FTId=PRO_0000129715. SQ SEQUENCE 242 AA; 26103 MW; 3EEDFA3E2C7C0E73 CRC64; MGKRLISQRR GRGSSVYTCP SHKRRGEAKY RRFDELEKKG KVLGKIVDIL HDPGRSAPVA KVEYETGEEG LLVVPEGVKV GDIIECGVSA EIKPGNILPL GAIPEGIPVF NIETVPGDGG KLVRAGGCYA HILTHDGERT YVKLPSGHIK ALHSMCRATI GVVAGGGRKE KPFVKAGKKY HAMKAKAVKW PRVRGVAMNA VDHPFGGGRH QHTGKPTTVS RKKVPPGRKV GHISARRTGV RK // ID RL30E_METJA Reviewed; 110 AA. AC P54061; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=50S ribosomal protein L30e; GN Name=rpl30e; OrderedLocusNames=MJ1044; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L30e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99048.1; -; Genomic_DNA. DR PIR; C64430; C64430. DR PDB; 3CPQ; X-ray; 1.90 A; A/B=1-110. DR PDBsum; 3CPQ; -. DR ProteinModelPortal; P54061; -. DR STRING; 243232.MJ_1044; -. DR EnsemblBacteria; AAB99048; AAB99048; MJ_1044. DR KEGG; mja:MJ_1044; -. DR eggNOG; arCOG01752; Archaea. DR eggNOG; COG1911; LUCA. DR InParanoid; P54061; -. DR KO; K02908; -. DR OMA; NIPVYQH; -. DR PhylomeDB; P54061; -. DR EvolutionaryTrace; P54061; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.30; -; 1. DR HAMAP; MF_00481; Ribosomal_L30e; 1. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR000231; Ribosomal_L30e. DR InterPro; IPR022991; Ribosomal_L30e_CS. DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45. DR PANTHER; PTHR11449; PTHR11449; 1. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR SUPFAM; SSF55315; SSF55315; 1. DR PROSITE; PS00709; RIBOSOMAL_L30E_1; 1. DR PROSITE; PS00993; RIBOSOMAL_L30E_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein. FT CHAIN 1 110 50S ribosomal protein L30e. FT /FTId=PRO_0000146147. FT HELIX 8 19 {ECO:0000244|PDB:3CPQ}. FT STRAND 20 25 {ECO:0000244|PDB:3CPQ}. FT HELIX 26 34 {ECO:0000244|PDB:3CPQ}. FT STRAND 39 43 {ECO:0000244|PDB:3CPQ}. FT HELIX 49 61 {ECO:0000244|PDB:3CPQ}. FT STRAND 66 68 {ECO:0000244|PDB:3CPQ}. FT HELIX 73 79 {ECO:0000244|PDB:3CPQ}. FT STRAND 87 93 {ECO:0000244|PDB:3CPQ}. FT HELIX 99 104 {ECO:0000244|PDB:3CPQ}. SQ SEQUENCE 110 AA; 12134 MW; EBECA4E135E098B6 CRC64; MRRRENMDVN KAIRTAVDTG KVILGSKRTI KFVKHGEGKL VVLAGNIPKD LEEDVKYYAK LSNIPVYQHK ITSLELGAVC GKPFPVAALL VLDEGLSNIM ELVEKKEGGE // ID RL10_METJA Reviewed; 338 AA. AC P54049; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=50S ribosomal protein L10 {ECO:0000255|HAMAP-Rule:MF_00280}; DE AltName: Full=Acidic ribosomal protein P0 homolog {ECO:0000255|HAMAP-Rule:MF_00280}; DE AltName: Full=MjaL10; GN Name=rpl10 {ECO:0000255|HAMAP-Rule:MF_00280}; GN Synonyms=rplP0 {ECO:0000255|HAMAP-Rule:MF_00280}; GN OrderedLocusNames=MJ0509; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 10-221. RX PubMed=20399793; DOI=10.1016/j.jmb.2010.04.017; RA Kravchenko O., Mitroshin I., Nikonov S., Piendl W., Garber M.; RT "Structure of a two-domain N-terminal fragment of ribosomal protein RT L10 from Methanococcus jannaschii reveals a specific piece of the RT archaeal ribosomal stalk."; RL J. Mol. Biol. 399:214-220(2010). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central CC role in the interaction of the ribosome with GTP-bound translation CC factors. {ECO:0000305}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms part of the CC ribosomal stalk which helps the ribosome interact with GTP-bound CC translation factors. Forms a heptameric L10(L12)2(L12)2(L12)2 CC complex, where L10 forms an elongated spine to which the L12 CC dimers bind in a sequential fashion (Probable). {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ribosomal protein L10P family. CC {ECO:0000255|HAMAP-Rule:MF_00280}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98499.1; -; Genomic_DNA. DR PDB; 3JSY; X-ray; 1.60 A; A/B=10-221. DR PDBsum; 3JSY; -. DR ProteinModelPortal; P54049; -. DR STRING; 243232.MJ_0509; -. DR EnsemblBacteria; AAB98499; AAB98499; MJ_0509. DR KEGG; mja:MJ_0509; -. DR eggNOG; arCOG04288; Archaea. DR eggNOG; COG0244; LUCA. DR InParanoid; P54049; -. DR KO; K02864; -. DR OMA; IGTNDNP; -. DR PhylomeDB; P54049; -. DR EvolutionaryTrace; P54049; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.380; -; 2. DR HAMAP; MF_00280; Ribosomal_L10_arch; 1. DR InterPro; IPR022909; 50S_L10_arch. DR InterPro; IPR013522; Ribosomal_L10_N_arc. DR InterPro; IPR001790; Ribosomal_L10P. DR Pfam; PF00466; Ribosomal_L10; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 338 50S ribosomal protein L10. FT /FTId=PRO_0000154793. FT HELIX 11 26 {ECO:0000244|PDB:3JSY}. FT STRAND 27 34 {ECO:0000244|PDB:3JSY}. FT HELIX 40 50 {ECO:0000244|PDB:3JSY}. FT TURN 51 53 {ECO:0000244|PDB:3JSY}. FT STRAND 54 58 {ECO:0000244|PDB:3JSY}. FT HELIX 61 74 {ECO:0000244|PDB:3JSY}. FT HELIX 78 86 {ECO:0000244|PDB:3JSY}. FT STRAND 89 98 {ECO:0000244|PDB:3JSY}. FT HELIX 100 109 {ECO:0000244|PDB:3JSY}. FT STRAND 112 114 {ECO:0000244|PDB:3JSY}. FT STRAND 126 128 {ECO:0000244|PDB:3JSY}. FT STRAND 130 132 {ECO:0000244|PDB:3JSY}. FT HELIX 140 146 {ECO:0000244|PDB:3JSY}. FT STRAND 151 154 {ECO:0000244|PDB:3JSY}. FT STRAND 157 160 {ECO:0000244|PDB:3JSY}. FT STRAND 164 167 {ECO:0000244|PDB:3JSY}. FT HELIX 175 183 {ECO:0000244|PDB:3JSY}. FT STRAND 189 192 {ECO:0000244|PDB:3JSY}. FT STRAND 194 200 {ECO:0000244|PDB:3JSY}. FT STRAND 203 205 {ECO:0000244|PDB:3JSY}. FT HELIX 207 213 {ECO:0000244|PDB:3JSY}. SQ SEQUENCE 338 AA; 36751 MW; 63A6AFD357E3052D CRC64; METKVKAHVA PWKIEEVKTL KGLIKSKPVV AIVDMMDVPA PQLQEIRDKI RDKVKLRMSR NTLIIRALKE AAEELNNPKL AELANYVERG AAILVTDMNP FKLYKLLEEN KSPAPVRGGQ IAPCDIKVEK GSTGMPPGPF LGELKSVGIP AAIEKGKIAI KEDKVVVKKG EVVSPKLAAV LDRLGIKPIK VGLNILAVYE DGIIYTPDVL KVDEEKLLAD IQAAYQNAFN LAFNTAYPAK EVLPFLIQKA FINARALSVE TAFVTKETAG DILAKAQAQA LALASKLPDE ALDEDIKAKL SSVEVSAAPA AEEEKEEEKK EEEKKEEDTG AAGLALLF // ID RL12_METJA Reviewed; 102 AA. AC P54048; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=50S ribosomal protein L12 {ECO:0000255|HAMAP-Rule:MF_01478}; GN Name=rpl12 {ECO:0000255|HAMAP-Rule:MF_01478}; GN OrderedLocusNames=MJ0508; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Forms part of the ribosomal stalk, playing a central CC role in the interaction of the ribosome with GTP-bound translation CC factors. {ECO:0000255|HAMAP-Rule:MF_01478}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Homodimer, it forms CC part of the ribosomal stalk which helps the ribosome interact with CC GTP-bound translation factors. Forms a heptameric CC L10(L12)2(L12)2(L12)2 complex, where L10 forms an elongated spine CC to which the L12 dimers bind in a sequential fashion. CC {ECO:0000255|HAMAP-Rule:MF_01478}. CC -!- SIMILARITY: Belongs to the ribosomal protein L12P family. CC {ECO:0000255|HAMAP-Rule:MF_01478}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98498.1; -; Genomic_DNA. DR PIR; D64363; D64363. DR ProteinModelPortal; P54048; -. DR STRING; 243232.MJ_0508; -. DR EnsemblBacteria; AAB98498; AAB98498; MJ_0508. DR KEGG; mja:MJ_0508; -. DR eggNOG; arCOG04287; Archaea. DR eggNOG; COG2058; LUCA. DR InParanoid; P54048; -. DR KO; K02869; -. DR OMA; HSVGKEI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006414; P:translational elongation; IEA:InterPro. DR HAMAP; MF_01478; Ribosomal_L12_arch; 1. DR InterPro; IPR027534; Ribosomal_L12. DR InterPro; IPR022295; Ribosomal_L12_arc. DR TIGRFAMs; TIGR03685; ribo_P1_arch; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 102 50S ribosomal protein L12. FT /FTId=PRO_0000157630. SQ SEQUENCE 102 AA; 10363 MW; 35306FFDE967C52C CRC64; MEYIYAALLL HSAGKEITED AIKAVLSAAG VEVDDARVKA LVAGLEGVDI EEAIANAAMP VAAAPAAAAP AAAAEEKKEE EKKEEKKEED TAAVAGLAAL FG // ID RL18E_METJA Reviewed; 121 AA. AC P54022; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-MAY-2016, entry version 87. DE RecName: Full=50S ribosomal protein L18e {ECO:0000255|HAMAP-Rule:MF_00329}; GN Name=rpl18e {ECO:0000255|HAMAP-Rule:MF_00329}; GN OrderedLocusNames=MJ0193; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L18e family. CC {ECO:0000255|HAMAP-Rule:MF_00329}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98173.1; -; Genomic_DNA. DR ProteinModelPortal; P54022; -. DR STRING; 243232.MJ_0193; -. DR EnsemblBacteria; AAB98173; AAB98173; MJ_0193. DR KEGG; mja:MJ_0193; -. DR eggNOG; arCOG00780; Archaea. DR eggNOG; COG1727; LUCA. DR InParanoid; P54022; -. DR KO; K02883; -. DR OMA; VAAWKFS; -. DR PhylomeDB; P54022; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00329; Ribosomal_L18e; 1. DR InterPro; IPR001196; Ribosomal_L15_CS. DR InterPro; IPR000039; Ribosomal_L18e. DR InterPro; IPR021131; Ribosomal_L18e/L15P. DR InterPro; IPR022947; Ribosomal_L18e_arc. DR InterPro; IPR021132; Ribosomal_L18e_CS. DR PANTHER; PTHR10934; PTHR10934; 1. DR Pfam; PF17135; Ribosomal_L18; 1. DR SUPFAM; SSF52080; SSF52080; 1. DR PROSITE; PS01106; RIBOSOMAL_L18E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 121 50S ribosomal protein L18e. FT /FTId=PRO_0000132790. SQ SEQUENCE 121 AA; 13532 MW; C61544AB196CAA17 CRC64; MAKKITATNP RLVKLIEILK QESYKNQAKI WKDIARRLAK PRRRRAEVNL SKINRYTKEG DVVLVPGKVL GAGKLEHKVV VAAFAFSETA KKLIKEAGGE AITIEELIKR NPKGSNVKIM A // ID RL15E_METJA Reviewed; 194 AA. AC P54060; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=50S ribosomal protein L15e; GN Name=rpl15e; OrderedLocusNames=MJ0983; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L15e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98986.1; -; Genomic_DNA. DR PIR; G64422; G64422. DR ProteinModelPortal; P54060; -. DR SMR; P54060; 4-193. DR STRING; 243232.MJ_0983; -. DR EnsemblBacteria; AAB98986; AAB98986; MJ_0983. DR KEGG; mja:MJ_0983; -. DR eggNOG; arCOG04209; Archaea. DR eggNOG; COG1632; LUCA. DR InParanoid; P54060; -. DR KO; K02877; -. DR OMA; QRKKQSD; -. DR PhylomeDB; P54060; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 3.40.1120.10; -; 1. DR HAMAP; MF_00256; Ribosomal_L15e; 1. DR InterPro; IPR024794; Rbsml_L15e_core_dom. DR InterPro; IPR000439; Ribosomal_L15e. DR InterPro; IPR020926; Ribosomal_L15e_arc. DR InterPro; IPR020925; Ribosomal_L15e_CS. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR PANTHER; PTHR11847; PTHR11847; 1. DR Pfam; PF00827; Ribosomal_L15e; 1. DR SMART; SM01384; Ribosomal_L15e; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR PROSITE; PS01194; RIBOSOMAL_L15E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 194 50S ribosomal protein L15e. FT /FTId=PRO_0000127573. SQ SEQUENCE 194 AA; 22578 MW; 8FAEB77FEA99BF5C CRC64; MGIYKYIREA WKRPKESYVR QLLWERLQQW RREPAVVRIE RPTRLDRARA LGYKPKQGII VVRVRVRRGG LRKPRPKNSK KPATLGVNKI TMGKSIQRIA EERAARKYPN MEVLNSYWVG EDGKHKWYEV ILVDPYHPAI KADPQLNWLC TGKHRGRAFR GLTSAGKKGR GLRNKGIGAE KVRPSIRAHG RRGK // ID RL18A_METJA Reviewed; 76 AA. AC P54052; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=50S ribosomal protein L18Ae {ECO:0000255|HAMAP-Rule:MF_00273}; DE AltName: Full=50S ribosomal protein L20e {ECO:0000255|HAMAP-Rule:MF_00273}; DE AltName: Full=50S ribosomal protein LX {ECO:0000255|HAMAP-Rule:MF_00273}; GN Name=rpl18a {ECO:0000255|HAMAP-Rule:MF_00273}; GN Synonyms=rpl20e {ECO:0000255|HAMAP-Rule:MF_00273}, GN rplX {ECO:0000255|HAMAP-Rule:MF_00273}; OrderedLocusNames=MJ0595; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Binds 23S rRNA. CC {ECO:0000255|HAMAP-Rule:MF_00273}. CC -!- SIMILARITY: Belongs to the ribosomal protein L18Ae family. CC {ECO:0000255|HAMAP-Rule:MF_00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98588.1; -; Genomic_DNA. DR PIR; C64374; C64374. DR ProteinModelPortal; P54052; -. DR STRING; 243232.MJ_0595; -. DR EnsemblBacteria; AAB98588; AAB98588; MJ_0595. DR KEGG; mja:MJ_0595; -. DR eggNOG; arCOG04175; Archaea. DR eggNOG; COG2157; LUCA. DR InParanoid; P54052; -. DR KO; K02944; -. DR OMA; RITGIMS; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00273; Ribosomal_L18Ae; 1. DR InterPro; IPR028877; 50S_L18Ae/Ribosomal_L18a/L20. DR InterPro; IPR002768; 50S_L18Ae_archaea. DR InterPro; IPR023573; Ribosomal_L18a//L18Ae/LX. DR Pfam; PF01775; Ribosomal_L18A; 1. DR ProDom; PD010302; Ribosomal_LX; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 76 50S ribosomal protein L18Ae. FT /FTId=PRO_0000153698. SQ SEQUENCE 76 AA; 8860 MW; 7C14762642D01E80 CRC64; MAKIFRITGI MSKKGKDPLY FRKEYKALKP EDALEILYSE FGGRYKVKRS RIKILNIEEI KPEDVTDPVL KKLVTA // ID RL21_METJA Reviewed; 98 AA. AC P54013; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 89. DE RecName: Full=50S ribosomal protein L21e; GN Name=rpl21e; OrderedLocusNames=MJ0040; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L21e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98021.1; -; Genomic_DNA. DR ProteinModelPortal; P54013; -. DR STRING; 243232.MJ_0040; -. DR EnsemblBacteria; AAB98021; AAB98021; MJ_0040. DR KEGG; mja:MJ_0040; -. DR eggNOG; arCOG04129; Archaea. DR eggNOG; COG2139; LUCA. DR InParanoid; P54013; -. DR KO; K02889; -. DR OMA; VHLKIDP; -. DR PhylomeDB; P54013; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.30.70; -; 1. DR HAMAP; MF_00369; Ribosomal_L21e; 1. DR InterPro; IPR001147; Ribosomal_L21e. DR InterPro; IPR022856; Ribosomal_L21e_arc. DR InterPro; IPR018259; Ribosomal_L21e_CS. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR20981; PTHR20981; 1. DR Pfam; PF01157; Ribosomal_L21e; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR PROSITE; PS01171; RIBOSOMAL_L21E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 98 50S ribosomal protein L21e. FT /FTId=PRO_0000149689. SQ SEQUENCE 98 AA; 11329 MW; 22C9DC88DF7583A3 CRC64; MVQMSEGFRR KTRKKLSKHP RERGLYPITR ALREFKEGEY VHIVIDPSVH KGMPHPRFHG RTGIVVGKQG RAFIVKVRDG GKYKQIIAYP QHLRPATA // ID RL24E_METJA Reviewed; 70 AA. AC P54064; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=50S ribosomal protein L24e {ECO:0000255|HAMAP-Rule:MF_00773}; GN Name=rpl24e {ECO:0000255|HAMAP-Rule:MF_00773}; GN OrderedLocusNames=MJ1201; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00773}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00773}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00773}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L3 and L14. {ECO:0000255|HAMAP-Rule:MF_00773}. CC -!- SIMILARITY: Belongs to the ribosomal protein L24e family. CC {ECO:0000255|HAMAP-Rule:MF_00773}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99205.1; -; Genomic_DNA. DR PIR; H64449; H64449. DR ProteinModelPortal; P54064; -. DR STRING; 243232.MJ_1201; -. DR EnsemblBacteria; AAB99205; AAB99205; MJ_1201. DR KEGG; mja:MJ_1201; -. DR eggNOG; arCOG01950; Archaea. DR eggNOG; COG2075; LUCA. DR InParanoid; P54064; -. DR KO; K02896; -. DR OMA; PGTGKMF; -. DR PhylomeDB; P54064; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:1902626; P:assembly of large subunit precursor of preribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.30.170.20; -; 1. DR HAMAP; MF_00773; Ribosomal_L24e; 1. DR InterPro; IPR023438; Ribosomal_L24e. DR InterPro; IPR000988; Ribosomal_L24e-rel. DR InterPro; IPR023442; Ribosomal_L24e_CS. DR InterPro; IPR023441; Ribosomal_L24e_dom. DR InterPro; IPR011017; TRASH_dom. DR PANTHER; PTHR10792; PTHR10792; 1. DR Pfam; PF01246; Ribosomal_L24e; 1. DR SMART; SM00746; TRASH; 1. DR PROSITE; PS01073; RIBOSOMAL_L24E; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1 70 50S ribosomal protein L24e. FT /FTId=PRO_0000136916. FT ZN_FING 7 37 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00773}. FT METAL 7 7 Zinc. {ECO:0000255|HAMAP-Rule:MF_00773}. FT METAL 10 10 Zinc. {ECO:0000255|HAMAP-Rule:MF_00773}. FT METAL 33 33 Zinc. {ECO:0000255|HAMAP-Rule:MF_00773}. FT METAL 37 37 Zinc. {ECO:0000255|HAMAP-Rule:MF_00773}. SQ SEQUENCE 70 AA; 8249 MW; 3EB6DE18F26E6FCF CRC64; MPEWRTCSFC GYEIEPGKGK MVVEKDGTVL YFCSSKCEKS YRMGRNPRKL KWTKVYQDMK AELKKAQESQ // ID RL24_METJA Reviewed; 120 AA. AC P54038; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=50S ribosomal protein L24P {ECO:0000255|HAMAP-Rule:MF_01326}; GN Name=rpl24p {ECO:0000255|HAMAP-Rule:MF_01326}; GN OrderedLocusNames=MJ0467; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of two assembly initiator proteins, it binds CC directly to the 5'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. CC -!- FUNCTION: Located at the polypeptide exit tunnel on the outside of CC the subunit. {ECO:0000255|HAMAP-Rule:MF_01326}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01326}. CC -!- SIMILARITY: Belongs to the ribosomal protein L24P family. CC {ECO:0000255|HAMAP-Rule:MF_01326}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98456.1; -; Genomic_DNA. DR PIR; C64358; C64358. DR ProteinModelPortal; P54038; -. DR STRING; 243232.MJ_0467; -. DR EnsemblBacteria; AAB98456; AAB98456; MJ_0467. DR KEGG; mja:MJ_0467; -. DR eggNOG; arCOG04094; Archaea. DR eggNOG; COG0198; LUCA. DR InParanoid; P54038; -. DR KO; K02895; -. DR OMA; VRIMRGD; -. DR PhylomeDB; P54038; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR GO; GO:0042273; P:ribosomal large subunit biogenesis; IBA:GO_Central. DR Gene3D; 2.30.30.30; -; 1. DR HAMAP; MF_01326_A; Ribosomal_L24_A; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR005825; Ribosomal_L24/26_CS. DR InterPro; IPR005756; Ribosomal_L26/L24P_euk/arc. DR InterPro; IPR008991; Translation_prot_SH3-like. DR PANTHER; PTHR11143; PTHR11143; 1. DR Pfam; PF00467; KOW; 1. DR Pfam; PF16906; Ribosomal_L26; 1. DR SMART; SM00739; KOW; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR01080; rplX_A_E; 1. DR PROSITE; PS01108; RIBOSOMAL_L24; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 120 50S ribosomal protein L24P. FT /FTId=PRO_0000130770. SQ SEQUENCE 120 AA; 14103 MW; 0FA953D929D18176 CRC64; MAFTKSKQPR KQRKALFNAP LHLRRKVMSA MLSKELKEKL GKNAIPVRKG DVVRIMRGDF KGLEGEVIKV DLKRYRIYVE GANNKRQDGR EVPYPIHPSN VMIIKLYDKD EKRFKHIKNE // ID RL30_METJA Reviewed; 154 AA. AC P54046; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=50S ribosomal protein L30P {ECO:0000255|HAMAP-Rule:MF_01371}; GN Name=rpl30p {ECO:0000255|HAMAP-Rule:MF_01371}; GN OrderedLocusNames=MJ0476; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01371}. CC -!- SIMILARITY: Belongs to the ribosomal protein L30P family. CC {ECO:0000255|HAMAP-Rule:MF_01371}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98465.1; -; Genomic_DNA. DR PIR; D64359; D64359. DR ProteinModelPortal; P54046; -. DR STRING; 243232.MJ_0476; -. DR EnsemblBacteria; AAB98465; AAB98465; MJ_0476. DR KEGG; mja:MJ_0476; -. DR eggNOG; arCOG04086; Archaea. DR eggNOG; COG1841; LUCA. DR InParanoid; P54046; -. DR KO; K02907; -. DR OMA; KEGGQLG; -. DR PhylomeDB; P54046; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0044822; F:poly(A) RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR GO; GO:0000463; P:maturation of LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR Gene3D; 1.10.15.30; -; 1. DR Gene3D; 3.30.1390.20; -; 2. DR HAMAP; MF_01371_A; Ribosomal_L30_A; 1. DR InterPro; IPR005997; Ribosomal_L30_arc. DR InterPro; IPR023106; Ribosomal_L30_central_dom_arc. DR InterPro; IPR018038; Ribosomal_L30_CS. DR InterPro; IPR016082; Ribosomal_L30_ferredoxin-like. DR Pfam; PF00327; Ribosomal_L30; 1. DR SUPFAM; SSF55129; SSF55129; 1. DR TIGRFAMs; TIGR01309; uL30_arch; 1. DR PROSITE; PS00634; RIBOSOMAL_L30; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 154 50S ribosomal protein L30P. FT /FTId=PRO_0000104624. SQ SEQUENCE 154 AA; 17586 MW; 66F69859AD56798B CRC64; MAYAVIRIRG RVGVRRDIAD TLKMLRLHKV NHCVIIPETE TFKGMLQKVK DYVTWGEIDK DTLVKLILKR GRLPGNKKVN PEIIKELTGM DVEELAEKII NGEIKLKETP LKPVFRLHPP RKGFERGGIK KPFSVGGALG YRGEKINELL EKMM // ID RL34_METJA Reviewed; 89 AA. AC P54053; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=50S ribosomal protein L34e; GN Name=rpl34e; OrderedLocusNames=MJ0655; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L34e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98650.1; -; Genomic_DNA. DR PIR; G64381; G64381. DR STRING; 243232.MJ_0655; -. DR EnsemblBacteria; AAB98650; AAB98650; MJ_0655. DR KEGG; mja:MJ_0655; -. DR eggNOG; arCOG04168; Archaea. DR eggNOG; COG2174; LUCA. DR InParanoid; P54053; -. DR KO; K02915; -. DR OMA; YLCPRCL; -. DR PhylomeDB; P54053; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00349; Ribosomal_L34e; 1. DR InterPro; IPR008195; Ribosomal_L34Ae. DR InterPro; IPR018065; Ribosomal_L34e_CS. DR PANTHER; PTHR10759; PTHR10759; 1. DR Pfam; PF01199; Ribosomal_L34e; 1. DR PRINTS; PR01250; RIBOSOMALL34. DR PROSITE; PS01145; RIBOSOMAL_L34E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 89 50S ribosomal protein L34e. FT /FTId=PRO_0000131848. SQ SEQUENCE 89 AA; 10524 MW; D86DC72F53BFA0C6 CRC64; MPAPRYRSRS YRRIYRRTPG GRIVIHYKRR KPGKPKCAIC GAELHGVPRG RPVEIRKLPK SQRRPERPYG GYLCPRCLKR LMIQKARNL // ID RL39_METJA Reviewed; 51 AA. AC P54056; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 28-MAR-2003, sequence version 2. DT 17-FEB-2016, entry version 91. DE RecName: Full=50S ribosomal protein L39e; GN Name=rpl39e; OrderedLocusNames=MJ0689; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L39e family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98684.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98684.1; ALT_INIT; Genomic_DNA. DR PIR; A64386; A64386. DR ProteinModelPortal; P54056; -. DR STRING; 243232.MJ_0689; -. DR EnsemblBacteria; AAB98684; AAB98684; MJ_0689. DR KEGG; mja:MJ_0689; -. DR eggNOG; arCOG04177; Archaea. DR eggNOG; COG2167; LUCA. DR InParanoid; P54056; -. DR KO; K02924; -. DR OMA; KMRYWRR; -. DR PhylomeDB; P54056; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.1620.10; -; 1. DR HAMAP; MF_00629; Ribosomal_L39e; 1. DR InterPro; IPR000077; Ribosomal_L39. DR InterPro; IPR020083; Ribosomal_L39_CS. DR InterPro; IPR023626; Ribosomal_L39e_dom. DR PANTHER; PTHR19970; PTHR19970; 1. DR Pfam; PF00832; Ribosomal_L39; 1. DR SUPFAM; SSF48662; SSF48662; 1. DR PROSITE; PS00051; RIBOSOMAL_L39E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 51 50S ribosomal protein L39e. FT /FTId=PRO_0000127050. SQ SEQUENCE 51 AA; 6144 MW; CEF905E1570B3B30 CRC64; MGSNKPLGKK VRLAKALKQN RRVPLFVIVK TRGRVRFHPK MRYWRRKKLK A // ID RL23_METJA Reviewed; 86 AA. AC P54016; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=50S ribosomal protein L23P {ECO:0000255|HAMAP-Rule:MF_01369}; GN Name=rpl23p {ECO:0000255|HAMAP-Rule:MF_01369}; GN OrderedLocusNames=MJ0178; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to 23S rRNA. One of the proteins that surrounds CC the polypeptide exit tunnel on the outside of the ribosome. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Contacts protein L29. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC -!- SIMILARITY: Belongs to the ribosomal protein L23P family. CC {ECO:0000255|HAMAP-Rule:MF_01369}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98163.1; -; Genomic_DNA. DR PIR; C64322; C64322. DR ProteinModelPortal; P54016; -. DR STRING; 243232.MJ_0178; -. DR EnsemblBacteria; AAB98163; AAB98163; MJ_0178. DR KEGG; mja:MJ_0178; -. DR eggNOG; arCOG04072; Archaea. DR eggNOG; COG0089; LUCA. DR InParanoid; P54016; -. DR KO; K02892; -. DR OMA; TQVTMKG; -. DR PhylomeDB; P54016; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_01369_A; Ribosomal_L23_A; 1. DR HAMAP; MF_01369_B; Ribosomal_L23_B; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR019985; Ribosomal_L23. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR001014; Ribosomal_L23/L25_CS. DR InterPro; IPR013025; Ribosomal_L25/23. DR Pfam; PF00276; Ribosomal_L23; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR TIGRFAMs; TIGR03636; uL23_arch; 1. DR PROSITE; PS00050; RIBOSOMAL_L23; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 86 50S ribosomal protein L23P. FT /FTId=PRO_0000129437. SQ SEQUENCE 86 AA; 9856 MW; DE53C1A1A361697B CRC64; MDAFDVIKAP VVTEKTVRMI EEENKLVFYV DRRATKQDIK RAMKELFDVE VEKVNTLITP KGEKKAYVKL KEGYDASKIA ASLGIY // ID RL31_METJA Reviewed; 87 AA. AC P54009; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=50S ribosomal protein L31e; GN Name=rpl31e; OrderedLocusNames=MJ0049; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L31e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98030.1; -; Genomic_DNA. DR PIR; A64306; A64306. DR ProteinModelPortal; P54009; -. DR STRING; 243232.MJ_0049; -. DR EnsemblBacteria; AAB98030; AAB98030; MJ_0049. DR KEGG; mja:MJ_0049; -. DR eggNOG; arCOG04473; Archaea. DR eggNOG; COG2097; LUCA. DR InParanoid; P54009; -. DR KO; K02910; -. DR OMA; MEERIYT; -. DR PhylomeDB; P54009; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 3.10.440.10; -; 1. DR HAMAP; MF_00410; Ribosomal_L31e; 1. DR InterPro; IPR000054; Ribosomal_L31e. DR InterPro; IPR020052; Ribosomal_L31e_CS. DR InterPro; IPR023621; Ribosomal_L31e_dom. DR PANTHER; PTHR10956; PTHR10956; 1. DR Pfam; PF01198; Ribosomal_L31e; 1. DR ProDom; PD006030; Ribosomal_L31e; 1. DR SMART; SM01380; Ribosomal_L31e; 1. DR SUPFAM; SSF54575; SSF54575; 1. DR PROSITE; PS01144; RIBOSOMAL_L31E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 87 50S ribosomal protein L31e. FT /FTId=PRO_0000153794. SQ SEQUENCE 87 AA; 10205 MW; 74DEEF8900A1BF68 CRC64; MEVLMMEERI YTIPLRDVIN KSVRTKRAPR AIKKIKQFLK RHMKAEIVKI DNELNEKIWE RGIQKPPARV RVKAVKEGNV VIATLAE // ID RL41_METJA Reviewed; 22 AA. AC P54025; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=50S ribosomal protein L41e; GN Name=rpl41e; OrderedLocusNames=MJ0242; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L41e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98230.1; -; Genomic_DNA. DR PIR; C64330; C64330. DR STRING; 243232.MJ_0242; -. DR EnsemblBacteria; AAB98230; AAB98230; MJ_0242. DR KEGG; mja:MJ_0242; -. DR KO; K02928; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 22 50S ribosomal protein L41e. FT /FTId=PRO_0000198075. SQ SEQUENCE 22 AA; 3089 MW; F948D74DD4EC98CB CRC64; MRWKWYKKRL RRLKRERKRA RS // ID RL5_METJA Reviewed; 190 AA. AC P54040; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=50S ribosomal protein L5 {ECO:0000255|HAMAP-Rule:MF_01333}; GN Name=rpl5 {ECO:0000255|HAMAP-Rule:MF_01333}; OrderedLocusNames=MJ0469; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This is 1 of the proteins that binds and probably CC mediates the attachment of the 5S RNA into the large ribosomal CC subunit, where it forms part of the central protuberance. In the CC 70S ribosome it contacts protein S13 of the 30S subunit (bridge CC B1b), connecting the 2 subunits; this bridge is implicated in CC subunit movement. May contact the P site tRNA; the 5S rRNA and CC some of its associated proteins might help stabilize positioning CC of ribosome-bound tRNAs. {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit; contacts the 5S rRNA CC and probably tRNA. Forms a bridge to the 30S subunit in the 70S CC ribosome. {ECO:0000255|HAMAP-Rule:MF_01333}. CC -!- SIMILARITY: Belongs to the ribosomal protein L5P family. CC {ECO:0000255|HAMAP-Rule:MF_01333}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98458.1; -; Genomic_DNA. DR PIR; E64358; E64358. DR ProteinModelPortal; P54040; -. DR STRING; 243232.MJ_0469; -. DR EnsemblBacteria; AAB98458; AAB98458; MJ_0469. DR KEGG; mja:MJ_0469; -. DR eggNOG; arCOG04092; Archaea. DR eggNOG; COG0094; LUCA. DR InParanoid; P54040; -. DR KO; K02931; -. DR OMA; EDTMAWF; -. DR PhylomeDB; P54040; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01333_A; Ribosomal_L5_A; 1. DR InterPro; IPR002132; Ribosomal_L5. DR InterPro; IPR022804; Ribosomal_L5_arc. DR InterPro; IPR031309; Ribosomal_L5_C. DR InterPro; IPR020929; Ribosomal_L5_CS. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR031310; Ribosomal_L5_N. DR Pfam; PF00281; Ribosomal_L5; 1. DR Pfam; PF00673; Ribosomal_L5_C; 1. DR PIRSF; PIRSF002161; Ribosomal_L5; 1. DR SUPFAM; SSF55282; SSF55282; 1. DR PROSITE; PS00358; RIBOSOMAL_L5; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding; tRNA-binding. FT CHAIN 1 190 50S ribosomal protein L5. FT /FTId=PRO_0000125056. SQ SEQUENCE 190 AA; 22169 MW; BD05366973C3A533 CRC64; MSFEELWQKN PMLKPRIEKV VVNFGVGESG DRLTKGAQVI EELTGQKPIR TRAKQTNPSF GIRKKLPIGL KVTLRGKKAE EFLKNAFEAF QKEGKKLYDY SFDDYGNFSF GIHEHIDFPG QKYDPMIGIF GMDVCVTLER PGFRVKRRKR CRAKIPRRHR LTREEAIEFI EKTFGVKVER VLLEEEEETQ // ID RL40_METJA Reviewed; 47 AA. AC P54058; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=50S ribosomal protein L40e {ECO:0000255|HAMAP-Rule:MF_00788}; GN Name=rpl40e {ECO:0000255|HAMAP-Rule:MF_00788}; GN OrderedLocusNames=MJ0707; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L40e family. CC {ECO:0000255|HAMAP-Rule:MF_00788}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98701.1; -; Genomic_DNA. DR PIR; C64388; C64388. DR ProteinModelPortal; P54058; -. DR STRING; 243232.MJ_0707; -. DR EnsemblBacteria; AAB98701; AAB98701; MJ_0707. DR KEGG; mja:MJ_0707; -. DR eggNOG; arCOG04049; Archaea. DR eggNOG; COG1552; LUCA. DR InParanoid; P54058; -. DR KO; K02927; -. DR PhylomeDB; P54058; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00788; Ribosomal_L40e; 1. DR InterPro; IPR001975; Ribosomal_L40e. DR InterPro; IPR023657; Ribosomal_L40e_arc. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01020; Ribosomal_L40e; 1. DR SMART; SM01377; Ribosomal_L40e; 1. DR SUPFAM; SSF57829; SSF57829; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 47 50S ribosomal protein L40e. FT /FTId=PRO_0000138781. SQ SEQUENCE 47 AA; 5618 MW; 3C79E7CBCE9341E3 CRC64; MPFEEAMKRL FMKKICMRCN ARNPWRATKC RKCGYKGLRP KAKEPRG // ID RLME_METJA Reviewed; 245 AA. AC Q58771; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Ribosomal RNA large subunit methyltransferase E {ECO:0000255|HAMAP-Rule:MF_01547}; DE EC=2.1.1.166 {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=23S rRNA Um2552 methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; DE AltName: Full=rRNA (uridine-2'-O-)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_01547}; GN Name=rlmE {ECO:0000255|HAMAP-Rule:MF_01547}; GN Synonyms=rrmJ {ECO:0000255|HAMAP-Rule:MF_01547}; GN OrderedLocusNames=MJ1376; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Specifically methylates the uridine in position 2552 of CC 23S rRNA at the 2'-O position of the ribose in the fully assembled CC 50S ribosomal subunit. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uridine(2552) in 23S CC rRNA = S-adenosyl-L-homocysteine + 2'-O-methyluridine(2552) in 23S CC rRNA. {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01547}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase RlmE family. CC {ECO:0000255|HAMAP-Rule:MF_01547}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99383.1; -; Genomic_DNA. DR PIR; G64471; G64471. DR ProteinModelPortal; Q58771; -. DR STRING; 243232.MJ_1376; -. DR EnsemblBacteria; AAB99383; AAB99383; MJ_1376. DR KEGG; mja:MJ_1376; -. DR eggNOG; arCOG00079; Archaea. DR eggNOG; COG0293; LUCA. DR InParanoid; Q58771; -. DR KO; K02427; -. DR OMA; DKRWVLQ; -. DR PhylomeDB; Q58771; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008173; F:RNA methyltransferase activity; IBA:GO_Central. DR GO; GO:0008650; F:rRNA (uridine-2'-O-)-methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0001510; P:RNA methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01547; RNA_methyltr_E; 1. DR InterPro; IPR015507; rRNA-MeTfrase_E. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR004512; rRNA_MeTrfase_gammaproteobac. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR10920; PTHR10920; 1. DR Pfam; PF01728; FtsJ; 1. DR PIRSF; PIRSF005461; 23S_rRNA_mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00438; rrmJ; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 245 Ribosomal RNA large subunit FT methyltransferase E. FT /FTId=PRO_0000155567. FT ACT_SITE 163 163 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 58 58 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 60 60 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_01547}. FT BINDING 78 78 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 96 96 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. FT BINDING 123 123 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01547}. SQ SEQUENCE 245 AA; 28559 MW; 64C0FB31726FFD97 CRC64; MGRKDKRWVL QRKRDFYYKL AKKLKYRSRA SFKLMQLNEK FNVIKPGKIV LDLGCAPGGW MQVAREIVGD KGFVIGIDLQ PVKPFEYDNV VAIKGDFTLE ENLNKIRELI PNDEKKVDVV ISDASPNISG YWDIDHARSI DLVTTALQIA TEMLKERGNF VAKVFYGDMI DDYVNLVKKY FEKVYITKPQ ASRKESAEVY VIAKRYTGKK WEEEDKIKRV KKVENEDNEL LAKKIKEIRK LKSKK // ID RL32_METJA Reviewed; 146 AA. AC P54010; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=50S ribosomal protein L32e; GN Name=rpl32e; OrderedLocusNames=MJ0472; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein L32e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98461.1; -; Genomic_DNA. DR PIR; H64358; H64358. DR ProteinModelPortal; P54010; -. DR STRING; 243232.MJ_0472; -. DR EnsemblBacteria; AAB98461; AAB98461; MJ_0472. DR KEGG; mja:MJ_0472; -. DR eggNOG; arCOG00781; Archaea. DR eggNOG; COG1717; LUCA. DR InParanoid; P54010; -. DR KO; K02912; -. DR OMA; FKNDPKW; -. DR PhylomeDB; P54010; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00810; Ribosomal_L32e; 1. DR InterPro; IPR001515; Ribosomal_L32e. DR InterPro; IPR023654; Ribosomal_L32e_arc. DR InterPro; IPR018263; Ribosomal_L32e_CS. DR Pfam; PF01655; Ribosomal_L32e; 1. DR ProDom; PD003823; Ribosomal_L32e; 1. DR SMART; SM01393; Ribosomal_L32e; 1. DR SUPFAM; SSF52042; SSF52042; 1. DR PROSITE; PS00580; RIBOSOMAL_L32E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 146 50S ribosomal protein L32e. FT /FTId=PRO_0000131151. SQ SEQUENCE 146 AA; 17274 MW; 0347A94FF9BEB9A4 CRC64; MNRLLRLRFK LKMKKPDFIR QEAHRHKRLG EKWRRPKGRH SKMRLKWKEK PPVVEIGYRS PKAVRGLHPS GLEDVLVYNV KDLEKLNPET QGARIASTVG KRKKIEIIIR ARELGIRILN ISEEKQEELL KLAEKQEAQE VNETNE // ID RL37_METJA Reviewed; 61 AA. AC P54011; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=50S ribosomal protein L37e; GN Name=rpl37e; OrderedLocusNames=MJ0098; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000250}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the ribosomal protein L37e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98078.1; -; Genomic_DNA. DR PIR; B64312; B64312. DR ProteinModelPortal; P54011; -. DR SMR; P54011; 3-53. DR STRING; 243232.MJ_0098; -. DR EnsemblBacteria; AAB98078; AAB98078; MJ_0098. DR KEGG; mja:MJ_0098; -. DR eggNOG; arCOG04126; Archaea. DR eggNOG; COG2126; LUCA. DR InParanoid; P54011; -. DR KO; K02922; -. DR OMA; RIRRYSW; -. DR PhylomeDB; P54011; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.20.25.30; -; 1. DR HAMAP; MF_00547; Ribosomal_L37e; 1. DR InterPro; IPR011331; Ribosomal_L37ae/L37e. DR InterPro; IPR001569; Ribosomal_L37e. DR InterPro; IPR018267; Ribosomal_L37e_CS. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01907; Ribosomal_L37e; 1. DR ProDom; PD005132; Ribosomal_L37e; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR PROSITE; PS01077; RIBOSOMAL_L37E; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1 61 50S ribosomal protein L37e. FT /FTId=PRO_0000139729. FT ZN_FING 20 38 C4-type. {ECO:0000255}. FT METAL 20 20 Zinc. {ECO:0000250}. FT METAL 23 23 Zinc. {ECO:0000250}. FT METAL 35 35 Zinc. {ECO:0000250}. FT METAL 38 38 Zinc. {ECO:0000250}. SQ SEQUENCE 61 AA; 7258 MW; 435283F8858B20CE CRC64; MSKGTPSMGK RNKGSYHIRC RRCGRRAYHV RKKRCAACGF PNKRMRKYSW QNKKVNGKRI K // ID RL44E_METJA Reviewed; 94 AA. AC P54027; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=50S ribosomal protein L44e {ECO:0000255|HAMAP-Rule:MF_01476}; GN Name=rpl44e {ECO:0000255|HAMAP-Rule:MF_01476}; GN OrderedLocusNames=MJ0249; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_01476}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01476}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01476}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01476}. CC -!- SIMILARITY: Belongs to the ribosomal protein L44e family. CC {ECO:0000255|HAMAP-Rule:MF_01476}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98236.1; -; Genomic_DNA. DR PIR; B64331; B64331. DR ProteinModelPortal; P54027; -. DR STRING; 243232.MJ_0249; -. DR EnsemblBacteria; AAB98236; AAB98236; MJ_0249. DR KEGG; mja:MJ_0249; -. DR eggNOG; arCOG04109; Archaea. DR eggNOG; COG1631; LUCA. DR InParanoid; P54027; -. DR KO; K02929; -. DR OMA; LDLRFRC; -. DR PhylomeDB; P54027; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0070180; F:large ribosomal subunit rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.450.80; -; 1. DR HAMAP; MF_01476; Ribosomal_L44e; 1. DR InterPro; IPR000552; Ribosomal_L44e. DR InterPro; IPR011332; Ribosomal_zn-bd. DR PANTHER; PTHR10369; PTHR10369; 1. DR Pfam; PF00935; Ribosomal_L44; 1. DR ProDom; PD002841; Ribosomal_L44e; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR PROSITE; PS01172; RIBOSOMAL_L44E; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1 94 50S ribosomal protein L44e. FT /FTId=PRO_0000149151. FT ZN_FING 11 73 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_01476}. FT METAL 11 11 Zinc. {ECO:0000255|HAMAP-Rule:MF_01476}. FT METAL 14 14 Zinc. {ECO:0000255|HAMAP-Rule:MF_01476}. FT METAL 70 70 Zinc. {ECO:0000255|HAMAP-Rule:MF_01476}. FT METAL 73 73 Zinc. {ECO:0000255|HAMAP-Rule:MF_01476}. SQ SEQUENCE 94 AA; 11029 MW; 57C5EC30ACC13BD7 CRC64; MKIPKKVRRY CPYCKKHTIH IVEKAKKGKP SELTWGQRQF RRVTAGYGGF PRPLPDRSKP VKKIDLRFKC TECGKMHTKA NGCFRSGRFE FVEK // ID RL4_METJA Reviewed; 252 AA. AC P54015; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=50S ribosomal protein L4 {ECO:0000255|HAMAP-Rule:MF_01328}; GN Name=rpl4 {ECO:0000255|HAMAP-Rule:MF_01328}; OrderedLocusNames=MJ0177; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins, this protein CC initially binds near the 5'-end of the 23S rRNA. It is important CC during the early stages of 50S assembly. It makes multiple CC contacts with different domains of the 23S rRNA in the assembled CC 50S subunit and ribosome. {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- FUNCTION: Forms part of the polypeptide exit tunnel. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01328}. CC -!- SIMILARITY: Belongs to the ribosomal protein L4P family. CC {ECO:0000255|HAMAP-Rule:MF_01328}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98162.1; -; Genomic_DNA. DR PIR; B64322; B64322. DR ProteinModelPortal; P54015; -. DR STRING; 243232.MJ_0177; -. DR EnsemblBacteria; AAB98162; AAB98162; MJ_0177. DR KEGG; mja:MJ_0177; -. DR eggNOG; arCOG04071; Archaea. DR eggNOG; COG0088; LUCA. DR InParanoid; P54015; -. DR KO; K02930; -. DR OMA; QANRKQD; -. DR PhylomeDB; P54015; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1370.10; -; 1. DR HAMAP; MF_01328_A; Ribosomal_L4_A; 1. DR InterPro; IPR002136; Ribosomal_L4/L1e. DR InterPro; IPR013000; Ribosomal_L4/L1e_euk/arc_CS. DR InterPro; IPR023574; Ribosomal_L4_dom. DR InterPro; IPR019970; Ribosomall_L4. DR Pfam; PF00573; Ribosomal_L4; 1. DR SUPFAM; SSF52166; SSF52166; 1. DR TIGRFAMs; TIGR03672; rpl4p_arch; 1. DR PROSITE; PS00939; RIBOSOMAL_L1E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 252 50S ribosomal protein L4. FT /FTId=PRO_0000129332. SQ SEQUENCE 252 AA; 27810 MW; 2C5E8C78F5C0BCF0 CRC64; MKAVVYNLNG EAVKEIDLPA VFEEEYRPDL IKRAFLSAFT ARLQPKGSDP LAGLRTSAKN IGKGHGRARV DRVPQGWAAR VPQAVGGRRA HPPKVEKILW ERVNKKERIK AIKSAIAATA NPELVKERGH VFETENLPII VESSFEELQK TKDVFAVFEK LGISDDVIRA KNGIKIRAGK GKMRGRKYKK PRSILVVVGD KCNAILASRN LPGVDVITAK DLGIIHLAPG GVAGRLTVWT ESALEKLKER FE // ID RL6_METJA Reviewed; 182 AA. AC P54042; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=50S ribosomal protein L6 {ECO:0000255|HAMAP-Rule:MF_01365}; GN Name=rpl6 {ECO:0000255|HAMAP-Rule:MF_01365}; OrderedLocusNames=MJ0471; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: This protein binds to the 23S rRNA, and is important in CC its secondary structure. It is located near the subunit interface CC in the base of the L7/L12 stalk, and near the tRNA binding site of CC the peptidyltransferase center. {ECO:0000255|HAMAP-Rule:MF_01365}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01365}. CC -!- SIMILARITY: Belongs to the ribosomal protein L6P family. CC {ECO:0000255|HAMAP-Rule:MF_01365}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98460.1; -; Genomic_DNA. DR PIR; G64358; G64358. DR ProteinModelPortal; P54042; -. DR STRING; 243232.MJ_0471; -. DR EnsemblBacteria; AAB98460; AAB98460; MJ_0471. DR KEGG; mja:MJ_0471; -. DR eggNOG; arCOG04090; Archaea. DR eggNOG; COG0097; LUCA. DR InParanoid; P54042; -. DR KO; K02933; -. DR OMA; RLWYPDI; -. DR PhylomeDB; P54042; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0002181; P:cytoplasmic translation; IBA:GO_Central. DR Gene3D; 3.90.930.12; -; 2. DR HAMAP; MF_01365_A; Ribosomal_L6_A; 1. DR InterPro; IPR000702; Ribosomal_L6. DR InterPro; IPR020040; Ribosomal_L6_a/b-dom. DR InterPro; IPR002359; Ribosomal_L6_CS2. DR InterPro; IPR019907; Ribosomal_L6P_arc. DR PANTHER; PTHR11655; PTHR11655; 1. DR Pfam; PF00347; Ribosomal_L6; 2. DR PIRSF; PIRSF002162; Ribosomal_L6; 1. DR SUPFAM; SSF56053; SSF56053; 2. DR TIGRFAMs; TIGR03653; uL6_arch; 1. DR PROSITE; PS00700; RIBOSOMAL_L6_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 182 50S ribosomal protein L6. FT /FTId=PRO_0000131085. SQ SEQUENCE 182 AA; 20655 MW; 3AB894EDB2AC18E3 CRC64; MPVAAYIEER VKIPENVQVE INNNEVVVKS GGKELRRRFE HPKIVIKKEG DEIVIFCEYP RRKDKAMVGT IRAHINNMIK GVTEGFTYKL KIRYAHFPMK VSVKGNEVII ENFLGEKHPR RARIMEGVTV KISGEDVIVT GIDKEKVGQT AANIEQATRI KGRDPRVFQD GIYIVEKAGK AI // ID RL37A_METJA Reviewed; 92 AA. AC P54051; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=50S ribosomal protein L37Ae {ECO:0000255|HAMAP-Rule:MF_00327}; DE AltName: Full=Ribosomal protein L43e {ECO:0000255|HAMAP-Rule:MF_00327}; GN Name=rpl37ae {ECO:0000255|HAMAP-Rule:MF_00327}; GN OrderedLocusNames=MJ0593; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds to the 23S rRNA. {ECO:0000255|HAMAP- CC Rule:MF_00327}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00327}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00327}; CC -!- SUBUNIT: Part of the 50S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00327}. CC -!- SIMILARITY: Belongs to the ribosomal protein L37Ae family. CC Putative zinc-binding subfamily. {ECO:0000255|HAMAP- CC Rule:MF_00327}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98587.1; -; Genomic_DNA. DR PIR; A64374; A64374. DR ProteinModelPortal; P54051; -. DR SMR; P54051; 11-82. DR STRING; 243232.MJ_0593; -. DR EnsemblBacteria; AAB98587; AAB98587; MJ_0593. DR KEGG; mja:MJ_0593; -. DR eggNOG; arCOG04208; Archaea. DR eggNOG; COG1997; LUCA. DR InParanoid; P54051; -. DR KO; K02921; -. DR OMA; RKCVGIW; -. DR PhylomeDB; P54051; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 2.20.25.30; -; 1. DR HAMAP; MF_00327; Ribosomal_L37Ae; 1. DR InterPro; IPR002674; Ribosomal_L37ae. DR InterPro; IPR011331; Ribosomal_L37ae/L37e. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01780; Ribosomal_L37ae; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR TIGRFAMs; TIGR00280; eL43_euk_arch; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc; KW Zinc-finger. FT CHAIN 1 92 50S ribosomal protein L37Ae. FT /FTId=PRO_0000139843. FT ZN_FING 39 60 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00327}. FT METAL 39 39 Zinc. {ECO:0000255|HAMAP-Rule:MF_00327}. FT METAL 42 42 Zinc. {ECO:0000255|HAMAP-Rule:MF_00327}. FT METAL 57 57 Zinc. {ECO:0000255|HAMAP-Rule:MF_00327}. FT METAL 60 60 Zinc. {ECO:0000255|HAMAP-Rule:MF_00327}. SQ SEQUENCE 92 AA; 10183 MW; 63DC201CCE508F9D CRC64; MFSHTKKVGP TGRFGPRYGL KIRVRVRDVE IKAKKKYKCP VCGFPKLKRA STSIWVCGKC GAKIAGGAYT PETGAGKAVM KAIRRIVERK EE // ID RL3_METJA Reviewed; 335 AA. AC P54014; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=50S ribosomal protein L3 {ECO:0000255|HAMAP-Rule:MF_01325}; GN Name=rpl3 {ECO:0000255|HAMAP-Rule:MF_01325}; OrderedLocusNames=MJ0176; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly near the 3'-end of the 23S rRNA, where it nucleates CC assembly of the 50S subunit. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Forms a cluster with CC proteins L14 and L24e. {ECO:0000255|HAMAP-Rule:MF_01325}. CC -!- SIMILARITY: Belongs to the ribosomal protein L3P family. CC {ECO:0000255|HAMAP-Rule:MF_01325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98161.1; -; Genomic_DNA. DR PIR; A64322; A64322. DR ProteinModelPortal; P54014; -. DR STRING; 243232.MJ_0176; -. DR EnsemblBacteria; AAB98161; AAB98161; MJ_0176. DR KEGG; mja:MJ_0176; -. DR eggNOG; arCOG04070; Archaea. DR eggNOG; COG0087; LUCA. DR InParanoid; P54014; -. DR KO; K02906; -. DR OMA; SPTEGME; -. DR PhylomeDB; P54014; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022625; C:cytosolic large ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000027; P:ribosomal large subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_01325_A; Ribosomal_L3_A; 1. DR InterPro; IPR000597; Ribosomal_L3. DR InterPro; IPR019928; Ribosomal_L3_arc. DR InterPro; IPR019926; Ribosomal_L3_CS. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF00297; Ribosomal_L3; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR TIGRFAMs; TIGR03626; L3_arch; 1. DR PROSITE; PS00474; RIBOSOMAL_L3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 335 50S ribosomal protein L3. FT /FTId=PRO_0000077210. SQ SEQUENCE 335 AA; 38117 MW; 63241BDE7DEF81C3 CRC64; MGLNINRPRR GSLAFSPRKR AKRPVPRIRS WPEEDTVRLQ AFPVYKAGMS HAFIKEDNPK SPNAGQEVFT PITILEAPPI NVCAIRVYGR NERNYLTTLT EVWADNLDKE LERKIKLPKK EDRKTVEDLE ALKDKIEDVR VLVHTNPKLT CLPKKKPEIL EIRIGGKDIE ERLNYAKEIL GKQLNITDVF QEGELVDTIG VTKGKGFQGQ VKRWGVKIQF GKHARKGVGR HVGSIGPWQP KMVMWSVPMP GQMGYHQRTE YNKRILKIGN NGDEITPKGG FLHYGVIRNN YVVLKGSVQG PAKRLIVLRR AIRPQEPLIK VPEITYISTT SKQGK // ID RL7A_METJA Reviewed; 117 AA. AC P54066; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-NOV-2015, entry version 105. DE RecName: Full=50S ribosomal protein L7Ae {ECO:0000255|HAMAP-Rule:MF_00326}; DE AltName: Full=Ribosomal protein L8e {ECO:0000255|HAMAP-Rule:MF_00326}; GN Name=rpl7ae {ECO:0000255|HAMAP-Rule:MF_00326}; GN OrderedLocusNames=MJ1203; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS), AND RNA-BINDING. RX PubMed=15130481; DOI=10.1016/j.str.2004.03.015; RA Hamma T., Ferre-D'Amare A.R.; RT "Structure of protein L7Ae bound to a K-turn derived from an archaeal RT box H/ACA sRNA at 1.8 A resolution."; RL Structure 12:893-903(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.45 ANGSTROMS). RX PubMed=16008351; DOI=10.1021/bi050568q; RA Suryadi J., Tran E.J., Maxwell E.S., Brown B.A. II; RT "The crystal structure of the Methanocaldococcus jannaschii RT multifunctional L7Ae RNA-binding protein reveals an induced-fit RT interaction with the box C/D RNAs."; RL Biochemistry 44:9657-9672(2005). CC -!- FUNCTION: Multifunctional RNA-binding protein that recognizes the CC K-turn motif in ribosomal RNA, the RNA component of RNase P, box CC H/ACA, box C/D and box C'/D' sRNAs. CC -!- SUBUNIT: Part of the 50S ribosomal subunit. Probably part of the CC RNase P complex. {ECO:0000255|HAMAP-Rule:MF_00326}. CC -!- INTERACTION: CC Q58105:MJ0694; NbExp=4; IntAct=EBI-2944269, EBI-2944259; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00326}. CC -!- SIMILARITY: Belongs to the ribosomal protein L7Ae family. CC {ECO:0000255|HAMAP-Rule:MF_00326}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99207.1; -; Genomic_DNA. DR PDB; 1RA4; X-ray; 1.86 A; A=1-117. DR PDB; 1SDS; X-ray; 1.80 A; A/B/C=1-117. DR PDB; 1XBI; X-ray; 1.45 A; A=1-117. DR PDB; 3PAF; X-ray; 1.70 A; A/B=1-117. DR PDBsum; 1RA4; -. DR PDBsum; 1SDS; -. DR PDBsum; 1XBI; -. DR PDBsum; 3PAF; -. DR ProteinModelPortal; P54066; -. DR SMR; P54066; 1-117. DR IntAct; P54066; 2. DR STRING; 243232.MJ_1203; -. DR EnsemblBacteria; AAB99207; AAB99207; MJ_1203. DR KEGG; mja:MJ_1203; -. DR eggNOG; arCOG01751; Archaea. DR eggNOG; COG1358; LUCA. DR InParanoid; P54066; -. DR KO; K02936; -. DR OMA; FIETQDD; -. DR PhylomeDB; P54066; -. DR EvolutionaryTrace; P54066; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.30; -; 1. DR HAMAP; MF_00326; Ribosomal_L7Ae_Arch; 1. DR InterPro; IPR029064; L30e-like. DR InterPro; IPR004038; Ribosomal_L7Ae/L30e/S12e/Gad45. DR InterPro; IPR018492; Ribosomal_L7Ae/L8/Nhp2. DR InterPro; IPR022481; Ribosomal_L7Ae_arc. DR InterPro; IPR004037; Ribosomal_L7Ae_CS. DR InterPro; IPR000948; Ribosomal_L7Ae_prok. DR Pfam; PF01248; Ribosomal_L7Ae; 1. DR PRINTS; PR00881; L7ARS6FAMILY. DR PRINTS; PR00884; RIBOSOMALHS6. DR SUPFAM; SSF55315; SSF55315; 1. DR TIGRFAMs; TIGR03677; eL8_ribo; 1. DR PROSITE; PS01082; RIBOSOMAL_L7AE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; KW tRNA processing. FT CHAIN 1 117 50S ribosomal protein L7Ae. FT /FTId=PRO_0000136793. FT HELIX 11 22 {ECO:0000244|PDB:1XBI}. FT STRAND 25 30 {ECO:0000244|PDB:1XBI}. FT HELIX 31 39 {ECO:0000244|PDB:1XBI}. FT STRAND 44 50 {ECO:0000244|PDB:1XBI}. FT HELIX 55 57 {ECO:0000244|PDB:1XBI}. FT TURN 58 60 {ECO:0000244|PDB:1XBI}. FT HELIX 61 67 {ECO:0000244|PDB:1XBI}. FT STRAND 72 76 {ECO:0000244|PDB:1XBI}. FT HELIX 78 84 {ECO:0000244|PDB:1XBI}. FT STRAND 92 98 {ECO:0000244|PDB:1XBI}. FT HELIX 102 115 {ECO:0000244|PDB:1XBI}. SQ SEQUENCE 117 AA; 12686 MW; 7CAB706F09371BA6 CRC64; MAVYVKFKVP EEIQKELLDA VAKAQKIKKG ANEVTKAVER GIAKLVIIAE DVKPEEVVAH LPYLCEEKGI PYAYVASKQD LGKAAGLEVA ASSVAIINEG DAEELKVLIE KVNVLKQ // ID RNH2_METJA Reviewed; 230 AA. AC Q57599; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=Ribonuclease HII; DE Short=RNase HII; DE EC=3.1.26.4; GN Name=rnhB; OrderedLocusNames=MJ0135; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP COFACTOR, AND MUTAGENESIS OF ASP-7; GLU-8; ASP-112 AND ASP-149. RX PubMed=12534291; DOI=10.1021/bi026960a; RA Lai B., Li Y., Cao A., Lai L.; RT "Metal ion binding and enzymatic mechanism of Methanococcus jannaschii RT RNase HII."; RL Biochemistry 42:785-791(2003). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS). RX PubMed=10997908; DOI=10.1016/S0969-2126(00)00179-9; RA Lai L., Yokota H., Hung L.-W., Kim R., Kim S.-H.; RT "Crystal structure of archaeal RNase HII: a homologue of human major RT RNase H."; RL Structure 8:897-904(2000). CC -!- FUNCTION: Endonuclease that specifically degrades the RNA of RNA- CC DNA hybrids. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage to 5'- CC phosphomonoester. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC Note=Manganese or magnesium. Binds 1 divalent metal ion per CC monomer in the absence of substrate. May bind a second metal ion CC after substrate binding. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNase HII family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98116.1; -; Genomic_DNA. DR PIR; G64316; G64316. DR PDB; 1EKE; X-ray; 2.00 A; A/B=1-230. DR PDBsum; 1EKE; -. DR ProteinModelPortal; Q57599; -. DR SMR; Q57599; 1-225. DR STRING; 243232.MJ_0135; -. DR EnsemblBacteria; AAB98116; AAB98116; MJ_0135. DR KEGG; mja:MJ_0135; -. DR eggNOG; arCOG04121; Archaea. DR eggNOG; COG0164; LUCA. DR InParanoid; Q57599; -. DR KO; K03470; -. DR OMA; VCAFAIE; -. DR PhylomeDB; Q57599; -. DR EvolutionaryTrace; Q57599; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0032299; C:ribonuclease H2 complex; IBA:GO_Central. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0004523; F:RNA-DNA hybrid ribonuclease activity; IBA:GO_Central. DR GO; GO:0043137; P:DNA replication, removal of RNA primer; IBA:GO_Central. DR GO; GO:0006298; P:mismatch repair; IBA:GO_Central. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR Gene3D; 1.10.10.460; -; 1. DR Gene3D; 3.30.420.10; -; 1. DR HAMAP; MF_00052_A; RNase_HII_A; 1. DR InterPro; IPR004649; RNase_H2_suA. DR InterPro; IPR001352; RNase_HII/HIII. DR InterPro; IPR024567; RNase_HII/HIII_dom. DR InterPro; IPR020787; RNase_HII_arc. DR InterPro; IPR023160; RNase_HII_hlx-loop-hlx_cap_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR PANTHER; PTHR10954; PTHR10954; 1. DR Pfam; PF01351; RNase_HII; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR TIGRFAMs; TIGR00729; TIGR00729; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Endonuclease; Hydrolase; KW Magnesium; Manganese; Metal-binding; Nuclease; Reference proteome. FT CHAIN 1 230 Ribonuclease HII. FT /FTId=PRO_0000111663. FT METAL 7 7 Divalent metal cation. {ECO:0000250}. FT METAL 8 8 Divalent metal cation. {ECO:0000250}. FT METAL 112 112 Divalent metal cation. {ECO:0000250}. FT MUTAGEN 7 7 D->N: Reduces activity 800-fold. FT {ECO:0000269|PubMed:12534291}. FT MUTAGEN 8 8 E->Q: Reduces activity 700-fold. FT {ECO:0000269|PubMed:12534291}. FT MUTAGEN 112 112 D->N: Reduces activity 600-fold. FT {ECO:0000269|PubMed:12534291}. FT MUTAGEN 149 149 D->N: Reduces activity 800-fold. FT {ECO:0000269|PubMed:12534291}. FT STRAND 2 9 {ECO:0000244|PDB:1EKE}. FT STRAND 14 16 {ECO:0000244|PDB:1EKE}. FT STRAND 18 26 {ECO:0000244|PDB:1EKE}. FT HELIX 27 29 {ECO:0000244|PDB:1EKE}. FT HELIX 30 34 {ECO:0000244|PDB:1EKE}. FT TURN 35 37 {ECO:0000244|PDB:1EKE}. FT HELIX 46 59 {ECO:0000244|PDB:1EKE}. FT STRAND 60 67 {ECO:0000244|PDB:1EKE}. FT HELIX 69 75 {ECO:0000244|PDB:1EKE}. FT TURN 76 78 {ECO:0000244|PDB:1EKE}. FT HELIX 81 99 {ECO:0000244|PDB:1EKE}. FT STRAND 104 112 {ECO:0000244|PDB:1EKE}. FT HELIX 118 133 {ECO:0000244|PDB:1EKE}. FT TURN 134 137 {ECO:0000244|PDB:1EKE}. FT STRAND 139 145 {ECO:0000244|PDB:1EKE}. FT HELIX 148 150 {ECO:0000244|PDB:1EKE}. FT HELIX 153 176 {ECO:0000244|PDB:1EKE}. FT HELIX 188 201 {ECO:0000244|PDB:1EKE}. FT HELIX 213 221 {ECO:0000244|PDB:1EKE}. SQ SEQUENCE 230 AA; 26506 MW; C454324C0C801299 CRC64; MIIIGIDEAG RGPVLGPMVV CAFAIEKERE EELKKLGVKD SKELTKNKRA YLKKLLENLG YVEKRILEAE EINQLMNSIN LNDIEINAFS KVAKNLIEKL NIRDDEIEIY IDACSTNTKK FEDSFKDKIE DIIKERNLNI KIIAEHKADA KYPVVSAASI IAKAERDEII DYYKKIYGDI GSGYPSDPKT IKFLEDYFKK HKKLPDIART HWKTCKRILD KSKQTKLIIE // ID RPOA1_METJA Reviewed; 1341 AA. AC Q58445; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 106. DE RecName: Full=DNA-directed RNA polymerase subunit A'; DE EC=2.7.7.6; DE Contains: DE RecName: Full=Mja rpoA1 intein; DE AltName: Full=Mja rpol A' intein; GN Name=rpoA1; OrderedLocusNames=MJ1042; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99046.1; -; Genomic_DNA. DR ProteinModelPortal; Q58445; -. DR STRING; 243232.MJ_1042; -. DR EnsemblBacteria; AAB99046; AAB99046; MJ_1042. DR KEGG; mja:MJ_1042; -. DR eggNOG; arCOG03158; Archaea. DR eggNOG; arCOG04257; Archaea. DR eggNOG; COG0086; LUCA. DR eggNOG; COG1372; LUCA. DR InParanoid; Q58445; -. DR KO; K03041; -. DR OMA; YFFHAMG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 3. DR Gene3D; 3.10.28.10; -; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR000722; RNA_pol_asu. DR InterPro; IPR006592; RNA_pol_N. DR InterPro; IPR007080; RNA_pol_Rpb1_1. DR InterPro; IPR007066; RNA_pol_Rpb1_3. DR InterPro; IPR007083; RNA_pol_Rpb1_4. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR Pfam; PF04997; RNA_pol_Rpb1_1; 1. DR Pfam; PF00623; RNA_pol_Rpb1_2; 2. DR Pfam; PF04983; RNA_pol_Rpb1_3; 1. DR Pfam; PF05000; RNA_pol_Rpb1_4; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00663; RPOLA_N; 1. DR SUPFAM; SSF51294; SSF51294; 3. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; KW DNA-directed RNA polymerase; Metal-binding; Nucleotidyltransferase; KW Protein splicing; Reference proteome; Transcription; Transferase; KW Zinc; Zinc-finger. FT CHAIN 1 460 DNA-directed RNA polymerase subunit A', FT 1st part. {ECO:0000255}. FT /FTId=PRO_0000031062. FT CHAIN 461 911 Mja rpoA1 intein. {ECO:0000255}. FT /FTId=PRO_0000031063. FT CHAIN 912 1341 DNA-directed RNA polymerase subunit A', FT 2nd part. {ECO:0000255}. FT /FTId=PRO_0000031064. FT DOMAIN 616 783 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT ZN_FING 62 105 C4-type. {ECO:0000255}. SQ SEQUENCE 1341 AA; 152781 MW; 4D98546ED552AF12 CRC64; MERYEIPKEI GEIMFGLLSP DYIRQMSVAK IVTPDTYDED GYPIDGGLMD TRLGVIDPGL VCKTCGGRIG ECPGHFGHIE LAKPVIHIGF AKTIYKILKA VCPHCGRVAI SETKRKEILE KMEKLERDGG NKWEVCEEVY KEASKVTICP HCGEIKYDIK FEKPTTYYRI DGNEEKTLTP SDVREILEKI PDEDCILLGL NPEVARPEWM VLTVLPVPPV TVRPSITLET GERSEDDLTH KLVDIIRINN RLEENIEGGA PNLIIEDLWN LLQYHVNTYF DNEAPGIPPA KHRSGRPLKT LAQRLKGKEG RFRYNLAGKR VNFSSRTVIS PDPCLSINEV GVPEVVAKEL TVPEKVTKYN IERIRQLLRN GSEKHPGVNY VIRKMIGRDG TEQEYKVKIT ESNKDFWAEN IREGDIVERH LMDGDIVLYN RQPSLHRMSI MAHRVRVLPY RTFRHNLCVC VDGDTTVLLD GKLIKIKDLE DKWKDVKVLT SDDLNPKLTS LSKYWKLNAD EYGKKIYKIK TELGREIIAT EDHPFYTTNG RKRCGELKVG DEVIIYPNDF PMFEDDNRVI VDEEKIKKVI NNIGGTYKNK IINELKDRKL IPLTYNDQKA SILARIVGHV MGDGSLIINN KNSRVVFRGD IEDLKTIKED LKELGYDGEE IKLHEGETEI TDYNGKKRII KGKGYSFEVR KKSLCILLKA LGCVGGDKTK KMYGIPNWIK TAPKYIKKEF LSAYFGSELT TPKIRNHGTS FKELSFKIAK IEEIFDEDRF IKDIKEMLKE FGIELKVRVE EGNLRKDGYK TKVYVASIYN HKEFFGRIGY TYANKKETLA RYAYEYLLTK EKYLKDRNIK KLENNTKFIT FDKFIKEKCL KNGFVKEKIV SIEETKVDYV YDITTISETH NFIANGFLTG NCPPYNADFD GDEMNLHVPQ SEEARAEAEA LMLVEKHILS PRFGGPIIGA IHDFISGAYL LTSNYFTKDE ATLILRSGGI KDELWEPDKV ENGVPLYSGK KIFSKALPKG LNLRYKAKIC RKCDVCKKEE CEYDAYVVIK DGELIKGVID KNGYGAEAGL ILHTIVKEFG PEAGRKFLDS ATKMAIRAVM LRGFTTGIDD EDLPEEALKE IEKVLDEAEE KVKEIIEKYE RGELELLPGL NLEESREAYI SNVLREARDK AGAIAERYLG LDNHAVIMAV TGARGNILNL TQMAACLGQQ SVRGKRIFRG YRGRVLPHFE KGDLGARSHG FVRSSYKKGL SPTEFFFHAM GGREGLVDQA VRTAQSGYMQ RRLINALQDL KTEFDGTVRD SRGIMIQFKY GEDGIDPMLA DRGKAVNIDR IIDKVKMKYN Q // ID RPON_METJA Reviewed; 73 AA. AC Q57649; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 98. DE RecName: Full=DNA-directed RNA polymerase subunit N; DE EC=2.7.7.6; GN Name=rpoN; OrderedLocusNames=MJ0196; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SIMILARITY: Belongs to the archaeal RpoN/eukaryotic RPB10 RNA CC polymerase subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98176.1; -; Genomic_DNA. DR ProteinModelPortal; Q57649; -. DR SMR; Q57649; 2-52. DR STRING; 243232.MJ_0196; -. DR EnsemblBacteria; AAB98176; AAB98176; MJ_0196. DR KEGG; mja:MJ_0196; -. DR eggNOG; arCOG04244; Archaea. DR eggNOG; COG1644; LUCA. DR InParanoid; Q57649; -. DR KO; K03058; -. DR OMA; KKYCCRR; -. DR PhylomeDB; Q57649; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.60; -; 1. DR HAMAP; MF_00250; RNApol_arch_N; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR023580; RNA_pol_su_RPB10. DR InterPro; IPR020789; RNA_pol_suN_Zn-BS. DR InterPro; IPR000268; RNAP_N/Rpb10. DR Pfam; PF01194; RNA_pol_N; 1. DR PIRSF; PIRSF005653; RNA_pol_N/8_sub; 1. DR ProDom; PD006539; RNA_pol_N/8_sub; 1. DR SUPFAM; SSF46924; SSF46924; 1. DR PROSITE; PS01112; RNA_POL_N_8KD; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; Metal-binding; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase; Zinc. FT CHAIN 1 73 DNA-directed RNA polymerase subunit N. FT /FTId=PRO_0000121349. FT METAL 7 7 Zinc. {ECO:0000250}. FT METAL 10 10 Zinc. {ECO:0000250}. FT METAL 44 44 Zinc. {ECO:0000250}. FT METAL 45 45 Zinc. {ECO:0000250}. SQ SEQUENCE 73 AA; 8695 MW; E716EA406D65B831 CRC64; MMFPIRCFSC GNVIAEVFEE YKERILKGEN PKDVLDDLGI KKYCCRRMFI SYRIGEDGRE IIDEIIAHDE RYL // ID RNP4_METJA Reviewed; 128 AA. AC Q58372; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Ribonuclease P protein component 4 {ECO:0000255|HAMAP-Rule:MF_00757}; DE Short=RNase P component 4 {ECO:0000255|HAMAP-Rule:MF_00757}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00757}; DE AltName: Full=Rpp21 {ECO:0000255|HAMAP-Rule:MF_00757}; GN Name=rnp4 {ECO:0000255|HAMAP-Rule:MF_00757}; OrderedLocusNames=MJ0962; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18558617; DOI=10.1093/nar/gkn360; RA Pulukkunat D.K., Gopalan V.; RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into RT the roles of RNA and protein cofactors in RNase P catalysis."; RL Nucleic Acids Res. 36:4172-4180(2008). RN [3] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012; RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.; RT "Cooperative RNP assembly: complementary rescue of structural defects RT by protein and RNA subunits of archaeal RNase P."; RL J. Mol. Biol. 411:368-383(2011). RN [4] RP FUNCTION, INTERACTION WITH RNP1, AND SUBUNIT. RX PubMed=22298511; DOI=10.1093/nar/gks013; RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., RA Gopalan V.; RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional RT dependence of archaeal and eukaryal RNase P on multiple protein RT cofactors."; RL Nucleic Acids Res. 40:4666-4680(2012). CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates CC mature tRNA molecules by cleaving their 5'-ends. CC {ECO:0000255|HAMAP-Rule:MF_00757, ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00757}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00757}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00757}; CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4 CC protein subunits. Forms a subcomplex with Rnp1 which stimulates CC the catalytic RNA. {ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00757}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 4 family. {ECO:0000255|HAMAP-Rule:MF_00757}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98964.1; -; Genomic_DNA. DR PIR; B64420; B64420. DR ProteinModelPortal; Q58372; -. DR SMR; Q58372; 6-104. DR STRING; 243232.MJ_0962; -. DR EnsemblBacteria; AAB98964; AAB98964; MJ_0962. DR KEGG; mja:MJ_0962; -. DR eggNOG; arCOG04345; Archaea. DR eggNOG; COG2023; LUCA. DR InParanoid; Q58372; -. DR KO; K03540; -. DR OMA; ECGHIMR; -. DR PhylomeDB; Q58372; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-HAMAP. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0090501; P:RNA phosphodiester bond hydrolysis; IBA:GOC. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00757; RNase_P_4; 1. DR InterPro; IPR016432; RNase_P_comp-4. DR InterPro; IPR007175; Rpr2. DR PANTHER; PTHR14742; PTHR14742; 1. DR Pfam; PF04032; Rpr2; 1. DR PIRSF; PIRSF004878; RNase_P_4; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Metal-binding; KW Nuclease; Reference proteome; tRNA processing; Zinc. FT CHAIN 1 128 Ribonuclease P protein component 4. FT /FTId=PRO_0000153852. FT METAL 63 63 Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}. FT METAL 66 66 Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}. FT METAL 92 92 Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}. FT METAL 95 95 Zinc. {ECO:0000255|HAMAP-Rule:MF_00757}. SQ SEQUENCE 128 AA; 15567 MW; 462D677CE5B159D3 CRC64; MKKFLEKKLK KIAYERIDIL MSLAEEEAKK GNWDRAKRYV YLARRIAMKM RIRFPKKWKR RICKKCGTFL LYGRNARVRI KSKRYPHVVI TCLECGAIYR IPMIREKKEK RRKKLEERLK AKSNSQTS // ID RNZ_METJA Reviewed; 317 AA. AC Q58897; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 17-FEB-2016, entry version 94. DE RecName: Full=Ribonuclease Z {ECO:0000255|HAMAP-Rule:MF_01818}; DE Short=RNase Z {ECO:0000255|HAMAP-Rule:MF_01818}; DE EC=3.1.26.11 {ECO:0000255|HAMAP-Rule:MF_01818}; DE AltName: Full=tRNA 3 endonuclease {ECO:0000255|HAMAP-Rule:MF_01818}; DE AltName: Full=tRNase Z {ECO:0000255|HAMAP-Rule:MF_01818}; GN Name=rnz {ECO:0000255|HAMAP-Rule:MF_01818}; OrderedLocusNames=MJ1502; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=12032089; DOI=10.1093/emboj/21.11.2769; RA Schiffer S., Roesch S., Marchfelder A.; RT "Assigning a function to a conserved group of proteins: the tRNA 3' - RT processing enzymes."; RL EMBO J. 21:2769-2777(2002). CC -!- FUNCTION: Zinc phosphodiesterase, which displays some tRNA 3'- CC processing endonuclease activity. Probably involved in tRNA CC maturation, by removing a 3'-trailer from precursor tRNA. CC {ECO:0000255|HAMAP-Rule:MF_01818, ECO:0000269|PubMed:12032089}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing CC extra 3' nucleotides from tRNA precursor, generating 3' termini of CC tRNAs. A 3'-hydroxy group is left at the tRNA terminus and a 5'- CC phosphoryl group is left at the trailer molecule. CC {ECO:0000255|HAMAP-Rule:MF_01818, ECO:0000269|PubMed:12032089}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01818}; CC Note=Binds 2 Zn(2+) ions. {ECO:0000255|HAMAP-Rule:MF_01818}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01818}. CC -!- SIMILARITY: Belongs to the RNase Z family. {ECO:0000255|HAMAP- CC Rule:MF_01818}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99515.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99515.1; ALT_INIT; Genomic_DNA. DR PIR; E64487; E64487. DR ProteinModelPortal; Q58897; -. DR STRING; 243232.MJ_1502; -. DR EnsemblBacteria; AAB99515; AAB99515; MJ_1502. DR KEGG; mja:MJ_1502; -. DR eggNOG; arCOG00501; Archaea. DR eggNOG; COG1234; LUCA. DR InParanoid; Q58897; -. DR KO; K00784; -. DR OMA; SYAFCSD; -. DR PhylomeDB; Q58897; -. DR BRENDA; 3.1.26.11; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GOC. DR Gene3D; 3.60.15.10; -; 2. DR HAMAP; MF_01818; RNase_Z_BN; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR013471; RNase_Z/BN. DR Pfam; PF12706; Lactamase_B_2; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR02651; RNase_Z; 1. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Metal-binding; Nuclease; KW Reference proteome; tRNA processing; Zinc. FT CHAIN 1 317 Ribonuclease Z. FT /FTId=PRO_0000155924. FT ACT_SITE 67 67 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 63 63 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 65 65 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 67 67 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 68 68 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 143 143 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 213 213 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 213 213 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. FT METAL 273 273 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01818}. SQ SEQUENCE 317 AA; 36034 MW; 9D8EE7E824063ED3 CRC64; MIIMKLIFLG TGAAVPSKNR NHIGIAFKFG GEVFLFDCGE NIQRQMLFTE VSPMKINHIF ITHLHGDHIL GIPGLLQSMG FFGREKELKI FGPEGTKEII ENSLKLGTHY IEFPIKVYEI YTKEPITIYK EENYEIIAYP TEHGIPSYAY IFKEIKKPRL DIEKAKKLGV KIGPDLKKLK NGEAVKNIYG EIIKPEYVLL PPKKGFCLAY SGDTLPLEDF GKYLKELGCD VLIHEATFDD SAKDAAKENM HSTIGDAVNI AKLANVKALI LTHISARYDK EEYFNLYKMN VKQYNESFKI IISEDLKSYD IKKDLLG // ID RPOB2_METJA Reviewed; 498 AA. AC Q58444; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=DNA-directed RNA polymerase subunit B''; DE EC=2.7.7.6; GN Name=rpoB2; OrderedLocusNames=MJ1040; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. The B (B''+B' and beta) subunits have been implicated CC in DNA promoter recognition and also in nucleotide binding. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99043.1; -; Genomic_DNA. DR PIR; G64429; G64429. DR ProteinModelPortal; Q58444; -. DR STRING; 243232.MJ_1040; -. DR EnsemblBacteria; AAB99043; AAB99043; MJ_1040. DR KEGG; mja:MJ_1040; -. DR eggNOG; arCOG01762; Archaea. DR eggNOG; COG0085; LUCA. DR InParanoid; Q58444; -. DR KO; K03045; -. DR OMA; GKICPSE; -. DR PhylomeDB; Q58444; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 3.90.1110.10; -; 1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007644; RNA_pol_bsu_protrusion. DR InterPro; IPR007642; RNA_pol_Rpb2_2. DR InterPro; IPR007645; RNA_pol_Rpb2_3. DR PANTHER; PTHR20856; PTHR20856; 1. DR Pfam; PF04563; RNA_pol_Rpb2_1; 1. DR Pfam; PF04561; RNA_pol_Rpb2_2; 1. DR Pfam; PF04565; RNA_pol_Rpb2_3; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase; Zinc. FT CHAIN 1 498 DNA-directed RNA polymerase subunit B''. FT /FTId=PRO_0000074034. SQ SEQUENCE 498 AA; 56487 MW; F57FD38EEEB79298 CRC64; MAIMRELVDA YFKEHGLIDH QIESYNDFVE NRLQKIIDEV GYIETEITGG YKVKLGKIKV GKPVIKEADG SIRPITPMEA RIRDLTYSVP LYLEMTPIIG EGEDAREGET VEVYIGELPV MLGSKICHLY GKSREELIDL GEDPEDPFGY FIINGTEKVL ITQEDLIPNR ILCEKAERSG KIVDVAKVFS TRHGFRALCT VERHPDGLLY ATFPGMPGQI PLVILMKALG AETDKDIIES IDDERFFMEI VLNIQEIREE HNINSPEDAL EFIGKRVAPG QAKDYRLKRA ETVLCNYLLP HLGVTKEDFP KKIRFLGIMA RNALELYFGY RGEDDKDHYA YKRAKLAGDL MEDLFRYAFS QLVKDIKYQL ERQTLRNKTP SIQAAVRSDI LTERIKHAMA TGTWVGGKTG VSQLLDRTSY LATNSQLRRI VSPLSRSQPH FEARELHGTH WGKICPSETP EGPNCGLVKN FAIMCKVTRE EDDSKVIELL KSFGINVS // ID RNP2_METJA Reviewed; 134 AA. AC Q57917; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 82. DE RecName: Full=Ribonuclease P protein component 2 {ECO:0000255|HAMAP-Rule:MF_00755}; DE Short=RNase P component 2 {ECO:0000255|HAMAP-Rule:MF_00755}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00755}; DE AltName: Full=Pop5 {ECO:0000255|HAMAP-Rule:MF_00755}; GN Name=rnp2 {ECO:0000255|HAMAP-Rule:MF_00755}; OrderedLocusNames=MJ0494; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18558617; DOI=10.1093/nar/gkn360; RA Pulukkunat D.K., Gopalan V.; RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into RT the roles of RNA and protein cofactors in RNase P catalysis."; RL Nucleic Acids Res. 36:4172-4180(2008). RN [3] RP FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012; RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.; RT "Cooperative RNP assembly: complementary rescue of structural defects RT by protein and RNA subunits of archaeal RNase P."; RL J. Mol. Biol. 411:368-383(2011). RN [4] RP FUNCTION, INTERACTION WITH RNP3, AND SUBUNIT. RX PubMed=22298511; DOI=10.1093/nar/gks013; RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., RA Gopalan V.; RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional RT dependence of archaeal and eukaryal RNase P on multiple protein RT cofactors."; RL Nucleic Acids Res. 40:4666-4680(2012). CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates CC mature tRNA molecules by cleaving their 5'-ends. CC {ECO:0000255|HAMAP-Rule:MF_00755, ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00755}. CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 CC protein subunits. Forms a subcomplex with Rnp3 which stimulates CC the catalytic RNA. {ECO:0000255|HAMAP-Rule:MF_00755, CC ECO:0000269|PubMed:18558617, ECO:0000269|PubMed:21683084, CC ECO:0000269|PubMed:22298511}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00755}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 2 family. {ECO:0000255|HAMAP-Rule:MF_00755}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98484.1; -; Genomic_DNA. DR PIR; F64361; F64361. DR ProteinModelPortal; Q57917; -. DR STRING; 243232.MJ_0494; -. DR EnsemblBacteria; AAB98484; AAB98484; MJ_0494. DR KEGG; mja:MJ_0494; -. DR eggNOG; arCOG01365; Archaea. DR eggNOG; COG1369; LUCA. DR InParanoid; Q57917; -. DR KO; K03537; -. DR OMA; NPWLIDY; -. DR PhylomeDB; Q57917; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-HAMAP. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009249; P:protein lipoylation; IBA:GO_Central. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00755; RNase_P_2; 1. DR InterPro; IPR002759; RNase_P/MRP_subunit. DR InterPro; IPR016434; RNase_P_comp-2. DR Pfam; PF01900; RNase_P_Rpp14; 1. DR PIRSF; PIRSF004952; RNase_P_2; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; tRNA processing. FT CHAIN 1 134 Ribonuclease P protein component 2. FT /FTId=PRO_0000140020. SQ SEQUENCE 134 AA; 15941 MW; 5BD64AB14CF0D9B7 CRC64; MIEMLKTLPP TLREKKRYIA FKILYDEELK EGEVVNLIRK AVLEYYGSWG TSKANPWLVY YDFPYGILRC QRDNVDYVKA SLILIREFKE KPVNIICLGV SGTIRKAKIK FLGIKKPKRW FVIRRERLKA KKQK // ID RNP3_METJA Reviewed; 232 AA. AC Q58539; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Ribonuclease P protein component 3 {ECO:0000255|HAMAP-Rule:MF_00756}; DE Short=RNase P component 3 {ECO:0000255|HAMAP-Rule:MF_00756}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00756}; DE AltName: Full=Rpp30 {ECO:0000255|HAMAP-Rule:MF_00756}; GN Name=rnp3 {ECO:0000255|HAMAP-Rule:MF_00756}; OrderedLocusNames=MJ1139; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, INTERACTION WITH RNP2, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18558617; DOI=10.1093/nar/gkn360; RA Pulukkunat D.K., Gopalan V.; RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into RT the roles of RNA and protein cofactors in RNase P catalysis."; RL Nucleic Acids Res. 36:4172-4180(2008). RN [3] RP FUNCTION, INTERACTION WITH RNP2, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012; RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.; RT "Cooperative RNP assembly: complementary rescue of structural defects RT by protein and RNA subunits of archaeal RNase P."; RL J. Mol. Biol. 411:368-383(2011). RN [4] RP FUNCTION, INTERACTION WITH RNP2, AND SUBUNIT. RX PubMed=22298511; DOI=10.1093/nar/gks013; RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., RA Gopalan V.; RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional RT dependence of archaeal and eukaryal RNase P on multiple protein RT cofactors."; RL Nucleic Acids Res. 40:4666-4680(2012). CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates CC mature tRNA molecules by cleaving their 5'-ends. CC {ECO:0000255|HAMAP-Rule:MF_00756, ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00756}. CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4-5 CC protein subunits. Forms a subcomplex with Rnp2 which stimulates CC the catalytic RNA. {ECO:0000255|HAMAP-Rule:MF_00756, CC ECO:0000269|PubMed:18558617, ECO:0000269|PubMed:21683084, CC ECO:0000269|PubMed:22298511}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00756}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 3 family. {ECO:0000255|HAMAP-Rule:MF_00756}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99146.1; -; Genomic_DNA. DR PIR; B64442; B64442. DR ProteinModelPortal; Q58539; -. DR STRING; 243232.MJ_1139; -. DR EnsemblBacteria; AAB99146; AAB99146; MJ_1139. DR KEGG; mja:MJ_1139; -. DR eggNOG; arCOG00307; Archaea. DR eggNOG; COG1603; LUCA. DR InParanoid; Q58539; -. DR KO; K03539; -. DR OMA; INHIFDE; -. DR PhylomeDB; Q58539; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030677; C:ribonuclease P complex; IEA:UniProtKB-HAMAP. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00756; RNase_P_3; 1. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR InterPro; IPR023539; RNase_P_comp-3_arc. DR InterPro; IPR002738; RNase_P_p30. DR Pfam; PF01876; RNase_P_p30; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; tRNA processing. FT CHAIN 1 232 Ribonuclease P protein component 3. FT /FTId=PRO_0000140039. SQ SEQUENCE 232 AA; 27346 MW; 5490A2447A7E897B CRC64; MRIDINRIEK EEDIKLLKEL KWNGFVFYQY DDEFSKDRYE EVKAIAESYK LKVYSGVKIK TESSKQLRDK VKKFRNKCHI ILIEGGVLKI NRAAVELHDV DILSTPELGR KDSGIDHVLA RLASNHRVAI ELNFKTLLNK DGYERARTLL FFRNNLKLAK KFDVPVVIST DAENKYQIKN PYDLRAFLNT LVEPLYAKKI METAYKICDF RDYLMRDNVV RYGVEIIKEE KE // ID RPIA_METJA Reviewed; 226 AA. AC Q58998; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Ribose-5-phosphate isomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE EC=5.3.1.6 {ECO:0000255|HAMAP-Rule:MF_00170}; DE AltName: Full=Phosphoriboisomerase A {ECO:0000255|HAMAP-Rule:MF_00170}; DE Short=PRI {ECO:0000255|HAMAP-Rule:MF_00170}; GN Name=rpiA {ECO:0000255|HAMAP-Rule:MF_00170}; OrderedLocusNames=MJ1603; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PATHWAY. RX PubMed=16237021; DOI=10.1128/JB.187.21.7382-7389.2005; RA Grochowski L.L., Xu H., White R.H.; RT "Ribose-5-phosphate biosynthesis in Methanocaldococcus jannaschii RT occurs in the absence of a pentose-phosphate pathway."; RL J. Bacteriol. 187:7382-7389(2005). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) IN COMPLEX WITH SUBSTRATE RP ANALOGS, ACTIVE SITE, AND SUBUNIT. RX PubMed=20054114; DOI=10.1107/S1744309109044923; RA Strange R.W., Antonyuk S.V., Ellis M.J., Bessho Y., Kuramitsu S., RA Yokoyama S., Hasnain S.S.; RT "The structure of an archaeal ribose-5-phosphate isomerase from RT Methanocaldococcus jannaschii (MJ1603)."; RL Acta Crystallogr. F 65:1214-1217(2009). CC -!- FUNCTION: Catalyzes the reversible conversion of ribose-5- CC phosphate to ribulose 5-phosphate. {ECO:0000255|HAMAP- CC Rule:MF_00170}. CC -!- CATALYTIC ACTIVITY: D-ribose 5-phosphate = D-ribulose 5-phosphate. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC -!- PATHWAY: Carbohydrate biosynthesis; D-ribose 5-phosphate CC biosynthesis. {ECO:0000269|PubMed:16237021}. CC -!- SUBUNIT: Homotetramer. {ECO:0000269|PubMed:20054114}. CC -!- SIMILARITY: Belongs to the ribose 5-phosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00170}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99623.1; -; Genomic_DNA. DR PIR; B64500; B64500. DR PDB; 3IXQ; X-ray; 1.78 A; A/B/C/D=1-226. DR PDBsum; 3IXQ; -. DR ProteinModelPortal; Q58998; -. DR SMR; Q58998; 2-226. DR STRING; 243232.MJ_1603; -. DR EnsemblBacteria; AAB99623; AAB99623; MJ_1603. DR KEGG; mja:MJ_1603; -. DR eggNOG; arCOG01122; Archaea. DR eggNOG; COG0120; LUCA. DR InParanoid; Q58998; -. DR KO; K01807; -. DR OMA; TINNPYA; -. DR PhylomeDB; Q58998; -. DR BRENDA; 5.3.1.6; 3260. DR UniPathway; UPA00293; -. DR EvolutionaryTrace; Q58998; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004751; F:ribose-5-phosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IDA:UniProtKB. DR HAMAP; MF_00170; Rib_5P_isom_A; 1. DR InterPro; IPR004788; Ribose5P_isomerase_typA. DR InterPro; IPR020672; Ribose5P_isomerase_typA_subgr. DR PANTHER; PTHR11934; PTHR11934; 1. DR Pfam; PF06026; Rib_5-P_isom_A; 1. DR TIGRFAMs; TIGR00021; rpiA; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; Isomerase; KW Reference proteome. FT CHAIN 1 226 Ribose-5-phosphate isomerase A. FT /FTId=PRO_0000158510. FT REGION 28 31 Substrate binding. FT REGION 83 86 Substrate binding. {ECO:0000305}. FT REGION 97 100 Substrate binding. {ECO:0000305}. FT ACT_SITE 106 106 Proton acceptor. FT {ECO:0000305|PubMed:20054114}. FT BINDING 124 124 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00170}. FT HELIX 4 14 {ECO:0000244|PDB:3IXQ}. FT HELIX 15 17 {ECO:0000244|PDB:3IXQ}. FT STRAND 23 26 {ECO:0000244|PDB:3IXQ}. FT HELIX 30 46 {ECO:0000244|PDB:3IXQ}. FT STRAND 51 56 {ECO:0000244|PDB:3IXQ}. FT HELIX 57 65 {ECO:0000244|PDB:3IXQ}. FT TURN 73 75 {ECO:0000244|PDB:3IXQ}. FT STRAND 79 83 {ECO:0000244|PDB:3IXQ}. FT STRAND 86 89 {ECO:0000244|PDB:3IXQ}. FT TURN 90 92 {ECO:0000244|PDB:3IXQ}. FT HELIX 103 112 {ECO:0000244|PDB:3IXQ}. FT STRAND 113 121 {ECO:0000244|PDB:3IXQ}. FT HELIX 122 124 {ECO:0000244|PDB:3IXQ}. FT STRAND 125 128 {ECO:0000244|PDB:3IXQ}. FT STRAND 131 133 {ECO:0000244|PDB:3IXQ}. FT STRAND 135 139 {ECO:0000244|PDB:3IXQ}. FT HELIX 141 143 {ECO:0000244|PDB:3IXQ}. FT HELIX 144 153 {ECO:0000244|PDB:3IXQ}. FT STRAND 157 160 {ECO:0000244|PDB:3IXQ}. FT STRAND 164 169 {ECO:0000244|PDB:3IXQ}. FT STRAND 177 182 {ECO:0000244|PDB:3IXQ}. FT HELIX 188 196 {ECO:0000244|PDB:3IXQ}. FT STRAND 201 207 {ECO:0000244|PDB:3IXQ}. FT STRAND 211 217 {ECO:0000244|PDB:3IXQ}. FT STRAND 220 224 {ECO:0000244|PDB:3IXQ}. SQ SEQUENCE 226 AA; 24830 MW; C0F1C2C1A5499123 CRC64; MSNEDLKLKV AKEAVKLVKD GMVIGLGTGS TAALFIRELG NRIREEELTV FGIPTSFEAK MLAMQYEIPL VTLDEYDVDI AFDGADEVEE TTLFLIKGGG GCHTQEKIVD YNANEFVVLV DESKLVKKLG EKFPIPVEVI PSAYRVVIRA LSEMGGEAVI RLGDRKRGPV ITDNGNMIID VFMNIDDAIE LEKEINNIPG VVENGIFTKV DKVLVGTKKG VKTLKK // ID RPOK_METJA Reviewed; 57 AA. AC Q57650; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=DNA-directed RNA polymerase subunit K; DE EC=2.7.7.6; GN Name=rpoK; OrderedLocusNames=MJ0197; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SIMILARITY: Belongs to the archaeal RpoK/eukaryotic RPB6 RNA CC polymerase subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98177.1; -; Genomic_DNA. DR PIR; F64324; F64324. DR ProteinModelPortal; Q57650; -. DR STRING; 243232.MJ_0197; -. DR EnsemblBacteria; AAB98177; AAB98177; MJ_0197. DR KEGG; mja:MJ_0197; -. DR eggNOG; arCOG01268; Archaea. DR eggNOG; COG1758; LUCA. DR InParanoid; Q57650; -. DR KO; K03055; -. DR OMA; LTKFEIA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.940.10; -; 1. DR HAMAP; MF_00192; RNApol_arch_K; 1. DR InterPro; IPR020708; DNA-dir_RNA_polK_14-18kDa_CS. DR InterPro; IPR006110; Pol_omega/K/RPB6. DR InterPro; IPR012293; RNAP_RPB6_omega. DR InterPro; IPR006111; RpoK/Rpb6. DR PANTHER; PTHR10773; PTHR10773; 1. DR Pfam; PF01192; RNA_pol_Rpb6; 1. DR PIRSF; PIRSF000778; RpoK/RPB6; 1. DR SMART; SM01409; RNA_pol_Rpb6; 1. DR SUPFAM; SSF63562; SSF63562; 1. DR PROSITE; PS01111; RNA_POL_K_14KD; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 57 DNA-directed RNA polymerase subunit K. FT /FTId=PRO_0000133813. SQ SEQUENCE 57 AA; 6292 MW; 46F97B2F02416C77 CRC64; MKLTKFEIAR ILGARSLQIS SGAYATIETK CDSSLKIAYE EIKQGKVPLK PIRPVKA // ID RNJ_METJA Reviewed; 448 AA. AC Q58271; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Ribonuclease J {ECO:0000255|HAMAP-Rule:MF_01492}; DE Short=RNase J {ECO:0000255|HAMAP-Rule:MF_01492}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_01492}; GN Name=rnj {ECO:0000255|HAMAP-Rule:MF_01492}; OrderedLocusNames=MJ0861; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: An RNase that has 5'-3' exonuclease activity. May be CC involved in RNA degradation. {ECO:0000255|HAMAP-Rule:MF_01492}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01492}; CC Note=Binds 2 Zn(2+) ions per subunit. It is not clear if Zn(2+) or CC Mg(2+) is physiologically important. {ECO:0000255|HAMAP- CC Rule:MF_01492}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01492}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01492}. CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC RNA-metabolizing metallo-beta-lactamase-like family. Archaeal CC RNase J subfamily. {ECO:0000255|HAMAP-Rule:MF_01492}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98866.1; -; Genomic_DNA. DR PIR; E64407; E64407. DR ProteinModelPortal; Q58271; -. DR STRING; 243232.MJ_0861; -. DR EnsemblBacteria; AAB98866; AAB98866; MJ_0861. DR KEGG; mja:MJ_0861; -. DR eggNOG; arCOG00546; Archaea. DR eggNOG; COG0595; LUCA. DR InParanoid; Q58271; -. DR KO; K12574; -. DR OMA; RVQIHED; -. DR PhylomeDB; Q58271; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004534; F:5'-3' exoribonuclease activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006401; P:RNA catabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01492; RNase_J_arch; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR InterPro; IPR004613; RNase_J. DR InterPro; IPR030879; RNase_J_arc. DR InterPro; IPR001587; RNase_J_CS. DR PANTHER; PTHR11203:SF22; PTHR11203:SF22; 1. DR Pfam; PF00753; Lactamase_B; 1. DR Pfam; PF07521; RMMBL; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR00649; MG423; 1. DR PROSITE; PS01292; UPF0036; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Exonuclease; Hydrolase; Metal-binding; KW Nuclease; Reference proteome; RNA-binding; Zinc. FT CHAIN 1 448 Ribonuclease J. FT /FTId=PRO_0000215275. FT REGION 383 387 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 81 81 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 83 83 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 85 85 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 86 86 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 151 151 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 173 173 Zinc 1; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 173 173 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. FT METAL 409 409 Zinc 2; catalytic. {ECO:0000255|HAMAP- FT Rule:MF_01492}. SQ SEQUENCE 448 AA; 50062 MW; FEF70CFCEF78770D CRC64; MKLEIIAIGG YEEVGRNMTA VNVDGEIIIL DMGIRLDRVL IHEDTDISKL HSLELIEKGI IPNDTVMKNI EGEVKAIVLS HGHLDHIGAV PKLAHRYNAP IIGTPYTIEL VKREILSEKK FDVRNPLIVL NAGESIDLTP NITLEFIRIT HSIPDSVLPV LHTPYGSIVY GNDFKFDNFP VVGERPDYRA IKKVGKNGVL CFISETTRIN HEGKTPPEII ASGLLKNDLL AADNDKHGII VTTFSSHIAR IKSITDIAEK MGRTPVLLGR SMMRFCGIAQ DIGLVKFPED LRIYGDPSSI EMALKNIVKE GKEKYLIIAT GHQGEEGAVL SRMATNKTPY KFEKYDCVVF SADPIPNPMN AAQRYMLESR LKLLGVRIFK GAHVSGHAAK EDHRDMLRWL NPEHIIPSHG DFNLTAEYTK LAEEEGYRLG EDVHLLRNGQ CLSFERII // ID RNP1_METJA Reviewed; 95 AA. AC Q57903; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=Ribonuclease P protein component 1 {ECO:0000255|HAMAP-Rule:MF_00754}; DE Short=RNase P component 1 {ECO:0000255|HAMAP-Rule:MF_00754}; DE EC=3.1.26.5 {ECO:0000255|HAMAP-Rule:MF_00754}; DE AltName: Full=Rpp29 {ECO:0000255|HAMAP-Rule:MF_00754}; GN Name=rnp1 {ECO:0000255|HAMAP-Rule:MF_00754}; OrderedLocusNames=MJ0464; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, INTERACTION WITH RNP4, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=18558617; DOI=10.1093/nar/gkn360; RA Pulukkunat D.K., Gopalan V.; RT "Studies on Methanocaldococcus jannaschii RNase P reveal insights into RT the roles of RNA and protein cofactors in RNase P catalysis."; RL Nucleic Acids Res. 36:4172-4180(2008). RN [3] RP FUNCTION, INTERACTION WITH RNP4, AND SUBUNIT. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21683084; DOI=10.1016/j.jmb.2011.05.012; RA Chen W.Y., Xu Y., Cho I.M., Oruganti S.V., Foster M.P., Gopalan V.; RT "Cooperative RNP assembly: complementary rescue of structural defects RT by protein and RNA subunits of archaeal RNase P."; RL J. Mol. Biol. 411:368-383(2011). RN [4] RP FUNCTION, INTERACTION WITH RNP4, AND SUBUNIT. RX PubMed=22298511; DOI=10.1093/nar/gks013; RA Chen W.Y., Singh D., Lai L.B., Stiffler M.A., Lai H.D., Foster M.P., RA Gopalan V.; RT "Fidelity of tRNA 5'-maturation: a possible basis for the functional RT dependence of archaeal and eukaryal RNase P on multiple protein RT cofactors."; RL Nucleic Acids Res. 40:4666-4680(2012). CC -!- FUNCTION: Part of ribonuclease P, a protein complex that generates CC mature tRNA molecules by cleaving their 5'-ends. CC {ECO:0000255|HAMAP-Rule:MF_00754, ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of RNA, removing 5'- CC extranucleotides from tRNA precursor. {ECO:0000255|HAMAP- CC Rule:MF_00754}. CC -!- SUBUNIT: Consists of a catalytic RNA component and at least 4 CC protein subunits. Forms a subcomplex with Rnp4 which stimulates CC the catalytic RNA. {ECO:0000269|PubMed:18558617, CC ECO:0000269|PubMed:21683084, ECO:0000269|PubMed:22298511}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00754}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal RNase P protein CC component 1 family. {ECO:0000255|HAMAP-Rule:MF_00754}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98453.1; -; Genomic_DNA. DR PIR; H64357; H64357. DR ProteinModelPortal; Q57903; -. DR STRING; 243232.MJ_0464; -. DR EnsemblBacteria; AAB98453; AAB98453; MJ_0464. DR KEGG; mja:MJ_0464; -. DR eggNOG; arCOG00784; Archaea. DR eggNOG; COG1588; LUCA. DR InParanoid; Q57903; -. DR KO; K03538; -. DR OMA; WHELIGL; -. DR PhylomeDB; Q57903; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0000172; C:ribonuclease MRP complex; IBA:GO_Central. DR GO; GO:0030677; C:ribonuclease P complex; IBA:GO_Central. DR GO; GO:0004526; F:ribonuclease P activity; IEA:UniProtKB-HAMAP. DR GO; GO:0033204; F:ribonuclease P RNA binding; IBA:GO_Central. DR GO; GO:0006379; P:mRNA cleavage; IEA:InterPro. DR GO; GO:0090502; P:RNA phosphodiester bond hydrolysis, endonucleolytic; IBA:GOC. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR GO; GO:0001682; P:tRNA 5'-leader removal; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.30.210; -; 1. DR HAMAP; MF_00754; RNase_P_1; 1. DR InterPro; IPR002730; RNase_P/MRP_p29. DR InterPro; IPR023538; RNP1. DR InterPro; IPR023534; Rof/RNase_P-like. DR Pfam; PF01868; UPF0086; 1. DR SMART; SM00538; POP4; 1. DR SUPFAM; SSF101744; SSF101744; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; tRNA processing. FT CHAIN 1 95 Ribonuclease P protein component 1. FT /FTId=PRO_0000128429. SQ SEQUENCE 95 AA; 10888 MW; 8D8DD531C165D09E CRC64; MITPHNILRH ELIGLKVEIV EAKNKAMIGI KGKVVDETRN TLVIEKEDGR EVVIPKDIAV FLFQLKGCKV KVDGRLLIGR PEERLKKKIK ILYPY // ID RPE_METJA Reviewed; 234 AA. AC Q58093; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Ribulose-phosphate 3-epimerase; DE EC=5.1.3.1; DE AltName: Full=Pentose-5-phosphate 3-epimerase; DE Short=PPE; DE AltName: Full=R5P3E; GN Name=rpe; OrderedLocusNames=MJ0680; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible epimerization of D-ribulose 5- CC phosphate to D-xylulose 5-phosphate. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: D-ribulose 5-phosphate = D-xylulose 5- CC phosphate. CC -!- COFACTOR: CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Name=Fe(2+); Xref=ChEBI:CHEBI:29033; Evidence={ECO:0000250}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 divalent metal cation per subunit. Active with CC Co(2+), Fe(2+), Mn(2+) and Zn(2+). {ECO:0000250}; CC -!- SIMILARITY: Belongs to the ribulose-phosphate 3-epimerase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98675.1; -; Genomic_DNA. DR PIR; H64384; H64384. DR ProteinModelPortal; Q58093; -. DR STRING; 243232.MJ_0680; -. DR EnsemblBacteria; AAB98675; AAB98675; MJ_0680. DR KEGG; mja:MJ_0680; -. DR eggNOG; arCOG05046; Archaea. DR eggNOG; COG0036; LUCA. DR InParanoid; Q58093; -. DR KO; K01783; -. DR OMA; GANYITF; -. DR PhylomeDB; Q58093; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IBA:GO_Central. DR GO; GO:0004750; F:ribulose-phosphate 3-epimerase activity; IBA:GO_Central. DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0019323; P:pentose catabolic process; IBA:GO_Central. DR GO; GO:0009052; P:pentose-phosphate shunt, non-oxidative branch; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR026019; Ribul_P_3_epim. DR InterPro; IPR000056; Ribul_P_3_epim-like. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR11749; PTHR11749; 1. DR Pfam; PF00834; Ribul_P_3_epim; 1. DR PIRSF; PIRSF001461; RPE; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR01163; rpe; 1. DR PROSITE; PS01085; RIBUL_P_3_EPIMER_1; 1. DR PROSITE; PS01086; RIBUL_P_3_EPIMER_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cobalt; Complete proteome; Iron; Isomerase; KW Manganese; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 234 Ribulose-phosphate 3-epimerase. FT /FTId=PRO_0000171584. FT REGION 139 142 Substrate binding. {ECO:0000250}. FT REGION 194 195 Substrate binding. {ECO:0000250}. FT ACT_SITE 34 34 Proton acceptor. {ECO:0000250}. FT ACT_SITE 172 172 Proton donor. {ECO:0000250}. FT METAL 32 32 Divalent metal cation. {ECO:0000250}. FT METAL 34 34 Divalent metal cation. {ECO:0000250}. FT METAL 65 65 Divalent metal cation. {ECO:0000250}. FT METAL 172 172 Divalent metal cation. {ECO:0000250}. FT BINDING 7 7 Substrate. {ECO:0000250}. FT BINDING 65 65 Substrate. {ECO:0000250}. FT BINDING 174 174 Substrate; via amide nitrogen. FT {ECO:0000250}. SQ SEQUENCE 234 AA; 25838 MW; 070E2CF7A2BC9D7F CRC64; MIKIGASILS ADFGHLREEI KKAEEAGVDF FHVDMMDGHF VPNISMGIGI AKHVKKLTEL PVEVHLMVEN VDLFVNEFEE MDYITFHIEA VKFPFRIINR IKSIGAKPIV ALNPATPLDA IEYILGDVYA VLVMTVEPGF SGQKFIPVMT KKIRKLKSMI VENGYDTKIF VDGGINVETA PLAVKAGADV LVAASAIFGK DDVKTAVKNL REAALEALNK DFLTKSFNSN EEKQ // ID RPOB1_METJA Reviewed; 636 AA. AC Q60181; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=DNA-directed RNA polymerase subunit B'; DE EC=2.7.7.6; GN Name=rpoB1; OrderedLocusNames=MJ1041; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. The B (B''+B' and beta) subunits have been implicated CC in DNA promoter recognition and also in nucleotide binding. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC -!- SIMILARITY: Belongs to the RNA polymerase beta chain family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99044.1; -; Genomic_DNA. DR PIR; H64429; H64429. DR ProteinModelPortal; Q60181; -. DR STRING; 243232.MJ_1041; -. DR EnsemblBacteria; AAB99044; AAB99044; MJ_1041. DR KEGG; mja:MJ_1041; -. DR eggNOG; arCOG01762; Archaea. DR eggNOG; COG0085; LUCA. DR InParanoid; Q60181; -. DR KO; K03044; -. DR OMA; QKLYHMV; -. DR PhylomeDB; Q60181; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0032549; F:ribonucleoside binding; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.40.270.10; -; 2. DR Gene3D; 2.40.50.150; -; 1. DR InterPro; IPR015712; DNA-dir_RNA_pol_su2. DR InterPro; IPR007120; DNA-dir_RNA_pol_su2_6. DR InterPro; IPR007121; RNA_pol_bsu_CS. DR InterPro; IPR007646; RNA_pol_Rpb2_4. DR InterPro; IPR007647; RNA_pol_Rpb2_5. DR InterPro; IPR007641; RNA_pol_Rpb2_7. DR InterPro; IPR014724; RNA_pol_RPB2_OB-fold. DR InterPro; IPR019969; RNAP_B. DR PANTHER; PTHR20856; PTHR20856; 1. DR Pfam; PF04566; RNA_pol_Rpb2_4; 1. DR Pfam; PF04567; RNA_pol_Rpb2_5; 1. DR Pfam; PF00562; RNA_pol_Rpb2_6; 1. DR Pfam; PF04560; RNA_pol_Rpb2_7; 1. DR TIGRFAMs; TIGR03670; rpoB_arch; 1. DR PROSITE; PS01166; RNA_POL_BETA; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-directed RNA polymerase; Metal-binding; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 636 DNA-directed RNA polymerase subunit B'. FT /FTId=PRO_0000048102. FT ZN_FING 551 572 {ECO:0000255}. SQ SEQUENCE 636 AA; 72193 MW; 81DE30267A572914 CRC64; MKNLASREVN IYVNGKLVGT TDKPEELVNF IREKRRKGEL PQYTTVAYNE ESNDIHINTD AGRIVRPLIV VENGKPKLTK EHIEKLKKGE ITFSDLVKEG VIEYLDAEEE ENAYIALSEE ELTEKHTHLE IDPLTILGIG AGVAPYPEHN SAPRITMAAA MGKQSLGIPM SNIKWRLDTR GHYLHYPQVP IVRTKHQEIL GFDKRPAGQN FVVAIMSYEG YNMEDAIVFN KSAIDRGLGR STFFRTYDAC ERRYPGGQMD RFEIPDKGVR GYRSEECYRY LEEDGIVAVE SHVKGGDVIV GKTSPPRFLE EHEITIQVKP QRRDSSVVVR HGEEGYIDKV ILTETKEGNR LVKVKVRDLR IPELGDKFAS RHGQKGVMGL TVPQEDLPFT ESGIVPDIII NPHAIPSRMT VGQLLEMLGG KVGALEGRRI DGTIFSGEKE WDLRKALEAL GFKHHGKEVM YDGKTGKKFE VEIYIGIAYY QKLHHLVAGK IHARSRGPVQ VLTRQPTEGR AREGGLRFGE MERDVLIGHG AAMLLKERLM DESDPYDICI CSKCGDFAIL DYKRGLKYCP ICGEIENLYS SKKIPFVRIP YAFKLLLDEL KSMCILPRIK VRDKVELEDF EEFVEKLEKE KVKQKQ // ID RPOL_METJA Reviewed; 99 AA. AC Q57832; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=DNA-directed RNA polymerase subunit L; DE EC=2.7.7.6; GN Name=rpoL; OrderedLocusNames=MJ0387; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- INTERACTION: CC Q57648:rpoD; NbExp=3; IntAct=EBI-2567038, EBI-2567023; CC -!- SIMILARITY: Belongs to the archaeal RpoL/eukaryotic RPB11/RPC19 CC RNA polymerase subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98373.1; -; Genomic_DNA. DR PIR; C64348; C64348. DR ProteinModelPortal; Q57832; -. DR IntAct; Q57832; 1. DR STRING; 243232.MJ_0387; -. DR PRIDE; Q57832; -. DR EnsemblBacteria; AAB98373; AAB98373; MJ_0387. DR KEGG; mja:MJ_0387; -. DR eggNOG; arCOG04111; Archaea. DR eggNOG; COG1761; LUCA. DR InParanoid; Q57832; -. DR KO; K03056; -. DR OMA; SYDMKHV; -. DR PhylomeDB; Q57832; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00261; RNApol_arch_L; 1. DR InterPro; IPR009025; RBP11-like_dimer. DR InterPro; IPR008193; RNA_pol_Rpb11_13-16kDa_CS. DR InterPro; IPR022905; RNAP_L. DR SUPFAM; SSF55257; SSF55257; 1. DR PROSITE; PS01154; RNA_POL_L_13KD; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 99 DNA-directed RNA polymerase subunit L. FT /FTId=PRO_0000149326. SQ SEQUENCE 99 AA; 11392 MW; 0C25307DDF5EE909 CRC64; MEIKILERKD NLVEIELINE DHSLPNLLKD ILLTKEGVKM ASYSIDHPLL HPETGRYISN PKITIITEEG TDPLEVLKEG LRDIIKMCDT LLDELKEKK // ID RPOP_METJA Reviewed; 46 AA. AC P59283; DT 12-FEB-2003, integrated into UniProtKB/Swiss-Prot. DT 12-FEB-2003, sequence version 1. DT 11-MAY-2016, entry version 59. DE RecName: Full=DNA-directed RNA polymerase subunit P; DE EC=2.7.7.6; GN Name=rpoP; OrderedLocusNames=MJ0593.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RX PubMed=11058130; DOI=10.1093/nar/28.21.4299; RA Werner F., Eloranta J.J., Weinzierl R.O.; RT "Archaeal RNA polymerase subunits F and P are bona fide homologs of RT eukaryotic RPB4 and RPB12."; RL Nucleic Acids Res. 28:4299-4305(2000). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SIMILARITY: Belongs to the archaeal RpoP/eukaryotic RPC10 RNA CC polymerase subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P59283; -. DR InParanoid; P59283; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.20.28.30; -; 1. DR HAMAP; MF_00615; RNApol_arch_P; 1. DR InterPro; IPR023464; RNAP_P. DR InterPro; IPR006591; RNAP_P/RPABC4. DR InterPro; IPR029040; RPABC4/Spt4. DR SMART; SM00659; RPOLCX; 1. DR SUPFAM; SSF63393; SSF63393; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-directed RNA polymerase; Metal-binding; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase; Zinc; Zinc-finger. FT CHAIN 1 46 DNA-directed RNA polymerase subunit P. FT /FTId=PRO_0000159758. FT ZN_FING 6 27 C4-type. {ECO:0000255}. SQ SEQUENCE 46 AA; 5452 MW; 6B66BC918364EFA0 CRC64; MVEYKCLNCK KIIKLEELGK RARCPHCSYK ILVKLRPKVV KHVKAR // ID RPA_METJA Reviewed; 645 AA. AC Q58559; DT 26-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Replication factor A; DE Short=RF-A; DE Short=RP-A; DE AltName: Full=Replication factor A protein 1; DE AltName: Full=Replication protein A; DE AltName: Full=Single-stranded DNA-binding protein; DE AltName: Full=mjaSSB; GN Name=rpa; OrderedLocusNames=MJ1159; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION, SUBUNIT, AND DNA-BINDING. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=9843941; DOI=10.1073/pnas.95.25.14634; RA Kelly T.J., Simancek P., Brush G.S.; RT "Identification and characterization of a single-stranded DNA-binding RT protein from the archaeon Methanococcus jannaschii."; RL Proc. Natl. Acad. Sci. U.S.A. 95:14634-14639(1998). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) OF 170-274. RG Northeast structural genomics consortium (NESG); RT "Crystal structure of a domain of a replication factor a protein, from RT Methanocaldococcus jannaschii. Northeast structural genomics target RT mjr118e."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Probably plays an essential for replication of the CC chromosome, DNA recombination and repair (By similarity). Binds CC approximately 20 nucleotides. {ECO:0000250}. CC -!- SUBUNIT: Monomer. Binds to single-stranded DNA sequences. CC {ECO:0000269|PubMed:9843941}. CC -!- SIMILARITY: Contains 4 OB DNA-binding domains. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99162.1; -; Genomic_DNA. DR PIR; F64444; F64444. DR PDB; 3DM3; X-ray; 2.40 A; A/B/C=170-274. DR PDBsum; 3DM3; -. DR ProteinModelPortal; Q58559; -. DR STRING; 243232.MJ_1159; -. DR EnsemblBacteria; AAB99162; AAB99162; MJ_1159. DR KEGG; mja:MJ_1159; -. DR eggNOG; arCOG01510; Archaea. DR eggNOG; COG1599; LUCA. DR InParanoid; Q58559; -. DR KO; K07466; -. DR OMA; NAFSRKW; -. DR PhylomeDB; Q58559; -. DR EvolutionaryTrace; Q58559; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 5. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR InterPro; IPR013955; Rep_factor-A_C. DR Pfam; PF08646; Rep_fac-A_C; 1. DR Pfam; PF01336; tRNA_anti-codon; 3. DR SUPFAM; SSF50249; SSF50249; 5. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA damage; DNA repair; KW DNA replication; DNA-binding; Metal-binding; Reference proteome; KW Repeat; Zinc; Zinc-finger. FT CHAIN 1 645 Replication factor A. FT /FTId=PRO_0000097430. FT DNA_BIND 78 158 OB 1. FT DNA_BIND 186 266 OB 2. FT DNA_BIND 291 378 OB 3. FT DNA_BIND 423 497 OB 4. FT ZN_FING 531 550 C4-type. {ECO:0000255}. FT HELIX 177 179 {ECO:0000244|PDB:3DM3}. FT STRAND 182 202 {ECO:0000244|PDB:3DM3}. FT STRAND 208 218 {ECO:0000244|PDB:3DM3}. FT STRAND 221 228 {ECO:0000244|PDB:3DM3}. FT HELIX 229 233 {ECO:0000244|PDB:3DM3}. FT STRAND 241 250 {ECO:0000244|PDB:3DM3}. FT STRAND 254 267 {ECO:0000244|PDB:3DM3}. SQ SEQUENCE 645 AA; 73842 MW; 3F0AD1B78065DD4F CRC64; MIGDYERFKQ LKKKVAEALN ISEEELDRMI DKKIEENGGI ILKDAALMMI AKEHGVYGEE KNDEEFLISD IEEGQIGVEI TGVITDISEI KTFKRRDGSL GKYKRITIAD KSGTIRMTLW DDLAELDVKV GDVIKIERAR ARKWRNNLEL SSTSETKIKK LENYEGELPE IKDTYNIGEL SPGMTATFEG EVISALPIKE FKRADGSIGK LKSFIVRDET GSIRVTLWDN LTDIDVGRGD YVRVRGYIRE GYYGGLECTA NYVEILKKGE KIESEEVNIE DLTKYEDGEL VSVKGRVIAI SNKKSVDLDG EIAKVQDIIL DNGTGRVRVS FWRGKTALLE NIKEGDLVRI TNCRVKTFYD REGNKRTDLV ATLETEVIKD ENIEAPEYEL KYCKIEDIYN RDVDWNDINL IAQVVEDYGV NEIEFEDKVR KVRNLLLEDG TGRIRLSLWD DLAEIEIKEG DIVEILHAYA KERGDYIDLV IGKYGRIIIN PEGVEIKTNR KFIADIEDGE TVEVRGAVVK ILSDTLFLYL CPNCRKRVVE IDGIYNCPIC GDVEPEEILR LNFVVDDGTG TLLCRAYDRR VEKMLKMNRE ELKNLTIEMV EDEILGEEFV LYGNVRVEND ELIMVVRRVN DVDVEKEIRI LEEME // ID RPOE1_METJA Reviewed; 187 AA. AC Q57840; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 105. DE RecName: Full=DNA-directed RNA polymerase subunit E'; DE EC=2.7.7.6; GN Name=rpoE1; OrderedLocusNames=MJ0397; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98387.1; -; Genomic_DNA. DR PIR; E64349; E64349. DR PDB; 1GO3; X-ray; 1.75 A; E/M=1-187. DR PDBsum; 1GO3; -. DR ProteinModelPortal; Q57840; -. DR SMR; Q57840; 1-181. DR IntAct; Q57840; 1. DR STRING; 243232.MJ_0397; -. DR EnsemblBacteria; AAB98387; AAB98387; MJ_0397. DR KEGG; mja:MJ_0397; -. DR eggNOG; arCOG00675; Archaea. DR eggNOG; COG1095; LUCA. DR InParanoid; Q57840; -. DR KO; K03049; -. DR OMA; YKRVRLK; -. DR PhylomeDB; Q57840; -. DR EvolutionaryTrace; Q57840; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.30.1490.120; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR005576; RNA_pol_Rpb7_N. DR InterPro; IPR004519; RNAP_E/RPC8. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF00575; S1; 1. DR Pfam; PF03876; SHS2_Rpb7-N; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF88798; SSF88798; 1. DR TIGRFAMs; TIGR00448; rpoE; 1. DR PROSITE; PS50126; S1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 187 DNA-directed RNA polymerase subunit E'. FT /FTId=PRO_0000074036. FT DOMAIN 82 166 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT STRAND 2 13 {ECO:0000244|PDB:1GO3}. FT HELIX 15 17 {ECO:0000244|PDB:1GO3}. FT HELIX 22 34 {ECO:0000244|PDB:1GO3}. FT TURN 40 42 {ECO:0000244|PDB:1GO3}. FT STRAND 43 54 {ECO:0000244|PDB:1GO3}. FT STRAND 65 77 {ECO:0000244|PDB:1GO3}. FT STRAND 84 93 {ECO:0000244|PDB:1GO3}. FT STRAND 96 100 {ECO:0000244|PDB:1GO3}. FT STRAND 102 109 {ECO:0000244|PDB:1GO3}. FT HELIX 110 112 {ECO:0000244|PDB:1GO3}. FT STRAND 118 120 {ECO:0000244|PDB:1GO3}. FT STRAND 127 129 {ECO:0000244|PDB:1GO3}. FT TURN 130 132 {ECO:0000244|PDB:1GO3}. FT STRAND 141 150 {ECO:0000244|PDB:1GO3}. FT STRAND 160 164 {ECO:0000244|PDB:1GO3}. FT HELIX 173 183 {ECO:0000244|PDB:1GO3}. SQ SEQUENCE 187 AA; 21216 MW; C0E4EA3C006D69DB CRC64; MYKILEIADV VKVPPEEFGK DLKETVKKIL MEKYEGRLDK DVGFVLSIVD VKDIGEGKVV HGDGSAYHPV VFETLVYIPE MYELIEGEVV DVVEFGSFVR LGPLDGLIHV SQIMDDYVSY DPKREAIIGK ETGKVLEIGD YVRARIVAIS LKAERKRGSK IALTMRQPYL GKLEWIEEEK AKKQNQE // ID RPOI_METJA Reviewed; 109 AA. AC Q58785; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=DNA-directed RNA polymerase subunit I; DE EC=2.7.7.6; GN Name=rpoI; OrderedLocusNames=MJ1390; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99398.1; -; Genomic_DNA. DR PIR; E64473; E64473. DR ProteinModelPortal; Q58785; -. DR STRING; 243232.MJ_1390; -. DR EnsemblBacteria; AAB99398; AAB99398; MJ_1390. DR KEGG; mja:MJ_1390; -. DR eggNOG; arCOG09634; Archaea. DR eggNOG; ENOG41110N8; LUCA. DR KO; K03054; -. DR OMA; IMVRRII; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 109 DNA-directed RNA polymerase subunit I. FT /FTId=PRO_0000074040. SQ SEQUENCE 109 AA; 12677 MW; E9A807C289430E4F CRC64; MKGMDEYEKI INDLNTINSK AKFIGIKIIM VRRIIDMHKD NDKLIKKVLE GIKNTDLYDL VLNACPELKG ERIKDVYFKK NDYFNVIKKT MSSENTVLKN VLINDESPP // ID RS10_METJA Reviewed; 101 AA. AC P54029; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 13-DEC-2001, sequence version 2. DT 11-MAY-2016, entry version 91. DE RecName: Full=30S ribosomal protein S10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN Name=rps10 {ECO:0000255|HAMAP-Rule:MF_00508}; GN OrderedLocusNames=MJ0322; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in the binding of tRNA to the ribosomes. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00508}. CC -!- SIMILARITY: Belongs to the ribosomal protein S10P family. CC {ECO:0000255|HAMAP-Rule:MF_00508}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98306.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98306.1; ALT_INIT; Genomic_DNA. DR PIR; C64340; C64340. DR ProteinModelPortal; P54029; -. DR STRING; 243232.MJ_0322; -. DR EnsemblBacteria; AAB98306; AAB98306; MJ_0322. DR KEGG; mja:MJ_0322; -. DR eggNOG; arCOG01758; Archaea. DR eggNOG; COG0051; LUCA. DR InParanoid; P54029; -. DR KO; K02946; -. DR OMA; YELKIHK; -. DR PhylomeDB; P54029; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.600; -; 1. DR HAMAP; MF_00508; Ribosomal_S10; 1. DR InterPro; IPR001848; Ribosomal_S10. DR InterPro; IPR018268; Ribosomal_S10_CS. DR InterPro; IPR027486; Ribosomal_S10_dom. DR InterPro; IPR005729; Ribosomal_S10_euk/arc. DR PANTHER; PTHR11700; PTHR11700; 1. DR Pfam; PF00338; Ribosomal_S10; 1. DR PRINTS; PR00971; RIBOSOMALS10. DR SMART; SM01403; Ribosomal_S10; 1. DR SUPFAM; SSF54999; SSF54999; 1. DR TIGRFAMs; TIGR01046; uS10_euk_arch; 1. DR PROSITE; PS00361; RIBOSOMAL_S10; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 101 30S ribosomal protein S10. FT /FTId=PRO_0000146646. SQ SEQUENCE 101 AA; 11673 MW; 7676C40BA48DAF07 CRC64; MQRARIKLSS TDHKVLDEIC RQIKEIAEKT GVDISGPIPL PTKVLRVVTR KSPDGEGSST FDRWTMKIHK RLIDIDADER ALRHIMKIRI PDNVQIEIQF K // ID RS17_METJA Reviewed; 117 AA. AC P54036; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=30S ribosomal protein S17P {ECO:0000255|HAMAP-Rule:MF_01345}; GN Name=rps17p {ECO:0000255|HAMAP-Rule:MF_01345}; GN OrderedLocusNames=MJ0465; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC specifically to the 5'-end of 16S ribosomal RNA. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01345}. CC -!- SIMILARITY: Belongs to the ribosomal protein S17P family. CC {ECO:0000255|HAMAP-Rule:MF_01345}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98454.1; -; Genomic_DNA. DR PIR; A64358; A64358. DR ProteinModelPortal; P54036; -. DR STRING; 243232.MJ_0465; -. DR EnsemblBacteria; AAB98454; AAB98454; MJ_0465. DR KEGG; mja:MJ_0465; -. DR eggNOG; arCOG04096; Archaea. DR eggNOG; COG0186; LUCA. DR InParanoid; P54036; -. DR KO; K02961; -. DR OMA; HGHLKVR; -. DR PhylomeDB; P54036; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01345_A; Ribosomal_S17_A; 1. DR HAMAP; MF_01345_B; Ribosomal_S17_B; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000266; Ribosomal_S17/S11. DR InterPro; IPR028333; Ribosomal_S17_arc-typ. DR InterPro; IPR019978; Ribosomal_S17_archaeal. DR InterPro; IPR019979; Ribosomal_S17_CS. DR PANTHER; PTHR10744; PTHR10744; 1. DR Pfam; PF00366; Ribosomal_S17; 1. DR PRINTS; PR00973; RIBOSOMALS17. DR ProDom; PD001295; Ribosomal_S17; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR03630; uS17_arch; 1. DR PROSITE; PS00056; RIBOSOMAL_S17; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 117 30S ribosomal protein S17P. FT /FTId=PRO_0000128499. SQ SEQUENCE 117 AA; 13266 MW; 476CFF0D79EF5D8C CRC64; MAARNIGIQV KAPEVECDDK NCPFHGNLPV RGQSFVGVVV SDKPHKTVII KREVVKYIKK YERYERRTTK LAAHNPPCIH ARVGDIVRVM ECRPISKTKA FVVVEKLGRI DEVKGEE // ID RPOA2_METJA Reviewed; 859 AA. AC Q58446; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=DNA-directed RNA polymerase subunit A''; DE EC=2.7.7.6; DE Contains: DE RecName: Full=Mja rpoA2 intein; DE AltName: Full=Mja rpol A'' intein; GN Name=rpoA2; OrderedLocusNames=MJ1043; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA polymerase beta' chain family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99047.1; -; Genomic_DNA. DR PIR; B64430; B64430. DR ProteinModelPortal; Q58446; -. DR SMR; Q58446; 695-847. DR STRING; 243232.MJ_1043; -. DR EnsemblBacteria; AAB99047; AAB99047; MJ_1043. DR KEGG; mja:MJ_1043; -. DR eggNOG; arCOG03145; Archaea. DR eggNOG; arCOG04256; Archaea. DR eggNOG; COG0086; LUCA. DR InParanoid; Q58446; -. DR KO; K03042; -. DR OMA; KVHWKRI; -. DR PhylomeDB; Q58446; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 3. DR HAMAP; MF_00411; RNApol_arch_A; 1. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR007081; RNA_pol_Rpb1_5. DR InterPro; IPR012757; RNAP_A2. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF04998; RNA_pol_Rpb1_5; 2. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR02389; RNA_pol_rpoA2; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; KW DNA-directed RNA polymerase; Endonuclease; Hydrolase; Intron homing; KW Nuclease; Nucleotidyltransferase; Protein splicing; KW Reference proteome; Transcription; Transferase; Zinc. FT CHAIN 1 75 DNA-directed RNA polymerase subunit A'', FT 1st part. {ECO:0000255}. FT /FTId=PRO_0000031065. FT CHAIN 76 546 Mja rpoA2 intein. {ECO:0000255}. FT /FTId=PRO_0000031066. FT CHAIN 547 859 DNA-directed RNA polymerase subunit A'', FT 2nd part. {ECO:0000255}. FT /FTId=PRO_0000031067. FT DOMAIN 248 380 DOD-type homing endonuclease. SQ SEQUENCE 859 AA; 97087 MW; A05799E007899015 CRC64; MDMEALKQKI EGLDIPQSLK DELFEKLSKE KDLTEEMVDE IIDEVVNAYR KALVEPYEAV GIVAAQSIGE PGTQMSLPYE EKIIIKEGEF IKPVEIGKLV DEMIERFGFE KIGNSEVCDL PIDIYALSLD QDEKVHWKRI ISCIRHKHNG KLIKIKTKSG REITATPYHS FVIRKDNKII PVKGSELKIG DRIPVVKHIP ANCVEAINIS DYVSGNYVVD NINNKIAPKI NGKSIPNNIK LDYDFGYFIG IYLAEGSVTK YFVSISNVDE LILNKIRAFA DKLGLNYGEY DNNNGFAESH DIRIYSSTLA EFLSNFGTSS NTKKIAEFVF GANKEFVRGL IRGYFDGDGN VNADRKVIRV TSNSKELIDG IAILLARFNI FSIKTKTKNQ FVLIIPHRYA KKFHEEINFS VEKKKSELER LVSSLNDDKT YDSIDMIPSI GDALTKLGEK VDYPKVILKK FERKQKIGRA TLQRHLRRIE ELAVKKGVNI LALKEYWLLK KAVESDVIWD EIVKIEEISC DKKYVYDISV EGLETFTTFD GVLTHNTMRT FHYAGVAEIN VTLGLPRMIE IVDARKEPST PIMTIYLKEE YKDNREKAEE IAKEIESLTL GSIAESISID LWTQSIKVEL DENRLADRGL TIDDVIEAIK KKLKVKIDVD GTTLYLKIKT PSIKALRKRI PKIKNIQLKG IPGIERVLVK KEGGEYVLYT QGSNLREVFK IDGVDTTRTI TNNIIEIQEV LGIEAARNAI INEMRNTLEQ QGLEVDIRHL MLVADIMTAD GEVKPIGRHG VAGEKGSVLA RAAFEETVKH LYAAAERGDV DKLKGVIENV IVGKPIYLGT GCVELTIDRE YEEGKNMEE // ID RPOD_METJA Reviewed; 191 AA. AC Q57648; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 106. DE RecName: Full=DNA-directed RNA polymerase subunit D; DE EC=2.7.7.6; GN Name=rpoD; OrderedLocusNames=MJ0192; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). CC -!- INTERACTION: CC Q57832:rpoL; NbExp=3; IntAct=EBI-2567023, EBI-2567038; CC -!- SIMILARITY: Belongs to the archaeal RpoD/eukaryotic RPB3 RNA CC polymerase subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98172.1; -; Genomic_DNA. DR PIR; A64324; A64324. DR ProteinModelPortal; Q57648; -. DR IntAct; Q57648; 3. DR STRING; 243232.MJ_0192; -. DR EnsemblBacteria; AAB98172; AAB98172; MJ_0192. DR KEGG; mja:MJ_0192; -. DR eggNOG; arCOG04241; Archaea. DR eggNOG; COG0202; LUCA. DR InParanoid; Q57648; -. DR KO; K03047; -. DR OMA; HAKWQPC; -. DR PhylomeDB; Q57648; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 2.170.120.12; -; 1. DR HAMAP; MF_00320; RNApol_arch_D; 1. DR InterPro; IPR001514; DNA-dir_RNA_pol_30-40kDasu_CS. DR InterPro; IPR011262; DNA-dir_RNA_pol_insert. DR InterPro; IPR011263; DNA-dir_RNA_pol_RpoA/D/Rpb3. DR InterPro; IPR009025; RBP11-like_dimer. DR InterPro; IPR022842; RNAP_D. DR Pfam; PF01000; RNA_pol_A_bac; 1. DR Pfam; PF01193; RNA_pol_L; 1. DR SMART; SM00662; RPOLD; 1. DR SUPFAM; SSF55257; SSF55257; 2. DR SUPFAM; SSF56553; SSF56553; 1. DR PROSITE; PS00446; RNA_POL_D_30KD; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 191 DNA-directed RNA polymerase subunit D. FT /FTId=PRO_0000132754. SQ SEQUENCE 191 AA; 21699 MW; 3F5B96CA0D242A96 CRC64; MITIKEKRKT RIGEEFIFSL KAPISFSNAI RRIMISEVPT FAIEDVYIYE NSSSMDDEIL AHRLGLIPIK GKPLLENEVI TFTLEKEGPC TVYSSDLKSE NGEVAFKNIP IVKLGKGQRI QIECEAIPGI GKVHAKWQPC NAVYKQIADD EVEFFVETFG QMEAEEILEE AVKILKNKAE SFLQQLEMIE Q // ID RS15_METJA Reviewed; 153 AA. AC P54012; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-MAY-2016, entry version 89. DE RecName: Full=30S ribosomal protein S15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN Name=rps15 {ECO:0000255|HAMAP-Rule:MF_01343}; GN OrderedLocusNames=MJ0036; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01343}. CC -!- SIMILARITY: Belongs to the ribosomal protein S15P family. CC {ECO:0000255|HAMAP-Rule:MF_01343}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98017.1; -; Genomic_DNA. DR ProteinModelPortal; P54012; -. DR STRING; 243232.MJ_0036; -. DR EnsemblBacteria; AAB98017; AAB98017; MJ_0036. DR KEGG; mja:MJ_0036; -. DR eggNOG; arCOG04185; Archaea. DR eggNOG; COG0184; LUCA. DR InParanoid; P54012; -. DR KO; K02956; -. DR OMA; WHLVKKA; -. DR PhylomeDB; P54012; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.287.10; -; 1. DR HAMAP; MF_01343_A; Ribosomal_S15_A; 1. DR InterPro; IPR012606; Ribosomal_S13/S15_N. DR InterPro; IPR000589; Ribosomal_S15. DR InterPro; IPR023029; Ribosomal_S15P. DR InterPro; IPR009068; S15_NS1_RNA-bd. DR Pfam; PF08069; Ribosomal_S13_N; 1. DR Pfam; PF00312; Ribosomal_S15; 1. DR SMART; SM01386; Ribosomal_S13_N; 1. DR SMART; SM01387; Ribosomal_S15; 1. DR SUPFAM; SSF47060; SSF47060; 1. DR PROSITE; PS00362; RIBOSOMAL_S15; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 153 30S ribosomal protein S15. FT /FTId=PRO_0000115606. SQ SEQUENCE 153 AA; 17845 MW; 7C1DAEA164CDEA39 CRC64; MARMHARKRG RSGSKRPVRK EVPEWVQYTP EQVEQLVVEL AKKGYQSAQI GLILRDTYGI PDVKLITGKK ISKIMKEHGL YPKVPEDLLN LMRRAVNLRK HLEQHPKDLH SKRGLQLIES KIRRLVKYYK SKGVLPADWR YTPETARLLV EQA // ID RS19E_METJA Reviewed; 148 AA. AC P54057; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=30S ribosomal protein S19e {ECO:0000255|HAMAP-Rule:MF_01474}; GN Name=rps19e {ECO:0000255|HAMAP-Rule:MF_01474}; GN OrderedLocusNames=MJ0692; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May be involved in maturation of the 30S ribosomal CC subunit. {ECO:0000255|HAMAP-Rule:MF_01474}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01474}. CC -!- SIMILARITY: Belongs to the ribosomal protein S19e family. CC {ECO:0000255|HAMAP-Rule:MF_01474}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98687.1; -; Genomic_DNA. DR PIR; D64386; D64386. DR ProteinModelPortal; P54057; -. DR SMR; P54057; 2-148. DR STRING; 243232.MJ_0692; -. DR EnsemblBacteria; AAB98687; AAB98687; MJ_0692. DR KEGG; mja:MJ_0692; -. DR eggNOG; arCOG01344; Archaea. DR eggNOG; COG2238; LUCA. DR InParanoid; P54057; -. DR KO; K02966; -. DR OMA; HIYLRKD; -. DR PhylomeDB; P54057; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_01474; Ribosomal_S19e; 1. DR InterPro; IPR001266; Ribosomal_S19e. DR InterPro; IPR027548; Ribosomal_S19e_archaeal. DR InterPro; IPR018277; Ribosomal_S19e_CS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR11710; PTHR11710; 1. DR Pfam; PF01090; Ribosomal_S19e; 1. DR ProDom; PD003854; Ribosomal_S19e; 1. DR SMART; SM01413; Ribosomal_S19e; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS00628; RIBOSOMAL_S19E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 148 30S ribosomal protein S19e. FT /FTId=PRO_0000153840. SQ SEQUENCE 148 AA; 17030 MW; CEE6467899CF89BE CRC64; MVTVYDVPAD KLIQKTAEKL KEMNIGVPEW VDFVKTGVSR ERRPDQDDWW YIRCASILRK IYIYGPVGVS RLRTAYGGRK NRGHEPEHFY KGSGNIIRKA LQELEKLGLV EKTPEGRVVT PKGRSFLDNI AKEVRDEIIN EIPALAKY // ID RPOH_METJA Reviewed; 78 AA. AC Q58443; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 103. DE RecName: Full=DNA-directed RNA polymerase subunit H {ECO:0000255|HAMAP-Rule:MF_00025}; DE EC=2.7.7.6 {ECO:0000255|HAMAP-Rule:MF_00025}; GN Name=rpoH {ECO:0000255|HAMAP-Rule:MF_00025}; OrderedLocusNames=MJ1039; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP STRUCTURE BY NMR. RX PubMed=10191143; DOI=10.1006/jmbi.1999.2638; RA Thiru A., Hodach M., Eloranta J.J., Kostourou V., Weinzierl R.O., RA Matthews S.; RT "RNA polymerase subunit H features a beta-ribbon motif within a novel RT fold that is present in archaea and eukaryotes."; RL J. Mol. Biol. 287:753-760(1999). CC -!- FUNCTION: DNA-dependent RNA polymerase catalyzes the transcription CC of DNA into RNA using the four ribonucleoside triphosphates as CC substrates. CC -!- CATALYTIC ACTIVITY: Nucleoside triphosphate + RNA(n) = diphosphate CC + RNA(n+1). {ECO:0000255|HAMAP-Rule:MF_00025}. CC -!- SIMILARITY: Belongs to the archaeal RpoH/eukaryotic RPB5 RNA CC polymerase subunit family. {ECO:0000255|HAMAP-Rule:MF_00025}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99042.1; -; Genomic_DNA. DR PIR; F64429; F64429. DR PDB; 1HMJ; NMR; -; A=1-78. DR PDBsum; 1HMJ; -. DR ProteinModelPortal; Q58443; -. DR STRING; 243232.MJ_1039; -. DR EnsemblBacteria; AAB99042; AAB99042; MJ_1039. DR KEGG; mja:MJ_1039; -. DR eggNOG; arCOG04258; Archaea. DR eggNOG; COG2012; LUCA. DR InParanoid; Q58443; -. DR KO; K03053; -. DR OMA; EHELVPK; -. DR PhylomeDB; Q58443; -. DR EvolutionaryTrace; Q58443; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR Gene3D; 3.90.940.20; -; 1. DR HAMAP; MF_00025; RNApol_RpoH_RPB5; 1. DR InterPro; IPR000783; RNA_pol_subH/Rpb5_C. DR InterPro; IPR020608; RNA_pol_subH/Rpb5_CS. DR InterPro; IPR020609; RpoH/RPB5. DR Pfam; PF01191; RNA_pol_Rpb5_C; 1. DR ProDom; PD005155; RNA_pol_subH/Rpb5_C; 1. DR SUPFAM; SSF55287; SSF55287; 1. DR PROSITE; PS01110; RNA_POL_H_23KD; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-directed RNA polymerase; KW Nucleotidyltransferase; Reference proteome; Transcription; KW Transferase. FT CHAIN 1 78 DNA-directed RNA polymerase subunit H. FT /FTId=PRO_0000146092. SQ SEQUENCE 78 AA; 9001 MW; CDF2DAF342E6D41B CRC64; MKVTDHILVP KHEIVPKEEV EEILKRYNIK IQQLPKIYED DPVIQEIGAK EGDVVRVIRK SPTAGVSIAY RLVIKRII // ID RS14Z_METJA Reviewed; 53 AA. AC P54110; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=30S ribosomal protein S14 type Z {ECO:0000255|HAMAP-Rule:MF_01364}; GN Name=rps14 {ECO:0000255|HAMAP-Rule:MF_01364}; GN OrderedLocusNames=MJ0469.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION. RA Veuthey A.-L., Bairoch A.; RL Unpublished observations (AUG-1996). CC -!- FUNCTION: Binds 16S rRNA, required for the assembly of 30S CC particles. {ECO:0000255|HAMAP-Rule:MF_01364}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01364}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01364}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01364}. CC -!- SIMILARITY: Belongs to the ribosomal protein S14P family. Zinc- CC binding S14P subfamily. {ECO:0000255|HAMAP-Rule:MF_01364}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P54110; -. DR SMR; P54110; 7-51. DR STRING; 243232.MJ_0469.1; -. DR eggNOG; arCOG00782; Archaea. DR eggNOG; COG0199; LUCA. DR InParanoid; P54110; -. DR OMA; FREIAHE; -. DR PhylomeDB; P54110; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01364_A; Ribosomal_S14_2_A; 1. DR InterPro; IPR001209; Ribosomal_S14. DR InterPro; IPR018271; Ribosomal_S14_CS. DR InterPro; IPR023676; Ribosomal_S14_type-Z_arc. DR Pfam; PF00253; Ribosomal_S14; 1. DR PROSITE; PS00527; RIBOSOMAL_S14; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding; Zinc. FT CHAIN 1 53 30S ribosomal protein S14 type Z. FT /FTId=PRO_0000130992. FT METAL 17 17 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 20 20 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 36 36 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. FT METAL 39 39 Zinc. {ECO:0000255|HAMAP-Rule:MF_01364}. SQ SEQUENCE 53 AA; 6192 MW; 975C67F2285BEFEF CRC64; MAKKPWKKKY GYGIRPCQRC GHVGPGLIRK YGLNLCRQCF REIAHKLGFK KLD // ID RS27A_METJA Reviewed; 60 AA. AC P54031; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=30S ribosomal protein S27ae {ECO:0000255|HAMAP-Rule:MF_00777}; GN Name=rps27ae {ECO:0000255|HAMAP-Rule:MF_00777}; GN OrderedLocusNames=MJ0393; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00777}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00777}; CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00777}. CC -!- SIMILARITY: Belongs to the ribosomal protein S27Ae family. CC {ECO:0000255|HAMAP-Rule:MF_00777}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98383.1; -; Genomic_DNA. DR PIR; A64349; A64349. DR ProteinModelPortal; P54031; -. DR SMR; P54031; 8-60. DR STRING; 243232.MJ_0393; -. DR EnsemblBacteria; AAB98383; AAB98383; MJ_0393. DR KEGG; mja:MJ_0393; -. DR eggNOG; arCOG04183; Archaea. DR eggNOG; COG1998; LUCA. DR InParanoid; P54031; -. DR KO; K02977; -. DR OMA; KWKLYEV; -. DR PhylomeDB; P54031; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00777; Ribosomal_S27ae; 1. DR InterPro; IPR002906; Ribosomal_S27a. DR InterPro; IPR022845; Ribosomal_S27ae. DR InterPro; IPR011332; Ribosomal_zn-bd. DR Pfam; PF01599; Ribosomal_S27; 1. DR SMART; SM01402; Ribosomal_S27; 1. DR SUPFAM; SSF57829; SSF57829; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger. FT CHAIN 1 60 30S ribosomal protein S27ae. FT /FTId=PRO_0000137694. FT ZN_FING 27 48 C4-type. {ECO:0000255|HAMAP- FT Rule:MF_00777}. FT COMPBIAS 1 25 Lys-rich (highly basic). FT METAL 27 27 Zinc. {ECO:0000255|HAMAP-Rule:MF_00777}. FT METAL 30 30 Zinc. {ECO:0000255|HAMAP-Rule:MF_00777}. FT METAL 45 45 Zinc. {ECO:0000255|HAMAP-Rule:MF_00777}. FT METAL 48 48 Zinc. {ECO:0000255|HAMAP-Rule:MF_00777}. SQ SEQUENCE 60 AA; 7048 MW; 796AA6E07CCA47F7 CRC64; MTKGKKTAKY KYYKIEGDKV IRLKKTCPRC GPGVFMAEHL NRYACGKCGY MEWKQPQKKE // ID RS12_METJA Reviewed; 148 AA. AC P54062; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 93. DE RecName: Full=30S ribosomal protein S12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN Name=rps12 {ECO:0000255|HAMAP-Rule:MF_00403}; GN OrderedLocusNames=MJ1046; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: With S4 and S5 plays an important role in translational CC accuracy. Located at the interface of the 30S and 50S subunits. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00403}. CC -!- SIMILARITY: Belongs to the ribosomal protein S12P family. CC {ECO:0000255|HAMAP-Rule:MF_00403}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99050.1; -; Genomic_DNA. DR ProteinModelPortal; P54062; -. DR STRING; 243232.MJ_1046; -. DR EnsemblBacteria; AAB99050; AAB99050; MJ_1046. DR KEGG; mja:MJ_1046; -. DR eggNOG; arCOG04255; Archaea. DR eggNOG; COG0048; LUCA. DR InParanoid; P54062; -. DR KO; K02950; -. DR OMA; MPGKKSP; -. DR PhylomeDB; P54062; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00403_A; Ribosomal_S12_A; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022863; Ribosomal_S12. DR InterPro; IPR006032; Ribosomal_S12/S23. DR InterPro; IPR005680; Ribosomal_S23_euk/arc. DR PANTHER; PTHR11652; PTHR11652; 1. DR Pfam; PF00164; Ribosom_S12_S23; 1. DR PIRSF; PIRSF002133; Ribosomal_S12/S23; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00982; uS12_E_A; 1. DR PROSITE; PS00055; RIBOSOMAL_S12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 148 30S ribosomal protein S12. FT /FTId=PRO_0000146369. SQ SEQUENCE 148 AA; 16829 MW; 6261744BDED62CFD CRC64; MSGSKSPRGE FAGRKLRLKR KWCRWHDYNY VRRVLKLKEK YDPLEGAPMA RGIVIEKVGL EAKQPNSAIR KCVRVQLIKN GRVVTAFCPG NHAINFIDEH DEVIIEGIGG PKGPRAKGDI PGVKYKVIMV GRNSLRELVR GRQEKIKR // ID RS13_METJA Reviewed; 150 AA. AC P54019; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 88. DE RecName: Full=30S ribosomal protein S13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN Name=rps13 {ECO:0000255|HAMAP-Rule:MF_01315}; GN OrderedLocusNames=MJ0189; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Located at the top of the head of the 30S subunit, it CC contacts several helices of the 16S rRNA. In the 70S ribosome it CC contacts the 23S rRNA (bridge B1a) and protein L5 of the 50S CC subunit (bridge B1b), connecting the 2 subunits; these bridges are CC implicated in subunit movement. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Forms a loose CC heterodimer with protein S19. Forms two bridges to the 50S subunit CC in the 70S ribosome. {ECO:0000255|HAMAP-Rule:MF_01315}. CC -!- SIMILARITY: Belongs to the ribosomal protein S13P family. CC {ECO:0000255|HAMAP-Rule:MF_01315}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98169.1; -; Genomic_DNA. DR ProteinModelPortal; P54019; -. DR STRING; 243232.MJ_0189; -. DR EnsemblBacteria; AAB98169; AAB98169; MJ_0189. DR KEGG; mja:MJ_0189; -. DR eggNOG; arCOG01722; Archaea. DR eggNOG; COG0099; LUCA. DR InParanoid; P54019; -. DR KO; K02952; -. DR OMA; SYKGVRH; -. DR PhylomeDB; P54019; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 4.10.910.10; -; 1. DR HAMAP; MF_01315; Ribosomal_S13_S18; 1. DR InterPro; IPR027437; 30s_Rbsml_prot_S13_C. DR InterPro; IPR001892; Ribosomal_S13. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR InterPro; IPR019977; Ribosomal_S13_archaeal. DR InterPro; IPR018269; Ribosomal_S13_CS. DR Pfam; PF00416; Ribosomal_S13; 1. DR PIRSF; PIRSF002134; Ribosomal_S13; 1. DR SUPFAM; SSF46946; SSF46946; 1. DR TIGRFAMs; TIGR03629; uS13_arch; 1. DR PROSITE; PS00646; RIBOSOMAL_S13_1; 1. DR PROSITE; PS50159; RIBOSOMAL_S13_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 150 30S ribosomal protein S13. FT /FTId=PRO_0000132181. SQ SEQUENCE 150 AA; 17380 MW; DD4014968FD075CB CRC64; MQNSEFKYLI RVSRTDLDGN KKLIMALQDI YGVGEAMARA IVRVAKLDPN KLAGYLTEEE VKKIEEVLAD PAKFGIPSWM FNRRKDYVTG EDKHVIESDL MIIKQEDINR LKRIRCYRGI RHELGLPCRG QRTKSTFRRG PTVGVSRRKK // ID RS11_METJA Reviewed; 129 AA. AC P54021; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=30S ribosomal protein S11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN Name=rps11 {ECO:0000255|HAMAP-Rule:MF_01310}; GN OrderedLocusNames=MJ0191; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Located on the platform of the 30S subunit. CC {ECO:0000255|HAMAP-Rule:MF_01310}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01310}. CC -!- SIMILARITY: Belongs to the ribosomal protein S11P family. CC {ECO:0000255|HAMAP-Rule:MF_01310}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98171.1; -; Genomic_DNA. DR PIR; H64323; H64323. DR ProteinModelPortal; P54021; -. DR STRING; 243232.MJ_0191; -. DR EnsemblBacteria; AAB98171; AAB98171; MJ_0191. DR KEGG; mja:MJ_0191; -. DR eggNOG; arCOG04240; Archaea. DR eggNOG; COG0100; LUCA. DR InParanoid; P54021; -. DR KO; K02948; -. DR OMA; NNTIIHA; -. DR PhylomeDB; P54021; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0048027; F:mRNA 5'-UTR binding; IBA:GO_Central. DR GO; GO:0070181; F:small ribosomal subunit rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.420.80; -; 1. DR HAMAP; MF_01310; Ribosomal_S11; 1. DR InterPro; IPR001971; Ribosomal_S11. DR InterPro; IPR019961; Ribosomal_S11_archaeal. DR InterPro; IPR018102; Ribosomal_S11_CS. DR PANTHER; PTHR11759; PTHR11759; 1. DR Pfam; PF00411; Ribosomal_S11; 1. DR PIRSF; PIRSF002131; Ribosomal_S11; 1. DR TIGRFAMs; TIGR03628; arch_S11P; 1. DR PROSITE; PS00054; RIBOSOMAL_S11; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 129 30S ribosomal protein S11. FT /FTId=PRO_0000123271. SQ SEQUENCE 129 AA; 13996 MW; 67C6C99468E2F75F CRC64; MAEQKKEKWG IVHIYSSYNN TIIHATDITG AETIARVSGG RVTRNQRDEG SPYAAMQAAF KLAEVLKERG IENIHIKVRA PGGSGQKNPG PGAQAAIRAL ARAGLRIGRI EDVTPVPHDG TTPKKRFKK // ID RS17E_METJA Reviewed; 62 AA. AC P54026; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 19-DEC-2001, sequence version 2. DT 17-FEB-2016, entry version 89. DE RecName: Full=30S ribosomal protein S17e {ECO:0000255|HAMAP-Rule:MF_00511}; GN Name=rps17e {ECO:0000255|HAMAP-Rule:MF_00511}; GN OrderedLocusNames=MJ0245; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S17e family. CC {ECO:0000255|HAMAP-Rule:MF_00511}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98233.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98233.1; ALT_INIT; Genomic_DNA. DR PIR; F64330; F64330. DR ProteinModelPortal; P54026; -. DR SMR; P54026; 1-61. DR STRING; 243232.MJ_0245; -. DR EnsemblBacteria; AAB98233; AAB98233; MJ_0245. DR KEGG; mja:MJ_0245; -. DR eggNOG; arCOG01885; Archaea. DR eggNOG; COG1383; LUCA. DR InParanoid; P54026; -. DR KO; K02962; -. DR OMA; FTTDFEQ; -. DR PhylomeDB; P54026; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.60.20; -; 1. DR HAMAP; MF_00511; Ribosomal_S17e; 1. DR InterPro; IPR001210; Ribosomal_S17e. DR InterPro; IPR018273; Ribosomal_S17e_CS. DR PANTHER; PTHR10732; PTHR10732; 1. DR Pfam; PF00833; Ribosomal_S17e; 1. DR SUPFAM; SSF116820; SSF116820; 1. DR PROSITE; PS00712; RIBOSOMAL_S17E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 62 30S ribosomal protein S17e. FT /FTId=PRO_0000141553. SQ SEQUENCE 62 AA; 7510 MW; 7D0DA547702EF62E CRC64; MGRIRQTLIK RTAMELIKKY RDLFTTDFET NKRVLEEVAQ ISTKRLRNRI AGYITHKMRQ LQ // ID RS4E_METJA Reviewed; 244 AA. AC P54039; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=30S ribosomal protein S4e; GN Name=rps4e; OrderedLocusNames=MJ0468; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S4e family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98457.1; -; Genomic_DNA. DR PIR; D64358; D64358. DR ProteinModelPortal; P54039; -. DR STRING; 243232.MJ_0468; -. DR EnsemblBacteria; AAB98457; AAB98457; MJ_0468. DR KEGG; mja:MJ_0468; -. DR eggNOG; arCOG04093; Archaea. DR eggNOG; COG1471; LUCA. DR InParanoid; P54039; -. DR KO; K02987; -. DR OMA; HIQLNLH; -. DR PhylomeDB; P54039; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00485; Ribosomal_S4e; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR000876; Ribosomal_S4e. DR InterPro; IPR013845; Ribosomal_S4e_central_region. DR InterPro; IPR013843; Ribosomal_S4e_N. DR InterPro; IPR018199; Ribosomal_S4e_N_CS. DR InterPro; IPR002942; S4_RNA-bd. DR PANTHER; PTHR11581; PTHR11581; 1. DR Pfam; PF00900; Ribosomal_S4e; 1. DR Pfam; PF08071; RS4NT; 1. DR Pfam; PF01479; S4; 1. DR PIRSF; PIRSF002116; Ribosomal_S4; 1. DR ProDom; PD002667; Ribosomal_S4e_central; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00363; S4; 1. DR PROSITE; PS00528; RIBOSOMAL_S4E; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 244 30S ribosomal protein S4e. FT /FTId=PRO_0000130849. FT DOMAIN 43 108 S4 RNA-binding. SQ SEQUENCE 244 AA; 27659 MW; 6759485019B86AC7 CRC64; MAKKGPKRHL KRLAAPVRWE LPRKIHKFTV RPLPGAHPMS ESLPLLLIVR DILKYADNAR EAKKIIKMGK VLVDGRVRKE EKLPVGLMDV VSLPDANENY RVLFDRKGRI KLKPTENPDV KLCKIKNKTV IKGGHIQLNL HDGRNIVIKV SDPTKAEEDV YKTGDTLLIS IPEQEIKAHI PFEVGKLAYI TGGKHVGDFA KIVEIERRGI YPDIVTLENM DGEKFKTVKD YVFVVGDEEP IIKL // ID RS5_METJA Reviewed; 217 AA. AC P54045; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=30S ribosomal protein S5 {ECO:0000255|HAMAP-Rule:MF_01307}; GN Name=rps5 {ECO:0000255|HAMAP-Rule:MF_01307}; OrderedLocusNames=MJ0475; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: With S4 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S4. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- DOMAIN: The N-terminal domain interacts with the head of the 30S CC subunit; the C-terminal domain interacts with the body and CC contacts protein S4. The interaction surface between S4 and S5 is CC involved in control of translational fidelity. CC -!- SIMILARITY: Belongs to the ribosomal protein S5P family. CC {ECO:0000255|HAMAP-Rule:MF_01307}. CC -!- SIMILARITY: Contains 1 S5 DRBM domain. {ECO:0000255|HAMAP- CC Rule:MF_01307}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98464.1; -; Genomic_DNA. DR PIR; C64359; C64359. DR ProteinModelPortal; P54045; -. DR STRING; 243232.MJ_0475; -. DR EnsemblBacteria; AAB98464; AAB98464; MJ_0475. DR KEGG; mja:MJ_0475; -. DR eggNOG; arCOG04087; Archaea. DR eggNOG; COG0098; LUCA. DR InParanoid; P54045; -. DR KO; K02988; -. DR OMA; GIKDVWT; -. DR PhylomeDB; P54045; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.160.20; -; 1. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_01307_A; Ribosomal_S5_A; 1. DR InterPro; IPR014720; dsRBD_dom. DR InterPro; IPR000851; Ribosomal_S5. DR InterPro; IPR005324; Ribosomal_S5_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005711; Ribosomal_S5_euk/arc. DR InterPro; IPR013810; Ribosomal_S5_N. DR InterPro; IPR018192; Ribosomal_S5_N_CS. DR PANTHER; PTHR13718; PTHR13718; 1. DR Pfam; PF00333; Ribosomal_S5; 1. DR Pfam; PF03719; Ribosomal_S5_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR01020; uS5_euk_arch; 1. DR PROSITE; PS00585; RIBOSOMAL_S5; 1. DR PROSITE; PS50881; S5_DSRBD; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 217 30S ribosomal protein S5. FT /FTId=PRO_0000131648. FT DOMAIN 49 112 S5 DRBM. {ECO:0000255|HAMAP- FT Rule:MF_01307}. SQ SEQUENCE 217 AA; 23839 MW; 4C84EB0E6D336A08 CRC64; MRFNIDEWEP KTTIGRMVKE GQITDIDYIL DNNLPILEPE IVDALLPDLE EKVLDVKLVQ RMHKSGRRAR FRATVVVGNR NGYVGVGKGK AKEVGPAIRK AIAQAKKNII RVKRGCGSWE CGCGTPHSIP YKGYGKCGST AIEILPAPKG VGLVAGDVAK AVLGLAGIKD VWTKTFGETR TTYNFAMATF EALKSLNFTR TMEKHKEKLG IVEGRVL // ID RS2_METJA Reviewed; 222 AA. AC P54109; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 17-FEB-2016, entry version 92. DE RecName: Full=30S ribosomal protein S2; GN Name=rps2; OrderedLocusNames=MJ0982; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S2P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98985.1; -; Genomic_DNA. DR ProteinModelPortal; P54109; -. DR SMR; P54109; 3-201. DR STRING; 243232.MJ_0982; -. DR EnsemblBacteria; AAB98985; AAB98985; MJ_0982. DR KEGG; mja:MJ_0982; -. DR eggNOG; arCOG04245; Archaea. DR eggNOG; COG0052; LUCA. DR InParanoid; P54109; -. DR KO; K02967; -. DR OMA; HTTRPYG; -. DR PhylomeDB; P54109; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000447; P:endonucleolytic cleavage in ITS1 to separate SSU-rRNA from 5.8S rRNA and LSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000461; P:endonucleolytic cleavage to generate mature 3'-end of SSU-rRNA from (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR HAMAP; MF_00291_A; Ribosomal_S2_A; 1. DR InterPro; IPR001865; Ribosomal_S2. DR InterPro; IPR023454; Ribosomal_S2_arc. DR InterPro; IPR018130; Ribosomal_S2_CS. DR InterPro; IPR005707; Ribosomal_S2_euk/arc. DR InterPro; IPR023591; Ribosomal_S2_flav_dom. DR PANTHER; PTHR11489; PTHR11489; 1. DR Pfam; PF00318; Ribosomal_S2; 2. DR PRINTS; PR00395; RIBOSOMALS2. DR SUPFAM; SSF52313; SSF52313; 1. DR TIGRFAMs; TIGR01012; uS2_euk_arch; 1. DR PROSITE; PS00963; RIBOSOMAL_S2_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 222 30S ribosomal protein S2. FT /FTId=PRO_0000134323. SQ SEQUENCE 222 AA; 25708 MW; 0271F5EAC0127616 CRC64; MSEKELLVPL DTYLASGIHI GTQQKTKDME KFIYRVRSDG LYVLDVRKTD ERLRIAAKFL ARYEPEDILA VSRRIYTMGP LEEFGKYTGI RTVAGRFVPG TLTNPAYKGF MEPEVVFISD PRVDRQALKE ATEIGVPIVG LCDTEHLTSF IDLVIPTNNK GKKAVALIYY LLTREYLKNR GVITDDTKLP FTYEEFLEKA ANPKYRIIIQ PKDKRRRRRR RK // ID RS3A_METJA Reviewed; 222 AA. AC P54059; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 85. DE RecName: Full=30S ribosomal protein S3Ae {ECO:0000255|HAMAP-Rule:MF_00359}; DE AltName: Full=Ribosomal protein S1e {ECO:0000255|HAMAP-Rule:MF_00359}; GN Name=rps3ae {ECO:0000255|HAMAP-Rule:MF_00359}; GN OrderedLocusNames=MJ0980; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the ribosomal protein S3Ae family. CC {ECO:0000255|HAMAP-Rule:MF_00359}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98983.1; -; Genomic_DNA. DR PIR; D64422; D64422. DR ProteinModelPortal; P54059; -. DR STRING; 243232.MJ_0980; -. DR EnsemblBacteria; AAB98983; AAB98983; MJ_0980. DR KEGG; mja:MJ_0980; -. DR eggNOG; arCOG04186; Archaea. DR eggNOG; COG1890; LUCA. DR InParanoid; P54059; -. DR KO; K02984; -. DR OMA; GHDTTRE; -. DR PhylomeDB; P54059; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00359; Ribosomal_S3Ae; 1. DR InterPro; IPR030838; 30S_S3Ae. DR InterPro; IPR001593; Ribosomal_S3Ae. DR InterPro; IPR018281; Ribosomal_S3Ae_CS. DR Pfam; PF01015; Ribosomal_S3Ae; 1. DR SMART; SM01397; Ribosomal_S3Ae; 1. DR PROSITE; PS01191; RIBOSOMAL_S3AE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 222 30S ribosomal protein S3Ae. FT /FTId=PRO_0000153548. SQ SEQUENCE 222 AA; 25777 MW; D3B18E711B25A41F CRC64; MATARTARSR RKVRKVRDKW KEKVWYEIYA TPEFGGVFIG YTPANDPSLV LGRVAETSLR DLTGDPTKHM HRVYFKIFGV TGNKAIAQYY GHDTTREFMK SQIRRRRSRI DAILDVKTQD GHKIRTKAMV LTAYRANTKQ KSDIRKKMEE IIKAMAKEKT FPQYVQAMLF GEMAEKIKNE CKKIFPIKNV IIYKSEVLSL AKKEENEGFV KEAEEETAEA QE // ID RS3_METJA Reviewed; 208 AA. AC P54034; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=30S ribosomal protein S3 {ECO:0000255|HAMAP-Rule:MF_01309}; GN Name=rps3 {ECO:0000255|HAMAP-Rule:MF_01309}; OrderedLocusNames=MJ0461; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Binds the lower part of the 30S subunit head. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_01309}. CC -!- SIMILARITY: Belongs to the ribosomal protein S3P family. CC {ECO:0000255|HAMAP-Rule:MF_01309}. CC -!- SIMILARITY: Contains 1 KH type-2 domain. {ECO:0000255|HAMAP- CC Rule:MF_01309}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98450.1; -; Genomic_DNA. DR PIR; E64357; E64357. DR ProteinModelPortal; P54034; -. DR STRING; 243232.MJ_0461; -. DR EnsemblBacteria; AAB98450; AAB98450; MJ_0461. DR KEGG; mja:MJ_0461; -. DR eggNOG; arCOG04097; Archaea. DR eggNOG; COG0092; LUCA. DR InParanoid; P54034; -. DR KO; K02982; -. DR OMA; DFIDHAT; -. DR PhylomeDB; P54034; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0003684; F:damaged DNA binding; IBA:GO_Central. DR GO; GO:0008534; F:oxidized purine nucleobase lesion DNA N-glycosylase activity; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006281; P:DNA repair; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1140.32; -; 1. DR Gene3D; 3.30.300.20; -; 1. DR HAMAP; MF_01309_A; Ribosomal_S3_A; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR027488; Ribosomal_S3_arc. DR InterPro; IPR001351; Ribosomal_S3_C. DR InterPro; IPR018280; Ribosomal_S3_CS. DR InterPro; IPR005703; Ribosomal_S3_euk/arc. DR Pfam; PF07650; KH_2; 1. DR SMART; SM00322; KH; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR SUPFAM; SSF54821; SSF54821; 1. DR TIGRFAMs; TIGR01008; uS3_euk_arch; 1. DR PROSITE; PS50823; KH_TYPE_2; 1. DR PROSITE; PS00548; RIBOSOMAL_S3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 208 30S ribosomal protein S3. FT /FTId=PRO_0000130250. FT DOMAIN 16 85 KH type-2. {ECO:0000255|HAMAP- FT Rule:MF_01309}. SQ SEQUENCE 208 AA; 23325 MW; C78D8E96A5A22A6A CRC64; MIERTFVKEN VKRLLIDEYF KKELSKAGYS HCDIRKTPIG TKIIIYAEKP GFVIGRRGSR IRELTETLAK EFGVEKPQID VKPVENPDLD AQVVAQKVAQ SLERGLHFRR VGHTAVRRVM NAGAKGVIVI ISGKLTGERA RTEKFMAGYM KHCGEPAEEL VDKGRAIAKT KPGVIGVTVK IMRPDVLLPD EIIIKEDAEV KHVVEEEQ // ID RS24_METJA Reviewed; 101 AA. AC P54032; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=30S ribosomal protein S24e {ECO:0000255|HAMAP-Rule:MF_00545}; GN Name=rps24e {ECO:0000255|HAMAP-Rule:MF_00545}; GN OrderedLocusNames=MJ0394; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S24e family. CC {ECO:0000255|HAMAP-Rule:MF_00545}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98384.1; -; Genomic_DNA. DR PIR; B64349; B64349. DR ProteinModelPortal; P54032; -. DR STRING; 243232.MJ_0394; -. DR EnsemblBacteria; AAB98384; AAB98384; MJ_0394. DR KEGG; mja:MJ_0394; -. DR eggNOG; arCOG04182; Archaea. DR eggNOG; COG2004; LUCA. DR InParanoid; P54032; -. DR KO; K02974; -. DR OMA; LHRTDVT; -. DR PhylomeDB; P54032; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.330; -; 1. DR HAMAP; MF_00545; Ribosomal_S24e; 1. DR InterPro; IPR012677; Nucleotide-bd_a/b_plait. DR InterPro; IPR012678; Ribosomal_L23/L15e_core_dom. DR InterPro; IPR001976; Ribosomal_S24e. DR InterPro; IPR018098; Ribosomal_S24e_CS. DR PANTHER; PTHR10496; PTHR10496; 1. DR Pfam; PF01282; Ribosomal_S24e; 1. DR ProDom; PD006052; Ribosomal_S24e; 1. DR SUPFAM; SSF54189; SSF54189; 1. DR PROSITE; PS00529; RIBOSOMAL_S24E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 101 30S ribosomal protein S24e. FT /FTId=PRO_0000137643. SQ SEQUENCE 101 AA; 11842 MW; F84A3BE414F09036 CRC64; MEIKILSERY NPLLKRKEYR FIVDHDGPTP TFKDVKLKLA AILNANKDLL IVEKIVEEAG MQRARGYAKL YDNEEMLKLV EREHILRKNK IEEETAAEEG E // ID RS6E_METJA Reviewed; 131 AA. AC P54067; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=30S ribosomal protein S6e {ECO:0000255|HAMAP-Rule:MF_00512}; GN Name=rps6e {ECO:0000255|HAMAP-Rule:MF_00512}; GN OrderedLocusNames=MJ1260; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S6e family. CC {ECO:0000255|HAMAP-Rule:MF_00512}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99263.1; -; Genomic_DNA. DR PIR; C64457; C64457. DR STRING; 243232.MJ_1260; -. DR EnsemblBacteria; AAB99263; AAB99263; MJ_1260. DR KEGG; mja:MJ_1260; -. DR eggNOG; arCOG01946; Archaea. DR eggNOG; COG2125; LUCA. DR InParanoid; P54067; -. DR KO; K02991; -. DR OMA; EQDANRF; -. DR PhylomeDB; P54067; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0042274; P:ribosomal small subunit biogenesis; IBA:GO_Central. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00512; Ribosomal_S6e; 1. DR InterPro; IPR001377; Ribosomal_S6e. DR InterPro; IPR020924; Ribosomal_S6e_arc. DR InterPro; IPR018282; Ribosomal_S6e_CS. DR PANTHER; PTHR11502; PTHR11502; 1. DR Pfam; PF01092; Ribosomal_S6e; 1. DR SMART; SM01405; Ribosomal_S6e; 1. DR PROSITE; PS00578; RIBOSOMAL_S6E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 131 30S ribosomal protein S6e. FT /FTId=PRO_0000137348. SQ SEQUENCE 131 AA; 14372 MW; 6BFD365C1BFF006D CRC64; MPTAKFVVAD PKTGRCYQIE ADNTPLVGKK IGEVFDGKII GLEGYKLQIR GGTDSSGFPM RPDIHGSRKV RVLLSAPPGF KPKRKGERRR KTVRGNTIAP DIVQINVKVV EYGEKSIPEL LGLEGGENQE Q // ID RS8E_METJA Reviewed; 129 AA. AC P54055; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=30S ribosomal protein S8e; GN Name=rps8e; OrderedLocusNames=MJ0673; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S8e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98667.1; -; Genomic_DNA. DR PIR; A64384; A64384. DR ProteinModelPortal; P54055; -. DR STRING; 243232.MJ_0673; -. DR EnsemblBacteria; AAB98667; AAB98667; MJ_0673. DR KEGG; mja:MJ_0673; -. DR eggNOG; arCOG04154; Archaea. DR eggNOG; COG2007; LUCA. DR InParanoid; P54055; -. DR KO; K02995; -. DR OMA; NPNYVRR; -. DR PhylomeDB; P54055; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00029; Ribosomal_S8e; 1. DR InterPro; IPR020919; Ribosomal_protein_S8e_arc. DR InterPro; IPR001047; Ribosomal_S8e. DR InterPro; IPR022309; Ribosomal_S8e/biogenesis_NSA2. DR InterPro; IPR018283; Ribosomal_S8e_CS. DR PANTHER; PTHR10394; PTHR10394; 1. DR Pfam; PF01201; Ribosomal_S8e; 1. DR TIGRFAMs; TIGR00307; eS8; 1. DR PROSITE; PS01193; RIBOSOMAL_S8E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 129 30S ribosomal protein S8e. FT /FTId=PRO_0000122267. SQ SEQUENCE 129 AA; 14539 MW; 1C51A1576A252E16 CRC64; MSVWQGRSRR KPTGGLYRPA RKKRKYEMGR EPIETHVAEE AFKIKKVRTR GGNLKVKVVR TGFANVLDPE TGTCKKVKII TVRENKANIH YVRRNVITKG AIIETEIGLA KVTSRPGQDG TVNAILIKE // ID RS8_METJA Reviewed; 130 AA. AC P54041; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=30S ribosomal protein S8; GN Name=rps8; OrderedLocusNames=MJ0470; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.6 ANGSTROMS). RX PubMed=11478863; DOI=10.1006/jmbi.2001.4877; RA Tishchenko S., Nikulin A., Fomenkova N., Nevskaya N., Nikonov O., RA Dumas P., Moine H., Ehresmann B., Ehresmann C., Piendl W., Lamzin V., RA Garber M.B., Nikonov S.; RT "Detailed analysis of RNA-protein interactions within the ribosomal RT protein S8-rRNA complex from the archaeon Methanococcus jannaschii."; RL J. Mol. Biol. 311:311-324(2001). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA central domain where it helps coordinate CC assembly of the platform of the 30S subunit. {ECO:0000250}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. CC -!- SIMILARITY: Belongs to the ribosomal protein S8P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98459.1; -; Genomic_DNA. DR PIR; F64358; F64358. DR PDB; 1I6U; X-ray; 2.60 A; A/B=1-130. DR PDBsum; 1I6U; -. DR ProteinModelPortal; P54041; -. DR SMR; P54041; 2-130. DR STRING; 243232.MJ_0470; -. DR EnsemblBacteria; AAB98459; AAB98459; MJ_0470. DR KEGG; mja:MJ_0470; -. DR eggNOG; arCOG04091; Archaea. DR eggNOG; COG0096; LUCA. DR InParanoid; P54041; -. DR KO; K02994; -. DR OMA; SHITNSE; -. DR PhylomeDB; P54041; -. DR EvolutionaryTrace; P54041; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:UniProtKB-KW. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01302_A; Ribosomal_S8_A; 1. DR InterPro; IPR000630; Ribosomal_S8. DR PANTHER; PTHR11758; PTHR11758; 1. DR Pfam; PF00410; Ribosomal_S8; 1. DR SUPFAM; SSF56047; SSF56047; 1. DR PROSITE; PS00053; RIBOSOMAL_S8; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 130 30S ribosomal protein S8. FT /FTId=PRO_0000126540. FT HELIX 6 19 {ECO:0000244|PDB:1I6U}. FT STRAND 23 29 {ECO:0000244|PDB:1I6U}. FT HELIX 32 43 {ECO:0000244|PDB:1I6U}. FT STRAND 50 53 {ECO:0000244|PDB:1I6U}. FT STRAND 56 58 {ECO:0000244|PDB:1I6U}. FT STRAND 60 64 {ECO:0000244|PDB:1I6U}. FT STRAND 72 74 {ECO:0000244|PDB:1I6U}. FT HELIX 87 93 {ECO:0000244|PDB:1I6U}. FT STRAND 101 106 {ECO:0000244|PDB:1I6U}. FT STRAND 109 112 {ECO:0000244|PDB:1I6U}. FT HELIX 113 118 {ECO:0000244|PDB:1I6U}. FT STRAND 123 129 {ECO:0000244|PDB:1I6U}. SQ SEQUENCE 130 AA; 14625 MW; 759E14F6344ADBA5 CRC64; MSLMDPLANA LNHISNCERV GKKVVYIKPA SKLIGRVLKV MQDNGYIGEF EFIEDGRAGI FKVELIGKIN KCGAIKPRFP VKKFGYEKFE KRYLPARDFG ILIVSTTQGV MSHEEAKKRG LGGRLLAYVY // ID RS19_METJA Reviewed; 152 AA. AC P54018; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=30S ribosomal protein S19; GN Name=rps19; OrderedLocusNames=MJ0180; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Protein S19 forms a complex with S13 that binds strongly CC to the 16S ribosomal RNA. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ribosomal protein S19P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98165.1; -; Genomic_DNA. DR PIR; E64322; E64322. DR ProteinModelPortal; P54018; -. DR SMR; P54018; 50-137. DR STRING; 243232.MJ_0180; -. DR PRIDE; P54018; -. DR EnsemblBacteria; AAB98165; AAB98165; MJ_0180. DR KEGG; mja:MJ_0180; -. DR eggNOG; arCOG04099; Archaea. DR eggNOG; COG0185; LUCA. DR InParanoid; P54018; -. DR KO; K02965; -. DR OMA; QHGSPGM; -. DR PhylomeDB; P54018; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IEA:InterPro. DR GO; GO:0019843; F:rRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.860.10; -; 1. DR HAMAP; MF_00531; Ribosomal_S19; 1. DR InterPro; IPR002222; Ribosomal_S19. DR InterPro; IPR020934; Ribosomal_S19_CS. DR InterPro; IPR023575; Ribosomal_S19_SF. DR InterPro; IPR005713; Ribosomal_S19A/S15e. DR PANTHER; PTHR11880; PTHR11880; 1. DR Pfam; PF00203; Ribosomal_S19; 1. DR PIRSF; PIRSF002144; Ribosomal_S19; 1. DR PRINTS; PR00975; RIBOSOMALS19. DR SUPFAM; SSF54570; SSF54570; 1. DR TIGRFAMs; TIGR01025; uS19_arch; 1. DR PROSITE; PS00323; RIBOSOMAL_S19; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 152 30S ribosomal protein S19. FT /FTId=PRO_0000130002. SQ SEQUENCE 152 AA; 17680 MW; F098F2AEA7DE6212 CRC64; MASARRRRIK KKKQVISKKI EFRYRGYTLE ELQQMPLREF AKLLPARQRR TLLRGLTPQQ KKLAMKIKKA RRLLNKGKEP RIIRTHCRDF VITPDMVGLT FGVYNGKEFV EVKVTPEMIG HYLGEFSLTR KPVQHGAPGM GATRSSMFVP IK // ID RS28_METJA Reviewed; 75 AA. AC P54065; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 11-JAN-2001, sequence version 2. DT 17-FEB-2016, entry version 87. DE RecName: Full=30S ribosomal protein S28e; GN Name=rps28e; OrderedLocusNames=MJ1202; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S28e family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99206.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99206.1; ALT_INIT; Genomic_DNA. DR PIR; A64450; A64450. DR ProteinModelPortal; P54065; -. DR SMR; P54065; 9-75. DR STRING; 243232.MJ_1202; -. DR EnsemblBacteria; AAB99206; AAB99206; MJ_1202. DR KEGG; mja:MJ_1202; -. DR eggNOG; arCOG04314; Archaea. DR eggNOG; COG2053; LUCA. DR InParanoid; P54065; -. DR KO; K02979; -. DR OMA; ILCLLET; -. DR PhylomeDB; P54065; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00292; Ribosomal_S28e; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR000289; Ribosomal_S28e. DR InterPro; IPR028626; Ribosomal_S28e_CS. DR PANTHER; PTHR10769; PTHR10769; 1. DR Pfam; PF01200; Ribosomal_S28e; 1. DR ProDom; PD005541; Ribosomal_S28e; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS00961; RIBOSOMAL_S28E; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 75 30S ribosomal protein S28e. FT /FTId=PRO_0000136848. SQ SEQUENCE 75 AA; 8364 MW; 9827B6CAB41B65E6 CRC64; MEDEFVYKEA VAAEVIEVIG RTGVTGGIIQ VRCKILGGKD TGRVLVRNVK GPVKVGDIIM LRETEREARP LDRRR // ID RTCB_METJA Reviewed; 968 AA. AC Q58095; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 102. DE RecName: Full=tRNA-splicing ligase RtcB; DE EC=6.5.1.-; DE Contains: DE RecName: Full=Mja hyp2 intein; DE EC=3.1.-.-; GN Name=rtcB; OrderedLocusNames=MJ0682; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: tRNA-splicing ligase that acts by directly joining CC spliced tRNA halves to mature-sized tRNAs by incorporating the CC precursor-derived splice junction phosphate into the mature tRNA CC as a canonical 3',5'-phosphodiester. May act as an RNA ligase with CC broad substrate specificity, and may function toward other RNAs CC (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- MISCELLANEOUS: Ligation proceeds through 3 nucleotidyl transfer CC steps, with 2',3'-cyclic phosphate termini being hydrolyzed to 3'- CC P termini in a step that precedes 3'-P activation with GMP. In the CC first nucleotidyl transfer step, RtcB reacts with GTP to form a CC covalent RtcB-histidine-GMP intermediate with release of PPi; in CC the second step, the GMP moiety is transferred to the RNA 3'-P; in CC the third step, the 5'-OH from the opposite RNA strand attacks the CC activated 3'-P to form a 3',5'-phosphodiester bond and release GMP CC (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the RtcB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98677.1; -; Genomic_DNA. DR PIR; B64385; B64385. DR ProteinModelPortal; Q58095; -. DR SMR; Q58095; 5-98, 585-968. DR STRING; 243232.MJ_0682; -. DR EnsemblBacteria; AAB98677; AAB98677; MJ_0682. DR KEGG; mja:MJ_0682; -. DR eggNOG; arCOG03158; Archaea. DR eggNOG; arCOG04246; Archaea. DR eggNOG; ENOG4102TCK; Archaea. DR eggNOG; COG1372; LUCA. DR eggNOG; COG1690; LUCA. DR InParanoid; Q58095; -. DR KO; K14415; -. DR OMA; VHNCGVR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008452; F:RNA ligase activity; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-KW. DR Gene3D; 2.170.16.10; -; 3. DR Gene3D; 3.10.28.10; -; 2. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR001233; RtcB. DR PANTHER; PTHR11118; PTHR11118; 2. DR Pfam; PF14528; LAGLIDADG_3; 1. DR Pfam; PF01139; RtcB; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF103365; SSF103365; 2. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS01288; UPF0027; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; DNA-binding; Endonuclease; KW Hydrolase; Intron homing; Ligase; Manganese; Metal-binding; Nuclease; KW Protein splicing; Reference proteome; tRNA processing. FT CHAIN 1 97 tRNA-splicing ligase RtcB, 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000036183. FT CHAIN 98 585 Mja hyp2 intein. {ECO:0000255}. FT /FTId=PRO_0000036184. FT CHAIN 586 968 tRNA-splicing ligase RtcB, 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000036185. FT DOMAIN 245 414 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT NP_BIND 816 817 GMP. {ECO:0000250}. FT NP_BIND 863 866 GMP. {ECO:0000250}. FT NP_BIND 891 894 GMP. {ECO:0000250}. FT ACT_SITE 891 891 GMP-histidine intermediate. FT {ECO:0000250}. FT METAL 95 95 Manganese 1. {ECO:0000250}. FT METAL 98 98 Manganese 1. {ECO:0000250}. FT METAL 98 98 Manganese 2. {ECO:0000250}. FT METAL 691 691 Manganese 1. {ECO:0000250}. FT METAL 722 722 Manganese 2. {ECO:0000250}. FT METAL 816 816 Manganese 2. {ECO:0000250}. FT BINDING 694 694 GMP. {ECO:0000250}. FT BINDING 872 872 GMP. {ECO:0000250}. FT BINDING 967 967 GMP. {ECO:0000250}. SQ SEQUENCE 968 AA; 110206 MW; 39A2A66280466130 CRC64; MKDVLKRVSD VVWELPKDYK DCMRVPGRIY LNEILLDELE PEVLEQIANV ACLPGIYKYS IAMPDVHYGY GFAIGGVAAF DQREGVISPG GVGFDINCLT SNSKILTDDG YYIKLEKLKE KLDLHIKIYN TEEGEKSSNI LFVSERYADE KIIRIKTESG RVLEGSKDHP VLTLNGYVPM GMLKEGDDVI VYPYEGVEYE EPSDEIILDE DDFAEYDKQI IKYLKDRGLL PLRMDNKNIG IIARLLGFAF GDGSIVKENG DRERLYVAFY GKRETLIKIR EDLEKLGIKA SRIYSRKREV EIRNAYGDEY TSLCEDNSIK ITSKAFALFM HKLGMPIGKK TEQIYKIPEW IKKAPKWVKR NFLAGLFGAD GSRAVFKNYT PLPINLTMSK SEELKENILE FLNEIKLLLA EFDIESMIYE IKSLDGRVSY RLAIVGEESI KNFLGRINYE YSGEKKVIGL LAYEYLRRKD IAKEIRKKCI KRAKELYKKG VTVSEMLKMD EFRNEFISKR LIERAVYENL DEDDVRISTK FPKFEEFIEK YGVIGGFVID KIKEIEEISY DSKLYDVGIV SKEHNFIANS IVVHNCGVRL IRTNLTKEEV QSKIKELIKT LFKNVPSGLG SKGILKFSKS VMDDVLEEGV RWAVKEGYGW KEDLEFIEEH GCLKDADASY VSDKAKERGR VQLGSLGSGN HFLEVQYVEK VFDEEAAEIY GIEENQVVVL VHTGSRGLGH QICTDYLRIM EKAAKNYGIK LPDRQLACAP FESEEGQSYF KAMCCGANYA WANRQMITHW VRESFEEVFK IHAEDLEMNI VYDVAHNIAK KEEHIIDGRK VKVIVHRKGA TRAFPPKHEA IPKEYWSVGQ PVIIPGDMGT ASYLMRGTEI AMKETFGSTA HGAGRKLSRA KALKLWKGKE IQRRLAEMGI VAMSDSKAVM AEEAPEAYKS VDLVADTCHK AGISLKVARM RPLGVIKG // ID RUBY_METJA Reviewed; 204 AA. AC Q58144; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Putative rubrerythrin; GN OrderedLocusNames=MJ0734; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May provide oxidative stress protection via catalytic CC reduction of intracellular hydrogen peroxide. {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; CC Note=Binds 3 Fe(3+) ions per subunit. {ECO:0000250}; CC -!- SUBUNIT: Homodimer. Possesses two rubredoxin-like centers and two CC non-sulfur oxo-bridged di-iron centers per dimer (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC -!- SIMILARITY: Contains 1 rubredoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00241}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98729.1; -; Genomic_DNA. DR PIR; F64391; F64391. DR ProteinModelPortal; Q58144; -. DR STRING; 243232.MJ_0734; -. DR EnsemblBacteria; AAB98729; AAB98729; MJ_0734. DR KEGG; mja:MJ_0734; -. DR eggNOG; arCOG01097; Archaea. DR eggNOG; COG1592; LUCA. DR InParanoid; Q58144; -. DR OMA; CKHAKKF; -. DR PhylomeDB; Q58144; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Electron transport; Iron; Metal-binding; KW Reference proteome; Transport. FT CHAIN 1 204 Putative rubrerythrin. FT /FTId=PRO_0000135067. FT DOMAIN 1 159 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT DOMAIN 166 204 Rubredoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 24 24 Iron 1. {ECO:0000250}. FT METAL 57 57 Iron 1. {ECO:0000250}. FT METAL 57 57 Iron 2. {ECO:0000250}. FT METAL 107 107 Iron 2. {ECO:0000250}. FT METAL 110 110 Iron 1. {ECO:0000250}. FT METAL 141 141 Iron 1. {ECO:0000250}. FT METAL 141 141 Iron 2. {ECO:0000250}. FT METAL 144 144 Iron 2. {ECO:0000250}. FT METAL 171 171 Iron 3. {ECO:0000250}. FT METAL 174 174 Iron 3. {ECO:0000250}. FT METAL 187 187 Iron 3. {ECO:0000250}. FT METAL 190 190 Iron 3. {ECO:0000250}. SQ SEQUENCE 204 AA; 23835 MW; 25B2ABFB53DB6769 CRC64; MINNFFVINM KETLKNLTKA YIGESLARNR YTCYAKIAKQ EGYEQIAEIF LLTAENEREH AKWLYYLITE LKKKYNIDDK AIKVDGVEVP IVLGNTAENL KASIEGEHFE HTEMYPKFAD IAEKEGLKEI ADRLRAIGIA EKHHEERFKK LLKEVEEGTV FKKDKPVEWV CRKCGFVHLG KEPPEKCPSC SHPRKYFEVK CEKY // ID RS27_METJA Reviewed; 62 AA. AC P54028; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=30S ribosomal protein S27e; GN Name=rps27e; OrderedLocusNames=MJ0250; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000305}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the ribosomal protein S27e family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98237.1; -; Genomic_DNA. DR PIR; C64331; C64331. DR ProteinModelPortal; P54028; -. DR STRING; 243232.MJ_0250; -. DR EnsemblBacteria; AAB98237; AAB98237; MJ_0250. DR KEGG; mja:MJ_0250; -. DR eggNOG; arCOG04108; Archaea. DR eggNOG; COG2051; LUCA. DR InParanoid; P54028; -. DR KO; K02978; -. DR OMA; QIVFSHP; -. DR PhylomeDB; P54028; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 2.20.25.100; -; 1. DR HAMAP; MF_00371; Ribosomal_S27e; 1. DR InterPro; IPR000592; Ribosomal_S27e. DR InterPro; IPR023407; Ribosomal_S27e_Zn-bd_dom. DR InterPro; IPR011332; Ribosomal_zn-bd. DR PANTHER; PTHR11594; PTHR11594; 1. DR Pfam; PF01667; Ribosomal_S27e; 1. DR SUPFAM; SSF57829; SSF57829; 1. DR PROSITE; PS01168; RIBOSOMAL_S27E; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; KW Ribonucleoprotein; Ribosomal protein; Zinc; Zinc-finger. FT CHAIN 1 62 30S ribosomal protein S27e. FT /FTId=PRO_0000149072. FT ZN_FING 17 39 C4-type. {ECO:0000255}. SQ SEQUENCE 62 AA; 6797 MW; 0BD2AD7F93157BCB CRC64; MMELIPQPRT KFLRVQCPEC NNEQIVFGSP ATVVKCLTCG KVLVEPRGGK GKVKAKILEI LG // ID RS9_METJA Reviewed; 136 AA. AC P54024; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=30S ribosomal protein S9; GN Name=rps9; OrderedLocusNames=MJ0195; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ribosomal protein S9P family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98175.1; -; Genomic_DNA. DR PIR; D64324; D64324. DR ProteinModelPortal; P54024; -. DR STRING; 243232.MJ_0195; -. DR EnsemblBacteria; AAB98175; AAB98175; MJ_0195. DR KEGG; mja:MJ_0195; -. DR eggNOG; arCOG04243; Archaea. DR eggNOG; COG0103; LUCA. DR InParanoid; P54024; -. DR KO; K02996; -. DR OMA; YYQKFVD; -. DR PhylomeDB; P54024; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000462; P:maturation of SSU-rRNA from tricistronic rRNA transcript (SSU-rRNA, 5.8S rRNA, LSU-rRNA); IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.30.230.10; -; 1. DR HAMAP; MF_00532_A; Ribosomal_S9_A; 1. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR000754; Ribosomal_S9. DR InterPro; IPR019958; Ribosomal_S9_archaeal. DR InterPro; IPR020574; Ribosomal_S9_CS. DR PANTHER; PTHR21569; PTHR21569; 1. DR Pfam; PF00380; Ribosomal_S9; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR TIGRFAMs; TIGR03627; uS9_arch; 1. DR PROSITE; PS00360; RIBOSOMAL_S9; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein. FT CHAIN 1 136 30S ribosomal protein S9. FT /FTId=PRO_0000111465. SQ SEQUENCE 136 AA; 15246 MW; 8AC2A9A7E67994C4 CRC64; MGKIVITVGK RKRAIARAVA REGKGRIRIN KIPIELIEPK YKRMKLMEPI LLAGEEVISQ MDIDVTVKGG GVMGQMDAAR TAIGKAIVEF TGSKELRDKF LAYDRTLLVS DARRTEPHKP SRSTKGPRAK RQKSYR // ID RS4_METJA Reviewed; 187 AA. AC P54020; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=30S ribosomal protein S4 {ECO:0000255|HAMAP-Rule:MF_01306}; GN Name=rps4 {ECO:0000255|HAMAP-Rule:MF_01306}; OrderedLocusNames=MJ0190; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the body of CC the 30S subunit. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- FUNCTION: With S5 and S12 plays an important role in translational CC accuracy. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. Contacts protein S5. CC The interaction surface between S4 and S5 is involved in control CC of translational fidelity. {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Belongs to the ribosomal protein S4P family. CC {ECO:0000255|HAMAP-Rule:MF_01306}. CC -!- SIMILARITY: Contains 1 S4 RNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98170.1; -; Genomic_DNA. DR PIR; G64323; G64323. DR ProteinModelPortal; P54020; -. DR SMR; P54020; 102-146. DR STRING; 243232.MJ_0190; -. DR EnsemblBacteria; AAB98170; AAB98170; MJ_0190. DR KEGG; mja:MJ_0190; -. DR eggNOG; arCOG04239; Archaea. DR eggNOG; COG0522; LUCA. DR InParanoid; P54020; -. DR KO; K02986; -. DR OMA; TIVYRKG; -. DR PhylomeDB; P54020; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015935; C:small ribosomal subunit; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0045903; P:positive regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0006412; P:translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.10.290.10; -; 1. DR HAMAP; MF_01306_A; Ribosomal_S4_A; 1. DR InterPro; IPR022801; Ribosomal_S4/S9. DR InterPro; IPR005710; Ribosomal_S4/S9_euk/arc. DR InterPro; IPR001912; Ribosomal_S4/S9_N. DR InterPro; IPR022802; Ribosomal_S4_arc. DR InterPro; IPR018079; Ribosomal_S4_CS. DR InterPro; IPR002942; S4_RNA-bd. DR PANTHER; PTHR11831; PTHR11831; 1. DR Pfam; PF00163; Ribosomal_S4; 1. DR Pfam; PF01479; S4; 1. DR SMART; SM01390; Ribosomal_S4; 1. DR SMART; SM00363; S4; 1. DR TIGRFAMs; TIGR01018; uS4_arch; 1. DR PROSITE; PS00632; RIBOSOMAL_S4; 1. DR PROSITE; PS50889; S4; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 187 30S ribosomal protein S4. FT /FTId=PRO_0000132508. FT DOMAIN 105 174 S4 RNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_01306}. SQ SEQUENCE 187 AA; 22050 MW; 7D4C51389D5C8A12 CRC64; MGDPRRRFKK TYETPNHPWI KERIEREKEL CRKYGLRRKR EVWKAETILR KYRRQARRLI SDRTEQGAKE AVQLFNVLKK YGILKIENPT LDDVLSLTVE DILERRLQTL VFRKGLARTP RQARQLIVHG HIAVNGRVVT APSYMVTVEE EDKISYAKNS PFNDDNHPER AKIVGLVAEE TQTQETE // ID RS7_METJA Reviewed; 191 AA. AC P54063; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=30S ribosomal protein S7 {ECO:0000255|HAMAP-Rule:MF_00480}; GN Name=rps7 {ECO:0000255|HAMAP-Rule:MF_00480}; OrderedLocusNames=MJ1047; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: One of the primary rRNA binding proteins, it binds CC directly to 16S rRNA where it nucleates assembly of the head CC domain of the 30S subunit. Is located at the subunit interface CC close to the decoding center. {ECO:0000255|HAMAP-Rule:MF_00480}. CC -!- SUBUNIT: Part of the 30S ribosomal subunit. {ECO:0000255|HAMAP- CC Rule:MF_00480}. CC -!- SIMILARITY: Belongs to the ribosomal protein S7P family. CC {ECO:0000255|HAMAP-Rule:MF_00480}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99051.1; -; Genomic_DNA. DR PIR; F64430; F64430. DR ProteinModelPortal; P54063; -. DR SMR; P54063; 6-191. DR STRING; 243232.MJ_1047; -. DR EnsemblBacteria; AAB99051; AAB99051; MJ_1047. DR KEGG; mja:MJ_1047; -. DR eggNOG; arCOG04254; Archaea. DR eggNOG; COG0049; LUCA. DR InParanoid; P54063; -. DR KO; K02992; -. DR OMA; KMNIVER; -. DR PhylomeDB; P54063; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0022627; C:cytosolic small ribosomal subunit; IBA:GO_Central. DR GO; GO:0003729; F:mRNA binding; IBA:GO_Central. DR GO; GO:0019843; F:rRNA binding; IBA:GO_Central. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0000028; P:ribosomal small subunit assembly; IBA:GO_Central. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 1.10.455.10; -; 1. DR HAMAP; MF_00480_A; Ribosomal_S7_A; 1. DR InterPro; IPR000235; Ribosomal_S5/S7. DR InterPro; IPR005716; Ribosomal_S5/S7_euk/arc. DR InterPro; IPR026018; Ribosomal_S7_arc. DR InterPro; IPR020606; Ribosomal_S7_CS. DR InterPro; IPR023798; Ribosomal_S7_dom. DR PANTHER; PTHR11205; PTHR11205; 1. DR Pfam; PF00177; Ribosomal_S7; 1. DR PIRSF; PIRSF002122; RPS7p_RPS7a_RPS5e_RPS7o; 1. DR SUPFAM; SSF47973; SSF47973; 1. DR TIGRFAMs; TIGR01028; uS7_euk_arch; 1. DR PROSITE; PS00052; RIBOSOMAL_S7; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Ribonucleoprotein; KW Ribosomal protein; RNA-binding; rRNA-binding. FT CHAIN 1 191 30S ribosomal protein S7. FT /FTId=PRO_0000124399. SQ SEQUENCE 191 AA; 21760 MW; 98A03F368921FD97 CRC64; MELDEIKVFG RWSTKDVVVK DPGLRNYINL TPIYVPHTAG RYTKRQFEKA KMNIVERLVN KVMRREENTG KKLKALKIVE NAFEIIEKRT KQNPIQVLVD AIENAGPRED TTRISYGGIV YLQSVDCSSL RRIDVALRNI ALGAYMAAHK SKKPIEEALA EEIIAAARGD MQKSYAVRKK EETERVAQSA R // ID RSMA_METJA Reviewed; 275 AA. AC Q58435; DT 13-DEC-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 103. DE RecName: Full=Probable ribosomal RNA small subunit methyltransferase A {ECO:0000255|HAMAP-Rule:MF_00607}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethyladenosine transferase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=16S rRNA dimethylase {ECO:0000255|HAMAP-Rule:MF_00607}; DE AltName: Full=S-adenosylmethionine-6-N',N'-adenosyl(rRNA) dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00607}; GN Name=rsmA {ECO:0000255|HAMAP-Rule:MF_00607}; GN Synonyms=ksgA {ECO:0000255|HAMAP-Rule:MF_00607}; GN OrderedLocusNames=MJ1029; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS), AND FUNCTION. RX PubMed=19520088; DOI=10.1016/j.jmb.2009.06.015; RA Pulicherla N., Pogorzala L.A., Xu Z., O'Farrell H.C., Musayev F.N., RA Scarsdale J.N., Sia E.A., Culver G.M., Rife J.P.; RT "Structural and functional divergence within the Dim1/KsgA family of RT rRNA methyltransferases."; RL J. Mol. Biol. 391:884-893(2009). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEXES WITH AMP; RP S-ADENOSYL-L-HOMOCYSTEINE; S-ADENOSYL-L-METHIONINE AND ADENOSINE, AND RP FUNCTION. RX PubMed=20163168; DOI=10.1021/bi901875x; RA O'Farrell H.C., Musayev F.N., Scarsdale J.N., Rife J.P.; RT "Binding of adenosine-based ligands to the MjDim1 rRNA RT methyltransferase: implications for reaction mechanism and drug RT design."; RL Biochemistry 49:2697-2704(2010). CC -!- FUNCTION: Specifically dimethylates two adjacent adenosines in the CC loop of a conserved hairpin near the 3'-end of 16S rRNA in the 30S CC particle. May play a critical role in biogenesis of 30S subunits. CC {ECO:0000255|HAMAP-Rule:MF_00607, ECO:0000269|PubMed:19520088, CC ECO:0000269|PubMed:20163168}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00607}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. rRNA adenine N(6)-methyltransferase CC family. RsmA subfamily. {ECO:0000255|HAMAP-Rule:MF_00607}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99033.1; -; Genomic_DNA. DR PIR; D64428; D64428. DR PDB; 3FYC; X-ray; 2.15 A; A/B=10-272. DR PDB; 3FYD; X-ray; 1.75 A; A=10-272. DR PDB; 3GRR; X-ray; 1.80 A; A=1-275. DR PDB; 3GRU; X-ray; 1.60 A; A=1-275. DR PDB; 3GRV; X-ray; 1.90 A; A=1-275. DR PDB; 3GRY; X-ray; 2.20 A; A=1-275. DR PDBsum; 3FYC; -. DR PDBsum; 3FYD; -. DR PDBsum; 3GRR; -. DR PDBsum; 3GRU; -. DR PDBsum; 3GRV; -. DR PDBsum; 3GRY; -. DR ProteinModelPortal; Q58435; -. DR STRING; 243232.MJ_1029; -. DR EnsemblBacteria; AAB99033; AAB99033; MJ_1029. DR KEGG; mja:MJ_1029; -. DR eggNOG; arCOG04131; Archaea. DR eggNOG; COG0030; LUCA. DR InParanoid; Q58435; -. DR KO; K02528; -. DR OMA; AQKKPFG; -. DR PhylomeDB; Q58435; -. DR EvolutionaryTrace; Q58435; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0000179; F:rRNA (adenine-N6,N6-)-dimethyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00607; 16SrRNA_methyltr_A; 1. DR InterPro; IPR001737; KsgA/Erm. DR InterPro; IPR020596; rRNA_Ade_Mease_Trfase_CS. DR InterPro; IPR020598; rRNA_Ade_methylase_Trfase_N. DR InterPro; IPR011530; rRNA_adenine_dimethylase. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR11727; PTHR11727; 1. DR Pfam; PF00398; RrnaAD; 1. DR SMART; SM00650; rADc; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00755; ksgA; 1. DR PROSITE; PS01131; RRNA_A_DIMETH; 1. DR PROSITE; PS51689; SAM_RNA_A_N6_MT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; RNA-binding; rRNA processing; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 275 Probable ribosomal RNA small subunit FT methyltransferase A. FT /FTId=PRO_0000101656. FT BINDING 13 13 S-adenosyl-L-methionine; via amide FT nitrogen. FT BINDING 38 38 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00607}. FT BINDING 59 59 S-adenosyl-L-methionine. FT BINDING 84 84 S-adenosyl-L-methionine. FT BINDING 101 101 S-adenosyl-L-methionine. FT HELIX 16 25 {ECO:0000244|PDB:3GRU}. FT STRAND 33 37 {ECO:0000244|PDB:3GRU}. FT HELIX 43 51 {ECO:0000244|PDB:3GRU}. FT STRAND 52 60 {ECO:0000244|PDB:3GRU}. FT HELIX 62 64 {ECO:0000244|PDB:3GRU}. FT HELIX 65 74 {ECO:0000244|PDB:3GRU}. FT STRAND 76 83 {ECO:0000244|PDB:3GRU}. FT TURN 85 87 {ECO:0000244|PDB:3GRU}. FT HELIX 90 92 {ECO:0000244|PDB:3GRU}. FT STRAND 96 101 {ECO:0000244|PDB:3GRU}. FT HELIX 104 106 {ECO:0000244|PDB:3GRU}. FT HELIX 107 117 {ECO:0000244|PDB:3GRU}. FT STRAND 120 127 {ECO:0000244|PDB:3GRU}. FT HELIX 128 135 {ECO:0000244|PDB:3GRU}. FT HELIX 145 151 {ECO:0000244|PDB:3GRU}. FT STRAND 154 162 {ECO:0000244|PDB:3GRU}. FT HELIX 164 166 {ECO:0000244|PDB:3GRU}. FT STRAND 167 169 {ECO:0000244|PDB:3GRU}. FT STRAND 175 182 {ECO:0000244|PDB:3GRU}. FT TURN 185 187 {ECO:0000244|PDB:3GRU}. FT HELIX 192 203 {ECO:0000244|PDB:3GRU}. FT TURN 204 207 {ECO:0000244|PDB:3GRU}. FT HELIX 210 216 {ECO:0000244|PDB:3GRU}. FT HELIX 218 221 {ECO:0000244|PDB:3GRU}. FT HELIX 225 236 {ECO:0000244|PDB:3GRU}. FT HELIX 240 246 {ECO:0000244|PDB:3GRU}. FT HELIX 250 252 {ECO:0000244|PDB:3GRU}. FT HELIX 255 271 {ECO:0000244|PDB:3GRU}. SQ SEQUENCE 275 AA; 31771 MW; BB4DD454BD36427A CRC64; MFKPKKKLGQ CFLIDKNFVN KAVESANLTK DDVVLEIGLG KGILTEELAK NAKKVYVIEI DKSLEPYANK LKELYNNIEI IWGDALKVDL NKLDFNKVVA NLPYQISSPI TFKLIKRGFD LAVLMYQYEF AKRMVAKEGT KDYGRLSVAV QSRADVEIVA KVPPSAFYPK PKVYSAIVKI KPNKGKYHIE NENFFDDFLR AIFQHRNKSV RKALIDSSKE LNYNKDEMKK ILEDFLNTNS EIKNLINEKV FKLSVKDIVN LSNEFYRFLQ NRGRL // ID RUBR2_METJA Reviewed; 55 AA. AC Q58150; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Probable Rubredoxin-2; DE Short=RD 2; GN OrderedLocusNames=MJ0740; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Rubredoxin is a small nonheme, iron protein lacking CC acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions CC as an electron acceptor and may also stabilize the conformation of CC the molecule (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 rubredoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00241}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98734.1; -; Genomic_DNA. DR PIR; D64392; D64392. DR ProteinModelPortal; Q58150; -. DR STRING; 243232.MJ_0740; -. DR EnsemblBacteria; AAB98734; AAB98734; MJ_0740. DR KEGG; mja:MJ_0740; -. DR eggNOG; arCOG04391; Archaea. DR eggNOG; COG1773; LUCA. DR InParanoid; Q58150; -. DR OMA; MARYQCM; -. DR PhylomeDB; Q58150; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR024922; Rubredoxin. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR024935; Rubredoxin_dom. DR Pfam; PF00301; Rubredoxin; 1. DR PIRSF; PIRSF000071; Rubredoxin; 1. DR PRINTS; PR00163; RUBREDOXIN. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Iron; Metal-binding; KW Reference proteome; Transport. FT CHAIN 1 55 Probable Rubredoxin-2. FT /FTId=PRO_0000135059. FT DOMAIN 4 54 Rubredoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 9 9 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 11 11 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 41 41 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 44 44 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. SQ SEQUENCE 55 AA; 6331 MW; 9A0DF94A976661D7 CRC64; MIEMARYQCM CGWVYDEDKG EPSQNIPPGT KFEDLPDTFR CPQCGLGKNA FRKID // ID RTCA_METJA Reviewed; 338 AA. AC Q60335; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-MAR-2016, entry version 94. DE RecName: Full=RNA 3'-terminal phosphate cyclase; DE Short=RNA cyclase; DE Short=RNA-3'-phosphate cyclase; DE EC=6.5.1.4; GN Name=rtcA; OrderedLocusNames=MJ0025; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the conversion of 3'-phosphate to a 2',3'- CC cyclic phosphodiester at the end of RNA. The mechanism of action CC of the enzyme occurs in 3 steps: (A) adenylation of the enzyme by CC ATP; (B) transfer of adenylate to an RNA-N3'P to produce RNA- CC N3'PP5'A; (C) and attack of the adjacent 2'-hydroxyl on the 3'- CC phosphorus in the diester linkage to produce the cyclic end CC product. The biological role of this enzyme is unknown but it is CC likely to function in some aspects of cellular RNA processing (By CC similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + RNA 3'-terminal-phosphate = AMP + CC diphosphate + RNA terminal-2',3'-cyclic-phosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the RNA 3'-terminal cyclase family. Type 1 CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98006.1; -; Genomic_DNA. DR PIR; A64303; A64303. DR ProteinModelPortal; Q60335; -. DR STRING; 243232.MJ_0025; -. DR EnsemblBacteria; AAB98006; AAB98006; MJ_0025. DR KEGG; mja:MJ_0025; -. DR eggNOG; arCOG04125; Archaea. DR eggNOG; COG0430; LUCA. DR InParanoid; Q60335; -. DR KO; K01974; -. DR OMA; GGTDVAW; -. DR PhylomeDB; Q60335; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0003963; F:RNA-3'-phosphate cyclase activity; IBA:GO_Central. DR GO; GO:0006396; P:RNA processing; IEA:InterPro. DR Gene3D; 3.30.360.20; -; 1. DR Gene3D; 3.65.10.20; -; 2. DR HAMAP; MF_00200; RTC; 1. DR InterPro; IPR013791; RNA3'-term_phos_cycl_insert. DR InterPro; IPR023797; RNA3'_phos_cyclase_dom. DR InterPro; IPR000228; RNA3'_term_phos_cyc. DR InterPro; IPR017770; RNA3'_term_phos_cyc_type_1. DR InterPro; IPR020719; RNA3'_term_phos_cycl-like_CS. DR InterPro; IPR013792; RNA3'P_cycl/enolpyr_Trfase_a/b. DR PANTHER; PTHR11096; PTHR11096; 1. DR PANTHER; PTHR11096:SF0; PTHR11096:SF0; 1. DR Pfam; PF01137; RTC; 1. DR Pfam; PF05189; RTC_insert; 1. DR PIRSF; PIRSF005378; RNA3'_term_phos_cycl_euk; 1. DR SUPFAM; SSF52913; SSF52913; 1. DR SUPFAM; SSF55205; SSF55205; 1. DR TIGRFAMs; TIGR03399; RNA_3prim_cycl; 1. DR PROSITE; PS01287; RTC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 338 RNA 3'-terminal phosphate cyclase. FT /FTId=PRO_0000156426. FT NP_BIND 280 284 ATP. {ECO:0000250}. FT ACT_SITE 304 304 Tele-AMP-histidine intermediate. FT {ECO:0000250}. FT BINDING 102 102 ATP. {ECO:0000250}. SQ SEQUENCE 338 AA; 37229 MW; 4681A2AB120FD6F0 CRC64; MDFIVIDGSY LEGGGQIIRT AVSLSALTQK PVKIINIRKK RKNKGLAPQH VSAVKAVKKL CNAEVFGLNV GSEELTFIPS KLSPKDFTID IGTAGSISLV IQTLLPLSLG INKKFTVKIK GGTDVKRAPP IDYVKNVTLK ILRNFGVLTE LKVLKRGFYP EGGGEVIFEV KPSKIKKFDL IEHSKSNLVE GISYVQNLDE SIARRMRKKA VDLLNKEKLL PNIKIECSKG ISTGAGIVLW NDTLGGSCLG EKGLRAEIVA ERAVNELLKE RESGMALDKY MGDQIIPFLA FGKGIVGVSE ITNHTKTNMW VVKHFLDVDF EIKEYKENNC NGFTIEVV // ID RUBPS_METJA Reviewed; 267 AA. AC Q58018; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 02-NOV-2010, sequence version 3. DT 11-MAY-2016, entry version 99. DE RecName: Full=Putative ribose 1,5-bisphosphate isomerase; DE EC=5.3.1.29; DE AltName: Full=Ribulose 1,5-bisphosphate synthase; DE Short=RuBP synthase; GN OrderedLocusNames=MJ0601; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF N-TERMINUS, FUNCTION IN CO(2) FIXATION WITH RP RUBISCO, COFACTOR, AND SUBUNIT. RX PubMed=15375115; DOI=10.1128/JB.186.19.6360-6366.2004; RA Finn M.W., Tabita F.R.; RT "Modified pathway to synthesize ribulose 1,5-bisphosphate in RT methanogenic archaea."; RL J. Bacteriol. 186:6360-6366(2004). CC -!- FUNCTION: Catalyzes the conversion of ribose 1,5-bisphosphate to CC ribulose 1,5-bisphosphate (RuBP), the CO(2) acceptor and substrate CC for RubisCO. {ECO:0000305}. CC -!- CATALYTIC ACTIVITY: Alpha-D-ribose 1,5-bisphosphate = D-ribulose CC 1,5-bisphosphate. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000305|PubMed:15375115}; CC -!- SUBUNIT: Homohexamer. {ECO:0000269|PubMed:15375115}. CC -!- MISCELLANEOUS: The D-ribose 1,5-bisphosphate used in the reaction CC appears to originate from 5-phospho-alpha-D-ribose 1-diphosphate CC (PRPP), which is converted to D-ribose 1,5-bisphosphate CC nonenzymatically at elevated temperatures in the presence of CC magnesium in a time-dependent fashion. CC -!- MISCELLANEOUS: M.jannaschii was shown to possess RubisCO activity CC but no phosphoribulokinase (PRK) activity (PubMed:12730164). Thus, CC the work done in PubMed:15375115 provided evidence for a CC previously uncharacterized pathway for RuBP synthesis, and so CC identified a novel means to synthesize the CO(2) acceptor and CC substrate for RubisCO in the absence of a detectable kinase, such CC as PRK. CC -!- SIMILARITY: Belongs to the THI4 family. {ECO:0000305}. CC -!- CAUTION: This protein is proposed to have ribose 1,5-bisphosphate CC isomerase activity but the recombinant protein does not seem to be CC active in vitro (PubMed:15375115). In contrast, another protein CC from M.jannaschii likely possesses this activity (MJ0122). CC {ECO:0000305|PubMed:15375115}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98592.1; -; Genomic_DNA. DR PIR; A64375; A64375. DR PDB; 4Y4M; X-ray; 2.71 A; A/B/C/D/E/F/G/H=1-267. DR PDBsum; 4Y4M; -. DR ProteinModelPortal; Q58018; -. DR STRING; 243232.MJ_0601; -. DR EnsemblBacteria; AAB98592; AAB98592; MJ_0601. DR KEGG; mja:MJ_0601; -. DR eggNOG; arCOG00574; Archaea. DR eggNOG; COG1635; LUCA. DR InParanoid; Q58018; -. DR KO; K03146; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0043917; F:ribose 1,5-bisphosphate isomerase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW. DR GO; GO:0019693; P:ribose phosphate metabolic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.50.50.60; -; 1. DR HAMAP; MF_00304; Thi4; 1. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR002922; Thi4_fam. DR InterPro; IPR022828; Thi4_putative. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR00292; TIGR00292; 1. PE 1: Evidence at protein level; KW 3D-structure; Carbohydrate metabolism; Complete proteome; KW Direct protein sequencing; Isomerase; NAD; Reference proteome. FT CHAIN 1 267 Putative ribose 1,5-bisphosphate FT isomerase. FT /FTId=PRO_0000153947. FT NP_BIND 34 62 NAD. {ECO:0000255}. SQ SEQUENCE 267 AA; 28655 MW; 2F359B900C838251 CRC64; MVNLMNIKDI KLNADETKTT KAILKASFDM WLDIVEADVV IVGAGPSGLT CARYLAKEGF KVVVLERHLA FGGGTWGGGM GFPYIVVEEP ADELLREVGI KLIDMGDGYY VADSVEVPAK LAVAAMDAGA KILTGIVVED LILREDGVAG VVINSYAIER AGLHIDPLTI RSKVVVDATG HEASIVNILV KKNKLEADVP GEKSMWAEKG ENALLRNTRE VYPNLFVCGM AANASHGGYR MGAIFGGMYL SGKLCAELIT EKLKNKE // ID RUBR1_METJA Reviewed; 80 AA. AC Q58145; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Probable Rubredoxin-1; DE Short=RD 1; GN OrderedLocusNames=MJ0735; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Rubredoxin is a small nonheme, iron protein lacking CC acid-labile sulfide. Its single Fe, chelated to 4 Cys, functions CC as an electron acceptor and may also stabilize the conformation of CC the molecule (By similarity). {ECO:0000250}. CC -!- COFACTOR: CC Name=Fe(3+); Xref=ChEBI:CHEBI:29034; Evidence={ECO:0000250}; CC Note=Binds 1 Fe(3+) ion per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the rubredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 rubredoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00241}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98730.1; -; Genomic_DNA. DR PIR; G64391; G64391. DR ProteinModelPortal; Q58145; -. DR STRING; 243232.MJ_0735; -. DR EnsemblBacteria; AAB98730; AAB98730; MJ_0735. DR KEGG; mja:MJ_0735; -. DR eggNOG; arCOG04391; Archaea. DR eggNOG; COG1773; LUCA. DR InParanoid; Q58145; -. DR OMA; SKDMFEP; -. DR PhylomeDB; Q58145; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR InterPro; IPR024935; Rubredoxin_dom. DR Pfam; PF00301; Rubredoxin; 1. DR PRINTS; PR00163; RUBREDOXIN. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Iron; Metal-binding; KW Reference proteome; Transport. FT CHAIN 1 80 Probable Rubredoxin-1. FT /FTId=PRO_0000135058. FT DOMAIN 19 72 Rubredoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 24 24 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 27 27 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 57 57 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. FT METAL 60 60 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. SQ SEQUENCE 80 AA; 9297 MW; 27D329FD6B608D09 CRC64; MVELKIACKL DGSCEKPRYR KYKCKVCGWV YDPLKGDPSQ NIPPKTPFEE LPDTWICPVC RGKVGKESFE PLDEWVEFDE // ID SAHH_METJA Reviewed; 415 AA. AC Q58783; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 108. DE RecName: Full=Adenosylhomocysteinase {ECO:0000255|HAMAP-Rule:MF_00563}; DE EC=3.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00563}; DE AltName: Full=S-adenosyl-L-homocysteine hydrolase {ECO:0000255|HAMAP-Rule:MF_00563}; DE Short=AdoHcyase {ECO:0000255|HAMAP-Rule:MF_00563}; GN Name=ahcY {ECO:0000255|HAMAP-Rule:MF_00563}; OrderedLocusNames=MJ1388; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May play a key role in the regulation of the CC intracellular concentration of adenosylhomocysteine. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-homocysteine + H(2)O = L- CC homocysteine + adenosine. {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- COFACTOR: CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00563}; CC Note=Binds 1 NAD(+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00563}; CC -!- PATHWAY: Amino-acid biosynthesis; L-homocysteine biosynthesis; L- CC homocysteine from S-adenosyl-L-homocysteine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00563}. CC -!- SIMILARITY: Belongs to the adenosylhomocysteinase family. CC {ECO:0000255|HAMAP-Rule:MF_00563}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99397.1; -; Genomic_DNA. DR PIR; C64473; C64473. DR ProteinModelPortal; Q58783; -. DR STRING; 243232.MJ_1388; -. DR EnsemblBacteria; AAB99397; AAB99397; MJ_1388. DR KEGG; mja:MJ_1388; -. DR eggNOG; arCOG04137; Archaea. DR eggNOG; COG0499; LUCA. DR InParanoid; Q58783; -. DR KO; K01251; -. DR OMA; KYGCRES; -. DR PhylomeDB; Q58783; -. DR UniPathway; UPA00314; UER00076. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004013; F:adenosylhomocysteinase activity; IBA:GO_Central. DR GO; GO:0006730; P:one-carbon metabolic process; IEA:UniProtKB-HAMAP. DR GO; GO:0033353; P:S-adenosylmethionine cycle; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 1. DR HAMAP; MF_00563; AdoHcyase; 1. DR InterPro; IPR000043; Adenosylhomocysteinase. DR InterPro; IPR015878; Ado_hCys_hydrolase_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR020082; S-Ado-L-homoCys_hydrolase_CS. DR PANTHER; PTHR23420; PTHR23420; 1. DR Pfam; PF05221; AdoHcyase; 2. DR Pfam; PF00670; AdoHcyase_NAD; 1. DR PIRSF; PIRSF001109; Ad_hcy_hydrolase; 1. DR SMART; SM00996; AdoHcyase; 1. DR SMART; SM00997; AdoHcyase_NAD; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR00936; ahcY; 1. DR PROSITE; PS00738; ADOHCYASE_1; 1. DR PROSITE; PS00739; ADOHCYASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; NAD; One-carbon metabolism; KW Reference proteome. FT CHAIN 1 415 Adenosylhomocysteinase. FT /FTId=PRO_0000117004. FT NP_BIND 149 151 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT NP_BIND 212 217 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT NP_BIND 291 293 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 123 123 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 148 148 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 178 178 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 182 182 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00563}. FT BINDING 183 183 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 235 235 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. FT BINDING 337 337 NAD. {ECO:0000255|HAMAP-Rule:MF_00563}. SQ SEQUENCE 415 AA; 46607 MW; 16B1456E74D180F5 CRC64; MYEVRDINLW KEGERKIQWA KQHMPVLNLI RERFKEEKPF KGITIGMALH LEAKTAVLAE TLMEGGAEIA ITGCNPLSTQ DDVAAACAKK GMHVYAWRGE TVEEYYENLN KVLDHKPDIV IDDGCDLIFL LHTKRTELLD NIMGGCEETT TGIIRLKAME KEGALKFPVM DVNDAYTKHL FDNRYGTGQS ALDGILRATN LLIAGKTVVV AGYGWCGRGV AMRAKGLGAE VVVTEVNPIR ALEARMDGFR VMKMEKAAEI GDIFITTTGC KDVIRKEHIL KMRNGAILAN AGHFDNEINK KHLEELAKSI KEVRNCVTEY DLGNKKIYLL GEGRLVNLAC ADGHPCEVMD MSFANQALAA EYILKNHEKL EPRVYNIPYE QDLMIASLKL KAMGIEIDEL TKEQKKYLED WREGT // ID SECE_METJA Reviewed; 74 AA. AC Q57817; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 116. DE RecName: Full=Protein translocase subunit SecE {ECO:0000255|HAMAP-Rule:MF_00422}; DE AltName: Full=Protein transport protein Sec61 gamma subunit homolog {ECO:0000255|HAMAP-Rule:MF_00422}; GN Name=secE {ECO:0000255|HAMAP-Rule:MF_00422}; OrderedLocusNames=MJ0371; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 11-66 IN COMPLEX WITH SECY RP AND SECG. RX PubMed=14661030; DOI=10.1038/nature02218; RA Van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., RA Hartmann E., Harrison S.C., Rapoport T.A.; RT "X-ray structure of a protein-conducting channel."; RL Nature 427:36-44(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002; RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.; RT "The plug domain of the SecY protein stabilizes the closed state of RT the translocation channel and maintains a membrane seal."; RL Mol. Cell 26:511-521(2007). RN [4] RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 2-433 DOCKED ONTO RP THE E.COLI RIBOSOME. RX PubMed=18158904; DOI=10.1016/j.molcel.2007.10.034; RA Menetret J.F., Schaletzky J., Clemons W.M. Jr., Osborne A.R., RA Skanland S.S., Denison C., Gygi S.P., Kirkpatrick D.S., Park E., RA Ludtke S.J., Rapoport T.A., Akey C.W.; RT "Ribosome binding of a single copy of the SecY complex: implications RT for protein translocation."; RL Mol. Cell 28:1083-1092(2007). RN [5] RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 3-67 DOCKED ONTO RP DOG RIBOSOMES. RX PubMed=18611385; DOI=10.1016/j.str.2008.05.003; RA Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., RA Rapoport T.A., Akey C.W.; RT "Single copies of Sec61 and TRAP associate with a nontranslating RT mammalian ribosome."; RL Structure 16:1126-1137(2008). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY OF 28-67 DOCKED ONTO E.COLI RP RIBOSOMES. RX PubMed=19913480; DOI=10.1016/j.str.2009.09.010; RA Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.; RT "Regulation of the protein-conducting channel by a bound ribosome."; RL Structure 17:1453-1464(2009). CC -!- FUNCTION: Essential subunit of the protein translocation channel CC SecYEG. Clamps together the 2 halves of SecY. May contact the CC channel plug during translocation. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma CC (SecE) subunits. The heterotrimers can form oligomers, although 1 CC heterotrimer is thought to be able to translocate proteins. CC Interacts with the ribosome. May interact with SecDF, and other CC proteins may be involved. {ECO:0000269|PubMed:14661030}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. CC -!- SIMILARITY: Belongs to the SecE/SEC61-gamma family. CC {ECO:0000255|HAMAP-Rule:MF_00422}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98360.1; -; Genomic_DNA. DR PIR; C64346; C64346. DR PDB; 1RH5; X-ray; 3.20 A; B=1-74. DR PDB; 1RHZ; X-ray; 3.50 A; B=1-74. DR PDB; 2YXQ; X-ray; 3.50 A; B=1-74. DR PDB; 2YXR; X-ray; 3.60 A; B=1-74. DR PDB; 3BO0; EM; 9.60 A; B=28-67. DR PDB; 3BO1; EM; 9.60 A; B=28-67. DR PDB; 3DKN; EM; 8.70 A; B=3-67. DR PDB; 4V4N; EM; 9.00 A; A7=1-67. DR PDB; 4V7I; EM; -; B=28-67. DR PDBsum; 1RH5; -. DR PDBsum; 1RHZ; -. DR PDBsum; 2YXQ; -. DR PDBsum; 2YXR; -. DR PDBsum; 3BO0; -. DR PDBsum; 3BO1; -. DR PDBsum; 3DKN; -. DR PDBsum; 4V4N; -. DR PDBsum; 4V7I; -. DR ProteinModelPortal; Q57817; -. DR SMR; Q57817; 3-67. DR IntAct; Q57817; 2. DR MINT; MINT-8378567; -. DR STRING; 243232.MJ_0371; -. DR EnsemblBacteria; AAB98360; AAB98360; MJ_0371. DR KEGG; mja:MJ_0371; -. DR eggNOG; arCOG02204; Archaea. DR eggNOG; COG2443; LUCA. DR InParanoid; Q57817; -. DR KO; K07342; -. DR OMA; VLMISRK; -. DR EvolutionaryTrace; Q57817; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro. DR Gene3D; 1.20.5.820; -; 1. DR HAMAP; MF_00422; SecE; 1. DR InterPro; IPR023391; Prot_translocase_SecE_dom. DR InterPro; IPR022943; SecE. DR InterPro; IPR008158; Translocase_Sec61-g. DR SUPFAM; SSF103456; SSF103456; 1. DR TIGRFAMs; TIGR00327; secE_euk_arch; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 74 Protein translocase subunit SecE. FT /FTId=PRO_0000104219. FT TOPO_DOM 1 36 Cytoplasmic. FT TRANSMEM 37 62 Helical. FT TOPO_DOM 63 74 Extracellular. FT HELIX 14 24 {ECO:0000244|PDB:1RH5}. FT STRAND 25 27 {ECO:0000244|PDB:1RH5}. FT HELIX 31 66 {ECO:0000244|PDB:1RH5}. SQ SEQUENCE 74 AA; 8438 MW; 10474AE938CC0ECD CRC64; MKTDFNQKIE QLKEFIEECR RVWLVLKKPT KDEYLAVAKV TALGISLLGI IGYIIHVPAT YIKGILKPPT TPRV // ID SECF_METJA Reviewed; 282 AA. AC Q58650; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Protein-export membrane protein SecF {ECO:0000255|HAMAP-Rule:MF_01464}; GN Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=MJ1253; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in protein export. {ECO:0000255|HAMAP- CC Rule:MF_01464}. CC -!- SUBUNIT: Part of the protein translocation apparatus. Forms a CC complex with SecD. {ECO:0000255|HAMAP-Rule:MF_01464}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01464}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99256.1; -; Genomic_DNA. DR PIR; D64456; D64456. DR ProteinModelPortal; Q58650; -. DR STRING; 243232.MJ_1253; -. DR EnsemblBacteria; AAB99256; AAB99256; MJ_1253. DR KEGG; mja:MJ_1253; -. DR eggNOG; arCOG03054; Archaea. DR eggNOG; COG0341; LUCA. DR InParanoid; Q58650; -. DR KO; K03074; -. DR OMA; YAIFRTP; -. DR PhylomeDB; Q58650; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR HAMAP; MF_01464_A; SecF_A; 1. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR InterPro; IPR024921; SecF_arc. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF02355; SecD_SecF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 282 Protein-export membrane protein SecF. FT /FTId=PRO_0000095991. FT TRANSMEM 9 29 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 120 140 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 149 169 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 174 194 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 214 234 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. FT TRANSMEM 236 256 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01464}. SQ SEQUENCE 282 AA; 31029 MW; D2AC5859AEFC1079 CRC64; MIKDYKVSIA IPIALLILSI LLIGFKGIPK SIDITGGTEI TIKVNENMDI TPLKESLNGI AEVKKLESAD GYYIVIRCKN EDVDIVKQKI KEFFHVDSLD KLNYSEKTIG ATLSSKFFEE GFKAVGFAFM FMAIVVYLYF RNPVPSGAII LSALSDIIMA LGAMSLLGIE LSSATIAALL MVIGYSVDSD ILLTTRVLKR LTKSFDETVK EAMKTGLTMT LTTITAMLIL LIVVKLFIPV ADILANIATV LILALIADII NTWLLNAGIL KYYITEYRAK KI // ID SELB_METJA Reviewed; 469 AA. AC Q57918; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Selenocysteine-specific elongation factor; DE AltName: Full=SelB translation factor; GN Name=selB; OrderedLocusNames=MJ0495; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=10860743; DOI=10.1006/jmbi.2000.3756; RA Rother M., Wilting R., Commans S., Boeck A.; RT "Identification and characterisation of the selenocysteine-specific RT translation factor SelB from the archaeon Methanococcus jannaschii."; RL J. Mol. Biol. 299:351-358(2000). CC -!- FUNCTION: Translation factor necessary for the incorporation of CC selenocysteine into proteins. It probably replaces EF-Tu for the CC insertion of selenocysteine directed by the UGA codon. SelB binds CC GTP and GDP. {ECO:0000269|PubMed:10860743}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase CC superfamily. Classic translation factor GTPase family. SelB CC subfamily. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC -!- SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01059}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98485.1; -; Genomic_DNA. DR PIR; G64361; G64361. DR ProteinModelPortal; Q57918; -. DR SMR; Q57918; 5-469. DR STRING; 243232.MJ_0495; -. DR EnsemblBacteria; AAB98485; AAB98485; MJ_0495. DR KEGG; mja:MJ_0495; -. DR eggNOG; arCOG01564; Archaea. DR eggNOG; COG3276; LUCA. DR InParanoid; Q57918; -. DR KO; K03833; -. DR OMA; FGHIDHG; -. DR PhylomeDB; Q57918; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro. DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro. DR GO; GO:0006412; P:translation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR000795; TF_GTP-bd_dom. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR InterPro; IPR004535; Transl_elong_SelB. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR PRINTS; PR00315; ELONGATNFCT. DR SUPFAM; SSF50447; SSF50447; 2. DR SUPFAM; SSF50465; SSF50465; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00475; selB; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51722; G_TR_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; GTP-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 469 Selenocysteine-specific elongation FT factor. FT /FTId=PRO_0000091477. FT DOMAIN 7 181 tr-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT NP_BIND 16 23 GTP. {ECO:0000250}. FT NP_BIND 69 73 GTP. {ECO:0000250}. FT NP_BIND 123 126 GTP. {ECO:0000250}. FT REGION 16 23 G1. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 48 52 G2. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 69 72 G3. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 123 126 G4. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. FT REGION 159 161 G5. {ECO:0000255|PROSITE- FT ProRule:PRU01059}. SQ SEQUENCE 469 AA; 51849 MW; F3C1863CAAF04A92 CRC64; MVISMEMKNV NVGLFGHIDH GKTQLAKQLT EIASTSALDK PKESQKRGIT IDLGFSSFTL DRYRITLVDA PGHSELIRTA IGAGNIIDAA LLVVDAKEGP KTQTGEHLLV LDLLNIPTIV VINKIDIAND EEIKRTEMFM KQILNSTINL KNSKIIKISA KTGEGIGELK KELKNLLDSL DIKRDINSYL KMPIDHAFKI KGVGTVVTGT IHKGKVEVGD NLRILPINHE VKVKSIQCFK QDVSIAYAGD RVGMALMGVE PESLFRGCIL TSEDTKLKVV DKFIAKVKIL ELFKYNLAPK MKVHINIGLL TVPATIIPYK IEKINDKEEP IILEEIKGGD SCYCIFKLEE RVVVDEGDKI LIMRLDLPPT TLRICGFGEV IDFGEVEVKK IVVKEGKVVK KKDKIYIEGL ASSKTAGEKL IGGKVYIPDK NIWGVIKGTF GTKGALIAEF DEEVNGGEKV VLKRVRKWG // ID SALL_METJA Reviewed; 263 AA. AC Q59045; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Chlorinase MJ1651; DE EC=2.5.1.-; GN OrderedLocusNames=MJ1651; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 2-261, AND SUBUNIT. RX PubMed=17910070; DOI=10.1002/prot.21646; RA Rao K.N., Burley S.K., Swaminathan S.; RT "Crystal structure of a conserved protein of unknown function (MJ1651) RT from Methanococcus jannaschii."; RL Proteins 70:572-577(2008). CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:17910070}. CC -!- SIMILARITY: Belongs to the SalL family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99672.1; -; Genomic_DNA. DR PIR; A64506; A64506. DR PDB; 2F4N; X-ray; 2.50 A; A/B/C=2-261. DR PDBsum; 2F4N; -. DR ProteinModelPortal; Q59045; -. DR SMR; Q59045; 9-261. DR STRING; 243232.MJ_1651; -. DR EnsemblBacteria; AAB99672; AAB99672; MJ_1651. DR KEGG; mja:MJ_1651; -. DR eggNOG; arCOG04309; Archaea. DR eggNOG; COG1912; LUCA. DR InParanoid; Q59045; -. DR KO; K09134; -. DR OMA; NIYHGAY; -. DR PhylomeDB; Q59045; -. DR EvolutionaryTrace; Q59045; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.30.90; -; 1. DR InterPro; IPR002747; SAM_Chlor/Fluor. DR InterPro; IPR023227; SAM_OH_AdoTrfase_C. DR InterPro; IPR023228; SAM_OH_AdoTrfase_N. DR Pfam; PF01887; SAM_adeno_trans; 1. DR PIRSF; PIRSF006779; UCP006779; 1. DR SUPFAM; SSF101852; SSF101852; 1. DR SUPFAM; SSF102522; SSF102522; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 263 Chlorinase MJ1651. FT /FTId=PRO_0000107459. FT REGION 80 82 Substrate binding. {ECO:0000250}. FT REGION 135 138 Substrate binding. {ECO:0000250}. FT BINDING 18 18 Substrate. {ECO:0000250}. FT BINDING 138 138 Chloride; via amide nitrogen. FT {ECO:0000250}. FT STRAND 12 18 {ECO:0000244|PDB:2F4N}. FT STRAND 21 24 {ECO:0000244|PDB:2F4N}. FT HELIX 25 38 {ECO:0000244|PDB:2F4N}. FT TURN 39 41 {ECO:0000244|PDB:2F4N}. FT STRAND 45 51 {ECO:0000244|PDB:2F4N}. FT HELIX 58 68 {ECO:0000244|PDB:2F4N}. FT HELIX 69 71 {ECO:0000244|PDB:2F4N}. FT STRAND 76 80 {ECO:0000244|PDB:2F4N}. FT STRAND 91 96 {ECO:0000244|PDB:2F4N}. FT STRAND 101 108 {ECO:0000244|PDB:2F4N}. FT HELIX 111 117 {ECO:0000244|PDB:2F4N}. FT STRAND 119 124 {ECO:0000244|PDB:2F4N}. FT HELIX 139 152 {ECO:0000244|PDB:2F4N}. FT STRAND 172 176 {ECO:0000244|PDB:2F4N}. FT STRAND 178 180 {ECO:0000244|PDB:2F4N}. FT STRAND 182 185 {ECO:0000244|PDB:2F4N}. FT HELIX 188 190 {ECO:0000244|PDB:2F4N}. FT STRAND 199 204 {ECO:0000244|PDB:2F4N}. FT STRAND 206 208 {ECO:0000244|PDB:2F4N}. FT STRAND 210 217 {ECO:0000244|PDB:2F4N}. FT STRAND 219 222 {ECO:0000244|PDB:2F4N}. FT TURN 223 226 {ECO:0000244|PDB:2F4N}. FT STRAND 229 232 {ECO:0000244|PDB:2F4N}. FT STRAND 238 241 {ECO:0000244|PDB:2F4N}. FT HELIX 247 251 {ECO:0000244|PDB:2F4N}. FT STRAND 258 261 {ECO:0000244|PDB:2F4N}. SQ SEQUENCE 263 AA; 30249 MW; 801E2C3E5A66CDD0 CRC64; MGIYMRDDIL DIITLTTDFG TNEGYVGAMK GRILNILKKY NKDAKIIDIS HEIKPFNIYH GAYVLLTAIP YFPPSVHVAV IDPTVGSERK SIVIETKSGY YLVGPDNGLF TYVAEKLGIK RIIKIDEERY KPSSTFHGRD VYAVVGAEIL INNGYDGEEL DEMVKIDETK KRVIHIDRFG NIITNIKKDE VTFKYYDTIM IKIRHKNGIE KIIKCKFVKS YFEEKNNFIC LINSEGFLEI SKFMDNASKL LNVDYLDEIE IIY // ID SECD_METJA Reviewed; 396 AA. AC Q57575; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Protein-export membrane protein SecD {ECO:0000255|HAMAP-Rule:MF_01463}; GN Name=secD {ECO:0000255|HAMAP-Rule:MF_01463}; OrderedLocusNames=MJ0111; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in protein export. {ECO:0000255|HAMAP- CC Rule:MF_01463}. CC -!- SUBUNIT: Part of the protein translocation apparatus. Forms a CC complex with SecF. {ECO:0000255|HAMAP-Rule:MF_01463}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP- CC Rule:MF_01463}; Multi-pass membrane protein {ECO:0000255|HAMAP- CC Rule:MF_01463}. CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily. CC {ECO:0000255|HAMAP-Rule:MF_01463}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98092.1; -; Genomic_DNA. DR PIR; G64313; G64313. DR ProteinModelPortal; Q57575; -. DR STRING; 243232.MJ_0111; -. DR EnsemblBacteria; AAB98092; AAB98092; MJ_0111. DR KEGG; mja:MJ_0111; -. DR eggNOG; arCOG03055; Archaea. DR eggNOG; COG0342; LUCA. DR InParanoid; Q57575; -. DR KO; K03072; -. DR OMA; RMGRAFF; -. DR PhylomeDB; Q57575; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR GO; GO:0015031; P:protein transport; IBA:GO_Central. DR HAMAP; MF_01463_A; SecD_A; 1. DR InterPro; IPR022813; SecD/SecF_arch_bac. DR InterPro; IPR022646; SecD/SecF_CS. DR InterPro; IPR024912; SecD_arc. DR Pfam; PF07549; Sec_GG; 1. DR Pfam; PF02355; SecD_SecF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Protein transport; KW Reference proteome; Translocation; Transmembrane; Transmembrane helix; KW Transport. FT CHAIN 1 396 Protein-export membrane protein SecD. FT /FTId=PRO_0000095990. FT TRANSMEM 12 32 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 243 263 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 272 292 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 298 318 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 338 358 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. FT TRANSMEM 360 380 Helical. {ECO:0000255|HAMAP- FT Rule:MF_01463}. SQ SEQUENCE 396 AA; 43052 MW; 70BA0A62C74E9251 CRC64; MDISKLLKDR KILILIIFVT LSVFLIVFKG LDFGIDLSGG TIIVLKAEKP MSDKEIEATI KIITERLNYN GLNDVVIYPR GNDEIIVEIP KSCDTDRIIK ILKQQGVFVA KIDNITAYTG SDVQNVELPT KIPQGETWAY GVPFELTLEG AKKFAEVAKG KAYHKVELYM DGKLISAPVL SPDLADGKPH PQQVITVGAY PPTKEEIDEA MAIYSALKSG ALPVKLDIEY ISTISPEFGK EFLKGTAIAL LLAFIAVGII VSIRYKQPKI AIPILITCIS EVIIILGFAS LIDWKLDLPS IAGIIAAVGT GVDNQIVITD EALKRGAGKI RASIKRAFFI IFASAATSIA AMLPLFVLGV GMLKGFAITT IAGVLIGIFI TRPAFARIIE EMFKKF // ID SERB_METJA Reviewed; 211 AA. AC Q58989; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 115. DE RecName: Full=Phosphoserine phosphatase; DE Short=PSP; DE Short=PSPase; DE EC=3.1.3.3 {ECO:0000269|PubMed:11438683, ECO:0000269|PubMed:12051918}; DE AltName: Full=O-phosphoserine phosphohydrolase; GN OrderedLocusNames=MJ1594; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) IN COMPLEX WITH BEF3 AND RP MAGNESIUM ION, CATALYTIC ACTIVITY, AND ACTIVE SITE. RX PubMed=11438683; DOI=10.1073/pnas.131213698; RA Cho H., Wang W., Kim R., Yokota H., Damo S., Kim S.H., Wemmer D., RA Kustu S., Yan D.; RT "BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on RT aspartate: structure of a BeF(3)(-) complex with phosphoserine RT phosphatase."; RL Proc. Natl. Acad. Sci. U.S.A. 98:8525-8530(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) IN COMPLEX WITH MAGNESIUM IONS RP AND PHOSPHATE, AND ACTIVE SITE. RX PubMed=11342136; DOI=10.1016/S0969-2126(00)00558-X; RA Wang W., Kim R., Jancarik J., Yokota H., Kim S.-H.; RT "Crystal structure of phosphoserine phosphatase from Methanococcus RT jannaschii, a hyperthermophile, at 1.8 A resolution."; RL Structure 9:65-71(2001). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS) IN COMPLEXES WITH MAGNESIUM; RP SUBSTRATE; PHOSPHATE AND TRANSITION STATE ANALOG, CATALYTIC ACTIVITY, RP BIOPHYSICOCHEMICAL PROPERTIES, ENZYME MECHANISM, COFACTOR, ACTIVE RP SITE, AND MUTAGENESIS OF ASP-11. RX PubMed=12051918; DOI=10.1016/S0022-2836(02)00324-8; RA Wang W., Cho H.S., Kim R., Jancarik J., Yokota H., Nguyen H.H., RA Grigoriev I.V., Wemmer D.E., Kim S.-H.; RT "Structural characterization of the reaction pathway in phosphoserine RT phosphatase: crystallographic 'snapshots' of intermediate states."; RL J. Mol. Biol. 319:421-431(2002). CC -!- CATALYTIC ACTIVITY: O-phospho-L(or D)-serine + H(2)O = L(or D)- CC serine + phosphate. {ECO:0000269|PubMed:11438683, CC ECO:0000269|PubMed:12051918}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000269|PubMed:12051918}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000269|PubMed:12051918}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=620 uM for O-phospho-L-serine (at 70 degrees Celsius and at CC pH 7.5) {ECO:0000269|PubMed:12051918}; CC pH dependence: CC Optimum pH is 7.5. {ECO:0000269|PubMed:12051918}; CC Temperature dependence: CC Optimum temperature is 70 degrees Celsius. CC {ECO:0000269|PubMed:12051918}; CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 3/3. CC -!- SIMILARITY: Belongs to the SerB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99612.1; -; Genomic_DNA. DR PIR; A64499; A64499. DR PDB; 1F5S; X-ray; 1.80 A; A/B=1-211. DR PDB; 1J97; X-ray; 1.50 A; A/B=1-211. DR PDB; 1L7M; X-ray; 1.48 A; A/B=1-211. DR PDB; 1L7N; X-ray; 1.80 A; A/B=1-211. DR PDB; 1L7O; X-ray; 2.20 A; A/B=1-211. DR PDB; 1L7P; X-ray; 1.90 A; A/B=1-211. DR PDBsum; 1F5S; -. DR PDBsum; 1J97; -. DR PDBsum; 1L7M; -. DR PDBsum; 1L7N; -. DR PDBsum; 1L7O; -. DR PDBsum; 1L7P; -. DR ProteinModelPortal; Q58989; -. DR SMR; Q58989; 2-211. DR STRING; 243232.MJ_1594; -. DR EnsemblBacteria; AAB99612; AAB99612; MJ_1594. DR KEGG; mja:MJ_1594; -. DR eggNOG; arCOG01158; Archaea. DR eggNOG; COG0560; LUCA. DR InParanoid; Q58989; -. DR KO; K01079; -. DR OMA; RVAFCAK; -. DR PhylomeDB; Q58989; -. DR BRENDA; 3.1.3.3; 3260. DR UniPathway; UPA00135; UER00198. DR EvolutionaryTrace; Q58989; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0000287; F:magnesium ion binding; IBA:GO_Central. DR GO; GO:0004647; F:phosphoserine phosphatase activity; IBA:GO_Central. DR GO; GO:0016311; P:dephosphorylation; IBA:GOC. DR GO; GO:0006564; P:L-serine biosynthetic process; IBA:GO_Central. DR Gene3D; 1.10.150.210; -; 1. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006383; HAD-SF_hydro_IB_PSP-like. DR InterPro; IPR023190; Pser_Pase_dom_2. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01488; HAD-SF-IB; 1. PE 1: Evidence at protein level; KW 3D-structure; Amino-acid biosynthesis; Complete proteome; Hydrolase; KW Magnesium; Metal-binding; Reference proteome; Serine biosynthesis. FT CHAIN 1 211 Phosphoserine phosphatase. FT /FTId=PRO_0000156891. FT REGION 99 100 Substrate binding. FT {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT ACT_SITE 11 11 Nucleophile. FT {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT ACT_SITE 13 13 Proton donor. FT {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT METAL 11 11 Magnesium. {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT METAL 13 13 Magnesium; via carbonyl oxygen. FT {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT METAL 167 167 Magnesium. {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT BINDING 20 20 Substrate. {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT BINDING 56 56 Substrate. {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT BINDING 144 144 Substrate. {ECO:0000269|PubMed:11342136, FT ECO:0000269|PubMed:11438683, FT ECO:0000269|PubMed:12051918}. FT BINDING 170 170 Substrate. {ECO:0000269|PubMed:12051918}. FT MUTAGEN 11 11 D->N: Loss of activity. FT {ECO:0000269|PubMed:12051918}. FT STRAND 6 11 {ECO:0000244|PDB:1L7M}. FT HELIX 12 16 {ECO:0000244|PDB:1L7M}. FT STRAND 17 19 {ECO:0000244|PDB:1L7M}. FT HELIX 21 28 {ECO:0000244|PDB:1L7M}. FT HELIX 32 43 {ECO:0000244|PDB:1L7M}. FT HELIX 49 58 {ECO:0000244|PDB:1L7M}. FT TURN 59 62 {ECO:0000244|PDB:1L7M}. FT HELIX 65 73 {ECO:0000244|PDB:1L7M}. FT HELIX 81 90 {ECO:0000244|PDB:1L7M}. FT STRAND 93 102 {ECO:0000244|PDB:1L7M}. FT HELIX 103 113 {ECO:0000244|PDB:1L7M}. FT STRAND 116 126 {ECO:0000244|PDB:1L7M}. FT STRAND 129 135 {ECO:0000244|PDB:1L7M}. FT HELIX 143 155 {ECO:0000244|PDB:1L7M}. FT HELIX 159 161 {ECO:0000244|PDB:1L7M}. FT STRAND 162 166 {ECO:0000244|PDB:1L7M}. FT HELIX 169 171 {ECO:0000244|PDB:1L7M}. FT HELIX 172 177 {ECO:0000244|PDB:1L7M}. FT STRAND 179 185 {ECO:0000244|PDB:1L7M}. FT HELIX 188 191 {ECO:0000244|PDB:1L7M}. FT STRAND 195 198 {ECO:0000244|PDB:1L7M}. FT HELIX 203 209 {ECO:0000244|PDB:1L7M}. SQ SEQUENCE 211 AA; 23594 MW; 8573E6D92D883AA6 CRC64; MEKKKKLILF DFDSTLVNNE TIDEIAREAG VEEEVKKITK EAMEGKLNFE QSLRKRVSLL KDLPIEKVEK AIKRITPTEG AEETIKELKN RGYVVAVVSG GFDIAVNKIK EKLGLDYAFA NRLIVKDGKL TGDVEGEVLK ENAKGEILEK IAKIEGINLE DTVAVGDGAN DISMFKKAGL KIAFCAKPIL KEKADICIEK RDLREILKYI K // ID SELD_METJA Reviewed; 349 AA. AC P60819; DT 13-APR-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 11-NOV-2015, entry version 62. DE RecName: Full=Selenide, water dikinase; DE EC=2.7.9.3; DE AltName: Full=Selenium donor protein; DE AltName: Full=Selenophosphate synthase; GN Name=selD; OrderedLocusNames=MJ1591; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-19. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- FUNCTION: Synthesizes selenophosphate from selenide and ATP. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + selenide + H(2)O = AMP + selenophosphate CC + phosphate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the selenophosphate synthase 1 family. CC Class I subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P60819; -. DR InParanoid; P60819; -. DR OMA; SVSQKMN; -. DR PhylomeDB; P60819; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004756; F:selenide, water dikinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_00625; SelD; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR023061; SelD_I. DR InterPro; IPR004536; SPS/SelD. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036407; Selenphspht_syn; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR00476; selD; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Nucleotide-binding; KW Reference proteome; Selenium; Selenocysteine; Transferase. FT CHAIN 1 349 Selenide, water dikinase. FT /FTId=PRO_0000127645. FT NP_BIND 249 255 ATP. {ECO:0000255}. FT ACT_SITE 19 19 {ECO:0000255}. FT SITE 22 22 Important for catalytic activity. FT {ECO:0000250}. FT NON_STD 19 19 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 349 AA; 38040 MW; 93B43EB552563680 CRC64; MERGNEKIKL TELVKLHGUA CKLPSTELEF LVKGIVTDDD LLDKNILVGL GDDASIIKRN GLVIAKTVDV FTPIVDDPYI QGKIAACNST SDIYAMGLLD IVGVLAIVGI PEKLPIHVVR EMLKGFQDFC RENKTTIVGG HTILNPWPLI GGAVTGVGRE EEVLTKAGVK VGDVLILTKP LGTQTAMALS RIPEEFKDLI SITEEERDYI INKAIEIMTT SNRYALKALR KAEERVGDKI ANALTDITGF GILGHSNEMA KNSNVLIEIN LLPCIKRTPE LSRLFGHALL DGYGAETAGG LLISAKEEYK DNLIDELEKA KCYAFEVGRV VKKGEGKAVL SKDVKVIEI // ID SDO1_METJA Reviewed; 240 AA. AC Q58011; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Ribosome maturation protein SDO1 homolog; GN OrderedLocusNames=MJ0592; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the SDO1/SBDS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98586.1; -; Genomic_DNA. DR PIR; H64373; H64373. DR ProteinModelPortal; Q58011; -. DR SMR; Q58011; 7-238. DR STRING; 243232.MJ_0592; -. DR EnsemblBacteria; AAB98586; AAB98586; MJ_0592. DR KEGG; mja:MJ_0592; -. DR eggNOG; arCOG04187; Archaea. DR eggNOG; COG1500; LUCA. DR InParanoid; Q58011; -. DR KO; K14574; -. DR OMA; AVNPQMD; -. DR PhylomeDB; Q58011; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0042256; P:mature ribosome assembly; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 3.30.1250.10; -; 1. DR InterPro; IPR009022; EFG_III-V. DR InterPro; IPR018978; Ribosome_mat_SBDS_C. DR InterPro; IPR018023; Ribosome_mat_SBDS_CS. DR InterPro; IPR019783; Ribosome_mat_SBDS_N. DR InterPro; IPR002140; Sdo1/SBDS. DR Pfam; PF01172; SBDS; 1. DR Pfam; PF09377; SBDS_C; 1. DR SUPFAM; SSF54980; SSF54980; 1. DR SUPFAM; SSF89895; SSF89895; 1. DR TIGRFAMs; TIGR00291; RNA_SBDS; 1. DR PROSITE; PS01267; UPF0023; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 240 Ribosome maturation protein SDO1 homolog. FT /FTId=PRO_0000123769. SQ SEQUENCE 240 AA; 27411 MW; 6517AF7EDBBA2F64 CRC64; MGRDIMVSLE EAVIARYTSH GEKFEILVDP YLAAKLKEGQ NVDFDELLAI EVVFRDASKG EKAPEELLSK IFGTTDVKEI AKKIILKGQV QLTAKQREEI REQKKRQIIT IISRNTINPQ TDTPHPPHRI EKAMEELRIN IDIYKSAEEQ VPEIVKKLKK VLPIRFEKRD IAVKIPAEFA SKAYNALYQF GAVKQEEWQP DGSLIVLIEI PSGIEAEFYA HLNKITKGNV QTKVVKKYSE // ID SECG_METJA Reviewed; 53 AA. AC P60460; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 16-FEB-2004, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Preprotein translocase subunit SecG; DE AltName: Full=Protein transport protein Sec61 subunit beta homolog; GN Name=secG; OrderedLocusNames=MJ0912.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 21-52 IN COMPLEX WITH SECY RP AND SECE. RX PubMed=14661030; DOI=10.1038/nature02218; RA Van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., RA Hartmann E., Harrison S.C., Rapoport T.A.; RT "X-ray structure of a protein-conducting channel."; RL Nature 427:36-44(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS). RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002; RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.; RT "The plug domain of the SecY protein stabilizes the closed state of RT the translocation channel and maintains a membrane seal."; RL Mol. Cell 26:511-521(2007). RN [4] RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 21-52 DOCKED ONTO RP E.COLI RIBOSOMES. RX PubMed=18158904; DOI=10.1016/j.molcel.2007.10.034; RA Menetret J.F., Schaletzky J., Clemons W.M. Jr., Osborne A.R., RA Skanland S.S., Denison C., Gygi S.P., Kirkpatrick D.S., Park E., RA Ludtke S.J., Rapoport T.A., Akey C.W.; RT "Ribosome binding of a single copy of the SecY complex: implications RT for protein translocation."; RL Mol. Cell 28:1083-1092(2007). RN [5] RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 21-52 DOCKED ONTO RP DOG RIBOSOMES. RX PubMed=18611385; DOI=10.1016/j.str.2008.05.003; RA Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., RA Rapoport T.A., Akey C.W.; RT "Single copies of Sec61 and TRAP associate with a nontranslating RT mammalian ribosome."; RL Structure 16:1126-1137(2008). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY DOCKED ONTO E.COLI RIBOSOMES. RX PubMed=19913480; DOI=10.1016/j.str.2009.09.010; RA Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.; RT "Regulation of the protein-conducting channel by a bound ribosome."; RL Structure 17:1453-1464(2009). CC -!- FUNCTION: Subunit of the protein translocation channel SecYEG. The CC function of the beta subunit is unknown, but it may be involved in CC stabilization of the trimeric complex. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma CC (SecE) subunits. The heterotrimers can form oligomers, although 1 CC heterotrimer is thought to be able to translocate proteins. CC Interacts with the ribosome. May interact with SecDF, and other CC proteins may be involved. {ECO:0000269|PubMed:14661030}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein. CC -!- SIMILARITY: Belongs to the SEC61-beta family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PDB; 1RH5; X-ray; 3.20 A; C=1-53. DR PDB; 1RHZ; X-ray; 3.50 A; C=1-53. DR PDB; 2YXQ; X-ray; 3.50 A; C=1-53. DR PDB; 2YXR; X-ray; 3.60 A; C=1-53. DR PDB; 3BO0; EM; 9.60 A; C=21-52. DR PDB; 3BO1; EM; 9.60 A; C=21-52. DR PDB; 3DKN; EM; 8.70 A; C=21-52. DR PDB; 4V4N; EM; 9.00 A; A8=1-52. DR PDB; 4V7I; EM; 9.60 A; AC=1-53. DR PDBsum; 1RH5; -. DR PDBsum; 1RHZ; -. DR PDBsum; 2YXQ; -. DR PDBsum; 2YXR; -. DR PDBsum; 3BO0; -. DR PDBsum; 3BO1; -. DR PDBsum; 3DKN; -. DR PDBsum; 4V4N; -. DR PDBsum; 4V7I; -. DR ProteinModelPortal; P60460; -. DR SMR; P60460; 21-52. DR IntAct; P60460; 2. DR MINT; MINT-8378640; -. DR OMA; GLIRYMD; -. DR EvolutionaryTrace; P60460; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015031; P:protein transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00751; SecG; 1. DR InterPro; IPR023531; Preprot_translocase_SecG. DR InterPro; IPR016482; SecG/Sec61-beta/Sbh. DR Pfam; PF03911; Sec61_beta; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 53 Preprotein translocase subunit SecG. FT /FTId=PRO_0000157268. FT TOPO_DOM 1 30 Cytoplasmic. FT TRANSMEM 31 49 Helical. FT TOPO_DOM 50 53 Extracellular. FT HELIX 30 49 {ECO:0000244|PDB:1RH5}. SQ SEQUENCE 53 AA; 5959 MW; D2D5DD22331BE2AF CRC64; MSKREETGLA TSAGLIRYMD ETFSKIRVKP EHVIGVTVAF VIIEAILTYG RFL // ID SECY_METJA Reviewed; 436 AA. AC Q60175; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 111. DE RecName: Full=Protein translocase subunit SecY; DE AltName: Full=Protein transport protein SEC61 subunit alpha homolog; GN Name=secY; OrderedLocusNames=MJ0478; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF 1-423 IN COMPLEX WITH SECE RP AND SECG. RX PubMed=14661030; DOI=10.1038/nature02218; RA Van den Berg B., Clemons W.M. Jr., Collinson I., Modis Y., RA Hartmann E., Harrison S.C., Rapoport T.A.; RT "X-ray structure of a protein-conducting channel."; RL Nature 427:36-44(2004). RN [3] RP X-RAY CRYSTALLOGRAPHY (3.5 ANGSTROMS) OF PLUG DELETION MUTANTS. RX PubMed=17531810; DOI=10.1016/j.molcel.2007.05.002; RA Li W., Schulman S., Boyd D., Erlandson K., Beckwith J., Rapoport T.A.; RT "The plug domain of the SecY protein stabilizes the closed state of RT the translocation channel and maintains a membrane seal."; RL Mol. Cell 26:511-521(2007). RN [4] RP STRUCTURE BY ELECTRON MICROSCOPY (9.6 ANGSTROMS) OF 2-433 DOCKED ONTO RP E.COLI RIBOSOMES. RX PubMed=18158904; DOI=10.1016/j.molcel.2007.10.034; RA Menetret J.F., Schaletzky J., Clemons W.M. Jr., Osborne A.R., RA Skanland S.S., Denison C., Gygi S.P., Kirkpatrick D.S., Park E., RA Ludtke S.J., Rapoport T.A., Akey C.W.; RT "Ribosome binding of a single copy of the SecY complex: implications RT for protein translocation."; RL Mol. Cell 28:1083-1092(2007). RN [5] RP STRUCTURE BY ELECTRON MICROSCOPY (8.7 ANGSTROMS) OF 2-433 DOCKED ONTO RP DOG RIBOSOMES. RX PubMed=18611385; DOI=10.1016/j.str.2008.05.003; RA Menetret J.F., Hegde R.S., Aguiar M., Gygi S.P., Park E., RA Rapoport T.A., Akey C.W.; RT "Single copies of Sec61 and TRAP associate with a nontranslating RT mammalian ribosome."; RL Structure 16:1126-1137(2008). RN [6] RP STRUCTURE BY ELECTRON MICROSCOPY OF 2-433 DOCKED ONTO E.COLI RP RIBOSOMES. RX PubMed=19913480; DOI=10.1016/j.str.2009.09.010; RA Gumbart J., Trabuco L.G., Schreiner E., Villa E., Schulten K.; RT "Regulation of the protein-conducting channel by a bound ribosome."; RL Structure 17:1453-1464(2009). CC -!- FUNCTION: The central subunit of the protein translocation channel CC SecYEG. Consists of two halves formed by TMs 1-5 and 6-10. These CC two domains form a lateral gate at the front which open onto the CC bilayer between TMs 2 and 7, and are clamped together by SecE at CC the back. The channel is closed by both a pore ring composed of CC hydrophobic SecY resides and a short helix (helix 2A) on the CC extracellular side of the membrane which forms a plug. The plug CC probably moves laterally to allow the channel to open. The ring CC and the pore may move independently. CC -!- SUBUNIT: Component of the Sec protein translocase complex. CC Heterotrimer consisting of alpha (SecY), beta (SecG) and gamma CC (SecE) subunits. The heterotrimers can form oligomers, although 1 CC heterotrimer is thought to be able to translocate proteins. CC Interacts with the ribosome. May interact with SecDF, and other CC proteins may be involved. {ECO:0000269|PubMed:14661030}. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the SecY/SEC61-alpha family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98469.1; -; Genomic_DNA. DR PDB; 1RH5; X-ray; 3.20 A; A=1-436. DR PDB; 1RHZ; X-ray; 3.50 A; A=1-436. DR PDB; 2YXQ; X-ray; 3.50 A; A=1-436. DR PDB; 2YXR; X-ray; 3.60 A; A=1-436. DR PDB; 3BO0; EM; 9.60 A; A=2-433. DR PDB; 3BO1; EM; 9.60 A; A=2-433. DR PDB; 3DKN; EM; 8.70 A; A=2-433. DR PDB; 4V4N; EM; 9.00 A; AX=1-436. DR PDB; 4V7I; EM; -; A=2-433. DR PDBsum; 1RH5; -. DR PDBsum; 1RHZ; -. DR PDBsum; 2YXQ; -. DR PDBsum; 2YXR; -. DR PDBsum; 3BO0; -. DR PDBsum; 3BO1; -. DR PDBsum; 3DKN; -. DR PDBsum; 4V4N; -. DR PDBsum; 4V7I; -. DR ProteinModelPortal; Q60175; -. DR SMR; Q60175; 2-433. DR STRING; 243232.MJ_0478; -. DR EnsemblBacteria; AAB98469; AAB98469; MJ_0478. DR KEGG; mja:MJ_0478; -. DR eggNOG; arCOG04169; Archaea. DR eggNOG; COG0201; LUCA. DR InParanoid; Q60175; -. DR KO; K03076; -. DR OMA; RYIPYVT; -. DR PhylomeDB; Q60175; -. DR EvolutionaryTrace; Q60175; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005622; C:intracellular; IEA:GOC. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-HAMAP. DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.3370.10; -; 1. DR HAMAP; MF_01465; SecY; 1. DR InterPro; IPR026593; SecY. DR InterPro; IPR002208; SecY/SEC61-alpha. DR InterPro; IPR030659; SecY_CS. DR InterPro; IPR023201; SecY_su_dom. DR InterPro; IPR019561; Translocon_Sec61/SecY_plug_dom. DR PANTHER; PTHR10906; PTHR10906; 1. DR Pfam; PF10559; Plug_translocon; 1. DR Pfam; PF00344; SecY; 1. DR PIRSF; PIRSF004557; SecY; 1. DR SUPFAM; SSF103491; SSF103491; 1. DR TIGRFAMs; TIGR00967; 3a0501s007; 1. DR PROSITE; PS00755; SECY_1; 1. DR PROSITE; PS00756; SECY_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Protein transport; Reference proteome; Translocation; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 436 Protein translocase subunit SecY. FT /FTId=PRO_0000131764. FT TOPO_DOM 1 28 Cytoplasmic. FT TRANSMEM 29 46 Helical; Name=Helix 1. FT TOPO_DOM 47 55 Extracellular. FT TRANSMEM 56 88 Discontinuously helical; Name=Helix 2. FT INTRAMEM 56 63 Helical; Name=Helix 2A. FT INTRAMEM 64 69 FT INTRAMEM 70 88 Helical; Name=Helix 2B. FT TOPO_DOM 89 110 Cytoplasmic. FT TRANSMEM 111 129 Helical; Name=Helix 3. FT TOPO_DOM 130 140 Extracellular. FT TRANSMEM 141 161 Helical; Name=Helix 4. FT TOPO_DOM 162 168 Cytoplasmic. FT TRANSMEM 169 191 Helical; Name=Helix 5. FT TOPO_DOM 192 209 Extracellular. FT TRANSMEM 210 227 Helical; Name=Helix 6. FT TOPO_DOM 228 255 Cytoplasmic. FT TRANSMEM 256 277 Helical; Name=Helix 7. FT TOPO_DOM 278 312 Extracellular. FT TRANSMEM 313 331 Helical; Name=Helix 8. FT TOPO_DOM 332 382 Cytoplasmic. FT TRANSMEM 383 397 Helical; Name=Helix 9. FT TOPO_DOM 398 398 Extracellular. FT TRANSMEM 399 412 Helical; Name=Helix 10. FT TOPO_DOM 413 436 Cytoplasmic. FT SITE 75 75 Pore ring. FT SITE 79 79 Pore ring. FT SITE 174 174 Pore ring. FT SITE 179 179 Pore ring. FT SITE 260 260 Pore ring. FT SITE 406 406 Pore ring. FT HELIX 5 10 {ECO:0000244|PDB:1RH5}. FT HELIX 23 40 {ECO:0000244|PDB:1RH5}. FT HELIX 54 57 {ECO:0000244|PDB:2YXQ}. FT HELIX 59 63 {ECO:0000244|PDB:1RH5}. FT TURN 70 75 {ECO:0000244|PDB:1RH5}. FT HELIX 76 91 {ECO:0000244|PDB:1RH5}. FT HELIX 101 128 {ECO:0000244|PDB:1RH5}. FT STRAND 131 133 {ECO:0000244|PDB:1RHZ}. FT HELIX 137 164 {ECO:0000244|PDB:1RH5}. FT STRAND 165 167 {ECO:0000244|PDB:1RH5}. FT HELIX 169 187 {ECO:0000244|PDB:1RH5}. FT HELIX 192 199 {ECO:0000244|PDB:1RH5}. FT TURN 200 203 {ECO:0000244|PDB:1RH5}. FT HELIX 207 209 {ECO:0000244|PDB:1RH5}. FT HELIX 211 226 {ECO:0000244|PDB:1RH5}. FT STRAND 230 234 {ECO:0000244|PDB:1RH5}. FT STRAND 238 240 {ECO:0000244|PDB:1RH5}. FT STRAND 246 251 {ECO:0000244|PDB:1RH5}. FT HELIX 253 255 {ECO:0000244|PDB:1RHZ}. FT HELIX 257 277 {ECO:0000244|PDB:1RH5}. FT STRAND 289 295 {ECO:0000244|PDB:1RH5}. FT HELIX 298 300 {ECO:0000244|PDB:1RH5}. FT STRAND 305 307 {ECO:0000244|PDB:1RH5}. FT HELIX 313 338 {ECO:0000244|PDB:1RH5}. FT HELIX 342 348 {ECO:0000244|PDB:1RH5}. FT STRAND 356 359 {ECO:0000244|PDB:1RHZ}. FT HELIX 363 395 {ECO:0000244|PDB:1RH5}. FT HELIX 402 419 {ECO:0000244|PDB:1RH5}. FT STRAND 427 429 {ECO:0000244|PDB:1RHZ}. SQ SEQUENCE 436 AA; 47444 MW; 3E67747A7B5BDC0A CRC64; MKKLIPILEK IPEVELPVKE ITFKEKLKWT GIVLVLYFIM GCIDVYTAGA QIPAIFEFWQ TITASRIGTL ITLGIGPIVT AGIIMQLLVG SGIIQMDLSI PENRALFQGC QKLLSIIMCF VEAVLFVGAG AFGILTPLLA FLVIIQIAFG SIILIYLDEI VSKYGIGSGI GLFIAAGVSQ TIFVGALGPE GYLWKFLNSL IQGVPNIEYI APIIGTIIVF LMVVYAECMR VEIPLAHGRI KGAVGKYPIK FVYVSNIPVI LAAALFANIQ LWGLALYRMG IPILGHYEGG RAVDGIAYYL STPYGLSSVI SDPIHAIVYM IAMIITCVMF GIFWVETTGL DPKSMAKRIG SLGMAIKGFR KSEKAIEHRL KRYIPPLTVM SSAFVGFLAT IANFIGALGG GTGVLLTVSI VYRMYEQLLR EKVSELHPAI AKLLNK // ID SERA_METJA Reviewed; 524 AA. AC Q58424; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 123. DE RecName: Full=D-3-phosphoglycerate dehydrogenase; DE Short=PGDH; DE EC=1.1.1.95; GN Name=serA; OrderedLocusNames=MJ1018; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 3-phospho-D-glycerate + NAD(+) = 3- CC phosphonooxypyruvate + NADH. CC -!- CATALYTIC ACTIVITY: 2-hydroxyglutarate + NAD(+) = 2-oxoglutarate + CC NADH. CC -!- PATHWAY: Amino-acid biosynthesis; L-serine biosynthesis; L-serine CC from 3-phospho-D-glycerate: step 1/3. CC -!- SIMILARITY: Belongs to the D-isomer specific 2-hydroxyacid CC dehydrogenase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99020.1; -; Genomic_DNA. DR PIR; A64427; A64427. DR ProteinModelPortal; Q58424; -. DR SMR; Q58424; 2-304. DR STRING; 243232.MJ_1018; -. DR EnsemblBacteria; AAB99020; AAB99020; MJ_1018. DR KEGG; mja:MJ_1018; -. DR eggNOG; arCOG01754; Archaea. DR eggNOG; COG0111; LUCA. DR InParanoid; Q58424; -. DR KO; K00058; -. DR OMA; EWKRSKF; -. DR PhylomeDB; Q58424; -. DR UniPathway; UPA00135; UER00196. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0030267; F:glyoxylate reductase (NADP) activity; IBA:GO_Central. DR GO; GO:0016618; F:hydroxypyruvate reductase activity; IBA:GO_Central. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0004617; F:phosphoglycerate dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0006564; P:L-serine biosynthetic process; IEA:UniProtKB-KW. DR Gene3D; 3.30.1330.90; -; 1. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR029009; ASB_dom. DR InterPro; IPR006139; D-isomer_2_OHA_DH_cat_dom. DR InterPro; IPR029753; D-isomer_DH_CS. DR InterPro; IPR029752; D-isomer_DH_CS1. DR InterPro; IPR006140; D-isomer_DH_NAD-bd. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006236; PGDH. DR Pfam; PF00389; 2-Hacid_dh; 1. DR Pfam; PF02826; 2-Hacid_dh_C; 1. DR Pfam; PF01842; ACT; 1. DR SUPFAM; SSF143548; SSF143548; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR TIGRFAMs; TIGR01327; PGDH; 1. DR PROSITE; PS51671; ACT; 1. DR PROSITE; PS00065; D_2_HYDROXYACID_DH_1; 1. DR PROSITE; PS00670; D_2_HYDROXYACID_DH_2; 1. DR PROSITE; PS00671; D_2_HYDROXYACID_DH_3; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; NAD; Oxidoreductase; KW Reference proteome; Serine biosynthesis. FT CHAIN 1 524 D-3-phosphoglycerate dehydrogenase. FT /FTId=PRO_0000076009. FT DOMAIN 452 524 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. FT NP_BIND 149 150 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT NP_BIND 229 231 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT NP_BIND 278 281 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT ACT_SITE 231 231 {ECO:0000250}. FT ACT_SITE 260 260 {ECO:0000250}. FT ACT_SITE 278 278 Proton donor. {ECO:0000250}. FT BINDING 169 169 NAD. {ECO:0000250|UniProtKB:P0A9T0}. FT BINDING 255 255 NAD. {ECO:0000250|UniProtKB:P0A9T0}. SQ SEQUENCE 524 AA; 56924 MW; 5C561BB68C170793 CRC64; MVKILVTDPL HEDAIKILEE VGEVEVATGL TKEELLEKIK DADVLVVRSG TKVTRDVIEK AEKLKVIGRA GVGVDNIDVE AATEKGIIVV NAPDASSISV AELTMGLMLA AARNIPQATA SLKRGEWDRK RFKGIELYGK TLGVIGLGRI GQQVVKRAKA FGMNIIGYDP YIPKEVAESM GVELVDDINE LCKRADFITL HVPLTPKTRH IIGREQIALM KKNAIIVNCA RGGLIDEKAL YEALKEGKIR AAALDVFEEE PPKDNPLLTL DNVIGTPHQG ASTEEAQKAA GTIVAEQIKK VLRGELAENV VNMPNIPQEK LGKLKPYMLL AEMLGNIVMQ VLDGSVNRVE LIYSGELAKE KTDLIKRAFL KGLLSPILLA GINLVNAPII AKNRNINVVE SSTSEEKYGN AIKITAESDK KKFSIVGAII NNKPVILEVD GYEVSFIPEG VLAIIKHIDR PGTIGRVCIT LGDYGINIAS MQVGRKEPGG ESVMLLNLDH TVPEEVIEKI KEIPNIKDVA VINL // ID SEPS_METJA Reviewed; 539 AA. AC Q59054; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 10-FEB-2009, sequence version 2. DT 17-FEB-2016, entry version 97. DE RecName: Full=O-phosphoserine--tRNA(Cys) ligase; DE Short=O-phosphoserine--tRNA ligase; DE EC=6.1.1.27; DE AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase; DE AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase; DE Short=SepRS; GN Name=sepS; OrderedLocusNames=MJ1660; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=15790858; DOI=10.1126/science.1108329; RA Sauerwald A., Zhu W., Major T.A., Roy H., Palioura S., Jahn D., RA Whitman W.B., Yates J.R. III, Ibba M., Soell D.; RT "RNA-dependent cysteine biosynthesis in archaea."; RL Science 307:1969-1972(2005). RN [3] RP INTERACTION WITH SEPCYSS, BIOPHYSICOCHEMICAL PROPERTIES, AND SUBUNIT. RX PubMed=18425141; DOI=10.1038/nsmb.1423; RA Zhang C.-M., Liu C., Slater S., Hou Y.-M.; RT "Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl- RT tRNA(Cys)."; RL Nat. Struct. Mol. Biol. 15:507-514(2008). RN [4] RP X-RAY CRYSTALLOGRAPHY (3.6 ANGSTROMS), AND SUBUNIT. RX PubMed=17351629; DOI=10.1038/nsmb1219; RA Fukunaga R., Yokoyama S.; RT "Structural insights into the first step of RNA-dependent cysteine RT biosynthesis in archaea."; RL Nat. Struct. Mol. Biol. 14:272-279(2007). CC -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to CC tRNA(Cys). {ECO:0000269|PubMed:15790858}. CC -!- CATALYTIC ACTIVITY: ATP + O-phospho-L-serine + tRNA(Cys) = AMP + CC diphosphate + O-phospho-L-seryl-tRNA(Cys). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.7 uM for tRNA(Cys) (at 60 degrees Celsius and pH 6.0) CC {ECO:0000269|PubMed:18425141}; CC -!- SUBUNIT: Homotetramer. Interacts with SepCysS. CC {ECO:0000269|PubMed:17351629, ECO:0000269|PubMed:18425141}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. O-phosphoseryl-tRNA(Cys) synthetase subfamily. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99678.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99678.1; ALT_INIT; Genomic_DNA. DR PIR; B64507; B64507. DR PDB; 2DU7; X-ray; 3.60 A; A/B/C/D=1-539. DR PDBsum; 2DU7; -. DR DIP; DIP-46382N; -. DR STRING; 243232.MJ_1660; -. DR EnsemblBacteria; AAB99678; AAB99678; MJ_1660. DR KEGG; mja:MJ_1660; -. DR eggNOG; arCOG00411; Archaea. DR eggNOG; COG2024; LUCA. DR InParanoid; Q59054; -. DR KO; K07587; -. DR OMA; PVMNLGL; -. DR PhylomeDB; Q59054; -. DR BioCyc; MetaCyc:MONOMER-14996; -. DR EvolutionaryTrace; Q59054; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR HAMAP; MF_01674; Sep_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR005246; O-Pseryl-tRNA(Cys)_ligase. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR Pfam; PF01409; tRNA-synt_2d; 1. DR TIGRFAMs; TIGR00470; sepS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Ligase; Nucleotide-binding; Protein biosynthesis; KW Reference proteome. FT CHAIN 1 539 O-phosphoserine--tRNA(Cys) ligase. FT /FTId=PRO_0000126829. FT REGION 188 190 Substrate binding. {ECO:0000250}. FT REGION 233 235 Substrate binding. {ECO:0000250}. FT REGION 275 276 Substrate binding. {ECO:0000250}. FT BINDING 319 319 Substrate. {ECO:0000250}. FT HELIX 5 9 FT TURN 19 21 FT TURN 31 34 FT STRAND 35 39 FT HELIX 48 61 FT TURN 62 64 FT HELIX 76 82 FT HELIX 87 90 FT HELIX 91 93 FT STRAND 96 98 FT STRAND 106 109 FT STRAND 127 129 FT STRAND 137 140 FT STRAND 144 146 FT STRAND 153 156 FT STRAND 165 169 FT STRAND 173 175 FT STRAND 180 184 FT HELIX 190 198 FT TURN 199 203 FT STRAND 206 216 FT STRAND 224 226 FT STRAND 231 239 FT HELIX 245 256 FT HELIX 257 259 FT TURN 278 280 FT STRAND 282 286 FT STRAND 289 292 FT STRAND 294 303 FT HELIX 305 310 FT STRAND 317 323 FT HELIX 324 331 FT HELIX 338 341 FT STRAND 342 346 FT HELIX 352 356 FT HELIX 368 381 FT STRAND 401 404 FT STRAND 431 433 FT STRAND 446 448 FT STRAND 452 460 FT HELIX 469 485 FT STRAND 499 502 FT STRAND 504 506 FT HELIX 511 517 FT TURN 518 521 SQ SEQUENCE 539 AA; 62153 MW; 301201548E9ADE40 CRC64; MRFDIKKVLE LAEKDFETAW RETRALIKDK HIDNKYPRLK PVYGKPHPVM ETIERLRQAY LRMGFEEMIN PVIVDEMEIY KQFGPEAMAV LDRCFYLAGL PRPDVGLGNE KVEIIKNLGI DIDEEKKERL REVLHLYKKG AIDGDDLVFE IAKALNVSNE MGLKVLETAF PEFKDLKPES TTLTLRSHMT SGWFITLSSL IKKRKLPLKL FSIDRCFRRE QREDRSHLMS YHSASCVVVG EDVSVDDGKV VAEGLLAQFG FTKFKFKPDE KKSKYYTPET QTEVYAYHPK LGEWIEVATF GVYSPIALAK YNIDVPVMNL GLGVERLAMI IYGYEDVRAM VYPQFYEYRL SDRDIAGMIR VDKVPILDEF YNFANELIDI CIANKDKESP CSVEVKREFN FNGERRVIKV EIFENEPNKK LLGPSVLNEV YVYDGNIYGI PPTFEGVKEQ YIPILKKAKE EGVSTNIRYI DGIIYKLVAK IEEALVSNVD EFKFRVPIVR SLSDINLKID ELALKQIMGE NKVIDVRGPV FLNAKVEIK // ID SPEH_METJA Reviewed; 124 AA. AC Q57763; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 14-AUG-2001, sequence version 2. DT 09-DEC-2015, entry version 104. DE RecName: Full=S-adenosylmethionine decarboxylase proenzyme; DE Short=AdoMetDC; DE Short=SAMDC; DE EC=4.1.1.50; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase beta chain; DE Contains: DE RecName: Full=S-adenosylmethionine decarboxylase alpha chain; DE Flags: Precursor; GN Name=speH; OrderedLocusNames=MJ0315; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, SELF-PROCESSING, CLEAVAGE SITE, RP AND MASS SPECTROMETRY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=11073910; DOI=10.1128/JB.182.23.6667-6672.2000; RA Kim A.D., Graham D.E., Seeholzer S.H., Markham G.D.; RT "S-adenosylmethionine decarboxylase from the archaeon Methanococcus RT jannaschii: identification of a novel family of pyruvoyl enzymes."; RL J. Bacteriol. 182:6667-6672(2000). RN [3] RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, RP SCHIFF BASE FORMATION, AND CATALYTIC MECHANISM. RX PubMed=14573607; DOI=10.1074/jbc.M308793200; RA Lu Z.J., Markham G.D.; RT "Catalytic properties of the archaeal S-adenosylmethionine RT decarboxylase from Methanococcus jannaschii."; RL J. Biol. Chem. 279:265-273(2004). CC -!- FUNCTION: Catalyzes the decarboxylation of S-adenosylmethionine to CC S-adenosylmethioninamine (dcAdoMet), the propylamine donor CC required for the synthesis of the polyamines spermine and CC spermidine from the diamine putrescine. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine = S-adenosyl 3- CC (methylthio)propylamine + CO(2). {ECO:0000269|PubMed:11073910, CC ECO:0000269|PubMed:14573607}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000269|PubMed:11073910}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000269|PubMed:11073910}; CC -!- ENZYME REGULATION: Competitively inhibited by methylglyoxal bis- CC guanylhydrazone. Inactivated by treatment with the imine reductant CC NaCNBH(3) only in the presence of substrate. CC {ECO:0000269|PubMed:14573607}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=95 uM for S-adenosyl-L-methionine (at pH 7.5 and 22 degrees CC Celsius) {ECO:0000269|PubMed:14573607}; CC Vmax=37 nmol/min/mg enzyme (at pH 7.5 and 22 degrees Celsius) CC {ECO:0000269|PubMed:14573607}; CC Note=The turnover number increases 30-fold when temperature is CC increased from 22 to 70 degrees Celsius, whereas the Km CC increases 3-fold.; CC pH dependence: CC Optimum pH is 6-8. {ECO:0000269|PubMed:14573607}; CC Temperature dependence: CC Optimum temperature is superior to 90 degrees Celsius. CC Thermostable. Retains full activity after 3 hours at 70 degrees CC Celsius. {ECO:0000269|PubMed:14573607}; CC -!- PATHWAY: Amine and polyamine biosynthesis; S- CC adenosylmethioninamine biosynthesis; S-adenosylmethioninamine from CC S-adenosyl-L-methionine: step 1/1. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged CC as a dimer of alpha/beta heterodimers. CC {ECO:0000269|PubMed:11073910}. CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation CC of the active enzyme involves a self-maturation process in which CC the active site pyruvoyl group is generated from an internal CC serine residue via an autocatalytic post-translational CC modification. Two non-identical subunits are generated from the CC proenzyme in this reaction, and the pyruvate is formed at the N- CC terminus of the alpha chain, which is derived from the carboxyl CC end of the proenzyme. The post-translation cleavage follows an CC unusual pathway, termed non-hydrolytic serinolysis, in which the CC side chain hydroxyl group of the serine supplies its oxygen atom CC to form the C-terminus of the beta chain, while the remainder of CC the serine residue undergoes an oxidative deamination to produce CC ammonia and the pyruvoyl group blocking the N-terminus of the CC alpha chain. {ECO:0000269|PubMed:11073910}. CC -!- MASS SPECTROMETRY: Mass=6793.1; Method=MALDI; Range=1-63; CC Evidence={ECO:0000269|PubMed:11073910}; CC -!- MASS SPECTROMETRY: Mass=6990.2; Method=MALDI; Range=64-124; CC Note=Pyruvoyl group-containing alpha subunit.; CC Evidence={ECO:0000269|PubMed:11073910}; CC -!- SIMILARITY: Belongs to the prokaryotic AdoMetDC family. Type 1 CC subfamily. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98301.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98301.1; ALT_INIT; Genomic_DNA. DR PIR; D64339; D64339. DR ProteinModelPortal; Q57763; -. DR STRING; 243232.MJ_0315; -. DR EnsemblBacteria; AAB98301; AAB98301; MJ_0315. DR KEGG; mja:MJ_0315; -. DR eggNOG; arCOG00279; Archaea. DR eggNOG; COG1586; LUCA. DR InParanoid; Q57763; -. DR KO; K01611; -. DR OMA; FMCGACD; -. DR PhylomeDB; Q57763; -. DR SABIO-RK; Q57763; -. DR UniPathway; UPA00331; UER00451. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004014; F:adenosylmethionine decarboxylase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006557; P:S-adenosylmethioninamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.90.10; -; 1. DR HAMAP; MF_00464; AdoMetDC_1; 1. DR InterPro; IPR003826; AdoMetDC_fam_prok. DR InterPro; IPR016067; S-AdoMet_deCO2ase_core. DR InterPro; IPR017716; S-AdoMet_deCOase_pro-enz. DR Pfam; PF02675; AdoMet_dc; 1. DR SUPFAM; SSF56276; SSF56276; 1. DR TIGRFAMs; TIGR03330; SAM_DCase_Bsu; 1. PE 1: Evidence at protein level; KW Autocatalytic cleavage; Complete proteome; Decarboxylase; Lyase; KW Polyamine biosynthesis; Pyruvate; Reference proteome; KW S-adenosyl-L-methionine; Schiff base; Spermidine biosynthesis; KW Zymogen. FT CHAIN 1 63 S-adenosylmethionine decarboxylase beta FT chain. FT /FTId=PRO_0000030133. FT CHAIN 64 124 S-adenosylmethionine decarboxylase alpha FT chain. FT /FTId=PRO_0000030134. FT ACT_SITE 64 64 Schiff-base intermediate with substrate; FT via pyruvic acid. FT ACT_SITE 69 69 Proton acceptor; for processing activity. FT {ECO:0000250}. FT ACT_SITE 84 84 Proton donor; for catalytic activity. FT {ECO:0000305}. FT SITE 63 64 Cleavage (non-hydrolytic); by autolysis. FT MOD_RES 64 64 Pyruvic acid (Ser); by autocatalysis. SQ SEQUENCE 124 AA; 13792 MW; BC1152CDE080F113 CRC64; MLKYLGKHLI LELWGCDPKA LDDIEGIEKM LVDSVKACGA TLICVRTHKF SPQGATGVAV LAESHIAIHT YPEYGYAALD VFTCGEHTDP YKALEVIREF LKPKSIQIID LKRGLMENGT FELK // ID SOR_METJA Reviewed; 116 AA. AC Q58151; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Putative superoxide reductase; DE Short=SOR; DE EC=1.15.1.2; GN OrderedLocusNames=MJ0741; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Uses electrons from reduced NADP, by way of rubredoxin CC and an oxidoreductase, to catalyze the reduction of superoxide to CC hydrogen peroxide. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Reduced rubredoxin + superoxide + 2 H(+) = CC oxidized rubredoxin + H(2)O(2). {ECO:0000250|UniProtKB:P82385}. CC -!- COFACTOR: CC Name=Fe cation; Xref=ChEBI:CHEBI:24875; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the desulfoferrodoxin family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98735.1; -; Genomic_DNA. DR PIR; E64392; E64392. DR ProteinModelPortal; Q58151; -. DR STRING; 243232.MJ_0741; -. DR EnsemblBacteria; AAB98735; AAB98735; MJ_0741. DR KEGG; mja:MJ_0741; -. DR eggNOG; arCOG02146; Archaea. DR eggNOG; COG2033; LUCA. DR InParanoid; Q58151; -. DR KO; K05919; -. DR OMA; NLHGIWE; -. DR PhylomeDB; Q58151; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR GO; GO:0050605; F:superoxide reductase activity; IEA:UniProtKB-EC. DR InterPro; IPR002742; Desulfoferrodoxin_Fe-bd_dom. DR Pfam; PF01880; Desulfoferrodox; 1. DR SUPFAM; SSF49367; SSF49367; 1. DR TIGRFAMs; TIGR00332; neela_ferrous; 1. PE 3: Inferred from homology; KW Complete proteome; Electron transport; Iron; Metal-binding; KW Oxidoreductase; Reference proteome; Transport. FT CHAIN 1 116 Putative superoxide reductase. FT /FTId=PRO_0000140871. FT METAL 20 20 Iron. {ECO:0000250}. FT METAL 46 46 Iron. {ECO:0000250}. FT METAL 52 52 Iron. {ECO:0000250}. FT METAL 101 101 Iron. {ECO:0000250}. FT METAL 104 104 Iron. {ECO:0000250}. SQ SEQUENCE 116 AA; 13950 MW; 4CF2C76237DE0673 CRC64; MTHYCGINRM KEGTDFEKKH TPFIECKDRV KANDYFEVKI STGIPHPMED NHFIHWIELY MGDLYLARVD FTQFMKPEVK LMVKAPSKEH EKFILRALMR CNLHGVWEYE KEILLE // ID SRP19_METJA Reviewed; 87 AA. AC Q58440; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=Signal recognition particle 19 kDa protein {ECO:0000255|HAMAP-Rule:MF_00305}; DE Short=SRP19 {ECO:0000255|HAMAP-Rule:MF_00305}; GN Name=srp19 {ECO:0000255|HAMAP-Rule:MF_00305}; GN OrderedLocusNames=MJ1034; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds directly to 7S RNA CC and mediates binding of the 54 kDa subunit of the SRP. CC {ECO:0000255|HAMAP-Rule:MF_00305}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. Archaeal CC SRP consists of a 7S RNA molecule of 300 nucleotides and two CC protein subunits: SRP54 and SRP19. {ECO:0000255|HAMAP- CC Rule:MF_00305}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00305}. CC -!- SIMILARITY: Belongs to the SRP19 family. {ECO:0000255|HAMAP- CC Rule:MF_00305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99038.1; -; Genomic_DNA. DR PIR; A64429; A64429. DR PDB; 1L9A; X-ray; 2.90 A; A=1-87. DR PDB; 1LNG; X-ray; 2.30 A; A=1-87. DR PDB; 2V3C; X-ray; 2.50 A; A/B=1-87. DR PDB; 3NDB; X-ray; 3.00 A; A=1-87. DR PDB; 4XCO; X-ray; 2.90 A; A/B=1-87. DR PDBsum; 1L9A; -. DR PDBsum; 1LNG; -. DR PDBsum; 2V3C; -. DR PDBsum; 3NDB; -. DR PDBsum; 4XCO; -. DR ProteinModelPortal; Q58440; -. DR SMR; Q58440; 1-87. DR DIP; DIP-46443N; -. DR STRING; 243232.MJ_1034; -. DR EnsemblBacteria; AAB99038; AAB99038; MJ_1034. DR KEGG; mja:MJ_1034; -. DR eggNOG; arCOG01217; Archaea. DR eggNOG; COG1400; LUCA. DR InParanoid; Q58440; -. DR KO; K03105; -. DR OMA; KAYPKSW; -. DR PhylomeDB; Q58440; -. DR EvolutionaryTrace; Q58440; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW. DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 3.30.56.30; -; 1. DR HAMAP; MF_00305; SRP19; 1. DR InterPro; IPR002778; Signal_recog_particle_SRP19. DR InterPro; IPR022938; SRP19_arc-type. DR PANTHER; PTHR17453; PTHR17453; 1. DR Pfam; PF01922; SRP19; 1. DR SUPFAM; SSF69695; SSF69695; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW Ribonucleoprotein; RNA-binding; Signal recognition particle. FT CHAIN 1 87 Signal recognition particle 19 kDa FT protein. FT /FTId=PRO_0000135217. FT HELIX 5 7 {ECO:0000244|PDB:1LNG}. FT STRAND 9 12 {ECO:0000244|PDB:3NDB}. FT TURN 14 17 {ECO:0000244|PDB:1LNG}. FT TURN 22 24 {ECO:0000244|PDB:1LNG}. FT STRAND 26 28 {ECO:0000244|PDB:1LNG}. FT HELIX 31 40 {ECO:0000244|PDB:1LNG}. FT STRAND 46 48 {ECO:0000244|PDB:1LNG}. FT HELIX 54 56 {ECO:0000244|PDB:1LNG}. FT STRAND 63 65 {ECO:0000244|PDB:1LNG}. FT HELIX 72 83 {ECO:0000244|PDB:1LNG}. SQ SEQUENCE 87 AA; 10352 MW; 0BF272957E69CBE8 CRC64; MIIWPSYIDK KKSRREGRKV PEELAIEKPS LKDIEKALKK LGLEPKIYRD KRYPRQHWEI CGCVEVDYKG NKLQLLKEIC KIIKGKN // ID SMC_METJA Reviewed; 1169 AA. AC Q59037; DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 104. DE RecName: Full=Chromosome partition protein Smc {ECO:0000255|HAMAP-Rule:MF_01894}; GN Name=smc {ECO:0000255|HAMAP-Rule:MF_01894}; OrderedLocusNames=MJ1643; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Required for chromosome condensation and partitioning. CC {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01894}. CC -!- DOMAIN: Contains large globular domains required for ATP CC hydrolysis at each terminus and a third globular domain forming a CC flexible hinge near the middle of the molecule. These domains are CC separated by coiled-coil structures. {ECO:0000255|HAMAP- CC Rule:MF_01894}. CC -!- SIMILARITY: Belongs to the SMC family. {ECO:0000255|HAMAP- CC Rule:MF_01894}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99663.1; -; Genomic_DNA. DR PIR; A64505; A64505. DR ProteinModelPortal; Q59037; -. DR SMR; Q59037; 1026-1168. DR STRING; 243232.MJ_1643; -. DR PRIDE; Q59037; -. DR EnsemblBacteria; AAB99663; AAB99663; MJ_1643. DR KEGG; mja:MJ_1643; -. DR eggNOG; arCOG00371; Archaea. DR eggNOG; COG1196; LUCA. DR InParanoid; Q59037; -. DR KO; K03529; -. DR OMA; AFQTASN; -. DR PhylomeDB; Q59037; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030261; P:chromosome condensation; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-HAMAP. DR GO; GO:0007062; P:sister chromatid cohesion; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR HAMAP; MF_01894; Smc_prok; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR003395; RecF/RecN/SMC_N. DR InterPro; IPR024704; SMC. DR InterPro; IPR010935; SMC_hinge. DR InterPro; IPR011890; SMC_prok. DR Pfam; PF06470; SMC_hinge; 1. DR Pfam; PF02463; SMC_N; 2. DR PIRSF; PIRSF005719; SMC; 1. DR SMART; SM00968; SMC_hinge; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF75553; SSF75553; 1. DR TIGRFAMs; TIGR02169; SMC_prok_A; 1. DR TIGRFAMs; TIGR02168; SMC_prok_B; 1. PE 3: Inferred from homology; KW ATP-binding; Coiled coil; Complete proteome; Cytoplasm; DNA-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 1169 Chromosome partition protein Smc. FT /FTId=PRO_0000119031. FT NP_BIND 32 39 ATP. {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 166 507 {ECO:0000255|HAMAP-Rule:MF_01894}. FT COILED 676 1030 {ECO:0000255|HAMAP-Rule:MF_01894}. SQ SEQUENCE 1169 AA; 136635 MW; B63CCE34E4C03F36 CRC64; MVTLEKIELK NFKSFKKLSL DIPKGFTAIV GPNGSGKSNI VDAILFVLGK TSAKKLRANR FSGLITYHNG KRADFAEVCL YFTNENNAFN VNADKVGILR RIKSSGETDY YLVWKENDKE KRKKMTKHEI IDLFRRLGLL GDNVISQGDL LKIINISPIE RRKIIDEISG IAEFDEKKKK AEEELKKARE LIEMIDIRIS EVENNLKKLK KEKEDAEKYI KLNEELKAAK YALILKKVSY LNVLLENIQN DIKNLEELKN EFLSKVREID VEIENLKLRL NNIINELNEK GNEEVLELHK SIKELEVEIE NDKKVLDSSI NELKKVEVEI ENKKKEIKET QKKIIENRDS IIEKEQQIKE IEEKIKNLNY EKERLKEAIA ESESIIKHLK ESEMEIADEI AKNQNELYRL KKELNDLDNL INRKNFEIEK NNEMIKKLKE ELETVEDVDT KPLYLELENL NVEIEFSKRG IKELEEKKKE LQAKLDELHA EYVKENARIK ALKEMEELSM DRAIREILNA NLPGIIDIVG NLGKTKIEYK TAIEVAAGNR LNHIVVKRMD DAVRAIKYLK ERKLGRATFL PLDRIEGREA YYIDEDGVIG RAIDLVEFDE KYRRVFEYVF GNTVVVENID IAKELAKKYR KVRFVTLDGD VIEPSGAMIG GTFKSKAKIK VDVDLSKLNK IADEIIAIES ELRKIKEEIE RLSKIVKRSS AKKMEIENTL EIIKKNEMRK REIAEKNTIK IKELELKNKD ILEELEELNL KREEILNRIN EIESKINELI ERREKIINEL KEYESDENLK RMNEIEGELK ILEKEKAKLK NEIDKGLTLV KEILIPKIEE LNKKVSELIN KKVILEKNIS FYKESIEKNL SILEEKRKRY EELAKNLKEL TEKKEQLEKE IETLERERRE ILRKVRDIEN RINELMVEKA KYESKLEEEE RKLYLCEKVD VSKELEKKDI EELEIYIGEL ENEIKSLEPV NMRAIEDYNY VAERYKELIE KRKEYERDEK KYLQLMEELE NKKKEVFMEV FNKVAKNFEE VYKEIGGIGK LSLENEKNPF EGGILIDASP RGKKLLSLDA MSGGEKSLTA LAFLFAIQRL NPSPFYVLDE VDAALDVKNV SLIADMIKNA SKDSQFIVIS HREQMVSKAD VVYGVYMENG LSKVVGIRL // ID SPEE_METJA Reviewed; 293 AA. AC Q57761; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Polyamine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198}; DE AltName: Full=Putrescine aminopropyltransferase {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=PAPT {ECO:0000255|HAMAP-Rule:MF_00198}; DE AltName: Full=Spermidine synthase {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=SPDS {ECO:0000255|HAMAP-Rule:MF_00198}; DE Short=SPDSY {ECO:0000255|HAMAP-Rule:MF_00198}; DE EC=2.5.1.16 {ECO:0000255|HAMAP-Rule:MF_00198}; GN Name=speE {ECO:0000255|HAMAP-Rule:MF_00198}; OrderedLocusNames=MJ0313; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the irreversible transfer of a propylamine CC group from the amino donor S-adenosylmethioninamine (decarboxy- CC AdoMet) to putrescine (1,4-diaminobutane) to yield spermidine. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- CATALYTIC ACTIVITY: S-adenosyl 3-(methylthio)propylamine + CC putrescine = 5'-S-methyl-5'-thioadenosine + spermidine. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- PATHWAY: Amine and polyamine biosynthesis; spermidine CC biosynthesis; spermidine from putrescine: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SUBUNIT: Homodimer or homotetramer. {ECO:0000255|HAMAP- CC Rule:MF_00198}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Belongs to the spermidine/spermine synthase family. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC -!- SIMILARITY: Contains 1 PABS (polyamine biosynthesis) domain. CC {ECO:0000255|HAMAP-Rule:MF_00198}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98300.1; -; Genomic_DNA. DR PIR; B64339; B64339. DR ProteinModelPortal; Q57761; -. DR STRING; 243232.MJ_0313; -. DR EnsemblBacteria; AAB98300; AAB98300; MJ_0313. DR KEGG; mja:MJ_0313; -. DR eggNOG; arCOG00050; Archaea. DR eggNOG; COG0421; LUCA. DR InParanoid; Q57761; -. DR KO; K00797; -. DR OMA; YTEPQTE; -. DR PhylomeDB; Q57761; -. DR UniPathway; UPA00248; UER00314. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004766; F:spermidine synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006596; P:polyamine biosynthetic process; IBA:GO_Central. DR GO; GO:0008295; P:spermidine biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00198; Spermidine_synth; 1. DR InterPro; IPR030374; PABS. DR InterPro; IPR030373; PABS_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR001045; Spermi_synthase. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00417; speE; 1. DR PROSITE; PS01330; PABS_1; 1. DR PROSITE; PS51006; PABS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Polyamine biosynthesis; KW Reference proteome; Spermidine biosynthesis; Transferase. FT CHAIN 1 293 Polyamine aminopropyltransferase. FT /FTId=PRO_0000156526. FT DOMAIN 10 244 PABS. {ECO:0000255|HAMAP-Rule:MF_00198}. FT REGION 145 146 S-adenosylmethioninamine binding. FT {ECO:0000255|HAMAP-Rule:MF_00198}. FT REGION 164 166 Polyamine binding. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT ACT_SITE 163 163 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 15 15 Polyamine. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 39 39 S-adenosylmethioninamine. FT {ECO:0000255|HAMAP-Rule:MF_00198}. FT BINDING 70 70 Polyamine. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 94 94 Polyamine. {ECO:0000255|HAMAP- FT Rule:MF_00198}. FT BINDING 114 114 S-adenosylmethioninamine. FT {ECO:0000255|HAMAP-Rule:MF_00198}. FT BINDING 170 170 S-adenosylmethioninamine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00198}. SQ SEQUENCE 293 AA; 33899 MW; 88E4A8C919E5452A CRC64; MNQNNDFKCH IWFTEYHNNN VALSVRVKDI LYREKSGFQE IEIIDTYDFG KALILDNTFQ TTERDEFIYH ELISHIPLFT HPNPRNVLVI GGGDGGTVRE VVKHKSVETV DFVELDEKVI EACKKYMPKL SCEIDNEKVN LIITDGIKYV AETEKKYDVI IVDCPDPVGP AKGLFEKEFY KNVFKCLNDD GIMVQQSESP LYNLDLIQNI CRYLKDAGFK IIMPYTYPMP TYPSGFWSFT LASKKYNPLE VDEARIKEAL KDMETKYYDE EVHKGIFLAA PKFLKDAVKK ALE // ID SPT5_METJA Reviewed; 147 AA. AC Q57818; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Transcription elongation factor Spt5 {ECO:0000255|HAMAP-Rule:MF_00950}; GN Name=spt5 {ECO:0000255|HAMAP-Rule:MF_00950}; OrderedLocusNames=MJ0372; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.04 ANGSTROMS) OF 1-83, DOMAIN, AND SUBUNIT. RX PubMed=19475703; DOI=10.1002/prot.22465; RA Zhou H., Liu Q., Gao Y., Teng M., Niu L.; RT "Crystal structure of NusG N-terminal (NGN) domain from RT Methanocaldococcus jannaschii and its interaction with rpoE''."; RL Proteins 76:787-793(2009). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 1-82, FUNCTION, SUBUNIT, RP DOMAIN, AND MUTAGENESIS OF ALA-4; TYR-42 AND LEU-44. RX PubMed=20197319; DOI=10.1093/nar/gkq135; RA Hirtreiter A., Damsma G.E., Cheung A.C., Klose D., Grohmann D., RA Vojnic E., Martin A.C., Cramer P., Werner F.; RT "Spt4/5 stimulates transcription elongation through the RNA polymerase RT clamp coiled-coil motif."; RL Nucleic Acids Res. 38:4040-4051(2010). CC -!- FUNCTION: Stimulates transcription elongation. {ECO:0000255|HAMAP- CC Rule:MF_00950, ECO:0000269|PubMed:20197319}. CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. Interacts with RNA CC polymerase (RNAP). Forms a homodimer in solution. CC {ECO:0000255|HAMAP-Rule:MF_00950, ECO:0000269|PubMed:19475703, CC ECO:0000269|PubMed:20197319}. CC -!- DOMAIN: Composed of only a NusG N-terminal (NGN) domain and a KOW CC domain, similar to bacterial NusG. The NGN domain is the effector CC domain of the complex that mediates the interaction with RNAP and CC is essential for elongation activity. CC {ECO:0000269|PubMed:19475703, ECO:0000269|PubMed:20197319}. CC -!- SIMILARITY: Belongs to the archaeal Spt5 family. CC {ECO:0000255|HAMAP-Rule:MF_00950}. CC -!- SIMILARITY: Contains 1 KOW domain. {ECO:0000255|HAMAP- CC Rule:MF_00950}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98361.1; -; Genomic_DNA. DR PIR; D64346; D64346. DR PDB; 3EWG; X-ray; 2.04 A; A=1-83. DR PDB; 3LPE; X-ray; 1.90 A; A/C/E/G=1-82. DR PDB; 4ZN1; X-ray; 2.80 A; A=1-147. DR PDB; 4ZN3; X-ray; 2.30 A; A=1-147. DR PDBsum; 3EWG; -. DR PDBsum; 3LPE; -. DR PDBsum; 4ZN1; -. DR PDBsum; 4ZN3; -. DR ProteinModelPortal; Q57818; -. DR DIP; DIP-46333N; -. DR STRING; 243232.MJ_0372; -. DR EnsemblBacteria; AAB98361; AAB98361; MJ_0372. DR KEGG; mja:MJ_0372; -. DR eggNOG; arCOG01920; Archaea. DR eggNOG; COG0250; LUCA. DR InParanoid; Q57818; -. DR KO; K02601; -. DR OMA; PIPITIR; -. DR PhylomeDB; Q57818; -. DR EvolutionaryTrace; Q57818; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005840; C:ribosome; IEA:InterPro. DR GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro. DR GO; GO:0003746; F:translation elongation factor activity; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.30.30.30; -; 1. DR Gene3D; 3.30.70.940; -; 1. DR HAMAP; MF_00950; Spt5_arch; 1. DR InterPro; IPR005824; KOW. DR InterPro; IPR006645; NGN_dom. DR InterPro; IPR014722; Rib_L2_dom2. DR InterPro; IPR005825; Ribosomal_L24/26_CS. DR InterPro; IPR011590; Spt5_arc. DR InterPro; IPR005100; TF_Spt5_NGN-domain. DR InterPro; IPR008991; Translation_prot_SH3-like. DR Pfam; PF00467; KOW; 1. DR Pfam; PF03439; Spt5-NGN; 1. DR SMART; SM00739; KOW; 1. DR SMART; SM00738; NGN; 1. DR SUPFAM; SSF50104; SSF50104; 1. DR TIGRFAMs; TIGR00405; KOW_elon_Spt5; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 147 Transcription elongation factor Spt5. FT /FTId=PRO_0000113978. FT DOMAIN 91 122 KOW. {ECO:0000255|HAMAP-Rule:MF_00950}. FT MUTAGEN 4 4 A->R: Abrogates binding to RNAP. FT Decreases elongation activity. FT {ECO:0000269|PubMed:20197319}. FT MUTAGEN 42 42 Y->A: Abrogates binding to RNAP. FT Decreases elongation activity. FT {ECO:0000269|PubMed:20197319}. FT MUTAGEN 44 44 L->A: Can still bind RNAP, but with a FT decreased affinity. Does not affect FT elongation activity. FT {ECO:0000269|PubMed:20197319}. FT MUTAGEN 44 44 L->R: Abrogates binding to RNAP. FT Decreases elongation activity. FT {ECO:0000269|PubMed:20197319}. FT STRAND 2 7 {ECO:0000244|PDB:3LPE}. FT HELIX 12 25 {ECO:0000244|PDB:3LPE}. FT STRAND 30 35 {ECO:0000244|PDB:3LPE}. FT STRAND 42 49 {ECO:0000244|PDB:3LPE}. FT HELIX 50 57 {ECO:0000244|PDB:3LPE}. FT STRAND 63 66 {ECO:0000244|PDB:3LPE}. FT HELIX 73 80 {ECO:0000244|PDB:3LPE}. SQ SEQUENCE 147 AA; 16136 MW; A8D917571BF5F215 CRC64; MIFAVRTMVG QEKNIAGLMA SRAEKEQLDV YSILASESLK GYVLVEAETK GDVEELIKGM PRVRGIVPGT IAIEEIEPLL TPKKIIENIE KGDVVEIIAG PFKGERAKVI RVDKHKEEVT LELENAAVPI PITLPVEGVK IVSKHKD // ID SRP54_METJA Reviewed; 451 AA. AC Q57565; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 110. DE RecName: Full=Signal recognition particle 54 kDa protein {ECO:0000255|HAMAP-Rule:MF_00306}; DE Short=SRP54 {ECO:0000255|HAMAP-Rule:MF_00306}; GN Name=srp54 {ECO:0000255|HAMAP-Rule:MF_00306}; GN OrderedLocusNames=MJ0101; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Involved in targeting and insertion of nascent membrane CC proteins into the cytoplasmic membrane. Binds to the hydrophobic CC signal sequence of the ribosome-nascent chain (RNC) as it emerges CC from the ribosomes. The SRP-RNC complex is then targeted to the CC cytoplasmic membrane where it interacts with the SRP receptor CC FtsY. {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- SUBUNIT: Part of the signal recognition particle protein CC translocation system, which is composed of SRP and FtsY. Archaeal CC SRP consists of a 7S RNA molecule of 300 nucleotides and two CC protein subunits: SRP54 and SRP19. {ECO:0000255|HAMAP- CC Rule:MF_00306}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00306}. CC Note=The SRP-RNC complex is targeted to the cytoplasmic membrane. CC {ECO:0000255|HAMAP-Rule:MF_00306}. CC -!- DOMAIN: Composed of three domains: the N-terminal N domain, which CC is responsible for interactions with the ribosome, the central G CC domain, which binds GTP, and the C-terminal M domain, which binds CC the RNA and the signal sequence of the RNC. {ECO:0000255|HAMAP- CC Rule:MF_00306}. CC -!- SIMILARITY: Belongs to the GTP-binding SRP family. SRP54 CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00306}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98081.1; -; Genomic_DNA. DR PIR; E64312; E64312. DR PDB; 2V3C; X-ray; 2.50 A; C/D=3-427. DR PDB; 3NDB; X-ray; 3.00 A; B=3-431. DR PDB; 4XCO; X-ray; 2.90 A; C/D=304-451. DR PDBsum; 2V3C; -. DR PDBsum; 3NDB; -. DR PDBsum; 4XCO; -. DR ProteinModelPortal; Q57565; -. DR SMR; Q57565; 2-427. DR DIP; DIP-46442N; -. DR STRING; 243232.MJ_0101; -. DR PRIDE; Q57565; -. DR EnsemblBacteria; AAB98081; AAB98081; MJ_0101. DR KEGG; mja:MJ_0101; -. DR eggNOG; arCOG01228; Archaea. DR eggNOG; COG0541; LUCA. DR InParanoid; Q57565; -. DR KO; K03106; -. DR OMA; VICADTF; -. DR PhylomeDB; Q57565; -. DR EvolutionaryTrace; Q57565; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005786; C:signal recognition particle, endoplasmic reticulum targeting; IEA:UniProtKB-KW. DR GO; GO:0008312; F:7S RNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006614; P:SRP-dependent cotranslational protein targeting to membrane; IEA:InterPro. DR Gene3D; 1.10.260.30; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00306; SRP54; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR013822; Signal_recog_particl_SRP54_hlx. DR InterPro; IPR004125; Signal_recog_particle_SRP54_M. DR InterPro; IPR022941; SRP54. DR InterPro; IPR000897; SRP54_GTPase_dom. DR Pfam; PF00448; SRP54; 1. DR Pfam; PF02881; SRP54_N; 1. DR Pfam; PF02978; SRP_SPB; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00962; SRP54; 1. DR SMART; SM00963; SRP54_N; 1. DR SUPFAM; SSF47364; SSF47364; 1. DR SUPFAM; SSF47446; SSF47446; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00300; SRP54; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; GTP-binding; KW Nucleotide-binding; Reference proteome; Ribonucleoprotein; KW RNA-binding; Signal recognition particle. FT CHAIN 1 451 Signal recognition particle 54 kDa FT protein. FT /FTId=PRO_0000101177. FT NP_BIND 107 114 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 188 192 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT NP_BIND 247 250 GTP. {ECO:0000255|HAMAP-Rule:MF_00306}. FT HELIX 4 15 {ECO:0000244|PDB:2V3C}. FT STRAND 18 20 {ECO:0000244|PDB:2V3C}. FT HELIX 28 40 {ECO:0000244|PDB:2V3C}. FT HELIX 45 51 {ECO:0000244|PDB:2V3C}. FT HELIX 53 59 {ECO:0000244|PDB:2V3C}. FT STRAND 60 62 {ECO:0000244|PDB:2V3C}. FT HELIX 70 86 {ECO:0000244|PDB:2V3C}. FT STRAND 97 99 {ECO:0000244|PDB:2V3C}. FT STRAND 103 106 {ECO:0000244|PDB:2V3C}. FT STRAND 109 112 {ECO:0000244|PDB:2V3C}. FT HELIX 115 128 {ECO:0000244|PDB:2V3C}. FT STRAND 131 134 {ECO:0000244|PDB:2V3C}. FT HELIX 143 145 {ECO:0000244|PDB:2V3C}. FT HELIX 148 153 {ECO:0000244|PDB:2V3C}. FT STRAND 158 160 {ECO:0000244|PDB:3NDB}. FT STRAND 162 164 {ECO:0000244|PDB:2V3C}. FT STRAND 167 169 {ECO:0000244|PDB:2V3C}. FT HELIX 172 177 {ECO:0000244|PDB:2V3C}. FT STRAND 183 188 {ECO:0000244|PDB:2V3C}. FT HELIX 196 205 {ECO:0000244|PDB:2V3C}. FT STRAND 208 210 {ECO:0000244|PDB:2V3C}. FT STRAND 213 220 {ECO:0000244|PDB:2V3C}. FT HELIX 221 226 {ECO:0000244|PDB:2V3C}. FT HELIX 227 235 {ECO:0000244|PDB:2V3C}. FT STRAND 242 247 {ECO:0000244|PDB:2V3C}. FT STRAND 249 251 {ECO:0000244|PDB:2V3C}. FT HELIX 256 264 {ECO:0000244|PDB:2V3C}. FT STRAND 269 272 {ECO:0000244|PDB:2V3C}. FT STRAND 275 280 {ECO:0000244|PDB:2V3C}. FT STRAND 281 283 {ECO:0000244|PDB:3NDB}. FT HELIX 286 293 {ECO:0000244|PDB:2V3C}. FT TURN 305 307 {ECO:0000244|PDB:2V3C}. FT TURN 308 311 {ECO:0000244|PDB:3NDB}. FT STRAND 312 315 {ECO:0000244|PDB:2V3C}. FT HELIX 318 321 {ECO:0000244|PDB:2V3C}. FT HELIX 327 334 {ECO:0000244|PDB:2V3C}. FT TURN 335 337 {ECO:0000244|PDB:2V3C}. FT HELIX 345 348 {ECO:0000244|PDB:4XCO}. FT HELIX 351 355 {ECO:0000244|PDB:4XCO}. FT HELIX 360 363 {ECO:0000244|PDB:4XCO}. FT HELIX 367 377 {ECO:0000244|PDB:2V3C}. FT HELIX 382 385 {ECO:0000244|PDB:2V3C}. FT HELIX 388 390 {ECO:0000244|PDB:3NDB}. FT HELIX 393 402 {ECO:0000244|PDB:2V3C}. FT HELIX 407 423 {ECO:0000244|PDB:2V3C}. FT TURN 424 427 {ECO:0000244|PDB:3NDB}. FT STRAND 434 436 {ECO:0000244|PDB:4XCO}. FT HELIX 437 445 {ECO:0000244|PDB:4XCO}. SQ SEQUENCE 451 AA; 50124 MW; 5EEAF505FD227914 CRC64; MLDKLGENLN KALNKLKAAA FVDKKLIKEV IKDIQRALIQ ADVNVKLVLK MSKEIERRAL EEKTPKGLSK KEHIIKIVYE ELVKLLGEEA KKLELNPKKQ NVILLVGIQG SGKTTTAAKL ARYIQKRGLK PALIAADTYR PAAYEQLKQL AEKIHVPIYG DETRTKSPVD IVKEGMEKFK KADVLIIDTA GRHKEEKGLL EEMKQIKEIT NPDEIILVID GTIGQQAGIQ AKAFKEAVGE IGSIIVTKLD GSAKGGGALS AVAETKAPIK FIGIGEGIDD LEPFDPKKFI SRLLGMGDLE SLLEKAEDMV DEKTEESIDA IMRGKFTLNE LMTQLEAIEN MGSMKKILSM IPGFGGAMPK ELSHLTEAKI KKYKVIISSM TKEERENPKI IKASRIRRIA RGSGTTENDV REVLRYYETT KNAIDKLRKG KMLRIGGPLG QIMRQLMFKE G // ID SPT4_METJA Reviewed; 59 AA. AC Q57839; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Transcription elongation factor Spt4 {ECO:0000255|HAMAP-Rule:MF_00949}; GN Name=spt4 {ECO:0000255|HAMAP-Rule:MF_00949}; Synonyms=rpoE'', rpoE2; GN OrderedLocusNames=MJ0396; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) IN COMPLEX WITH ZINC, FUNCTION, RP AND SUBUNIT. RX PubMed=20197319; DOI=10.1093/nar/gkq135; RA Hirtreiter A., Damsma G.E., Cheung A.C., Klose D., Grohmann D., RA Vojnic E., Martin A.C., Cramer P., Werner F.; RT "Spt4/5 stimulates transcription elongation through the RNA polymerase RT clamp coiled-coil motif."; RL Nucleic Acids Res. 38:4040-4051(2010). CC -!- FUNCTION: Stimulates transcription elongation. {ECO:0000255|HAMAP- CC Rule:MF_00949, ECO:0000269|PubMed:20197319}. CC -!- SUBUNIT: Heterodimer composed of Spt4 and Spt5. CC {ECO:0000255|HAMAP-Rule:MF_00949, ECO:0000269|PubMed:20197319}. CC -!- SIMILARITY: Belongs to the archaeal Spt4 family. CC {ECO:0000255|HAMAP-Rule:MF_00949}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98386.1; -; Genomic_DNA. DR PIR; D64349; D64349. DR PDB; 3LPE; X-ray; 1.90 A; B/D/F/H=1-59. DR PDB; 4ZN1; X-ray; 2.80 A; B=2-59. DR PDB; 4ZN3; X-ray; 2.30 A; B=2-59. DR PDBsum; 3LPE; -. DR PDBsum; 4ZN1; -. DR PDBsum; 4ZN3; -. DR ProteinModelPortal; Q57839; -. DR DIP; DIP-46332N; -. DR STRING; 243232.MJ_0396; -. DR EnsemblBacteria; AAB98386; AAB98386; MJ_0396. DR KEGG; mja:MJ_0396; -. DR eggNOG; arCOG04077; Archaea. DR eggNOG; COG2093; LUCA. DR InParanoid; Q57839; -. DR KO; K03050; -. DR OMA; CLKCKYL; -. DR EvolutionaryTrace; Q57839; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR HAMAP; MF_00949; Spt4_arch; 1. DR InterPro; IPR029040; RPABC4/Spt4. DR InterPro; IPR022800; Spt4/RpoE2_Znf. DR InterPro; IPR007178; Spt4_arch. DR Pfam; PF06093; Spt4; 1. DR ProDom; PD019197; DNA-dir_RNA_pol_RpoE2_arc; 1. DR SMART; SM01389; Spt4; 1. DR SUPFAM; SSF63393; SSF63393; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Reference proteome; KW Transcription; Transcription regulation; Zinc. FT CHAIN 1 59 Transcription elongation factor Spt4. FT /FTId=PRO_0000074037. FT METAL 4 4 Zinc. {ECO:0000255|HAMAP-Rule:MF_00949, FT ECO:0000269|PubMed:20197319}. FT METAL 7 7 Zinc. {ECO:0000255|HAMAP-Rule:MF_00949, FT ECO:0000269|PubMed:20197319}. FT METAL 16 16 Zinc. {ECO:0000255|HAMAP-Rule:MF_00949, FT ECO:0000269|PubMed:20197319}. FT METAL 19 19 Zinc. {ECO:0000255|HAMAP-Rule:MF_00949, FT ECO:0000269|PubMed:20197319}. FT STRAND 2 4 {ECO:0000244|PDB:3LPE}. FT TURN 5 7 {ECO:0000244|PDB:3LPE}. FT STRAND 9 15 {ECO:0000244|PDB:3LPE}. FT TURN 17 19 {ECO:0000244|PDB:3LPE}. FT STRAND 22 25 {ECO:0000244|PDB:3LPE}. FT STRAND 30 34 {ECO:0000244|PDB:3LPE}. FT TURN 36 38 {ECO:0000244|PDB:3LPE}. FT HELIX 40 44 {ECO:0000244|PDB:3LPE}. FT STRAND 51 53 {ECO:0000244|PDB:3LPE}. FT STRAND 55 57 {ECO:0000244|PDB:3LPE}. SQ SEQUENCE 59 AA; 6578 MW; CFC635FF7C1B0919 CRC64; MRACLKCKYL TNDEICPICH SPTSENWIGL LIVINPEKSE IAKKAGIDIK GKYALSVKE // ID SUMT_METJA Reviewed; 242 AA. AC Q58375; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 16-JAN-2004, sequence version 2. DT 17-FEB-2016, entry version 95. DE RecName: Full=Uroporphyrinogen-III C-methyltransferase; DE Short=Urogen III methylase; DE EC=2.1.1.107; DE AltName: Full=SUMT; DE AltName: Full=Uroporphyrinogen III methylase; DE Short=UROM; GN Name=cobA; Synonyms=corA; OrderedLocusNames=MJ0965; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes both methylations at C-2 and C-7 of CC uroporphyrinogen III leading to precorrin-1 and precorrin-2; their CC oxidative esterification gives respectively factor I octamethyl CC ester and sirohydrochlorin. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III CC = S-adenosyl-L-homocysteine + precorrin-1. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S- CC adenosyl-L-homocysteine + precorrin-2. CC -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis; CC precorrin-2 from uroporphyrinogen III: step 1/1. CC -!- SIMILARITY: Belongs to the precorrin methyltransferase family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98967.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98967.1; ALT_INIT; Genomic_DNA. DR PIR; E64420; E64420. DR ProteinModelPortal; Q58375; -. DR STRING; 243232.MJ_0965; -. DR EnsemblBacteria; AAB98967; AAB98967; MJ_0965. DR KEGG; mja:MJ_0965; -. DR eggNOG; arCOG00644; Archaea. DR eggNOG; COG0007; LUCA. DR InParanoid; Q58375; -. DR KO; K02303; -. DR OMA; EEVKWEN; -. DR PhylomeDB; Q58375; -. DR UniPathway; UPA00148; UER00211. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:InterPro. DR GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IBA:GO_Central. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019354; P:siroheme biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.950.10; -; 1. DR Gene3D; 3.40.1010.10; -; 1. DR InterPro; IPR000878; 4pyrrol_Mease. DR InterPro; IPR014777; 4pyrrole_Mease_sub1. DR InterPro; IPR014776; 4pyrrole_Mease_sub2. DR InterPro; IPR006366; CobA/CysG_C. DR InterPro; IPR003043; Uropor_MeTrfase_CS. DR Pfam; PF00590; TP_methylase; 1. DR SUPFAM; SSF53790; SSF53790; 1. DR TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1. DR PROSITE; PS00839; SUMT_1; 1. DR PROSITE; PS00840; SUMT_2; 1. PE 3: Inferred from homology; KW Cobalamin biosynthesis; Complete proteome; Methyltransferase; KW Porphyrin biosynthesis; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 242 Uroporphyrinogen-III C-methyltransferase. FT /FTId=PRO_0000150371. FT REGION 88 90 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 12 12 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250}. FT BINDING 118 118 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 170 170 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000250}. SQ SEQUENCE 242 AA; 26340 MW; BBE8388F036B6851 CRC64; MTGKVILVGA GPGDPELITI KGLKAIKEAD VVVYDDLISK ELLNYAKKDA ELIYVGKRKG KHSFKQEEIN KILVEKAKEG KLVVRLKGGD PFVFGRGGEE ILELKKHNIP YEVIPGITSA IAVPEVAGIP VTHRKVATSF TVVTGHEAED KKEKQVDLSK LNADTIVILM GITNLENLVK ELLQNPKRSK ETPVAIIMEG TTKNQRVIKG TLGDIVEKAK KENARPPGVI VVGEVVNVLD SQ // ID SPCS_METJA Reviewed; 434 AA. AC Q58027; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 88. DE RecName: Full=O-phosphoseryl-tRNA(Sec) selenium transferase; DE EC=2.9.1.2 {ECO:0000250|UniProtKB:Q6LZM9}; DE AltName: Full=Selenocysteine synthase; DE Short=Sec synthase; DE AltName: Full=Selenocysteinyl-tRNA(Sec) synthase; DE AltName: Full=Sep-tRNA:Sec-tRNA synthase; DE Short=SepSecS; GN Name=spcS; OrderedLocusNames=MJ0610; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, PYRIDOXAL PHOSPHATE AT LYS-277, AND MUTAGENESIS OF LYS-277. RX PubMed=17142313; DOI=10.1073/pnas.0609703104; RA Yuan J., Palioura S., Salazar J.C., Su D., O'Donoghue P., Hohn M.J., RA Cardoso A.M., Whitman W.B., Soell D.; RT "RNA-dependent conversion of phosphoserine forms selenocysteine in RT eukaryotes and archaea."; RL Proc. Natl. Acad. Sci. U.S.A. 103:18923-18927(2006). CC -!- FUNCTION: Converts O-phosphoseryl-tRNA(Sec) to selenocysteinyl- CC tRNA(Sec) required for selenoprotein biosynthesis. CC {ECO:0000269|PubMed:17142313}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-seryl-tRNA(Sec) + selenophosphate CC + H(2)O = L-selenocysteinyl-tRNA(Sec) + 2 phosphate. CC {ECO:0000250|UniProtKB:Q6LZM9}. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250|UniProtKB:Q6LZM9}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; selenocysteinyl-tRNA(Sec) from L-seryl-tRNA(Sec) CC (archaeal/eukaryal route): step 2/2. CC {ECO:0000250|UniProtKB:Q6LZM9}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250|UniProtKB:Q6LZM9}. CC -!- SIMILARITY: Belongs to the SepSecS family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98603.1; -; Genomic_DNA. DR PIR; B64376; B64376. DR ProteinModelPortal; Q58027; -. DR SMR; Q58027; 1-433. DR STRING; 243232.MJ_0610; -. DR EnsemblBacteria; AAB98603; AAB98603; MJ_0610. DR KEGG; mja:MJ_0610; -. DR eggNOG; arCOG00119; Archaea. DR eggNOG; COG0076; LUCA. DR InParanoid; Q58027; -. DR KO; K03341; -. DR OMA; HIINGAY; -. DR BRENDA; 2.9.1.2; 3260. DR UniPathway; UPA00906; UER00898. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016785; F:transferase activity, transferring selenium-containing groups; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR019872; Sec-tRNA_Se_transferase. DR InterPro; IPR008829; SepSecS/SepCysS. DR PANTHER; PTHR12944; PTHR12944; 1. DR Pfam; PF05889; SepSecS; 1. DR PIRSF; PIRSF017689; SepSecS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03531; selenium_SpcS; 1. PE 1: Evidence at protein level; KW Complete proteome; Protein biosynthesis; Pyridoxal phosphate; KW Reference proteome; RNA-binding; Selenium; Transferase; tRNA-binding. FT CHAIN 1 434 O-phosphoseryl-tRNA(Sec) selenium FT transferase. FT /FTId=PRO_0000219881. FT REGION 1 40 Tetramerization. FT {ECO:0000250|UniProtKB:Q6P6M7}. FT REGION 92 102 Phosphate loop (P-loop). FT {ECO:0000250|UniProtKB:Q6P6M7}. FT BINDING 71 71 Pyridoxal phosphate. FT {ECO:0000250|UniProtKB:Q6LZM9}. FT BINDING 93 93 Substrate. FT {ECO:0000250|UniProtKB:Q6LZM9}. FT BINDING 94 94 Substrate. FT {ECO:0000250|UniProtKB:Q6LZM9}. FT BINDING 101 101 Substrate. FT {ECO:0000250|UniProtKB:Q6LZM9}. FT BINDING 306 306 Substrate. FT {ECO:0000250|UniProtKB:Q6LZM9}. FT SITE 70 70 May act as a substrate filter by FT repelling compounds with a negatively FT charged alpha-carboxylate. {ECO:0000250}. FT MOD_RES 277 277 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250|UniProtKB:Q6LZM9, FT ECO:0000269|PubMed:17142313}. FT MUTAGEN 277 277 K->A: Loss of activity. FT {ECO:0000269|PubMed:17142313}. SQ SEQUENCE 434 AA; 48684 MW; 09AFBC5819613EF5 CRC64; MGLNITGLIP KHMENRGKLT LKENLKIIEN ILEQRKAPEN GIDEEHIKLL LRLLSFMDTD KDPNVVQIGE REARVYTKLQ RDGVFDFCHG VGRSGNLIDP QPKAPGASVM YKLTNKLLES FLKALGLKVN AIATPVATGM SLALCLSAAR KKYNSNVVIY PYAAHKSPIK ATSFIGMRMR LVETVLDGDI VKVEVSDIED AIRKEINENN NPVVLSTLTF FPPRKSDDIK EIAKICQDYD IPHIINGAYA IQNFYYIEKL KKALKYRIDA VVSSSDKNLF TPIGGGIIYT KDESFLKEIS LTYPGRASAN PIVNILISLL AIGTKDYLNL MKEQKECKKL LNELLEDLAK KKGEKVLNVE NPISSCITTK KDPLDVAGKL YNLRVTGPRG VRRNDKFGTC YLKEYPYDYI VVNSAIGVKK EDIYKVIEKL DEVL // ID SPSS_METJA Reviewed; 377 AA. AC Q59072; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 20-JAN-2009, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase; DE EC=2.5.1.73; DE AltName: Full=Sep-tRNA:Cys-tRNA synthase; DE Short=SepCysS; GN OrderedLocusNames=MJ1678; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION. RX PubMed=15790858; DOI=10.1126/science.1108329; RA Sauerwald A., Zhu W., Major T.A., Roy H., Palioura S., Jahn D., RA Whitman W.B., Yates J.R. III, Ibba M., Soell D.; RT "RNA-dependent cysteine biosynthesis in archaea."; RL Science 307:1969-1972(2005). RN [3] RP INTERACTION WITH SEPRS, AND SUBUNIT. RX PubMed=18425141; DOI=10.1038/nsmb.1423; RA Zhang C.-M., Liu C., Slater S., Hou Y.-M.; RT "Aminoacylation of tRNA with phosphoserine for synthesis of cysteinyl- RT tRNA(Cys)."; RL Nat. Struct. Mol. Biol. 15:507-514(2008). CC -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to CC L-cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). CC {ECO:0000269|PubMed:15790858}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-seryl-tRNA(Cys) + sulfide = L- CC cysteinyl-tRNA(Cys) + phosphate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000305}; CC -!- SUBUNIT: Homodimer. Interacts with SepRS. CC {ECO:0000269|PubMed:18425141}. CC -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99700.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99700.1; ALT_INIT; Genomic_DNA. DR PIR; D64509; D64509. DR PDB; 3WKR; X-ray; 2.80 A; A/B/E/F=2-377. DR PDB; 3WKS; X-ray; 3.03 A; A/B=2-377. DR PDBsum; 3WKR; -. DR PDBsum; 3WKS; -. DR ProteinModelPortal; Q59072; -. DR DIP; DIP-46383N; -. DR STRING; 243232.MJ_1678; -. DR EnsemblBacteria; AAB99700; AAB99700; MJ_1678. DR KEGG; mja:MJ_1678; -. DR eggNOG; arCOG00091; Archaea. DR eggNOG; COG1103; LUCA. DR InParanoid; Q59072; -. DR KO; K06868; -. DR OMA; WDGYSVC; -. DR PhylomeDB; Q59072; -. DR BioCyc; MetaCyc:MONOMER-14997; -. DR BRENDA; 2.5.1.73; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR013375; Sep_Cys-tRNA_synth_arc. DR InterPro; IPR008829; SepSecS/SepCysS. DR Pfam; PF05889; SepSecS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR02539; SepCysS; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Protein biosynthesis; KW Pyridoxal phosphate; Reference proteome; Transferase. FT CHAIN 1 377 O-phospho-L-seryl-tRNA:Cys-tRNA synthase. FT /FTId=PRO_0000107475. FT REGION 82 83 Pyridoxal phosphate binding. FT {ECO:0000250}. FT REGION 212 214 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 83 83 Sulfur donor or Sep-tRNA(Cys). FT {ECO:0000305}. FT BINDING 107 107 Sulfur donor or Sep-tRNA(Cys). FT {ECO:0000305}. FT BINDING 108 108 Sulfur donor or Sep-tRNA(Cys). FT {ECO:0000305}. FT BINDING 189 189 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 273 273 Sulfur donor or Sep-tRNA(Cys). FT {ECO:0000305}. FT BINDING 276 276 Sulfur donor or Sep-tRNA(Cys). FT {ECO:0000305}. FT MOD_RES 215 215 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. FT TURN 3 5 {ECO:0000244|PDB:3WKR}. FT TURN 12 14 {ECO:0000244|PDB:3WKR}. FT STRAND 15 17 {ECO:0000244|PDB:3WKR}. FT HELIX 20 22 {ECO:0000244|PDB:3WKR}. FT TURN 23 25 {ECO:0000244|PDB:3WKR}. FT HELIX 29 37 {ECO:0000244|PDB:3WKR}. FT HELIX 60 70 {ECO:0000244|PDB:3WKR}. FT STRAND 74 81 {ECO:0000244|PDB:3WKR}. FT HELIX 82 92 {ECO:0000244|PDB:3WKR}. FT STRAND 99 103 {ECO:0000244|PDB:3WKR}. FT HELIX 108 116 {ECO:0000244|PDB:3WKR}. FT STRAND 120 124 {ECO:0000244|PDB:3WKR}. FT STRAND 126 128 {ECO:0000244|PDB:3WKR}. FT TURN 130 132 {ECO:0000244|PDB:3WKR}. FT HELIX 139 148 {ECO:0000244|PDB:3WKR}. FT TURN 149 151 {ECO:0000244|PDB:3WKR}. FT STRAND 154 162 {ECO:0000244|PDB:3WKR}. FT STRAND 164 166 {ECO:0000244|PDB:3WKR}. FT HELIX 172 182 {ECO:0000244|PDB:3WKR}. FT STRAND 186 189 {ECO:0000244|PDB:3WKR}. FT TURN 191 193 {ECO:0000244|PDB:3WKR}. FT TURN 201 205 {ECO:0000244|PDB:3WKR}. FT STRAND 207 212 {ECO:0000244|PDB:3WKR}. FT HELIX 213 216 {ECO:0000244|PDB:3WKR}. FT STRAND 224 228 {ECO:0000244|PDB:3WKR}. FT HELIX 230 232 {ECO:0000244|PDB:3WKR}. FT HELIX 233 236 {ECO:0000244|PDB:3WKR}. FT STRAND 241 247 {ECO:0000244|PDB:3WKR}. FT TURN 248 250 {ECO:0000244|PDB:3WKR}. FT HELIX 258 265 {ECO:0000244|PDB:3WKR}. FT HELIX 267 273 {ECO:0000244|PDB:3WKR}. FT HELIX 278 291 {ECO:0000244|PDB:3WKR}. FT TURN 292 295 {ECO:0000244|PDB:3WKR}. FT STRAND 297 303 {ECO:0000244|PDB:3WKR}. FT STRAND 306 312 {ECO:0000244|PDB:3WKR}. FT HELIX 314 321 {ECO:0000244|PDB:3WKR}. FT HELIX 326 328 {ECO:0000244|PDB:3WKR}. FT HELIX 329 335 {ECO:0000244|PDB:3WKR}. FT TURN 336 338 {ECO:0000244|PDB:3WKR}. FT STRAND 348 353 {ECO:0000244|PDB:3WKR}. FT HELIX 359 375 {ECO:0000244|PDB:3WKR}. SQ SEQUENCE 377 AA; 42764 MW; 791842FF733C72BA CRC64; MDKYKNLTRS LTREFINLNP IQRGGILPKE AKKAVYEYWD GYSVCDYCHG RLDEVTCPPI KDFLEDIAKF LNMDCARPTH GAREGKFIVM HAICKEGDYV VLDKNAHYTS YVAAERAKLN VAEVGYEEEY PTYKINLEGY KEVIDNLEDK GKNVGLILLT HVDGEYGNLN DAKKVGKIAK EKGIPFLLNC AYTVGRMPVN GKEVKADFIV ASGHKSMAAS APCGILAFSE EFSDKITKTS EKFPVKEIEM LGCTSRGLPI VTLMASFPHV VERVKKWDEE LKKTRYVVDE LEKIGFKQLG IKPKEHDLIK FETPVLDEIA KKDKRRGFFF YDELKKRGIG GIRAGVTKEI KMSVYGLEWE QVEYVVNAIK EIVESCK // ID SUCC_METJA Reviewed; 364 AA. AC Q57663; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 101. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE EC=6.2.1.5 {ECO:0000255|HAMAP-Rule:MF_00558}; DE AltName: Full=Succinyl-CoA synthetase subunit beta {ECO:0000255|HAMAP-Rule:MF_00558}; DE Short=SCS-beta {ECO:0000255|HAMAP-Rule:MF_00558}; GN Name=sucC {ECO:0000255|HAMAP-Rule:MF_00558}; OrderedLocusNames=MJ0210; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00558}; CC Note=Binds 1 Mg(2+) or Mn(2+) ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00558}; CC -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; CC succinate from succinyl-CoA (ligase route): step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase beta CC subunit family. {ECO:0000255|HAMAP-Rule:MF_00558}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|HAMAP- CC Rule:MF_00558}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98195.1; -; Genomic_DNA. DR PIR; C64326; C64326. DR ProteinModelPortal; Q57663; -. DR STRING; 243232.MJ_0210; -. DR EnsemblBacteria; AAB98195; AAB98195; MJ_0210. DR KEGG; mja:MJ_0210; -. DR eggNOG; arCOG01337; Archaea. DR eggNOG; COG0045; LUCA. DR InParanoid; Q57663; -. DR KO; K01903; -. DR OMA; YIESGCD; -. DR PhylomeDB; Q57663; -. DR UniPathway; UPA00223; UER00999. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0030145; F:manganese ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR Gene3D; 3.40.50.261; -; 1. DR HAMAP; MF_00558; Succ_CoA_beta; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR013650; ATP-grasp_succ-CoA_synth-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR017866; Succ-CoA_synthase_bsu_CS. DR InterPro; IPR005809; Succ_CoA_synthase_bsu. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR PANTHER; PTHR11815; PTHR11815; 1. DR Pfam; PF08442; ATP-grasp_2; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001554; SucCS_beta; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01016; sucCoAbeta; 1. DR PROSITE; PS50975; ATP_GRASP; 1. DR PROSITE; PS01217; SUCCINYL_COA_LIG_3; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Ligase; Magnesium; Manganese; KW Metal-binding; Nucleotide-binding; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 364 Succinyl-CoA ligase [ADP-forming] subunit FT beta. FT /FTId=PRO_0000102885. FT DOMAIN 9 229 ATP-grasp. {ECO:0000255|HAMAP- FT Rule:MF_00558}. FT NP_BIND 35 98 ATP. {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 187 187 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. FT METAL 189 189 Magnesium or manganese. FT {ECO:0000255|HAMAP-Rule:MF_00558}. SQ SEQUENCE 364 AA; 40907 MW; 16937FC54694770C CRC64; MKLHEYEAKN IFKKYGIPVP ESFLVSKEDD LNSINVDKEV VLKAQVLVGG RGKAGGILFA SNKEEFIKKA EELFNKEVKG EKVEKILVEE KLPIEKEYYV SIIIDRDAKK PLIIFSTEGG VDIEEVAEKN PEKIIKYHID VRKPFLPYIA RWIVKEAKLP SNEIGKVADV IYKLYKIFKE LDATMVEINP LVITKDGNVY AADAVLHLDD DAAFRHNYEE FEEYKNKEKL PFAYVELDGD VAVIGNGAGL TLASMDIINN LGRKPACFLD IGGGADAETV KLALRKVLEN KNVKGIFINI LGGITRCDEV AKGIVEVLKE HPNVKFAVRM MGTNEEIGRK ILEEHGIPYE TSMEEAGRKL IEQL // ID SYA_METJA Reviewed; 892 AA. AC Q57984; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 102. DE RecName: Full=Alanine--tRNA ligase; DE EC=6.1.1.7; DE AltName: Full=Alanyl-tRNA synthetase; DE Short=AlaRS; GN Name=alaS; OrderedLocusNames=MJ0564; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION IN EDITING ACTIVITY ON MISCHARGED TRNA(ALA). RX PubMed=14663147; DOI=10.1073/pnas.2136934100; RA Ahel I., Korencic D., Ibba M., Soll D.; RT "Trans-editing of mischarged tRNAs."; RL Proc. Natl. Acad. Sci. U.S.A. 100:15422-15427(2003). CC -!- FUNCTION: Catalyzes the attachment of alanine to tRNA(Ala) in a CC two-step reaction: alanine is first activated by ATP to form Ala- CC AMP and then transferred to the acceptor end of tRNA(Ala) (By CC similarity). Also functions in trans to edit the amino acid moiety CC from incorrectly charged Ser-tRNA(Ala), and maybe also from Gly- CC tRNA(Ala). {ECO:0000250, ECO:0000269|PubMed:14663147}. CC -!- CATALYTIC ACTIVITY: ATP + L-alanine + tRNA(Ala) = AMP + CC diphosphate + L-alanyl-tRNA(Ala). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Consists of three domains; the N-terminal catalytic CC domain, the editing domain and the C-terminal C-Ala domain. The CC editing domain removes incorrectly charged amino acids, while the CC C-Ala domain, along with tRNA(Ala), serves as a bridge to CC cooperatively bring together the editing and aminoacylation CC centers thus stimulating deacylation of misacylated tRNAs (By CC similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98556.1; -; Genomic_DNA. DR PIR; D64370; D64370. DR ProteinModelPortal; Q57984; -. DR STRING; 243232.MJ_0564; -. DR DNASU; 1451429; -. DR EnsemblBacteria; AAB98556; AAB98556; MJ_0564. DR KEGG; mja:MJ_0564; -. DR eggNOG; arCOG01255; Archaea. DR eggNOG; COG0013; LUCA. DR InParanoid; Q57984; -. DR KO; K01872; -. DR OMA; LDVTHYK; -. DR PhylomeDB; Q57984; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004813; F:alanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IDA:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002196; F:Ser-tRNA(Ala) hydrolase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006419; P:alanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR GO; GO:0006450; P:regulation of translational fidelity; IDA:GOC. DR HAMAP; MF_00036_A; Ala_tRNA_synth_A; 1. DR InterPro; IPR002318; Ala-tRNA-lgiase_IIc. DR InterPro; IPR018162; Ala-tRNA-ligase_IIc_anticod-bd. DR InterPro; IPR018165; Ala-tRNA-synth_IIc_core. DR InterPro; IPR018164; Ala-tRNA-synth_IIc_N. DR InterPro; IPR022429; Ala-tRNA_lgiase_arc. DR InterPro; IPR018163; Thr/Ala-tRNA-synth_IIc_edit. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR012947; tRNA_SAD. DR Pfam; PF01411; tRNA-synt_2c; 1. DR Pfam; PF07973; tRNA_SAD; 1. DR PRINTS; PR00980; TRNASYNTHALA. DR SMART; SM00863; tRNA_SAD; 1. DR SUPFAM; SSF101353; SSF101353; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR SUPFAM; SSF55186; SSF55186; 1. DR TIGRFAMs; TIGR03683; A-tRNA_syn_arch; 1. DR TIGRFAMs; TIGR00344; alaS; 1. DR PROSITE; PS50860; AA_TRNA_LIGASE_II_ALA; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 892 Alanine--tRNA ligase. FT /FTId=PRO_0000075264. FT METAL 590 590 Zinc. {ECO:0000250}. FT METAL 594 594 Zinc. {ECO:0000250}. FT METAL 699 699 Zinc. {ECO:0000250}. FT METAL 703 703 Zinc. {ECO:0000250}. SQ SEQUENCE 892 AA; 102851 MW; 409A542E72C8188B CRC64; MKHNYKVKLF DELGFVRKKC KKCGQWFWTL DEERETCGDA PCDIYSFIGK PITKKPYTYK EMVKEFINFF KEHGHEPIKR APVTARRWRD DILLTIASIA VFQPWITKGI VKPKANPLVI AQPCIRLNDI DNVGRTGRHL TCFTMGGHHA FNREDDFKYW QDETVELCFN FFKKLGIDEK SITFIESWWE GGGNAGPCYE VITHGVELAT LVFMQYEKVG DNYKEIPLKI VDTGYGIERF VWASTGEPTI YDAIFKNIVN KLKEDAGVKD IDKEILAKIT EVAGLMDVKD VGDLRKLREE VANKVNIPVE ELDKLISPYE DIYAIVDHTR ALAFMLGDGI VPSNVKDGYL VRMLIRKTLR HMDRLNLSTP ITEIVAMQLN ELKDLYPELL DMEDYIMEIL EIETNKYRQT IERGKGIVER LLKSKKEIDL ENLIELYDSH GLPPEIVKDV AKSLGKDVKI PDNFYTIVAE RHENKKEVKE KIKLPEVNVD KTELLFYEYP KMKEFEAKIL RIVDDYVILD RTAFYPEGGG QKADTGYIIK GDKKFRVVDV QKENNIVYHK IENLNDELKE GDIVKGVIDW KRRLSLMRNH TATHIINAAA QKVLGRHVWQ AGSDVDVDKA RLDITHYKRI SREELKDIER VANEIVLNNY NIKSIFMDRN EAEEKFGFRI YQGGVVPGNV LRIVIIEDEN GNIVDVQACG GTHCQNTGEV GFIKIIKTER VQDGVERLIY SSGLSALKAV QEMEDILEES AEILRCPTEE LPKVIKRFFE EWKEQRKKIE ELEKKIGELK KFELINKFET IGNYKVLVEK VEANPKEMLN IADNLATENA IVVLLNDKGN ILCKRGENVD IKMNELIRYI AKGGGREHLA QGKYEGDVEE IKKKVIEFIK NK // ID SUI1_METJA Reviewed; 103 AA. AC Q57902; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Protein translation factor SUI1 homolog {ECO:0000255|HAMAP-Rule:MF_00604}; GN OrderedLocusNames=MJ0463; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the SUI1 family. {ECO:0000255|HAMAP- CC Rule:MF_00604}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98452.1; -; Genomic_DNA. DR PIR; G64357; G64357. DR PDB; 4MO0; X-ray; 2.10 A; A=2-103. DR PDBsum; 4MO0; -. DR ProteinModelPortal; Q57902; -. DR STRING; 243232.MJ_0463; -. DR EnsemblBacteria; AAB98452; AAB98452; MJ_0463. DR KEGG; mja:MJ_0463; -. DR eggNOG; arCOG04223; Archaea. DR eggNOG; COG0023; LUCA. DR InParanoid; Q57902; -. DR KO; K03113; -. DR OMA; MPEICPR; -. DR PhylomeDB; Q57902; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003743; F:translation initiation factor activity; IEA:InterPro. DR GO; GO:0006417; P:regulation of translation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.780.10; -; 1. DR HAMAP; MF_00604; SUI1; 1. DR InterPro; IPR022851; SUI1_arc. DR InterPro; IPR005872; SUI1_arc_bac. DR InterPro; IPR001950; TIF_SUI1. DR Pfam; PF01253; SUI1; 1. DR PIRSF; PIRSF037511; Transl_init_SUI1_pro; 1. DR SUPFAM; SSF55159; SSF55159; 1. DR TIGRFAMs; TIGR01158; SUI1_rel; 1. DR PROSITE; PS50296; SUI1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Protein biosynthesis; KW Reference proteome; Translation regulation. FT CHAIN 1 103 Protein translation factor SUI1 homolog. FT /FTId=PRO_0000130580. FT STRAND 28 34 {ECO:0000244|PDB:4MO0}. FT STRAND 40 45 {ECO:0000244|PDB:4MO0}. FT TURN 49 51 {ECO:0000244|PDB:4MO0}. FT HELIX 54 65 {ECO:0000244|PDB:4MO0}. FT STRAND 69 72 {ECO:0000244|PDB:4MO0}. FT STRAND 75 80 {ECO:0000244|PDB:4MO0}. FT HELIX 83 92 {ECO:0000244|PDB:4MO0}. FT HELIX 97 99 {ECO:0000244|PDB:4MO0}. FT STRAND 100 102 {ECO:0000244|PDB:4MO0}. SQ SEQUENCE 103 AA; 11732 MW; 766728FD824A809C CRC64; MMPEICPRCG LPKELCVCEE IAKEEQKIKI YVTKRRFGKL MTIIEGFDTS VIDLKELAKK LKDICACGGT VKDNTIELQG DHRKKVAEEL VKMGFSRDSI EIR // ID SUCD_METJA Reviewed; 294 AA. AC Q58643; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 109. DE RecName: Full=Succinyl-CoA ligase [ADP-forming] subunit alpha; DE EC=6.2.1.5; DE AltName: Full=Succinyl-CoA synthetase subunit alpha; DE Short=SCS-alpha; GN Name=sucD; OrderedLocusNames=MJ1246; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + succinate + CoA = ADP + phosphate + CC succinyl-CoA. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the succinate/malate CoA ligase alpha CC subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99250.1; -; Genomic_DNA. DR PIR; E64455; E64455. DR PDB; 2YV1; X-ray; 1.70 A; A=1-294. DR PDBsum; 2YV1; -. DR ProteinModelPortal; Q58643; -. DR SMR; Q58643; 7-293. DR STRING; 243232.MJ_1246; -. DR EnsemblBacteria; AAB99250; AAB99250; MJ_1246. DR KEGG; mja:MJ_1246; -. DR eggNOG; arCOG01339; Archaea. DR eggNOG; COG0074; LUCA. DR InParanoid; Q58643; -. DR KO; K01902; -. DR OMA; FEQDPQT; -. DR PhylomeDB; Q58643; -. DR EvolutionaryTrace; Q58643; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0048037; F:cofactor binding; IEA:InterPro. DR GO; GO:0004775; F:succinate-CoA ligase (ADP-forming) activity; IBA:GO_Central. DR GO; GO:0009142; P:nucleoside triphosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0006105; P:succinate metabolic process; IBA:GO_Central. DR GO; GO:0006104; P:succinyl-CoA metabolic process; IBA:GO_Central. DR GO; GO:0006099; P:tricarboxylic acid cycle; IBA:GO_Central. DR Gene3D; 3.40.50.261; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR017440; Cit_synth/succinyl-CoA_lig_AS. DR InterPro; IPR003781; CoA-bd. DR InterPro; IPR005810; CoA_lig_alpha. DR InterPro; IPR005811; CoA_ligase. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR016102; Succinyl-CoA_synth-like. DR Pfam; PF02629; CoA_binding; 1. DR Pfam; PF00549; Ligase_CoA; 1. DR PIRSF; PIRSF001553; SucCS_alpha; 1. DR PRINTS; PR01798; SCOASYNTHASE. DR SMART; SM00881; CoA_binding; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52210; SSF52210; 1. DR TIGRFAMs; TIGR01019; sucCoAalpha; 1. DR PROSITE; PS01216; SUCCINYL_COA_LIG_1; 1. DR PROSITE; PS00399; SUCCINYL_COA_LIG_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Ligase; KW Nucleotide-binding; Phosphoprotein; Reference proteome; KW Tricarboxylic acid cycle. FT CHAIN 1 294 Succinyl-CoA ligase [ADP-forming] subunit FT alpha. FT /FTId=PRO_0000102810. FT ACT_SITE 251 251 Tele-phosphohistidine intermediate. FT {ECO:0000250}. FT STRAND 16 19 {ECO:0000244|PDB:2YV1}. FT TURN 20 22 {ECO:0000244|PDB:2YV1}. FT HELIX 24 35 {ECO:0000244|PDB:2YV1}. FT STRAND 40 44 {ECO:0000244|PDB:2YV1}. FT STRAND 56 61 {ECO:0000244|PDB:2YV1}. FT HELIX 62 69 {ECO:0000244|PDB:2YV1}. FT STRAND 73 76 {ECO:0000244|PDB:2YV1}. FT HELIX 80 92 {ECO:0000244|PDB:2YV1}. FT STRAND 96 100 {ECO:0000244|PDB:2YV1}. FT HELIX 107 120 {ECO:0000244|PDB:2YV1}. FT STRAND 123 125 {ECO:0000244|PDB:2YV1}. FT STRAND 131 134 {ECO:0000244|PDB:2YV1}. FT TURN 135 137 {ECO:0000244|PDB:2YV1}. FT STRAND 138 141 {ECO:0000244|PDB:2YV1}. FT HELIX 145 147 {ECO:0000244|PDB:2YV1}. FT STRAND 150 158 {ECO:0000244|PDB:2YV1}. FT HELIX 161 172 {ECO:0000244|PDB:2YV1}. FT STRAND 177 182 {ECO:0000244|PDB:2YV1}. FT STRAND 185 188 {ECO:0000244|PDB:2YV1}. FT HELIX 193 201 {ECO:0000244|PDB:2YV1}. FT STRAND 207 218 {ECO:0000244|PDB:2YV1}. FT HELIX 219 227 {ECO:0000244|PDB:2YV1}. FT STRAND 234 239 {ECO:0000244|PDB:2YV1}. FT HELIX 263 273 {ECO:0000244|PDB:2YV1}. FT HELIX 283 292 {ECO:0000244|PDB:2YV1}. SQ SEQUENCE 294 AA; 30923 MW; 97BAAE1C0D311E6D CRC64; MVLRDKMILL DENTKAIVQG ITGRQGSFHT KKMLECGTKI VGGVTPGKGG QNVHGVPVFD TVKEAVKETD ANASVIFVPA PFAKDAVFEA IDAGIELIVV ITEHIPVHDT MEFVNYAEDV GVKIIGPNTP GIASPKVGKL GIIPMEVLKE GSVGMVSRSG TLTYEIAHQI KKAGFGVSTC VGIGGDPIVG LRYKEVLDLF EKDDETEAIV MIGEIGGGAE EEAAKFIEKM KKPVIGYIAG QSAPEGKRMG HAGAIVEKGK GTAESKMKAL EEAGAYVAKN ISDIPKLLAG ILGK // ID SYDND_METJA Reviewed; 438 AA. AC Q58950; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 112. DE RecName: Full=Aspartate--tRNA(Asp/Asn) ligase {ECO:0000255|HAMAP-Rule:MF_00044}; DE EC=6.1.1.23 {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; DE AltName: Full=Non-discriminating aspartyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00044}; DE Short=ND-AspRS {ECO:0000255|HAMAP-Rule:MF_00044}; GN Name=aspS {ECO:0000255|HAMAP-Rule:MF_00044}; OrderedLocusNames=MJ1555; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Aspartyl-tRNA synthetase with relaxed tRNA specificity CC since it is able to aspartylate not only its cognate tRNA(Asp) but CC also tRNA(Asn). Reaction proceeds in two steps: aspartate is first CC activated by ATP to form Asp-AMP and then transferred to the CC acceptor end of tRNA(Asp/Asn). {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asx) = AMP + CC diphosphate + L-aspartyl-tRNA(Asx). {ECO:0000255|HAMAP- CC Rule:MF_00044}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00044}; CC Note=Binds 3 Mg(2+) cations per subunit. The strongest magnesium CC site (Mg1) is bound to the beta- and gamma-phosphates of ATP and CC four water molecules complete its coordination sphere. CC {ECO:0000255|HAMAP-Rule:MF_00044}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00044}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99575.1; -; Genomic_DNA. DR PIR; B64494; B64494. DR ProteinModelPortal; Q58950; -. DR SMR; Q58950; 8-438. DR STRING; 243232.MJ_1555; -. DR EnsemblBacteria; AAB99575; AAB99575; MJ_1555. DR KEGG; mja:MJ_1555; -. DR eggNOG; arCOG00406; Archaea. DR eggNOG; COG0017; LUCA. DR InParanoid; Q58950; -. DR KO; K01876; -. DR OMA; HEVIDSI; -. DR PhylomeDB; Q58950; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro. DR GO; GO:0050560; F:aspartate-tRNA(Asn) ligase activity; IEA:UniProtKB-EC. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_00044; Asp_tRNA_synth; 1. DR InterPro; IPR004364; aa-tRNA-synt_II. DR InterPro; IPR018150; aa-tRNA-synt_II-like. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004523; Asp-tRNA_synthase_arc. DR InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR PANTHER; PTHR22594; PTHR22594; 1. DR PANTHER; PTHR22594:SF10; PTHR22594:SF10; 1. DR Pfam; PF00152; tRNA-synt_2; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PRINTS; PR01042; TRNASYNTHASP. DR SUPFAM; SSF50249; SSF50249; 1. DR TIGRFAMs; TIGR00458; aspS_nondisc; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 438 Aspartate--tRNA(Asp/Asn) ligase. FT /FTId=PRO_0000110995. FT NP_BIND 220 222 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 228 230 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT NP_BIND 409 412 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT REGION 198 201 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT METAL 361 361 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT METAL 361 361 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT METAL 364 364 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 176 176 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 220 220 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 361 361 ATP. {ECO:0000255|HAMAP-Rule:MF_00044}. FT BINDING 364 364 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT BINDING 368 368 Aspartate. {ECO:0000255|HAMAP- FT Rule:MF_00044}. FT SITE 91 91 Important for tRNA non-discrimination. FT {ECO:0000255|HAMAP-Rule:MF_00044}. SQ SEQUENCE 438 AA; 50350 MW; 13752FF19CBE5337 CRC64; MVNKMKWRRT HYSADIKPEM DGQEVIIMGW VHSIRALGKI IFVILRDREG TVQIVAPKQK VGDELFSQIK KLGAEDVIAV KGKVIANEKA PNGFEILPLE LEVINTAKRP LPLDPAEKVP AELDTRLENR FLDLRRPKVQ AIFKIRSEML KSVRNTLYNE GFIEVNTPKL VASCTEGGTE LFPISYFERE AFLGQSPQLY KQMLMATGLD RVFEIAPIFR AEEHNTRRHL NEATSIDIEM AFADDKDAMD ILEKVVYNAF VDVYENRKKE IETLGIEFEL PPEKFDRITY DEAIDIANAK GVEISWGEDL SREAEKAIGE EMEGLYFITD WPSEIRPFYT MPDEKNPNIC KAFDLMYKDL EISSGAQRIH LYDLLVENIK KKGLNPDGFT YYLEAFKYGM PPHAGWGLGA DRFTMVLTQQ ENIRECVLFP RDRQRLTP // ID SYE_METJA Reviewed; 553 AA. AC Q58772; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Glutamate--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00022}; DE EC=6.1.1.17 {ECO:0000255|HAMAP-Rule:MF_00022}; DE AltName: Full=Glutamyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00022}; DE Short=GluRS {ECO:0000255|HAMAP-Rule:MF_00022}; GN Name=gltX {ECO:0000255|HAMAP-Rule:MF_00022}; OrderedLocusNames=MJ1377; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Glu) in a CC two-step reaction: glutamate is first activated by ATP to form CC Glu-AMP and then transferred to the acceptor end of tRNA(Glu). CC {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- CATALYTIC ACTIVITY: ATP + L-glutamate + tRNA(Glu) = AMP + CC diphosphate + L-glutamyl-tRNA(Glu). {ECO:0000255|HAMAP- CC Rule:MF_00022}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00022}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00022}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99384.1; -; Genomic_DNA. DR PIR; H64471; H64471. DR ProteinModelPortal; Q58772; -. DR STRING; 243232.MJ_1377; -. DR EnsemblBacteria; AAB99384; AAB99384; MJ_1377. DR KEGG; mja:MJ_1377; -. DR eggNOG; arCOG04302; Archaea. DR eggNOG; COG0008; LUCA. DR InParanoid; Q58772; -. DR KO; K01885; -. DR OMA; MRFAPNP; -. DR PhylomeDB; Q58772; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004818; F:glutamate-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006424; P:glutamyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1160.10; -; 1. DR Gene3D; 2.40.240.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00022_A; Glu_tRNA_synth_A; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR004526; Glu-tRNA-synth_arc/euk. DR InterPro; IPR000924; Glu/Gln-tRNA-synth. DR InterPro; IPR020061; Glu/Gln-tRNA-synth_Ib_a-bdl. DR InterPro; IPR020058; Glu/Gln-tRNA-synth_Ib_cat-dom. DR InterPro; IPR020059; Glu/Gln-tRNA-synth_Ib_codon-bd. DR InterPro; IPR022888; Glu_tRNA_synth_arc. DR InterPro; IPR020056; Rbsml_L25/Gln-tRNA_synth_b-brl. DR InterPro; IPR011035; Ribosomal_L25/Gln-tRNA_synth. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF00749; tRNA-synt_1c; 1. DR Pfam; PF03950; tRNA-synt_1c_C; 1. DR PRINTS; PR00987; TRNASYNTHGLU. DR SUPFAM; SSF50715; SSF50715; 1. DR TIGRFAMs; TIGR00463; gltX_arch; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 553 Glutamate--tRNA ligase. FT /FTId=PRO_0000119717. FT MOTIF 98 108 "HIGH" region. SQ SEQUENCE 553 AA; 64577 MW; B19D4177990454A0 CRC64; MEEKILPIAL RNAIKYNGKA NPKAVLGIFL SENPEYRSKA KEVMPIVEKV VEEVNKLSLD EIKKKLEELG EDVKKKEKKE KGLELPNVKD KVVMRFAPNP SGPLHIGHAR AAVLNDYFVK KYGGKLILRL EDTDPKRVLP EAYDMIKEDL DWLGVKVDEV VIQSDRIELY YEYGRKLIEM GHAYVCDCNP EEFRELRNKG VPCKCRDRAI EDNLELWEKM LNGELENVAV RLKTDIKHKN PSIRDFPIFR VEKTPHPRTG DKYCVYPLMN FSVPVDDHLL GMTHVLRGKD HIVNTEKQAY IYKYFGWEMP EFIHYGILKI EDIVLSTSSM YKGIKEGLYS GWDDVRLGTL RALRRRGIKP EAIYEIMKRI GIKQADVKFS WENLYAINKE LIDKDARRFF FVWNPKKLII EGAEKKVLKL RMHPDRPEFG ERELIFDGEV YVVGDELEEN KMYRLMELFN IVVEKVDDIA LAKYHSDDFK IARKNKAKII HWIPVKDSVK VKVLMPDGEI KEGFAEKDFA KVEVDDIIQF ERFGFVRIDK KDNDGFVCCY AHR // ID SYH_METJA Reviewed; 416 AA. AC Q58406; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Histidine--tRNA ligase; DE EC=6.1.1.21; DE AltName: Full=Histidyl-tRNA synthetase; DE Short=HisRS; GN Name=hisS; OrderedLocusNames=MJ1000; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-histidine + tRNA(His) = AMP + CC diphosphate + L-histidyl-tRNA(His). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99003.1; -; Genomic_DNA. DR PIR; G64424; G64424. DR ProteinModelPortal; Q58406; -. DR STRING; 243232.MJ_1000; -. DR EnsemblBacteria; AAB99003; AAB99003; MJ_1000. DR KEGG; mja:MJ_1000; -. DR eggNOG; arCOG00404; Archaea. DR eggNOG; COG0124; LUCA. DR InParanoid; Q58406; -. DR KO; K01892; -. DR OMA; YRQFWQF; -. DR PhylomeDB; Q58406; -. DR BRENDA; 6.1.1.21; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004821; F:histidine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IEA:InterPro. DR GO; GO:0006427; P:histidyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00125; HisZ; 1. DR HAMAP; MF_00127; His_tRNA_synth; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR015807; His-tRNA-ligase. DR InterPro; IPR004516; HisRS/HisZ. DR InterPro; IPR004517; HisZ. DR PANTHER; PTHR11476; PTHR11476; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR PIRSF; PIRSF001549; His-tRNA_synth; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00442; hisS; 1. DR TIGRFAMs; TIGR00443; hisZ_biosyn_reg; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 416 Histidine--tRNA ligase. FT /FTId=PRO_0000136312. SQ SEQUENCE 416 AA; 48322 MW; D7541F81CEAA8679 CRC64; MIVMFQKPRG TRDFLPEEMK KRRFVENKLR EVFERYGYKE ILTPTFESFE LIAKKTGEEI RKQLYVFKDH GGREMALRPE MTSPVVRFYL NELKNLQKPL RLYYFANCFR YERPQAGRFR EFWQMGCELI GCKEPLADAE VLNLAMDGLI NIGLDFDVHI GHLGVLKGVL EKFNVSEEEE VKIRRLIDKE DYDNLKIYLT QILGEEKKEL IFEILKFKGS REVLDELKEI LKDFPKSMEA INNLEEILEF VIHDKYTINL GIARGLDYYT GMVFEIYGKK GAKQICGGGR YDNLIETFGG EPTPAVGFAY GFDRIMMNID DLDIEEESIL IIPVKKDKEL IKKSLIIADK LRKAGKIVEL EIMGRKLRKA LDYANSRGFK KVIIVGEKEL NEGKVTVKDM ITGEQKLIGI DELTNF // ID SYFB_METJA Reviewed; 548 AA. AC Q58508; DT 08-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Phenylalanine--tRNA ligase beta subunit; DE EC=6.1.1.20; DE AltName: Full=Phenylalanyl-tRNA synthetase beta subunit; DE Short=PheRS; GN Name=pheT; OrderedLocusNames=MJ1108; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the phenylalanyl-tRNA synthetase beta CC subunit family. Type 2 subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B5 domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99110.1; -; Genomic_DNA. DR PIR; C64438; C64438. DR ProteinModelPortal; Q58508; -. DR STRING; 243232.MJ_1108; -. DR EnsemblBacteria; AAB99110; AAB99110; MJ_1108. DR KEGG; mja:MJ_1108; -. DR eggNOG; arCOG00412; Archaea. DR eggNOG; COG0072; LUCA. DR InParanoid; Q58508; -. DR KO; K01890; -. DR OMA; ERPYVTG; -. DR PhylomeDB; Q58508; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009328; C:phenylalanine-tRNA ligase complex; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.30.56.20; -; 1. DR HAMAP; MF_00284; Phe_tRNA_synth_beta2; 1. DR InterPro; IPR005146; B3/B4_tRNA-bd. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR004531; Phe-tRNA-synth_IIc_bsu_arc. DR InterPro; IPR020825; Phe-tRNA_synthase_B3/B4. DR InterPro; IPR022918; Phe_tRNA_ligase_beta2_bac/arc. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR InterPro; IPR005147; tRNA_synthase_B5-dom. DR Pfam; PF03483; B3_4; 1. DR Pfam; PF03484; B5; 1. DR Pfam; PF01409; tRNA-synt_2d; 1. DR SMART; SM00873; B3_4; 1. DR SMART; SM00874; B5; 1. DR SUPFAM; SSF46955; SSF46955; 2. DR SUPFAM; SSF56037; SSF56037; 1. DR TIGRFAMs; TIGR00471; pheT_arch; 1. DR PROSITE; PS51483; B5; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 548 Phenylalanine--tRNA ligase beta subunit. FT /FTId=PRO_0000127002. FT DOMAIN 275 350 B5. SQ SEQUENCE 548 AA; 62697 MW; 4EE8DE2CD93BB0DA CRC64; MPTINVKKAD LERLVNMPLE DEFIEEKFPM MGVEVEGIFE EDGEKIIQFS INPNRPDYLS AEGLARGFRG IIGIETGLKK YDIESSDVKL YVENVETRPY IAMALVKGVI VDDYVLESII NLQEKLHWVM GRDRKKVAIG IHDADKVKPP FYYKEVSGDG IKFVPLNSDE EMTPREILEK HEKGIKYAHL IKDDKFPIIL DSEGDVLSMP PIINGELTRV TTETRNLLID VTGTDKYAVE KTLNIIVTAL AERKYGKIHA VEVIKDNQST IYPNLKEDVL ETTSEYINKV LGANLTPGTI INYLRRCRLD AQFVDNKIKV FIPAYRVDIF GEIDIAEEVA IAYGYNKFSG EYPIIGTIGE LNQLEKKCDF IREIMVGFGF YEVINLMLSN DEVLFKKMRI EDNNYIEVLK PASIEHRIVR KSILPLLMET LRINKHKELP QKIFEIGDCV VIDENAETKS RVVKKIAGVI VDNETNFNEI KSYVEGLLRE LKIEYELDNF EHPSFIKGRC AKILKDGKII GYFGEIHPEV ITNFELEFPV VGFELEIE // ID SYP_METJA Reviewed; 455 AA. AC Q58635; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 115. DE RecName: Full=Proline--tRNA ligase; DE EC=6.1.1.15; DE AltName: Full=Prolyl-tRNA synthetase; DE Short=ProRS; GN Name=proS; OrderedLocusNames=MJ1238; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-18, FUNCTION AS A PROLYL-TRNA SYNTHETASE, AND RP PUTATIVE FUNCTION AS A CYSTEINYL-TRNA SYNTHETASE. RX PubMed=10642548; DOI=10.1126/science.287.5452.479; RA Stathopoulos C., Li T., Longman R., Vothknecht U.C., Becker H.D., RA Ibba M., Soell D.; RT "One polypeptide with two aminoacyl-tRNA synthetase activities."; RL Science 287:479-482(2000). RN [3] RP FUNCTION AS A PROLYL-TRNA SYNTHETASE, PUTATIVE FUNCTION AS A RP CYSTEINYL-TRNA SYNTHETASE, AND INHIBITION BY PROLINAMIDE. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10869184; DOI=10.1021/bi0004955; RA Lipman R.S.A., Sowers K.R., Hou Y.-M.; RT "Synthesis of cysteinyl-tRNA(Cys) by a genome that lacks the normal RT cysteine-tRNA synthetase."; RL Biochemistry 39:7792-7798(2000). RN [4] RP FUNCTION AS A PROLYL-TRNA SYNTHETASE, PUTATIVE FUNCTION AS A RP CYSTEINYL-TRNA SYNTHETASE, AND KINETIC PARAMETERS. RX PubMed=11141055; DOI=10.1021/bi002108x; RA Stathopoulos C., Jacquin-Becker C., Becker H.D., Li T., Ambrogelly A., RA Longman R., Soell D.; RT "Methanococcus jannaschii prolyl-cysteinyl-tRNA synthetase possesses RT overlapping amino acid binding sites."; RL Biochemistry 40:46-52(2001). RN [5] RP MISAMINOACYLATION OF TRNA(PRO) WITH ALANINE OR CYSTEINE, EDITING RP ACTIVITY AGAINST ALANINE, AND KINETIC PARAMETERS. RX PubMed=11408489; DOI=10.1074/jbc.M104761200; RA Beuning P.J., Musier-Forsyth K.; RT "Species-specific differences in amino acid editing by class II RT prolyl-tRNA synthetase."; RL J. Biol. Chem. 276:30779-30785(2001). RN [6] RP MISAMINOACYLATION OF TRNA(PRO) WITH CYSTEINE, AND KINETIC PARAMETERS. RX PubMed=12130657; DOI=10.1074/jbc.M206928200; RA Ahel I., Stathopoulos C., Ambrogelly A., Sauerwald A., Toogood H., RA Hartsch T., Soell D.; RT "Cysteine activation is an inherent in vitro property of prolyl-tRNA RT synthetases."; RL J. Biol. Chem. 277:34743-34748(2002). RN [7] RP MISAMINOACYLATION OF TRNA(PRO) WITH CYSTEINE, INABILITY TO SYNTHESIZE RP CYSTEINYL-TRNA(CYS), AND LACK OF EDITING ACTIVITY. RX PubMed=12130658; DOI=10.1074/jbc.M206929200; RA Ambrogelly A., Ahel I., Polycarpo C., Bunjun-Srihari S., Krett B., RA Jacquin-Becker C., Ruan B., Koehrer C., Stathopoulos C., RA RajBhandary U.L., Soell D.; RT "Methanocaldococcus jannaschii prolyl-tRNA synthetase charges RT tRNA(Pro) with cysteine."; RL J. Biol. Chem. 277:34749-34754(2002). RN [8] RP FUNCTION IN CYSTEINE ACTIVATION. RX PubMed=11866507; DOI=10.1006/jmbi.2001.5373; RA Lipman R.S.A., Beuning P.J., Musier-Forsyth K., Hou Y.-M.; RT "Amino acid activation of a dual-specificity tRNA synthetase is RT independent of tRNA."; RL J. Mol. Biol. 316:421-427(2002). RN [9] RP INABILITY TO SYNTHESIZE CYSTEINYL-TRNA(CYS). RX PubMed=14679218; DOI=10.1128/JB.186.1.8-14.2004; RA Ruan B., Nakano H., Tanaka M., Mills J.A., DeVito J.A., Min B., RA Low K.B., Battista J.R., Soell D.; RT "Cysteinyl-tRNA(Cys) formation in Methanocaldococcus jannaschii: the RT mechanism is still unknown."; RL J. Bacteriol. 186:8-14(2004). RN [10] RP SUBUNIT. RX PubMed=16226256; DOI=10.1016/j.febslet.2005.09.025; RA Ambrogelly A., Kamtekar S., Stathopoulos C., Kennedy D., Soell D.; RT "Asymmetric behavior of archaeal prolyl-tRNA synthetase."; RL FEBS Lett. 579:6017-6022(2005). RN [11] RP X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF APOENZYME, AND SUBUNIT. RX PubMed=12578991; DOI=10.1073/pnas.0437911100; RA Kamtekar S., Kennedy W.D., Wang J., Stathopoulos C., Soell D., RA Steitz T.A.; RT "The structural basis of cysteine aminoacylation of tRNAPro by prolyl- RT tRNA synthetases."; RL Proc. Natl. Acad. Sci. U.S.A. 100:1673-1678(2003). CC -!- FUNCTION: Catalyzes the attachment of proline to tRNA(Pro) in a CC two-step reaction: proline is first activated by ATP to form Pro- CC AMP and then transferred to the acceptor end of tRNA(Pro). Can CC inadvertently accommodate and process non-cognate amino acids such CC as cysteine and alanine. {ECO:0000269|PubMed:10642548, CC ECO:0000269|PubMed:10869184, ECO:0000269|PubMed:11141055, CC ECO:0000269|PubMed:11866507}. CC -!- CATALYTIC ACTIVITY: ATP + L-proline + tRNA(Pro) = AMP + CC diphosphate + L-prolyl-tRNA(Pro). CC -!- ENZYME REGULATION: Inhibited by high concentrations of CC prolinamide. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=0.28 mM for proline (at 60 degrees Celsius) CC {ECO:0000269|PubMed:11141055, ECO:0000269|PubMed:11408489, CC ECO:0000269|PubMed:12130657}; CC KM=0.09 mM for cysteine (at 60 degrees Celsius) CC {ECO:0000269|PubMed:11141055, ECO:0000269|PubMed:11408489, CC ECO:0000269|PubMed:12130657}; CC -!- SUBUNIT: Homodimer. The dimer is functionally asymmetric: only one CC of the two active sites at a time is able to form prolyl- CC adenylate, and only one tRNA molecule binds per dimer. CC {ECO:0000269|PubMed:12578991, ECO:0000269|PubMed:16226256}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- DOMAIN: Consists of three domains: the N-terminal catalytic CC domain, the anticodon-binding domain and the C-terminal extension. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. ProS type 3 subfamily. {ECO:0000305}. CC -!- CAUTION: Was originally (PubMed:10642548, PubMed:10869184 and CC PubMed:11141055) thought to have both prolyl- and cysteinyl-tRNA CC synthetase activities (ProCysRS). However, recent biochemical and CC structural studies show that ProRS misaminoacylates tRNA(Pro) with CC cysteine but is unable to aminoacylate tRNA(Cys). These CC conflicting results may be due to the fact that much of the CC previous work was done with unfractionated tRNA. {ECO:0000305}. CC -!- CAUTION: According to PubMed:12130658, ProRS is unable to edit the CC misacylated Cys-tRNA(Pro) and Ala-tRNA(Pro), whereas according to CC PubMed:11408489, it hydrolyzes Ala-AMP and Ala-tRNA(Pro) by CC 'pretransfer' and 'posttransfer' editing activities, respectively. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99242.1; -; Genomic_DNA. DR PIR; E64454; E64454. DR PDB; 1NJ8; X-ray; 3.20 A; A/B/C/D=2-455. DR PDBsum; 1NJ8; -. DR ProteinModelPortal; Q58635; -. DR SMR; Q58635; 1-455. DR STRING; 243232.MJ_1238; -. DR EnsemblBacteria; AAB99242; AAB99242; MJ_1238. DR KEGG; mja:MJ_1238; -. DR eggNOG; arCOG00402; Archaea. DR eggNOG; COG0442; LUCA. DR InParanoid; Q58635; -. DR KO; K01881; -. DR OMA; QNSPGWK; -. DR PhylomeDB; Q58635; -. DR BRENDA; 6.1.1.15; 3260. DR SABIO-RK; Q58635; -. DR EvolutionaryTrace; Q58635; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004827; F:proline-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006433; P:prolyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.110.30; -; 1. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_01571; Pro_tRNA_synth_type3; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR002316; Pro-tRNA-ligase_IIa. DR InterPro; IPR004499; Pro-tRNA-ligase_IIa_arc-type. DR InterPro; IPR016061; Pro-tRNA_ligase_II_C. DR InterPro; IPR017449; Pro-tRNA_synth_II. DR InterPro; IPR015264; Pro-tRNA_synth_II_arc. DR PANTHER; PTHR11451:SF6; PTHR11451:SF6; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF09181; ProRS-C_2; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01046; TRNASYNTHPRO. DR SUPFAM; SSF52954; SSF52954; 1. DR SUPFAM; SSF64586; SSF64586; 1. DR TIGRFAMs; TIGR00408; proS_fam_I; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Direct protein sequencing; Ligase; KW Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 455 Proline--tRNA ligase. FT /FTId=PRO_0000139351. FT REGION 329 359 Interaction with tRNA. {ECO:0000250}. FT BINDING 101 101 Proline. {ECO:0000250}. FT BINDING 103 103 Proline. {ECO:0000250}. FT BINDING 132 132 ATP. {ECO:0000250}. FT BINDING 132 132 Proline. {ECO:0000250}. FT BINDING 134 134 ATP. {ECO:0000250}. FT BINDING 216 216 ATP. {ECO:0000250}. FT BINDING 219 219 ATP. {ECO:0000250}. FT BINDING 221 221 Proline. {ECO:0000250}. FT BINDING 253 253 ATP. {ECO:0000250}. FT BINDING 255 255 ATP. {ECO:0000250}. FT HELIX 3 13 {ECO:0000244|PDB:1NJ8}. FT HELIX 31 50 {ECO:0000244|PDB:1NJ8}. FT STRAND 60 63 {ECO:0000244|PDB:1NJ8}. FT HELIX 64 70 {ECO:0000244|PDB:1NJ8}. FT STRAND 72 74 {ECO:0000244|PDB:1NJ8}. FT HELIX 75 80 {ECO:0000244|PDB:1NJ8}. FT STRAND 82 98 {ECO:0000244|PDB:1NJ8}. FT STRAND 100 102 {ECO:0000244|PDB:1NJ8}. FT HELIX 103 111 {ECO:0000244|PDB:1NJ8}. FT STRAND 124 128 {ECO:0000244|PDB:1NJ8}. FT TURN 140 142 {ECO:0000244|PDB:1NJ8}. FT STRAND 150 159 {ECO:0000244|PDB:1NJ8}. FT HELIX 160 181 {ECO:0000244|PDB:1NJ8}. FT STRAND 186 190 {ECO:0000244|PDB:1NJ8}. FT STRAND 200 208 {ECO:0000244|PDB:1NJ8}. FT STRAND 214 224 {ECO:0000244|PDB:1NJ8}. FT HELIX 226 230 {ECO:0000244|PDB:1NJ8}. FT STRAND 234 236 {ECO:0000244|PDB:1NJ8}. FT STRAND 240 244 {ECO:0000244|PDB:1NJ8}. FT STRAND 246 252 {ECO:0000244|PDB:1NJ8}. FT HELIX 255 264 {ECO:0000244|PDB:1NJ8}. FT STRAND 278 285 {ECO:0000244|PDB:1NJ8}. FT HELIX 292 307 {ECO:0000244|PDB:1NJ8}. FT STRAND 312 314 {ECO:0000244|PDB:1NJ8}. FT HELIX 321 330 {ECO:0000244|PDB:1NJ8}. FT STRAND 334 339 {ECO:0000244|PDB:1NJ8}. FT HELIX 341 345 {ECO:0000244|PDB:1NJ8}. FT STRAND 348 353 {ECO:0000244|PDB:1NJ8}. FT TURN 354 356 {ECO:0000244|PDB:1NJ8}. FT STRAND 359 363 {ECO:0000244|PDB:1NJ8}. FT HELIX 367 393 {ECO:0000244|PDB:1NJ8}. FT STRAND 394 396 {ECO:0000244|PDB:1NJ8}. FT HELIX 402 408 {ECO:0000244|PDB:1NJ8}. FT TURN 409 412 {ECO:0000244|PDB:1NJ8}. FT STRAND 414 419 {ECO:0000244|PDB:1NJ8}. FT HELIX 422 424 {ECO:0000244|PDB:1NJ8}. FT HELIX 427 433 {ECO:0000244|PDB:1NJ8}. FT STRAND 437 442 {ECO:0000244|PDB:1NJ8}. FT STRAND 444 452 {ECO:0000244|PDB:1NJ8}. SQ SEQUENCE 455 AA; 53309 MW; 3D155A36AFE0CC3B CRC64; MEFSEWYSDI LEKAEIYDVR YPIKGCGVYL PYGFKIRRYT FEIIRNLLDE SGHDEALFPM LIPEDLLAKE AEHIKGFEDE VYWVTHGGKT QLDVKLALRP TSETPIYYMM KLWVKVHTDL PIKIYQIVNT FRYETKHTRP LIRLREIMTF KEAHTAHSTK EEAENQVKEA ISIYKKFFDT LGIPYLISKR PEWDKFPGAE YTMAFDTIFP DGRTMQIATV HNLGQNFSKT FEIIFETPTG DKDYAYQTCY GISDRVIASI IAIHGDEKGL ILPPIVAPIQ VVIVPLIFKG KEDIVMEKAK EIYEKLKGKF RVHIDDRDIR PGRKFNDWEI KGVPLRIEVG PKDIENKKIT LFRRDTMEKF QVDETQLMEV VEKTLNNIME NIKNRAWEKF ENFITILEDI NPDEIKNILS EKRGVILVPF KEEIYNEELE EKVEATILGE TEYKGNKYIA IAKTY // ID SURE_METJA Reviewed; 266 AA. AC Q57979; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 98. DE RecName: Full=5'-nucleotidase SurE {ECO:0000255|HAMAP-Rule:MF_00060}; DE EC=3.1.3.5 {ECO:0000255|HAMAP-Rule:MF_00060}; DE AltName: Full=Nucleoside 5'-monophosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00060}; GN Name=surE {ECO:0000255|HAMAP-Rule:MF_00060}; OrderedLocusNames=MJ0559; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Nucleotidase that shows phosphatase activity on CC nucleoside 5'-monophosphates. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- CATALYTIC ACTIVITY: A 5'-ribonucleotide + H(2)O = a ribonucleoside CC + phosphate. {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00060}; CC Note=Binds 1 divalent metal cation per subunit. CC {ECO:0000255|HAMAP-Rule:MF_00060}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- SIMILARITY: Belongs to the SurE nucleotidase family. CC {ECO:0000255|HAMAP-Rule:MF_00060}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98553.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98553.1; ALT_INIT; Genomic_DNA. DR PIR; G64369; G64369. DR ProteinModelPortal; Q57979; -. DR STRING; 243232.MJ_0559; -. DR EnsemblBacteria; AAB98553; AAB98553; MJ_0559. DR KEGG; mja:MJ_0559; -. DR eggNOG; arCOG02303; Archaea. DR eggNOG; COG0496; LUCA. DR InParanoid; Q57979; -. DR KO; K03787; -. DR OMA; NTSLQVI; -. DR PhylomeDB; Q57979; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008253; F:5'-nucleotidase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.1210.10; -; 1. DR HAMAP; MF_00060; SurE; 1. DR InterPro; IPR030048; SurE. DR InterPro; IPR002828; SurE-like_Pase/nucleotidase. DR Pfam; PF01975; SurE; 1. DR SUPFAM; SSF64167; SSF64167; 1. DR TIGRFAMs; TIGR00087; surE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Hydrolase; Metal-binding; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 266 5'-nucleotidase SurE. FT /FTId=PRO_0000111864. FT METAL 8 8 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 9 9 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 42 42 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. FT METAL 98 98 Divalent metal cation. FT {ECO:0000255|HAMAP-Rule:MF_00060}. SQ SEQUENCE 266 AA; 29771 MW; A5D5D497F15D7281 CRC64; MEILIVNDDG IYSPSLIALY NALKEKFSDA NITIVAPTNQ QSGIGRAISL FEPLRMTKVK LAKDIVGYAV SGTPTDCVIL GIYQILKKVP DLVISGINIG ENLGTEIMTS GTLGAAFEAA HHGAKSIASS LQITSDHLKF KELDIPINFE IPAKITAKIA EKYLDYDMPC DVLNINIPEN ATLETPIEIT RLARKMYTTH VEERIDPRGR SYYWIDGYPI FEEEEDTDVY VLRKKRHISI TPLTLDTTIK NLDEFKEKYG KILCEM // ID SYS2_METJA Reviewed; 521 AA. AC Q58477; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 97. DE RecName: Full=Type-2 serine--tRNA ligase; DE EC=6.1.1.11; DE AltName: Full=Seryl-tRNA synthetase; DE Short=SerRS; DE AltName: Full=Seryl-tRNA(Ser/Sec) synthetase; GN Name=serS; OrderedLocusNames=MJ1077; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, SUBUNIT, AND TEMPERATURE DEPENDENCE. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=14764085; DOI=10.1111/j.1432-1033.2003.03971.x; RA Bilokapic S., Korencic D., Soell D., Weygand-Durasevic I.; RT "The unusual methanogenic seryl-tRNA synthetase recognizes tRNASer RT species from all three kingdoms of life."; RL Eur. J. Biochem. 271:694-702(2004). CC -!- FUNCTION: Catalyzes the attachment of serine to tRNA(Ser). Is also CC able to aminoacylate tRNA(Sec) with serine, to form the CC misacylated tRNA L-seryl-tRNA(Sec), which will be further CC converted into selenocysteinyl-tRNA(Sec). CC {ECO:0000269|PubMed:14764085}. CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Ser) = AMP + diphosphate CC + L-seryl-tRNA(Ser). CC -!- CATALYTIC ACTIVITY: ATP + L-serine + tRNA(Sec) = AMP + diphosphate CC + L-seryl-tRNA(Sec). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 Zn(2+) ion per subunit. This ion is coordinated with CC 2 cysteines, 1 glutamate and a water molecule that dissociates CC from the zinc ion to allow the coordination of the amino group of CC the serine substrate, which is essential for catalysis. CC {ECO:0000250}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC Thermostable. Fully active at 80 degrees Celsius. CC {ECO:0000269|PubMed:14764085}; CC -!- PATHWAY: Aminoacyl-tRNA biosynthesis; selenocysteinyl-tRNA(Sec) CC biosynthesis; L-seryl-tRNA(Sec) from L-serine and tRNA(Sec): step CC 1/1. CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14764085}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- DOMAIN: Consists of two distinct domains, a catalytic core and a CC N-terminal extension that is presumably involved in tRNA binding. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Type-2 seryl-tRNA synthetase subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99075.1; -; Genomic_DNA. DR PIR; D64434; D64434. DR ProteinModelPortal; Q58477; -. DR STRING; 243232.MJ_1077; -. DR EnsemblBacteria; AAB99075; AAB99075; MJ_1077. DR KEGG; mja:MJ_1077; -. DR eggNOG; arCOG00403; Archaea. DR eggNOG; COG0172; LUCA. DR InParanoid; Q58477; -. DR KO; K01875; -. DR OMA; AQCEPFY; -. DR UniPathway; UPA00906; UER00895. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004828; F:serine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016260; P:selenocysteine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0006434; P:seryl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01278; Ser_tRNA_synth_type2; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR004503; Ser-tRNA-ligase_IIa_arc. DR Pfam; PF00587; tRNA-synt_2b; 1. DR TIGRFAMs; TIGR00415; serS_MJ; 1. PE 1: Evidence at protein level; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 521 Type-2 serine--tRNA ligase. FT /FTId=PRO_0000122174. FT NP_BIND 347 349 ATP. {ECO:0000250}. FT NP_BIND 358 359 ATP. {ECO:0000250}. FT REGION 364 366 Serine binding. {ECO:0000250}. FT METAL 318 318 Zinc; catalytic. {ECO:0000250}. FT METAL 366 366 Zinc; catalytic. {ECO:0000250}. FT METAL 473 473 Zinc; catalytic. {ECO:0000250}. FT BINDING 316 316 Serine; via carbonyl oxygen. FT {ECO:0000250}. FT BINDING 347 347 Serine. {ECO:0000250}. FT BINDING 480 480 ATP. {ECO:0000250}. SQ SEQUENCE 521 AA; 60632 MW; E8D40DB16915B4FE CRC64; MKLTFDLDGK IIFSKELSEE AKNAVEEVLK NADSIFLKGV PKGKENEASK IKSYEFEGNI LKLKIASGTY TRAHEGLIRL RKPLAEKLGR NFRIGVRGIE IDNYVITIET DEDKAKKLEG IKVPECEAKV EGNKIILTFK DIGESELKRN IIDRAIKFVK TELEKEEEDL TFKVCKIPPG TIVSEYKAKR KITFDKDPTD VAEKLGWVKK FPGRGQWFYT PPITALFRAL EELIVEEVVK KIGFQECLFP KLIPLEIMYK MRYLEGLPEG MYYVCPPKRE PELFKEFVNE MMIKKEIPIE KLKNLLRDPG YVLAPAQCEP FYQFFEGEVI DVDKPIMFFD RSGWTYRWEG GGARGLDRVN EFLRVECVWI GSPEFVEETR DKTLKYAEKL AEKLDLEYWV EVGDDPFYLE GRKKEDRGIE FPDVPKYEMR LWLPHIKDER KGVAVTSANV HGTHFVEGFR IKDYKGRRVW TGCTGYGITR WVVGYLAQYG FNFDDWHPII KKKIKKLPEV PQLITWPKKD E // ID SYV_METJA Reviewed; 878 AA. AC Q58413; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Valine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02005}; DE EC=6.1.1.9 {ECO:0000255|HAMAP-Rule:MF_02005}; DE AltName: Full=Valyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02005}; DE Short=ValRS {ECO:0000255|HAMAP-Rule:MF_02005}; GN Name=valS {ECO:0000255|HAMAP-Rule:MF_02005}; OrderedLocusNames=MJ1007; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the attachment of valine to tRNA(Val). As CC ValRS can inadvertently accommodate and process structurally CC similar amino acids such as threonine, to avoid such errors, it CC has a "posttransfer" editing activity that hydrolyzes mischarged CC Thr-tRNA(Val) in a tRNA-dependent manner. {ECO:0000255|HAMAP- CC Rule:MF_02005}. CC -!- CATALYTIC ACTIVITY: ATP + L-valine + tRNA(Val) = AMP + diphosphate CC + L-valyl-tRNA(Val). {ECO:0000255|HAMAP-Rule:MF_02005}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02005}. CC -!- DOMAIN: ValRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated threonine is CC translocated from the active site to the editing site. CC {ECO:0000255|HAMAP-Rule:MF_02005}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. ValS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02005}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99009.1; -; Genomic_DNA. DR PIR; F64425; F64425. DR ProteinModelPortal; Q58413; -. DR STRING; 243232.MJ_1007; -. DR EnsemblBacteria; AAB99009; AAB99009; MJ_1007. DR KEGG; mja:MJ_1007; -. DR eggNOG; arCOG00808; Archaea. DR eggNOG; COG0525; LUCA. DR InParanoid; Q58413; -. DR KO; K01873; -. DR OMA; SENSIHI; -. DR PhylomeDB; Q58413; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006438; P:valyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02005; Val_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR InterPro; IPR022874; Valine-tRNA_ligase_type_2. DR InterPro; IPR002303; Valyl-tRNA_ligase. DR PANTHER; PTHR11946:SF5; PTHR11946:SF5; 1. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00986; TRNASYNTHVAL. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00422; valS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 878 Valine--tRNA ligase. FT /FTId=PRO_0000106249. FT MOTIF 43 53 "HIGH" region. FT MOTIF 527 531 "KMSKS" region. FT BINDING 530 530 ATP. {ECO:0000255|HAMAP-Rule:MF_02005}. SQ SEQUENCE 878 AA; 102572 MW; 4D78BCA0D1F2022E CRC64; MEMPKDYNIE IEKQIQKKWE ESKIYKFDEE SNKPPYIIDT PPPYPTGRLH LGHALNWTYM DIIARYKRMK GFNVLFPQGW DCHGLPTEVK VEEIHGITKS DVDRHKFREL CIELTKENIE KMRRQIKSLG ISIDWDKEYI TMTPEYIKKS QTAFVRMYKD GLIYRGKFPV NWCPRCQTAI AFAEVEYKER ESKLNYIKFP AADGEGHLLI ATTRPELMAA CVAILVHPED ERYKHLIGKE FIVPLFGHKV KLLADEDVEK EFGTGAVMVC TFGDKTDVLW VNRHKLEIKK AIDEKGELTE IAGKYKGLKT EEAREKIIED LKKEGYLVKQ EPIKQNVGVC WRCKTPIEII VTEQWFVNVR KLIPKVREVA DEIKWIPEHM KIRLLNWIED MDWDWVISRQ RIFATPIPVW YCPKCGNVVV AKEEDLPIDP TKTGYVCDKC GNKDLIPETD VLDTWMDSSI TPMVITKWLD DDKFFEKHYP VQLRPQGHDI IRTWAFYTIV KSVALTGKKP WDEIVINGMV FGEDGHKMSK SRGNVVEPDE IIAKYGADAL RLWASNSVVG DDVQFLWKEV DYGYRFLRKS WNACRFAKMH ISDDIIDELK KPMEISNPID LWILSKLQRL IERVDKDLEN YRFNTIVEIY KFVWHEFCDN YIEMVKYRLY GDDEEAKKEA RWTLYYVIDK VVRLLCPFAP HFSDYIAEIY KIDNLHFSFP EVDNRFINEE AEKFGEIAKN TVISIRRFKA NSGMALNAPL KYVEIYTEDE ETYLALNKTA EDIKGTLKIE ELKIIKGKPA LESKIVEIIP DKSKIGPEFK KNAKAVMDLI KNADEETLEK IINEGLETEY GVIRKEHIKD VKRALFCEGE EVDSVDIEGV LAMAIIRK // ID SYW_METJA Reviewed; 370 AA. AC Q58810; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Tryptophan--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00140}; DE EC=6.1.1.2 {ECO:0000255|HAMAP-Rule:MF_00140}; DE AltName: Full=Tryptophanyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00140}; DE Short=TrpRS {ECO:0000255|HAMAP-Rule:MF_00140}; GN Name=trpS {ECO:0000255|HAMAP-Rule:MF_00140}; OrderedLocusNames=MJ1415; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-tryptophan + tRNA(Trp) = AMP + CC diphosphate + L-tryptophyl-tRNA(Trp). {ECO:0000255|HAMAP- CC Rule:MF_00140}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00140}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00140}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99425.1; -; Genomic_DNA. DR PIR; F64476; F64476. DR ProteinModelPortal; Q58810; -. DR STRING; 243232.MJ_1415; -. DR EnsemblBacteria; AAB99425; AAB99425; MJ_1415. DR KEGG; mja:MJ_1415; -. DR eggNOG; arCOG01887; Archaea. DR eggNOG; COG0180; LUCA. DR InParanoid; Q58810; -. DR KO; K01867; -. DR OMA; FFFSHRD; -. DR PhylomeDB; Q58810; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004830; F:tryptophan-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006436; P:tryptophanyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00140_A; Trp_tRNA_synth_A; 1. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002306; Trp-tRNA-ligase. DR InterPro; IPR020653; Tryptophan-tRNA-ligase_arc. DR PANTHER; PTHR10055; PTHR10055; 1. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PRINTS; PR01039; TRNASYNTHTRP. DR TIGRFAMs; TIGR00233; trpS; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 370 Tryptophan--tRNA ligase. FT /FTId=PRO_0000136723. FT MOTIF 75 83 "HIGH" region. FT MOTIF 255 259 "KMSKS" region. SQ SEQUENCE 370 AA; 42661 MW; E6C71107CF82B59D CRC64; MKLMELTPWE TPAVIDYKKT MEQFGVKPIV DVLGDLKEEH HFFRRNIILG HRDFERIVDA IKNNKEFAVV SGMMPSGKMH FGHKMVVDLL KFYQKYTDNI NIPIADLEAY WARNMSFETT KELALNEYIT NYIALGLDPE KINVYLQSKY QKVKDLALIL SKRTNWSEMK AIYGFKGETN IGHVFAPIVQ VADILHPQLD ENLSPEPKPV VVPVGIDQDP HIRLTRDIAN RAKEFKFIPP SSTYHRFMTG LLGGKMSSSK PETAIFLTDD EKTVKKKIFS AKTGGRETLE EHKKYGGVPE ECVVYELFLY HLILDDKELA EIYQKCRSGE LTCGKCKKMA YERVVEFLKD LKEKREQAKE IAVKILEGKY // ID T1SH_METJA Reviewed; 432 AA. AC Q60296; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative type-1 restriction enzyme MjaXP specificity protein; DE Short=S.MjaXP; DE AltName: Full=Type I restriction enzyme MjaXP specificity protein; DE Short=S protein; GN OrderedLocusNames=MJECL41; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of bipartite DNA recognition sequence. Subunit S dictates CC DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37110.1; -; Genomic_DNA. DR PIR; H64514; H64514. DR ProteinModelPortal; Q60296; -. DR REBASE; 3909; S.MjaORFCL42P. DR EnsemblBacteria; AAC37110; AAC37110; MJ_ECL41. DR KEGG; mja:MJECL41; -. DR HOGENOM; HOG000002669; -. DR InParanoid; Q60296; -. DR KO; K01154; -. DR OMA; TRASCES; -. DR PhylomeDB; Q60296; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Plasmid; Reference proteome; KW Restriction system. FT CHAIN 1 432 Putative type-1 restriction enzyme MjaXP FT specificity protein. FT /FTId=PRO_0000198053. SQ SEQUENCE 432 AA; 50160 MW; 84CD44CF20EBC42C CRC64; MLFMVKFRWE TEFKETDIGK IPKDWDVKKI KDIGEVAGGS TPSTKIKEYW GGDIPWITPK DLANYEYIYI SRGERNITEK AVKECSLRIF PKGTILLTSR APIGYVAIAK NPLTTNQGFR NIIPKDGVVS EYLYYLFKTK TMSEYLKDIS GGSTFPELKG STLKEVEIPY PSPEEQQKIA TVLSYFDDLI ENKKKQNEIL EKIALELFKN WFIDFEPFKN EEFVYNDELD KEIPKGWEVK RLGDILKVES GSNAPQREIY FENAKIPFVR VKHLVKGVCI ESSDFINELA LKDYKMKLYN EKSIIFQKSG ESLKEARVNI VPFKFTAVNH LAVIDSSMLN EKHYFIYCLL RFLLKEIVYS VKGTTLPYLK ISDIENKYII IPPQPILQKF HSLVQPLFEK IINNQKQIMV LKKIRDALLP KLVFGELRVE EL // ID SYFA_METJA Reviewed; 480 AA. AC Q57911; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Phenylalanine--tRNA ligase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282}; DE EC=6.1.1.20 {ECO:0000255|HAMAP-Rule:MF_00282}; DE AltName: Full=Phenylalanyl-tRNA synthetase alpha subunit {ECO:0000255|HAMAP-Rule:MF_00282}; DE Short=PheRS {ECO:0000255|HAMAP-Rule:MF_00282}; GN Name=pheS {ECO:0000255|HAMAP-Rule:MF_00282}; OrderedLocusNames=MJ0487; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-phenylalanine + tRNA(Phe) = AMP + CC diphosphate + L-phenylalanyl-tRNA(Phe). {ECO:0000255|HAMAP- CC Rule:MF_00282}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00282}; CC Note=Binds 2 magnesium ions per tetramer. {ECO:0000255|HAMAP- CC Rule:MF_00282}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000255|HAMAP-Rule:MF_00282}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00282}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. Phe-tRNA synthetase alpha subunit type 2 subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00282}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98478.1; -; Genomic_DNA. DR PIR; G64360; G64360. DR ProteinModelPortal; Q57911; -. DR STRING; 243232.MJ_0487; -. DR PRIDE; Q57911; -. DR EnsemblBacteria; AAB98478; AAB98478; MJ_0487. DR KEGG; mja:MJ_0487; -. DR eggNOG; arCOG00410; Archaea. DR eggNOG; COG0016; LUCA. DR InParanoid; Q57911; -. DR KO; K01889; -. DR OMA; PEFYQCE; -. DR PhylomeDB; Q57911; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IBA:GO_Central. DR HAMAP; MF_00282; Phe_tRNA_synth_alpha2; 1. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004529; Phe-tRNA-synth_IIc_asu. DR InterPro; IPR022917; Phe_tRNA_ligase_alpha_bac/arc. DR InterPro; IPR002319; Phenylalanyl-tRNA_Synthase. DR Pfam; PF01409; tRNA-synt_2d; 1. DR TIGRFAMs; TIGR00468; pheS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Magnesium; Metal-binding; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 480 Phenylalanine--tRNA ligase alpha subunit. FT /FTId=PRO_0000126810. SQ SEQUENCE 480 AA; 57027 MW; 1DC2599CF0D97B72 CRC64; MELHIDEKRL LKIFQDNNRD EFNLNELEKF MPKEKILRVS LWLKGKNLVE TEEKVKKIIK LIKEEEFPER KIANYLKQHN IKEIEIKNLK DILPKEEINA ALGAIKRKGI ARIEKGKIIF DNLDYKDVEE QLLQKIKENK YLDDFSEEEK KIIDILKKRG YVDFDEEKEI KIKLTEKGKE FIKNPIEIEE EITQLTRDII ISGKWKKAYI RPYDVKVPTK PIYPAKVHPL TRIIREVKEI LLAMGFKEVK SPIVETEFWN FDMLFEPQDH PAREMQDTFF LKYPNEGDIP EDLLSKVKEV HERCWKYKFD ENVSRRLILR THTTASSIRY LASLSDEEKN KPHKVFCIDR VFRNEAIDYK HLPEFYQCEG IIMDDNVNFN NLIGVLKEFL NRLGFEKVRF RPAYFPFTEP SLEAEVYLEG KGWLEILGAG IFRPEVLEPI GIEKPVLAWG IGFSRLAMLR YGLTDIRDLH KNDLDWLKRV // ID SYI_METJA Reviewed; 1039 AA. AC Q58357; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Isoleucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_02003}; DE EC=6.1.1.5 {ECO:0000255|HAMAP-Rule:MF_02003}; DE AltName: Full=Isoleucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_02003}; DE Short=IleRS {ECO:0000255|HAMAP-Rule:MF_02003}; GN Name=ileS {ECO:0000255|HAMAP-Rule:MF_02003}; OrderedLocusNames=MJ0947; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the attachment of isoleucine to tRNA(Ile). As CC IleRS can inadvertently accommodate and process structurally CC similar amino acids such as valine, to avoid such errors it has CC two additional distinct tRNA(Ile)-dependent editing activities. CC One activity is designated as 'pretransfer' editing and involves CC the hydrolysis of activated Val-AMP. The other activity is CC designated 'posttransfer' editing and involves deacylation of CC mischarged Val-tRNA(Ile). {ECO:0000255|HAMAP-Rule:MF_02003}. CC -!- CATALYTIC ACTIVITY: ATP + L-isoleucine + tRNA(Ile) = AMP + CC diphosphate + L-isoleucyl-tRNA(Ile). {ECO:0000255|HAMAP- CC Rule:MF_02003}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_02003}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_02003}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_02003}. CC -!- DOMAIN: IleRS has two distinct active sites: one for CC aminoacylation and one for editing. The misactivated valine is CC translocated from the active site to the editing site, which CC sterically excludes the correctly activated isoleucine. The single CC editing site contains two valyl binding pockets, one specific for CC each substrate (Val-AMP or Val-tRNA(Ile)). {ECO:0000255|HAMAP- CC Rule:MF_02003}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. IleS type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_02003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98949.1; -; Genomic_DNA. DR PIR; C64418; C64418. DR ProteinModelPortal; Q58357; -. DR STRING; 243232.MJ_0947; -. DR EnsemblBacteria; AAB98949; AAB98949; MJ_0947. DR KEGG; mja:MJ_0947; -. DR eggNOG; arCOG00807; Archaea. DR eggNOG; COG0060; LUCA. DR InParanoid; Q58357; -. DR KO; K01870; -. DR OMA; IWICEEC; -. DR PhylomeDB; Q58357; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004822; F:isoleucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006428; P:isoleucyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_02003; Ile_tRNA_synth_type2; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR002301; Ile-tRNA-ligase. DR InterPro; IPR023586; Ile-tRNA-ligase_type2. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR PRINTS; PR00984; TRNASYNTHILE. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 1. DR TIGRFAMs; TIGR00392; ileS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; Zinc. FT CHAIN 1 1039 Isoleucine--tRNA ligase. FT /FTId=PRO_0000098580. FT MOTIF 46 56 "HIGH" region. FT MOTIF 600 604 "KMSKS" region. FT BINDING 603 603 ATP. {ECO:0000255|HAMAP-Rule:MF_02003}. SQ SEQUENCE 1039 AA; 122234 MW; 7163C46B4AE08AC0 CRC64; MKKVEPVNFR ELDKKIKKFW EENDIYQKVK KKNERNKEFY FVDGPPYCSG AIHLGTAWNK IIKDTYLRFK RMQGYNVLDK AGWDMHGLPI EVKVENEFGI KNKKEIETKI GVKQFIEKCK EFALKHKEIM EKQFKNLGVW LDWENAYMPI TKEYMEIGWW TLKVAHEKGL LTRDLRVVYW CPRCETALAE HEVRGEYKEV YDPSVYVKFR LANEENTYIV IWTTTPWTLV ANLAVTVHPD YDYAYVEVEF DDKKEVWIIA EKLVEEVINK AKKFHNIKNY KIIKKVKGKE LEGIKYIHPL LEENERQKEF AELENAHTVI LGEHVTLEGG TGLVHTAPGH GEEDFEVGKK YNLPIYSPID DEGKYVEGKW KGVFVKDADA EIIETLKNKG LLVYAGKIKH SYPHCWRCKT PLLFRATEQW FLEISKIKDN IIEHAKTVQW IPHWVETRYI NGVKFVGDWN ISRQRYWGIP IPVWVCEKCG KYIVVGSVEE LEEKMINKDE VGEINDLHKP TVDKIKLRCE CGGEMKRVPD VLDVWFDSGL APYASIGVKE LKKADFITEG HDQVTKWFYS QHALSAIVFN DIPYKKCLMH GFTLDEHGDK MSKSLGNVVN PDDVVEKYGA DLLRFYLLSA NKVWEDLRFV WSEMDDVLSL FNTLWNAYMF AVNYMVLDNF KPDEKYFEYL KDEDRWIVSR INSVAKIAIE NLEVPYFHTY TWTLKDFILN DLSRWYIRLI RDRTWKEKDD ADKLAAYQTL YYVLLKLATI LAPVAPHTAE AIYQNLKTED MEESIFMNKI EVDEEFIDEE LERDMAIVRD VVDAIYRGRD RIKYTLRYPL KEITIAGGEE VKKAVERFEY IIKEQGNVKN IKFGEVEGSK YIIKPNYREL GKRYRSEVPK VVEALNKADA KELMERLKEG AVILDGYEIK PEYVEIRLEI PEHIAGVEFS KGTVFINTEI TDDLIKEGLM REVIRRIQAM RKDMDLDIEE KIKIKVEGID LDEFKEIIER EVRGQFVDEI KADYEKDWEI KTPNGEKYNV KIAIERINK // ID SYT_METJA Reviewed; 620 AA. AC Q58597; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 105. DE RecName: Full=Threonine--tRNA ligase; DE EC=6.1.1.3; DE AltName: Full=Threonyl-tRNA synthetase; DE Short=ThrRS; GN Name=thrS; OrderedLocusNames=MJ1197; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-threonine + tRNA(Thr) = AMP + CC diphosphate + L-threonyl-tRNA(Thr). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99201.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99201.1; ALT_INIT; Genomic_DNA. DR PIR; D64449; D64449. DR PDB; 4RRF; X-ray; 1.70 A; A/B/C/D/E/F=1-141. DR PDB; 4RRG; X-ray; 1.93 A; A/B/C/D=1-141. DR PDBsum; 4RRF; -. DR PDBsum; 4RRG; -. DR ProteinModelPortal; Q58597; -. DR SMR; Q58597; 1-139. DR STRING; 243232.MJ_1197; -. DR PRIDE; Q58597; -. DR DNASU; 1452092; -. DR EnsemblBacteria; AAB99201; AAB99201; MJ_1197. DR KEGG; mja:MJ_1197; -. DR eggNOG; arCOG00401; Archaea. DR eggNOG; COG0441; LUCA. DR InParanoid; Q58597; -. DR KO; K01868; -. DR OMA; MYELTRY; -. DR PhylomeDB; Q58597; -. DR BRENDA; 6.1.1.3; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004829; F:threonine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006435; P:threonyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00184; Thr_tRNA_synth; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR002320; Thr-tRNA-ligase_IIa. DR InterPro; IPR015011; Threonyl-tRNA_syn_edit_dom_arc. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR Pfam; PF08915; tRNA-Thr_ED; 1. DR PRINTS; PR01047; TRNASYNTHTHR. DR ProDom; PD016189; tRNA-Thr_ED_arc; 1. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00418; thrS; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Metal-binding; KW Nucleotide-binding; Protein biosynthesis; Reference proteome; Zinc. FT CHAIN 1 620 Threonine--tRNA ligase. FT /FTId=PRO_0000101101. FT REGION 197 496 Catalytic. FT METAL 289 289 Zinc; catalytic. {ECO:0000250}. FT METAL 341 341 Zinc; catalytic. {ECO:0000250}. FT METAL 465 465 Zinc; catalytic. {ECO:0000250}. FT STRAND 2 18 {ECO:0000244|PDB:4RRF}. FT STRAND 28 41 {ECO:0000244|PDB:4RRF}. FT HELIX 44 48 {ECO:0000244|PDB:4RRF}. FT HELIX 50 68 {ECO:0000244|PDB:4RRF}. FT STRAND 72 77 {ECO:0000244|PDB:4RRF}. FT HELIX 79 81 {ECO:0000244|PDB:4RRF}. FT STRAND 83 85 {ECO:0000244|PDB:4RRF}. FT HELIX 88 104 {ECO:0000244|PDB:4RRF}. FT STRAND 108 111 {ECO:0000244|PDB:4RRF}. FT STRAND 116 124 {ECO:0000244|PDB:4RRF}. FT STRAND 130 135 {ECO:0000244|PDB:4RRF}. SQ SEQUENCE 620 AA; 72357 MW; 514D190E790F64F6 CRC64; MKMLLIHSDY LEFEAKEKTK IAEETENLKG KLDECLACFI AVEREDENNP EGTAIGAVEE IEKVANQLKV NNIVVYPYAH LSSDLSSPET AVKVLKDIES ILKERGYNVL RAPFGWYKAF KISCKGHPLS ELSRKIVAKE EKKEEGEESK FYLLNPETEE IIELNENNIN IIKDEELLAL AKHELGIREH KEHDEPPHVK FIKEKDICSY EEASDPGHFR WYPKGKLMRD LLADYVYNLV VNMGAMPVET PIMYDLGNPA IREHADKFGE RQYRFRQGNK ELMLRFAACF GQFMMKKDMY LLPRYLPLKL YELSTYSFRY EQRGELVGLK RLRCFTMPDM HTVCLNLEQA MEEFEKQFWE CLKTGDDLNL SYSVIFRFTK DFFDEHRDWF FKIAKEYKNK YGKDVILEIL PKRKHYWVGK VDIAVIDSLG RPIENPTVQI DVESAKRFDI KVHTNEGEIY PIILHCSPTG SIERVLCGLL EKAAIEAEKG NAPMLPVWLS PIQVRVIPVA ERHYDYALKV AEKLRENNIR ADFDDREESV SKKIRNAGKE WVPYVVVIGD EEMESDKLTV TIREKSTLKK PYKEKMTLDE LIERIKKETA NYPYRPLPLP IRCSLQPKFH // ID SYY_METJA Reviewed; 306 AA. AC Q57834; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 114. DE RecName: Full=Tyrosine--tRNA ligase; DE EC=6.1.1.1; DE AltName: Full=Tyrosyl-tRNA synthetase; DE Short=TyrRS; GN Name=tyrS; OrderedLocusNames=MJ0389; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, SUBUNIT, AND KINETIC PARAMETERS. RX PubMed=10585437; DOI=10.1074/jbc.274.50.35601; RA Steer B.A., Schimmel P.; RT "Major anticodon-binding region missing from an archaebacterial tRNA RT synthetase."; RL J. Biol. Chem. 274:35601-35606(1999). RN [3] RP MUTAGENESIS OF ASP-286 AND LYS-288. RX PubMed=10570126; DOI=10.1073/pnas.96.24.13644; RA Steer B.A., Schimmel P.; RT "Domain-domain communication in a miniature archaebacterial tRNA RT synthetase."; RL Proc. Natl. Acad. Sci. U.S.A. 96:13644-13649(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS) IN COMPLEX WITH TRNA(TYR) AND RP TYROSINE, MUTAGENESIS OF ASP-286, AND SUBUNIT. RX PubMed=12754495; DOI=10.1038/nsb934; RA Kobayashi T., Nureki O., Ishitani R., Yaremchuk A., Tukalo M., RA Cusack S., Sakamoto K., Yokoyama S.; RT "Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA RT synthetases for genetic code expansion."; RL Nat. Struct. Biol. 10:425-432(2003). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.66 ANGSTROMS) OF WILD-TYPE AND RP O-METHYL-TYROSINE-SPECIFIC MUTANT APOENZYME. RX PubMed=15840835; DOI=10.1110/ps.041239305; RA Zhang Y., Wang L., Schultz P.G., Wilson I.A.; RT "Crystal structures of apo wild-type M. jannaschii tyrosyl-tRNA RT synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L- RT tyrosine."; RL Protein Sci. 14:1340-1349(2005). CC -!- FUNCTION: Catalyzes the attachment of tyrosine to tRNA(Tyr) in a CC two-step reaction: tyrosine is first activated by ATP to form Tyr- CC AMP and then transferred to the acceptor end of tRNA(Tyr). CC {ECO:0000269|PubMed:10585437}. CC -!- CATALYTIC ACTIVITY: ATP + L-tyrosine + tRNA(Tyr) = AMP + CC diphosphate + L-tyrosyl-tRNA(Tyr). CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=15 uM for tRNA(Tyr) (at 45 degrees Celsius) CC {ECO:0000269|PubMed:10585437}; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10585437, CC ECO:0000269|PubMed:12754495}. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. TyrS type 3 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98375.1; -; Genomic_DNA. DR PIR; E64348; E64348. DR PDB; 1J1U; X-ray; 1.95 A; A=1-306. DR PDB; 1U7D; X-ray; 2.65 A; A/B=1-306. DR PDB; 1U7X; X-ray; 3.00 A; A/B=1-306. DR PDB; 1ZH0; X-ray; 1.90 A; A=1-306. DR PDB; 1ZH6; X-ray; 2.50 A; A=1-306. DR PDB; 2AG6; X-ray; 1.90 A; A=1-306. DR PDB; 2HGZ; X-ray; 2.50 A; A=2-306. DR PDB; 2PXH; X-ray; 1.97 A; A=1-306. DR PDB; 2ZP1; X-ray; 1.70 A; A=1-306. DR PDB; 3D6U; X-ray; 2.20 A; A=1-306. DR PDB; 3D6V; X-ray; 2.20 A; A=1-306. DR PDB; 3N2Y; X-ray; 2.49 A; A/B=1-306. DR PDB; 3QE4; X-ray; 2.30 A; A/B=1-306. DR PDB; 4HJR; X-ray; 2.50 A; A/B=1-306. DR PDB; 4HJX; X-ray; 2.91 A; A/B=1-306. DR PDB; 4HK4; X-ray; 2.30 A; A=1-306. DR PDB; 4HPW; X-ray; 2.00 A; A=1-306. DR PDB; 4ND6; X-ray; 2.00 A; A=1-306. DR PDB; 4ND7; X-ray; 2.00 A; A=1-306. DR PDB; 4NDA; X-ray; 1.70 A; A=1-306. DR PDB; 4NX2; X-ray; 2.00 A; A=1-306. DR PDB; 4PBR; X-ray; 1.90 A; A=1-306. DR PDB; 4PBS; X-ray; 2.01 A; A=1-306. DR PDB; 4PBT; X-ray; 1.90 A; A=1-306. DR PDBsum; 1J1U; -. DR PDBsum; 1U7D; -. DR PDBsum; 1U7X; -. DR PDBsum; 1ZH0; -. DR PDBsum; 1ZH6; -. DR PDBsum; 2AG6; -. DR PDBsum; 2HGZ; -. DR PDBsum; 2PXH; -. DR PDBsum; 2ZP1; -. DR PDBsum; 3D6U; -. DR PDBsum; 3D6V; -. DR PDBsum; 3N2Y; -. DR PDBsum; 3QE4; -. DR PDBsum; 4HJR; -. DR PDBsum; 4HJX; -. DR PDBsum; 4HK4; -. DR PDBsum; 4HPW; -. DR PDBsum; 4ND6; -. DR PDBsum; 4ND7; -. DR PDBsum; 4NDA; -. DR PDBsum; 4NX2; -. DR PDBsum; 4PBR; -. DR PDBsum; 4PBS; -. DR PDBsum; 4PBT; -. DR ProteinModelPortal; Q57834; -. DR SMR; Q57834; 1-306. DR STRING; 243232.MJ_0389; -. DR EnsemblBacteria; AAB98375; AAB98375; MJ_0389. DR KEGG; mja:MJ_0389; -. DR eggNOG; arCOG01886; Archaea. DR eggNOG; COG0162; LUCA. DR InParanoid; Q57834; -. DR KO; K01866; -. DR OMA; FEYHVFP; -. DR PhylomeDB; Q57834; -. DR BRENDA; 6.1.1.1; 3260. DR EvolutionaryTrace; Q57834; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004831; F:tyrosine-tRNA ligase activity; IEA:UniProtKB-EC. DR GO; GO:0004832; F:valine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006437; P:tyrosyl-tRNA aminoacylation; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_02008; Tyr_tRNA_synth_type3; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002305; aa-tRNA-synth_Ic. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002307; Tyr-tRNA-ligase. DR InterPro; IPR023684; Tyr-tRNA-ligase_3. DR InterPro; IPR023617; Tyr-tRNA-ligase_arc/euk-type. DR Pfam; PF00579; tRNA-synt_1b; 1. DR PIRSF; PIRSF006588; TyrRS_arch_euk; 1. DR PRINTS; PR01040; TRNASYNTHTYR. DR TIGRFAMs; TIGR00234; tyrS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 1: Evidence at protein level; KW 3D-structure; Aminoacyl-tRNA synthetase; ATP-binding; KW Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Protein biosynthesis; Reference proteome. FT CHAIN 1 306 Tyrosine--tRNA ligase. FT /FTId=PRO_0000055669. FT REGION 151 158 Tyrosine. FT REGION 228 231 Interaction with t-RNA. FT REGION 283 288 Interaction with t-RNA. FT MOTIF 37 45 "HIGH" region. FT MOTIF 204 208 "KMSKS" region. FT BINDING 32 32 Tyrosine. {ECO:0000269|PubMed:12754495}. FT BINDING 36 36 Tyrosine. {ECO:0000269|PubMed:12754495}. FT BINDING 173 173 Tyrosine. {ECO:0000269|PubMed:12754495}. FT BINDING 207 207 ATP. {ECO:0000255}. FT SITE 143 143 Interaction with t-RNA. FT MUTAGEN 32 32 Y->Q: Confers specificity for the non- FT natural amino acid O-methyl-tyrosine; FT when associated with T-107; A-158 and P- FT 162. FT MUTAGEN 107 107 E->T: Confers specificity for the non- FT natural amino acid O-methyl-tyrosine; FT when associated with Q-32; A-158 and P- FT 162. FT MUTAGEN 158 158 D->A: Confers specificity for the non- FT natural amino acid O-methyl-tyrosine; FT when associated with Q-32; T-107 and P- FT 162. FT MUTAGEN 162 162 L->P: Confers specificity for the non- FT natural amino acid O-methyl-tyrosine; FT when associated with Q-32; T-107 and A- FT 158. FT MUTAGEN 286 286 D->A: Decreases the rate of FT aminoacylation more than 10-fold, without FT effect on tyrosyl adenylate synthesis. FT {ECO:0000269|PubMed:10570126, FT ECO:0000269|PubMed:12754495}. FT MUTAGEN 286 286 D->R: Decreases the rate of FT aminoacylation with wild-type tRNA and FT increases aminoacylation with amber FT suppressor tRNA 8-fold. Decreases FT affinity for wild-type tRNA and increases FT affinity for amber suppressor tRNA. FT {ECO:0000269|PubMed:10570126, FT ECO:0000269|PubMed:12754495}. FT MUTAGEN 288 288 K->A: Decreases the rate of FT aminoacylation more than 200-fold, FT without effect on tyrosyl adenylate FT synthesis. {ECO:0000269|PubMed:10570126}. FT HELIX 3 8 {ECO:0000244|PDB:2ZP1}. FT STRAND 12 15 {ECO:0000244|PDB:2ZP1}. FT HELIX 17 24 {ECO:0000244|PDB:2ZP1}. FT STRAND 26 35 {ECO:0000244|PDB:2ZP1}. FT HELIX 43 57 {ECO:0000244|PDB:2ZP1}. FT STRAND 60 66 {ECO:0000244|PDB:2ZP1}. FT HELIX 68 73 {ECO:0000244|PDB:2ZP1}. FT HELIX 79 95 {ECO:0000244|PDB:2ZP1}. FT STRAND 101 104 {ECO:0000244|PDB:2ZP1}. FT HELIX 105 107 {ECO:0000244|PDB:2ZP1}. FT TURN 108 110 {ECO:0000244|PDB:2ZP1}. FT HELIX 112 124 {ECO:0000244|PDB:2ZP1}. FT HELIX 127 133 {ECO:0000244|PDB:2ZP1}. FT TURN 134 137 {ECO:0000244|PDB:2ZP1}. FT HELIX 147 162 {ECO:0000244|PDB:2ZP1}. FT STRAND 165 170 {ECO:0000244|PDB:2ZP1}. FT HELIX 171 173 {ECO:0000244|PDB:2ZP1}. FT HELIX 174 183 {ECO:0000244|PDB:2ZP1}. FT STRAND 184 186 {ECO:0000244|PDB:2ZP1}. FT STRAND 189 193 {ECO:0000244|PDB:2ZP1}. FT STRAND 201 204 {ECO:0000244|PDB:2ZP1}. FT TURN 207 210 {ECO:0000244|PDB:2ZP1}. FT STRAND 214 216 {ECO:0000244|PDB:1U7X}. FT HELIX 219 228 {ECO:0000244|PDB:2ZP1}. FT HELIX 240 248 {ECO:0000244|PDB:2ZP1}. FT STRAND 251 255 {ECO:0000244|PDB:2ZP1}. FT HELIX 259 261 {ECO:0000244|PDB:2ZP1}. FT STRAND 265 269 {ECO:0000244|PDB:2ZP1}. FT HELIX 270 278 {ECO:0000244|PDB:2ZP1}. FT HELIX 284 306 {ECO:0000244|PDB:2ZP1}. SQ SEQUENCE 306 AA; 35049 MW; 1887760ABAF2DD5E CRC64; MDEFEMIKRN TSEIISEEEL REVLKKDEKS AYIGFEPSGK IHLGHYLQIK KMIDLQNAGF DIIILLADLH AYLNQKGELD EIRKIGDYNK KVFEAMGLKA KYVYGSEFQL DKDYTLNVYR LALKTTLKRA RRSMELIARE DENPKVAEVI YPIMQVNDIH YLGVDVAVGG MEQRKIHMLA RELLPKKVVC IHNPVLTGLD GEGKMSSSKG NFIAVDDSPE EIRAKIKKAY CPAGVVEGNP IMEIAKYFLE YPLTIKRPEK FGGDLTVNSY EELESLFKNK ELHPMDLKNA VAEELIKILE PIRKRL // ID T2M2_METJA Reviewed; 370 AA. AC Q58844; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Type-2 restriction enzyme MjaII; DE Short=R.MjaII; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaII; DE AltName: Full=Type II restriction enzyme MjaII; GN Name=mjaIIR; OrderedLocusNames=MJ1449; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: Recognizes the double-stranded sequence GGNCC. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99461.1; -; Genomic_DNA. DR PIR; H64480; H64480. DR STRING; 243232.MJ_1449; -. DR REBASE; 1222; MjaII. DR EnsemblBacteria; AAB99461; AAB99461; MJ_1449. DR KEGG; mja:MJ_1449; -. DR eggNOG; arCOG07628; Archaea. DR eggNOG; ENOG410XTRD; LUCA. DR InParanoid; Q58844; -. DR OMA; PNAGEMR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR019045; Restrct_endonuc_II_TdeIII. DR Pfam; PF09520; RE_TdeIII; 1. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 370 Type-2 restriction enzyme MjaII. FT /FTId=PRO_0000077333. SQ SEQUENCE 370 AA; 43911 MW; 8B4CF6208F914B33 CRC64; MPLSKNVIEK ISIETIRVLK SRFDTISDED IKIRNMPFHM AFLRAFYGKI GINDDTEALK FLTLSQWFHG LSTTLGQSYF ENIAHILSNG EKRTFKNYKI KRSVRDKISE IINDLKSGER LPNVEKENKE LREATSKNSE YVNGLEFTAD VYFEDKDKVV MIELKTVRPN AGEMRGEKQK ILYGKAYMME TKPNKKVYYF IGFPYDPTEN PENPCGYDKD RFMSSLIEFS KYFDKREVLI AEELWSFLSG EENTMKKILD IINSIAKPDF KEKFDFINTF PFINQDRLYT KDAIDEQKFK KYMDILQEWR LYSEIECAKA VKELSLLKLS SRDRRTFERL INNSMFSNNN KYNENRKMKI LELYNKYMQK // ID T2M6_METJA Reviewed; 226 AA. AC P81326; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Putative type-2 restriction enzyme MjaVIP; DE Short=R.MjaVIP; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaVIP; DE AltName: Full=Type II restriction enzyme MjaVIP; GN Name=mjaVIRP; OrderedLocusNames=MJ1208.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Recognizes the double-stranded unmethylated sequence CC CCGG. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC -!- SIMILARITY: To H.pylori HP0262. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99221.1; -; Genomic_DNA. DR REBASE; 16564; MjaVIP. DR EnsemblBacteria; AAB99221; AAB99221; MJ_1208.1. DR eggNOG; ENOG4102U9A; Archaea. DR eggNOG; ENOG4111RPA; LUCA. DR InParanoid; P81326; -. DR OMA; KRALWVH; -. DR PhylomeDB; P81326; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 226 Putative type-2 restriction enzyme FT MjaVIP. FT /FTId=PRO_0000077337. SQ SEQUENCE 226 AA; 26711 MW; 9A7B306A28A6A2F2 CRC64; MLHFGGFIME INHISKILEK EREEYIRNKV EEYLKQGFSK DDAVNKANQS WRTYIGHRIQ DVIYNLLKKF LKDSGLKVTT DKALNNRNLP EELDKVKRLI AINYGEYLFL PDADVIVYKV ENNDIKIIAI ISVKNSFRER RFETTYWKLK LKESPVTSHI KVFLATPDKD NEISYKCPNG KPKKMRIILE YELDGIYFLK EDFEETEKAK HFGKIVEDII EISKKL // ID SYG_METJA Reviewed; 577 AA. AC Q57681; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 100. DE RecName: Full=Glycine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00253}; DE EC=6.1.1.14 {ECO:0000255|HAMAP-Rule:MF_00253}; DE AltName: Full=Glycyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00253}; DE Short=GlyRS {ECO:0000255|HAMAP-Rule:MF_00253}; GN Name=glyS {ECO:0000255|HAMAP-Rule:MF_00253}; OrderedLocusNames=MJ0228; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the attachment of glycine to tRNA(Gly). CC {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- CATALYTIC ACTIVITY: ATP + glycine + tRNA(Gly) = AMP + diphosphate CC + glycyl-tRNA(Gly). {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00253}. CC -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98213.1; -; Genomic_DNA. DR PIR; E64328; E64328. DR ProteinModelPortal; Q57681; -. DR STRING; 243232.MJ_0228; -. DR EnsemblBacteria; AAB98213; AAB98213; MJ_0228. DR KEGG; mja:MJ_0228; -. DR eggNOG; arCOG00405; Archaea. DR eggNOG; COG0423; LUCA. DR InParanoid; Q57681; -. DR KO; K01880; -. DR OMA; ERFGWVE; -. DR PhylomeDB; Q57681; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004820; F:glycine-tRNA ligase activity; ISS:UniProtKB. DR GO; GO:0046983; F:protein dimerization activity; ISS:UniProtKB. DR GO; GO:0006426; P:glycyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 3.40.50.800; -; 1. DR HAMAP; MF_00253_A; Gly_tRNA_synth_A; 1. DR InterPro; IPR002314; aa-tRNA-synt_IIb. DR InterPro; IPR006195; aa-tRNA-synth_II. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR027031; Gly-tRNA_synthase/POLG2. DR InterPro; IPR022960; Gly_tRNA_ligase_arc. DR InterPro; IPR002315; tRNA-synt_gly. DR PANTHER; PTHR10745; PTHR10745; 1. DR Pfam; PF03129; HGTP_anticodon; 1. DR Pfam; PF00587; tRNA-synt_2b; 1. DR PRINTS; PR01043; TRNASYNTHGLY. DR SUPFAM; SSF52954; SSF52954; 1. DR TIGRFAMs; TIGR00389; glyS_dimeric; 1. DR PROSITE; PS50862; AA_TRNA_LIGASE_II; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 577 Glycine--tRNA ligase. FT /FTId=PRO_0000072990. FT NP_BIND 196 198 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 206 211 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 328 329 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT NP_BIND 451 454 ATP. {ECO:0000255|HAMAP-Rule:MF_00253}. FT REGION 211 215 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT REGION 447 451 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 98 98 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. FT BINDING 164 164 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00253}. SQ SEQUENCE 577 AA; 67121 MW; 598F8D2D9A57C61F CRC64; MEKDIYEKIM DLAKRRGYLW SSFEIYGGIA GFVDYGPLGC LLKNNIISKF REQYIIKEGF YEIESPTVTP YEVLKASGHV DNFTDPIVEC KNCLESFRAD HLIEEFVDVD TEGKTLKELD ELIRKHNIRC PKCGGELGEV KKFNLMFVTS IGPGGKRTGY MRPETAQGIF IQFRRLAQFF RNKLPFGVVQ IGKSYRNEIS PRQGVIRLRE FTQAEIEYFV HPERKEHEKF DLVKDEVVPL LPAERQMDEN LSDDEKVIKI SIGEAVEKGI IRHQTIAYFI ALTKRFLEAI GIDKDKIRFR QHLPNEMAHY AIDCWDAEIY TERFGWIECV GIADRTDYDL RSHSAHSGVE LSVFVELDEE REIETYEINL NYKVVGKIFK KDTKAIEAYI NNLSEKEKEE FVKNIENDGK VIINIDGKEF EILKDYVEIK KVKKVIKGEK VIPHVIEPSY GIDRITYCLL EHSYREEEDR VYLDLKPSIA PIKAYVLPLV NKDDMPKIAK EIEQMLRENG IIAEYDDSGA IGRRYMRADE IGVPFCITVD GQTLEDRTVT VRERNTREQV RVKIDELVDY LKERLKE // ID SYL_METJA Reviewed; 942 AA. AC Q58050; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 101. DE RecName: Full=Leucine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00049}; DE EC=6.1.1.4 {ECO:0000255|HAMAP-Rule:MF_00049}; DE AltName: Full=Leucyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00049}; DE Short=LeuRS {ECO:0000255|HAMAP-Rule:MF_00049}; GN Name=leuS {ECO:0000255|HAMAP-Rule:MF_00049}; OrderedLocusNames=MJ0633; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-leucine + tRNA(Leu) = AMP + CC diphosphate + L-leucyl-tRNA(Leu). {ECO:0000255|HAMAP- CC Rule:MF_00049}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00049}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000255|HAMAP-Rule:MF_00049}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98628.1; -; Genomic_DNA. DR PIR; A64379; A64379. DR ProteinModelPortal; Q58050; -. DR SMR; Q58050; 5-787. DR STRING; 243232.MJ_0633; -. DR EnsemblBacteria; AAB98628; AAB98628; MJ_0633. DR KEGG; mja:MJ_0633; -. DR eggNOG; arCOG00809; Archaea. DR eggNOG; COG0495; LUCA. DR InParanoid; Q58050; -. DR KO; K01869; -. DR OMA; TADDWKY; -. DR PhylomeDB; Q58050; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0002161; F:aminoacyl-tRNA editing activity; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004823; F:leucine-tRNA ligase activity; IBA:GO_Central. DR GO; GO:0006429; P:leucyl-tRNA aminoacylation; IBA:GO_Central. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR Gene3D; 3.90.740.10; -; 1. DR HAMAP; MF_00049_A; Leu_tRNA_synth_A; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002300; aa-tRNA-synth_Ia. DR InterPro; IPR020791; Leu-tRNA-lgase_arc. DR InterPro; IPR004493; Leu-tRNA-synth_Ia_arc/euk. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR InterPro; IPR009008; Val/Leu/Ile-tRNA-synth_edit. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF00133; tRNA-synt_1; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50677; SSF50677; 2. DR TIGRFAMs; TIGR00395; leuS_arch; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 942 Leucine--tRNA ligase. FT /FTId=PRO_0000152131. FT MOTIF 41 51 "HIGH" region. FT MOTIF 633 637 "KMSKS" region. FT BINDING 636 636 ATP. {ECO:0000255|HAMAP-Rule:MF_00049}. SQ SEQUENCE 942 AA; 110184 MW; 25A551461566A399 CRC64; MMVMIDFKEI EKKWQKRWEE AKIFEANPDD REKFFITAAF PYLNGVLHAG HLRTFTIPEV VARFQRMKNK NVLWTFGYHV TGTPILGLAE LIKNRDEKTI WAYTELHGIP KEELLELTTP EKIVEYFSKK AEEAFKRMGF SLDWRRNFKT DDKVFNKFIE WQFHKLKEKG LIVKGSHPVR YCPRCDNPVE DHDILVGENA TLVEYILIKF TTEDGCIMPM ATLRPETVFG VTNVWVNPEA TYVKAKVYLE KETENGIELI ENGIWIMAKE CAEKLKHQDR KIEIIEEFKG EQLINKKVKN PVTGKEVPIL PAKFVKTNIG TGCVMSVPAH APYDYIALRD LGLVDEIGLI PLINVPGYGK YPAKEIVEKM GIKSQEEEDK LEEATKKIYK DEFHKGVLNE NCLDYEGIPV REIKDKLTKD LIDKGLAEIM YEFSEEKVIC RCGTPCIVKM VKGQWFIKYS DEKWKELAHK CIDKMRFIPE NLRQVFHEKI DWMKDKACVR RRGLGTKFPF EEGWVIESLS DSTIYPAYYT VAKYINQHNI KPEQLTLELF DYVFLGKGDV DKIAKETGIP KDIIEGMRKE FIYYYPVDWR CSAKDLIPNH LTFYIFNHVA IFPEEFWPRG IVVNGYVTIE GKKLSKSKGP VLPVLEVAEK FGADVGRFYI TTCAELPQDA DIKFKEMENT KKVLERLYLF AKEIAERRGE TGEEFSYIDK WLLSRLYKAV KQYDEYMENF ELRKAGILLY QLLDDLKWYR RRGGNNIRVL EEFLEVIIKL MMPFTPHLCE EMWEILGKEG FVSLAKFPEV KEEFINDEIE KGEEYLKAVM EDIKEIINVA KVQPKRIYLY TADDWKYEIL KIIKENEGKT IKELMPIIMK NPEFRKYGKE IPKLVNQLIK LNAEIINEVE VLENAKEFLK KEVGVEDIII NGEDKANKKR VAIPFKPAIY LE // ID SYM_METJA Reviewed; 651 AA. AC Q58659; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 113. DE RecName: Full=Methionine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00098}; DE EC=6.1.1.10 {ECO:0000255|HAMAP-Rule:MF_00098}; DE AltName: Full=Methionyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00098}; DE Short=MetRS {ECO:0000255|HAMAP-Rule:MF_00098}; GN Name=metG {ECO:0000255|HAMAP-Rule:MF_00098}; OrderedLocusNames=MJ1263; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Is required not only for elongation of protein synthesis CC but also for the initiation of all mRNA translation through CC initiator tRNA(fMet) aminoacylation. {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC -!- CATALYTIC ACTIVITY: ATP + L-methionine + tRNA(Met) = AMP + CC diphosphate + L-methionyl-tRNA(Met). {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00098}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00098}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. MetG type 1 subfamily. {ECO:0000255|HAMAP-Rule:MF_00098}. CC -!- SIMILARITY: Contains 1 tRNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_00098}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99269.1; -; Genomic_DNA. DR PIR; F64457; F64457. DR ProteinModelPortal; Q58659; -. DR STRING; 243232.MJ_1263; -. DR EnsemblBacteria; AAB99269; AAB99269; MJ_1263. DR KEGG; mja:MJ_1263; -. DR eggNOG; arCOG00810; Archaea. DR eggNOG; COG0073; LUCA. DR eggNOG; COG0143; LUCA. DR InParanoid; Q58659; -. DR KO; K01874; -. DR OMA; FWPAMLD; -. DR PhylomeDB; Q58659; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004825; F:methionine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006431; P:methionyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 2.20.28.20; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00098; Met_tRNA_synth_type1; 1. DR InterPro; IPR013155; M/V/L/I-tRNA-synth_anticd-bd. DR InterPro; IPR004495; Met-tRNA-synth_bsu_C. DR InterPro; IPR023458; Met-tRNA_ligase_1. DR InterPro; IPR014758; Met-tRNA_synth. DR InterPro; IPR015413; Methionyl/Leucyl_tRNA_Synth. DR InterPro; IPR029038; MetRS_Zn. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR002547; tRNA-bd_dom. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR Pfam; PF08264; Anticodon_1; 1. DR Pfam; PF09334; tRNA-synt_1g; 1. DR Pfam; PF01588; tRNA_bind; 1. DR PRINTS; PR01041; TRNASYNTHMET. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF57770; SSF57770; 1. DR TIGRFAMs; TIGR00398; metG; 1. DR TIGRFAMs; TIGR00399; metG_C_term; 1. DR PROSITE; PS50886; TRBD; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; KW Reference proteome; RNA-binding; tRNA-binding; Zinc. FT CHAIN 1 651 Methionine--tRNA ligase. FT /FTId=PRO_0000139187. FT DOMAIN 550 651 tRNA-binding. {ECO:0000255|HAMAP- FT Rule:MF_00098}. FT MOTIF 10 20 "HIGH" region. FT MOTIF 320 324 "KMSKS" region. FT METAL 142 142 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 145 145 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 154 154 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT METAL 157 157 Zinc. {ECO:0000255|HAMAP-Rule:MF_00098}. FT BINDING 323 323 ATP. {ECO:0000255|HAMAP-Rule:MF_00098}. SQ SEQUENCE 651 AA; 75559 MW; C5C58DF5AA591E07 CRC64; MRYLITTALA YTNGPLHLGH ARSTYIPADI IYKYLKLRGE DVIHVGGTDN HGVPITLTAE KEGKSPEEIV EKYHNEIKED LDLLGVEFDA FGKTHSQIHI ETAQEFYLKL KENGYIYEKE IEQFYCPNCK KFLPDRYVEG ICPYCGGEAR GDHCEVCGRH LEPFELKDPY CVICKGKPEI RKTKHHFFKL SALKKELEEY IKNAKEMPEH VKNMALNWIK ELHDWDISRD ISWGVPIPGT NQVMYVWLEA PIGYISFTKM LGEIWKKYWL EKDTKIYHFI GKDITVHHAV FWPGMLIAHG SFNLPTAVVS GGYLTLEGRK MSTSKRWVVW VKDFVKNFDA DYLRYYLIMS APLFKDCDFS FDDFKNKINN ELINIIGNFT HRVLTFTHRK FKKVPIVDED RLKEEDKELL KKCEETLEAV DKNIRSFKFR DALVNILHLA IEGNSYFQKM EPWAVDDEER LKEILYTCCK TVKTLVYLLY PYMPKKSLAL LELMNEELDL ELRGNELKKP KIIFKKIDNK KIEEMKKKLY ENKKEETKGG EKMEQIDISY LEKIDLRVGE VVEAEDIPKS KKLLKLMVDL GDEKRQIVSG IKGYYKPEDL VGKKVIVICN LKPAKLCGVL SEGMILAAED DEGNVSLLTV DKDIKAGSKV R // ID SYR_METJA Reviewed; 566 AA. AC Q57689; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Arginine--tRNA ligase; DE EC=6.1.1.19; DE AltName: Full=Arginyl-tRNA synthetase; DE Short=ArgRS; GN Name=argS; OrderedLocusNames=MJ0237; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-arginine + tRNA(Arg) = AMP + CC diphosphate + L-arginyl-tRNA(Arg). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98223.1; -; Genomic_DNA. DR PIR; F64329; F64329. DR ProteinModelPortal; Q57689; -. DR STRING; 243232.MJ_0237; -. DR EnsemblBacteria; AAB98223; AAB98223; MJ_0237. DR KEGG; mja:MJ_0237; -. DR eggNOG; arCOG00487; Archaea. DR eggNOG; COG0018; LUCA. DR InParanoid; Q57689; -. DR KO; K01887; -. DR OMA; HVGHIRN; -. DR PhylomeDB; Q57689; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004814; F:arginine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006420; P:arginyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.730.10; -; 1. DR Gene3D; 3.30.1360.70; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00123; Arg_tRNA_synth; 1. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR001278; Arg-tRNA-ligase. DR InterPro; IPR005148; Arg-tRNA-synth_N. DR InterPro; IPR008909; DALR_anticod-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR009080; tRNAsynth_1a_anticodon-bd. DR PANTHER; PTHR11956; PTHR11956; 1. DR Pfam; PF03485; Arg_tRNA_synt_N; 1. DR Pfam; PF05746; DALR_1; 1. DR Pfam; PF00750; tRNA-synt_1d; 1. DR PRINTS; PR01038; TRNASYNTHARG. DR SMART; SM01016; Arg_tRNA_synt_N; 1. DR SMART; SM00836; DALR_1; 1. DR SUPFAM; SSF47323; SSF47323; 1. DR SUPFAM; SSF55190; SSF55190; 1. DR TIGRFAMs; TIGR00456; argS; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 566 Arginine--tRNA ligase. FT /FTId=PRO_0000151646. FT MOTIF 124 134 "HIGH" region. SQ SEQUENCE 566 AA; 64979 MW; E02A48181481D655 CRC64; MDIKSNIINA LKEVISKEIC KEIDIKLDKT PNLELGDYSV NICFRLAKEL KKNPKIIAEE LVDKLKAMNI EGVKEIKAVN GYINFYIDYN KFAKNLMEEI DKKGNNYGRG DKKSIKIILE HTSANPNGPL HIGHLRNAII GDCLKRILEF YGYDVETHYY VNDMGRQMAL VVYGIELFGL DKEKKKDHAI AETYVKINKY LEEHPEEEEK ILELMRKYED ALENNEDNEI TKKFEFAVNY ALDGIKETLK NLNIKHDTFV WESSYVRNGM VKKVIEKLME TGKVIKEETY MLDLSDFGIE KKMVLARANG TSLYSTRDIA YHLDKLSKCD IGIDVLGADH KLTAEMVKAA LKLLGSKVPE VIFYEFISLP EGSMSTRRGR FISTDELLEE AIKRAKEECN KRGVEENIAY DIGLGAVRYN IARISPEKPM VFRWEEALDF EKVGCPFIQY AHARCCSILK EAENKGVKDE AVFNYELTSE EKELIKMLDE FKDIIKESAE SRRVHILANY LLELAKAFNR FYANCPILMT KVDDDVKKSR LKLVKSTKTV LETGLELLGI NCPGRM // ID SYK_METJA Reviewed; 530 AA. AC Q57959; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-NOV-2015, entry version 101. DE RecName: Full=Lysine--tRNA ligase; DE EC=6.1.1.6; DE AltName: Full=Lysyl-tRNA synthetase; DE Short=LysRS; GN Name=lysS; OrderedLocusNames=MJ0539; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + L-lysine + tRNA(Lys) = AMP + diphosphate CC + L-lysyl-tRNA(Lys). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98532.1; -; Genomic_DNA. DR ProteinModelPortal; Q57959; -. DR STRING; 243232.MJ_0539; -. DR EnsemblBacteria; AAB98532; AAB98532; MJ_0539. DR KEGG; mja:MJ_0539; -. DR eggNOG; arCOG00485; Archaea. DR eggNOG; COG1384; LUCA. DR InParanoid; Q57959; -. DR KO; K04566; -. DR OMA; HENKKIM; -. DR PhylomeDB; Q57959; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004824; F:lysine-tRNA ligase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0006430; P:lysyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.350; -; 1. DR Gene3D; 2.30.30.300; -; 1. DR Gene3D; 3.40.50.620; -; 2. DR HAMAP; MF_00177; Lys_tRNA_synth_class1; 1. DR InterPro; IPR008925; aa-tRNA-synth_I_codon-bd. DR InterPro; IPR020751; aa-tRNA-synth_I_codon-bd_sub2. DR InterPro; IPR001412; aa-tRNA-synth_I_CS. DR InterPro; IPR002904; Lys-tRNA-ligase. DR InterPro; IPR023386; Lys-tRNA-ligase_insertion. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR SUPFAM; SSF48163; SSF48163; 1. DR TIGRFAMs; TIGR00467; lysS_arch; 1. DR PROSITE; PS00178; AA_TRNA_LIGASE_I; 1. PE 3: Inferred from homology; KW Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm; KW Ligase; Nucleotide-binding; Protein biosynthesis; Reference proteome. FT CHAIN 1 530 Lysine--tRNA ligase. FT /FTId=PRO_0000152753. FT MOTIF 28 36 "HIGH" region. FT MOTIF 278 282 "KMSKS" region. SQ SEQUENCE 530 AA; 61921 MW; 5811837C8A349E9C CRC64; MHWADVIAEK LIEERKADKY IVASGITPSG HIHVGNARET LTADAIYKGL INKGVEAELI FIADTYDPLR KLYPFLPKEF EQYIGMPLSE IPCPEGCCES YAEHFLRPYL ESLDDLGVEL TTYRADENYK KGLYDEKIKI ALDNREKIME ILNKFRANPL PDDWWPINIV CENCGKLKTK VIKYDSEKEE ITYRCEICGF ENTVKPYKGR AKLPWRVDWP ARWSIFNVTI EPMGKDHAAA GGSYDTGVLI AKEIYNYIPP KKVVYEWIQL KVGDKAIPMS SSKGVVFAVK DWTNIAHPEI LRFLLLRSKP TKHIDFDLKK IPDLVDEYDR LEDFYFNNKD KDELSEEEQE KIRIYELSTP KIPETKPFVI PYRFCSIIAQ LTYDEEKEDI NMERVFEILR RNNYSIDDID EFSMKKLKDR LLMARNWALK YGEKLVIISE DEAKEIYEKL KDKQKEWIKY FAEKLKTAEF DALNLHELIY QTAKELGLNP RDAFQASYMI LLGKKYGPKL GAFLATLGKD FVIRRYSLFE // ID T1RH_METJA Reviewed; 1042 AA. AC Q60295; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Putative type-1 restriction enzyme MjaXP R protein; DE EC=3.1.21.3; DE AltName: Full=Putative type I restriction enzyme MjaXP R protein; GN OrderedLocusNames=MJECL40; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Subunit R is required for both nuclease and ATPase CC activities, but not for modification. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give random CC double-stranded fragments with terminal 5'-phosphates; ATP is CC simultaneously hydrolyzed. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the HsdR family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37109.1; -; Genomic_DNA. DR PIR; G64514; G64514. DR ProteinModelPortal; Q60295; -. DR REBASE; 3908; MjaORFCL42P. DR PRIDE; Q60295; -. DR EnsemblBacteria; AAC37109; AAC37109; MJ_ECL40. DR KEGG; mja:MJECL40; -. DR HOGENOM; HOG000240457; -. DR InParanoid; Q60295; -. DR KO; K01153; -. DR OMA; IRYFVLF; -. DR PhylomeDB; Q60295; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR021810; DUF3387. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011254; Prismane-like. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR. DR Pfam; PF11867; DUF3387; 1. DR Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF56821; SSF56821; 1. DR TIGRFAMs; TIGR00348; hsdR; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Hydrolase; KW Nucleotide-binding; Plasmid; Reference proteome; Restriction system. FT CHAIN 1 1042 Putative type-1 restriction enzyme MjaXP FT R protein. FT /FTId=PRO_0000077273. FT DOMAIN 323 487 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 551 731 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. SQ SEQUENCE 1042 AA; 121523 MW; 3C8E5A103E7B59D3 CRC64; MPISANKYFL LVGVFIGDKM KKEAAKLNED YVVENAAIQR LKNLGYSYKH GSELTPEYNE RESYRDAILK NRFIKAIKNI NPWLTEELAL KVYKTVTNID NPDFNMRGKI FYEMLINGVK LEFKENGEKK TRFVKLIDFE NINKNEFLVA NQFEVEYYYE NGRFRRPDLV VFINGIPIAI FEFKSPKSNQ TAKDAFNDHK TKMKDIPQLY QYAQILVVSD GLETKYGSPT SDWDRFFVWE GVESDDDVEV IEVDNYGNTM YKYKGNPYTS LDILLMGLFK KEHLIEFLED FIIHDKKKII ATYYQFYTVK KAVDRTIKSV LYGETPEDRR IGIVWHAQGT GKSITMLFYA KKALKQKELN YPLLVFLTDR LELDEQLYNV FSSVFSEAER AESIAELQEL IKKTPGGIIF ATIQKFGRKS KDEHYPFLTD RNNIIIIADE AHRSHYGTLA QNLRKAIPNA SFLAFTATPI DYKDRSTFLV FGDYISAYPI DKAKRHGVVV PIYYEARLVE LHLTNEFIDL EFDEISERVA NDPETKESIK EVFAKLEKIM LTEDYLSKVS KDIIEHFNKR LQDFDGKAMV VTISRKVAVE LYKWITKQPN APKIAVVMSG NKSKDPEDFH PHIRTKKELE NLAKEFKDPE SDLKMVIVVD MWLTGFDVPC LHTMYFLKPM KNHSLAQAIA RVNRVFKDKP GGLIVDYIGI ADDLSKSLSK YSSEARKDLM TDIKVVIEEM KRRYEKVTSY FKNINYKDWK KLSSEDLSLL TVKAYQRVAK DDNTKKEFVR NVIALKKLYL LARPHPETIG IKDDLEFFEM IKKMIVKYST KKIREISQDL ENDIQSLISK SISAKELVDV FEMLKKEKPE LSVLSDEFLS EIAKIEYKDY VRDVLIKILN DDIRVRMAKN PIRFKKFSER LNEVIEKYRI KVITTAEMIE ELVNLAKEIR KAAEEGKELG LTEEELAFYD LLLSYPNIPL TDKKRVEKIA KEIARMMSGY IKARDWKKKK NLQSKIRAKL KIILMKEGIK DYSLINKISD DLFEYAKNIY AI // ID T2M4_METJA Reviewed; 245 AA. AC Q58723; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Type-2 restriction enzyme MjaIV; DE Short=R.MjaIV; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaIV; DE AltName: Full=Type II restriction enzyme MjaIV; GN Name=mjaIVR; OrderedLocusNames=MJ1327; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: Recognizes the double-stranded unmethylated sequence CC GTNNAC. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99343.1; -; Genomic_DNA. DR PIR; F64465; F64465. DR ProteinModelPortal; Q58723; -. DR STRING; 243232.MJ_1327; -. DR REBASE; 3894; MjaIV. DR EnsemblBacteria; AAB99343; AAB99343; MJ_1327. DR KEGG; mja:MJ_1327; -. DR BRENDA; 3.1.21.4; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 245 Type-2 restriction enzyme MjaIV. FT /FTId=PRO_0000077335. SQ SEQUENCE 245 AA; 28779 MW; 4597C2B8EF1FA973 CRC64; MVVKLVNNEL KILSGKLRDI FREIYNKIKN DENINDRNLD DKVLSLLKDY TISEENLKIK FSEPKDEIYS YEGRRTPYDL LCYGIINGKN FLIFINNKFG DLKSNTRNDV TTYNNLLRLY LGIKRQRLTS EITINGELVY NRISGNEIVS YGIFVVDKYR RGYKFFLLEE IKDDFYVNPR NNMFQIRYSP NLGDPIDYFA FVKKLIDAIL ESLEKSLNSI KTEILVLNSI KIQLINIKEG KHGED // ID TDXH_METJA Reviewed; 217 AA. AC Q58146; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=Peroxiredoxin {ECO:0000255|HAMAP-Rule:MF_00401}; DE EC=1.11.1.15 {ECO:0000255|HAMAP-Rule:MF_00401}; GN OrderedLocusNames=MJ0736; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Protects cells against oxidative stress. Can reduce CC hydrogen peroxide and/or alkyl hydroperoxides using dithiothreitol CC as an electron donor (in vitro). {ECO:0000255|HAMAP- CC Rule:MF_00401}. CC -!- CATALYTIC ACTIVITY: 2 R'-SH + ROOH = R'-S-S-R' + H(2)O + ROH. CC {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SUBUNIT: Homodecamer. Pentamer of dimers that assemble into a ring CC structure. {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SIMILARITY: Belongs to the AhpC/TSA family. TDXH subfamily. CC {ECO:0000255|HAMAP-Rule:MF_00401}. CC -!- SIMILARITY: Contains 1 thioredoxin domain. {ECO:0000255|HAMAP- CC Rule:MF_00401}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98731.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98731.1; ALT_INIT; Genomic_DNA. DR PIR; H64391; H64391. DR ProteinModelPortal; Q58146; -. DR SMR; Q58146; 1-215. DR STRING; 243232.MJ_0736; -. DR EnsemblBacteria; AAB98731; AAB98731; MJ_0736. DR KEGG; mja:MJ_0736; -. DR eggNOG; arCOG00312; Archaea. DR eggNOG; COG0450; LUCA. DR InParanoid; Q58146; -. DR KO; K03386; -. DR OMA; IPANWPN; -. DR PhylomeDB; Q58146; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:UniProtKB-HAMAP. DR GO; GO:0045454; P:cell redox homeostasis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.30.10; -; 1. DR HAMAP; MF_00401; Peroxiredoxin; 1. DR InterPro; IPR000866; AhpC/TSA. DR InterPro; IPR024706; Peroxiredoxin_AhpC-typ. DR InterPro; IPR019479; Peroxiredoxin_C. DR InterPro; IPR022915; Peroxiredoxin_TDXH. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF10417; 1-cysPrx_C; 1. DR Pfam; PF00578; AhpC-TSA; 1. DR PIRSF; PIRSF000239; AHPC; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR PROSITE; PS51352; THIOREDOXIN_2; 1. PE 3: Inferred from homology; KW Antioxidant; Complete proteome; Cytoplasm; Oxidoreductase; KW Redox-active center; Reference proteome. FT CHAIN 1 217 Peroxiredoxin. FT /FTId=PRO_0000135155. FT DOMAIN 2 159 Thioredoxin. {ECO:0000255|HAMAP- FT Rule:MF_00401}. FT ACT_SITE 46 46 Cysteine sulfenic acid (-SOH) FT intermediate. {ECO:0000255|HAMAP- FT Rule:MF_00401}. FT BINDING 122 122 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00401}. SQ SEQUENCE 217 AA; 25010 MW; 6D64B6CF1BC0CAA5 CRC64; MPVIGEKFPE VEVKTTHGAI KLPDYYVEKG KWFVLFSHPA DFTPVCTTEF VGFQKRYDEF RKLNTELIGL SIDQVFSHLK WVEWIKEKLN VEIEFPIIAD DRGELAEKLG MISPYKGNNT VRAVFVVDNK GIIRAIIYYP QEVGRNLDEI VRLVKALQVS DEKGVAMPAN WPENDLIGDK VIIPPASSVE EIKQRKEACE KGEIECLDWW FCYKKLD // ID T2M5_METJA Reviewed; 230 AA. AC Q58895; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 76. DE RecName: Full=Type-2 restriction enzyme MjaV; DE Short=R.MjaV; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaV; DE AltName: Full=Type II restriction enzyme MjaV; GN Name=mjaVR; OrderedLocusNames=MJ1500; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: Recognizes the double-stranded unmethylated sequence CC GTAC. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99521.1; -; Genomic_DNA. DR PIR; C64487; C64487. DR ProteinModelPortal; Q58895; -. DR STRING; 243232.MJ_1500; -. DR REBASE; 3898; MjaV. DR EnsemblBacteria; AAB99521; AAB99521; MJ_1500. DR KEGG; mja:MJ_1500; -. DR eggNOG; arCOG08288; Archaea. DR eggNOG; ENOG41110JH; LUCA. DR OMA; KREFNAS; -. DR BRENDA; 3.1.21.4; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 230 Type-2 restriction enzyme MjaV. FT /FTId=PRO_0000077336. SQ SEQUENCE 230 AA; 26764 MW; 9566FE2061C144D5 CRC64; MDDKSYYEEI ESILRQILQP IEKISFSTFI RVVSGYKIIP IDLSKKEDKE LINDLAKACN EVIEEIKKTG GVKTKEGKTP KRVNEVGNHI EHYVKDVLNK YGYAITPKTK KGKQKSTGYP DIEFWYKGKK ERDGRVVYIE IKTFNEKNIN SSHRTFYASP SKDEEGVKIR YDAPHLCLSF KIEKLGRDYY ATGFKIIDLS KLKGGIKREF NASNRELYKK DLIIYEKDLK // ID T1MH_METJA Reviewed; 558 AA. AC Q60297; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative type I restriction enzyme MjaXP M protein; DE Short=M.MjaXP; DE EC=2.1.1.72; GN OrderedLocusNames=MJECL42; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Methylation of specific adenine residues; required for CC both restriction and modification activities. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37111.1; -; Genomic_DNA. DR PIR; A64515; A64515. DR ProteinModelPortal; Q60297; -. DR REBASE; 3910; M.MjaORFCL42P. DR DNASU; 1450824; -. DR EnsemblBacteria; AAC37111; AAC37111; MJ_ECL42. DR KEGG; mja:MJECL42; -. DR HOGENOM; HOG000239473; -. DR InParanoid; Q60297; -. DR KO; K03427; -. DR OMA; LAENIFW; -. DR PhylomeDB; Q60297; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR022749; D12N6_MeTrfase_N. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF12161; HsdM_N; 1. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Plasmid; Reference proteome; KW Restriction system; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 558 Putative type I restriction enzyme MjaXP FT M protein. FT /FTId=PRO_0000088029. FT REGION 227 232 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 256 258 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 283 283 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 558 AA; 64552 MW; 0DD8568C71C3AF37 CRC64; MATLDKFLSI KENDEKTKKK ESKKKSSKSN KTSESLVSHD HFELTPEFEN QLWKVADKLR KKMEVHQYKY VVLGLIFLRA LTCRFYERRK EIEEELSNPN SELYTEDPEL RKMILEDEDF YLSEGVLYLP KETRWDYFVE NVMSPNIGEI IDTAIEILEE KYPDRLKDVI PKIYAQSPLD NHDYSYLINK FSEISFGKEH RVKDVFGRIY EYFLGKFTEV EGKLGGKFYT PRSLTKLIVD VLDVKGGSIF DPACGSGGFF VSALEKLERE GIDINELSIY GQDSDPMAYR LTKMNLIIRG AEGDIRIDDS YHDDKFMDMT FDYVVANPPF NDSEWDANRI KPDDPRLRIG NKKVPVPPNG NANYMWILHF IYHTAPNGKA GFVMANGALS AGNVEGEIRK AIIENDLVYG IVACPPKLFY NVSLPVSLWF IRKEKPDYMK GKVLFINAKN LYKQISRRQN ILTEEHIKKI VDKFRMFESG EDEDKINELG FAKVATIDEI AKNGYVLTPG RYVGVKIEDD GIPFEVKMKE YSEELKKLLD EEEKLRNKVK EILDALGF // ID T1S1_METJA Reviewed; 425 AA. AC Q57594; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 03-OCT-2006, sequence version 3. DT 09-DEC-2015, entry version 87. DE RecName: Full=Type-1 restriction enzyme MjaXIP specificity protein; DE Short=S.MjaXIP; DE AltName: Full=Type I restriction enzyme MjaXIP specificity protein; DE Short=S protein; GN OrderedLocusNames=MJ0130; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. RN [3] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). RX PubMed=15728358; DOI=10.1073/pnas.0409851102; RA Kim J.-S., DeGiovanni A., Jancarik J., Adams P.D., Yokota H., Kim R., RA Kim S.-H.; RT "Crystal structure of DNA sequence specificity subunit of a type I RT restriction-modification enzyme and its functional implications."; RL Proc. Natl. Acad. Sci. U.S.A. 102:3248-3253(2005). CC -!- FUNCTION: The M and S subunits together form a methyltransferase CC (MTase) that methylates two adenine residues in complementary CC strands of a bipartite DNA recognition sequence. In the presence CC of the R subunit the complex can also act as an endonuclease, CC binding to the same target sequence but cutting the DNA some CC distance from this site. Whether the DNA is cut or modified CC depends on the methylation state of the target sequence. When the CC target site is unmodified, the DNA is cut. When the target site is CC hemimethylated, the complex acts as a maintenance MTase modifying CC the DNA so that both strands become methylated. Subunit S dictates CC DNA sequences specificity (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The type I restriction/modification system is composed of CC three polypeptides R, M and S. {ECO:0000250}. CC -!- DOMAIN: Contains two DNA recognition domains, each specifying CC recognition of one of the two defined components of the target CC sequence. These two domains show high sequence and structural CC similarities to each other and each forms a globular structure. CC -!- DOMAIN: The two globular DNA recognition domains are structurally CC separated by an antiparallel double helix which is composed of two CC highly similar 40 residues long coiled-coil regions. These CC conserved regions may act as a molecular ruler for the separation CC between the two recognized DNA sequences. CC -!- SIMILARITY: Belongs to the type-I restriction system S methylase CC family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98112.1; Type=Frameshift; Positions=331; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98112.1; ALT_FRAME; Genomic_DNA. DR PDB; 1YF2; X-ray; 2.40 A; A/B=1-425. DR PDBsum; 1YF2; -. DR ProteinModelPortal; Q57594; -. DR SMR; Q57594; 1-425. DR STRING; 243232.MJ_0130m; -. DR REBASE; 3901; S.MjaORF132P. DR EnsemblBacteria; AAB98112; AAB98112; MJ_0130. DR eggNOG; arCOG02626; Archaea. DR eggNOG; COG0732; LUCA. DR InParanoid; Q57594; -. DR OMA; GMIPEDW; -. DR PhylomeDB; Q57594; -. DR EvolutionaryTrace; Q57594; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 1: Evidence at protein level; KW 3D-structure; Coiled coil; Complete proteome; DNA-binding; KW Reference proteome; Repeat; Restriction system. FT CHAIN 1 425 Type-1 restriction enzyme MjaXIP FT specificity protein. FT /FTId=PRO_0000106708. FT REPEAT 169 208 1; CCR. FT REPEAT 369 418 2; DCR. FT REGION 9 168 DNA recognition domain 1. FT REGION 209 368 DNA recognition domain 2. FT COILED 169 208 FT COILED 369 418 FT STRAND 12 15 {ECO:0000244|PDB:1YF2}. FT STRAND 17 19 {ECO:0000244|PDB:1YF2}. FT HELIX 25 28 {ECO:0000244|PDB:1YF2}. FT STRAND 29 34 {ECO:0000244|PDB:1YF2}. FT HELIX 43 45 {ECO:0000244|PDB:1YF2}. FT TURN 46 48 {ECO:0000244|PDB:1YF2}. FT STRAND 51 54 {ECO:0000244|PDB:1YF2}. FT HELIX 56 60 {ECO:0000244|PDB:1YF2}. FT STRAND 62 66 {ECO:0000244|PDB:1YF2}. FT STRAND 70 73 {ECO:0000244|PDB:1YF2}. FT HELIX 75 79 {ECO:0000244|PDB:1YF2}. FT STRAND 91 94 {ECO:0000244|PDB:1YF2}. FT STRAND 96 98 {ECO:0000244|PDB:1YF2}. FT STRAND 102 107 {ECO:0000244|PDB:1YF2}. FT STRAND 109 111 {ECO:0000244|PDB:1YF2}. FT STRAND 113 120 {ECO:0000244|PDB:1YF2}. FT TURN 122 124 {ECO:0000244|PDB:1YF2}. FT HELIX 127 136 {ECO:0000244|PDB:1YF2}. FT HELIX 138 142 {ECO:0000244|PDB:1YF2}. FT STRAND 145 149 {ECO:0000244|PDB:1YF2}. FT HELIX 155 159 {ECO:0000244|PDB:1YF2}. FT HELIX 168 209 {ECO:0000244|PDB:1YF2}. FT STRAND 222 225 {ECO:0000244|PDB:1YF2}. FT STRAND 229 232 {ECO:0000244|PDB:1YF2}. FT HELIX 233 236 {ECO:0000244|PDB:1YF2}. FT STRAND 237 241 {ECO:0000244|PDB:1YF2}. FT HELIX 250 252 {ECO:0000244|PDB:1YF2}. FT TURN 253 255 {ECO:0000244|PDB:1YF2}. FT STRAND 258 261 {ECO:0000244|PDB:1YF2}. FT HELIX 263 267 {ECO:0000244|PDB:1YF2}. FT TURN 268 271 {ECO:0000244|PDB:1YF2}. FT STRAND 273 275 {ECO:0000244|PDB:1YF2}. FT STRAND 279 282 {ECO:0000244|PDB:1YF2}. FT HELIX 284 289 {ECO:0000244|PDB:1YF2}. FT STRAND 300 303 {ECO:0000244|PDB:1YF2}. FT STRAND 305 307 {ECO:0000244|PDB:1YF2}. FT STRAND 311 316 {ECO:0000244|PDB:1YF2}. FT STRAND 318 320 {ECO:0000244|PDB:1YF2}. FT STRAND 324 330 {ECO:0000244|PDB:1YF2}. FT HELIX 337 346 {ECO:0000244|PDB:1YF2}. FT HELIX 348 355 {ECO:0000244|PDB:1YF2}. FT STRAND 357 360 {ECO:0000244|PDB:1YF2}. FT HELIX 365 370 {ECO:0000244|PDB:1YF2}. FT STRAND 372 375 {ECO:0000244|PDB:1YF2}. FT HELIX 378 416 {ECO:0000244|PDB:1YF2}. FT STRAND 418 420 {ECO:0000244|PDB:1YF2}. SQ SEQUENCE 425 AA; 48568 MW; E196A947574FE91D CRC64; MFYKEENFKK TEIGEIPEDW EIVELKDVCK KIKAGGTPKT SVEEYYKNGT IPFVKIEDIT NSNKYLTNTK IKITEEGLNN SNAWIVPKNS VLFAMYGSIG ETAINKIEVA TNQAILGIIP KDNILESEFL YYILAKNKNY YSKLGMQTTQ KNLNAQIVKS FKIPLPPLEE QKQIAKILTK IDEGIEIIEK SINKLERIKK GLMHKLLTKG IGHSRFKKSE IGEIPEDWEV FEIKDIFEVK TGTTPSTKKS EYWENGEINW ITPLDLSRLN EKIYIGSSER KVTKIALEKC NLNLIPKGSI IISTRAPVGY VAVLTVESTF NQGCKGLFQK NNDSVNTEFY AYYLKFKKNL LENLSGGSTF KELSKSMLEN FKIPLPPLEE QKQIAKILSS VDKSIELKKQ KKEKLQRMKK KIMELLLTGK VRVKT // ID T2M1_METJA Reviewed; 222 AA. AC Q58391; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Type-2 restriction enzyme MjaI; DE Short=R.MjaI; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaI; DE AltName: Full=Type II restriction enzyme MjaI; GN Name=mjaIR; OrderedLocusNames=MJ0984; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: Recognizes the double-stranded sequence CTAG and cleaves CC after C-1. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98987.1; -; Genomic_DNA. DR PIR; H64422; H64422. DR ProteinModelPortal; Q58391; -. DR STRING; 243232.MJ_0984; -. DR REBASE; 1221; MjaI. DR EnsemblBacteria; AAB98987; AAB98987; MJ_0984. DR KEGG; mja:MJ_0984; -. DR eggNOG; arCOG11279; Archaea. DR eggNOG; ENOG4111NKK; LUCA. DR InParanoid; Q58391; -. DR OMA; QMSELIK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR019068; Restrct_endonuc_II_MjaI. DR Pfam; PF09568; RE_MjaI; 1. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 222 Type-2 restriction enzyme MjaI. FT /FTId=PRO_0000077332. SQ SEQUENCE 222 AA; 25962 MW; 9A254A208AB8AC02 CRC64; MVKLMKKLED KKGIIEITFE EEREILELPS KPELPKYASQ LINLANIFSQ GTRPKVVGQM SELIKEFRKT GGRTFEDWKK WYLQKYPNAI DEATEKIWNM LNNFKETLEQ LERDDVRKWV EDLVLIKTYE GLMLQDAILK KVAEELGGNY RPSTIEEESK GIDGVIIIDD KEIPVSIKSK TYVNQEKHLS EELKGHLIIY EKKKNKIIVD YSDLLDLVEN TK // ID T2M3_METJA Reviewed; 290 AA. AC Q58017; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Type-2 restriction enzyme MjaIII; DE Short=R.MjaIII; DE EC=3.1.21.4; DE AltName: Full=Endonuclease MjaIII; DE AltName: Full=Type II restriction enzyme MjaIII; GN Name=mjaIIIR; OrderedLocusNames=MJ0600; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP CHARACTERIZATION. RA Noren C.J., Roberts R.J., Patti J., Byrd D.R., Morgan R.D.; RT "Method for screening restriction endonucleases."; RL Patent number WO9911821, 11-MAR-1999. CC -!- FUNCTION: Recognizes the double-stranded unmethylated sequence CC GATC and cleaves before G-1. CC -!- CATALYTIC ACTIVITY: Endonucleolytic cleavage of DNA to give CC specific double-stranded fragments with terminal 5'-phosphates. CC -!- SIMILARITY: Belongs to the type II restriction enzyme DpnII CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98591.1; -; Genomic_DNA. DR PIR; H64374; H64374. DR ProteinModelPortal; Q58017; -. DR STRING; 243232.MJ_0600; -. DR REBASE; 3891; MjaIII. DR EnsemblBacteria; AAB98591; AAB98591; MJ_0600. DR KEGG; mja:MJ_0600; -. DR eggNOG; arCOG06575; Archaea. DR eggNOG; ENOG410YTH4; LUCA. DR KO; K01155; -. DR OMA; RKNRGGH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009036; F:Type II site-specific deoxyribonuclease activity; IEA:UniProtKB-EC. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:UniProtKB-KW. DR InterPro; IPR021191; Restrct_endonuc_II_DpmII. DR InterPro; IPR007637; Restrct_endonuc_II_DpmII-like. DR Pfam; PF04556; DpnII; 1. DR PIRSF; PIRSF016080; Restrict_endonuc_II_DpmII; 1. PE 1: Evidence at protein level; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome; Restriction system. FT CHAIN 1 290 Type-2 restriction enzyme MjaIII. FT /FTId=PRO_0000077334. SQ SEQUENCE 290 AA; 34392 MW; ACEBAE31B029900D CRC64; MNFEYIINSL LETIKTYNFF VDWEKIENNI KKIEKRLHIL NYLIGKENFK EEFFELLKEY PEVITVFPIL IAVRDNKITI LNENMELETL EFKEKKYLTD EEIERYYKFF KETGLEDLLK NRKIKNLVDY VFGVEVGMDT NARKNRIGDL MENIVKKYIE NLCKQNKNLD YIFQATKDKI KQKWGINLTL DKTNRKFDFA VFNKNTKKLY LIEVNFYSGG GSKLKATAGE YRSLNEFIKN NNNNVQFIWI TDGKGWNTAK NPLKESFNSG VVILNLKMVK EGLLKEILTQ // ID THII_METJA Reviewed; 381 AA. AC Q58341; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Probable tRNA sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE EC=2.8.1.4 {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Sulfur carrier protein ThiS sulfurtransferase {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=Thiamine biosynthesis protein ThiI {ECO:0000255|HAMAP-Rule:MF_00021}; DE AltName: Full=tRNA 4-thiouridine synthase {ECO:0000255|HAMAP-Rule:MF_00021}; GN Name=thiI {ECO:0000255|HAMAP-Rule:MF_00021}; OrderedLocusNames=MJ0931; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent transfer of a sulfur to tRNA CC to produce 4-thiouridine in position 8 of tRNAs, which functions CC as a near-UV photosensor. Also catalyzes the transfer of sulfur to CC the sulfur carrier protein ThiS, forming ThiS-thiocarboxylate. CC This is a step in the synthesis of thiazole, in the thiamine CC biosynthesis pathway. The sulfur is donated as persulfide by IscS. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: L-cysteine + 'activated' tRNA = L-serine + CC tRNA containing a thionucleotide. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- CATALYTIC ACTIVITY: [IscS]-SSH + [ThiS]-COAMP = [IscS]-SH + CC [ThiS]-COSH + AMP. {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00021}. CC -!- SIMILARITY: Belongs to the ThiI family. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|HAMAP- CC Rule:MF_00021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98933.1; -; Genomic_DNA. DR PIR; C64416; C64416. DR ProteinModelPortal; Q58341; -. DR STRING; 243232.MJ_0931; -. DR EnsemblBacteria; AAB98933; AAB98933; MJ_0931. DR KEGG; mja:MJ_0931; -. DR eggNOG; arCOG00038; Archaea. DR eggNOG; COG0301; LUCA. DR InParanoid; Q58341; -. DR KO; K03151; -. DR OMA; PDEDCCT; -. DR PhylomeDB; Q58341; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0016783; F:sulfurtransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0004810; F:tRNA adenylyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0034227; P:tRNA thio-modification; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.620; -; 1. DR HAMAP; MF_00021; ThiI; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR020536; ThiI_AANH. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR003720; tRNA_STrfase. DR Pfam; PF02568; ThiI; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR TIGRFAMs; TIGR00342; TIGR00342; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Reference proteome; RNA-binding; Thiamine biosynthesis; Transferase; KW tRNA-binding. FT CHAIN 1 381 Probable tRNA sulfurtransferase. FT /FTId=PRO_0000154894. FT DOMAIN 68 176 THUMP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT NP_BIND 194 195 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 276 276 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 298 298 ATP; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00021}. FT BINDING 307 307 ATP. {ECO:0000255|HAMAP-Rule:MF_00021}. SQ SEQUENCE 381 AA; 43437 MW; 0A31F1069DA3357B CRC64; MKKLKVSKME ILVRYGEIGL KSDPIRKNLE EILRKNIIKL LRKYEIDAEV KILHRKLLVK INTKDKEDLA LKLLKKVAGI VSYSPVYECP LDINEIVSFA VQIMKKKLKT LNKEKVTFAV KTKRSYKKFP FTSVEVNKKV GEAIVEKLGL EVDLENPDIV LGIEILNDGA YIFTEKYEGI GGLPAGSQGK VLCLISDGID SPVAAFMMIR RGCRAVLLHL KMSEEALNKV RKIVEVLSDY DTELEFVVYD YKKDIEDIVE KLKSIKKENY TCIFCKRKML KVAEKYAKYL DCDAIVTGDN LGQVASQTLK NLRVISENIN YPILRPLIGL DKNDIVKIAK EIGTYEISTE KEIKCPYLPK HPKTIAKPEE VKKIKEKVKL V // ID THIRX_METJA Reviewed; 86 AA. AC Q58001; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Thioredoxin {ECO:0000250|UniProtKB:O26981}; GN OrderedLocusNames=MJ0581; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Does not function as a glutathione-disulfide CC oxidoreductase in the presence of glutathione and glutathione CC reductase (By similarity). Has low thioredoxin activity in vitro CC (By similarity). {ECO:0000250|UniProtKB:O26981}. CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98575.1; -; Genomic_DNA. DR PIR; E64372; E64372. DR ProteinModelPortal; Q58001; -. DR STRING; 243232.MJ_0581; -. DR EnsemblBacteria; AAB98575; AAB98575; MJ_0581. DR KEGG; mja:MJ_0581; -. DR eggNOG; arCOG02713; Archaea. DR eggNOG; COG0526; LUCA. DR InParanoid; Q58001; -. DR OMA; CNQTYEN; -. DR PhylomeDB; Q58001; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; ISS:UniProtKB. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR005243; Redox_disulphide_2. DR InterPro; IPR012336; Thioredoxin-like_fold. DR Pfam; PF13192; Thioredoxin_3; 1. DR PIRSF; PIRSF037031; Redox_disulphide_2; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00412; redox_disulf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Disulfide bond; Electron transport; KW Redox-active center; Reference proteome; Transport. FT CHAIN 1 86 Thioredoxin. FT /FTId=PRO_0000141653. FT ACT_SITE 15 15 Nucleophile. FT {ECO:0000250|UniProtKB:P0AA25}. FT ACT_SITE 18 18 Nucleophile. FT {ECO:0000250|UniProtKB:P0AA25}. FT DISULFID 15 18 Redox-active. FT {ECO:0000250|UniProtKB:O26981}. SQ SEQUENCE 86 AA; 9634 MW; AA89FE52EC6C0D67 CRC64; MVRVMVVIRI FGTGCPKCNQ TYENVKKAVE ELGIDAEIVK VTDVNEIAEW VFVTPGVAFD DVIVFEGKIP SVEEIKEELK SYLEGK // ID TAL_METJA Reviewed; 217 AA. AC Q58370; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 102. DE RecName: Full=Probable transaldolase; DE EC=2.2.1.2; GN Name=tal; OrderedLocusNames=MJ0960; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Transaldolase is important for the balance of CC metabolites in the pentose-phosphate pathway. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-erythrose 4-phosphate + D-fructose 6-phosphate. CC -!- PATHWAY: Carbohydrate degradation; pentose phosphate pathway; D- CC glyceraldehyde 3-phosphate and beta-D-fructose 6-phosphate from D- CC ribose 5-phosphate and D-xylulose 5-phosphate (non-oxidative CC stage): step 2/3. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the transaldolase family. Type 3B CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98962.1; -; Genomic_DNA. DR PIR; H64419; H64419. DR ProteinModelPortal; Q58370; -. DR SMR; Q58370; 1-214. DR STRING; 243232.MJ_0960; -. DR EnsemblBacteria; AAB98962; AAB98962; MJ_0960. DR KEGG; mja:MJ_0960; -. DR eggNOG; arCOG05061; Archaea. DR eggNOG; COG0176; LUCA. DR InParanoid; Q58370; -. DR KO; K00616; -. DR OMA; GRDFYEV; -. DR PhylomeDB; Q58370; -. DR UniPathway; UPA00115; UER00414. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004801; F:sedoheptulose-7-phosphate:D-glyceraldehyde-3-phosphate glyceronetransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00494; Transaldolase_3b; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001585; TAL/FSA. DR InterPro; IPR022999; Transaldolase_3B. DR InterPro; IPR004731; Transaldolase_3B/F6P_aldolase. DR InterPro; IPR018225; Transaldolase_AS. DR PANTHER; PTHR10683; PTHR10683; 1. DR Pfam; PF00923; Transaldolase; 1. DR TIGRFAMs; TIGR00875; fsa_talC_mipB; 1. DR PROSITE; PS01054; TRANSALDOLASE_1; 1. DR PROSITE; PS00958; TRANSALDOLASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Pentose shunt; Reference proteome; KW Schiff base; Transferase. FT CHAIN 1 217 Probable transaldolase. FT /FTId=PRO_0000173689. FT ACT_SITE 83 83 Schiff-base intermediate with substrate. FT {ECO:0000250}. SQ SEQUENCE 217 AA; 23960 MW; E2FEDF98DDDA2F82 CRC64; MKFFLDTANV EEIKKYAELG LVDGVTTNPT LVAKEGRDFY EVVKEICEIV EGPVSAEVIS TDAEGMVKEA RELAKLADNI VIKIPMTKDG MKAVKILSAE GIKTNVTLVF SPLQALVAAK AGATYVSPFV GRLDDIGHVG MKLIEDVVKI YKNYDIKTEV IVASVRHPWH VLEAAKIGAD IATMPPAVMD KLFNHPLTDI GLERFLKDWD EYLKSRK // ID TFS_METJA Reviewed; 108 AA. AC Q58548; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 113. DE RecName: Full=Transcription factor S {ECO:0000250|UniProtKB:Q9P9I8}; DE AltName: Full=Transcription elongation factor IIS/RNA polymerase subunit homolog {ECO:0000250|UniProtKB:Q9P9I8}; DE Short=TFIIS/RPSU homolog {ECO:0000250|UniProtKB:Q9P9I8}; GN Name=tfs {ECO:0000250|UniProtKB:Q9P9I8}; OrderedLocusNames=MJ1148; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Induces RNA cleavage activity in the RNA polymerase. In CC its presence, the cleavage activity of the RNA polymerase CC truncates the RNA back to position +15 in a stepwise manner by CC releasing mainly dinucleotides from the 3'-end of the nascent RNA. CC The truncated RNAs are able to continue elongation. Involved in CC transcriptional proofreading and fidelity. Misincorporation of CC nucleotides during elongation of transcription leads to arrested CC elongation complexes which are rescued by TFS-promoted removal of CC a dinucleotide from the 3'-end. TFS is able to induce a cleavage CC resynthesis cycle in stalled elongation complexes (resulting from CC the next missing nucleotide or a reduced incorporation rate of a CC wrong nucleotide) preventing misincorporation and enabling CC proofreading in a post-incorporation manner. Pausing of elongation CC complexes is the main determinant of TFS-induced RNA cleavage. CC {ECO:0000250|UniProtKB:Q9P9I8}. CC -!- SIMILARITY: Belongs to the archaeal RpoM/eukaryotic CC RPA12/RPB9/RPC11 RNA polymerase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 TFIIS-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00472}. CC -!- CAUTION: More similar by sequence similarity to the eukaryotic RNA CC polymerase subunits. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99148.1; -; Genomic_DNA. DR PIR; C64443; C64443. DR ProteinModelPortal; Q58548; -. DR SMR; Q58548; 57-108. DR STRING; 243232.MJ_1148; -. DR EnsemblBacteria; AAB99148; AAB99148; MJ_1148. DR KEGG; mja:MJ_1148; -. DR eggNOG; arCOG00579; Archaea. DR eggNOG; COG1594; LUCA. DR InParanoid; Q58548; -. DR KO; K03057; -. DR OMA; MEFCDEC; -. DR PhylomeDB; Q58548; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000428; C:DNA-directed RNA polymerase complex; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; ISS:UniProtKB. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; ISS:UniProtKB. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR InterPro; IPR019761; DNA-dir_RNA_pol-M_15_CS. DR InterPro; IPR001529; DNA-dir_RNA_pol_M/15kDasu. DR InterPro; IPR012164; Rpa12/Rpb9/Rpc10/TFS. DR InterPro; IPR006288; TFS. DR InterPro; IPR001222; Znf_TFIIS. DR Pfam; PF02150; RNA_POL_M_15KD; 1. DR Pfam; PF01096; TFIIS_C; 1. DR PIRSF; PIRSF005586; RNApol_RpoM; 1. DR SMART; SM00661; RPOL9; 1. DR SMART; SM00440; ZnF_C2C2; 1. DR TIGRFAMs; TIGR01384; TFS_arch; 1. DR PROSITE; PS01030; RNA_POL_M_15KD; 1. DR PROSITE; PS00466; ZF_TFIIS_1; 1. DR PROSITE; PS51133; ZF_TFIIS_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Metal-binding; Reference proteome; KW Transcription; Transcription regulation; Zinc; Zinc-finger. FT CHAIN 1 108 Transcription factor S. FT /FTId=PRO_0000121481. FT ZN_FING 5 24 C4-type. {ECO:0000255}. FT ZN_FING 65 105 TFIIS-type. {ECO:0000255|PROSITE- FT ProRule:PRU00472}. FT METAL 69 69 Zinc. {ECO:0000250|UniProtKB:Q56254}. FT METAL 72 72 Zinc. {ECO:0000250|UniProtKB:Q56254}. FT METAL 97 97 Zinc. {ECO:0000250|UniProtKB:Q56254}. FT METAL 100 100 Zinc. {ECO:0000250|UniProtKB:Q56254}. SQ SEQUENCE 108 AA; 12750 MW; 33AE963C576AD1BC CRC64; MVKFCPKCNN LMLPKDGKLK CAVCGYEEET TAEGSKEYEY KEHLENKKEK ITVIESEGLE TLPTTRIECP KCGHNEAYWW LQQTRCADEP ETRFYKCKKC GHTWREYD // ID THIC_METJA Reviewed; 426 AA. AC Q58432; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-2002, sequence version 2. DT 17-FEB-2016, entry version 90. DE RecName: Full=Phosphomethylpyrimidine synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE EC=4.1.99.17 {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Hydroxymethylpyrimidine phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-P synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMP-phosphate synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE Short=HMPP synthase {ECO:0000255|HAMAP-Rule:MF_00089}; DE AltName: Full=Thiamine biosynthesis protein ThiC {ECO:0000255|HAMAP-Rule:MF_00089}; GN Name=thiC {ECO:0000255|HAMAP-Rule:MF_00089}; OrderedLocusNames=MJ1026; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the synthesis of the hydroxymethylpyrimidine CC phosphate (HMP-P) moiety of thiamine from aminoimidazole ribotide CC (AIR) in a radical S-adenosyl-L-methionine (SAM)-dependent CC reaction. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- CATALYTIC ACTIVITY: 5-amino-1-(5-phospho-D-ribosyl)imidazole + S- CC adenosyl-L-methionine = 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine + 5'-deoxyadenosine + L-methionine + CC formate + CO. {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00089}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. The cluster is CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000255|HAMAP-Rule:MF_00089}; CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00089}. CC -!- SIMILARITY: Belongs to the ThiC family. {ECO:0000255|HAMAP- CC Rule:MF_00089}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99030.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99030.1; ALT_INIT; Genomic_DNA. DR PIR; A64428; A64428. DR ProteinModelPortal; Q58432; -. DR STRING; 243232.MJ_1026; -. DR EnsemblBacteria; AAB99030; AAB99030; MJ_1026. DR KEGG; mja:MJ_1026; -. DR eggNOG; arCOG02741; Archaea. DR eggNOG; COG0422; LUCA. DR InParanoid; Q58432; -. DR KO; K03147; -. DR OMA; MTLHCGI; -. DR PhylomeDB; Q58432; -. DR UniPathway; UPA00060; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR HAMAP; MF_00089; ThiC; 1. DR InterPro; IPR002817; ThiC. DR Pfam; PF01964; ThiC_Rad_SAM; 1. DR TIGRFAMs; TIGR00190; thiC; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Thiamine biosynthesis; KW Zinc. FT CHAIN 1 426 Phosphomethylpyrimidine synthase. FT /FTId=PRO_0000152862. FT REGION 184 186 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT REGION 225 228 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT METAL 268 268 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 332 332 Zinc. {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 408 408 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 411 411 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT METAL 415 415 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|HAMAP-Rule:MF_00089}. FT BINDING 65 65 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 94 94 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 123 123 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 162 162 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 264 264 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. FT BINDING 291 291 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00089}. SQ SEQUENCE 426 AA; 47477 MW; 7B17477FA327E8EB CRC64; MTQMDDAKNG IITEEMKIVA EKEKIDIEKL RKLIAKGYVV ILKNVNRDTN PVGIGQSLRT KVNANIGTSP DCVDIELEIK KAKIAEKYGA DAVMDLSTGG NLEEIRKAIM DAVKIPIGTV PIYEVGKLAR EKYGRVIDMN EDLMFKVIEK QAKEGVDFMT LHCGITKQSV ERLKRSGRIM GVVSRGGAFL TAYILYHNEE NPLYKNFDYL LDILKEHDVT ISLGDGMRPG CLADNTDRAQ IEELITLGEL VERCREKGVQ CMVEGPGHIP INYIETNIRL QKSLCKNAPF YVLGPIVTDI APGYDHITAA IGGALAGYYG ADFLCYVTPS EHLRLPTIED VKEGVIATKI AAQAADVAKG NKLAWEKETE MAYARKNHDW EKQFELAIDK EKARKMREEI PSKEEKACSI CGDYCALLMV EELGKR // ID TBP_METJA Reviewed; 183 AA. AC Q57930; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=TATA-box-binding protein; DE AltName: Full=Box A-binding protein; DE Short=BAP; DE AltName: Full=TATA sequence-binding protein; DE Short=TBP; DE AltName: Full=TATA-box factor; GN Name=tbp; OrderedLocusNames=MJ0507; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 4-183. RX PubMed=19090808; DOI=10.1111/j.1365-2443.2008.01233.x; RA Adachi N., Senda M., Natsume R., Senda T., Horikoshi M.; RT "Crystal structure of Methanococcus jannaschii TATA box-binding RT protein."; RL Genes Cells 13:1127-1140(2008). CC -!- FUNCTION: General factor that plays a role in the activation of CC archaeal genes transcribed by RNA polymerase. Binds specifically CC to the TATA box promoter element which lies close to the position CC of transcription initiation (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TBP family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98497.1; -; Genomic_DNA. DR PIR; C64363; C64363. DR PDB; 2Z8U; X-ray; 1.90 A; A/B/P/Q=4-183. DR PDBsum; 2Z8U; -. DR ProteinModelPortal; Q57930; -. DR STRING; 243232.MJ_0507; -. DR EnsemblBacteria; AAB98497; AAB98497; MJ_0507. DR KEGG; mja:MJ_0507; -. DR eggNOG; arCOG01764; Archaea. DR eggNOG; COG2101; LUCA. DR InParanoid; Q57930; -. DR KO; K03120; -. DR OMA; MDCLEAI; -. DR PhylomeDB; Q57930; -. DR EvolutionaryTrace; Q57930; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 3.30.310.10; -; 2. DR HAMAP; MF_00408; TATA_bind_prot_arch; 1. DR InterPro; IPR012295; Beta2_adaptin/TBP_C_dom. DR InterPro; IPR000814; TBP. DR InterPro; IPR030491; TBP_CS. DR PANTHER; PTHR10126; PTHR10126; 1. DR Pfam; PF00352; TBP; 2. DR PRINTS; PR00686; TIFACTORIID. DR PROSITE; PS00351; TFIID; 2. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome; KW Repeat; Transcription; Transcription regulation. FT CHAIN 1 183 TATA-box-binding protein. FT /FTId=PRO_0000154008. FT REPEAT 10 86 1. FT REPEAT 101 177 2. FT STRAND 9 18 {ECO:0000244|PDB:2Z8U}. FT HELIX 25 31 {ECO:0000244|PDB:2Z8U}. FT TURN 39 41 {ECO:0000244|PDB:2Z8U}. FT STRAND 45 49 {ECO:0000244|PDB:2Z8U}. FT TURN 50 53 {ECO:0000244|PDB:2Z8U}. FT STRAND 54 58 {ECO:0000244|PDB:2Z8U}. FT STRAND 62 71 {ECO:0000244|PDB:2Z8U}. FT HELIX 72 88 {ECO:0000244|PDB:2Z8U}. FT STRAND 100 109 {ECO:0000244|PDB:2Z8U}. FT HELIX 116 122 {ECO:0000244|PDB:2Z8U}. FT STRAND 126 128 {ECO:0000244|PDB:2Z8U}. FT TURN 130 132 {ECO:0000244|PDB:2Z8U}. FT STRAND 133 140 {ECO:0000244|PDB:2Z8U}. FT TURN 141 144 {ECO:0000244|PDB:2Z8U}. FT STRAND 145 149 {ECO:0000244|PDB:2Z8U}. FT STRAND 153 159 {ECO:0000244|PDB:2Z8U}. FT HELIX 163 180 {ECO:0000244|PDB:2Z8U}. SQ SEQUENCE 183 AA; 20233 MW; 3C648FA0FC404944 CRC64; MKIMEPEIKI VNVVVSTKIG DNIDLEEVAM ILENAEYEPE QFPGLVCRLS VPKVALLIFR SGKVNCTGAK SKEEAEIAIK KIIKELKDAG IDVIENPEIK IQNMVATADL GIEPNLDDIA LMVEGTEYEP EQFPGLVYRL DDPKVVVLIF GSGKVVITGL KSEEDAKRAL KKILDTIKEV QEL // ID TFE_METJA Reviewed; 173 AA. AC Q58187; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 09-DEC-2015, entry version 91. DE RecName: Full=Transcription factor E; DE Short=TFE; DE AltName: Full=TFIIE subunit alpha homolog; DE AltName: Full=Transcription initiation factor TFIIE; GN Name=tfe; OrderedLocusNames=MJ0777; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND SUBUNIT. RX PubMed=15485836; DOI=10.1074/jbc.C400446200; RA Ouhammouch M., Werner F., Weinzierl R.O., Geiduschek E.P.; RT "A fully recombinant system for activator-dependent archaeal RT transcription."; RL J. Biol. Chem. 279:51719-51721(2004). RN [3] RP FUNCTION, AND INTERACTION WITH TBP AND RNA POLYMERASE. RX PubMed=16135821; DOI=10.1128/MCB.25.18.8344-8355.2005; RA Werner F., Weinzierl R.O.; RT "Direct modulation of RNA polymerase core functions by basal RT transcription factors."; RL Mol. Cell. Biol. 25:8344-8355(2005). CC -!- FUNCTION: Transcription factor that plays a role in the activation CC of archaeal genes transcribed by RNA polymerase. Facilitates CC transcription initiation by enhancing TATA-box recognition by CC TATA-box-binding protein (Tbp), and transcription factor B (Tfb) CC and RNA polymerase recruitment. Not absolutely required for CC transcription in vitro, but particularly important in cases where CC Tbp or Tfb function is not optimal. It dynamically alters the CC nucleic acid-binding properties of RNA polymerases by stabilizing CC the initiation complex and destabilizing elongation complexes. CC Seems to translocate with the RNA polymerase following initiation CC and acts by binding to the non template strand of the CC transcription bubble in elongation complexes. CC {ECO:0000269|PubMed:15485836, ECO:0000269|PubMed:16135821}. CC -!- SUBUNIT: Monomer (By similarity). Interaction with RNA polymerase CC subunits RpoF and RpoE is necessary for Tfe stimulatory CC transcription activity. Able to interact with RNA polymerase in CC the absence of Tbp or DNA promoter. Interacts both with the CC preinitiation and elongation complexes (By similarity). CC {ECO:0000250}. CC -!- DOMAIN: The winged helix domain is involved in binding to DNA in CC the preinitiation complex. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TFE family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HTH TFE/IIEalpha-type domain. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98767.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98767.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q58187; -. DR STRING; 243232.MJ_0777; -. DR EnsemblBacteria; AAB98767; AAB98767; MJ_0777. DR KEGG; mja:MJ_0777; -. DR eggNOG; arCOG04270; Archaea. DR eggNOG; COG1675; LUCA. DR InParanoid; Q58187; -. DR KO; K03136; -. DR OMA; DSGWLTY; -. DR PhylomeDB; Q58187; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-HAMAP. DR GO; GO:0006367; P:transcription initiation from RNA polymerase II promoter; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_01909; TFE_arch; 1. DR InterPro; IPR016481; TF_E_archaea. DR InterPro; IPR017919; TFIIE/TFIIEa_HTH. DR InterPro; IPR002853; TFIIE_asu. DR InterPro; IPR024550; TFIIEa/SarR/Rpc3_HTH_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR InterPro; IPR013137; Znf_TFIIB. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR Pfam; PF02002; TFIIE_alpha; 1. DR PIRSF; PIRSF006373; TF_E_archaea; 1. DR SMART; SM00531; TFIIE; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR TIGRFAMs; TIGR00373; TIGR00373; 1. DR PROSITE; PS51344; HTH_TFE_IIE; 1. PE 1: Evidence at protein level; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 173 Transcription factor E. FT /FTId=PRO_0000107028. FT DOMAIN 3 88 HTH TFE/IIEalpha-type. SQ SEQUENCE 173 AA; 20667 MW; F78759126582C7B6 CRC64; MLNDPLVQEV LFNIFEGDEK GFEVIDVLLE KGETTEEEIA KELGVKLNVV RKLLYKLYDA RLVDYKRWKD EDTNWYSYTW LPTLEKLPYV VKKKINELIK DLEKKLEFEK NNMFFFCPNC NVRFTFEEAM DYGFSCPGCG NMLQEFDNSE LIKDLEEQIK FLKEELKNNP FLK // ID THIDN_METJA Reviewed; 417 AA. AC Q57688; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 25-JAN-2012, sequence version 2. DT 17-FEB-2016, entry version 85. DE RecName: Full=Bifunctional thiamine biosynthesis protein ThiDN; DE Includes: DE RecName: Full=Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase; DE EC=2.7.1.49 {ECO:0000250|UniProtKB:P76422}; DE EC=2.7.4.7 {ECO:0000250|UniProtKB:P76422}; DE AltName: Full=Hydroxymethylpyrimidine kinase; DE Short=HMP kinase; DE AltName: Full=Hydroxymethylpyrimidine phosphate kinase; DE Short=HMP-P kinase; DE Short=HMP-phosphate kinase; DE Short=HMPP kinase; DE Includes: DE RecName: Full=Thiamine-phosphate synthase ThiN; DE Short=TP synthase; DE Short=TPS; DE EC=2.5.1.3; DE AltName: Full=Thiamine-phosphate pyrophosphorylase; DE Short=TMP pyrophosphorylase; DE Short=TMP-PPase; GN Name=thiDN; OrderedLocusNames=MJ0236; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.03 ANGSTROMS) OF 236-416. RG New York structural genomix research consortium (NYSGXRC); RT "Crystal structure of the C-terminal domain of protein MJ0236 RT (Y236_METJA)."; RL Submitted (FEB-2009) to the PDB data bank. CC -!- FUNCTION: Catalyzes the phosphorylation of hydroxymethylpyrimidine CC phosphate (HMP-P) to HMP-PP, and of HMP to HMP-P. CC {ECO:0000250|UniProtKB:P76422}. CC -!- FUNCTION: Condenses 4-methyl-5-(beta-hydroxyethyl)thiazole CC monophosphate (THZ-P) and 4-amino-5-hydroxymethyl pyrimidine CC pyrophosphate (HMP-PP) to form thiamine monophosphate (TMP). CC {ECO:0000250|UniProtKB:Q9WZP7}. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-5-hydroxymethyl-2- CC methylpyrimidine = ADP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine. {ECO:0000250|UniProtKB:P76422}. CC -!- CATALYTIC ACTIVITY: ATP + 4-amino-2-methyl-5- CC (phosphomethyl)pyrimidine = ADP + 4-amino-2-methyl-5- CC (diphosphomethyl)pyrimidine. {ECO:0000250|UniProtKB:P76422}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-((2R,5Z)-2-carboxy-4-methylthiazol-5(2H)-ylidene)ethyl phosphate CC = diphosphate + thiamine phosphate + CO(2). CC {ECO:0000250|UniProtKB:Q9WZP7}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 2-(2-carboxy-4-methylthiazol-5-yl)ethyl phosphate = diphosphate + CC thiamine phosphate + CO(2). {ECO:0000250|UniProtKB:Q9WZP7}. CC -!- CATALYTIC ACTIVITY: 4-amino-2-methyl-5-diphosphomethylpyrimidine + CC 4-methyl-5-(2-phosphono-oxyethyl)thiazole = diphosphate + thiamine CC phosphate. {ECO:0000250|UniProtKB:Q9WZP7}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC 4-amino-2-methyl-5-diphosphomethylpyrimidine from 5-amino-1-(5- CC phospho-D-ribosyl)imidazole. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine phosphate from 4-amino-2-methyl-5- CC diphosphomethylpyrimidine and 4-methyl-5-(2-phosphoethyl)- CC thiazole: step 1/1. CC -!- SIMILARITY: In the N-terminal section; belongs to the ThiD family. CC {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the ThiN family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98222.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98222.1; ALT_INIT; Genomic_DNA. DR PIR; E64329; E64329. DR PDB; 2PHP; X-ray; 2.03 A; A/B/D/E=236-416. DR PDBsum; 2PHP; -. DR ProteinModelPortal; Q57688; -. DR STRING; 243232.MJ_0236; -. DR EnsemblBacteria; AAB98222; AAB98222; MJ_0236. DR KEGG; mja:MJ_0236; -. DR eggNOG; arCOG00020; Archaea. DR eggNOG; COG0351; LUCA. DR eggNOG; COG1992; LUCA. DR InParanoid; Q57688; -. DR KO; K00941; -. DR UniPathway; UPA00060; UER00141. DR EvolutionaryTrace; Q57688; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008902; F:hydroxymethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0008972; F:phosphomethylpyrimidine kinase activity; IEA:UniProtKB-EC. DR GO; GO:0004789; F:thiamine-phosphate diphosphorylase activity; IEA:UniProtKB-EC. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.1190.20; -; 1. DR Gene3D; 3.40.225.10; -; 1. DR InterPro; IPR001303; Aldolase_II/adducin_N. DR InterPro; IPR013749; PM/HMP-P_kinase-1. DR InterPro; IPR029056; Ribokinase-like. DR InterPro; IPR019293; ThiN. DR Pfam; PF08543; Phos_pyr_kin; 1. DR Pfam; PF10120; ThiP_synth; 1. DR SUPFAM; SSF53613; SSF53613; 1. DR SUPFAM; SSF53639; SSF53639; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Kinase; KW Multifunctional enzyme; Nucleotide-binding; Reference proteome; KW Thiamine biosynthesis; Transferase. FT CHAIN 1 417 Bifunctional thiamine biosynthesis FT protein ThiDN. FT /FTId=PRO_0000106755. FT REGION 1 235 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine kinase. FT REGION 236 417 Thiamine-phosphate synthase. FT BINDING 41 41 Hydroxymethylpyrimidine/ FT phosphomethylpyrimidine. {ECO:0000250}. FT HELIX 240 255 {ECO:0000244|PDB:2PHP}. FT STRAND 269 272 {ECO:0000244|PDB:2PHP}. FT HELIX 279 281 {ECO:0000244|PDB:2PHP}. FT STRAND 282 287 {ECO:0000244|PDB:2PHP}. FT STRAND 289 291 {ECO:0000244|PDB:2PHP}. FT STRAND 295 299 {ECO:0000244|PDB:2PHP}. FT STRAND 303 305 {ECO:0000244|PDB:2PHP}. FT HELIX 309 319 {ECO:0000244|PDB:2PHP}. FT STRAND 327 331 {ECO:0000244|PDB:2PHP}. FT HELIX 335 341 {ECO:0000244|PDB:2PHP}. FT TURN 342 344 {ECO:0000244|PDB:2PHP}. FT STRAND 347 349 {ECO:0000244|PDB:2PHP}. FT HELIX 352 354 {ECO:0000244|PDB:2PHP}. FT HELIX 361 373 {ECO:0000244|PDB:2PHP}. FT STRAND 378 382 {ECO:0000244|PDB:2PHP}. FT STRAND 391 398 {ECO:0000244|PDB:2PHP}. FT HELIX 399 414 {ECO:0000244|PDB:2PHP}. SQ SEQUENCE 417 AA; 47056 MW; 810246AD46805E27 CRC64; MVILAIGGYD PTSGAGISAD IKTAHTLGVY CPTITTSVIP QNNKMVYEKF DLPEENIKNQ FKAVFEEFDI EYVKTGVLTK PAIDTLLKYI DKYDLKVICD PVLASTTKFS FVDEKLMEKY IELFNKSFLI TPNKEEYKKI MEFIKNNNLM IRNDLYILAT GIDDILMKNF KPIKTFKGFR VDKEVHGTGC VYSTAITAFL SKGYDLEEAI KEAKRFVLSS VIYAKKSKFG YNSNPTYINK EKVIKNLSYA IYLLKKMNFT LIPEVGSNIA ESLPFPKDFK DVAALTGRII KNKLGGFYIV GDIEFGASEH IAKIILSASK FNPEIRACMN IKYDGGLIKL LKDKFAVSSF DRKEEPPNVS TMEWGTKIAC EKFGGVPDII YDRGGEGKEP MIRVLGRDAI EVVKKVEVIQ KIYNTLM // ID THIO_METJA Reviewed; 85 AA. AC Q57755; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 107. DE RecName: Full=Thioredoxin; GN Name=trx; OrderedLocusNames=MJ0307; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND STRUCTURE BY NMR. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10828983; DOI=10.1021/bi000035b; RA Lee D.Y., Ahn B.-Y., Kim K.-S.; RT "A thioredoxin from the hyperthermophilic archaeon Methanococcus RT jannaschii has a glutaredoxin-like fold but thioredoxin-like RT activities."; RL Biochemistry 39:6652-6659(2000). CC -!- FUNCTION: Acts to maintain redox homeostasis; functions as a CC protein disulfide reductase. {ECO:0000269|PubMed:10828983}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Redox potential: CC E(0) is -277 mV.; CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the glutaredoxin family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 glutaredoxin domain. {ECO:0000255|PROSITE- CC ProRule:PRU00686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98293.1; -; Genomic_DNA. DR PIR; D64338; D64338. DR PDB; 1FO5; NMR; -; A=1-85. DR PDBsum; 1FO5; -. DR ProteinModelPortal; Q57755; -. DR SMR; Q57755; 1-85. DR STRING; 243232.MJ_0307; -. DR EnsemblBacteria; AAB98293; AAB98293; MJ_0307. DR KEGG; mja:MJ_0307; -. DR eggNOG; arCOG01972; Archaea. DR eggNOG; COG0526; LUCA. DR InParanoid; Q57755; -. DR OMA; YGIMAVP; -. DR PhylomeDB; Q57755; -. DR EvolutionaryTrace; Q57755; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0016671; F:oxidoreductase activity, acting on a sulfur group of donors, disulfide as acceptor; IBA:GO_Central. DR GO; GO:0015035; F:protein disulfide oxidoreductase activity; IBA:GO_Central. DR GO; GO:0045454; P:cell redox homeostasis; IBA:GO_Central. DR GO; GO:0034599; P:cellular response to oxidative stress; IBA:GO_Central. DR GO; GO:0006662; P:glycerol ether metabolic process; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006457; P:protein folding; IBA:GO_Central. DR GO; GO:0000103; P:sulfate assimilation; IBA:GO_Central. DR Gene3D; 3.40.30.10; -; 1. DR InterPro; IPR011767; GLR_AS. DR InterPro; IPR002109; Glutaredoxin. DR InterPro; IPR004502; Thio_glut. DR InterPro; IPR005746; Thioredoxin. DR InterPro; IPR012336; Thioredoxin-like_fold. DR PANTHER; PTHR10438; PTHR10438; 1. DR Pfam; PF13192; Thioredoxin_3; 1. DR SUPFAM; SSF52833; SSF52833; 1. DR TIGRFAMs; TIGR00411; redox_disulf_1; 1. DR PROSITE; PS00195; GLUTAREDOXIN_1; 1. DR PROSITE; PS51354; GLUTAREDOXIN_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Disulfide bond; KW Electron transport; Redox-active center; Reference proteome; KW Transport. FT CHAIN 1 85 Thioredoxin. FT /FTId=PRO_0000141645. FT DOMAIN 1 85 Glutaredoxin. {ECO:0000255|PROSITE- FT ProRule:PRU00686}. FT DISULFID 14 17 Redox-active. FT STRAND 4 10 {ECO:0000244|PDB:1FO5}. FT HELIX 20 30 {ECO:0000244|PDB:1FO5}. FT STRAND 32 45 {ECO:0000244|PDB:1FO5}. FT TURN 48 50 {ECO:0000244|PDB:1FO5}. FT TURN 52 54 {ECO:0000244|PDB:1FO5}. FT STRAND 57 62 {ECO:0000244|PDB:1FO5}. FT STRAND 65 67 {ECO:0000244|PDB:1FO5}. FT STRAND 70 74 {ECO:0000244|PDB:1FO5}. FT HELIX 75 84 {ECO:0000244|PDB:1FO5}. SQ SEQUENCE 85 AA; 9404 MW; A38309843CD81A2D CRC64; MSKVKIELFT SPMCPHCPAA KRVVEEVANE MPDAVEVEYI NVMENPQKAM EYGIMAVPTI VINGDVEFIG APTKEALVEA IKKRL // ID TIAS_METJA Reviewed; 423 AA. AC Q58495; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=tRNA(Ile2) 2-agmatinylcytidine synthetase TiaS {ECO:0000255|HAMAP-Rule:MF_01892}; DE Short=tRNA(Ile2)-agm2C synthetase {ECO:0000255|HAMAP-Rule:MF_01892}; DE EC=6.3.4.22 {ECO:0000255|HAMAP-Rule:MF_01892}; DE AltName: Full=tRNA(Ile2) agmatidine synthetase {ECO:0000255|HAMAP-Rule:MF_01892}; GN Name=tiaS {ECO:0000255|HAMAP-Rule:MF_01892}; OrderedLocusNames=MJ1095; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: ATP-dependent agmatine transferase that catalyzes the CC formation of 2-agmatinylcytidine (agm2C) at the wobble position CC (C34) of tRNA(Ile2), converting the codon specificity from AUG to CC AUA. {ECO:0000255|HAMAP-Rule:MF_01892}. CC -!- CATALYTIC ACTIVITY: ATP + agmatine + (tRNA(Ile)(2))-cytidine(34) + CC H(2)O = (tRNA(Ile)(2))-2-agmatinylcytidine(34) + AMP + 2 CC phosphate. {ECO:0000255|HAMAP-Rule:MF_01892}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01892}. CC -!- SIMILARITY: Belongs to the TiaS family. {ECO:0000255|HAMAP- CC Rule:MF_01892}. CC -!- SIMILARITY: Contains 1 OB DNA-binding domain. {ECO:0000255|HAMAP- CC Rule:MF_01892}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99098.1; -; Genomic_DNA. DR PIR; F64436; F64436. DR ProteinModelPortal; Q58495; -. DR STRING; 243232.MJ_1095; -. DR EnsemblBacteria; AAB99098; AAB99098; MJ_1095. DR KEGG; mja:MJ_1095; -. DR eggNOG; arCOG01115; Archaea. DR eggNOG; COG1571; LUCA. DR InParanoid; Q58495; -. DR KO; K06932; -. DR OMA; GMCTTYL; -. DR PhylomeDB; Q58495; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016879; F:ligase activity, forming carbon-nitrogen bonds; IEA:UniProtKB-HAMAP. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0002101; P:tRNA wobble cytosine modification; IEA:UniProtKB-HAMAP. DR Gene3D; 2.40.50.140; -; 1. DR HAMAP; MF_01892; tRNA_Ile2_agm2C_synt; 1. DR InterPro; IPR013696; DUF1743. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR InterPro; IPR024913; tRNA_Ile2__agm2C_synt. DR Pfam; PF08489; DUF1743; 1. DR Pfam; PF01336; tRNA_anti-codon; 1. DR SUPFAM; SSF50249; SSF50249; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Ligase; Nucleotide-binding; KW Reference proteome; tRNA processing. FT CHAIN 1 423 tRNA(Ile2) 2-agmatinylcytidine synthetase FT TiaS. FT /FTId=PRO_0000107166. FT DNA_BIND 273 347 OB. {ECO:0000255|HAMAP-Rule:MF_01892}. SQ SEQUENCE 423 AA; 48557 MW; 2B8936E352DB74BB CRC64; MVMMFIGIDD TDSPNKYCTT YIATLLIEEL KGCGYSVDMP KLIRMNPMVK YKTRGNGGVA IHILDELYSK DKEEIKNITI SLVEKYTDFE CENTNPGIVF LDEAKYKENR EKLTNYYKKV LYDIVSVDYA EKFILKVGGE FIKYKLGRGI IGALGAISST PPYTYELLAY RKKEMWGKKR EIDEKSVIEM DKETFPYTFD NYDYENEKIL IAPNTPCPVL FGIRGIDAEI LLKAMHKIEG EKPERFMIFK TNHGTDVHLR KMNIKDIYPN TGVIVYGRVV EEPRDIEGGH VIFKLSDGTG EIDCMAYEPT KGFRDIIRKL IVGDYIAVYG TVREKPLGIN IEKIKILKLE KKFVKDKRCP YCGGTLKAKG KKAGYKCKKC KKTIAYDEIK MIEVERDLKT GFYEVPGSAR RHLSKPIQLI DLI // ID TF2B_METJA Reviewed; 673 AA. AC Q58192; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 118. DE RecName: Full=Transcription initiation factor IIB; DE Short=TFIIB; DE Contains: DE RecName: Full=Endonuclease Mja Tfb; DE EC=3.1.-.-; DE AltName: Full=Mja TFIIB intein; DE AltName: Full=Mja Tfb intein; GN Name=tfb; OrderedLocusNames=MJ0782; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Stabilizes TBP binding to an archaeal box-A promoter. CC Also responsible for recruiting RNA polymerase II to the pre- CC initiation complex (DNA-TBP-TFIIB). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TFIIB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 TFIIB-type zinc finger. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98771.1; -; Genomic_DNA. DR PIR; F64397; F64397. DR ProteinModelPortal; Q58192; -. DR SMR; Q58192; 41-83, 477-673. DR STRING; 243232.MJ_0782; -. DR EnsemblBacteria; AAB98771; AAB98771; MJ_0782. DR KEGG; mja:MJ_0782; -. DR eggNOG; arCOG01981; Archaea. DR eggNOG; COG1372; LUCA. DR eggNOG; COG1405; LUCA. DR InParanoid; Q58192; -. DR KO; K03124; -. DR OMA; MFEIVVE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.472.10; -; 2. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. DR HAMAP; MF_00383; TF2B_arch; 1. DR InterPro; IPR013763; Cyclin-like. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR000812; TFIIB. DR InterPro; IPR023484; TFIIB_arc. DR InterPro; IPR023486; TFIIB_CS. DR InterPro; IPR013150; TFIIB_cyclin. DR InterPro; IPR013137; Znf_TFIIB. DR PANTHER; PTHR11618; PTHR11618; 2. DR Pfam; PF08271; TF_Zn_Ribbon; 1. DR Pfam; PF00382; TFIIB; 2. DR PRINTS; PR00379; INTEIN. DR PRINTS; PR00685; TIFACTORIIB. DR SMART; SM00385; CYCLIN; 2. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF47954; SSF47954; 2. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF55608; SSF55608; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. DR PROSITE; PS00782; TFIIB; 2. DR PROSITE; PS51134; ZF_TFIIB; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; Endonuclease; Hydrolase; KW Intron homing; Metal-binding; Nuclease; Protein splicing; KW Reference proteome; Repeat; Transcription; Transcription regulation; KW Zinc; Zinc-finger. FT CHAIN 1 99 Transcription initiation factor IIB, 1st FT part. {ECO:0000255}. FT /FTId=PRO_0000033642. FT CHAIN 100 434 Endonuclease Mja Tfb. {ECO:0000255}. FT /FTId=PRO_0000033643. FT CHAIN 435 673 Transcription initiation factor IIB, 2nd FT part. {ECO:0000255}. FT /FTId=PRO_0000033644. FT DOMAIN 238 357 DOD-type homing endonuclease. FT REPEAT 490 573 1. FT REPEAT 584 665 2. FT ZN_FING 38 69 TFIIB-type. FT METAL 42 42 Zinc. {ECO:0000250}. FT METAL 45 45 Zinc. {ECO:0000250}. FT METAL 61 61 Zinc. {ECO:0000250}. FT METAL 64 64 Zinc. {ECO:0000250}. SQ SEQUENCE 673 AA; 76969 MW; 20EA4713EAB031A9 CRC64; MVWLMEALKT KENETTKEKK LTTKVEKSEK KEENVREEEI VCPICGSKEV VKDYERAEIV CAKCGCVIKE KLFDIGPEWR AFDHEQKIKR CRVGAPMTYS VDYNEPIIIK ENGEIKVVKI GELIDKIIEN SENIRREGIL EIAKCKGIEV IAFNSNYKFK FMPVSEVSRH PVSEMFEIVV EGNKKVRVTR SHSVFTIRDN EVVPIRVDEL KVGDILVLAK ELPNIEEDIE IDKKFSKILG YIIAEGYYDD KKIVLSYDYN EKEFINETID YFKSLNSDIT IYSKDLNIQI EVKNKKIINL LKKLRVKNKR IPSIIFKSPY EIKKSFIDGI FNGKDAKVFV SKELAEDVIF LLLQIKENAT INKKSINDIE VYEVRRITNI YTNRKLEKLI NSDFIFLKIK EINKVEPTSG YAYDLTVPNA ENFVAGFGGF VLHNTIHDKG LSTVIDWRNK DSYGKDLSAN KRAQLYRLRK WQRRIRVSDA AERNLAFALS ELDRITSKLG LPRHVRENAA IIYRGAVEKG LIRGRSIEGV VAAAIYAACR RCRVPRTLDE IAEASRVDRK EIGRTYRFLA RELNIKLTPT NPIDYVPRFA SELGLPGEVE SKAIQILQQA AEKGLTSGRG PTGVAAAAIY IASVLLGCRR TQREVAEVAG VTEVTIRNRY KELTEHLDID VTL // ID THPR_METJA Reviewed; 173 AA. AC Q58963; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=RNA 2',3'-cyclic phosphodiesterase {ECO:0000255|HAMAP-Rule:MF_01940}; DE Short=RNA 2',3'-CPDase {ECO:0000255|HAMAP-Rule:MF_01940}; DE EC=3.1.4.- {ECO:0000255|HAMAP-Rule:MF_01940}; GN OrderedLocusNames=MJ1568; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Hydrolyzes RNA 2',3'-cyclic phosphodiester to an RNA 2'- CC phosphomonoester. {ECO:0000255|HAMAP-Rule:MF_01940}. CC -!- SIMILARITY: Belongs to the 2H phosphoesterase superfamily. ThpR CC family. {ECO:0000255|HAMAP-Rule:MF_01940}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99586.1; -; Genomic_DNA. DR PIR; G64495; G64495. DR ProteinModelPortal; Q58963; -. DR STRING; 243232.MJ_1568; -. DR EnsemblBacteria; AAB99586; AAB99586; MJ_1568. DR KEGG; mja:MJ_1568; -. DR eggNOG; arCOG01736; Archaea. DR eggNOG; COG1514; LUCA. DR InParanoid; Q58963; -. DR KO; K01975; -. DR OMA; IGVFPNP; -. DR PhylomeDB; Q58963; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004113; F:2',3'-cyclic-nucleotide 3'-phosphodiesterase activity; IEA:InterPro. DR GO; GO:0008664; F:2'-5'-RNA ligase activity; IEA:InterPro. DR Gene3D; 3.90.1140.10; -; 1. DR HAMAP; MF_01940; RNA_CPDase; 1. DR InterPro; IPR014051; Phosphoesterase_HXTX. DR InterPro; IPR004175; RNA_CPDase. DR InterPro; IPR009097; RNA_ligase/cNuc_Pdiesterase. DR Pfam; PF02834; LigT_PEase; 2. DR SUPFAM; SSF55144; SSF55144; 1. DR TIGRFAMs; TIGR02258; 2_5_ligase; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 173 RNA 2',3'-cyclic phosphodiesterase. FT /FTId=PRO_0000138963. FT MOTIF 38 41 HXTX 1. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT MOTIF 118 121 HXTX 2. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT ACT_SITE 38 38 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_01940}. FT ACT_SITE 118 118 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01940}. SQ SEQUENCE 173 AA; 20545 MW; 34F03BCE0159E5B1 CRC64; MRLFLAIDIP ENIKEEIAKF QEQFKMKGIK LVEKENLHIT VKFLGEVDEE KLKEILNLDL SIQPIKIKLK YIGTFPNSNY IRVIWIGAYN NNLVEIFKEI DEKLSNLGFK KEREYVPHLT IGRVKFIDNK KKLKDRIEKY KDVDFGEFEA KHIKLYKSTL TPNGPIYEVI KEW // ID THIL_METJA Reviewed; 319 AA. AC Q60337; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Thiamine-monophosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE Short=TMP kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE Short=Thiamine-phosphate kinase {ECO:0000255|HAMAP-Rule:MF_02128}; DE EC=2.7.4.16 {ECO:0000255|HAMAP-Rule:MF_02128}; GN Name=thiL {ECO:0000255|HAMAP-Rule:MF_02128}; OrderedLocusNames=MJ0028; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the ATP-dependent phosphorylation of thiamine- CC monophosphate (TMP) to form thiamine-pyrophosphate (TPP), the CC active form of vitamin B1. {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- CATALYTIC ACTIVITY: ATP + thiamine phosphate = ADP + thiamine CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- PATHWAY: Cofactor biosynthesis; thiamine diphosphate biosynthesis; CC thiamine diphosphate from thiamine phosphate: step 1/1. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- MISCELLANEOUS: Reaction mechanism of ThiL seems to utilize a CC direct, inline transfer of the gamma-phosphate of ATP to TMP CC rather than a phosphorylated enzyme intermediate. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC -!- SIMILARITY: Belongs to the thiamine-monophosphate kinase family. CC {ECO:0000255|HAMAP-Rule:MF_02128}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98008.1; -; Genomic_DNA. DR PIR; D64303; D64303. DR ProteinModelPortal; Q60337; -. DR STRING; 243232.MJ_0028; -. DR DNASU; 1450866; -. DR EnsemblBacteria; AAB98008; AAB98008; MJ_0028. DR KEGG; mja:MJ_0028; -. DR eggNOG; arCOG00638; Archaea. DR eggNOG; COG0611; LUCA. DR InParanoid; Q60337; -. DR KO; K00946; -. DR OMA; IAAMCAK; -. DR PhylomeDB; Q60337; -. DR UniPathway; UPA00060; UER00142. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0009229; P:thiamine diphosphate biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR HAMAP; MF_02128; TMP_kinase; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR006283; ThiL. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR PIRSF; PIRSF005303; Thiam_monoph_kin; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR01379; thiL; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Kinase; Magnesium; Metal-binding; KW Nucleotide-binding; Reference proteome; Thiamine biosynthesis; KW Transferase. FT CHAIN 1 319 Thiamine-monophosphate kinase. FT /FTId=PRO_0000096201. FT NP_BIND 121 122 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 28 28 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 28 28 Magnesium 4; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 43 43 Magnesium 4. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 44 44 Magnesium 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_02128}. FT METAL 45 45 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 45 45 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 73 73 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 73 73 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 73 73 Magnesium 4. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 122 122 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 218 218 Magnesium 3. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT METAL 221 221 Magnesium 5. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 52 52 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 104 104 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT BINDING 145 145 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT BINDING 220 220 ATP. {ECO:0000255|HAMAP-Rule:MF_02128}. FT BINDING 268 268 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. FT BINDING 315 315 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_02128}. SQ SEQUENCE 319 AA; 36160 MW; 92607D5AD59A723F CRC64; MDEMKVIEII KKTLKFSNEN IVKGIDDDCA IIKIDENFYL VATTDMMVKK AHIPSILSPY EIGGRILTAN VSDIASMGAK PLAFLVSISL SKEEANEKFI KELYSGLDDF SKLYDCPVVG GDTNRGDELI LSGTAFGITD NPIYRRGKVG DDICVTNDLG RVYCALTLYY MLKENKISYK EFERLCQKYP KIIEKLRKPI ARIKEGLLMN KLINGCCDIS DGLGKEITYF KNFEIYSDRI FKLIPEDVIE FCDAFNLNPI KVALNSGEEF ELLFTTSKFN KVKDSLKGYS KIYKIGKIIE DGQFIDGEEF YGGGYIHKW // ID TKTC_METJA Reviewed; 316 AA. AC Q58092; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Putative transketolase C-terminal section; DE Short=TK; DE EC=2.2.1.1; GN OrderedLocusNames=MJ0679; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. Corresponds to the CC C-terminal of members of this family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98674.1; -; Genomic_DNA. DR PIR; G64384; G64384. DR ProteinModelPortal; Q58092; -. DR STRING; 243232.MJ_0679; -. DR EnsemblBacteria; AAB98674; AAB98674; MJ_0679. DR KEGG; mja:MJ_0679; -. DR eggNOG; arCOG01051; Archaea. DR eggNOG; COG3958; LUCA. DR InParanoid; Q58092; -. DR KO; K00615; -. DR OMA; PVYVRMP; -. DR PhylomeDB; Q58092; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.920; -; 1. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR009014; Transketo_C/PFOR_II. DR InterPro; IPR005475; Transketolase-like_Pyr-bd. DR InterPro; IPR020826; Transketolase_BS. DR InterPro; IPR033248; Transketolase_C. DR InterPro; IPR033247; Transketolase_fam. DR PANTHER; PTHR11624; PTHR11624; 1. DR Pfam; PF02779; Transket_pyr; 1. DR Pfam; PF02780; Transketolase_C; 1. DR SMART; SM00861; Transket_pyr; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR SUPFAM; SSF52922; SSF52922; 1. DR PROSITE; PS00802; TRANSKETOLASE_2; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome; Thiamine pyrophosphate; KW Transferase. FT CHAIN 1 316 Putative transketolase C-terminal FT section. FT /FTId=PRO_0000191915. SQ SEQUENCE 316 AA; 34580 MW; ABAB04A6DBB35199 CRC64; MVKLSGVYKG MRKGYGETLI ELGKKYENLV VLDADLSGST QTAMFAKEFP ERFFNAGVAE QNMIGMAAGL ATTGKIVFAS SFSMFASGRA WEIIRNLVAY PKLNVKIVAT HAGITVGEDG ASHQMCEDIA IMRAIPNMVV IAPTDYYHTK NVIRTIAEYK GPVYVRMPRR DTEIIYENEE EATFEIGKGK ILVDGEDLTI IATGEEVPEA LRAGEILKEN GISAEIVEMA TIKPIDEEII KKSKDFVVTV EDHSIIGGLG GAVAEVIASN GLNKKLLRIG INDVFGRSGK ADELLKYYGL DGESIAKRIM EEMKKE // ID TKTN_METJA Reviewed; 274 AA. AC Q58094; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Putative transketolase N-terminal section; DE Short=TK; DE EC=2.2.1.1; GN OrderedLocusNames=MJ0681; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Sedoheptulose 7-phosphate + D-glyceraldehyde CC 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate. CC -!- COFACTOR: CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250}; CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250}; CC -!- COFACTOR: CC Name=thiamine diphosphate; Xref=ChEBI:CHEBI:58937; CC Evidence={ECO:0000250}; CC Note=Binds 1 thiamine pyrophosphate per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the transketolase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. Corresponds to the CC N-terminal of members of this family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98676.1; -; Genomic_DNA. DR PIR; A64385; A64385. DR ProteinModelPortal; Q58094; -. DR STRING; 243232.MJ_0681; -. DR EnsemblBacteria; AAB98676; AAB98676; MJ_0681. DR KEGG; mja:MJ_0681; -. DR eggNOG; arCOG01053; Archaea. DR eggNOG; COG3959; LUCA. DR InParanoid; Q58094; -. DR KO; K00615; -. DR OMA; QIDGCTE; -. DR PhylomeDB; Q58094; -. DR BioCyc; RETL1328306-WGS:GSTH-2412-MONOMER; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004802; F:transketolase activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.970; -; 1. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR033247; Transketolase_fam. DR InterPro; IPR005474; Transketolase_N. DR PANTHER; PTHR11624; PTHR11624; 1. DR Pfam; PF00456; Transketolase_N; 1. DR SUPFAM; SSF52518; SSF52518; 1. DR PROSITE; PS00801; TRANSKETOLASE_1; 1. PE 5: Uncertain; KW Calcium; Complete proteome; Metal-binding; Reference proteome; KW Thiamine pyrophosphate; Transferase. FT CHAIN 1 274 Putative transketolase N-terminal FT section. FT /FTId=PRO_0000191914. FT METAL 149 149 Calcium. {ECO:0000250}. FT METAL 179 179 Calcium. {ECO:0000250}. SQ SEQUENCE 274 AA; 30336 MW; FE3C053AC09F0A4E CRC64; MDNNLEIKDL EKIAKKVRYN IVKMVGLAKS GHPGGSLSAT DIIVALYFKL MNYSPDNPYK KDRDRFVLSK GHAAPALYAV LSELGIIEEE ELWKLRRLEG KLQGHPSMDT PGVEICTGSL GQGFSAAVGM ALGCRLDKLN NYVYVLLGDG ECQEGIVWEA AMAAAHYKLD NLIAFIDRNK LQIDGCTEDV MSLGDIKAKF EAFGWDVFEI DGHNFEEIIN TVEKAKSMKN GKPKMIIAYT VKGKGVSFME NNVAFHGKAP NEEQLKQALE ELSE // ID THRC_METJA Reviewed; 405 AA. AC Q58860; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=Threonine synthase; DE Short=TS; DE EC=4.2.3.1; GN Name=thrC; OrderedLocusNames=MJ1465; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the gamma-elimination of phosphate from L- CC phosphohomoserine and the beta-addition of water to produce L- CC threonine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: O-phospho-L-homoserine + H(2)O = L-threonine + CC phosphate. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L- CC threonine from L-aspartate: step 5/5. CC -!- SIMILARITY: Belongs to the threonine synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99473.1; -; Genomic_DNA. DR PIR; H64482; H64482. DR ProteinModelPortal; Q58860; -. DR SMR; Q58860; 51-387. DR STRING; 243232.MJ_1465; -. DR EnsemblBacteria; AAB99473; AAB99473; MJ_1465. DR KEGG; mja:MJ_1465; -. DR eggNOG; arCOG01434; Archaea. DR eggNOG; COG0498; LUCA. DR InParanoid; Q58860; -. DR KO; K01733; -. DR OMA; REIGVWR; -. DR PhylomeDB; Q58860; -. DR BioCyc; MetaCyc:MONOMER-14634; -. DR UniPathway; UPA00050; UER00065. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004795; F:threonine synthase activity; IBA:GO_Central. DR GO; GO:0009088; P:threonine biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR000634; Ser/Thr_deHydtase_PyrdxlP-BS. DR InterPro; IPR004450; Thr_synthase-like. DR InterPro; IPR026260; Thr_Synthase_bac/arc. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF038945; Thr_synthase; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00260; thrC; 1. DR PROSITE; PS00165; DEHYDRATASE_SER_THR; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Complete proteome; Lyase; KW Pyridoxal phosphate; Reference proteome; Threonine biosynthesis. FT CHAIN 1 405 Threonine synthase. FT /FTId=PRO_0000185642. FT REGION 233 237 Pyridoxal phosphate binding. FT {ECO:0000250}. FT BINDING 132 132 Pyridoxal phosphate. {ECO:0000250}. FT BINDING 371 371 Pyridoxal phosphate. {ECO:0000250}. FT MOD_RES 106 106 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 405 AA; 44601 MW; FAD055FB041E2DF0 CRC64; MLQRCIKCGK TYDVDEIIYT CECGGLLEII YDYEEIKDKV SEEKLRKREI GVWRYLEYLP VKDESKIVSL CEGGTPLYRC NNLEKELGIK ELYVKNEGAN PTGSFKDRGM TVGVTRANEL GVEVVGCAST GNTSASLAAY SARSGKKCIV LLPEGKVALG KLAQAMFYGA KVIQVKGNFD DALDMVKQLA KEKLIYLLNS INPFRLEGQK TIAFEICDQL NWQVPDRVIV PVGNAGNISA IWKGFKEFEI TGIIDELPKM TGIQADGAKP IVEAFRKRAK DIIPYKNPET IATAIRIGNP VNAPKALDAI YSSGGYAEAV TDEEIVEAQK LLARKEGIFV EPASASSIAG LKKLLEEGII DRDERIVCIT TGHGLKDPDA AIRASEEPIK IECDMNVLKR ILKEL // ID THS_METJA Reviewed; 542 AA. AC Q58405; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Thermosome subunit; DE AltName: Full=Chaperonin subunit; GN Name=ths; OrderedLocusNames=MJ0999; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Molecular chaperone; binds unfolded polypeptides in CC vitro, and has a weak ATPase activity. {ECO:0000250}. CC -!- SUBUNIT: Forms an oligomeric complex of eight-membered rings. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TCP-1 chaperonin family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99002.1; -; Genomic_DNA. DR PIR; F64424; F64424. DR ProteinModelPortal; Q58405; -. DR STRING; 243232.MJ_0999; -. DR EnsemblBacteria; AAB99002; AAB99002; MJ_0999. DR KEGG; mja:MJ_0999; -. DR eggNOG; arCOG01257; Archaea. DR eggNOG; COG0459; LUCA. DR InParanoid; Q58405; -. DR OMA; VIEPIRV; -. DR PhylomeDB; Q58405; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.10.560.10; -; 2. DR Gene3D; 3.30.260.10; -; 2. DR Gene3D; 3.50.7.10; -; 1. DR InterPro; IPR017998; Chaperone_TCP-1. DR InterPro; IPR002194; Chaperonin_TCP-1_CS. DR InterPro; IPR002423; Cpn60/TCP-1. DR InterPro; IPR027409; GroEL-like_apical_dom. DR InterPro; IPR027413; GROEL-like_equatorial. DR InterPro; IPR027410; TCP-1-like_intermed. DR InterPro; IPR012714; Thermosome_arc. DR Pfam; PF00118; Cpn60_TCP1; 1. DR PRINTS; PR00304; TCOMPLEXTCP1. DR SUPFAM; SSF52029; SSF52029; 1. DR TIGRFAMs; TIGR02339; thermosome_arch; 1. DR PROSITE; PS00750; TCP1_1; 1. DR PROSITE; PS00751; TCP1_2; 1. DR PROSITE; PS00995; TCP1_3; 1. PE 3: Inferred from homology; KW ATP-binding; Chaperone; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 542 Thermosome subunit. FT /FTId=PRO_0000128390. SQ SEQUENCE 542 AA; 58772 MW; D505F08531D4668D CRC64; MAMAGAPIVV LPQNVKRYVG RDAQRMNILA GRIIAETVRT TLGPKGMDKM LVDELGDIVV TNDGVTILKE MSVEHPAAKM LIEVAKTQEK EVGDGTTTAV VIAGELLRKA EELLDQNIHP SVIINGYEMA RNKAVEELKS IAKEVKPEDT EMLKKIAMTS ITGKGAEKAR EQLAEIVVEA VRAVVDEETG KVDKDLIKVE KKEGAPIEET KLIRGVVIDK ERVNPQMPKK VENAKIALLN CPIEVKETET DAEIRITDPA KLMEFIEQEE KMIKDMVEKI AATGANVVFC QKGIDDLAQH YLAKKGILAV RRVKKSDMEK LAKATGARIV TKIDDLTPED LGEAGLVEER KVAGDAMIFV EQCKHPKAVT ILARGSTEHV VEEVARAIDD AIGVVKCALE EGKIVAGGGA TEIELAKRLR KFAESVAGRE QLAVKAFADA LEVIPRTLAE NSGLDPIDML VKLRAAHEKE GGEVYGLDVF EGEVVDMLEK GVVEPLKVKT QAIDSATEAS VMLLRIDDVI AAEKVKGDEK GGEGGDMGGD EF // ID TMG10_METJA Reviewed; 351 AA. AC Q58120; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=tRNA (guanine(10)-N2)-dimethyltransferase; DE EC=2.1.1.213; DE AltName: Full=tRNA:G10 dimethyltransferase; GN Name=trmG10; OrderedLocusNames=MJ0710; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the adenosylmethionine-dependent methylation CC of the exocyclic amino group (N(2)) of guanosine at position 10 of CC various tRNAs. Acts via a two-step process that leads to the CC formation of either N(2)-monomethyl (m(2)G) or N(2)- CC dimethylguanosine (m(2)(2)G) (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + guanine(10) in CC tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(10) in CC tRNA. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. Trm-G10 CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00529}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98704.1; -; Genomic_DNA. DR PIR; F64388; F64388. DR ProteinModelPortal; Q58120; -. DR STRING; 243232.MJ_0710; -. DR EnsemblBacteria; AAB98704; AAB98704; MJ_0710. DR KEGG; mja:MJ_0710; -. DR eggNOG; arCOG00047; Archaea. DR eggNOG; COG1041; LUCA. DR InParanoid; Q58120; -. DR KO; K07446; -. DR OMA; NGEHEEI; -. DR PhylomeDB; Q58120; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IEA:InterPro. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR000241; RNA_methylase_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004114; THUMP_dom. DR InterPro; IPR005885; TrmG10. DR Pfam; PF02926; THUMP; 1. DR Pfam; PF01170; UPF0020; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR01177; TIGR01177; 1. DR PROSITE; PS51165; THUMP; 1. DR PROSITE; PS01261; UPF0020; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing; KW tRNA-binding. FT CHAIN 1 351 tRNA (guanine(10)-N2)- FT dimethyltransferase. FT /FTId=PRO_0000140481. FT DOMAIN 57 165 THUMP. {ECO:0000255|PROSITE- FT ProRule:PRU00529}. SQ SEQUENCE 351 AA; 40483 MW; 4D0E17229D924E91 CRC64; MIGYVLNGEH EEIPYGELMA LLEIFNYNGS VERLKRYVIT EDSPAKDIVK RSGYIDEGHR IIFRYNLEEK SVDLVDKIVN DFINSFKDFV ANIDYPDIDE SKSYAVRVLK LHKDEFTKSI DSLRIEKEIG GIIKLKTNAK VNLTKPDILV RVVILENTFF ISNVLEMRDR EYFQKNRPHL RKYFHPGCML PKLARAMVNL ARVKEGDIVL DPFCGTGGFL IEAGLIGAKL IGCDIDWRMA SGTLINLEEY NLLDKVIKVK RLDAKYVKEF LNELNIEKVD AIVTDPPYGI STAKKGEIEK ILETLPEVIK DNGYFVFAYP KKIELDMELE GLYKVYIHKG LIRHIHVYKK I // ID TMPS_METJA Reviewed; 260 AA. AC Q58167; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Thymidylate synthase; DE Short=TS; DE Short=TSase; DE EC=2.1.1.-; GN OrderedLocusNames=MJ0757; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION AS A THYMIDYLATE SYNTHASE. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10426953; DOI=10.1038/11525; RA Xu H., Aurora R., Rose G.D., White R.H.; RT "Identifying two ancient enzymes in Archaea using predicted secondary RT structure alignment."; RL Nat. Struct. Biol. 6:750-754(1999). CC -!- FUNCTION: Is able to catalyze the biosynthesis of dTMP using dUMP, CC tetrahydrofolate and formaldehyde in vitro, i.e. a reaction CC equivalent to that catalyzed by bacterial thymidylate synthases CC (EC 2.1.1.45). However, M.jannaschii like most methanogenic CC Archaea lacks folates, thus the physiological cosubstrate is CC unknown but is likely one of the non-methylated methanopterin CC biosynthetic intermediates. {ECO:0000269|PubMed:10426953}. CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98749.1; -; Genomic_DNA. DR PIR; E64394; E64394. DR ProteinModelPortal; Q58167; -. DR STRING; 243232.MJ_0757; -. DR DNASU; 1451634; -. DR EnsemblBacteria; AAB98749; AAB98749; MJ_0757. DR KEGG; mja:MJ_0757; -. DR eggNOG; arCOG02468; Archaea. DR eggNOG; COG1810; LUCA. DR OMA; AHHNYPC; -. DR PhylomeDB; Q58167; -. DR BioCyc; MetaCyc:MONOMER-14571; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004799; F:thymidylate synthase activity; IDA:UniProtKB. DR GO; GO:0006231; P:dTMP biosynthetic process; IDA:UniProtKB. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway. DR InterPro; IPR003745; DUF166. DR Pfam; PF02593; DUF166; 1. PE 1: Evidence at protein level; KW Complete proteome; Methyltransferase; Nucleotide biosynthesis; KW Reference proteome; Transferase. FT CHAIN 1 260 Thymidylate synthase. FT /FTId=PRO_0000107016. SQ SEQUENCE 260 AA; 30434 MW; F0BBD83A4143BF08 CRC64; MVLNINSFYK NCRGEFMRAV FIYHKNNQRM EKFYKNLLNE PDFCRICDDC YNCRGNWTFK NNVKNIVIEE VYEEFVDNPY DYLPELPEGD ICIAQLHEDL LYELPLLLKE KGYKALIVPS ETPHDLSLAL RRDLKRVCSN YNIEFENPKP FCSLEKKEGN EYINKFIDYF KIGKPELEIE VENGLIKDVK VKISAPCGET YYIAKRLKGK AIDDLKEEIA NAHHNYPCLA SMEMDKELGD TILHKAGYIA FEVVEKALKK // ID TRM4_METJA Reviewed; 274 AA. AC Q60343; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=tRNA (cytosine(48)-C(5))-methyltransferase; DE EC=2.1.1.-; DE AltName: Full=aTrm4; DE AltName: Full=tRNA (cytosine-5-)-methyltransferase Trm4; GN Name=trm4; OrderedLocusNames=MJ0026; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.27 ANGSTROMS) IN COMPLEX WITH SINEFUNGIN, RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=20600111; DOI=10.1016/j.jmb.2010.06.046; RA Kuratani M., Hirano M., Goto-Ito S., Itoh Y., Hikida Y., Nishimoto M., RA Sekine S., Bessho Y., Ito T., Grosjean H., Yokoyama S.; RT "Crystal structure of Methanocaldococcus jannaschii Trm4 complexed RT with sinefungin."; RL J. Mol. Biol. 401:323-333(2010). CC -!- FUNCTION: Catalyzes AdoMet-dependent formation of m5C in tRNA. CC Cytidine residue at either position 40 or position 48 is likely to CC be methylated. {ECO:0000269|PubMed:20600111}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytosine(48) in tRNA CC precursor = S-adenosyl-L-homocysteine + 5-methylcytosine(48) in CC tRNA precursor. {ECO:0000269|PubMed:20600111}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. RsmB/NOP family. CC {ECO:0000255|PROSITE-ProRule:PRU01023}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98007.1; -; Genomic_DNA. DR PIR; B64303; B64303. DR PDB; 3A4T; X-ray; 2.30 A; A/B=1-274. DR PDB; 3AJD; X-ray; 1.27 A; A=1-274. DR PDBsum; 3A4T; -. DR PDBsum; 3AJD; -. DR ProteinModelPortal; Q60343; -. DR STRING; 243232.MJ_0026; -. DR EnsemblBacteria; AAB98007; AAB98007; MJ_0026. DR KEGG; mja:MJ_0026; -. DR eggNOG; arCOG00973; Archaea. DR eggNOG; COG0144; LUCA. DR InParanoid; Q60343; -. DR OMA; PPNEPFF; -. DR PhylomeDB; Q60343; -. DR EvolutionaryTrace; Q60343; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016428; F:tRNA (cytosine-5-)-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0006364; P:rRNA processing; IEA:InterPro. DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR018314; Fmu/NOL1/Nop2p_CS. DR InterPro; IPR001678; MeTrfase_RsmB/NOP2. DR InterPro; IPR011023; Nop2p. DR InterPro; IPR023267; RCMT. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF01189; Methyltr_RsmB-F; 1. DR PRINTS; PR02008; RCMTFAMILY. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00446; nop2p; 1. DR PROSITE; PS01153; NOL1_NOP2_SUN; 1. DR PROSITE; PS51686; SAM_MT_RSMB_NOP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; RNA-binding; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 274 tRNA (cytosine(48)-C(5))- FT methyltransferase. FT /FTId=PRO_0000211821. FT REGION 91 97 S-adenosyl-L-methionine binding. FT ACT_SITE 212 212 Nucleophile. {ECO:0000305}. FT BINDING 115 115 S-adenosyl-L-methionine. FT BINDING 120 120 S-adenosyl-L-methionine. FT BINDING 142 142 S-adenosyl-L-methionine. FT BINDING 163 163 S-adenosyl-L-methionine. FT BINDING 169 169 S-adenosyl-L-methionine. FT BINDING 189 189 S-adenosyl-L-methionine. FT STRAND 11 15 {ECO:0000244|PDB:3AJD}. FT TURN 17 19 {ECO:0000244|PDB:3AJD}. FT HELIX 22 30 {ECO:0000244|PDB:3AJD}. FT TURN 31 33 {ECO:0000244|PDB:3AJD}. FT STRAND 35 38 {ECO:0000244|PDB:3AJD}. FT STRAND 44 49 {ECO:0000244|PDB:3AJD}. FT HELIX 58 61 {ECO:0000244|PDB:3AJD}. FT STRAND 64 67 {ECO:0000244|PDB:3AJD}. FT HELIX 71 73 {ECO:0000244|PDB:3AJD}. FT HELIX 74 79 {ECO:0000244|PDB:3AJD}. FT STRAND 86 89 {ECO:0000244|PDB:3AJD}. FT HELIX 96 104 {ECO:0000244|PDB:3AJD}. FT TURN 105 107 {ECO:0000244|PDB:3AJD}. FT STRAND 109 116 {ECO:0000244|PDB:3AJD}. FT HELIX 118 130 {ECO:0000244|PDB:3AJD}. FT STRAND 135 141 {ECO:0000244|PDB:3AJD}. FT HELIX 143 152 {ECO:0000244|PDB:3AJD}. FT STRAND 157 164 {ECO:0000244|PDB:3AJD}. FT HELIX 167 169 {ECO:0000244|PDB:3A4T}. FT HELIX 180 183 {ECO:0000244|PDB:3AJD}. FT HELIX 185 187 {ECO:0000244|PDB:3AJD}. FT HELIX 190 200 {ECO:0000244|PDB:3AJD}. FT STRAND 201 212 {ECO:0000244|PDB:3AJD}. FT HELIX 216 218 {ECO:0000244|PDB:3A4T}. FT HELIX 220 229 {ECO:0000244|PDB:3AJD}. FT STRAND 231 236 {ECO:0000244|PDB:3AJD}. FT STRAND 248 250 {ECO:0000244|PDB:3AJD}. FT STRAND 257 259 {ECO:0000244|PDB:3AJD}. FT STRAND 266 273 {ECO:0000244|PDB:3AJD}. SQ SEQUENCE 274 AA; 31490 MW; F7396827523369CF CRC64; MMIVYKGEKM QFIRVNTLKI NPEVLKKRLE NKGVVLEKTF LDYAFEVKKS PFSIGSTPEY LFGYYMPQSI SSMIPPIVLN PREDDFILDM CAAPGGKTTH LAQLMKNKGT IVAVEISKTR TKALKSNINR MGVLNTIIIN ADMRKYKDYL LKNEIFFDKI LLDAPCSGNI IKDKNRNVSE EDIKYCSLRQ KELIDIGIDL LKKDGELVYS TCSMEVEENE EVIKYILQKR NDVELIIIKA NEFKGINIKE GYIKGTLRVF PPNEPFFIAK LRKI // ID TOP6A_METJA Reviewed; 369 AA. AC Q57815; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 124. DE RecName: Full=Type 2 DNA topoisomerase 6 subunit A {ECO:0000255|HAMAP-Rule:MF_00132}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00132, ECO:0000269|PubMed:10545127}; DE AltName: Full=Type II DNA topoisomerase VI subunit A {ECO:0000255|HAMAP-Rule:MF_00132}; GN Name=top6A {ECO:0000255|HAMAP-Rule:MF_00132}; GN OrderedLocusNames=MJ0369; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROTEIN SEQUENCE OF 1-69, X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF RP 69-369 IN COMPLEX WITH MAGNESIUM IONS, FUNCTION, CATALYTIC ACTIVITY, RP COFACTOR, SUBUNIT, AND MUTAGENESIS OF GLU-197. RX PubMed=10545127; DOI=10.1093/emboj/18.21.6177; RA Nichols M.D., DeAngelis K., Keck J.L., Berger J.M.; RT "Structure and function of an archaeal topoisomerase VI subunit with RT homology to the meiotic recombination factor Spo11."; RL EMBO J. 18:6177-6188(1999). CC -!- FUNCTION: Relaxes both positive and negative superturns and CC exhibits a strong decatenase activity. {ECO:0000255|HAMAP- CC Rule:MF_00132, ECO:0000269|PubMed:10545127}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00132, CC ECO:0000269|PubMed:10545127}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00132, CC ECO:0000269|PubMed:10545127}; CC Note=Mg(2+) is directly coordinated by Glu-197 and Asp-249 as well CC as indirectly coordinated through 2 water molecules by Asp-251 CC (PubMed:10545127). {ECO:0000269|PubMed:10545127}; CC -!- SUBUNIT: Homodimer (PubMed:10545127). Heterotetramer of two Top6A CC and two Top6B chains. {ECO:0000255|HAMAP-Rule:MF_00132, CC ECO:0000269|PubMed:10545127}. CC -!- SIMILARITY: Belongs to the TOP6A family. {ECO:0000255|HAMAP- CC Rule:MF_00132}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98358.1; -; Genomic_DNA. DR PIR; A64346; A64346. DR PDB; 1D3Y; X-ray; 2.00 A; A/B=69-369. DR PDBsum; 1D3Y; -. DR ProteinModelPortal; Q57815; -. DR SMR; Q57815; 71-369. DR STRING; 243232.MJ_0369; -. DR EnsemblBacteria; AAB98358; AAB98358; MJ_0369. DR KEGG; mja:MJ_0369; -. DR eggNOG; arCOG04143; Archaea. DR eggNOG; COG1697; LUCA. DR InParanoid; Q57815; -. DR KO; K03166; -. DR OMA; WEEQIEL; -. DR PhylomeDB; Q57815; -. DR EvolutionaryTrace; Q57815; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000737; P:DNA catabolic process, endonucleolytic; IEA:InterPro. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00132; Top6A; 1. DR InterPro; IPR002815; Spo11/TopoVI_A. DR InterPro; IPR013049; Spo11/TopoVI_A_N. DR InterPro; IPR004085; TopoVI_A. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PANTHER; PTHR10848; PTHR10848; 1. DR Pfam; PF04406; TP6A_N; 1. DR PRINTS; PR01550; TOP6AFAMILY. DR PRINTS; PR01552; TPISMRASE6A. DR SUPFAM; SSF56726; SSF56726; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; KW Direct protein sequencing; DNA-binding; Isomerase; Magnesium; KW Metal-binding; Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 369 Type 2 DNA topoisomerase 6 subunit A. FT /FTId=PRO_0000145449. FT ACT_SITE 103 103 Nucleophile. FT {ECO:0000250|UniProtKB:Q9M4A2}. FT METAL 197 197 Magnesium. {ECO:0000269|PubMed:10545127}. FT METAL 249 249 Magnesium. {ECO:0000269|PubMed:10545127}. FT MUTAGEN 197 197 E->A: Reduces affinity for DNA. FT {ECO:0000269|PubMed:10545127}. FT HELIX 73 91 {ECO:0000244|PDB:1D3Y}. FT HELIX 98 104 {ECO:0000244|PDB:1D3Y}. FT HELIX 105 107 {ECO:0000244|PDB:1D3Y}. FT HELIX 109 111 {ECO:0000244|PDB:1D3Y}. FT HELIX 116 130 {ECO:0000244|PDB:1D3Y}. FT HELIX 134 137 {ECO:0000244|PDB:1D3Y}. FT STRAND 147 151 {ECO:0000244|PDB:1D3Y}. FT STRAND 153 158 {ECO:0000244|PDB:1D3Y}. FT STRAND 161 166 {ECO:0000244|PDB:1D3Y}. FT STRAND 173 176 {ECO:0000244|PDB:1D3Y}. FT STRAND 185 187 {ECO:0000244|PDB:1D3Y}. FT STRAND 191 197 {ECO:0000244|PDB:1D3Y}. FT HELIX 199 207 {ECO:0000244|PDB:1D3Y}. FT HELIX 210 213 {ECO:0000244|PDB:1D3Y}. FT STRAND 216 220 {ECO:0000244|PDB:1D3Y}. FT HELIX 227 240 {ECO:0000244|PDB:1D3Y}. FT STRAND 244 247 {ECO:0000244|PDB:1D3Y}. FT HELIX 252 256 {ECO:0000244|PDB:1D3Y}. FT HELIX 258 263 {ECO:0000244|PDB:1D3Y}. FT STRAND 282 286 {ECO:0000244|PDB:1D3Y}. FT HELIX 288 293 {ECO:0000244|PDB:1D3Y}. FT HELIX 303 315 {ECO:0000244|PDB:1D3Y}. FT HELIX 317 320 {ECO:0000244|PDB:1D3Y}. FT HELIX 323 335 {ECO:0000244|PDB:1D3Y}. FT STRAND 337 339 {ECO:0000244|PDB:1D3Y}. FT HELIX 341 347 {ECO:0000244|PDB:1D3Y}. FT HELIX 351 354 {ECO:0000244|PDB:1D3Y}. FT HELIX 356 362 {ECO:0000244|PDB:1D3Y}. FT HELIX 364 366 {ECO:0000244|PDB:1D3Y}. SQ SEQUENCE 369 AA; 41829 MW; 7F75282B3E547834 CRC64; MVKLPAISKK PREIAKQKII ELAKKMYEDL MKGKRPKITM PIRSLSNAMF DKEKGSFTLV GKEKARTLTV NQAKIFAQTT KMLEFAKQLL ETDDFSTLRE AYYVSKNWGE ARFDDQQASN NVIEDLEAAL GVLREHLGFI PEEDGSSVVG PLKIIEETPE GELVVDCTKL GTGAYNIPND VTKLNLETDA DFILAIETSG MFARLNAERF WDKHNCILVS LKGVPARATR RFIKRLHEEH DLPVLVFTDG DPYGYLNIYR TLKVGSGKAI HLADKLSIPA ARLIGVTPQD IIDYDLPTHP LKEQDIKRIK DGLKNDDFVR SFPEWQKALK QMLDMGVRAE QQSLAKYGLK YVVNTYLPEK IKDESTWLP // ID TOP6B_METJA Reviewed; 660 AA. AC Q58434; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 21-FEB-2001, sequence version 2. DT 17-FEB-2016, entry version 103. DE RecName: Full=Type 2 DNA topoisomerase 6 subunit B {ECO:0000255|HAMAP-Rule:MF_00322}; DE EC=5.99.1.3 {ECO:0000255|HAMAP-Rule:MF_00322}; DE AltName: Full=Type II DNA topoisomerase VI subunit B {ECO:0000255|HAMAP-Rule:MF_00322}; DE Short=TopoVI-B {ECO:0000255|HAMAP-Rule:MF_00322}; GN Name=top6B {ECO:0000255|HAMAP-Rule:MF_00322}; GN OrderedLocusNames=MJ1028; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Relaxes both positive and negative superturns and CC exhibits a strong decatenase activity. {ECO:0000255|HAMAP- CC Rule:MF_00322}. CC -!- CATALYTIC ACTIVITY: ATP-dependent breakage, passage and rejoining CC of double-stranded DNA. {ECO:0000255|HAMAP-Rule:MF_00322}. CC -!- SUBUNIT: Homodimer. Heterotetramer of two Top6A and two Top6B CC chains. {ECO:0000255|HAMAP-Rule:MF_00322}. CC -!- SIMILARITY: Belongs to the TOP6B family. {ECO:0000255|HAMAP- CC Rule:MF_00322}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99032.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99032.1; ALT_INIT; Genomic_DNA. DR PIR; C64428; C64428. DR ProteinModelPortal; Q58434; -. DR STRING; 243232.MJ_1028; -. DR EnsemblBacteria; AAB99032; AAB99032; MJ_1028. DR KEGG; mja:MJ_1028; -. DR eggNOG; arCOG01165; Archaea. DR eggNOG; COG1389; LUCA. DR InParanoid; Q58434; -. DR KO; K03167; -. DR OMA; AIVNPHA; -. DR PhylomeDB; Q58434; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003918; F:DNA topoisomerase type II (ATP-hydrolyzing) activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003735; F:structural constituent of ribosome; IBA:GO_Central. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR GO; GO:0006268; P:DNA unwinding involved in DNA replication; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.230.10; -; 1. DR Gene3D; 3.30.565.10; -; 1. DR HAMAP; MF_00322; Top6B; 1. DR InterPro; IPR003594; HATPase_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR InterPro; IPR005734; TopoVI_B. DR InterPro; IPR015320; TopoVI_B_transducer. DR PANTHER; PTHR10871:SF4; PTHR10871:SF4; 1. DR Pfam; PF02518; HATPase_c; 1. DR Pfam; PF09239; Topo-VIb_trans; 1. DR PIRSF; PIRSF006553; TopoVI_B; 1. DR ProDom; PD013790; TopoVI_B_transducer; 1. DR SMART; SM00387; HATPase_c; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR SUPFAM; SSF55874; SSF55874; 1. DR TIGRFAMs; TIGR01052; top6b; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Isomerase; KW Nucleotide-binding; Reference proteome; Topoisomerase. FT CHAIN 1 660 Type 2 DNA topoisomerase 6 subunit B. FT /FTId=PRO_0000145462. FT NP_BIND 101 102 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT NP_BIND 111 118 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 48 48 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 80 80 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. FT BINDING 581 581 ATP. {ECO:0000255|HAMAP-Rule:MF_00322}. SQ SEQUENCE 660 AA; 75674 MW; 8F6E4606EE8833C3 CRC64; MVGFMGDELF KEFKEHSVAE FFRKNKHMLG YSGKIRSLTT IIHELVTNSL DACEEAGILP DIKVEIEKLG ADHYKVAVED NGPGIPLEFI PKVFGKMLAG SKMHRFIQSR GQQGIGAAGV LLFSQITTGK PLKIITSTGD GNIYEVEVKM NVEKNEGEIV SKKVRKGKWR GTRVEGEFKE VSYNRGEFGP FEYLRRISLA TPHAKIVLKD PYGEVVFDRV VNELPKKPEE MKPHPYGLTT DELLYIARKT KSKKVSSMLV SELSRVTTKR IKELINYMLR DLILKKFKDS VFWNMVVSCY LNIDIESYLN KFKDYITDDE IETVRMLIKN LPESLDELKR YALKYITMEY LFNKLSEEEI NKLKNHFKKI PENFMEWAEK NYLSATVVDE LNKKVKNIVK NPEEFIAEIK NKGLISDEEL KKFEDEVKSI LNKNPKELTW DEAEMIVNCL QSMEFMAPPT TGLRPIGAEN IEKSLKELLQ PDFVKAITRN PKTYKGGIPF AVEVAIAYGG NAGRQGDEGR RMEIMRFANH VPLLYDASAC GLTKAVKSIN WKRYGLRGED APITVFVNLI STFIPYTSAG KQAVACSENE NEEIYNEIRH ALMICGRELE KYLSRIRREA EEEKKRKYVM KYARIFAEAL ANILNKPVDE IEEKVVKLLE // ID TRKA_METJA Reviewed; 218 AA. AC Q58505; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 110. DE RecName: Full=Trk system potassium uptake protein TrkA homolog; DE Short=K(+)-uptake protein TrkA homolog; GN Name=trkA; OrderedLocusNames=MJ1105; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.30 ANGSTROMS) OF 1-136 IN COMPLEX WITH NAD, RP DOMAIN, AND SUBUNIT. RX PubMed=12086676; DOI=10.1016/S0092-8674(02)00768-7; RA Roosild T.P., Miller S., Booth I.R., Choe S.; RT "A mechanism of regulating transmembrane potassium flux through a RT ligand-mediated conformational switch."; RL Cell 109:781-791(2002). CC -!- FUNCTION: Part of a potassium transport system. {ECO:0000250}. CC -!- SUBUNIT: Homotetramer. Dimer of dimers. CC {ECO:0000269|PubMed:12086676}. CC -!- DOMAIN: The RCK N-terminal domain binds NAD and possibly other CC effectors. This is expected to cause a conformation change that CC regulates potassium transport. {ECO:0000269|PubMed:12086676}. CC -!- SIMILARITY: Contains 1 RCK C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00544}. CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99108.1; -; Genomic_DNA. DR PIR; H64437; H64437. DR PDB; 1LSS; X-ray; 2.30 A; A/B/C/D=1-136. DR PDBsum; 1LSS; -. DR ProteinModelPortal; Q58505; -. DR SMR; Q58505; 1-132. DR STRING; 243232.MJ_1105; -. DR EnsemblBacteria; AAB99108; AAB99108; MJ_1105. DR KEGG; mja:MJ_1105; -. DR eggNOG; arCOG01957; Archaea. DR eggNOG; COG0569; LUCA. DR InParanoid; Q58505; -. DR KO; K03499; -. DR OMA; FNDSWGV; -. DR PhylomeDB; Q58505; -. DR EvolutionaryTrace; Q58505; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:InterPro. DR GO; GO:0015079; F:potassium ion transmembrane transporter activity; IEA:InterPro. DR Gene3D; 3.30.70.1450; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR006036; K_uptake_TrkA. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR006037; RCK_C. DR InterPro; IPR003148; RCK_N. DR Pfam; PF02080; TrkA_C; 1. DR Pfam; PF02254; TrkA_N; 1. DR PRINTS; PR00335; KUPTAKETRKA. DR SUPFAM; SSF116726; SSF116726; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51202; RCK_C; 1. DR PROSITE; PS51201; RCK_N; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Ion transport; NAD; Potassium; KW Potassium transport; Reference proteome; Transport. FT CHAIN 1 218 Trk system potassium uptake protein TrkA FT homolog. FT /FTId=PRO_0000148725. FT DOMAIN 2 124 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. FT DOMAIN 136 217 RCK C-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00544}. FT NP_BIND 7 11 NAD. {ECO:0000269|PubMed:12086676}. FT NP_BIND 73 74 NAD. {ECO:0000269|PubMed:12086676}. FT BINDING 30 30 NAD. {ECO:0000269|PubMed:12086676}. FT BINDING 51 51 NAD. {ECO:0000269|PubMed:12086676}. FT BINDING 97 97 NAD; shared with dimeric partner. FT {ECO:0000269|PubMed:12086676}. FT STRAND 2 6 {ECO:0000244|PDB:1LSS}. FT HELIX 10 21 {ECO:0000244|PDB:1LSS}. FT STRAND 25 31 {ECO:0000244|PDB:1LSS}. FT HELIX 33 42 {ECO:0000244|PDB:1LSS}. FT STRAND 44 50 {ECO:0000244|PDB:1LSS}. FT HELIX 55 60 {ECO:0000244|PDB:1LSS}. FT TURN 61 65 {ECO:0000244|PDB:1LSS}. FT STRAND 67 71 {ECO:0000244|PDB:1LSS}. FT HELIX 76 88 {ECO:0000244|PDB:1LSS}. FT STRAND 94 97 {ECO:0000244|PDB:1LSS}. FT HELIX 103 109 {ECO:0000244|PDB:1LSS}. FT STRAND 113 116 {ECO:0000244|PDB:1LSS}. FT HELIX 118 130 {ECO:0000244|PDB:1LSS}. SQ SEQUENCE 218 AA; 23996 MW; 28CFD33E8791E0CC CRC64; MYIIIAGIGR VGYTLAKSLS EKGHDIVLID IDKDICKKAS AEIDALVING DCTKIKTLED AGIEDADMYI AVTGKEEVNL MSSLLAKSYG INKTIARISE IEYKDVFERL GVDVVVSPEL IAANYIEKLI ERPGILDLAI VGRGEAEILE FIIPEKAKVV NKKIKELGRP QDYLIIAIYD GDELKIPSGD TELKSGDRVL VLVKKDAADA IRKMFLEE // ID TRPB_METJA Reviewed; 404 AA. AC Q60179; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 104. DE RecName: Full=Tryptophan synthase beta chain; DE EC=4.2.1.20; GN Name=trpB; OrderedLocusNames=MJ1037; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: The beta subunit is responsible for the synthesis of L- CC tryptophan from indole and L-serine. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the TrpB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99040.1; -; Genomic_DNA. DR PIR; D64429; D64429. DR ProteinModelPortal; Q60179; -. DR SMR; Q60179; 18-401. DR STRING; 243232.MJ_1037; -. DR EnsemblBacteria; AAB99040; AAB99040; MJ_1037. DR KEGG; mja:MJ_1037; -. DR eggNOG; arCOG01433; Archaea. DR eggNOG; COG0133; LUCA. DR InParanoid; Q60179; -. DR KO; K01696; -. DR OMA; IPEMLYP; -. DR PhylomeDB; Q60179; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR HAMAP; MF_00133; Trp_synth_beta; 1. DR InterPro; IPR006653; Trp_synth_b_CS. DR InterPro; IPR006654; Trp_synth_beta. DR InterPro; IPR023026; Trp_synth_beta/beta-like. DR InterPro; IPR001926; TrpB-like_PLP-dep. DR PANTHER; PTHR10314:SF3; PTHR10314:SF3; 1. DR Pfam; PF00291; PALP; 1. DR PIRSF; PIRSF001413; Trp_syn_beta; 1. DR SUPFAM; SSF53686; SSF53686; 1. DR TIGRFAMs; TIGR00263; trpB; 1. DR PROSITE; PS00168; TRP_SYNTHASE_BETA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Pyridoxal phosphate; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 404 Tryptophan synthase beta chain. FT /FTId=PRO_0000099038. FT MOD_RES 98 98 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 404 AA; 44364 MW; A75D876F95EA8529 CRC64; MSILKKYKDM YPDENGKFGI YGGKFVPETL MPAIAELEEA FKRFWINNEG NFREEFYALL RDYVGRPTPL YYAERLSEEL GCKVYLKRED LAHLGAHKIN NALGQALLAK KMGKKRVIAE TGAGQHGVAT AAACAKLGLE CIIYMGAKDV ERQKLNVFRM ELMGAKVIPV FGGSQTLKDA VNEALRDWTT NVRTTYYLLG SALGPHPYPM MVREFQRVIG KELKEQILEK EGRLPDVIVA CVGGGSNAIG AFYEFLDDDV ELYAVEAGGK GIETGMHGAS LCAGEVGVLH GAKIYVKEDE FGQIEESYSI SAGLDYPGVG PELSFLKDEG RIKAVCVTDD EALEAFQLLC RLEGILPALE SSHALAYAVK LADKLDKDDI MVINLSGRGD KDVQTVAKAL GREI // ID TRM14_METJA Reviewed; 381 AA. AC Q57880; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=tRNA (guanine(6)-N2)-methyltransferase; DE EC=2.1.1.256; DE AltName: Full=tRNA m2G6-methyltransferase; GN Name=trm14; OrderedLocusNames=MJ0438; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND GENE NAME. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=21693558; DOI=10.1093/nar/gkr475; RA Menezes S., Gaston K.W., Krivos K.L., Apolinario E.E., Reich N.O., RA Sowers K.R., Limbach P.A., Perona J.J.; RT "Formation of m2G6 in Methanocaldococcus jannaschii tRNA catalyzed by RT the novel methyltransferase Trm14."; RL Nucleic Acids Res. 39:7641-7655(2011). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC catalyzes the methylation of the guanosine nucleotide at position CC 6 (m2G6) in tRNA(Cys). {ECO:0000269|PubMed:21693558}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(6) in tRNA = CC S-adenosyl-L-homocysteine + N(2)-methylguanine(6) in tRNA. CC {ECO:0000269|PubMed:21693558}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00529}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98426.1; -; Genomic_DNA. DR PIR; F64354; F64354. DR ProteinModelPortal; Q57880; -. DR STRING; 243232.MJ_0438; -. DR EnsemblBacteria; AAB98426; AAB98426; MJ_0438. DR KEGG; mja:MJ_0438; -. DR eggNOG; arCOG00048; Archaea. DR eggNOG; COG0116; LUCA. DR InParanoid; Q57880; -. DR KO; K16318; -. DR OMA; DKRGYRV; -. DR PhylomeDB; Q57880; -. DR BRENDA; 2.1.1.256; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0016423; F:tRNA (guanine) methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 2. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR000241; RNA_methylase_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF02926; THUMP; 1. DR Pfam; PF01170; UPF0020; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. DR PROSITE; PS51165; THUMP; 1. DR PROSITE; PS01261; UPF0020; 1. PE 1: Evidence at protein level; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 381 tRNA (guanine(6)-N2)-methyltransferase. FT /FTId=PRO_0000140480. FT DOMAIN 43 157 THUMP. {ECO:0000255|PROSITE- FT ProRule:PRU00529}. SQ SEQUENCE 381 AA; 43738 MW; 9BB972D94479444D CRC64; MDYYVTLSPG LEKISKNEIE SFGGKIKEIR ENKGRIFFSG DLKLIPKINY LSRTIERMNI LLHREEIPNI ALDDIYKRVY NIDWTEWIKE NQSFAIRPLR AGEHNFTSID IGRVAGEAVI KSYQRDKNIR LKVNLDEPDV IVRVEVIFDE LIVGIDTTGD IALDKRGYRV FNHPAHLNAT IASSLVYLSD WKDDEMLLDP MCGSGTIPIE GALMKRNIPP GKFRENKYGF KFIDIFGYEL LDKIKKEIVE NKNIYKIIGL DKNQKYLDGA KDNAKNAEVL DTIEFICGDA TKLHEKFNES DVIIANPPYG IRIGSKRSVK KLYDEFLSSA KEIMHGSSRL IVITAEDKMF KDAIAKNNFE VKEEFNVMFG GLMTRVFYLT L // ID TOP1_METJA Reviewed; 761 AA. AC Q59046; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 111. DE RecName: Full=DNA topoisomerase 1 {ECO:0000255|HAMAP-Rule:MF_00952}; DE EC=5.99.1.2 {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=DNA topoisomerase I {ECO:0000255|HAMAP-Rule:MF_00952}; DE AltName: Full=Omega-protein; DE AltName: Full=Relaxing enzyme; DE AltName: Full=Swivelase; DE AltName: Full=Untwisting enzyme; GN Name=topA {ECO:0000255|HAMAP-Rule:MF_00952}; OrderedLocusNames=MJ1652; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Releases the supercoiling and torsional tension of DNA, CC which is introduced during the DNA replication and transcription, CC by transiently cleaving and rejoining one strand of the DNA CC duplex. Introduces a single-strand break via transesterification CC at a target site in duplex DNA. The scissile phosphodiester is CC attacked by the catalytic tyrosine of the enzyme, resulting in the CC formation of a DNA-(5'-phosphotyrosyl)-enzyme intermediate and the CC expulsion of a 3'-OH DNA strand. The free DNA strand then CC undergoes passage around the unbroken strand, thus removing DNA CC supercoils. Finally, in the religation step, the DNA 3'-OH attacks CC the covalent intermediate to expel the active-site tyrosine and CC restore the DNA phosphodiester backbone. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- CATALYTIC ACTIVITY: ATP-independent breakage of single-stranded CC DNA, followed by passage and rejoining. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00952}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00952}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Belongs to the type IA topoisomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00952}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_00952}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99673.1; -; Genomic_DNA. DR PIR; B64506; B64506. DR ProteinModelPortal; Q59046; -. DR STRING; 243232.MJ_1652; -. DR PRIDE; Q59046; -. DR EnsemblBacteria; AAB99673; AAB99673; MJ_1652. DR KEGG; mja:MJ_1652; -. DR eggNOG; arCOG01527; Archaea. DR eggNOG; COG0550; LUCA. DR eggNOG; COG0551; LUCA. DR InParanoid; Q59046; -. DR KO; K03168; -. DR OMA; RIKYNEI; -. DR PhylomeDB; Q59046; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003917; F:DNA topoisomerase type I activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006265; P:DNA topological change; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.290.10; -; 1. DR Gene3D; 1.10.460.10; -; 2. DR Gene3D; 3.40.50.140; -; 1. DR HAMAP; MF_00952; Topoisom_1_prok; 1. DR InterPro; IPR000380; Topo_IA. DR InterPro; IPR003601; Topo_IA_2. DR InterPro; IPR023406; Topo_IA_AS. DR InterPro; IPR013497; Topo_IA_cen. DR InterPro; IPR013824; Topo_IA_cen_sub1. DR InterPro; IPR013826; Topo_IA_cen_sub3. DR InterPro; IPR023405; Topo_IA_core_domain. DR InterPro; IPR003602; Topo_IA_DNA-bd_dom. DR InterPro; IPR013498; Topo_IA_Znf. DR InterPro; IPR005739; TopoI_arch. DR InterPro; IPR028612; Topoisom_1_IA. DR InterPro; IPR006171; Toprim_domain. DR PANTHER; PTHR11390; PTHR11390; 2. DR Pfam; PF01131; Topoisom_bac; 1. DR Pfam; PF01751; Toprim; 1. DR Pfam; PF01396; zf-C4_Topoisom; 3. DR PRINTS; PR00417; PRTPISMRASEI. DR SMART; SM00437; TOP1Ac; 1. DR SMART; SM00436; TOP1Bc; 1. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF56712; SSF56712; 1. DR TIGRFAMs; TIGR01057; topA_arch; 1. DR PROSITE; PS00396; TOPOISOMERASE_I_PROK; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Isomerase; Magnesium; Metal-binding; KW Reference proteome; Repeat; Topoisomerase; Zinc; Zinc-finger. FT CHAIN 1 761 DNA topoisomerase 1. FT /FTId=PRO_0000145178. FT DOMAIN 6 143 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ZN_FING 600 626 C4-type 1. FT ZN_FING 680 706 C4-type 2. FT ZN_FING 721 747 C4-type 3. FT REGION 196 201 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT ACT_SITE 315 315 O-(5'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 12 12 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 111 111 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_00952}. FT METAL 111 111 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT METAL 113 113 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 55 55 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 167 167 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 171 171 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 317 317 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. FT SITE 502 502 Interaction with DNA. {ECO:0000255|HAMAP- FT Rule:MF_00952}. SQ SEQUENCE 761 AA; 87833 MW; 2F9C95753E202D82 CRC64; MAEIMTALII CEKPSVAKKI ANALGKAKKK SIDGVPYYEL ERDGKKIIVA SAVGHLFTLV EKENKEFGFY PVFDIKWVPA SVDKGKEYVN KYIKALKKLS KDADEFYIAT DWDIEGELIG YHALKYCCGR EKAKRMRFSS LTKKEIVRAF ENPDEIDYGL VDAGESRHIL DWYFGINLSR ALMNAIRAVN RWKTMSVGRV QGPALAFLTE RELEIKKFIP KPYWVIEALL KDNLKAIHEK EKFWNEKEAK NVYEKIKDEK SAKVVEIKKT KRKLKPLPPF DLGTLQREAY SYFKISPKET QEIAQKLYEN ALISYPRTSS QKLPKDRKYL EDILNIIKNH PVYGKWAERI LKENLKPVEG KKEDPAHPAI HIVDIPKEEL SEKEKEIYDL IARRTLAAFW DNAEREYLNV KIDIKGEKFK LSGSRTVKEG WHEIYYFPKF DEIELPPLKK NDIIKVEKIT ITRKETQPPK RYTVASIIKE LEKRGLGTKA TRAEIIDKLI KRGYVIDDGS LKVTDLGISV IETLKRFCPE IIDEKMTRDL EEKLEKIQFR KIKKDDVLDE AEKRLRKILE EFKKKEEDIG IYLIKNLDAT NKKAKIVGKC PKCGGDLILI RHKKGRFVGC SNYPECDVKY SLPDKGRIKI PNKVCDACKS PILKIGDREI CINPECPLKQ VEVKEEDRIC PKCGAKLILK KGVYGAFYGC SNYPKCKYTE PINKKEVVGK CPKCGGDLVV REGKFGKFVG CSNYPKCRYT EKLKLNEKEE K // ID TRM1_METJA Reviewed; 374 AA. AC Q58356; DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=tRNA (guanine(26)-N(2))-dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290}; DE EC=2.1.1.216 {ECO:0000255|HAMAP-Rule:MF_00290}; DE AltName: Full=tRNA 2,2-dimethylguanosine-26 methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290}; DE AltName: Full=tRNA(guanine-26,N(2)-N(2)) methyltransferase {ECO:0000255|HAMAP-Rule:MF_00290}; DE AltName: Full=tRNA(m(2,2)G26)dimethyltransferase {ECO:0000255|HAMAP-Rule:MF_00290}; GN Name=trm1 {ECO:0000255|HAMAP-Rule:MF_00290}; OrderedLocusNames=MJ0946; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Dimethylates a single guanine residue at position 26 of CC a number of tRNAs using S-adenosyl-L-methionine as donor of the CC methyl groups. {ECO:0000255|HAMAP-Rule:MF_00290}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + guanine(26) in CC tRNA = 2 S-adenosyl-L-homocysteine + N(2)-dimethylguanine(26) in CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00290}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. Trm1 family. {ECO:0000255|HAMAP- CC Rule:MF_00290}. CC -!- SIMILARITY: Contains 1 Trm1 methyltransferase domain. CC {ECO:0000255|HAMAP-Rule:MF_00290}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98948.1; -; Genomic_DNA. DR PIR; B64418; B64418. DR ProteinModelPortal; Q58356; -. DR STRING; 243232.MJ_0946; -. DR EnsemblBacteria; AAB98948; AAB98948; MJ_0946. DR KEGG; mja:MJ_0946; -. DR eggNOG; arCOG01219; Archaea. DR eggNOG; COG1867; LUCA. DR InParanoid; Q58356; -. DR KO; K00555; -. DR OMA; TEYHAEV; -. DR PhylomeDB; Q58356; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004809; F:tRNA (guanine-N2-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0002940; P:tRNA N2-guanine methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00290; tRNA_dimethyltr_TRM1; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR002905; Trm1. DR InterPro; IPR022923; TRM1_arc_bac. DR PANTHER; PTHR10631; PTHR10631; 1. DR Pfam; PF02005; TRM; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00308; TRM1; 1. DR PROSITE; PS51626; SAM_MT_TRM1; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; RNA-binding; KW S-adenosyl-L-methionine; Transferase; tRNA processing; tRNA-binding. FT CHAIN 1 374 tRNA (guanine(26)-N(2))- FT dimethyltransferase. FT /FTId=PRO_0000147683. FT DOMAIN 1 367 Trm1 methyltransferase. FT {ECO:0000255|HAMAP-Rule:MF_00290}. SQ SEQUENCE 374 AA; 42588 MW; E6394A090120165C CRC64; MILKEGEVVF EVPDKLTVTK KDEVFYNPRM KTCRDISIAV IQAFLNLYHK RDKFYIADAL AGSGIRGLRY AKELEFNGEL KVFLNDINPK AYEKIINNAK LNEIENIDVF NEDANTFLSK HFRFFNVVDI DPFGSPAPYV EQAIRALVTR NGLLCLTATD TAALCGRSKK SCLRKYLAYP LFGRDCHEFA LRVLVGYVMR MATKYELALK PVFCHATDHY VRVYLVTDRG AKRADKVFEM LGYVKDVNGI KIIKKFEEGY EKGFAGPLYI GNLYDKALVE EALKIAEKRE FSERVLKILN AIKGESAINQ VGCYDTHQIG KMLKISVPPM QDIINKLKEM GFNAVVTHYN PKGIKTDATL KNVIEAIYQC TKIR // ID TRM5B_METJA Reviewed; 336 AA. AC Q58293; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=tRNA (guanine(37)-N1)-methyltransferase Trm5b; DE EC=2.1.1.228; DE AltName: Full=M1G-methyltransferase; DE AltName: Full=tRNA [GM37] methyltransferase; GN Name=trm5b; OrderedLocusNames=MJ0883; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT. RX PubMed=15165845; DOI=10.1016/j.jmb.2004.04.025; RA Christian T., Evilia C., Williams S., Hou Y.M.; RT "Distinct origins of tRNA(m1G37) methyltransferase."; RL J. Mol. Biol. 339:707-719(2004). RN [3] RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, AND MUTAGENESIS OF ARG-145; RP TYR-177; GLY-205; GLY-207; ASP-223; ASN-225; PRO-226; ASN-265 AND RP PRO-267. RX PubMed=16768442; DOI=10.1021/bi0602314; RA Christian T., Evilia C., Hou Y.M.; RT "Catalysis by the second class of tRNA(m1G37) methyl transferase RT requires a conserved proline."; RL Biochemistry 45:7463-7473(2006). RN [4] RP FUNCTION. RX PubMed=20980671; DOI=10.1261/rna.2376210; RA Christian T., Lahoud G., Liu C., Hoffmann K., Perona J.J., Hou Y.M.; RT "Mechanism of N-methylation by the tRNA m1G37 methyltransferase RT Trm5."; RL RNA 16:2484-2492(2010). RN [5] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS), AND SUBUNIT. RX PubMed=18384044; DOI=10.1002/prot.22019; RA Goto-Ito S., Ito T., Ishii R., Muto Y., Bessho Y., Yokoyama S.; RT "Crystal structure of archaeal tRNA(m(1)G37)methyltransferase aTrm5."; RL Proteins 72:1274-1289(2008). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE AND TRNA. RX PubMed=19749755; DOI=10.1038/nsmb.1653; RA Goto-Ito S., Ito T., Kuratani M., Bessho Y., Yokoyama S.; RT "Tertiary structure checkpoint at anticodon loop modification in tRNA RT functional maturation."; RL Nat. Struct. Mol. Biol. 16:1109-1115(2009). CC -!- FUNCTION: Specifically methylates the N1 position of guanosine-37 CC in various tRNAs. {ECO:0000269|PubMed:15165845, CC ECO:0000269|PubMed:16768442, ECO:0000269|PubMed:20980671}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + guanine(37) in tRNA CC = S-adenosyl-L-homocysteine + N(1)-methylguanine(37) in tRNA. CC {ECO:0000269|PubMed:15165845}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=1.0 uM for S-adenosyl-L-methionine CC {ECO:0000269|PubMed:16768442}; CC KM=0.7 uM for tRNA {ECO:0000269|PubMed:16768442}; CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15165845, CC ECO:0000269|PubMed:18384044, ECO:0000269|PubMed:19749755}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TRM5/TYW2 family. CC {ECO:0000255|PROSITE-ProRule:PRU01021}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98887.1; -; Genomic_DNA. DR PIR; C64410; C64410. DR PDB; 2YX1; X-ray; 2.20 A; A/B=1-336. DR PDB; 2ZZM; X-ray; 2.65 A; A=1-336. DR PDB; 2ZZN; X-ray; 2.95 A; A/B=1-336. DR PDB; 3AY0; X-ray; 3.05 A; A/B=1-336. DR PDBsum; 2YX1; -. DR PDBsum; 2ZZM; -. DR PDBsum; 2ZZN; -. DR PDBsum; 3AY0; -. DR ProteinModelPortal; Q58293; -. DR SMR; Q58293; 2-336. DR STRING; 243232.MJ_0883; -. DR EnsemblBacteria; AAB98887; AAB98887; MJ_0883. DR KEGG; mja:MJ_0883; -. DR eggNOG; arCOG00033; Archaea. DR eggNOG; COG2520; LUCA. DR InParanoid; Q58293; -. DR KO; K15429; -. DR OMA; VIMNLPK; -. DR PhylomeDB; Q58293; -. DR BRENDA; 2.1.1.228; 3260. DR EvolutionaryTrace; Q58293; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0052906; F:tRNA (guanine(37)-N(1))-methyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009019; F:tRNA (guanine-N1-)-methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR030382; MeTrfase_TRM5/TYW2. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02475; Met_10; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 336 tRNA (guanine(37)-N1)-methyltransferase FT Trm5b. FT /FTId=PRO_0000107090. FT REGION 223 224 S-adenosyl-L-methionine binding. FT REGION 251 252 S-adenosyl-L-methionine binding. FT BINDING 186 186 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01021, FT ECO:0000269|PubMed:19749755}. FT BINDING 265 265 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01021, FT ECO:0000269|PubMed:19749755}. FT MUTAGEN 145 145 R->A: 16-fold decrease in FT methyltransferase activity. Lack of tRNA- FT binding. {ECO:0000269|PubMed:16768442}. FT MUTAGEN 177 177 Y->A: 20-fold decrease in FT methyltransferase activity. Reduced FT affinity for tRNA. FT {ECO:0000269|PubMed:16768442}. FT MUTAGEN 205 205 G->A: 33-fold decrease in FT methyltransferase activity and reduced FT affinity for tRNA; when associated with FT A-207. {ECO:0000269|PubMed:16768442}. FT MUTAGEN 207 207 G->A: 33-fold decrease in FT methyltransferase activity and reduced FT affinity for tRNA; when associated with FT A-205. {ECO:0000269|PubMed:16768442}. FT MUTAGEN 223 223 D->A: 100-fold decrease in FT methyltransferase activity. Lack of tRNA- FT binding. {ECO:0000269|PubMed:16768442}. FT MUTAGEN 225 225 N->A: 20-fold decrease in FT methyltransferase activity. FT {ECO:0000269|PubMed:16768442}. FT MUTAGEN 226 226 P->A: 16-fold decrease in FT methyltransferase activity. FT {ECO:0000269|PubMed:16768442}. FT MUTAGEN 265 265 N->A,Q: 100-fold decrease in FT methyltransferase activity. FT {ECO:0000269|PubMed:16768442}. FT MUTAGEN 265 265 N->H: 3-fold decrease in FT methyltransferase activity. FT {ECO:0000269|PubMed:16768442}. FT MUTAGEN 267 267 P->A: 1000-fold decrease in FT methyltransferase activity. No change in FT affinity for tRNA. FT {ECO:0000269|PubMed:16768442}. FT STRAND 3 8 {ECO:0000244|PDB:2YX1}. FT HELIX 9 11 {ECO:0000244|PDB:2YX1}. FT HELIX 12 21 {ECO:0000244|PDB:2YX1}. FT STRAND 27 29 {ECO:0000244|PDB:2ZZM}. FT STRAND 32 34 {ECO:0000244|PDB:2YX1}. FT STRAND 37 42 {ECO:0000244|PDB:2YX1}. FT HELIX 47 50 {ECO:0000244|PDB:2YX1}. FT TURN 51 53 {ECO:0000244|PDB:2YX1}. FT STRAND 59 62 {ECO:0000244|PDB:2YX1}. FT HELIX 77 83 {ECO:0000244|PDB:2YX1}. FT HELIX 85 88 {ECO:0000244|PDB:2YX1}. FT STRAND 91 93 {ECO:0000244|PDB:2YX1}. FT STRAND 98 100 {ECO:0000244|PDB:2YX1}. FT STRAND 103 106 {ECO:0000244|PDB:2YX1}. FT STRAND 110 112 {ECO:0000244|PDB:3AY0}. FT HELIX 114 127 {ECO:0000244|PDB:2YX1}. FT STRAND 131 136 {ECO:0000244|PDB:2YX1}. FT TURN 142 145 {ECO:0000244|PDB:2ZZM}. FT STRAND 149 154 {ECO:0000244|PDB:2YX1}. FT STRAND 159 164 {ECO:0000244|PDB:2YX1}. FT STRAND 167 172 {ECO:0000244|PDB:2YX1}. FT TURN 173 175 {ECO:0000244|PDB:2YX1}. FT HELIX 180 182 {ECO:0000244|PDB:2YX1}. FT HELIX 183 192 {ECO:0000244|PDB:2YX1}. FT STRAND 198 201 {ECO:0000244|PDB:2YX1}. FT HELIX 208 212 {ECO:0000244|PDB:2YX1}. FT TURN 213 215 {ECO:0000244|PDB:2YX1}. FT STRAND 216 224 {ECO:0000244|PDB:2YX1}. FT HELIX 226 238 {ECO:0000244|PDB:2YX1}. FT TURN 242 244 {ECO:0000244|PDB:2YX1}. FT STRAND 245 250 {ECO:0000244|PDB:2YX1}. FT HELIX 252 254 {ECO:0000244|PDB:2YX1}. FT STRAND 259 264 {ECO:0000244|PDB:2YX1}. FT TURN 267 269 {ECO:0000244|PDB:2YX1}. FT HELIX 270 273 {ECO:0000244|PDB:2YX1}. FT HELIX 274 280 {ECO:0000244|PDB:2YX1}. FT STRAND 281 296 {ECO:0000244|PDB:2YX1}. FT HELIX 297 306 {ECO:0000244|PDB:2YX1}. FT STRAND 307 321 {ECO:0000244|PDB:2YX1}. FT STRAND 324 335 {ECO:0000244|PDB:2YX1}. SQ SEQUENCE 336 AA; 39000 MW; 3E4811F0932EE95F CRC64; MPLCLKINKK HGEQTRRILI ENNLLNKDYK ITSEGNYLYL PIKDVDEDIL KSILNIEFEL VDKELEEKKI IKKPSFREII SKKYRKEIDE GLISLSYDVV GDLVILQISD EVDEKIRKEI GELAYKLIPC KGVFRRKSEV KGEFRVRELE HLAGENRTLT IHKENGYRLW VDIAKVYFSP RLGGERARIM KKVSLNDVVV DMFAGVGPFS IACKNAKKIY AIDINPHAIE LLKKNIKLNK LEHKIIPILS DVREVDVKGN RVIMNLPKFA HKFIDKALDI VEEGGVIHYY TIGKDFDKAI KLFEKKCDCE VLEKRIVKSY APREYILALD FKINKK // ID TPIS_METJA Reviewed; 219 AA. AC Q58923; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 16-MAR-2016, entry version 115. DE RecName: Full=Triosephosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17242514}; DE Short=TIM {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000303|PubMed:17242514}; DE Short=TPI {ECO:0000255|HAMAP-Rule:MF_00147}; DE EC=5.3.1.1 {ECO:0000255|HAMAP-Rule:MF_00147, ECO:0000269|PubMed:17242514}; DE AltName: Full=Triose-phosphate isomerase {ECO:0000255|HAMAP-Rule:MF_00147}; GN Name=tpiA {ECO:0000255|HAMAP-Rule:MF_00147}; OrderedLocusNames=MJ1528; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 3-219, FUNCTION AS A RP TRIOSEPHOSPHATE ISOMERASE, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL RP PROPERTIES, AND SUBUNIT. RX PubMed=17242514; DOI=10.1107/S0907444906046488; RA Gayathri P., Banerjee M., Vijayalakshmi A., Azeez S., Balaram H., RA Balaram P., Murthy M.R.; RT "Structure of triosephosphate isomerase (TIM) from Methanocaldococcus RT jannaschii."; RL Acta Crystallogr. D 63:206-220(2007). CC -!- FUNCTION: Involved in the gluconeogenesis. Catalyzes CC stereospecifically the conversion of dihydroxyacetone phosphate CC (DHAP) to D-glyceraldehyde-3-phosphate (G3P). {ECO:0000255|HAMAP- CC Rule:MF_00147, ECO:0000269|PubMed:17242514}. CC -!- CATALYTIC ACTIVITY: D-glyceraldehyde 3-phosphate = glycerone CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00147, CC ECO:0000269|PubMed:17242514}. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Temperature dependence: CC The enzyme is active over the temperature range 20-60 degrees CC Celsius, showing an increase in specific activity with CC temperature. {ECO:0000269|PubMed:17242514}; CC -!- PATHWAY: Carbohydrate biosynthesis; gluconeogenesis. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- PATHWAY: Carbohydrate degradation; glycolysis; D-glyceraldehyde 3- CC phosphate from glycerone phosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00147}. CC -!- SUBUNIT: Homotetramer; dimer of dimers. {ECO:0000255|HAMAP- CC Rule:MF_00147, ECO:0000269|PubMed:17242514}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00147}. CC -!- SIMILARITY: Belongs to the triosephosphate isomerase family. CC {ECO:0000255|HAMAP-Rule:MF_00147}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99546.1; -; Genomic_DNA. DR PIR; G64490; G64490. DR PDB; 2H6R; X-ray; 2.30 A; A/B/C/D/E/F/G/H=1-219. DR PDBsum; 2H6R; -. DR ProteinModelPortal; Q58923; -. DR SMR; Q58923; 1-217. DR STRING; 243232.MJ_1528; -. DR EnsemblBacteria; AAB99546; AAB99546; MJ_1528. DR KEGG; mja:MJ_1528; -. DR eggNOG; arCOG01087; Archaea. DR eggNOG; COG0149; LUCA. DR InParanoid; Q58923; -. DR KO; K01803; -. DR OMA; ETWAQHV; -. DR PhylomeDB; Q58923; -. DR BioCyc; MetaCyc:MONOMER-14589; -. DR BRENDA; 5.3.1.1; 3260. DR UniPathway; UPA00109; UER00189. DR UniPathway; UPA00138; -. DR EvolutionaryTrace; Q58923; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0004807; F:triose-phosphate isomerase activity; IBA:GO_Central. DR GO; GO:0006094; P:gluconeogenesis; IBA:GO_Central. DR GO; GO:0046166; P:glyceraldehyde-3-phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0019563; P:glycerol catabolic process; IBA:GO_Central. DR GO; GO:0006096; P:glycolytic process; IBA:GO_Central. DR GO; GO:0006098; P:pentose-phosphate shunt; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00147_A; TIM_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000652; Triosephosphate_isomerase. DR InterPro; IPR022891; Triosephosphate_isomerase_arc. DR InterPro; IPR020861; Triosephosphate_isomerase_AS. DR PANTHER; PTHR21139; PTHR21139; 1. DR Pfam; PF00121; TIM; 1. DR SUPFAM; SSF51351; SSF51351; 1. DR TIGRFAMs; TIGR00419; tim; 1. DR PROSITE; PS00171; TIM_1; 1. DR PROSITE; PS51440; TIM_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Gluconeogenesis; KW Glycolysis; Isomerase; Pentose shunt; Reference proteome. FT CHAIN 1 219 Triosephosphate isomerase. FT /FTId=PRO_0000090335. FT REGION 6 8 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT REGION 199 200 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 90 90 Electrophile. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT ACT_SITE 138 138 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00147}. FT BINDING 143 143 Substrate; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT BINDING 178 178 Substrate; via amide nitrogen. FT {ECO:0000255|HAMAP-Rule:MF_00147}. FT STRAND 3 6 {ECO:0000244|PDB:2H6R}. FT HELIX 11 13 {ECO:0000244|PDB:2H6R}. FT HELIX 16 32 {ECO:0000244|PDB:2H6R}. FT STRAND 36 39 {ECO:0000244|PDB:2H6R}. FT TURN 42 44 {ECO:0000244|PDB:2H6R}. FT HELIX 45 51 {ECO:0000244|PDB:2H6R}. FT STRAND 56 59 {ECO:0000244|PDB:2H6R}. FT STRAND 66 68 {ECO:0000244|PDB:2H6R}. FT HELIX 75 80 {ECO:0000244|PDB:2H6R}. FT STRAND 85 90 {ECO:0000244|PDB:2H6R}. FT HELIX 97 110 {ECO:0000244|PDB:2H6R}. FT STRAND 113 121 {ECO:0000244|PDB:2H6R}. FT HELIX 122 127 {ECO:0000244|PDB:2H6R}. FT TURN 128 130 {ECO:0000244|PDB:2H6R}. FT STRAND 133 137 {ECO:0000244|PDB:2H6R}. FT HELIX 158 167 {ECO:0000244|PDB:2H6R}. FT STRAND 172 175 {ECO:0000244|PDB:2H6R}. FT HELIX 182 189 {ECO:0000244|PDB:2H6R}. FT TURN 190 192 {ECO:0000244|PDB:2H6R}. FT STRAND 196 199 {ECO:0000244|PDB:2H6R}. FT HELIX 200 203 {ECO:0000244|PDB:2H6R}. FT HELIX 208 215 {ECO:0000244|PDB:2H6R}. SQ SEQUENCE 219 AA; 23319 MW; C6BC49A2DEE8A026 CRC64; MLIVINYKTY NESIGNRGLE IAKIAEKVSE ESGITIGVAP QFVDLRMIVE NVNIPVYAQH IDNINPGSHT GHILAEAIKD CGCKGTLINH SEKRMLLADI EAVINKCKNL GLETIVCTNN INTSKAVAAL SPDYIAVEPP ELIGTGIPVS KANPEVVEGT VRAVKEINKD VKVLCGAGIS KGEDVKAALD LGAEGVLLAS GVVKAKNVEE AIRELIKFI // ID TRPF_METJA Reviewed; 226 AA. AC Q57893; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 94. DE RecName: Full=N-(5'-phosphoribosyl)anthranilate isomerase; DE Short=PRAI; DE EC=5.3.1.24; GN Name=trpF; OrderedLocusNames=MJ0451; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: N-(5-phospho-beta-D-ribosyl)anthranilate = 1- CC (2-carboxyphenylamino)-1-deoxy-D-ribulose 5-phosphate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 3/5. CC -!- SIMILARITY: Belongs to the TrpF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98440.1; -; Genomic_DNA. DR PIR; C64356; C64356. DR ProteinModelPortal; Q57893; -. DR STRING; 243232.MJ_0451; -. DR EnsemblBacteria; AAB98440; AAB98440; MJ_0451. DR KEGG; mja:MJ_0451; -. DR eggNOG; arCOG01983; Archaea. DR eggNOG; COG0135; LUCA. DR InParanoid; Q57893; -. DR KO; K01817; -. DR OMA; THDWERT; -. DR PhylomeDB; Q57893; -. DR UniPathway; UPA00035; UER00042. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00135; PRAI; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001240; PRAI. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00697; PRAI; 1. DR SUPFAM; SSF51366; SSF51366; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Isomerase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 226 N-(5'-phosphoribosyl)anthranilate FT isomerase. FT /FTId=PRO_0000154403. SQ SEQUENCE 226 AA; 25306 MW; 7B83DC1F16C5957E CRC64; MGDDLVKVKI CGITNEEDIA YISKKVHAVG VIVDVPVKTP RKISLDKAIE LKKYVAPFTS LVTVLMPNSI EEVLEIYNAL KPNAIQLHGF ESLDFVKELN KLKNTGELNA HIIKVIHIPK DEEIDFKTLL NTAKEYEKYV EAILVDTKIE SIKLEGKTHN WAVSKKLRES LEKPLILAGG LNKDNVLEAI KTVKPYAIDV SSSLEAYGGK KDLKKVDEFL EVIKKV // ID TRMY_METJA Reviewed; 205 AA. AC Q59034; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=tRNA (pseudouridine(54)-N(1))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00587}; DE EC=2.1.1.257 {ECO:0000255|HAMAP-Rule:MF_00587}; GN Name=trmY {ECO:0000255|HAMAP-Rule:MF_00587}; OrderedLocusNames=MJ1640; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=22274954; DOI=10.1261/rna.028498.111; RA Wurm J.P., Griese M., Bahr U., Held M., Heckel A., Karas M., Soppa J., RA Woehnert J.; RT "Identification of the enzyme responsible for N1-methylation of RT pseudouridine 54 in archaeal tRNAs."; RL RNA 18:412-420(2012). RN [3] RP FUNCTION, CATALYTIC ACTIVITY, AND GENE NAME. RX PubMed=22274953; DOI=10.1261/rna.030841.111; RA Chatterjee K., Blaby I.K., Thiaville P.C., Majumder M., Grosjean H., RA Yuan Y.A., Gupta R., de Crecy-Lagard V.; RT "The archaeal COG1901/DUF358 SPOUT-methyltransferase members, together RT with pseudouridine synthase Pus10, catalyze the formation of 1- RT methylpseudouridine at position 54 of tRNA."; RL RNA 18:421-433(2012). RN [4] RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, AND SUBUNIT. RX PubMed=21098051; DOI=10.1093/jmcb/mjq034; RA Chen H.Y., Yuan Y.A.; RT "Crystal structure of Mj1640/DUF358 protein reveals a putative SPOUT- RT class RNA methyltransferase."; RL J. Mol. Cell Biol. 2:366-374(2010). CC -!- FUNCTION: Specifically catalyzes the N1-methylation of CC pseudouridine at position 54 (Psi54) in tRNAs. {ECO:0000255|HAMAP- CC Rule:MF_00587, ECO:0000269|PubMed:22274953, CC ECO:0000269|PubMed:22274954}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + pseudouridine(54) in CC tRNA = S-adenosyl-L-homocysteine + N(1)-methylpseudouridine(54) in CC tRNA. {ECO:0000255|HAMAP-Rule:MF_00587, CC ECO:0000269|PubMed:22274953, ECO:0000269|PubMed:22274954}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00587, CC ECO:0000269|PubMed:21098051}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00587}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. TrmY CC family. {ECO:0000255|HAMAP-Rule:MF_00587}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99660.1; -; Genomic_DNA. DR PIR; F64504; F64504. DR PDB; 3AI9; X-ray; 1.55 A; X=1-205. DR PDB; 3AIA; X-ray; 1.40 A; A/B=1-205. DR PDBsum; 3AI9; -. DR PDBsum; 3AIA; -. DR ProteinModelPortal; Q59034; -. DR STRING; 243232.MJ_1640; -. DR EnsemblBacteria; AAB99660; AAB99660; MJ_1640. DR KEGG; mja:MJ_1640; -. DR eggNOG; arCOG01239; Archaea. DR eggNOG; COG1901; LUCA. DR InParanoid; Q59034; -. DR KO; K16317; -. DR OMA; LGDHIGL; -. DR PhylomeDB; Q59034; -. DR BRENDA; 2.1.1.257; 3260. DR EvolutionaryTrace; Q59034; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IDA:UniProtKB. DR GO; GO:0008175; F:tRNA methyltransferase activity; IDA:UniProtKB. DR GO; GO:0030488; P:tRNA methylation; IDA:UniProtKB. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00587; tRNA_methyltr_TrmY; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR007158; TrmY. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF04013; Methyltrn_RNA_2; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase; KW tRNA processing. FT CHAIN 1 205 tRNA (pseudouridine(54)-N(1))- FT methyltransferase. FT /FTId=PRO_0000157948. FT REGION 179 184 S-adenosyl-L-methionine binding. FT BINDING 136 136 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP-Rule:MF_00587, FT ECO:0000269|PubMed:21098051}. FT BINDING 156 156 S-adenosyl-L-methionine; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00587, FT ECO:0000269|PubMed:21098051}. FT BINDING 189 189 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_00587, FT ECO:0000269|PubMed:21098051}. FT STRAND 2 10 {ECO:0000244|PDB:3AIA}. FT HELIX 19 21 {ECO:0000244|PDB:3AIA}. FT TURN 22 27 {ECO:0000244|PDB:3AIA}. FT HELIX 29 40 {ECO:0000244|PDB:3AIA}. FT STRAND 43 46 {ECO:0000244|PDB:3AIA}. FT STRAND 50 56 {ECO:0000244|PDB:3AIA}. FT STRAND 59 61 {ECO:0000244|PDB:3AIA}. FT STRAND 64 69 {ECO:0000244|PDB:3AIA}. FT TURN 70 72 {ECO:0000244|PDB:3AIA}. FT HELIX 80 96 {ECO:0000244|PDB:3AIA}. FT HELIX 101 103 {ECO:0000244|PDB:3AIA}. FT STRAND 106 109 {ECO:0000244|PDB:3AIA}. FT STRAND 112 115 {ECO:0000244|PDB:3AIA}. FT HELIX 119 128 {ECO:0000244|PDB:3AIA}. FT STRAND 132 136 {ECO:0000244|PDB:3AIA}. FT STRAND 140 142 {ECO:0000244|PDB:3AIA}. FT HELIX 143 145 {ECO:0000244|PDB:3AIA}. FT STRAND 150 156 {ECO:0000244|PDB:3AIA}. FT HELIX 163 171 {ECO:0000244|PDB:3AIA}. FT STRAND 175 178 {ECO:0000244|PDB:3AIA}. FT HELIX 186 199 {ECO:0000244|PDB:3AIA}. SQ SEQUENCE 205 AA; 23704 MW; EBED16985B07E132 CRC64; MREFIFKANK TITSSDINLK DLPGSCGRLD LLCRCVSDAF FLSHDIRRDV VFYAVLYGQP NPPVCIKFVG SELKKVSPDE RNIAIFIKKA LKKFEELDEE QRKDWNQSTP GIYVRRLGFR NLVLEKLEEG KNIYYLHMNG EDVENVDIEN PVFIIGDHIG IGEEDERFLD EIKAKRISLS PLELHANHCI TIIHNVLDKK RICEI // ID TRPC_METJA Reviewed; 266 AA. AC Q58328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Indole-3-glycerol phosphate synthase; DE Short=IGPS; DE EC=4.1.1.48; GN Name=trpC; OrderedLocusNames=MJ0918; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: 1-(2-carboxyphenylamino)-1-deoxy-D-ribulose 5- CC phosphate = 1-C-(3-indolyl)-glycerol 3-phosphate + CO(2) + H(2)O. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 4/5. CC -!- SIMILARITY: Belongs to the TrpC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98923.1; -; Genomic_DNA. DR PIR; F64414; F64414. DR ProteinModelPortal; Q58328; -. DR STRING; 243232.MJ_0918; -. DR EnsemblBacteria; AAB98923; AAB98923; MJ_0918. DR KEGG; mja:MJ_0918; -. DR eggNOG; arCOG01088; Archaea. DR eggNOG; COG0134; LUCA. DR InParanoid; Q58328; -. DR KO; K01609; -. DR OMA; EPKYFNG; -. DR PhylomeDB; Q58328; -. DR UniPathway; UPA00035; UER00043. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004425; F:indole-3-glycerol-phosphate synthase activity; IBA:GO_Central. DR GO; GO:0004640; F:phosphoribosylanthranilate isomerase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00134_A; IGPS_A; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013798; Indole-3-glycerol_P_synth. DR InterPro; IPR001468; Indole-3-GlycerolPSynthase_CS. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00218; IGPS; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR PROSITE; PS00614; IGPS; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Decarboxylase; Lyase; Reference proteome; KW Tryptophan biosynthesis. FT CHAIN 1 266 Indole-3-glycerol phosphate synthase. FT /FTId=PRO_0000154292. SQ SEQUENCE 266 AA; 30027 MW; 0BFD8F7C3C6A5002 CRC64; MKVLDEIVAN RKKMVEIEKR KDIIKNLRSF IDELDIDVEK KRKLRLSKAI KKAKEIKNPI ITEIKPSSPS KGSIREINLE DVKNIANEMV EGGATALSIL TEPKYFNGSY KNLIVAREFD IPILMKDFIV DFYQIDVASE IGANAVLLIV SSLKEDIGEF LDYAKENDLE CLVETHSEDE IDIALDAGAK IIGINNRDLK TLKIDLSTTE KLAPLIPKNK IKVGESGIYT KEQLNYVLKF TDAALIGSSI MESENIREKV REFVIK // ID TRUD2_METJA Reviewed; 422 AA. AC Q58759; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 2. DT 17-FEB-2016, entry version 82. DE RecName: Full=Probable tRNA pseudouridine synthase D 2 {ECO:0000255|HAMAP-Rule:MF_01082}; DE EC=5.4.99.27 {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA pseudouridine(13) synthase {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA pseudouridylate synthase D 2 {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA-uridine isomerase D 2 {ECO:0000255|HAMAP-Rule:MF_01082}; GN Name=truD2 {ECO:0000255|HAMAP-Rule:MF_01082}; GN OrderedLocusNames=MJ1364; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Could be responsible for synthesis of pseudouridine from CC uracil-13 in transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(13) = tRNA pseudouridine(13). CC {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family. CC {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- SIMILARITY: Contains 1 TRUD domain. {ECO:0000255|HAMAP- CC Rule:MF_01082}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99372.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99372.1; ALT_INIT; Genomic_DNA. DR PIR; C64470; C64470. DR ProteinModelPortal; Q58759; -. DR STRING; 243232.MJ_1364; -. DR EnsemblBacteria; AAB99372; AAB99372; MJ_1364. DR KEGG; mja:MJ_1364; -. DR eggNOG; arCOG04252; Archaea. DR eggNOG; COG0585; LUCA. DR InParanoid; Q58759; -. DR KO; K06176; -. DR OMA; YFDDQRF; -. DR PhylomeDB; Q58759; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01082; TruD; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001656; PsdUridine_synth_TruD. DR InterPro; IPR020119; PsdUridine_synth_TruD_CS. DR InterPro; IPR011760; PsdUridine_synth_TruD_insert. DR PANTHER; PTHR13326; PTHR13326; 1. DR Pfam; PF01142; TruD; 1. DR SUPFAM; SSF55120; SSF55120; 2. DR PROSITE; PS50984; TRUD; 1. DR PROSITE; PS01268; UPF0024; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 422 Probable tRNA pseudouridine synthase D 2. FT /FTId=PRO_0000152541. FT DOMAIN 160 371 TRUD. {ECO:0000255|HAMAP-Rule:MF_01082}. FT ACT_SITE 89 89 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01082}. SQ SEQUENCE 422 AA; 50180 MW; BDADF2BBA901F6E4 CRC64; MKNISTKESF FKFKFNNRSL YCWGAFMKLR MKPEDFIVEE IIDFNKIAGD RCYLYKLTKR NIESLKAFSY IAKKFKIPLK DIGYCGLKDR HALTTQYISI PKKYGKLSLD EPNLKLELIG ESKFLLLGDL EGNRFTITVR GLKKEDIPKI KENLKYLEFG APNYFDSQRF GSVFDKKFIA KEVIKGNYEE AVKILLTKYK KSEKKLIKDL KRFIDKNWGD WDKIWEYIKE NNIKSRLYVN MVKELKKSND YKKALSYVDD RLKKIFVAAY QSYLWNECVK ELLRKYVPEE DRVYYEYECG TLMFYKKMDE EVFNILKDKK FPTIAPDIEY SGEEKEIIEE ILKREGLTME ELNNIGELGK FIYSERKILS IPKNLKIGEF EEDELNKGKY KITLSYELEK GSYATIIIKR AFLGVKTKKR KR // ID TRM56_METJA Reviewed; 179 AA. AC Q58780; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=tRNA (cytidine(56)-2'-O)-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00077}; DE EC=2.1.1.206 {ECO:0000255|HAMAP-Rule:MF_00077}; DE AltName: Full=tRNA ribose 2'-O-methyltransferase aTrm56 {ECO:0000255|HAMAP-Rule:MF_00077}; GN OrderedLocusNames=MJ1385; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Specifically catalyzes the AdoMet-dependent 2'-O-ribose CC methylation of cytidine at position 56 in tRNAs. CC {ECO:0000255|HAMAP-Rule:MF_00077}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + cytidine(56) in tRNA CC = S-adenosyl-L-homocysteine + 2'-O-methylcytidine(56) in tRNA. CC {ECO:0000255|HAMAP-Rule:MF_00077}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00077}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00077}. CC -!- SIMILARITY: Belongs to the aTrm56 family. {ECO:0000255|HAMAP- CC Rule:MF_00077}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99395.1; -; Genomic_DNA. DR PIR; H64472; H64472. DR ProteinModelPortal; Q58780; -. DR SMR; Q58780; 2-175. DR STRING; 243232.MJ_1385; -. DR EnsemblBacteria; AAB99395; AAB99395; MJ_1385. DR KEGG; mja:MJ_1385; -. DR eggNOG; arCOG01857; Archaea. DR eggNOG; COG1303; LUCA. DR InParanoid; Q58780; -. DR KO; K07254; -. DR OMA; LGHRPER; -. DR PhylomeDB; Q58780; -. DR BioCyc; MetaCyc:MONOMER-2005; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1280.10; -; 1. DR HAMAP; MF_00077; tRNA_methyltr_aTrm56; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR InterPro; IPR002845; tRNA_mtfrase_aTrm56. DR Pfam; PF01994; Trm56; 1. DR PIRSF; PIRSF016123; UCP016123; 1. DR ProDom; PD016584; DUF127; 1. DR SUPFAM; SSF75217; SSF75217; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 179 tRNA (cytidine(56)-2'-O)- FT methyltransferase. FT /FTId=PRO_0000146929. FT REGION 110 114 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00077}. FT REGION 128 135 S-adenosyl-L-methionine binding. FT {ECO:0000255|HAMAP-Rule:MF_00077}. FT BINDING 82 82 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000255|HAMAP- FT Rule:MF_00077}. SQ SEQUENCE 179 AA; 20573 MW; 05A10B97B3303B31 CRC64; MVVEVLRLGH RGDRDKRIST HVALTARALG ADKIIFTTED EHVENSVKKV VESWGGNFEF VVEKHWRKYI REFKKRGIVV HLTMYGANIN EIMPEIREIS RDKDILVIVG AEKVPKEVYE LADYNVSVGN QPHSEVAALA IFLDRLFEGK TLYRDFEDAK IKIVPSKDGK VVIREKQNK // ID TRMI_METJA Reviewed; 282 AA. AC Q57598; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 88. DE RecName: Full=tRNA (adenine(57)-N(1)/adenine(58)-N(1))-methyltransferase TrmI; DE EC=2.1.1.219; DE AltName: Full=tRNA(m1A57/58)-methyltransferase; GN Name=trmI; OrderedLocusNames=MJ0134; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the S-adenosyl-L-methionine-dependent CC formation of N(1)-methyladenosine at position(s) 57 (m1A57) and 58 CC (m1A58) in the T-loop of some tRNAs. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: 2 S-adenosyl-L-methionine + CC adenine(57)/adenine(58) in tRNA = 2 S-adenosyl-L-homocysteine + CC N(1)-methyladenine(57)/N(1)-methyladenine(58) in tRNA. CC {ECO:0000255|PROSITE-ProRule:PRU00952}. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TRM61 family. {ECO:0000255|PROSITE- CC ProRule:PRU00952}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98115.1; -; Genomic_DNA. DR PIR; F64316; F64316. DR ProteinModelPortal; Q57598; -. DR STRING; 243232.MJ_0134; -. DR EnsemblBacteria; AAB98115; AAB98115; MJ_0134. DR KEGG; mja:MJ_0134; -. DR eggNOG; arCOG00978; Archaea. DR eggNOG; COG2519; LUCA. DR InParanoid; Q57598; -. DR KO; K07442; -. DR OMA; GAPMMPR; -. DR PhylomeDB; Q57598; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0031515; C:tRNA (m1A) methyltransferase complex; IBA:GO_Central. DR GO; GO:0016429; F:tRNA (adenine-N1-)-methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR014816; tRNA_MeTrfase_Gcd14. DR Pfam; PF08704; GCD14; 1. DR PIRSF; PIRSF017269; GCD14; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS51620; SAM_TRM61; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 282 tRNA (adenine(57)-N(1)/adenine(58)-N(1))- FT methyltransferase TrmI. FT /FTId=PRO_0000106712. FT REGION 98 101 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 119 119 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00952}. FT BINDING 172 172 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00952}. FT BINDING 188 188 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU00952}. SQ SEQUENCE 282 AA; 32207 MW; 558FB972B21CFA9C CRC64; MFAYKLLVDE RGKRYLLKKN VEKFGTDLGI VDMKDIEEGV ELKSHKGHTF YLVEPTMFDI LKRMKRTVTT LLPKDIGFII ARAGIREGET VVEAGTGSGA LTMYLSNAVG KTGKVITYDI RPEFAKVARK NLLRVGAIKK GQKIIGLDEE FDDEDEIEIE DGLFNVIQKI GDVREKIDEK DVDVIVLDLP DPWNVVENAK KALNKKRGRI VTYLPYIEQV KKTVEKLKEE GFWDIHTYEI IEREIEISEK GVRPSTRMIG HTGYITVARV PPEPLDREEE KE // ID TRPA_METJA Reviewed; 281 AA. AC Q60180; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 100. DE RecName: Full=Tryptophan synthase alpha chain {ECO:0000255|HAMAP-Rule:MF_00131}; DE EC=4.2.1.20 {ECO:0000255|HAMAP-Rule:MF_00131}; GN Name=trpA {ECO:0000255|HAMAP-Rule:MF_00131}; OrderedLocusNames=MJ1038; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: The alpha subunit is responsible for the aldol cleavage CC of indoleglycerol phosphate to indole and glyceraldehyde 3- CC phosphate. {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- CATALYTIC ACTIVITY: L-serine + 1-C-(indol-3-yl)glycerol 3- CC phosphate = L-tryptophan + D-glyceraldehyde 3-phosphate + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 5/5. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. CC {ECO:0000255|HAMAP-Rule:MF_00131}. CC -!- SIMILARITY: Belongs to the TrpA family. {ECO:0000255|HAMAP- CC Rule:MF_00131}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99041.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99041.1; ALT_INIT; Genomic_DNA. DR PIR; E64429; E64429. DR ProteinModelPortal; Q60180; -. DR STRING; 243232.MJ_1038; -. DR PRIDE; Q60180; -. DR EnsemblBacteria; AAB99041; AAB99041; MJ_1038. DR KEGG; mja:MJ_1038; -. DR eggNOG; arCOG01086; Archaea. DR eggNOG; COG0159; LUCA. DR InParanoid; Q60180; -. DR KO; K01695; -. DR OMA; DYNPHIP; -. DR PhylomeDB; Q60180; -. DR UniPathway; UPA00035; UER00044. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030170; F:pyridoxal phosphate binding; IBA:GO_Central. DR GO; GO:0004834; F:tryptophan synthase activity; IBA:GO_Central. DR GO; GO:0000162; P:tryptophan biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_00131; Trp_synth_alpha; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR InterPro; IPR018204; Trp_synthase_alpha_AS. DR InterPro; IPR002028; Trp_synthase_suA. DR Pfam; PF00290; Trp_syntA; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00262; trpA; 1. DR PROSITE; PS00167; TRP_SYNTHASE_ALPHA; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 281 Tryptophan synthase alpha chain. FT /FTId=PRO_0000098889. FT ACT_SITE 49 49 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. FT ACT_SITE 60 60 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_00131}. SQ SEQUENCE 281 AA; 31271 MW; D68E352004FB1E9F CRC64; MIMKLAEKFE ELKNKGEKAF VAFYVGGDPN LEISEKALEV ICKHADIVEI GIPFSDPVAD GITIQKADVR ALNSGMNPLK AFELAKKLNE KAPNVPKVFL TYYNIIFKMG EEEFVKKCKE AGVSGIIVPD LPIEEADSLY NYCKKYGVDL IFLVAPTTPD ERLKKILEKC SGFVYVVSVT GITGAREKVA EETKELIKRV KKFSKIPACV GFGISKREHV EEITEIADGA IVGSAIVKIV EKHLDENGQI KDEEKFLKEL EEFVKNLKEG TKKKAKVAIK N // ID TRUB_METJA Reviewed; 336 AA. AC Q57612; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 107. DE RecName: Full=Probable tRNA pseudouridine synthase B {ECO:0000255|HAMAP-Rule:MF_01081}; DE EC=5.4.99.25 {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA pseudouridine(55) synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE Short=Psi55 synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA pseudouridylate synthase {ECO:0000255|HAMAP-Rule:MF_01081}; DE AltName: Full=tRNA-uridine isomerase {ECO:0000255|HAMAP-Rule:MF_01081}; GN Name=truB {ECO:0000255|HAMAP-Rule:MF_01081}; OrderedLocusNames=MJ0148; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Could be responsible for synthesis of pseudouridine from CC uracil-55 in the psi GC loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_01081}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(55) = tRNA pseudouridine(55). CC {ECO:0000255|HAMAP-Rule:MF_01081}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruB family. CC Type 2 subfamily. {ECO:0000255|HAMAP-Rule:MF_01081}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|HAMAP- CC Rule:MF_01081}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98132.1; -; Genomic_DNA. DR PIR; E64318; E64318. DR PDB; 2APO; X-ray; 1.95 A; A=1-336. DR PDBsum; 2APO; -. DR ProteinModelPortal; Q57612; -. DR SMR; Q57612; 17-331. DR DIP; DIP-60499N; -. DR STRING; 243232.MJ_0148; -. DR EnsemblBacteria; AAB98132; AAB98132; MJ_0148. DR KEGG; mja:MJ_0148; -. DR eggNOG; arCOG00987; Archaea. DR eggNOG; COG0130; LUCA. DR InParanoid; Q57612; -. DR KO; K11131; -. DR OMA; HIPPKEY; -. DR PhylomeDB; Q57612; -. DR EvolutionaryTrace; Q57612; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0000495; P:box H/ACA snoRNA 3'-end processing; IBA:GO_Central. DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031118; P:rRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031120; P:snRNA pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 2.30.130.10; -; 1. DR HAMAP; MF_01081; TruB_arch; 1. DR InterPro; IPR012960; Dyskerin-like. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR002501; PsdUridine_synth_N. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR004802; tRNA_PsdUridine_synth_B_fam. DR InterPro; IPR026326; TruB_arch. DR InterPro; IPR032819; TruB_C. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR PANTHER; PTHR23127; PTHR23127; 1. DR Pfam; PF08068; DKCLD; 1. DR Pfam; PF01472; PUA; 1. DR Pfam; PF16198; TruB_C_2; 1. DR Pfam; PF01509; TruB_N; 1. DR SMART; SM01136; DKCLD; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00425; CBF5; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Isomerase; Reference proteome; KW tRNA processing. FT CHAIN 1 336 Probable tRNA pseudouridine synthase B. FT /FTId=PRO_0000121959. FT DOMAIN 248 323 PUA. {ECO:0000255|HAMAP-Rule:MF_01081}. FT ACT_SITE 81 81 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01081}. FT STRAND 18 22 {ECO:0000244|PDB:2APO}. FT HELIX 34 36 {ECO:0000244|PDB:2APO}. FT HELIX 39 44 {ECO:0000244|PDB:2APO}. FT STRAND 46 52 {ECO:0000244|PDB:2APO}. FT STRAND 54 56 {ECO:0000244|PDB:2APO}. FT HELIX 58 68 {ECO:0000244|PDB:2APO}. FT STRAND 74 78 {ECO:0000244|PDB:2APO}. FT STRAND 85 92 {ECO:0000244|PDB:2APO}. FT HELIX 93 101 {ECO:0000244|PDB:2APO}. FT STRAND 107 117 {ECO:0000244|PDB:2APO}. FT HELIX 121 131 {ECO:0000244|PDB:2APO}. FT STRAND 132 136 {ECO:0000244|PDB:2APO}. FT STRAND 151 163 {ECO:0000244|PDB:2APO}. FT STRAND 166 173 {ECO:0000244|PDB:2APO}. FT HELIX 179 189 {ECO:0000244|PDB:2APO}. FT STRAND 194 204 {ECO:0000244|PDB:2APO}. FT HELIX 209 211 {ECO:0000244|PDB:2APO}. FT HELIX 215 226 {ECO:0000244|PDB:2APO}. FT HELIX 232 237 {ECO:0000244|PDB:2APO}. FT STRAND 238 240 {ECO:0000244|PDB:2APO}. FT HELIX 241 245 {ECO:0000244|PDB:2APO}. FT STRAND 248 253 {ECO:0000244|PDB:2APO}. FT HELIX 255 257 {ECO:0000244|PDB:2APO}. FT HELIX 258 262 {ECO:0000244|PDB:2APO}. FT HELIX 269 271 {ECO:0000244|PDB:2APO}. FT STRAND 272 276 {ECO:0000244|PDB:2APO}. FT STRAND 284 288 {ECO:0000244|PDB:2APO}. FT STRAND 294 302 {ECO:0000244|PDB:2APO}. FT HELIX 304 309 {ECO:0000244|PDB:2APO}. FT STRAND 311 321 {ECO:0000244|PDB:2APO}. SQ SEQUENCE 336 AA; 38483 MW; F29E3EC979A5A89A CRC64; MILLEKTQEK KINDKEELIV KEEVETNWDY GCNPYERKIE DLIKYGVVVV DKPRGPTSHE VSTWVKKILN LDKAGHGGTL DPKVTGVLPV ALERATKTIP MWHIPPKEYV CLMHLHRDAS EEDILRVFKE FTGRIYQRPP LKAAVKRRLR IRKIHELELL DKDGKDVLFR VKCQSGTYIR KLCEDIGEAL GTSAHMQELR RTKSGCFEEK DAVYLQDLLD AYVFWKEDGD EEELRRVIKP MEYGLRHLKK VVVKDSAVDA ICHGADVYVR GIAKLSKGIG KGETVLVETL KGEAVAVGKA LMNTKEILNA DKGVAVDVER VYMDRGTYPR MWKRKK // ID TRXB_METJA Reviewed; 301 AA. AC Q58931; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 96. DE RecName: Full=Putative thioredoxin reductase; DE Short=TRXR; DE EC=1.8.1.9; GN OrderedLocusNames=MJ1536; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: Thioredoxin + NADP(+) = thioredoxin disulfide CC + NADPH. CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; CC Evidence={ECO:0000250|UniProtKB:P0A9P4}; CC Note=Binds 1 FAD per subunit. {ECO:0000250|UniProtKB:P0A9P4}; CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:P0A9P4}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- MISCELLANEOUS: The active site is a redox-active disulfide bond. CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridine nucleotide-disulfide CC oxidoreductase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99556.1; -; Genomic_DNA. DR PIR; G64491; G64491. DR ProteinModelPortal; Q58931; -. DR STRING; 243232.MJ_1536; -. DR EnsemblBacteria; AAB99556; AAB99556; MJ_1536. DR KEGG; mja:MJ_1536; -. DR eggNOG; arCOG01296; Archaea. DR eggNOG; COG0492; LUCA. DR InParanoid; Q58931; -. DR KO; K00384; -. DR OMA; TDSGQVW; -. DR PhylomeDB; Q58931; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004791; F:thioredoxin-disulfide reductase activity; IEA:UniProtKB-EC. DR GO; GO:0019430; P:removal of superoxide radicals; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR008255; Pyr_nucl-diS_OxRdtase_2_AS. DR InterPro; IPR000103; Pyridine_nuc-diS_OxRdtase_2. DR InterPro; IPR005982; Thioredox_Rdtase. DR Pfam; PF07992; Pyr_redox_2; 1. DR PRINTS; PR00469; PNDRDTASEII. DR SUPFAM; SSF51905; SSF51905; 1. DR TIGRFAMs; TIGR01292; TRX_reduct; 1. DR PROSITE; PS00573; PYRIDINE_REDOX_2; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Disulfide bond; FAD; Flavoprotein; NADP; KW Oxidoreductase; Redox-active center; Reference proteome. FT CHAIN 1 301 Putative thioredoxin reductase. FT /FTId=PRO_0000166759. FT NP_BIND 32 39 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT NP_BIND 272 280 FAD. {ECO:0000250|UniProtKB:P0A9P4}. FT DISULFID 130 133 Redox-active. FT {ECO:0000250|UniProtKB:P0A9P4}. SQ SEQUENCE 301 AA; 33035 MW; B8319F2B33559AD8 CRC64; MIHDTIIIGA GPGGLTAGIY AMRGKLNALC IEKENAGGRI AEAGIVENYP GFEEIRGYEL AEKFKNHAEK FKLPIIYDEV IKIETKERPF KVITKNSEYL TKTIVIATGT KPKKLGLNED KFIGRGISYC TMCDAFFYLN KEVIVIGRDT PAIMSAINLK DIAKKVIVIT DKSELKAAES IMLDKLKEAN NVEIIYNAKP LEIVGEERAE GVKISVNGKE EIIKADGIFI SLGHVPNTEF LKDSGIELDK KGFIKTDENC RTNIDGIYAV GDVRGGVMQV AKAVGDGCVA MANIIKYLQK L // ID TTDA_METJA Reviewed; 285 AA. AC Q58690; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Putative L(+)-tartrate dehydratase subunit alpha {ECO:0000250|UniProtKB:P05847}; DE Short=L-TTD alpha {ECO:0000250|UniProtKB:P05847}; DE EC=4.2.1.32 {ECO:0000250|UniProtKB:P05847}; GN OrderedLocusNames=MJ1294; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: (R,R)-tartrate = oxaloacetate + H(2)O. CC {ECO:0000250|UniProtKB:P05847}. CC -!- COFACTOR: CC Name=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408; CC Evidence={ECO:0000250|UniProtKB:P05847}; CC -!- SUBUNIT: Tetramer of two alpha and two beta subunits. CC {ECO:0000250|UniProtKB:P05847}. CC -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99301.1; -; Genomic_DNA. DR PIR; E64461; E64461. DR ProteinModelPortal; Q58690; -. DR STRING; 243232.MJ_1294; -. DR EnsemblBacteria; AAB99301; AAB99301; MJ_1294. DR KEGG; mja:MJ_1294; -. DR eggNOG; arCOG04407; Archaea. DR eggNOG; COG1951; LUCA. DR InParanoid; Q58690; -. DR KO; K01677; -. DR OMA; IQCWANR; -. DR PhylomeDB; Q58690; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0008730; F:L(+)-tartrate dehydratase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR004646; Fe-S_hydro-lyase_TtdA-typ_cat. DR Pfam; PF05681; Fumerase; 1. DR TIGRFAMs; TIGR00722; ttdA_fumA_fumB; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Lyase; Metal-binding; KW Reference proteome. FT CHAIN 1 285 Putative L(+)-tartrate dehydratase FT subunit alpha. FT /FTId=PRO_0000195661. FT METAL 60 60 Iron-sulfur. {ECO:0000250}. FT METAL 182 182 Iron-sulfur. {ECO:0000250}. FT METAL 269 269 Iron-sulfur. {ECO:0000250}. SQ SEQUENCE 285 AA; 31088 MW; 49BA64703BBC7ABC CRC64; MKISDVVVEL FREAAIYLPE DVKNALEEAY KKESSEISKN TLKAIIENNK IAEETQVPLC QDTGVPIVFL KIGKNINSSE IMKIIEEIKE GVKKATEEVP LRPNVVHPLT RENFKTNVGL NSPFINIEFD ESLDREIEII AFPKGAGSEN MSALKMLKPS DGIEGIKNFV LETIANAGGK PCPPIVVGIG IGGTADVALK LAKKALLRKI GERHRDKEIA NLEKELLEKI NSLGIGAMGL GGDITALDVF IEIAGCHTAS LPVGICIQCW ADRRAIKRIK LDAKL // ID TTDB_METJA Reviewed; 195 AA. AC Q58034; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative L(+)-tartrate dehydratase subunit beta {ECO:0000250|UniProtKB:P0AC35}; DE Short=L-TTD beta {ECO:0000250|UniProtKB:P0AC35}; DE EC=4.2.1.32 {ECO:0000250|UniProtKB:P0AC35}; GN OrderedLocusNames=MJ0617; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: (R,R)-tartrate = oxaloacetate + H(2)O. CC {ECO:0000250|UniProtKB:P0AC35}. CC -!- SUBUNIT: Heterotetramer of two alpha and two beta subunits. CC {ECO:0000250|UniProtKB:P0AC35}. CC -!- SIMILARITY: Belongs to the class-I fumarase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98612.1; -; Genomic_DNA. DR PIR; A64377; A64377. DR ProteinModelPortal; Q58034; -. DR STRING; 243232.MJ_0617; -. DR EnsemblBacteria; AAB98612; AAB98612; MJ_0617. DR KEGG; mja:MJ_0617; -. DR eggNOG; arCOG04406; Archaea. DR eggNOG; COG1838; LUCA. DR InParanoid; Q58034; -. DR KO; K01678; -. DR OMA; IYHAGPI; -. DR PhylomeDB; Q58034; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008730; F:L(+)-tartrate dehydratase activity; IEA:UniProtKB-EC. DR Gene3D; 3.20.130.10; -; 1. DR InterPro; IPR004647; Fe-S_hydro-lyase_TtdB-typ_cat. DR Pfam; PF05683; Fumerase_C; 1. DR SUPFAM; SSF117457; SSF117457; 1. DR TIGRFAMs; TIGR00723; ttdB_fumA_fumB; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 195 Putative L(+)-tartrate dehydratase FT subunit beta. FT /FTId=PRO_0000195662. FT ACT_SITE 36 36 {ECO:0000255}. FT BINDING 104 104 Substrate. {ECO:0000255}. SQ SEQUENCE 195 AA; 21868 MW; A5FDEB0E77D00902 CRC64; MEYTFNKLTK KDVKKLKVGD IVYLNGKIYT ARDEAHLKII EMLKSNEKLP FDLNESIIYH AGPIMKKVND SWVCVSIGPT TSARMNDVEE EFIKLTNISA IVGKGGMKKE LLKTFEDYGV VYLAAPGGCA ALLANSVKRV DNVYFLDELG MPEAVWELEV NNFGPLIVAM DSHGNSIYEE VNKKVYEKLN ELIGL // ID TSAC_METJA Reviewed; 207 AA. AC Q60369; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Putative threonylcarbamoyl-AMP synthase; DE Short=TC-AMP synthase; DE EC=2.7.7.87; DE AltName: Full=L-threonylcarbamoyladenylate synthase; DE AltName: Full=tRNA threonylcarbamoyladenosine biosynthesis protein MJ0062; GN OrderedLocusNames=MJ0062; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Required for the formation of a threonylcarbamoyl group CC on adenosine at position 37 (t(6)A37) in tRNAs that read codons CC beginning with adenine. Catalyzes the conversion of L-threonine, CC HCO(3)(-)/CO(2) and ATP to give threonylcarbamoyl-AMP (TC-AMP) as CC the acyladenylate intermediate, with the release of diphosphate. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: L-threonine + ATP + HCO(3)(-) = L- CC threonylcarbamoyladenylate + diphosphate + H(2)O. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the SUA5 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 YrdC-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00518}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98044.1; -; Genomic_DNA. DR PIR; F64307; F64307. DR ProteinModelPortal; Q60369; -. DR STRING; 243232.MJ_0062; -. DR EnsemblBacteria; AAB98044; AAB98044; MJ_0062. DR KEGG; mja:MJ_0062; -. DR eggNOG; arCOG01952; Archaea. DR eggNOG; COG0009; LUCA. DR InParanoid; Q60369; -. DR KO; K07566; -. DR OMA; FMPGPIT; -. DR PhylomeDB; Q60369; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003725; F:double-stranded RNA binding; IEA:InterPro. DR GO; GO:0061710; F:L-threonylcarbamoyladenylate synthase; IEA:UniProtKB-EC. DR GO; GO:0016779; F:nucleotidyltransferase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central. DR GO; GO:0006450; P:regulation of translational fidelity; IBA:GO_Central. DR GO; GO:0002949; P:tRNA threonylcarbamoyladenosine modification; IBA:GO_Central. DR Gene3D; 3.90.870.10; -; 1. DR InterPro; IPR017945; DHBP_synth_RibB-like_a/b_dom. DR InterPro; IPR006070; YrdC-like_dom. DR Pfam; PF01300; Sua5_yciO_yrdC; 1. DR SUPFAM; SSF55821; SSF55821; 1. DR TIGRFAMs; TIGR00057; TIGR00057; 1. DR PROSITE; PS51163; YRDC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Cytoplasm; Nucleotide-binding; KW Nucleotidyltransferase; Reference proteome; Transferase; KW tRNA processing. FT CHAIN 1 207 Putative threonylcarbamoyl-AMP synthase. FT /FTId=PRO_0000202028. FT DOMAIN 15 199 YrdC-like. {ECO:0000255|PROSITE- FT ProRule:PRU00518}. SQ SEQUENCE 207 AA; 23496 MW; B7EF4298F2432774 CRC64; MGLKNKIIKI YELNEEERKK VLEFLKKEIL NGKIVICGTD TLYGISANAL NEKAVRKVYN IKRREFNKPL SICVRDKNEI EKYAYVNDLA KKIIDKFLPG PLTIILKKKP GIPDIVAKDY IGIRIPDEPI IRELSIVPLT TTSANISGKE SPTTVDEIDK EVLKKVDYVI DIGKCKYSKP STIIKIEDDK IISIREGVIP IQKLARC // ID TSR3_METJA Reviewed; 172 AA. AC Q58118; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 81. DE RecName: Full=Probable ribosome biogenesis protein MJ0708 {ECO:0000255|HAMAP-Rule:MF_01116}; GN OrderedLocusNames=MJ0708; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probable pre-rRNA processing protein involved in CC ribosome biogenesis. {ECO:0000255|HAMAP-Rule:MF_01116}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01116}. CC -!- SIMILARITY: Belongs to the TSR3 family. {ECO:0000255|HAMAP- CC Rule:MF_01116}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98702.1; -; Genomic_DNA. DR PIR; D64388; D64388. DR STRING; 243232.MJ_0708; -. DR EnsemblBacteria; AAB98702; AAB98702; MJ_0708. DR KEGG; mja:MJ_0708; -. DR eggNOG; arCOG04733; Archaea. DR eggNOG; COG2042; LUCA. DR InParanoid; Q58118; -. DR KO; K09140; -. DR OMA; DCSWESA; -. DR PhylomeDB; Q58118; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030490; P:maturation of SSU-rRNA; IBA:GO_Central. DR HAMAP; MF_01116; TSR3; 1. DR InterPro; IPR022968; Rbsm_biogenesis. DR InterPro; IPR007209; RNaseL-inhib_metal-bd_dom. DR InterPro; IPR007177; TDD_dom. DR PANTHER; PTHR20426; PTHR20426; 1. DR Pfam; PF04034; DUF367; 1. DR Pfam; PF04068; RLI; 1. DR ProDom; PD016638; DUF367; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Reference proteome; Ribosome biogenesis; KW rRNA processing. FT CHAIN 1 172 Probable ribosome biogenesis protein FT MJ0708. FT /FTId=PRO_0000094418. SQ SEQUENCE 172 AA; 20030 MW; 01CF25475AD10B2A CRC64; MITMPKLFIY HANQCNPKKC TSLKMAKMNK AILLKNPYKV PKNSLILNPY AEKALSPEDK EIVEKFGITA LDCSWKEAEL MFKKFKFKNQ RSLPFLVACN PINYGKPCML STLEAFIAAL YITNFKDEAW DLTSCFKWAE TFIKVNYELL ERYSNAKNSM EVVEIQQDFL RK // ID TRPD_METJA Reviewed; 336 AA. AC Q57686; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 110. DE RecName: Full=Anthranilate phosphoribosyltransferase {ECO:0000255|HAMAP-Rule:MF_00211}; DE EC=2.4.2.18 {ECO:0000255|HAMAP-Rule:MF_00211}; GN Name=trpD {ECO:0000255|HAMAP-Rule:MF_00211}; OrderedLocusNames=MJ0234; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the transfer of the phosphoribosyl group of 5- CC phosphorylribose-1-pyrophosphate (PRPP) to anthranilate to yield CC N-(5'-phosphoribosyl)-anthranilate (PRA). {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- CATALYTIC ACTIVITY: N-(5-phospho-D-ribosyl)-anthranilate + CC diphosphate = anthranilate + 5-phospho-alpha-D-ribose 1- CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00211}; CC Note=Binds 2 magnesium ions per monomer. {ECO:0000255|HAMAP- CC Rule:MF_00211}; CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 2/5. {ECO:0000255|HAMAP- CC Rule:MF_00211}. CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00211}. CC -!- SIMILARITY: Belongs to the anthranilate phosphoribosyltransferase CC family. {ECO:0000255|HAMAP-Rule:MF_00211}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98221.1; -; Genomic_DNA. DR PIR; C64329; C64329. DR ProteinModelPortal; Q57686; -. DR STRING; 243232.MJ_0234; -. DR EnsemblBacteria; AAB98221; AAB98221; MJ_0234. DR KEGG; mja:MJ_0234; -. DR eggNOG; arCOG02012; Archaea. DR eggNOG; COG0547; LUCA. DR InParanoid; Q57686; -. DR KO; K00766; -. DR OMA; MIVLNAG; -. DR PhylomeDB; Q57686; -. DR UniPathway; UPA00035; UER00041. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004048; F:anthranilate phosphoribosyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1030.10; -; 1. DR HAMAP; MF_00211; TrpD; 1. DR InterPro; IPR005940; Anthranilate_Pribosyl_Tfrase. DR InterPro; IPR000312; Glycosyl_Trfase_fam3. DR InterPro; IPR017459; Glycosyl_Trfase_fam3_N_dom. DR Pfam; PF02885; Glycos_trans_3N; 1. DR Pfam; PF00591; Glycos_transf_3; 1. DR SUPFAM; SSF47648; SSF47648; 1. DR SUPFAM; SSF52418; SSF52418; 1. DR TIGRFAMs; TIGR01245; trpD; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glycosyltransferase; Magnesium; Metal-binding; KW Reference proteome; Transferase; Tryptophan biosynthesis. FT CHAIN 1 336 Anthranilate phosphoribosyltransferase. FT /FTId=PRO_0000154512. FT REGION 83 84 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 90 93 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT REGION 107 115 Phosphoribosylpyrophosphate binding. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT METAL 92 92 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 223 223 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 224 224 Magnesium 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT METAL 224 224 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 80 80 Anthranilate 1; via carbonyl oxygen. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 80 80 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 88 88 Phosphoribosylpyrophosphate. FT {ECO:0000255|HAMAP-Rule:MF_00211}. FT BINDING 110 110 Anthranilate 1. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 119 119 Phosphoribosylpyrophosphate; via amide FT nitrogen. {ECO:0000255|HAMAP- FT Rule:MF_00211}. FT BINDING 165 165 Anthranilate 2. {ECO:0000255|HAMAP- FT Rule:MF_00211}. SQ SEQUENCE 336 AA; 36630 MW; DF360D25328F71B6 CRC64; MITEALKKVI EFKDLDEKEA EAVMKDIMSG NAKPTQIAAI LTALRMKGET IEEITAFAKI MREFSLKINP NVPKLLDTCG TGGDNLNTFN ISTATAFVVS AYVPVAKHGN KAVSSKSGSA DVLEALGVNL NVPIERVKES IEKIGIGFLF APHFHPAMKF ATPVRKELGI RTVFNVLGPL TNPANANYQL MGVYDEKLTE KLANVLKNLG LKGALVVHGS GMDEITTIGK TKISELRNGE IKSYYIEPED FGIKKAKLED IRGGDAEENA KIIGEIFEGE EVGAKRDIVV LNAAFALYIA EEAKDVEEGI KLAEKSIDEG KALKKLEDLI EFYREG // ID TRPE_METJA Reviewed; 474 AA. AC Q58475; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Anthranilate synthase component 1; DE Short=AS; DE Short=ASI; DE EC=4.1.3.27; GN Name=trpE; OrderedLocusNames=MJ1075; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:P00897}; CC Note=Binds 1 Mg(2+) ion per subunit. CC {ECO:0000250|UniProtKB:P00897}; CC -!- ENZYME REGULATION: Feedback inhibited by tryptophan. CC {ECO:0000250}. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Belongs to the anthranilate synthase component I CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99074.1; -; Genomic_DNA. DR PIR; B64434; B64434. DR ProteinModelPortal; Q58475; -. DR STRING; 243232.MJ_1075; -. DR EnsemblBacteria; AAB99074; AAB99074; MJ_1075. DR KEGG; mja:MJ_1075; -. DR eggNOG; arCOG02014; Archaea. DR eggNOG; COG0147; LUCA. DR InParanoid; Q58475; -. DR KO; K01657; -. DR OMA; GELIQCV; -. DR PhylomeDB; Q58475; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.60.120.10; -; 1. DR InterPro; IPR005801; ADC_synthase. DR InterPro; IPR019999; Anth_synth_I-like. DR InterPro; IPR006805; Anth_synth_I_N. DR InterPro; IPR010116; Anthranilate_synth_I_arc_typ. DR InterPro; IPR015890; Chorismate_C. DR Pfam; PF04715; Anth_synt_I_N; 1. DR Pfam; PF00425; Chorismate_bind; 1. DR PRINTS; PR00095; ANTSNTHASEI. DR SUPFAM; SSF56322; SSF56322; 1. DR TIGRFAMs; TIGR01820; TrpE-arch; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Lyase; Magnesium; Metal-binding; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 474 Anthranilate synthase component 1. FT /FTId=PRO_0000154128. FT REGION 254 256 Tryptophan binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 293 294 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT REGION 442 444 Chorismate binding. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 320 320 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT METAL 457 457 Magnesium. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 29 29 Tryptophan. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 408 408 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 428 428 Chorismate. FT {ECO:0000250|UniProtKB:P00897}. FT BINDING 444 444 Chorismate; via amide nitrogen. FT {ECO:0000250|UniProtKB:P00897}. SQ SEQUENCE 474 AA; 54300 MW; 7094E20F7C2A5124 CRC64; MIIKKIKMDV CPLDVYEQIR GENTFLLESA EGVPKVARYS ILGKAEGKVI FKNGKLKVES FTEFGDKAKD LEGKYECPLD ALREVRNEYL KYIDISNIEP IPRFKGGLVG YLSYDIIRYW IDLSNINPKP INDLKFPDAE FFIVKDFISF DLKEKVINLI AEDDEGIREL ERIIKNAKIG NNDNKEEKTT ENKDLKIKSN MSKEEFIEAV KKAKEYIFAG DIFQVVLSRR IEIDLDNLDH LKIYKKVREI NPSPYMYYLD FGDRKIIGSS PEILVRTDYK DNKRLVITRP IAGTIRRGKT EEEDKELEKK LLSDEKERAE HVMLVDLARN DIGKISKFGT VEVTDFMIIE KYSHVQHIVS NVVGELKDNY DSFLAVKATF PAGTLSGAPK VRAMEIIEEL EKTWRGPYGG GVGYFGWDDL MDLAITIRTF VISKNKGYIQ VGAGIVADSI PENEWEETER KGMANVKTIE SLLK // ID TRUD1_METJA Reviewed; 392 AA. AC Q58008; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 26-SEP-2003, sequence version 2. DT 17-FEB-2016, entry version 90. DE RecName: Full=Probable tRNA pseudouridine synthase D 1 {ECO:0000255|HAMAP-Rule:MF_01082}; DE EC=5.4.99.27 {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA pseudouridine(13) synthase {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA pseudouridylate synthase D 1 {ECO:0000255|HAMAP-Rule:MF_01082}; DE AltName: Full=tRNA-uridine isomerase D 1 {ECO:0000255|HAMAP-Rule:MF_01082}; GN Name=truD1 {ECO:0000255|HAMAP-Rule:MF_01082}; GN OrderedLocusNames=MJ0588; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Could be responsible for synthesis of pseudouridine from CC uracil-13 in transfer RNAs. {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(13) = tRNA pseudouridine(13). CC {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family. CC {ECO:0000255|HAMAP-Rule:MF_01082}. CC -!- SIMILARITY: Contains 1 TRUD domain. {ECO:0000255|HAMAP- CC Rule:MF_01082}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98579.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98579.1; ALT_INIT; Genomic_DNA. DR PIR; D64373; D64373. DR ProteinModelPortal; Q58008; -. DR STRING; 243232.MJ_0588; -. DR EnsemblBacteria; AAB98579; AAB98579; MJ_0588. DR KEGG; mja:MJ_0588; -. DR eggNOG; arCOG04252; Archaea. DR eggNOG; COG0585; LUCA. DR InParanoid; Q58008; -. DR KO; K06176; -. DR OMA; LRYERAM; -. DR PhylomeDB; Q58008; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01082; TruD; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001656; PsdUridine_synth_TruD. DR InterPro; IPR011760; PsdUridine_synth_TruD_insert. DR PANTHER; PTHR13326; PTHR13326; 1. DR Pfam; PF01142; TruD; 2. DR SUPFAM; SSF55120; SSF55120; 2. DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1. DR PROSITE; PS50984; TRUD; 1. DR PROSITE; PS01268; UPF0024; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 392 Probable tRNA pseudouridine synthase D 1. FT /FTId=PRO_0000152540. FT DOMAIN 167 354 TRUD. {ECO:0000255|HAMAP-Rule:MF_01082}. FT ACT_SITE 92 92 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_01082}. SQ SEQUENCE 392 AA; 46320 MW; DC00CC533E6E065C CRC64; MPLNMNKYLT DAYTGGIIKK YPEDFIVEEI TPEGIILEVG KSIEFKDEEN WKGNYIHFTL EKRNWTTLDA IREIANRVGK QRKHFGFAGN KDKYAVTTQR VGCFNVKLED LMKVKIKGII LRDFQKTNRK IRLGDLWGNR FTIRVREPEL KGKELEEALN KLCKLKYFLN YYGVQRFGTT RPITHIVGRF IIERDWEGAF HAYCGTPLPY DDKKSKLARE LVDEENFKEA YKKFPKAFFY ERRMIKAYIE TGSYQKAFMI LPPYLRCMFI NAYQSYLFNE IINRRFEYGF EPMEGDILID NVPSGALFGY KTRFASGIQG EIEREIYERE NLSPEDFKIG EFGSFIGDRR AMIGKIYNMK YWIEDDSYVL QFCLKKGNYA TSVLREFIEK KD // ID TYW1_METJA Reviewed; 311 AA. AC Q57705; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=S-adenosyl-L-methionine-dependent tRNA 4-demethylwyosine synthase {ECO:0000255|HAMAP-Rule:MF_01921}; DE EC=4.1.3.44 {ECO:0000255|HAMAP-Rule:MF_01921}; DE AltName: Full=MjTYW1; DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw1 {ECO:0000255|HAMAP-Rule:MF_01921}; GN Name=taw1 {ECO:0000255|HAMAP-Rule:MF_01921}; OrderedLocusNames=MJ0257; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP GENE NAME. RX PubMed=20382657; DOI=10.1093/molbev/msq096; RA de Crecy-Lagard V., Brochier-Armanet C., Urbonavicius J., RA Fernandez B., Phillips G., Lyons B., Noma A., Alvarez S., RA Droogmans L., Armengaud J., Grosjean H.; RT "Biosynthesis of wyosine derivatives in tRNA: an ancient and highly RT diverse pathway in Archaea."; RL Mol. Biol. Evol. 27:2062-2077(2010). RN [3] RP CATALYTIC ACTIVITY, AND FUNCTION. RX PubMed=22026549; DOI=10.1021/bi2015053; RA Young A.P., Bandarian V.; RT "Pyruvate is the source of the two carbons that are required for RT formation of the imidazoline ring of 4-demethylwyosine."; RL Biochemistry 50:10573-10575(2011). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS), COFACTOR, AND SUBUNIT. RX PubMed=17727881; DOI=10.1016/j.jmb.2007.07.024; RA Suzuki Y., Noma A., Suzuki T., Senda M., Senda T., Ishitani R., RA Nureki O.; RT "Crystal structure of the radical SAM enzyme catalyzing tricyclic RT modified base formation in tRNA."; RL J. Mol. Biol. 372:1204-1214(2007). CC -!- FUNCTION: Component of the wyosine derivatives biosynthesis CC pathway that catalyzes the condensation of N-methylguanine with 2 CC carbon atoms from pyruvate to form the tricyclic 4-demethylwyosine CC (imG-14) on guanosine-37 of tRNA(Phe). {ECO:0000255|HAMAP- CC Rule:MF_01921, ECO:0000269|PubMed:22026549}. CC -!- CATALYTIC ACTIVITY: N(1)-methylguanine(37) in tRNA(Phe) + pyruvate CC + S-adenosyl-L-methionine = 4-demethylwyosine(37) in tRNA(Phe) + CC L-methionine + 5'-deoxyadenosine + CO(2) + H(2)O. CC {ECO:0000255|HAMAP-Rule:MF_01921, ECO:0000269|PubMed:22026549}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305|PubMed:17727881}; CC Note=Binds 2 [4Fe-4S] clusters. Binds 1 [4Fe-4S] cluster CC coordinated with 3 cysteines and an exchangeable S-adenosyl-L- CC methionine. {ECO:0000305|PubMed:17727881}; CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01921, CC ECO:0000269|PubMed:17727881}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01921}. CC -!- SIMILARITY: Belongs to the TYW1 family. {ECO:0000255|HAMAP- CC Rule:MF_01921}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98244.1; -; Genomic_DNA. DR PIR; B64332; B64332. DR PDB; 2Z2U; X-ray; 2.40 A; A=1-311. DR PDBsum; 2Z2U; -. DR ProteinModelPortal; Q57705; -. DR SMR; Q57705; 1-311. DR STRING; 243232.MJ_0257; -. DR EnsemblBacteria; AAB98244; AAB98244; MJ_0257. DR KEGG; mja:MJ_0257; -. DR eggNOG; arCOG04174; Archaea. DR eggNOG; COG0731; LUCA. DR InParanoid; Q57705; -. DR KO; K15449; -. DR OMA; KLCGWVR; -. DR PhylomeDB; Q57705; -. DR BRENDA; 4.1.3.44; 3260. DR EvolutionaryTrace; Q57705; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016833; F:oxo-acid-lyase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0008033; P:tRNA processing; IEA:UniProtKB-HAMAP. DR Gene3D; 3.20.20.70; -; 1. DR HAMAP; MF_01921; TYW1_archaea; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR013917; tRNA_wybutosine-synth. DR InterPro; IPR023993; TYW1_archaea. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF08608; Wyosine_form; 1. DR TIGRFAMs; TIGR03972; rSAM_TYW1; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Complete proteome; Cytoplasm; Iron; Iron-sulfur; KW Lyase; Metal-binding; Reference proteome; S-adenosyl-L-methionine; KW tRNA processing. FT CHAIN 1 311 S-adenosyl-L-methionine-dependent tRNA 4- FT demethylwyosine synthase. FT /FTId=PRO_0000217862. FT METAL 26 26 Iron-sulfur 1 (4Fe-4S). {ECO:0000305}. FT METAL 39 39 Iron-sulfur 1 (4Fe-4S). {ECO:0000305}. FT METAL 52 52 Iron-sulfur 1 (4Fe-4S). {ECO:0000305}. FT METAL 62 62 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT METAL 66 66 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT METAL 69 69 Iron-sulfur 2 (4Fe-4S-S-AdoMet). FT {ECO:0000305}. FT HELIX 4 11 {ECO:0000244|PDB:2Z2U}. FT TURN 12 14 {ECO:0000244|PDB:2Z2U}. FT STRAND 16 18 {ECO:0000244|PDB:2Z2U}. FT STRAND 21 24 {ECO:0000244|PDB:2Z2U}. FT HELIX 29 33 {ECO:0000244|PDB:2Z2U}. FT HELIX 40 45 {ECO:0000244|PDB:2Z2U}. FT HELIX 49 51 {ECO:0000244|PDB:2Z2U}. FT STRAND 52 57 {ECO:0000244|PDB:2Z2U}. FT HELIX 92 108 {ECO:0000244|PDB:2Z2U}. FT HELIX 109 113 {ECO:0000244|PDB:2Z2U}. FT HELIX 114 117 {ECO:0000244|PDB:2Z2U}. FT HELIX 119 125 {ECO:0000244|PDB:2Z2U}. FT STRAND 130 133 {ECO:0000244|PDB:2Z2U}. FT STRAND 135 137 {ECO:0000244|PDB:2Z2U}. FT HELIX 139 141 {ECO:0000244|PDB:2Z2U}. FT HELIX 145 154 {ECO:0000244|PDB:2Z2U}. FT STRAND 158 163 {ECO:0000244|PDB:2Z2U}. FT HELIX 168 173 {ECO:0000244|PDB:2Z2U}. FT STRAND 177 182 {ECO:0000244|PDB:2Z2U}. FT TURN 188 190 {ECO:0000244|PDB:2Z2U}. FT HELIX 199 212 {ECO:0000244|PDB:2Z2U}. FT STRAND 215 224 {ECO:0000244|PDB:2Z2U}. FT TURN 226 228 {ECO:0000244|PDB:2Z2U}. FT HELIX 232 234 {ECO:0000244|PDB:2Z2U}. FT HELIX 236 242 {ECO:0000244|PDB:2Z2U}. FT STRAND 245 251 {ECO:0000244|PDB:2Z2U}. FT HELIX 270 281 {ECO:0000244|PDB:2Z2U}. FT STRAND 283 292 {ECO:0000244|PDB:2Z2U}. FT TURN 293 296 {ECO:0000244|PDB:2Z2U}. FT STRAND 297 302 {ECO:0000244|PDB:2Z2U}. SQ SEQUENCE 311 AA; 36712 MW; 7B05311C25A29F3D CRC64; MIPEEIYKIL RKQRYQIDGH TAVKLCGWVR KKMLEDKNCY KSKFYGIETH RCIQCTPSVI WCQQNCIFCW RVLPRDIGID ISQIKEPKWE EPEVVYEKIL AMHKRIIMGY AGVLDRVGEK KFKEALEPKH VAISLSGEPT LYPYLDELIK IFHKNGFTTF VVSNGILTDV IEKIEPTQLY ISLDAYDLDS YRRICGGKKE YWESILNTLD ILKEKKRTCI RTTLIRGYND DILKFVELYE RADVHFIELK SYMHVGYSQK RLKKEDMLQH DEILKLAKML DENSSYKLID DSEDSRVALL QNENRKINPK L // ID TYW3_METJA Reviewed; 193 AA. AC Q58905; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase {ECO:0000255|HAMAP-Rule:MF_00266}; DE EC=2.1.1.282 {ECO:0000255|HAMAP-Rule:MF_00266}; DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw3 {ECO:0000255|HAMAP-Rule:MF_00266}; GN Name=taw3 {ECO:0000255|HAMAP-Rule:MF_00266}; OrderedLocusNames=MJ1510; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP GENE NAME. RX PubMed=20382657; DOI=10.1093/molbev/msq096; RA de Crecy-Lagard V., Brochier-Armanet C., Urbonavicius J., RA Fernandez B., Phillips G., Lyons B., Noma A., Alvarez S., RA Droogmans L., Armengaud J., Grosjean H.; RT "Biosynthesis of wyosine derivatives in tRNA: an ancient and highly RT diverse pathway in Archaea."; RL Mol. Biol. Evol. 27:2062-2077(2010). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent methyltransferase that CC acts as a component of the wyosine derivatives biosynthesis CC pathway. Probably methylates N-4 position of wybutosine-86 to CC produce wybutosine-72. {ECO:0000255|HAMAP-Rule:MF_00266}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 7-((3S)-(3-amino-3- CC carboxypropyl))-4-demethylwyosine(37) in tRNA(Phe) = S-adenosyl-L- CC homocysteine + 7-((3S)-(3-amino-3-carboxypropyl))wyosine(37) in CC tRNA(Phe). {ECO:0000255|HAMAP-Rule:MF_00266}. CC -!- SIMILARITY: Belongs to the TYW3 family. {ECO:0000255|HAMAP- CC Rule:MF_00266}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99529.1; -; Genomic_DNA. DR PIR; E64488; E64488. DR ProteinModelPortal; Q58905; -. DR STRING; 243232.MJ_1510; -. DR EnsemblBacteria; AAB99529; AAB99529; MJ_1510. DR KEGG; mja:MJ_1510; -. DR eggNOG; arCOG04156; Archaea. DR eggNOG; COG1590; LUCA. DR InParanoid; Q58905; -. DR KO; K15450; -. DR OMA; GKWHHYA; -. DR PhylomeDB; Q58905; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008175; F:tRNA methyltransferase activity; IEA:InterPro. DR GO; GO:0031591; P:wybutosine biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1960.10; -; 1. DR HAMAP; MF_00266; TYW3_archaea; 1. DR InterPro; IPR022908; Taw3. DR InterPro; IPR003827; tRNA_yW-synthesising. DR Pfam; PF02676; TYW3; 1. DR SUPFAM; SSF111278; SSF111278; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 193 tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4- FT demethylwyosine(37)-N(4))- FT methyltransferase. FT /FTId=PRO_0000157093. SQ SEQUENCE 193 AA; 22401 MW; D8E149EC7B4A51C9 CRC64; MGFLEDKKRT LMNLELAIRE GLVDEEIIPI LNKINEIDNY YTTSSCIGRV GIMEIPKDKN PKLYSRWLGK WHHYASYDEL FNALKNKKEG YIVFVMNSPI LHIACKDIES AKKMLELAIH SGLKASSIKS ISDKRVIVEI LTTYKVDTPI GEDGEIFVDN NYLKFLLDYS NSKLKRAREI LMRWANRLDE LKK // ID TRPG_METJA Reviewed; 197 AA. AC Q57690; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Anthranilate synthase component 2; DE Short=AS; DE Short=ASII; DE EC=4.1.3.27; DE AltName: Full=Anthranilate synthase, GATase component; DE AltName: Full=Anthranilate synthase, glutamine amidotransferase component; GN Name=trpG; OrderedLocusNames=MJ0238; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of a heterotetrameric complex that catalyzes the CC two-step biosynthesis of anthranilate, an intermediate in the CC biosynthesis of L-tryptophan. In the first step, the glutamine- CC binding beta subunit (TrpG) of anthranilate synthase (AS) provides CC the glutamine amidotransferase activity which generates ammonia as CC a substrate that, along with chorismate, is used in the second CC step, catalyzed by the large alpha subunit of AS (TrpE) to produce CC anthranilate. In the absence of TrpG, TrpE can synthesize CC anthranilate directly from chorismate and high concentrations of CC ammonia (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: Chorismate + L-glutamine = anthranilate + CC pyruvate + L-glutamate. CC -!- PATHWAY: Amino-acid biosynthesis; L-tryptophan biosynthesis; L- CC tryptophan from chorismate: step 1/5. CC -!- SUBUNIT: Heterotetramer consisting of two non-identical subunits: CC a beta subunit (TrpG) and a large alpha subunit (TrpE). CC {ECO:0000250}. CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98224.1; -; Genomic_DNA. DR PIR; G64329; G64329. DR ProteinModelPortal; Q57690; -. DR STRING; 243232.MJ_0238; -. DR MEROPS; C26.959; -. DR EnsemblBacteria; AAB98224; AAB98224; MJ_0238. DR KEGG; mja:MJ_0238; -. DR eggNOG; arCOG00086; Archaea. DR eggNOG; COG0512; LUCA. DR InParanoid; Q57690; -. DR KO; K01658; -. DR OMA; MHGIVDT; -. DR PhylomeDB; Q57690; -. DR UniPathway; UPA00035; UER00040. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004049; F:anthranilate synthase activity; IEA:UniProtKB-EC. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0000162; P:tryptophan biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR017926; GATASE. DR InterPro; IPR006221; TrpG/PapA_dom. DR Pfam; PF00117; GATase; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR00566; trpG_papA; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Amino-acid biosynthesis; Aromatic amino acid biosynthesis; KW Complete proteome; Glutamine amidotransferase; Lyase; KW Reference proteome; Tryptophan biosynthesis. FT CHAIN 1 197 Anthranilate synthase component 2. FT /FTId=PRO_0000056888. FT DOMAIN 5 197 Glutamine amidotransferase type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT REGION 55 57 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT REGION 130 131 Glutamine binding. FT {ECO:0000250|UniProtKB:P00900}. FT ACT_SITE 80 80 Nucleophile; for GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 168 168 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT ACT_SITE 170 170 For GATase activity. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. FT BINDING 84 84 Glutamine. FT {ECO:0000250|UniProtKB:P00900}. SQ SEQUENCE 197 AA; 22061 MW; 982A3475C4155B7D CRC64; MEVKKVLVID NIDSFVWNLV QYVGTLGYKV KLVDNKITLD EIKKINPDRI IISPGPKTPK EAGNCIKIIQ EVDIPILGVC LGHQCIVEAF GGEVGRAKRV MHGKASLINH DGEGIFKDIP NPFYGGRYHS LIAKEVPKEL KITAKSLDDN YIMGVRHKKL PIEGVQFHPE SILTESDNLK FPDLGLKLIK NFVESEY // ID TRUA_METJA Reviewed; 259 AA. AC Q59069; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=tRNA pseudouridine synthase A {ECO:0000255|HAMAP-Rule:MF_00171}; DE EC=5.4.99.12 {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridine(38-40) synthase {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA pseudouridylate synthase I {ECO:0000255|HAMAP-Rule:MF_00171}; DE AltName: Full=tRNA-uridine isomerase I {ECO:0000255|HAMAP-Rule:MF_00171}; GN Name=truA {ECO:0000255|HAMAP-Rule:MF_00171}; OrderedLocusNames=MJ1675; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Formation of pseudouridine at positions 38, 39 and 40 in CC the anticodon stem and loop of transfer RNAs. {ECO:0000255|HAMAP- CC Rule:MF_00171}. CC -!- CATALYTIC ACTIVITY: tRNA uridine(38-40) = tRNA pseudouridine(38- CC 40). {ECO:0000255|HAMAP-Rule:MF_00171}. CC -!- SIMILARITY: Belongs to the tRNA pseudouridine synthase TruA CC family. {ECO:0000255|HAMAP-Rule:MF_00171}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99697.1; -; Genomic_DNA. DR PIR; A64509; A64509. DR ProteinModelPortal; Q59069; -. DR STRING; 243232.MJ_1675; -. DR EnsemblBacteria; AAB99697; AAB99697; MJ_1675. DR KEGG; mja:MJ_1675; -. DR eggNOG; arCOG04449; Archaea. DR eggNOG; COG0101; LUCA. DR InParanoid; Q59069; -. DR KO; K06173; -. DR OMA; HYRYILP; -. DR PhylomeDB; Q59069; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009982; F:pseudouridine synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR GO; GO:0031119; P:tRNA pseudouridine synthesis; IEA:UniProtKB-HAMAP. DR Gene3D; 3.30.70.580; -; 1. DR Gene3D; 3.30.70.660; -; 1. DR HAMAP; MF_00171; TruA; 1. DR InterPro; IPR020103; PsdUridine_synth_cat_dom. DR InterPro; IPR001406; PsdUridine_synth_TruA. DR InterPro; IPR020097; PsdUridine_synth_TruA_a/b_dom. DR InterPro; IPR020095; PsdUridine_synth_TruA_C. DR InterPro; IPR020094; PsdUridine_synth_TruA_N. DR PANTHER; PTHR11142; PTHR11142; 1. DR Pfam; PF01416; PseudoU_synth_1; 1. DR PIRSF; PIRSF001430; tRNA_psdUrid_synth; 1. DR SUPFAM; SSF55120; SSF55120; 1. DR TIGRFAMs; TIGR00071; hisT_truA; 1. PE 3: Inferred from homology; KW Complete proteome; Isomerase; Reference proteome; tRNA processing. FT CHAIN 1 259 tRNA pseudouridine synthase A. FT /FTId=PRO_0000057503. FT ACT_SITE 50 50 Nucleophile. {ECO:0000255|HAMAP- FT Rule:MF_00171}. FT BINDING 101 101 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00171}. SQ SEQUENCE 259 AA; 30110 MW; 3B6A8C4AF03A5C85 CRC64; MYILKIAYDG RYSFQQQPHK QTVCDILLDA LEETGFLAKK KVIYSGGRTD KGVSALGNFV VVELKKEPIL SYINAKLKDK GIWVLGYREI DEIPKVKYRH YRYILPNIGY DVDAIKEGAK KMIGTHSFHN LSKRDRTKEK SPIRTIYDIK ISENEFYLTV DIIGESFLWN MVRKIVGALD LVGRGKKPVE WIDKLLDENH REGVPTFPPE GLILVEAKVD IEYIYDNYSI RKFKEYWGEF FKLQVMKIGI AKTVLEFTK // ID UBIX_METJA Reviewed; 184 AA. AC Q57566; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Flavin prenyltransferase UbiX {ECO:0000255|HAMAP-Rule:MF_01984}; DE EC=2.5.1.129 {ECO:0000255|HAMAP-Rule:MF_01984}; GN Name=ubiX {ECO:0000255|HAMAP-Rule:MF_01984}; OrderedLocusNames=MJ0102; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Flavin prenyltransferase that catalyzes the synthesis of CC the prenylated FMN cofactor (prenyl-FMN) for 4-hydroxy-3- CC polyprenylbenzoic acid decarboxylase UbiD. The prenyltransferase CC is metal-independent and links a dimethylallyl moiety from CC dimethylallyl monophosphate (DMAP) to the flavin N5 and C6 atoms CC of FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl phosphate + FMNH(2) = prenylated CC FMNH(2) + phosphate. {ECO:0000255|HAMAP-Rule:MF_01984}. CC -!- SIMILARITY: Belongs to the UbiX/PAD1 family. {ECO:0000255|HAMAP- CC Rule:MF_01984}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98082.1; -; Genomic_DNA. DR PIR; F64312; F64312. DR ProteinModelPortal; Q57566; -. DR SMR; Q57566; 2-177. DR STRING; 243232.MJ_0102; -. DR EnsemblBacteria; AAB98082; AAB98082; MJ_0102. DR KEGG; mja:MJ_0102; -. DR eggNOG; arCOG01703; Archaea. DR eggNOG; COG0163; LUCA. DR InParanoid; Q57566; -. DR KO; K03186; -. DR OMA; IIMPREM; -. DR PhylomeDB; Q57566; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0051188; P:cofactor biosynthetic process; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.1950; -; 1. DR HAMAP; MF_01984; ubiX_pad; 1. DR InterPro; IPR003382; Flavoprotein. DR InterPro; IPR004507; UbiX_Pad1. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR00421; ubiX_pad; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Prenyltransferase; KW Reference proteome; Transferase. FT CHAIN 1 184 Flavin prenyltransferase UbiX. FT /FTId=PRO_0000134978. FT NP_BIND 9 11 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT NP_BIND 85 88 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 34 34 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 120 120 FMN. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 150 150 DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}. FT BINDING 166 166 DMAP. {ECO:0000255|HAMAP-Rule:MF_01984}. SQ SEQUENCE 184 AA; 20643 MW; F3EDBFE5B48A82C5 CRC64; MKIIVCITGA SGVIYAKRLL EVLKDRAEVN LIISNSAKKI IKEELDIDWK EIKKLATDYY ENDDFFSPLA SGSNKFDAVV VVPCSMKTLS AIANGYSANL IVRVCDIALK ERRKLIIMPR EMPFNSIHLE NMLKLSNLGA IVMPPIPAFY NKPKNVNDII NFVVGRVLDI LGIDNSLFKR WGTV // ID TYW2_METJA Reviewed; 249 AA. AC Q58952; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=tRNA(Phe) (4-demethylwyosine(37)-C(7)) aminocarboxypropyltransferase {ECO:0000255|HAMAP-Rule:MF_01922}; DE EC=2.5.1.114 {ECO:0000255|HAMAP-Rule:MF_01922}; DE AltName: Full=MjTYW2; DE AltName: Full=tRNA wyosine derivatives biosynthesis protein Taw2 {ECO:0000255|HAMAP-Rule:MF_01922}; GN Name=taw2 {ECO:0000255|HAMAP-Rule:MF_01922}; OrderedLocusNames=MJ1557; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP GENE NAME. RX PubMed=20382657; DOI=10.1093/molbev/msq096; RA de Crecy-Lagard V., Brochier-Armanet C., Urbonavicius J., RA Fernandez B., Phillips G., Lyons B., Noma A., Alvarez S., RA Droogmans L., Armengaud J., Grosjean H.; RT "Biosynthesis of wyosine derivatives in tRNA: an ancient and highly RT diverse pathway in Archaea."; RL Mol. Biol. Evol. 27:2062-2077(2010). RN [3] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH RP S-ADENOSYL-L-METHIONINE, FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY. RX PubMed=19717466; DOI=10.1073/pnas.0905270106; RA Umitsu M., Nishimasu H., Noma A., Suzuki T., Ishitani R., Nureki O.; RT "Structural basis of AdoMet-dependent aminocarboxypropyl transfer RT reaction catalyzed by tRNA-wybutosine synthesizing enzyme, TYW2."; RL Proc. Natl. Acad. Sci. U.S.A. 106:15616-15621(2009). CC -!- FUNCTION: S-adenosyl-L-methionine-dependent transferase that acts CC as a component of the wyosine derivatives biosynthesis pathway. CC Catalyzes the transfer of the alpha-amino-alpha-carboxypropyl CC (acp) group from S-adenosyl-L-methionine to 4-demethylwyosine CC (imG-14), forming 7-aminocarboxypropyl-demethylwyosine CC (wybutosine-86) at position 37 of tRNA(Phe). {ECO:0000255|HAMAP- CC Rule:MF_01922, ECO:0000269|PubMed:19717466}. CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + 4- CC demethylwyosine(37) in tRNA(Phe) = S-methyl-5'-thioadenosine + 7- CC ((3S)-3-amino-3-carboxypropyl)-4-demethylwyosine(37) in tRNA(Phe). CC {ECO:0000255|HAMAP-Rule:MF_01922, ECO:0000269|PubMed:19717466}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01922}. CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. TRM5/TYW2 family. CC {ECO:0000255|HAMAP-Rule:MF_01922}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99577.1; -; Genomic_DNA. DR PIR; D64494; D64494. DR PDB; 3A27; X-ray; 2.00 A; A=1-249. DR PDBsum; 3A27; -. DR ProteinModelPortal; Q58952; -. DR STRING; 243232.MJ_1557; -. DR EnsemblBacteria; AAB99577; AAB99577; MJ_1557. DR KEGG; mja:MJ_1557; -. DR eggNOG; arCOG10124; Archaea. DR eggNOG; COG2520; LUCA. DR InParanoid; Q58952; -. DR KO; K07055; -. DR OMA; KYQKIGD; -. DR PhylomeDB; Q58952; -. DR BRENDA; 2.5.1.114; 3260. DR EvolutionaryTrace; Q58952; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB. DR GO; GO:0006400; P:tRNA modification; IDA:UniProtKB. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_01922; TYW2_archaea; 1. DR InterPro; IPR030382; MeTrfase_TRM5/TYW2. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR030867; TYW2_archaea. DR Pfam; PF02475; Met_10; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51684; SAM_MT_TRM5_TYW2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Reference proteome; KW S-adenosyl-L-methionine; Transferase; tRNA processing. FT CHAIN 1 249 tRNA(Phe) (4-demethylwyosine(37)-C(7)) FT aminocarboxypropyltransferase. FT /FTId=PRO_0000107411. FT REGION 154 155 S-adenosyl-L-methionine binding. FT BINDING 80 80 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01922, FT ECO:0000269|PubMed:19717466}. FT BINDING 87 87 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01922}. FT BINDING 127 127 S-adenosyl-L-methionine. FT {ECO:0000255|HAMAP-Rule:MF_01922, FT ECO:0000269|PubMed:19717466}. FT STRAND 6 8 {ECO:0000244|PDB:3A27}. FT STRAND 11 14 {ECO:0000244|PDB:3A27}. FT STRAND 34 38 {ECO:0000244|PDB:3A27}. FT STRAND 52 55 {ECO:0000244|PDB:3A27}. FT STRAND 60 65 {ECO:0000244|PDB:3A27}. FT STRAND 68 73 {ECO:0000244|PDB:3A27}. FT TURN 74 76 {ECO:0000244|PDB:3A27}. FT HELIX 81 83 {ECO:0000244|PDB:3A27}. FT HELIX 84 91 {ECO:0000244|PDB:3A27}. FT STRAND 99 102 {ECO:0000244|PDB:3A27}. FT TURN 106 110 {ECO:0000244|PDB:3A27}. FT HELIX 111 117 {ECO:0000244|PDB:3A27}. FT STRAND 121 127 {ECO:0000244|PDB:3A27}. FT HELIX 130 142 {ECO:0000244|PDB:3A27}. FT STRAND 146 153 {ECO:0000244|PDB:3A27}. FT HELIX 155 157 {ECO:0000244|PDB:3A27}. FT STRAND 164 169 {ECO:0000244|PDB:3A27}. FT HELIX 175 178 {ECO:0000244|PDB:3A27}. FT HELIX 179 185 {ECO:0000244|PDB:3A27}. FT STRAND 186 199 {ECO:0000244|PDB:3A27}. FT HELIX 200 202 {ECO:0000244|PDB:3A27}. FT TURN 203 205 {ECO:0000244|PDB:3A27}. FT HELIX 206 217 {ECO:0000244|PDB:3A27}. FT STRAND 220 234 {ECO:0000244|PDB:3A27}. FT STRAND 237 248 {ECO:0000244|PDB:3A27}. SQ SEQUENCE 249 AA; 29302 MW; A4D1EB10B63CA51C CRC64; MGIKYQKIGD VVIVKKELSE DEIREIVKRT KCKAILLYTT QITGEFRTPH VKILYGKETE TIHKEYGCLF KLDVAKIMWS QGNIEERKRM AFISNENEVV VDMFAGIGYF TIPLAKYSKP KLVYAIEKNP TAYHYLCENI KLNKLNNVIP ILADNRDVEL KDVADRVIMG YVHKTHKFLD KTFEFLKDRG VIHYHETVAE KIMYERPIER LKFYAEKNGY KLIDYEVRKI KKYAPGVWHV VVDAKFERI // ID TYSY_METJA Reviewed; 222 AA. AC Q57931; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 106. DE RecName: Full=Putative thymidylate synthase {ECO:0000255|HAMAP-Rule:MF_01686}; DE Short=TS {ECO:0000255|HAMAP-Rule:MF_01686}; DE Short=TSase {ECO:0000255|HAMAP-Rule:MF_01686}; DE EC=2.1.1.- {ECO:0000255|HAMAP-Rule:MF_01686}; GN Name=thyA {ECO:0000255|HAMAP-Rule:MF_01686}; OrderedLocusNames=MJ0511; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May catalyze the biosynthesis of dTMP using an unknown CC cosubstrate. {ECO:0000255|HAMAP-Rule:MF_01686}. CC -!- PATHWAY: Pyrimidine metabolism; dTTP biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_01686}. CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_01686}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_01686}. CC -!- SIMILARITY: Belongs to the thymidylate synthase family. Archaeal- CC type ThyA subfamily. {ECO:0000255|HAMAP-Rule:MF_01686}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98502.1; -; Genomic_DNA. DR PIR; G64363; G64363. DR ProteinModelPortal; Q57931; -. DR STRING; 243232.MJ_0511; -. DR EnsemblBacteria; AAB98502; AAB98502; MJ_0511. DR KEGG; mja:MJ_0511; -. DR eggNOG; arCOG03214; Archaea. DR eggNOG; COG0207; LUCA. DR InParanoid; Q57931; -. DR KO; K00560; -. DR OMA; HHSVSMH; -. DR PhylomeDB; Q57931; -. DR UniPathway; UPA00575; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004799; F:thymidylate synthase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0006231; P:dTMP biosynthetic process; IEA:UniProtKB-HAMAP. DR GO; GO:0006235; P:dTTP biosynthetic process; IEA:UniProtKB-UniPathway. DR Gene3D; 3.30.572.10; -; 1. DR HAMAP; MF_01686; Thymidy_synth_arch; 1. DR InterPro; IPR023451; Thymidate_synth/dCMP_Mease. DR InterPro; IPR014620; Thymidylate_synthase_arc. DR InterPro; IPR020940; Thymidylate_synthase_AS. DR Pfam; PF00303; Thymidylat_synt; 1. DR PIRSF; PIRSF036752; TSase_MJ051; 1. DR SUPFAM; SSF55831; SSF55831; 1. DR TIGRFAMs; TIGR03283; thy_syn_methano; 1. DR PROSITE; PS00091; THYMIDYLATE_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; KW Nucleotide biosynthesis; Reference proteome; Transferase. FT CHAIN 1 222 Putative thymidylate synthase. FT /FTId=PRO_0000141055. FT ACT_SITE 139 139 {ECO:0000255|HAMAP-Rule:MF_01686}. SQ SEQUENCE 222 AA; 25933 MW; 3BC5E8C38237CE92 CRC64; MLCIKKPSVA SAFNELIPKI LKDGEVVETE FEERTKEIRN TIIEITNPKL KKVPEKYPLG EKAVEEYTKN LLYGSKNVFS YDYHQRLFEY PYADEKINQI DYIIEKLNQQ KNSRRAVAIT WNPKIDIEVS RDERGSVPCL QLVQFLIRNG KLYQTVIFRS NDALLAFVSN AIGLITLGEY IAKKVGVGYG TYTHHAISMH IYVDRDFDYI KKYFPECLKY LW // ID UPPS_METJA Reviewed; 280 AA. AC Q58767; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Tritrans,polycis-undecaprenyl-diphosphate synthase (geranylgeranyl-diphosphate specific) {ECO:0000255|HAMAP-Rule:MF_01139}; DE EC=2.5.1.89 {ECO:0000255|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139}; DE Short=UDS {ECO:0000255|HAMAP-Rule:MF_01139}; DE AltName: Full=Undecaprenyl pyrophosphate synthase {ECO:0000255|HAMAP-Rule:MF_01139}; DE Short=UPP synthase {ECO:0000255|HAMAP-Rule:MF_01139}; GN Name=uppS {ECO:0000255|HAMAP-Rule:MF_01139}; OrderedLocusNames=MJ1372; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the sequential condensation of isopentenyl CC diphosphate (IPP) with geranylgeranyl diphosphate (GGPP) to yield CC (2Z,6Z,10Z,14Z,18Z,22Z,26Z,30E,34E,38E)-undecaprenyl diphosphate CC (tritrans,heptacis-UPP). It is probably the precursor of glycosyl CC carrier lipids. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- CATALYTIC ACTIVITY: Geranylgeranyl diphosphate + 7 isopentenyl CC diphosphate = 7 diphosphate + tritrans,heptacis-undecaprenyl CC diphosphate. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01139}; CC Note=Binds 2 magnesium ions per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01139}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01139}. CC -!- SIMILARITY: Belongs to the UPP synthase family. CC {ECO:0000255|HAMAP-Rule:MF_01139}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99380.1; -; Genomic_DNA. DR PIR; C64471; C64471. DR ProteinModelPortal; Q58767; -. DR STRING; 243232.MJ_1372; -. DR EnsemblBacteria; AAB99380; AAB99380; MJ_1372. DR KEGG; mja:MJ_1372; -. DR eggNOG; arCOG01532; Archaea. DR eggNOG; COG0020; LUCA. DR InParanoid; Q58767; -. DR KO; K15888; -. DR OMA; WAKLKNK; -. DR PhylomeDB; Q58767; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004659; F:prenyltransferase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.1180.10; -; 1. DR HAMAP; MF_01139; ISPT; 1. DR InterPro; IPR001441; UPP_synth-like. DR InterPro; IPR018520; UPP_synth-like_CS. DR PANTHER; PTHR10291; PTHR10291; 1. DR Pfam; PF01255; Prenyltransf; 1. DR SUPFAM; SSF64005; SSF64005; 1. DR TIGRFAMs; TIGR00055; uppS; 1. DR PROSITE; PS01066; UPP_SYNTHASE; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome; KW Transferase. FT CHAIN 1 280 Tritrans,polycis-undecaprenyl-diphosphate FT synthase (geranylgeranyl-diphosphate FT specific). FT /FTId=PRO_0000123731. FT REGION 58 61 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 102 104 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT REGION 235 237 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT ACT_SITE 57 57 {ECO:0000255|HAMAP-Rule:MF_01139}. FT ACT_SITE 105 105 Proton acceptor. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 57 57 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT METAL 248 248 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 70 70 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 74 74 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 106 106 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 108 108 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. FT BINDING 229 229 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_01139}. SQ SEQUENCE 280 AA; 33286 MW; FCB6C9FF5C65CC76 CRC64; MGILGKIKNK LKSIGKRVII DFYRFLDNSG VLKIYEKILE EAIDKDNLPK HVAIIMDGNR RAAEIYGKDR YYGHYLGAEK VREVLRWARD LGINVVTLYA FSTENFRRPK EEVDKLMELF EKKFYEIADD EEIHRYEVRV RAIGRINLLP KNVQKAIKYA EERTKNYNKF FVNIAIAYGG QQEIIDAVKK IAEKVKRGEI EPEDIDKELI DKHLYTANLP FPNPDLIIRT SGEERISNFL IWQSSYSELY FCDIYWPLFR RVDFLRAVRD YQRRQRRFGK // ID VAPB2_METJA Reviewed; 64 AA. AC Q58385; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 09-DEC-2015, entry version 69. DE RecName: Full=Putative antitoxin MJ0975; GN Name=vapB2; OrderedLocusNames=MJ0975; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. Its cognate toxin is VapC2 (Potential). CC {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0165 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98981.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98981.1; ALT_INIT; Genomic_DNA. DR PIR; G64421; G64421. DR ProteinModelPortal; Q58385; -. DR STRING; 243232.MJ_0975; -. DR EnsemblBacteria; AAB98981; AAB98981; MJ_0975. DR KEGG; mja:MJ_0975; -. DR InParanoid; Q58385; -. DR OMA; CEVEIKI; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 4.10.1150.10; -; 1. DR InterPro; IPR024069; AF2212-like_dom. DR InterPro; IPR008203; UPF0165. DR Pfam; PF01954; DUF104; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 64 Putative antitoxin MJ0975. FT /FTId=PRO_0000156858. SQ SEQUENCE 64 AA; 7214 MW; C10D5F4CA7C7094F CRC64; MEIVVDAIYE KGVLKLKKSI NLPEGCEVEI KIIPKKISEK TFGILKLSDK EIKEILEEIE NGGE // ID VAPB3_METJA Reviewed; 77 AA. AC Q58522; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Putative antitoxin VapB3 {ECO:0000255|HAMAP-Rule:MF_00794}; GN Name=vapB3; OrderedLocusNames=MJ1122; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. Its cognate toxin is VapC3 (Potential). CC {ECO:0000255|HAMAP-Rule:MF_00794}. CC -!- SIMILARITY: Belongs to the UPF0330 family. {ECO:0000255|HAMAP- CC Rule:MF_00794}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99124.1; -; Genomic_DNA. DR PIR; A64440; A64440. DR STRING; 243232.MJ_1122; -. DR EnsemblBacteria; AAB99124; AAB99124; MJ_1122. DR KEGG; mja:MJ_1122; -. DR eggNOG; arCOG02681; Archaea. DR eggNOG; COG1753; LUCA. DR InParanoid; Q58522; -. DR OMA; TIMIRDE; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00794; UPF0330; 1. DR InterPro; IPR003847; Put_antitoxin. DR Pfam; PF02697; DUF217; 1. DR ProDom; PD188822; DUF217; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 77 Putative antitoxin VapB3. FT /FTId=PRO_0000157108. SQ SEQUENCE 77 AA; 9135 MW; 461C4E194C235556 CRC64; MINMATITID DDVYKELLKL KGRKSVSEFI KELLEERKRK NLDVFMIAFG SRSEEDVEKL KKELKEAEKW MQSLIQV // ID VAPB4_METJA Reviewed; 57 AA. AC P0CW38; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 1. DT 11-NOV-2015, entry version 13. DE RecName: Full=Putative antitoxin VapB4; GN Name=vapB4; OrderedLocusNames=MJ1319.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, AND POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. Its cognate toxin is VapC4 (Potential). CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR STRING; 243232.MJ_1321; -. DR eggNOG; arCOG03890; Archaea. DR eggNOG; COG1431; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR003165; Piwi. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF02171; Piwi; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Putative antitoxin VapB4. FT /FTId=PRO_0000408088. SQ SEQUENCE 57 AA; 6797 MW; 4CD6D05CE6D4950A CRC64; MQLLYDLTKM NYSALYGEGR YLRIPAPIHY ADKFVKALGK NWKIDEELLK HGFLYFI // ID VAPB5_METJA Reviewed; 107 AA. AC P0CW39; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 9. DE RecName: Full=Putative antitoxin VapB5; GN Name=vapB5; OrderedLocusNames=MJ1473.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, AND POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. Its cognate toxin is VapC5 (Potential). CC {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 107 Putative antitoxin VapB5. FT /FTId=PRO_0000408089. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. SQ SEQUENCE 107 AA; 11649 MW; 7A18906E90BFAC8E CRC64; MQGPVIIPLI STLGLSFLAI LLAYKISFSV IGFINSTLPT TLFPSKPYML FVKISTISPL TCPSLIILTP ALTWSLTALS MAYLYSSYKP NTFFTLSKNV SSFLTTG // ID VAPC1_METJA Reviewed; 136 AA. AC Q58324; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Ribonuclease VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Putative toxin VapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC1 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=MJ0914; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION, AND POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. Its cognate antitoxin is VapB1 (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98919.1; -; Genomic_DNA. DR PIR; B64414; B64414. DR ProteinModelPortal; Q58324; -. DR STRING; 243232.MJ_0914; -. DR EnsemblBacteria; AAB98919; AAB98919; MJ_0914. DR KEGG; mja:MJ_0914; -. DR eggNOG; arCOG02219; Archaea. DR eggNOG; COG1487; LUCA. DR InParanoid; Q58324; -. DR KO; K07062; -. DR OMA; MPLWTRN; -. DR PhylomeDB; Q58324; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 136 Ribonuclease VapC1. FT /FTId=PRO_0000107102. FT DOMAIN 18 129 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT COMPBIAS 2 17 Lys-rich. FT METAL 21 21 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 101 101 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 136 AA; 16210 MW; 0620F9DFB7831918 CRC64; MKILKKLKKK LEKEESKILV DTSVLIDYFK KRRLEELGGE AISIITAVEF IRGISEHKQE QVLNIFKELF EIVYIDEEII IPFSKIYRQL KKRGMLIDDA DLYIACTAII KNYPLWTKNK KHFERLKEFG LKIYDK // ID VATF_METJA Reviewed; 98 AA. AC Q57671; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 99. DE RecName: Full=V-type ATP synthase subunit F; DE AltName: Full=V-ATPase subunit F; GN Name=atpF; OrderedLocusNames=MJ0218; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the V-ATPase F subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98201.1; -; Genomic_DNA. DR PIR; C64327; C64327. DR ProteinModelPortal; Q57671; -. DR STRING; 243232.MJ_0218; -. DR EnsemblBacteria; AAB98201; AAB98201; MJ_0218. DR KEGG; mja:MJ_0218; -. DR eggNOG; arCOG04102; Archaea. DR eggNOG; COG1436; LUCA. DR InParanoid; Q57671; -. DR KO; K02122; -. DR OMA; QIPDKFG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0033180; C:proton-transporting V-type ATPase, V1 domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0042625; F:ATPase coupled ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 3.40.50.10580; -; 1. DR HAMAP; MF_00312; ATP_synth_F_arch; 1. DR InterPro; IPR008218; ATPase_V1-cplx_f_g_su. DR InterPro; IPR022944; ATPase_V1-cplx_fsu_bac/arc. DR InterPro; IPR005772; ATPase_V1-cplx_fsu_euk. DR PANTHER; PTHR13861; PTHR13861; 1. DR Pfam; PF01990; ATP-synt_F; 1. DR SUPFAM; SSF159468; SSF159468; 1. PE 3: Inferred from homology; KW ATP synthesis; Complete proteome; Hydrogen ion transport; KW Ion transport; Reference proteome; Transport. FT CHAIN 1 98 V-type ATP synthase subunit F. FT /FTId=PRO_0000144818. SQ SEQUENCE 98 AA; 10941 MW; 5D8680EFEB8FA08F CRC64; MKVGVVGDRE TAIGFRLAGL TDVYEVKNDE EAVKAINELA NNENIAFIII TERIAESIKD KLKNINKVIV EIPDKHGKLE RIDPVKELIR KAIGVSMK // ID VHUG_METJA Reviewed; 288 AA. AC Q58591; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=F420-non-reducing hydrogenase vhu subunit G; DE EC=1.12.99.-; GN Name=vhuG; OrderedLocusNames=MJ1191; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBUNIT: The F420-non-reducing hydrogenase vhu is composed of four CC subunits; VhuA, VhuD, VhuG and VhuU. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase small CC subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99193.1; -; Genomic_DNA. DR PIR; F64448; F64448. DR ProteinModelPortal; Q58591; -. DR STRING; 243232.MJ_1191; -. DR EnsemblBacteria; AAB99193; AAB99193; MJ_1191. DR KEGG; mja:MJ_1191; -. DR eggNOG; arCOG02472; Archaea. DR eggNOG; COG1941; LUCA. DR InParanoid; Q58591; -. DR KO; K14128; -. DR OMA; FTCCEGC; -. DR PhylomeDB; Q58591; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR Pfam; PF01058; Oxidored_q6; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 288 F420-non-reducing hydrogenase vhu subunit FT G. FT /FTId=PRO_0000204361. SQ SEQUENCE 288 AA; 31438 MW; 82F598BBD9B068B3 CRC64; MITLAVKVGM IQLCGCSGCH ISLLDLHDKL LEVLPNLEIV YAPIIADPKE IPEGIDVFLV EGGIRNEHDE HLIHEIREKS KIVIAWGTCA AYGGIPGLGN LYKKEELLNY VYSTDSTENK GEIPSEEIPP LEEYVKPIKD FIKVDYTIPG CPPTPKMIAD AIIALLNGEE PKLPTKIVCD ECPRKKENVF PETFKRTHEG RPDPERCLFE QGYTCLGFAT RAGCGAKCPS AGVPCRGCFG KTDKSLDLGA NAANVLANAG EAALEIPDKV ALLNRFTLPD ALINRKAK // ID VAPC3_METJA Reviewed; 94 AA. AC Q58521; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribonuclease VapC3; DE Short=RNase VapC3; DE EC=3.1.-.-; DE AltName: Full=Putative toxin VapC3; GN Name=vapC3; OrderedLocusNames=MJ1121; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. Its cognate antitoxin is VapB3 (By similarity). CC {ECO:0000250}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99123.1; -; Genomic_DNA. DR PIR; H64439; H64439. DR ProteinModelPortal; Q58521; -. DR STRING; 243232.MJ_1121; -. DR EnsemblBacteria; AAB99123; AAB99123; MJ_1121. DR KEGG; mja:MJ_1121; -. DR eggNOG; arCOG02219; Archaea. DR eggNOG; COG1487; LUCA. DR InParanoid; Q58521; -. DR KO; K07062; -. DR OMA; CKITSIT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR029060; PIN_domain-like. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 94 Ribonuclease VapC3. FT /FTId=PRO_0000107176. FT COMPBIAS 63 80 Lys-rich. FT METAL 6 6 Magnesium. {ECO:0000255}. SQ SEQUENCE 94 AA; 10719 MW; BBA60946D299EFB4 CRC64; MDAVIDTSVI IEIFRGNKDT LYQICDYNCK ITSITVFELY CGNLKENEMI MIDSLPKLNF DDKSSKIAGN IFKKLKKEGK IPSVKDLLIA SIFY // ID VHUU_METJA Reviewed; 50 AA. AC P81335; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 24-JUN-2015, entry version 72. DE RecName: Full=F420-non-reducing hydrogenase vhu subunit U; DE EC=1.12.99.-; DE Flags: Precursor; GN Name=vhuU; OrderedLocusNames=MJ1192.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-27. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305}; CC -!- SUBUNIT: The F420-non-reducing hydrogenase vhu is composed of four CC subunits; VhuA, VhuD, VhuG and VhuU. {ECO:0000250}. CC -!- MISCELLANEOUS: The large subunit of Vhu is split into VhuA and CC VhuU. Each contributes two ligands to the [NiFeSe] center. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large CC subunit family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99197.1; Type=Erroneous termination; Positions=27; Note=Translated as Sec.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99197.1; ALT_SEQ; Genomic_DNA. DR EnsemblBacteria; AAB99197; AAB99197; MJ_1192.1. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 1.10.645.10; -; 1. DR InterPro; IPR029014; NiFe_Hase-like. DR SUPFAM; SSF56762; SSF56762; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Nickel; Oxidoreductase; KW Reference proteome; Selenocysteine. FT CHAIN 1 33 F420-non-reducing hydrogenase vhu subunit FT U. FT /FTId=PRO_0000013409. FT PROPEP 34 50 Removed in mature form. {ECO:0000250}. FT /FTId=PRO_0000013410. FT METAL 27 27 Nickel. {ECO:0000255}. FT METAL 30 30 Nickel. {ECO:0000255}. FT NON_STD 27 27 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 50 AA; 5726 MW; A0BF6051D99602A0 CRC64; MAEKSTVKVD EVKLNLIEMV LRAYDPUYSC AAHIIVKDEK GNKIIEVIKE // ID VATC_METJA Reviewed; 381 AA. AC Q57672; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 11-NOV-2015, entry version 96. DE RecName: Full=V-type ATP synthase subunit C; DE AltName: Full=V-ATPase subunit C; GN Name=atpC; OrderedLocusNames=MJ0219; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the V-ATPase V0D/AC39 subunit family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98202.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98202.1; ALT_INIT; Genomic_DNA. DR PIR; D64327; D64327. DR ProteinModelPortal; Q57672; -. DR STRING; 243232.MJ_0219; -. DR EnsemblBacteria; AAB98202; AAB98202; MJ_0219. DR KEGG; mja:MJ_0219; -. DR eggNOG; arCOG02459; Archaea. DR eggNOG; COG1527; LUCA. DR InParanoid; Q57672; -. DR KO; K02119; -. DR OMA; PFGVGPI; -. DR PhylomeDB; Q57672; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00314; ATP_synth_C_arch; 1. DR InterPro; IPR014272; ATPase_V0-cplx_c_su. DR InterPro; IPR002843; ATPase_V0-cplx_csu/dsu. DR Pfam; PF01992; vATP-synt_AC39; 1. DR SUPFAM; SSF103486; SSF103486; 1. DR TIGRFAMs; TIGR02923; AhaC; 1. PE 3: Inferred from homology; KW ATP synthesis; Complete proteome; Hydrogen ion transport; KW Ion transport; Reference proteome; Transport. FT CHAIN 1 381 V-type ATP synthase subunit C. FT /FTId=PRO_0000119366. SQ SEQUENCE 381 AA; 42777 MW; D0D603481686D362 CRC64; MTYFDNPLTL LIVVATIIIV LIVIVWITKM VIDLAPYAYV NARIRSKEAK LFDDAKLNEL IESGSLEELV GLLEDTDYGQ YVIEVMNELK DPVAVEKALD MYLADLYGLI YRISPDSAKK VLKVFAKKFD IKNIKTLIRA KFVGLSAEET YALLIPLGNI PVEKLKELAE VKTVEEVVRG LDGTEYFKIL QEELSNYDQT SNIIGFELAL DKYYLESLRK TIMTEGKEED IFREFVGTII DVENLKVILK GKADGLSAEE LSKYVTLTGY ELADWKLKDL MSAGGIEGVL SGLEGTSYAE VLAEAMEEYE KTKSIYAFEK ALDKFVLEKG KKLSTRKPFG VGPIIGLIVS KELEVKNLKA IIKGKIENLK PEEIRSLLIS L // ID VAPB1_METJA Reviewed; 64 AA. AC P0CW37; DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot. DT 03-MAY-2011, sequence version 1. DT 07-JAN-2015, entry version 6. DE RecName: Full=Putative antitoxin VapB1; GN Name=vapB1; OrderedLocusNames=MJ0913.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. Its cognate toxin is VapC1 (Potential). CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 64 Putative antitoxin VapB1. FT /FTId=PRO_0000408087. SQ SEQUENCE 64 AA; 7775 MW; 6E1AF77F98D8FCF1 CRC64; MISAKSKTKR ITITFEIPED IDAKKFKDDV KRYVRYKLLA NKLYELLEGE NIEEIEEEIR KRRE // ID VATA_METJA Reviewed; 587 AA. AC Q57670; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 24-JAN-2001, sequence version 2. DT 11-MAY-2016, entry version 107. DE RecName: Full=V-type ATP synthase alpha chain; DE EC=3.6.3.14; DE AltName: Full=V-ATPase subunit A; GN Name=atpA; OrderedLocusNames=MJ0217; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The archaeal alpha chain is a CC catalytic subunit (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP + H(2)O + H(+)(In) = ADP + phosphate + CC H(+)(Out). CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98200.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98200.1; ALT_INIT; Genomic_DNA. DR PIR; B64327; B64327. DR ProteinModelPortal; Q57670; -. DR SMR; Q57670; 60-561. DR STRING; 243232.MJ_0217; -. DR PRIDE; Q57670; -. DR EnsemblBacteria; AAB98200; AAB98200; MJ_0217. DR KEGG; mja:MJ_0217; -. DR eggNOG; arCOG00868; Archaea. DR eggNOG; COG1155; LUCA. DR InParanoid; Q57670; -. DR KO; K02117; -. DR OMA; DARMNDV; -. DR PhylomeDB; Q57670; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1140.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00309; ATP_synth_A_arch; 1. DR InterPro; IPR031686; ATP-synt_a_Xtn. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR005726; ATPase_asu_arc. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR024034; ATPase_F1_bsu/V1_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022878; V-ATPase_asu. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR Pfam; PF16886; ATP-synt_ab_Xtn; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF50615; SSF50615; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01043; ATP_syn_A_arch; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; ATP-binding; Complete proteome; Hydrogen ion transport; KW Hydrolase; Ion transport; Nucleotide-binding; Reference proteome; KW Transport. FT CHAIN 1 587 V-type ATP synthase alpha chain. FT /FTId=PRO_0000144599. FT NP_BIND 234 241 ATP. {ECO:0000255}. SQ SEQUENCE 587 AA; 65557 MW; 26BDD64E6D7FEEC5 CRC64; MPVVGKIIKI AGPVVVAEGM KGAQMYEVVK VGEEKLTGEI IQLHDDKAVI QVYEETSGIK PGEPVVGTGA PLSVELGPGM LRAMYDGIQR PLTAIEEKTG SIFIPRGVDV PALPRDIKWE FKPVVNEGDY VEEGDIIGTV DETPSIVHKI LVPIGVKGKI VEIKEGKFTV EETVAVVETE NGERKEITMM QKWPVRKPRP YKEKLPPEIP LITGQRVEDT FFTLAKGGTA AIPGPFGSGK TVTQHQLAKW SDADVVVYIG CGERGNEMTE VIEEFPHLED IRTGNKLMDR TVLIANTSNM PVAAREASVY TGITIAEYFR DMGYGVLLTA DSTSRWAEAM REISGRLEEM PGEEGYPAYL ASRLAQFYER AGRVITLGKD NRQGFVCIVG AVSPPGGDFS EPVTSNTLRI VKVFWALDAN LARRRHFPAI NWLQSYSLYI DDVTEWWNTN TGPDWRQLRD EAMSLLQKEA ELQEIVQLVG PDALPDRERV ILEVARMLRE DFLQQDAFDE VDTYCPPMKQ YLMLKIIMTF YQEALKAVER GVEPAKILGV SVKQDIARMK YIPHDEFINV KSKEIMEKIK NELGSLN // ID VATE_METJA Reviewed; 206 AA. AC Q57673; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=V-type ATP synthase subunit E; DE AltName: Full=V-ATPase subunit E; GN Name=atpE; OrderedLocusNames=MJ0220; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the V-ATPase E subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98203.1; -; Genomic_DNA. DR PIR; E64327; E64327. DR PDB; 2KK7; NMR; -; A=2-50. DR PDB; 3LG8; X-ray; 4.10 A; A/B=101-206. DR PDBsum; 2KK7; -. DR PDBsum; 3LG8; -. DR ProteinModelPortal; Q57673; -. DR STRING; 243232.MJ_0220; -. DR EnsemblBacteria; AAB98203; AAB98203; MJ_0220. DR KEGG; mja:MJ_0220; -. DR eggNOG; arCOG00869; Archaea. DR eggNOG; COG1390; LUCA. DR InParanoid; Q57673; -. DR KO; K02121; -. DR OMA; WALEKEM; -. DR EvolutionaryTrace; Q57673; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IEA:InterPro. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.20.5.620; -; 1. DR HAMAP; MF_00311; ATP_synth_E_arch; 1. DR InterPro; IPR028987; ATPase_B-like_membr. DR InterPro; IPR002842; ATPase_V1/A1-cplx_esu. DR Pfam; PF01991; vATP-synt_E; 1. DR SUPFAM; SSF81573; SSF81573; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP synthesis; Complete proteome; KW Hydrogen ion transport; Ion transport; Reference proteome; Transport. FT CHAIN 1 206 V-type ATP synthase subunit E. FT /FTId=PRO_0000117316. FT HELIX 6 45 {ECO:0000244|PDB:2KK7}. SQ SEQUENCE 206 AA; 23137 MW; 5787427812D715A6 CRC64; MKLMGVDKIK SKILDDAKAE ANKIISEAEA EKAKILEKAK EEAEKRKAEI LKKGEKEAEM TKSRIISEAK LEAKKKLLEA KEEIIEMAIN KLKEELVKLP EQPEYKDKLI KLIKDGAISL GGGELIVRLN KRDMELIDDS TLWNLEKEVE NATKKVTVLK KGEPVDIAGG CIIETADGLK SLDNSLEAIF NRNLNVIRAR ITEKLF // ID VATI_METJA Reviewed; 695 AA. AC Q57675; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 100. DE RecName: Full=V-type ATP synthase subunit I; DE AltName: Full=V-ATPase subunit I; GN Name=atpI; OrderedLocusNames=MJ0222; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the V-ATPase 116 kDa subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98208.1; -; Genomic_DNA. DR PIR; G64327; G64327. DR ProteinModelPortal; Q57675; -. DR STRING; 243232.MJ_0222; -. DR EnsemblBacteria; AAB98208; AAB98208; MJ_0222. DR KEGG; mja:MJ_0222; -. DR eggNOG; arCOG04138; Archaea. DR eggNOG; COG1269; LUCA. DR InParanoid; Q57675; -. DR KO; K02123; -. DR OMA; EFFGTFY; -. DR PhylomeDB; Q57675; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0033179; C:proton-transporting V-type ATPase, V0 domain; IEA:InterPro. DR GO; GO:0051117; F:ATPase binding; IBA:GO_Central. DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IBA:GO_Central. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0015986; P:ATP synthesis coupled proton transport; IBA:GO_Central. DR GO; GO:0007035; P:vacuolar acidification; IBA:GO_Central. DR InterPro; IPR002490; V-ATPase_116kDa_su. DR PANTHER; PTHR11629; PTHR11629; 1. DR Pfam; PF01496; V_ATPase_I; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrogen ion transport; KW Ion transport; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix; Transport. FT CHAIN 1 695 V-type ATP synthase subunit I. FT /FTId=PRO_0000119229. FT TRANSMEM 392 412 Helical. {ECO:0000255}. FT TRANSMEM 425 445 Helical. {ECO:0000255}. FT TRANSMEM 497 517 Helical. {ECO:0000255}. FT TRANSMEM 534 554 Helical. {ECO:0000255}. FT TRANSMEM 556 576 Helical. {ECO:0000255}. FT TRANSMEM 605 625 Helical. {ECO:0000255}. FT TRANSMEM 627 647 Helical. {ECO:0000255}. SQ SEQUENCE 695 AA; 76954 MW; F03E5CEBEE29D53D CRC64; MILVRPVRMK KLKAVILDEK IDNVVRSLHE EGIVELCDLS EKLEDLEWKT LLSPSSSADY VRNVTSLMIK AGRILDMFSS VSQKETSIKD ILNPKPVEKK KVSFNSYQEV IDYAEKVLNE ISKEVDGPAE RLSELDNKKS KLLQLKEQIS YLKGLEFDLK YLGSGEYVFI GAGSVPKEKL GELKAELDKV ADGYIGIFSG SEFEKDKKIR VPIVFVTLKE KLENVLSEIR KFEFERYDIS DVEGTPSEAL SKIESELKAI ESERNSLIEK LKALAQKWEK ELLAVYELLS IEKARGDAYS QFGKTDRTYY IEAWVPARDA EKAKSLIENS ADGFAFVEIT EPDEPEEKIP VLLDNPKVIK PFEMLTEMYA LPKYNEVDPT LLLVPGFLLF YGIMLTDAVY GLLLTIIGLF IWKKIGKVSE GANKLGYILT LAGISTVIMG IITGGYLGDF TYEFFGFDVT KTPLALVNPL GESYYINNNN PLFTLGSISV TNGPMAILVF SIFVGLIHLL IGLFVGFKEN VKRGNMGDAF INQGVWILLI LSIFVGIGLM FAGANTMIAG GIIGIFVVLA ILASMYKGYK SGGVMEAILG AMDVTGFLGN VLSYARLLAL CLATGGLAMA VNIMAKLVGE SIPVIGIIVA IIILLVGHTF NFVMNGLGAF IHSLRLHYVE FFSQFYEGGG KKFSPFKANR EYTTA // ID VHUB_METJA Reviewed; 394 AA. AC Q58593; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Polyferredoxin protein VhuB; GN Name=vhuB; OrderedLocusNames=MJ1193; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 10 [4Fe-4S] clusters. {ECO:0000305}; CC -!- SIMILARITY: Contains 10 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99195.1; -; Genomic_DNA. DR PIR; H64448; H64448. DR ProteinModelPortal; Q58593; -. DR STRING; 243232.MJ_1193; -. DR EnsemblBacteria; AAB99195; AAB99195; MJ_1193. DR KEGG; mja:MJ_1193; -. DR eggNOG; arCOG02181; Archaea. DR eggNOG; COG1145; LUCA. DR InParanoid; Q58593; -. DR OMA; ECIGCEK; -. DR PhylomeDB; Q58593; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF13237; Fer4_10; 1. DR Pfam; PF12800; Fer4_4; 1. DR Pfam; PF12838; Fer4_7; 3. DR PROSITE; PS00198; 4FE4S_FER_1; 10. DR PROSITE; PS51379; 4FE4S_FER_2; 10. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 394 Polyferredoxin protein VhuB. FT /FTId=PRO_0000159146. FT DOMAIN 4 33 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 26 56 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 64 93 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 92 121 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 133 162 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 162 191 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 201 230 4Fe-4S ferredoxin-type 7. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 231 260 4Fe-4S ferredoxin-type 8. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 292 326 4Fe-4S ferredoxin-type 9. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 334 363 4Fe-4S ferredoxin-type 10. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 13 13 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 16 16 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 19 19 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 23 23 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 36 36 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 39 39 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 42 42 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 46 46 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 73 73 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 76 76 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 79 79 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 101 101 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 104 104 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 107 107 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 111 111 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 142 142 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 145 145 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 148 148 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 152 152 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 171 171 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 174 174 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 177 177 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 181 181 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 210 210 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 213 213 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 216 216 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 220 220 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 240 240 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 243 243 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 246 246 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 250 250 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 306 306 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 309 309 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 312 312 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 316 316 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 343 343 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 346 346 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 349 349 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 353 353 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 394 AA; 43343 MW; 08C53D5F6C41D104 CRC64; MRLMSITIQK DACLVCYACQ AECPTKAIDI DSFKVCNLCM ECVKVCPTGA LVEEEIEVNG KKLKRVNYLA HKCEKCGQCA EACPIGIKKV DDDFPYSKGH CVLCQKCIDV CPIEIISLPG VIDKPKKEIK PPKEPIAVTD ACVGCGICVP ECPVNAITLE NNKAVIDKSK CIYCSICAQT CPWNAIFVAG KIPKKRRKEV KKFEVNAEKC IYCLKCVEVC PGDMIKVDEE NLIVIPPKSC PACKLCVNIC PVDALDLEVK LSSPHPITDE GLVIVEEDFE VLKKCASVCP TEAIVVDEEK KEVRMCIVCG ACTVACPTGA LKLGKIEHNG KEYNRIEFSP YLCDKCGKCV EVCPMKTLRL SRGKLPLKGY CVMCLLCLSV AEKEKKGKKV LELR // ID VHUD_METJA Reviewed; 134 AA. AC P81334; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 3. DT 11-NOV-2015, entry version 69. DE RecName: Full=F420-non-reducing hydrogenase vhu iron-sulfur subunit D; DE EC=1.12.99.-; GN Name=vhuD; OrderedLocusNames=MJ1190.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP PROBABLE SELENOCYSTEINE AT SEC-13 AND SEC-64. RX PubMed=9102456; DOI=10.1006/jmbi.1996.0812; RA Wilting R., Schorling S., Persson B.C., Boeck A.; RT "Selenoprotein synthesis in archaea: identification of an mRNA element RT of Methanococcus jannaschii probably directing selenocysteine RT insertion."; RL J. Mol. Biol. 266:637-641(1997). CC -!- COFACTOR: CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:49601; CC Evidence={ECO:0000250}; CC Note=Binds 1 [2Fe-2S] cluster. {ECO:0000250}; CC -!- SUBUNIT: The F420-non-reducing hydrogenase vhu is composed of four CC subunits; VhuA, VhuD, VhuG and VhuU. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the MvhD/VhuD family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99196.1; Type=Erroneous termination; Positions=13, 64; Note=Translated as Sec, Sec.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99196.1; ALT_SEQ; Genomic_DNA. DR STRING; 243232.MJ_1190a; -. DR EnsemblBacteria; AAB99196; AAB99196; MJ_1190.1. DR eggNOG; arCOG02475; Archaea. DR eggNOG; COG1908; LUCA. DR InParanoid; P81334; -. DR OMA; XGYGAAD; -. DR PhylomeDB; P81334; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0015948; P:methanogenesis; IEA:InterPro. DR InterPro; IPR003813; FlpD. DR Pfam; PF02662; FlpD; 1. PE 3: Inferred from homology; KW 2Fe-2S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; Selenocysteine; KW Transport. FT CHAIN 1 134 F420-non-reducing hydrogenase vhu iron- FT sulfur subunit D. FT /FTId=PRO_0000218278. FT NON_STD 13 13 Selenocysteine. {ECO:0000305}. FT NON_STD 64 64 Selenocysteine. {ECO:0000305}. SQ SEQUENCE 134 AA; 14710 MW; 45AB45DDF8A7C8C0 CRC64; MDPVIIAFCC YQUGYGAADL AGTSRMQYPA TVRIVRLPCT GKFDITYALR AFQKGADAVM VVGUKKGECA YETGNLKAEE RVRFAKQLLD ELGIGGDRID MFFMSAAEAD KFVSAVNEMT ARVEKLGPNP LKAQ // ID VAPC2_METJA Reviewed; 149 AA. AC Q58384; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Ribonuclease VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Putative toxin VapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC2 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=MJ0974; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. Its cognate antitoxin is VapB2 (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98979.1; -; Genomic_DNA. DR PIR; F64421; F64421. DR ProteinModelPortal; Q58384; -. DR STRING; 243232.MJ_0974; -. DR EnsemblBacteria; AAB98979; AAB98979; MJ_0974. DR KEGG; mja:MJ_0974; -. DR eggNOG; arCOG00710; Archaea. DR eggNOG; COG1848; LUCA. DR InParanoid; Q58384; -. DR KO; K07064; -. DR OMA; RIPWLKV; -. DR PhylomeDB; Q58384; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 149 Ribonuclease VapC2. FT /FTId=PRO_0000107125. FT DOMAIN 11 149 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 14 14 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 116 116 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 149 AA; 17733 MW; 58C7AF9A12FC27C2 CRC64; MRRLKMEENK IFFDSNILIY HLCGKVEAKK LIEKVENKEI CGFINPIVIS EVLFFYIRAT TNKRHYDIKK HPEILKSLDL DIVFELFSIF QILDLNSEIV KISREIIKKY CLLPNDALIC STCKFYKINK ICSFDDDFKR VDFLEIIEI // ID VATB_METJA Reviewed; 465 AA. AC Q57669; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 105. DE RecName: Full=V-type ATP synthase beta chain; DE AltName: Full=V-ATPase subunit B; GN Name=atpB; OrderedLocusNames=MJ0216; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. The archaeal beta chain is a CC regulatory subunit. CC -!- SIMILARITY: Belongs to the ATPase alpha/beta chains family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98199.1; -; Genomic_DNA. DR PIR; A64327; A64327. DR ProteinModelPortal; Q57669; -. DR SMR; Q57669; 18-462. DR STRING; 243232.MJ_0216; -. DR PRIDE; Q57669; -. DR EnsemblBacteria; AAB98199; AAB98199; MJ_0216. DR KEGG; mja:MJ_0216; -. DR eggNOG; arCOG00865; Archaea. DR eggNOG; COG1156; LUCA. DR InParanoid; Q57669; -. DR KO; K02118; -. DR OMA; WRERRYL; -. DR PhylomeDB; Q57669; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0033178; C:proton-transporting two-sector ATPase complex, catalytic domain; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0015991; P:ATP hydrolysis coupled proton transport; IEA:InterPro. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.1140.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_00310; ATP_synth_B_arch; 1. DR InterPro; IPR020003; ATPase_a/bsu_AS. DR InterPro; IPR005724; ATPase_A1-cplx_bsu. DR InterPro; IPR000793; ATPase_F1/V1/A1-cplx_a/bsu_C. DR InterPro; IPR000194; ATPase_F1/V1/A1_a/bsu_nucl-bd. DR InterPro; IPR004100; ATPase_F1_a/bsu_N. DR InterPro; IPR024034; ATPase_F1_bsu/V1_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022879; V-ATPase_su_B/beta. DR Pfam; PF00006; ATP-synt_ab; 1. DR Pfam; PF02874; ATP-synt_ab_N; 1. DR PIRSF; PIRSF039114; V-ATPsynth_beta/V-ATPase_B; 1. DR SUPFAM; SSF47917; SSF47917; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01041; ATP_syn_B_arch; 1. DR PROSITE; PS00152; ATPASE_ALPHA_BETA; 1. PE 3: Inferred from homology; KW ATP synthesis; Complete proteome; Hydrogen ion transport; KW Ion transport; Reference proteome; Transport. FT CHAIN 1 465 V-type ATP synthase beta chain. FT /FTId=PRO_0000144656. SQ SEQUENCE 465 AA; 51375 MW; F18924CD83450AC7 CRC64; MATAASAIEY SSVKSIAGPL LIVEGVEGAA YGEIVEVICP DGEKRMGQVL EAREGLAVVQ VFEGTTGLST KDTRVRFTGR TAKIGVSMEM LGRIFNGAGK PIDGGPEIVP EKELDINGYP LNPVSRKVPS DFIQTGISTI DGMNTLVRGQ KLPIFSGSGL PHNQLAAQIA RQAKVRGEGE KFAVVFAAMG ITSEEANFFM EEFRKTGALE RAVVFINLAD DPAIERILTP RIALTVAEYL AYEKDMHVLV ILTDMTNYCE ALREISAARN EVPGRRGYPG YMYTDLATIY ERAGRVKGRT GTITQIPILT MPDDDITHPI PDLTGYITEG QIVLSRELHR KGIYPPVDVL PSLSRLAGNG QGPGKTREDH KKVVNQAYAA YAEGRSLRDL VAVVGEEALT DRDRAYLKFA DEFEDKFVRQ GKDEDRSIEE TLDLLWELLA ILPEEELKRV DRELIEKYHP KYRKK // ID VHUA_METJA Reviewed; 418 AA. AC Q58592; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=F420-non-reducing hydrogenase vhu subunit A; DE EC=1.12.99.-; GN Name=vhuA; OrderedLocusNames=MJ1192; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786; Evidence={ECO:0000305}; CC -!- SUBUNIT: The F420-non-reducing hydrogenase vhu is composed of four CC subunits; VhuA, VhuD, VhuG and VhuU. {ECO:0000250}. CC -!- MISCELLANEOUS: The large subunit of Vhu is split into VhuA and CC VhuU. Each contributes two ligands to the [NiFeSe] center. CC -!- SIMILARITY: Belongs to the [NiFe]/[NiFeSe] hydrogenase large CC subunit family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99194.1; -; Genomic_DNA. DR PIR; G64448; G64448. DR ProteinModelPortal; Q58592; -. DR STRING; 243232.MJ_1192m; -. DR EnsemblBacteria; AAB99194; AAB99194; MJ_1192. DR eggNOG; arCOG01549; Archaea. DR eggNOG; COG3259; LUCA. DR InParanoid; Q58592; -. DR OMA; HNVPTME; -. DR PhylomeDB; Q58592; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 1. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00374; NiFeSe_Hases; 2. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Nickel; Oxidoreductase; KW Reference proteome. FT CHAIN 1 418 F420-non-reducing hydrogenase vhu subunit FT A. FT /FTId=PRO_0000199730. FT METAL 61 61 Nickel. {ECO:0000255}. FT METAL 64 64 Nickel. {ECO:0000255}. SQ SEQUENCE 418 AA; 46652 MW; 0BF7333C53360FA4 CRC64; MGKIVIEPLS RLEGHGKVTI TLDENGKPKD VKLHITALRG FEQFVVGRPA EEVPRIVPRI CGICQTAHHL ASVKAIDAAW GVEIPEPAKK LRELMHIGNM IHSHALHFYF LAAPDFVLGP DADPAIRNIV GVIDKAPDVA KQAIALRKFG QKIVEAVGGK AIHPVTGIPG GQAKRLTEEE RDELLKDADQ MIEYAKNGVE LIKQLNEQYM EQIKTLGVID TYYLGLVKDG KHNFYDDTLR FLSPDGKEKV EFKPEEYLNY IGEYVVPYNY VKHPYYKKVG YPEGVYRVGP LAMLNVCDEM ETPLAEEYRK EFLEIFGFPA NQSLAYNHAR LIELVEACEK AKILLEDNDI TSDDIKADVE PKAGNGVGVV YAPRGVLIHN YETDENGIVV KANMIVATTH NVPTMEKAIQ QAAQVIFK // ID VAPC4_METJA Reviewed; 131 AA. AC Q58716; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Ribonuclease VapC4 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC4 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Putative toxin VapC4 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC4 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=MJ1320; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP POSSIBLE FUNCTION. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=15718296; DOI=10.1093/nar/gki201; RA Pandey D.P., Gerdes K.; RT "Toxin-antitoxin loci are highly abundant in free-living but lost from RT host-associated prokaryotes."; RL Nucleic Acids Res. 33:966-976(2005). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. Its cognate antitoxin is VapB4 (By similarity). CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99330.1; -; Genomic_DNA. DR PIR; G64464; G64464. DR ProteinModelPortal; Q58716; -. DR STRING; 243232.MJ_1320; -. DR EnsemblBacteria; AAB99330; AAB99330; MJ_1320. DR KEGG; mja:MJ_1320; -. DR eggNOG; arCOG04312; Archaea. DR eggNOG; COG1412; LUCA. DR InParanoid; Q58716; -. DR KO; K07158; -. DR OMA; DTNFLIY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0032040; C:small-subunit processome; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR006984; Fcf1/Utp23. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF04900; Fcf1; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Reference proteome; Toxin. FT CHAIN 1 131 Ribonuclease VapC4. FT /FTId=PRO_0000107274. FT DOMAIN 4 106 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 7 7 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 102 102 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 131 AA; 15452 MW; BD4589FBD5A56693 CRC64; MYKIVPDTNF LIYVFKHKIN FDYEIERALN TKFEIVILSP IKEELERLLK SRDLKGKEKL AVNLALAKIK NYKLVDYTAN YADEAILNYA KENENVIVAT NDKELKEKLM ENNIPVMVVR QKKYFEIFGM V // ID VAPC6_METJA Reviewed; 153 AA. AC Q60288; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Ribonuclease VapC6 {ECO:0000255|HAMAP-Rule:MF_00265}; DE Short=RNase VapC6 {ECO:0000255|HAMAP-Rule:MF_00265}; DE EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_00265}; DE AltName: Full=Putative toxin VapC6 {ECO:0000255|HAMAP-Rule:MF_00265}; GN Name=vapC6 {ECO:0000255|HAMAP-Rule:MF_00265}; GN OrderedLocusNames=MJECL30; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Toxic component of a toxin-antitoxin (TA) module. An CC RNase. {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00265}; CC -!- SIMILARITY: Belongs to the PINc/VapC protein family. CC {ECO:0000255|HAMAP-Rule:MF_00265}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000255|HAMAP- CC Rule:MF_00265}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37100.1; -; Genomic_DNA. DR PIR; E64513; E64513. DR ProteinModelPortal; Q60288; -. DR EnsemblBacteria; AAC37100; AAC37100; MJ_ECL30. DR KEGG; mja:MJECL30; -. DR HOGENOM; HOG000244866; -. DR InParanoid; Q60288; -. DR KO; K07064; -. DR OMA; IQKIATF; -. DR PhylomeDB; Q60288; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro. DR Gene3D; 3.40.50.1010; -; 1. DR HAMAP; MF_00265; VapC_Nob1; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR022907; VapC_family. DR Pfam; PF01850; PIN; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Magnesium; Metal-binding; Nuclease; KW Plasmid; Reference proteome; Toxin. FT CHAIN 1 153 Ribonuclease VapC6. FT /FTId=PRO_0000107515. FT DOMAIN 6 152 PINc. {ECO:0000255|HAMAP-Rule:MF_00265}. FT METAL 9 9 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. FT METAL 120 120 Magnesium. {ECO:0000255|HAMAP- FT Rule:MF_00265}. SQ SEQUENCE 153 AA; 17845 MW; BDD035D67F615755 CRC64; MSPSNVFIDS SVMVGLFIGD EKAHKLLSKL INDGFMLCIN PIVFSETMFK VTFHIALEDG IRGVYDLKKN LNRYSWVYEE VREKIDKMIK MNYLKILDTN WEVLKLAPEI GKKYNLLTND AIIIATCKYY RINKLATFDS DFEKVDFIEI IKE // ID VATD_METJA Reviewed; 216 AA. AC Q58032; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=V-type ATP synthase subunit D; DE AltName: Full=V-ATPase subunit D; GN Name=atpD; OrderedLocusNames=MJ0615; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Produces ATP from ADP in the presence of a proton CC gradient across the membrane. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the V-ATPase D subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98610.1; -; Genomic_DNA. DR PIR; G64376; G64376. DR ProteinModelPortal; Q58032; -. DR STRING; 243232.MJ_0615; -. DR EnsemblBacteria; AAB98610; AAB98610; MJ_0615. DR KEGG; mja:MJ_0615; -. DR eggNOG; arCOG04101; Archaea. DR eggNOG; COG1394; LUCA. DR InParanoid; Q58032; -. DR KO; K02120; -. DR OMA; YQDGVDT; -. DR PhylomeDB; Q58032; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IEA:UniProtKB-HAMAP. DR GO; GO:0042777; P:plasma membrane ATP synthesis coupled proton transport; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00271; ATP_synth_D_arch; 1. DR InterPro; IPR002699; V_ATPase_D. DR PANTHER; PTHR11671; PTHR11671; 1. DR Pfam; PF01813; ATP-synt_D; 1. DR TIGRFAMs; TIGR00309; V_ATPase_subD; 1. PE 3: Inferred from homology; KW ATP synthesis; Complete proteome; Hydrogen ion transport; KW Ion transport; Reference proteome; Transport. FT CHAIN 1 216 V-type ATP synthase subunit D. FT /FTId=PRO_0000144250. SQ SEQUENCE 216 AA; 24951 MW; DBF27A987C56913A CRC64; MQRVNPTRME LLKLKNKIKL AEKGHKLLKQ KRDALIMEFF QIIEQASDLR DKVEAKLAEA YKDLIMAQTV MGTLAVKEAA LAAKNDKLEV DMDTKNIMGV TVPTFEIYNV RRKVGERGYS PYGVSSKLDE AAKKFEEALE LITELAEIET SIKLLAEEII TTKRRVNALE YVIIPRLKSL KKYISMRLDE MERENFFRLK LIKSRIEKRE AEGETV // ID Y008_METJA Reviewed; 220 AA. AC Q60319; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0008; GN OrderedLocusNames=MJ0008; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97997.1; -; Genomic_DNA. DR PIR; H64300; H64300. DR ProteinModelPortal; Q60319; -. DR STRING; 243232.MJ_0008; -. DR EnsemblBacteria; AAB97997; AAB97997; MJ_0008. DR KEGG; mja:MJ_0008; -. DR eggNOG; arCOG01899; Archaea. DR eggNOG; COG1082; LUCA. DR OMA; YLTIHLH; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 220 Uncharacterized protein MJ0008. FT /FTId=PRO_0000106649. SQ SEQUENCE 220 AA; 25836 MW; 955DF4A0FAB71B88 CRC64; MFCGSMIAIC MRSKEGFLFN NKLMDWGLHY NPKIVKDNNI IGYHAPILDL DKKESIIILK NIIENIKGRD YLTIHLHNGK YGKINKETLI ENLSIVNEFA EKNGIKLCIE NLRKGFSSNP NNIIEIADEI NCYITFDVGH IPYNRRLEFL EICSDRVYNS HVYEIEVDGK HLPPKNLNNL KPILDRLLDI KCKMFLIELM DIKEVLRTER MLKDYLEMYR // ID Y014_METJA Reviewed; 213 AA. AC Q60329; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Uncharacterized protein MJ0014; GN OrderedLocusNames=MJ0014; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 resolvase/invertase-type recombinase CC catalytic domain. {ECO:0000255|PROSITE-ProRule:PRU01072}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97992.1; -; Genomic_DNA. DR PIR; F64301; F64301. DR PDB; 3LHK; X-ray; 2.20 A; A/B/C/D=63-213. DR PDBsum; 3LHK; -. DR ProteinModelPortal; Q60329; -. DR STRING; 243232.MJ_0014; -. DR EnsemblBacteria; AAB97992; AAB97992; MJ_0014. DR KEGG; mja:MJ_0014; -. DR eggNOG; arCOG03164; Archaea. DR eggNOG; COG2452; LUCA. DR InParanoid; Q60329; -. DR KO; K07450; -. DR OMA; RLMGIVR; -. DR PhylomeDB; Q60329; -. DR EvolutionaryTrace; Q60329; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR Gene3D; 3.40.50.1390; -; 1. DR InterPro; IPR009061; DNA-bd_dom_put. DR InterPro; IPR006119; Resolv_N. DR InterPro; IPR010093; SinI_DNA-bd. DR Pfam; PF00239; Resolvase; 1. DR SMART; SM00857; Resolvase; 1. DR SUPFAM; SSF46955; SSF46955; 1. DR SUPFAM; SSF53041; SSF53041; 1. DR TIGRFAMs; TIGR01764; excise; 1. DR PROSITE; PS51736; RECOMBINASES_3; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 213 Uncharacterized protein MJ0014. FT /FTId=PRO_0000106654. FT DOMAIN 63 213 Resolvase/invertase-type recombinase FT catalytic. {ECO:0000255|PROSITE- FT ProRule:PRU01072}. FT ACT_SITE 71 71 O-(5'-phospho-DNA)-serine intermediate. FT {ECO:0000255|PROSITE-ProRule:PRU01072}. FT STRAND 63 72 {ECO:0000244|PDB:3LHK}. FT HELIX 73 75 {ECO:0000244|PDB:3LHK}. FT HELIX 76 92 {ECO:0000244|PDB:3LHK}. FT STRAND 98 104 {ECO:0000244|PDB:3LHK}. FT HELIX 112 122 {ECO:0000244|PDB:3LHK}. FT STRAND 126 133 {ECO:0000244|PDB:3LHK}. FT HELIX 134 137 {ECO:0000244|PDB:3LHK}. FT HELIX 142 151 {ECO:0000244|PDB:3LHK}. FT STRAND 155 159 {ECO:0000244|PDB:3LHK}. FT HELIX 167 186 {ECO:0000244|PDB:3LHK}. FT HELIX 191 204 {ECO:0000244|PDB:3LHK}. SQ SEQUENCE 213 AA; 25041 MW; 7786C8202AA34898 CRC64; MMIMERHYTL KEASKILGVS IKTLQRWDKA GKIKCIRTLG GKRRVPESEI KRILGIKDKE QRKIIGYARV SFNAQKDDLE RQIQLIKSYA EENGWDIQIL KDIGSGLNEK RKNYKKLLKM VMNRKVEKVI IAYPDRLTRF GFETLKEFFK SYGTEIVIIN KKHKTPQEEL VEDLITIVSH FAGKLYGMHS HKYKKLTKTV KEIVREEDAK EKE // ID Y033_METJA Reviewed; 539 AA. AC Q60356; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 95. DE RecName: Full=Uncharacterized FAD-dependent oxidoreductase MJ0033; GN OrderedLocusNames=MJ0033; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the FAD-dependent oxidoreductase 2 family. CC FRD/SDH subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98014.1; -; Genomic_DNA. DR PIR; A64304; A64304. DR ProteinModelPortal; Q60356; -. DR STRING; 243232.MJ_0033; -. DR EnsemblBacteria; AAB98014; AAB98014; MJ_0033. DR KEGG; mja:MJ_0033; -. DR eggNOG; arCOG00571; Archaea. DR eggNOG; COG1053; LUCA. DR InParanoid; Q60356; -. DR KO; K18209; -. DR OMA; GKNHNSV; -. DR PhylomeDB; Q60356; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 1.20.58.100; -; 1. DR Gene3D; 3.50.50.60; -; 2. DR Gene3D; 3.90.700.10; -; 1. DR InterPro; IPR003953; FAD-binding_2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR015939; Fum_Rdtase/Succ_DH_flav-like_C. DR InterPro; IPR030664; SdhA/FrdA/AprA. DR InterPro; IPR027477; Succ_DH/fumarate_Rdtase_cat. DR Pfam; PF00890; FAD_binding_2; 1. DR Pfam; PF02910; Succ_DH_flav_C; 1. DR PIRSF; PIRSF000171; SDHA_APRA_LASPO; 1. DR SUPFAM; SSF46977; SSF46977; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR SUPFAM; SSF56425; SSF56425; 1. PE 3: Inferred from homology; KW Complete proteome; FAD; Flavoprotein; Oxidoreductase; KW Reference proteome. FT CHAIN 1 539 Uncharacterized FAD-dependent FT oxidoreductase MJ0033. FT /FTId=PRO_0000158670. FT NP_BIND 6 20 FAD. {ECO:0000255}. FT ACT_SITE 227 227 {ECO:0000250}. FT ACT_SITE 243 243 {ECO:0000250}. SQ SEQUENCE 539 AA; 60398 MW; 89FF7AE3D6268795 CRC64; MKTDILIIGG GGAAARAAIE CRDKNVIIAV KGLFGKSGCT VMAEGGYNAV FNPKDSFKKH FYDTVKGGGF INNPKLVEIL VKNAPKELLN LERFGALFDR TEDGFIAQRP FGGQSFNRTC YCGDRTGHEI MRGLMEYISK FERIKILEEV MAIKLIVKDN RCYGAIFLDL KTGNIFPIFA KATILATGGA GQLYPITSNP IQKTGDGFAI AYNEGAELID MEMVQFHPTG MVGTGILVTE AVRGEGGILY NKYKERFMVR YDKERMELST RDVVARAIYK EIQEGRGVNG GVYLDVSHLP NEVIEKKLET MLKQFLRVGI DIRKEPMIVS PTAHHFMGGL KINERCETNI IGLFACGEVT GGVHGANRLG GNALADTQVF GAIAGKSAKE FVENHDFNNI DAEEDVAKIL EEINSLKGDL NVYNLIEDLR KVMWDYVSII RNEDGLKKAL EKIDEIERNI DNVKVNGIID LQNYFELKNM VVVAKLVTKS ALYRKESRGA HYREDFPETK EEWRGNIIIK GKKMWFEKLD YSVFQNFLE // ID Y038_METJA Reviewed; 217 AA. AC Q60345; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0038; GN OrderedLocusNames=MJ0038; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98019.1; -; Genomic_DNA. DR PIR; F64304; F64304. DR ProteinModelPortal; Q60345; -. DR STRING; 243232.MJ_0038; -. DR EnsemblBacteria; AAB98019; AAB98019; MJ_0038. DR KEGG; mja:MJ_0038; -. DR eggNOG; arCOG04130; Archaea. DR eggNOG; COG1491; LUCA. DR InParanoid; Q60345; -. DR KO; K07572; -. DR OMA; PITNRLH; -. DR PhylomeDB; Q60345; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR007003; DUF655. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF04919; DUF655; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 217 Uncharacterized protein MJ0038. FT /FTId=PRO_0000106662. SQ SEQUENCE 217 AA; 26274 MW; 00C21A7773BD9813 CRC64; MVRGQYKKGN DERMRFPKKN KPQKFENYAW VLDYLPYGYP DKPDEPIVQG LGEYQFLLME MIPKPNVDIE LGERVYIGKG KRDKIDHVRR MIKYEQLTPT AKSELLYVVM EAVKIQEDRF VRFFNECPPI TTRLHTLELL PEIKKKYMWK IIEEREAKKF ESFKDFEERI GKNPVRIIAK RIEKELSDDK KDKYYLFVKW KKGIILNEDN MTFYLKE // ID Y045_METJA Reviewed; 221 AA. AC Q60353; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0045; GN OrderedLocusNames=MJ0045; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98025.1; -; Genomic_DNA. DR PIR; E64305; E64305. DR ProteinModelPortal; Q60353; -. DR STRING; 243232.MJ_0045; -. DR EnsemblBacteria; AAB98025; AAB98025; MJ_0045. DR KEGG; mja:MJ_0045; -. DR eggNOG; arCOG04855; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q60353; -. DR OMA; HFLFLYS; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 221 Uncharacterized protein MJ0045. FT /FTId=PRO_0000106667. SQ SEQUENCE 221 AA; 26679 MW; B9873BF0B1171336 CRC64; MRYLNLKDTV LLGRNFNEYV RMFNLNEDLL SNKILDVASG VSSFCAEGNK KGYNITSSDK IYNLKPEEIE EKCKKDLDFM EKHLRGMFKN NFNWNEFKTV DEWKKTRERT YKTFIEDYKT NRKRYIYTTY PKTNFKDDEF AISLVGHFLL LYDNILNYQF HKETIDELLR ISEEIRIFPI LNLRGEKSIF LDKILKEYKA RIEKTDYEFM KGGNKVLIIR R // ID Y073_METJA Reviewed; 93 AA. AC Q60379; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0073; GN OrderedLocusNames=MJ0073; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98055.1; -; Genomic_DNA. DR PIR; A64309; A64309. DR ProteinModelPortal; Q60379; -. DR STRING; 243232.MJ_0073; -. DR EnsemblBacteria; AAB98055; AAB98055; MJ_0073. DR KEGG; mja:MJ_0073; -. DR eggNOG; arCOG05114; Archaea. DR eggNOG; COG4087; LUCA. DR OMA; TYNIIVV; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR SUPFAM; SSF56784; SSF56784; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 93 Uncharacterized protein MJ0073. FT /FTId=PRO_0000106681. SQ SEQUENCE 93 AA; 10335 MW; 749F111B601BBD2F CRC64; MKVDREKYGS EKIAKLKILE ELKKENPNKK IIAIGNGNND ELLLKNADLG ICVIGDEGAW SKTILSSDIV VKDINDALDL LLNENRLKAT SRD // ID WECC_METJA Reviewed; 427 AA. AC Q57871; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=UDP-N-acetyl-D-mannosamine dehydrogenase; DE EC=1.1.1.336; DE AltName: Full=UDP-ManNAc 6-dehydrogenase; GN Name=wecC; OrderedLocusNames=MJ0428; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the four-electron oxidation of UDP-N-acetyl-D- CC mannosamine (UDP-ManNAc), reducing NAD(+) and releasing UDP-N- CC acetylmannosaminuronic acid (UDP-ManNAcA). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-mannosamine + 2 NAD(+) + CC H(2)O = UDP-N-acetyl-alpha-D-mannosaminuronate + 2 NADH. CC -!- SUBUNIT: Homotetramer. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98413.1; -; Genomic_DNA. DR PIR; D64353; D64353. DR ProteinModelPortal; Q57871; -. DR STRING; 243232.MJ_0428; -. DR EnsemblBacteria; AAB98413; AAB98413; MJ_0428. DR KEGG; mja:MJ_0428; -. DR eggNOG; arCOG00252; Archaea. DR eggNOG; COG0677; LUCA. DR InParanoid; Q57871; -. DR KO; K02472; -. DR OMA; SMLAIQG; -. DR PhylomeDB; Q57871; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IBA:GO_Central. DR GO; GO:0089714; F:UDP-N-acetyl-D-mannosamine dehydrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.720; -; 2. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR017476; UDP-Glc/GDP-Man. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR InterPro; IPR028359; UDP_ManNAc/GlcNAc_DH. DR PANTHER; PTHR11374; PTHR11374; 1. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR PIRSF; PIRSF500136; UDP_ManNAc_DH; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52413; SSF52413; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. PE 3: Inferred from homology; KW Complete proteome; NAD; Oxidoreductase; Reference proteome. FT CHAIN 1 427 UDP-N-acetyl-D-mannosamine dehydrogenase. FT /FTId=PRO_0000074083. FT NP_BIND 12 29 NAD. {ECO:0000255}. FT ACT_SITE 263 263 {ECO:0000250}. SQ SEQUENCE 427 AA; 47749 MW; 0F0EAAFC17F8BB76 CRC64; MTKVEKNGIG KRICVIGLGY IGLPTASMLA IQGFDVIGVD INEKRVKEIK ELSFKTTEKD LMTLVKGAIN SGNLKVQTKP EKADVFIICV PTPCIECDGE KKCDLTYLNK AIESIKPYLE NGNLIIIEST IPPGTTDDIY KKLSKDKKIY VAHCPERVLP GSILKELVEN DRVIGGVDEK SAEMAKEIYE TFVTGKIYLT DAKTAEMVKL MENTYRDVNI ALANEFAKIA EEIGINVWEA IELANKHPRV NILKPGPGVG GHCISIDPWF IVEKSKNAKL IRTARELNDS MPLFVVEKIK KIIKKDIGKV AIFGVTYKGN VDDTRESPAE KVVSKLIDEG FEVKCYDKYA RDFIYPLNSL DEAVEGADII VILAEHDEYK NFDKEDIKNI ASKVKNKIIL DTKNILNREL WEKEGFKVYV LGDGKNA // ID Y016_METJA Reviewed; 58 AA. AC Q60322; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized IS-like element protein MJ0016/MJ1621.1; GN OrderedLocusNames=MJ0016; GN and GN OrderedLocusNames=MJ1621.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98001.1; -; Genomic_DNA. DR EMBL; L77117; AAB99645.1; -; Genomic_DNA. DR PIR; H64301; H64301. DR EnsemblBacteria; AAB98001; AAB98001; MJ_0016. DR EnsemblBacteria; AAB99645; AAB99645; MJ_1621.1. DR KEGG; mja:MJ_0016; -. DR KEGG; mja:MJ_1621.1; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 58 Uncharacterized IS-like element protein FT MJ0016/MJ1621.1. FT /FTId=PRO_0000106656. SQ SEQUENCE 58 AA; 6622 MW; 1667E9FB91E42B63 CRC64; MLFIDAMPIK TKELVRKTRH ERIGISKLIK KTVVLVTIHR KNVGILDIKQ LSLPMGSI // ID Y018_METJA Reviewed; 524 AA. AC Q60324; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0018; GN OrderedLocusNames=MJ0018; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98002.1; -; Genomic_DNA. DR PIR; B64302; B64302. DR ProteinModelPortal; Q60324; -. DR EnsemblBacteria; AAB98002; AAB98002; MJ_0018. DR KEGG; mja:MJ_0018; -. DR eggNOG; arCOG09657; Archaea. DR eggNOG; ENOG4110ZR6; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR Pfam; PF04021; Class_IIIsignal; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 524 Uncharacterized protein MJ0018. FT /FTId=PRO_0000106658. FT TRANSMEM 13 33 Helical. {ECO:0000255}. SQ SEQUENCE 524 AA; 56565 MW; 0F878499773FF87C CRC64; MIFKKRKGQL TLEFILLILG MTVVGIVITM GLVEKSPIFI GDKPLEVKKE TMGLFINESK FNLTVENTTI SNLGNNNTES NNSNNETGGG YLYIRVSGSS KGLITKDLIV SGDAKDVSGD ISKTINSKCV EENAIGEVYG DIYLEGSANY KLGNLLCINK FQTYLTGSGS LKVYVPYIQE FIIRDKNSGE SQIGGSVSLT VGNTNINRFY VEKITGGAKV KFKDFAINTF ETNSGNFGGG AETVFENGRI STMKLGDIVS GGNVKFKNVN IGNMIINNMI GSPTFELSNS TINNMKINKL IGSPKILVED SSIINSLETD QLGGSDIEVK DGSIIKEITI HGSTGTNGKI FVGYGGKVEK LFVEGNINSR IDLKGFSGLI DVSIGNIAGG GKLYVDNVIG NSISTGIIGN NKGLEIEDSS LSVVNIEGVS NSGSAFIKNT LIYQLKINSL PDWGSDMTLN KVNITKLSIN EIRNGKLTIK NSEIGELHIT KISGKGKIIV KKSYVNGKYY KKLVIKKSNY KKWS // ID Y021_METJA Reviewed; 375 AA. AC Q60332; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=Putative glycyl-radical enzyme activating enzyme MJ0021 {ECO:0000305}; DE Short=GRE activating enzyme MJ0021 {ECO:0000305}; DE EC=1.97.1.- {ECO:0000305}; GN OrderedLocusNames=MJ0021; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0A9N4}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:P0A9N4}; CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98003.1; -; Genomic_DNA. DR PIR; E64302; E64302. DR ProteinModelPortal; Q60332; -. DR STRING; 243232.MJ_0021; -. DR EnsemblBacteria; AAB98003; AAB98003; MJ_0021. DR KEGG; mja:MJ_0021; -. DR eggNOG; arCOG00932; Archaea. DR eggNOG; COG2108; LUCA. DR InParanoid; Q60332; -. DR KO; K07129; -. DR OMA; AWWLLEE; -. DR PhylomeDB; Q60332; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 375 Putative glycyl-radical enzyme activating FT enzyme MJ0021. FT /FTId=PRO_0000200544. FT REGION 44 46 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 42 42 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 87 87 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 375 AA; 43446 MW; 5AEA168D21383CC8 CRC64; MNVEEIEKYL EENFDKLPEG CKQCVKGGKL VLFITGICNN NCYYCPLSEK RKNKDVIYAN ERLITTVEEA IEEAKLCSSK GVGITGGNPL LKINRTVKFL KALKKEFDEF HAHLYTTPET VNEENLKLLK EADLDEIRLH PTKIFNEGYD EEYIKFLCNK LNLCNKYIED VGVEIPAIPN MENEILKLAE AIDGIAKFMN INELEFSEEN YHELEKRGFM PKDDVSNAIA GSEETALKVI KEFKGDLFIN YCPSVLKDAI QMRNRLINRA KNVAKPYEVI TEDGLLLRGI MIFDNEDDLK EMAEILEENE IEFEIIDKNI CLNPFILEDI IEEMKRQRFP ITFSAYISEL YPTADALEVE RIPLITKKLK FRRRR // ID Y043_METJA Reviewed; 785 AA. AC Q60348; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Uncharacterized protein MJ0043; DE Contains: DE RecName: Full=Mja hyp1 intein; GN OrderedLocusNames=MJ0043; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98023.1; -; Genomic_DNA. DR PIR; C64305; C64305. DR ProteinModelPortal; Q60348; -. DR STRING; 243232.MJ_0043; -. DR EnsemblBacteria; AAB98023; AAB98023; MJ_0043. DR KEGG; mja:MJ_0043; -. DR eggNOG; arCOG04881; Archaea. DR eggNOG; COG1372; LUCA. DR eggNOG; COG1379; LUCA. DR InParanoid; Q60348; -. DR OMA; THENRFK; -. DR PhylomeDB; Q60348; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 2. DR InterPro; IPR005287; CHP00375. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF51294; SSF51294; 4. DR SUPFAM; SSF89550; SSF89550; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR00375; TIGR00375; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; Protein splicing; KW Reference proteome. FT CHAIN 1 128 Uncharacterized protein MJ0043, 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000013988. FT CHAIN 129 520 Mja hyp1 intein. {ECO:0000255}. FT /FTId=PRO_0000013989. FT CHAIN 521 785 Uncharacterized protein MJ0043, 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000013990. FT DOMAIN 293 421 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 785 AA; 91459 MW; 4167A59032511F17 CRC64; MIANVDLHIH SRFSGGTSKD MNVENILKYG KLKGLNIIGT GDCTHPDYLE EIKQYKDREL ILTTEIEDKN RVHHLILLPS ISKVEELREI LKKYSKDIDK EGRPRVSIGG AELLEIVRDV GGLIGPAHCV PPDTLLILEN GFKRIVDIKV GDKVLTHENR FKKVEKVYKR RYIGDIIKIK VRYFPEEIIL TPEHPVYAIK TEKRCDGSHG ICKFNCLTQY TNPSCKKRYR KYKREWIIAK DLKVGDVIVY PIPNRVRDIK YLSLDKYLSN IKREFCRSRI PEKIEVSEEF CRLVGYFLSE GYCFRDGIGF ALGENEKKII DDIEYLMKKI FNLKPKIRDD GRSEGIELKY YSRVLRDFFG DMFYCGDEKR AWNKALPNEF LYLPKNKQLQ IFIGWWRGDK GVTTSEILMN QLRLISLRLG FIITFSKHVP KNPKIGDREV IKYHARWQGR VSILDEKIVD ELKNEDIKLP KKDVRYGWIK GNYLYAPIIR IGREYYDGFV YNLEVEDDSS YVTVSGTLHN CFTPWTSLYK SFDSIYDCYN KKPDFVELGL SADTDMADMI PELRDLPFLS NSDAHSYHPH RLGREFNQIE VDYIGGIEDN FEQIKKAIKH NKIIANYGLD PKLGKYHLTA CSKCHTRFKL EDAKKYNWKC PKCGGSIKKG VLSRVEELSD GKIEHPKFRP PYYKLIPLAE MISLTIGKGI FTKAVQSLWE EFIKKYGNEI EVLINADIDE LSKIHPKVAE TINLFRKGKI YIYPGGGGEY GKISFKPQKV EWYREEVTLD RWLKQ // ID Y04A_METJA Reviewed; 105 AA. AC P81302; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MJ0047.1; GN OrderedLocusNames=MJ0047.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98040.1; -; Genomic_DNA. DR STRING; 243232.MJ_0047.1; -. DR EnsemblBacteria; AAB98040; AAB98040; MJ_0047.1. DR KEGG; mja:MJ_0047.1; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 105 Uncharacterized protein MJ0047.1. FT /FTId=PRO_0000106669. SQ SEQUENCE 105 AA; 12400 MW; 645187616A9D9DFB CRC64; MKYNTHPFPS SIHSLRGLIL IFSKYCFNAF NLIYFHPPRG LILTIIWEKG KVSITDKFPF RNGLILTNAK NLHYPQHNNW ISIPKRSDFN RAIIHNIIYF ITLNI // ID Y066_METJA Reviewed; 480 AA. AC Q60377; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0066; GN OrderedLocusNames=MJ0066; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS CC reductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98046.1; -; Genomic_DNA. DR PIR; B64308; B64308. DR ProteinModelPortal; Q60377; -. DR STRING; 243232.MJ_0066; -. DR EnsemblBacteria; AAB98046; AAB98046; MJ_0066. DR KEGG; mja:MJ_0066; -. DR eggNOG; arCOG00073; Archaea. DR eggNOG; COG0175; LUCA. DR eggNOG; COG5270; LUCA. DR InParanoid; Q60377; -. DR KO; K00390; -. DR OMA; GQRKYES; -. DR PhylomeDB; Q60377; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR Pfam; PF01507; PAPS_reduct; 1. DR Pfam; PF01472; PUA; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 480 Uncharacterized protein MJ0066. FT /FTId=PRO_0000100693. FT DOMAIN 131 207 PUA. {ECO:0000255|PROSITE- FT ProRule:PRU00161}. SQ SEQUENCE 480 AA; 56371 MW; 8076C1D9A79B53D3 CRC64; MWEVIIMKTY IGKIHLKWCK NCNVPLLGRV CEVCGSKAEE VKLTPPGDPR LGFQYDMDFI NKILEEEFGA KNVLNGKIIL LNKIPGNEEA YEIIVDGEVK YLIYFDEDKE KWKVKLKLNG AKDLMEKGAY KKIIKIKNDV VEFLKNRKGS VLRPGIVEFT DDIEEKDDVI IVDENDRVVG VGLAVVSSED IKNMEKGKVV KVRFFIKDNE DYKPGKIYDN LEEAFDLMVR ANEGVIDNYE RNAIGFIKNT YEKIKKPVMV AFSGGKDSLV TLILTLKALG KDIDVVFIDT GLEFEETLKN VEDVERHYGI KIIRLRGENF WEKVKEYGIP ARDYRWCSEI CKLEPLKKFI EENYEDDVLS FVGIRKYESF NRATKKRIHR NTYIKKQINA LPIFHWSSLH VWIYLLREKA PYNKLYEKGF DRIGCFMCPA MEMGEMNKIK REFPKLWEKW ENVLREYAEK HNLGEGWIKK GLWRWKHKRQ // ID Y1024_METJA Reviewed; 403 AA. AC Q58430; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Uncharacterized protein MJ1024; GN OrderedLocusNames=MJ1024; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To B.subtilis YhaP. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99028.1; -; Genomic_DNA. DR PIR; G64427; G64427. DR STRING; 243232.MJ_1024; -. DR EnsemblBacteria; AAB99028; AAB99028; MJ_1024. DR KEGG; mja:MJ_1024; -. DR eggNOG; arCOG01462; Archaea. DR eggNOG; COG1668; LUCA. DR InParanoid; Q58430; -. DR KO; K01992; -. DR OMA; TQFLIWI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015562; F:efflux transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0055085; P:transmembrane transport; IBA:GO_Central. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 403 Uncharacterized protein MJ1024. FT /FTId=PRO_0000107147. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. FT TRANSMEM 238 258 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 303 323 Helical. {ECO:0000255}. FT TRANSMEM 355 375 Helical. {ECO:0000255}. FT COMPBIAS 307 315 Poly-Ile. SQ SEQUENCE 403 AA; 45294 MW; 6242E4EF26F7191C CRC64; MNSGDIMKLN IKKILTIGKR EVLSNIKRKQ FLIATIIGPL IIIALAIIGS FMMFDIKEIK VGYVDEFGLG IPNKVVENNF GKNTTIYFIK YENIEKGKED VLNKSIDALI VIPKDYLDSG KIILYSTTKS PNPIITDTLN KFLLKKLLKG KVDNKTYNRV INPMNLEIYS VSKKGFEKET FLSQLLPIGF VFLLYMAISS LSGIIVSSII EEKQNRIMEL LLCYSSAENL MFGKILGISA VGLLQIGIWV LFALPIIITY AVKVSLYLAI FALIYFVLGY LFYSSLLCGL SSLFSHPKDA SQLISPIIII QIIPIMFMNT IMVNPNHYMA KILSYVPFTA PYAVVLRASV TQLPLIEIVL STAIMIVSIV ISFILSIKLF KIGVLLYEEN LTLKRVIKII FKK // ID Y1062_METJA Reviewed; 484 AA. AC Q58462; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Uncharacterized protein MJ1062; GN OrderedLocusNames=MJ1062; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99065.1; -; Genomic_DNA. DR PIR; E64432; E64432. DR PDB; 3EO4; X-ray; 2.19 A; A/B/C/D=324-484. DR PDBsum; 3EO4; -. DR ProteinModelPortal; Q58462; -. DR STRING; 243232.MJ_1062; -. DR DNASU; 1451959; -. DR EnsemblBacteria; AAB99065; AAB99065; MJ_1062. DR KEGG; mja:MJ_1062; -. DR eggNOG; arCOG06581; Archaea. DR eggNOG; COG1670; LUCA. DR eggNOG; COG3980; LUCA. DR InParanoid; Q58462; -. DR OMA; RIDIFCE; -. DR EvolutionaryTrace; Q58462; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008080; F:N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0016758; F:transferase activity, transferring hexosyl groups; IEA:InterPro. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR007235; Glyco_trans_28_C. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR020023; PseG. DR Pfam; PF13302; Acetyltransf_3; 1. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR03590; PseG; 1. DR PROSITE; PS51186; GNAT; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 484 Uncharacterized protein MJ1062. FT /FTId=PRO_0000107155. FT DOMAIN 334 484 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. FT STRAND 324 326 {ECO:0000244|PDB:3EO4}. FT STRAND 333 338 {ECO:0000244|PDB:3EO4}. FT HELIX 341 343 {ECO:0000244|PDB:3EO4}. FT HELIX 344 351 {ECO:0000244|PDB:3EO4}. FT HELIX 354 357 {ECO:0000244|PDB:3EO4}. FT HELIX 369 378 {ECO:0000244|PDB:3EO4}. FT STRAND 383 391 {ECO:0000244|PDB:3EO4}. FT STRAND 394 404 {ECO:0000244|PDB:3EO4}. FT STRAND 408 410 {ECO:0000244|PDB:3EO4}. FT STRAND 412 417 {ECO:0000244|PDB:3EO4}. FT HELIX 427 441 {ECO:0000244|PDB:3EO4}. FT STRAND 446 452 {ECO:0000244|PDB:3EO4}. FT HELIX 456 464 {ECO:0000244|PDB:3EO4}. FT STRAND 468 472 {ECO:0000244|PDB:3EO4}. FT STRAND 477 483 {ECO:0000244|PDB:3EO4}. SQ SEQUENCE 484 AA; 56694 MW; E1764675A97CFCB2 CRC64; MKIAIITDGS VEMGMGHVYR TLSLANELRK FNVNEIIFFT KSDEDVIKKI EENGFKVIKC SDNNDILKNI KNIKPDVVII DDLGIEEDFA KNIRELCKKL IFFDNPNPSS NKYADIVVNA IVGSELKNRK YFDEENKTLY FYGPKYLILR NEFYKVKKEM LSRSKNKETK NILIAFGGSD PSNLTCKVLE ELLSKDRDFN INVVLGPKFQ YEDELNNLLK RYSKSDKIKI YKNIDNMAEL MKDNDLIITS PGMTMFEALF LGIPVVVLYQ NELQRECYDD YLKKISKTHL NPLKEGYFID AEHTDLHIGK GKFEIIEAIT NIYNCKKIGE DSKIIIRQIT DNDLELLMAW RSNPLIYKFF YIQKEPLKWE EHYSWWMSRE NRVDWIILLR ENNTIRKVGS VNVSQLNTDN PEIGILIGEF FLWGKHIGRH SVSLVLKWLK NIGYKKAHAR ILENNIRSIK LFESLGFKKT KKGRENEWIY EVNL // ID Y1070_METJA Reviewed; 157 AA. AC Q58470; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ1070; DE Flags: Precursor; GN OrderedLocusNames=MJ1070; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99077.1; -; Genomic_DNA. DR PIR; E64433; E64433. DR ProteinModelPortal; Q58470; -. DR STRING; 243232.MJ_1070; -. DR EnsemblBacteria; AAB99077; AAB99077; MJ_1070. DR KEGG; mja:MJ_1070; -. DR eggNOG; arCOG05067; Archaea. DR eggNOG; ENOG410Z5JH; LUCA. DR OMA; FVHYGNI; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 157 Uncharacterized protein MJ1070. FT /FTId=PRO_0000014007. SQ SEQUENCE 157 AA; 18240 MW; 75CD5561820D9429 CRC64; MRKYLIILVL LLFLSSSFGY YFDYIKVSES NPIKTITFKI NKAENYSYKL SFVHYGNINK SMKVNIYLNG NLAYTIDDSN DASPAYKKNA SIDITNYLKD GENVLKVEGM NLIGNENYHP YYVLKDIYIN EPAKTPIDFK LMIYALLIIC FLIYKKC // ID Y1071_METJA Reviewed; 313 AA. AC Q58471; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1071; GN OrderedLocusNames=MJ1071; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0977 C-terminal region. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99078.1; -; Genomic_DNA. DR PIR; F64433; F64433. DR ProteinModelPortal; Q58471; -. DR STRING; 243232.MJ_1071; -. DR EnsemblBacteria; AAB99078; AAB99078; MJ_1071. DR KEGG; mja:MJ_1071; -. DR eggNOG; arCOG00433; Archaea. DR eggNOG; COG0608; LUCA. DR OMA; YFGKWNI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 313 Uncharacterized protein MJ1071. FT /FTId=PRO_0000107157. SQ SEQUENCE 313 AA; 37221 MW; AE71D9EB59B7C800 CRC64; MAFDEICDEI ILNYEDAKDF AYILKLTYLN EFKKLENLNL NKFGIIKKDD LSFYGKNYPL FKSLLFFNEI PVFRGEKESI LFLKSIGLSP RITLNSLTYK EKIKLGNEFL KRCINFVPKE YISYIPQLIF GKEYYFRGVC LKEYVSALNG LYKIGKKKKV KKLIINMELP DEKDVKKYKK KLAKKITLFN KKLENYEINY FNLKFNNKNF ECQYIYVKQS VWDKILGLFG EGIELKYYPT LVNIAYSSEK VDFLKPFFIF VDKGDISVYA KVPKLIYLKD GLSLNYLNLR GKYVYFGNWE KDKFWEIIER GVL // ID Y1074_METJA Reviewed; 112 AA. AC Q58474; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1074; GN OrderedLocusNames=MJ1074; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99080.1; -; Genomic_DNA. DR PIR; A64434; A64434. DR STRING; 243232.MJ_1074; -. DR EnsemblBacteria; AAB99080; AAB99080; MJ_1074. DR KEGG; mja:MJ_1074; -. DR eggNOG; arCOG09652; Archaea. DR eggNOG; ENOG4110ZR7; LUCA. DR OMA; KIDERFY; -. DR PhylomeDB; Q58474; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 112 Uncharacterized protein MJ1074. FT /FTId=PRO_0000107159. FT TRANSMEM 85 105 Helical. {ECO:0000255}. SQ SEQUENCE 112 AA; 13233 MW; 892E21E4BA7B24B3 CRC64; MAIAYAKLYE LIHKKIKDER EADELYNAII EIIKESKVIV KNELKDELKD ELATKKDIDL VREEMKAMEE RILRYVDNRF NQLLIVQLII LFAIIITNPN AIELIKLLFG FK // ID Y1078_METJA Reviewed; 234 AA. AC Q58478; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=UPF0104 membrane protein MJ1078; GN OrderedLocusNames=MJ1078; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0104 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99082.1; -; Genomic_DNA. DR PIR; E64434; E64434. DR ProteinModelPortal; Q58478; -. DR STRING; 243232.MJ_1078; -. DR EnsemblBacteria; AAB99082; AAB99082; MJ_1078. DR KEGG; mja:MJ_1078; -. DR eggNOG; arCOG00899; Archaea. DR eggNOG; COG0392; LUCA. DR InParanoid; Q58478; -. DR KO; K07027; -. DR OMA; IRYELLI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016740; F:transferase activity; IBA:GO_Central. DR InterPro; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. DR TIGRFAMs; TIGR00374; TIGR00374; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 234 UPF0104 membrane protein MJ1078. FT /FTId=PRO_0000138104. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 198 218 Helical. {ECO:0000255}. SQ SEQUENCE 234 AA; 26481 MW; 2929A35F27ED0BE0 CRC64; MFINSLVPAK LGDVYRGYLL KKKTNESISL GVGTVFIERV FDLVAMISLL FISAYLSFKS DIPKEILYSI KWGVIIILFL IILIFGFLIV NSKINLKNKK LEAILMNFEK GLKAVKLNTL PLLITLSFTG WFIEGLTVYF IFLSLNLNLE ILFGVFSDLA SSLLTAIPLT PSGLGVVEYA LIYILKLKNI DYSGAFAVLI LYRLISYFSI VLFGAIMFYI VERNILKEPK NEKY // ID Y107_METJA Reviewed; 525 AA. AC Q57571; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Uncharacterized protein MJ0107; GN OrderedLocusNames=MJ0107; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP LACK OF DHPS ACTIVITY. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=10426953; DOI=10.1038/11525; RA Xu H., Aurora R., Rose G.D., White R.H.; RT "Identifying two ancient enzymes in Archaea using predicted secondary RT structure alignment."; RL Nat. Struct. Biol. 6:750-754(1999). CC -!- FUNCTION: Unknown. Does not possess dihydropteroate synthase CC (DHPS) activity since it does not catalyze the condensation of 6- CC hydroxymethyl-7,8-dihydropterin pyrophosphate (DHPP) and 4- CC aminobenzoate to form 7,8-dihydropteroate. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 pterin-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00334}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98089.1; -; Genomic_DNA. DR PIR; C64313; C64313. DR ProteinModelPortal; Q57571; -. DR STRING; 243232.MJ_0107; -. DR PRIDE; Q57571; -. DR EnsemblBacteria; AAB98089; AAB98089; MJ_0107. DR KEGG; mja:MJ_0107; -. DR eggNOG; arCOG01978; Archaea. DR eggNOG; COG0294; LUCA. DR InParanoid; Q57571; -. DR OMA; DMIDLGM; -. DR PhylomeDB; Q57571; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0042558; P:pteridine-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.20; -; 2. DR InterPro; IPR005236; Dihydropt_synth. DR InterPro; IPR011005; Dihydropteroate_synth-like. DR InterPro; IPR025595; DUF4346. DR InterPro; IPR000489; Pterin-binding_dom. DR Pfam; PF14251; DUF4346; 1. DR Pfam; PF00809; Pterin_bind; 1. DR SUPFAM; SSF51717; SSF51717; 1. DR TIGRFAMs; TIGR00284; TIGR00284; 1. DR PROSITE; PS50972; PTERIN_BINDING; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 525 Uncharacterized protein MJ0107. FT /FTId=PRO_0000106696. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 353 373 Helical. {ECO:0000255}. FT DOMAIN 146 394 Pterin-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00334}. SQ SEQUENCE 525 AA; 59645 MW; AA8BA61C6B81863D CRC64; MREIMKILII TGKLAERKVK DAVKKYDFID VHVANISVAA FLTPNLIIKE IKKLENKLGK KLKDIYDFVL VTGLIRHDLK NVEEETGIKC FKSTREASDI PILIENLDKI KLSTKEYADL QLLEIIRKKC EEEIKKAEEQ ELGEGDIKIG KLKVGDKFPM RVLGEIVHAP WLKEKELEEK IIYYLESGAD MIDLGMVSNE NNADKIKDML KIARDLTDNP ISVDTLNTKE LIEAINLGAD MILSVDAGNL DELIPYLKDS ETAVVVLPTN YKTNYVPETI EGKIKSLEEN IKKLIDAGIE KIVADPILEP INNAGCSFIE SVIACREFKK RNKLPLFFGV GNVTELFDAD SNGVNALLAA IGAEIGANIL FTPEASAKCK FSIKELKIAS KMMFLAKKRN SLPKDIGYNL INYKDKRFEE EITFNSYNIP IIKAEEDERQ ILDEGSFKIE IDRKNKEIVA IYFNKRREPV LIIRGKKPKE IYETAIRLNL IKKLDHASYF GRELAKAEIA LRIGKKYNQD FDLFL // ID Y1081_METJA Reviewed; 138 AA. AC Q58481; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=UPF0047 protein MJ1081; GN OrderedLocusNames=MJ1081; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0047 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99083.1; -; Genomic_DNA. DR PIR; H64434; H64434. DR ProteinModelPortal; Q58481; -. DR SMR; Q58481; 9-135. DR STRING; 243232.MJ_1081; -. DR EnsemblBacteria; AAB99083; AAB99083; MJ_1081. DR KEGG; mja:MJ_1081; -. DR eggNOG; arCOG04214; Archaea. DR eggNOG; COG0432; LUCA. DR InParanoid; Q58481; -. DR OMA; DSHIRAM; -. DR PhylomeDB; Q58481; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.60.120.460; -; 1. DR InterPro; IPR001602; UPF0047. DR Pfam; PF01894; UPF0047; 1. DR PIRSF; PIRSF004681; UCP004681; 1. DR SUPFAM; SSF111038; SSF111038; 1. DR TIGRFAMs; TIGR00149; TIGR00149_YjbQ; 1. DR PROSITE; PS01314; UPF0047; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 138 UPF0047 protein MJ1081. FT /FTId=PRO_0000088525. SQ SEQUENCE 138 AA; 15613 MW; F7D702871A9A3665 CRC64; MLVIKMLFKY QIKTNKREEL VDITPYIISA ISESKVKDGI AVIYVPHTTA GITINENADP SVKHDIINFL SHLIPKNWNF THLEGNSDAH IKSSLVGCSQ TIIIKDGKPL LGTWQGIFFA EFDGPRRREF YVKIIGDK // ID Y1134_METJA Reviewed; 226 AA. AC Q58534; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 68. DE RecName: Full=Uncharacterized protein MJ1134; GN OrderedLocusNames=MJ1134; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99136.1; -; Genomic_DNA. DR PIR; E64441; E64441. DR ProteinModelPortal; Q58534; -. DR STRING; 243232.MJ_1134; -. DR EnsemblBacteria; AAB99136; AAB99136; MJ_1134. DR KEGG; mja:MJ_1134; -. DR eggNOG; arCOG02610; Archaea. DR eggNOG; COG1354; LUCA. DR InParanoid; Q58534; -. DR KO; K05896; -. DR OMA; GKVDPWN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR003768; ScpA. DR Pfam; PF02616; SMC_ScpA; 1. PE 4: Predicted; KW Coiled coil; Complete proteome; Reference proteome. FT CHAIN 1 226 Uncharacterized protein MJ1134. FT /FTId=PRO_0000107182. FT COILED 121 163 {ECO:0000255}. SQ SEQUENCE 226 AA; 26892 MW; 12AFAF1A3DAE32EF CRC64; MIDSNFDIVL WVRMIKEGIE KKNLNPWDVN IAEIADYYIQ KIKELKKFDI RLSADVILVA GILLRMKSEA LYDECKVEEE EDYDYCDDYY DYDDIEEKPK KGKKKEKEDK DKNKKSKKPV TVDELIKTIE KELNKVKKSR KNREKKTNEV EEIIEELIEE DDISDIIAEL LDDLMKEGII VYQEKFKTRE DRVRYFIPSL YLANDGKAEL IQEKLFGELI IKLKSF // ID Y1150_METJA Reviewed; 184 AA. AC Q58550; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 77. DE RecName: Full=UPF0215 protein MJ1150 {ECO:0000255|HAMAP-Rule:MF_00582}; GN OrderedLocusNames=MJ1150; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0215 family. {ECO:0000255|HAMAP- CC Rule:MF_00582}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99150.1; -; Genomic_DNA. DR PIR; E64443; E64443. DR ProteinModelPortal; Q58550; -. DR STRING; 243232.MJ_1150; -. DR PRIDE; Q58550; -. DR EnsemblBacteria; AAB99150; AAB99150; MJ_1150. DR KEGG; mja:MJ_1150; -. DR eggNOG; arCOG00928; Archaea. DR eggNOG; COG1628; LUCA. DR InParanoid; Q58550; -. DR KO; K09120; -. DR OMA; HMIASAV; -. DR PhylomeDB; Q58550; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00582; UPF0215; 1. DR InterPro; IPR002802; DUF99. DR Pfam; PF01949; DUF99; 1. DR PIRSF; PIRSF006380; UCP006380; 1. DR ProDom; PD016744; DUF99; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 184 UPF0215 protein MJ1150. FT /FTId=PRO_0000149233. SQ SEQUENCE 184 AA; 21384 MW; 121B036339B7BE15 CRC64; MVLMKDEVEV IGFDDAPFNK ADKVCILIGT YMRGNRIIDG IYFRKFKKDG MDVTEKIIDI VKEKHYKKIK VIFLAGITFG GFNIADLWEI NKETEKPVIV VIDKYPNKEK IFLALKKYFD DADERIKLIN SFPEPEKMEN IYVQYVGADK EFVKNVIKKT KLKSKIPECL RISHLIGRGF LGLR // ID Y1156_METJA Reviewed; 903 AA. AC Q58556; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 108. DE RecName: Full=Cell division cycle protein 48 homolog MJ1156; GN OrderedLocusNames=MJ1156; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the AAA ATPase family. CDC48 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99153.1; -; Genomic_DNA. DR PIR; C64444; C64444. DR ProteinModelPortal; Q58556; -. DR SMR; Q58556; 441-675. DR STRING; 243232.MJ_1156; -. DR PRIDE; Q58556; -. DR EnsemblBacteria; AAB99153; AAB99153; MJ_1156. DR KEGG; mja:MJ_1156; -. DR eggNOG; arCOG01308; Archaea. DR eggNOG; COG0464; LUCA. DR InParanoid; Q58556; -. DR KO; K13525; -. DR OMA; GPEIMGS; -. DR PhylomeDB; Q58556; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.10.330.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR005938; AAA_ATPase_CDC48. DR InterPro; IPR009010; Asp_de-COase-like_dom. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR003960; ATPase_AAA_CS. DR InterPro; IPR004201; Cdc48_dom2. DR InterPro; IPR029067; CDC48_domain_2-like. DR InterPro; IPR003338; CDC4_N-term_subdom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR015415; Vps4_C. DR Pfam; PF00004; AAA; 2. DR Pfam; PF02933; CDC48_2; 1. DR Pfam; PF02359; CDC48_N; 1. DR Pfam; PF09336; Vps4_C; 1. DR SMART; SM00382; AAA; 2. DR SMART; SM01072; CDC48_2; 1. DR SMART; SM01073; CDC48_N; 1. DR SUPFAM; SSF50692; SSF50692; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR SUPFAM; SSF54585; SSF54585; 1. DR TIGRFAMs; TIGR01243; CDC48; 1. DR PROSITE; PS00674; AAA; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat. FT CHAIN 1 903 Cell division cycle protein 48 homolog FT MJ1156. FT /FTId=PRO_0000084591. FT NP_BIND 220 227 ATP. {ECO:0000255}. FT NP_BIND 493 500 ATP. {ECO:0000255}. SQ SEQUENCE 903 AA; 100403 MW; 99F2ABEE2D544DC2 CRC64; MVKELKVAEA YQGDVGRGIA RIDPYTMEEL GLKPGDVIEI EGPKGKAYAI VYRGFLEDAG KGIIRIDGYL RQNAGVAIGD RVKVKRVEIK EAKKVVLAPT QPIRFGPGFE DFVKRKILGQ VLSKGSKVTI GVLGTALTFV VVSTTPAGPV RVTDFTHVEL KEEPVSEIKE TKVPDVTYED IGGLKEEVKK VREMIELPMR HPELFEKLGI EPPKGVLLVG PPGTGKTLLA KAVANEAGAN FYVINGPEIM SKYVGETEEN LRKIFEEAEE NAPSIIFIDE IDAIAPKRDE ATGEVERRLV AQLLTLMDGL KGRGQVVVIG ATNRPNALDP ALRRPGRFDR EIVIGVPDRE GRKEILQIHT RNMPLAEDVD LDYLADVTHG FVGADLAALC KEAAMRALRR VLPSIDLEAE EIPKEVLDNL KVTMDDFKEA LKDVEPSAMR EVLVEVPNVK WEDIGGLEEV KQELREAVEW PLKAKEVFEK IGVRPPKGVL LFGPPGTGKT LLAKAVANES GANFISVKGP EIFSKWVGES EKAIREIFRK ARQSAPCIIF FDEIDAIAPK RGRDLSSAVT DKVVNQLLTE LDGMEEPKDV VVIAATNRPD IIDPALLRPG RLDRVILVPV PDEKARLDIF KIHTRSMNLA EDVNLEELAK KTEGYTGADI EALCREAAML AVRESIGKPW DIEVKLRELI NYLQSISGTF RAAAVELNSV IKATKERESA EAGEFSELKN AIGKIISVLS PAKEKIEAVE KEIDKFLEVI NKEELKPSEK DEAQKLAKYL KDILGKLKEM IDNIYELENK LNTLKEQVSA EEIDEIIKTT QNIIQRFTTS LDELKNILKD IESIRLKVST KDVKIKKEHF MKALEKIKPS VSKEDMRVYE KLAQEYGRAT SVEKKKEEGK EVI // ID Y1177_METJA Reviewed; 334 AA. AC Q58578; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 88. DE RecName: Full=UPF0118 membrane protein MJ1177; GN OrderedLocusNames=MJ1177; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0118 (PerM) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99180.1; -; Genomic_DNA. DR PIR; A64447; A64447. DR STRING; 243232.MJ_1177; -. DR DNASU; 1452076; -. DR EnsemblBacteria; AAB99180; AAB99180; MJ_1177. DR KEGG; mja:MJ_1177; -. DR eggNOG; arCOG02642; Archaea. DR eggNOG; COG0628; LUCA. DR InParanoid; Q58578; -. DR OMA; YISIAIY; -. DR PhylomeDB; Q58578; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002549; AI-2E-like. DR PANTHER; PTHR21716; PTHR21716; 1. DR Pfam; PF01594; UPF0118; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 334 UPF0118 membrane protein MJ1177. FT /FTId=PRO_0000148326. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT TRANSMEM 191 211 Helical. {ECO:0000255}. FT TRANSMEM 234 254 Helical. {ECO:0000255}. FT TRANSMEM 259 279 Helical. {ECO:0000255}. FT TRANSMEM 293 313 Helical. {ECO:0000255}. SQ SEQUENCE 334 AA; 38445 MW; FD7429A229130200 CRC64; MRFEEFKYVR KGVIVGLLIM LLYIIWPFID VLAYSCAFAY MALPVYNILR KKFNKTISAG LAISIYILPI MTITIYALLT FMEIILSFNT KSIEPYINEI LSIYNSFMLE RIINNEQIIA KYIDEFIKYL VSQFSGKIID VGYLIVKVIM VLFLTFYFLR DGDKAKNLII SFVPDEYKEK MRIYLSYLHD SYKNLFISCV SLSIIITILS YIGYLILGVP YAELFAIITG IFALLPILGG WMVYISIAIY FFLIHDYTKA VFMFIYGELF LSIAPDFVIR PYLVKKEVDI HPVLVVIAFL MAPLSLGLSG FAIGPLVVGA LNAFYLAKYR DKKI // ID Y1215_METJA Reviewed; 86 AA. AC Q58612; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1215; GN OrderedLocusNames=MJ1215; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99216.1; -; Genomic_DNA. DR PIR; F64451; F64451. DR ProteinModelPortal; Q58612; -. DR STRING; 243232.MJ_1215; -. DR EnsemblBacteria; AAB99216; AAB99216; MJ_1215. DR KEGG; mja:MJ_1215; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q58612; -. DR KO; K07075; -. DR OMA; EFYEPIG; -. DR PhylomeDB; Q58612; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 86 Uncharacterized protein MJ1215. FT /FTId=PRO_0000107218. SQ SEQUENCE 86 AA; 10281 MW; CD9296D0B135FD14 CRC64; MRGRMKTLSE IKEILRKHKK ELKENYKVKS IAIFGSYARG EQKETSDIDI MVEFYETPDY LKFFELEDYL ENILNIKVDL ITKNSI // ID Y1221_METJA Reviewed; 299 AA. AC Q58618; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Uncharacterized protein MJ1221; GN OrderedLocusNames=MJ1221; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0678. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99234.1; -; Genomic_DNA. DR PIR; D64452; D64452. DR ProteinModelPortal; Q58618; -. DR STRING; 243232.MJ_1221; -. DR EnsemblBacteria; AAB99234; AAB99234; MJ_1221. DR KEGG; mja:MJ_1221; -. DR eggNOG; arCOG02264; Archaea. DR eggNOG; COG1808; LUCA. DR InParanoid; Q58618; -. DR OMA; IEHNIPT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR005240; DUF389. DR Pfam; PF04087; DUF389; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 299 Uncharacterized protein MJ1221. FT /FTId=PRO_0000107222. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. FT TRANSMEM 210 230 Helical. {ECO:0000255}. FT TRANSMEM 236 256 Helical. {ECO:0000255}. FT TRANSMEM 261 281 Helical. {ECO:0000255}. SQ SEQUENCE 299 AA; 32538 MW; 82A1E3BE398C9DFF CRC64; MWFGERMRYM KIIIPKKFLN TVEEILKKNN AYSISIIEPL KTSIEDGIII TCNADARDAE KIVLELKKLG LGEKGHGSVT IMPANITFSC REEGIASTSL SPLELYYKAK TMVKITKNVI IKVILASIMG VIGLIEHNIP TLIGAMIIAP LVDTVMGSAI GTVLGDKELF IQGMKKELLC SGIVIVCAFI PSLFFVSKEL VLQYLSETSI ILSAIVAIIA GISGGMSIAS GKEYEIIGVT IDVSILIPAL LMGMALATMD LYLIYITFIL LAINIVLLDV GGYIGLKYKV GKINQKIKY // ID Y004_METJA Reviewed; 243 AA. AC Q60315; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0004; GN OrderedLocusNames=MJ0004; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000305}; CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97985.1; -; Genomic_DNA. DR PIR; D64300; D64300. DR ProteinModelPortal; Q60315; -. DR STRING; 243232.MJ_0004; -. DR EnsemblBacteria; AAB97985; AAB97985; MJ_0004. DR KEGG; mja:MJ_0004; -. DR eggNOG; arCOG02678; Archaea. DR eggNOG; COG1924; LUCA. DR InParanoid; Q60315; -. DR OMA; GKGANYF; -. DR PhylomeDB; Q60315; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002731; ATPase_BadF. DR InterPro; IPR008275; CoA_E_activase. DR Pfam; PF01869; BcrAD_BadFG; 1. DR TIGRFAMs; TIGR00241; CoA_E_activ; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 243 Uncharacterized protein MJ0004. FT /FTId=PRO_0000106647. FT METAL 120 120 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000255}. FT METAL 157 157 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000255}. SQ SEQUENCE 243 AA; 26897 MW; 288C4F4190575E53 CRC64; MILGIDVGST TTKMVLMEDS KIIWYKIEDI GVVIEEDILL KMVKEIEQKY PIDKIVATGY GRHKVSFADK IVPEVIALGK GANYFFNEAD GVIDIGGQDT KVLKIDKNGK VVDFILSDKC AAGTGKFLEK ALDILKIDKN EINKYKSDNI AKISSMCAVF AESEIISLLS KKVPKEGILM GVYESIINRV IPMTNRLKIQ NIVFSGGVAK NKVLVEMFEK KLNKKLLIPK EPQIVCCVGA ILV // ID Y017_METJA Reviewed; 214 AA. AC Q60323; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 74. DE RecName: Full=Uncharacterized protein MJ0017; GN OrderedLocusNames=MJ0017; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97994.1; -; Genomic_DNA. DR PIR; A64302; A64302. DR STRING; 243232.MJ_0017; -. DR EnsemblBacteria; AAB97994; AAB97994; MJ_0017. DR KEGG; mja:MJ_0017; -. DR eggNOG; arCOG02134; Archaea. DR eggNOG; COG3316; LUCA. DR InParanoid; Q60323; -. DR OMA; VTILRWV; -. DR PhylomeDB; Q60323; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR032874; DDE_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13610; DDE_Tnp_IS240; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 214 Uncharacterized protein MJ0017. FT /FTId=PRO_0000106657. SQ SEQUENCE 214 AA; 25506 MW; 0F135E2C748F933D CRC64; MRLTIEVIKE KIVERKLFKR NRKSIEVKIL AGLLYYLGLS LRKVSLFLSQ FEDISHESVR IYYHKIKEVL NEPERKERNL IAIDEIKLKV GDKYIYAWSA IDVETKECLG VYISKTRNYL DTILFVKSIL KFCSNKPKIL VDGGKWYPWA LRKLGLEFEK VKFGLRNCVE SFFSVLKRRT KAFFNRFPNN SKFDTVISWI KSFMMFYNWV KSLT // ID Y068_METJA Reviewed; 115 AA. AC Q60372; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0212 protein MJ0068 {ECO:0000255|HAMAP-Rule:MF_01223}; GN OrderedLocusNames=MJ0068; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0212 family. {ECO:0000255|HAMAP- CC Rule:MF_01223}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98047.1; -; Genomic_DNA. DR PIR; D64308; D64308. DR STRING; 243232.MJ_0068; -. DR EnsemblBacteria; AAB98047; AAB98047; MJ_0068. DR KEGG; mja:MJ_0068; -. DR eggNOG; arCOG02119; Archaea. DR eggNOG; COG1885; LUCA. DR InParanoid; Q60372; -. DR KO; K09731; -. DR OMA; HFESAFV; -. DR PhylomeDB; Q60372; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01223; UPF0212; 1. DR InterPro; IPR007564; UPF0212. DR Pfam; PF04475; DUF555; 1. DR PIRSF; PIRSF016934; UCP016934; 1. DR ProDom; PD020367; DUF555; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 115 UPF0212 protein MJ0068. FT /FTId=PRO_0000068276. SQ SEQUENCE 115 AA; 12515 MW; 2FE056FFC3A9A076 CRC64; MPNYHVTLQA AYIVRNVDDV EDAISVTISQ IGKMLNKEGL NYVDIDIGLT ICPKCGELVD CVLVVARTAL VGVLLSMKVF NAESPEHAIR IAKATIGKVL KNIPLEPVDV VELEK // ID Y093_METJA Reviewed; 142 AA. AC Q57558; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0093; GN OrderedLocusNames=MJ0093; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98076.1; -; Genomic_DNA. DR PIR; E64311; E64311. DR STRING; 243232.MJ_0093; -. DR EnsemblBacteria; AAB98076; AAB98076; MJ_0093. DR KEGG; mja:MJ_0093; -. DR eggNOG; arCOG05020; Archaea. DR eggNOG; ENOG410YNM8; LUCA. DR OMA; YIFLFTE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 142 Uncharacterized protein MJ0093. FT /FTId=PRO_0000106689. SQ SEQUENCE 142 AA; 16643 MW; B268466A1D45CEDD CRC64; MENFNFKCYD IDEKEIPIPP GLPQSIIARL IEICNVKFDI REDEIYNVKY PVLIGKEEDL KEAKKYLELI TEAKLTLRDI ARLARRFKVK AKIYTDDEDL RYILDVLSND IANKDYIEIV EEMPEGDKEV IEIGDKKIYV GI // ID Y100_METJA Reviewed; 509 AA. AC Q57564; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ0100; GN OrderedLocusNames=MJ0100; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98080.1; -; Genomic_DNA. DR PIR; D64312; D64312. DR PDB; 3KPB; X-ray; 1.60 A; A/B/C/D=388-509. DR PDB; 3KPC; X-ray; 1.79 A; A=386-509. DR PDB; 3KPD; X-ray; 2.91 A; A/B/C/D=388-509. DR PDBsum; 3KPB; -. DR PDBsum; 3KPC; -. DR PDBsum; 3KPD; -. DR ProteinModelPortal; Q57564; -. DR STRING; 243232.MJ_0100; -. DR EnsemblBacteria; AAB98080; AAB98080; MJ_0100. DR KEGG; mja:MJ_0100; -. DR eggNOG; arCOG00620; Archaea. DR eggNOG; COG0517; LUCA. DR eggNOG; COG1900; LUCA. DR InParanoid; Q57564; -. DR OMA; GTFEPME; -. DR PhylomeDB; Q57564; -. DR EvolutionaryTrace; Q57564; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR002708; HcyBio. DR InterPro; IPR016426; UCP004698_CBS_type. DR Pfam; PF00571; CBS; 2. DR Pfam; PF01837; HcyBio; 1. DR PIRSF; PIRSF004698; UCP004698_CBS_MJ0100; 1. DR ProDom; PD011569; DUF39; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure; CBS domain; Complete proteome; Reference proteome; KW Repeat. FT CHAIN 1 509 Uncharacterized protein MJ0100. FT /FTId=PRO_0000106693. FT DOMAIN 394 450 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 455 509 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT HELIX 390 393 {ECO:0000244|PDB:3KPB}. FT STRAND 394 397 {ECO:0000244|PDB:3KPD}. FT HELIX 407 417 {ECO:0000244|PDB:3KPB}. FT STRAND 422 425 {ECO:0000244|PDB:3KPB}. FT STRAND 429 435 {ECO:0000244|PDB:3KPB}. FT HELIX 437 445 {ECO:0000244|PDB:3KPB}. FT HELIX 451 453 {ECO:0000244|PDB:3KPB}. FT STRAND 455 458 {ECO:0000244|PDB:3KPB}. FT HELIX 468 478 {ECO:0000244|PDB:3KPB}. FT STRAND 481 486 {ECO:0000244|PDB:3KPB}. FT STRAND 491 497 {ECO:0000244|PDB:3KPB}. FT HELIX 498 505 {ECO:0000244|PDB:3KPB}. SQ SEQUENCE 509 AA; 56458 MW; 81417970CD74F38F CRC64; MIMKTIKEIN EKIKKGEAVV VTAEEMIKIV EEEGAKRAAD YVDVVTTGTF GAMCSSGVFI NFGHSDPPIK MLRIYLNNVE AYGGLAAVDA YIGAAQPNED PDVDIDYGGA HVIEDLVRGK EVELYAEGYT TDCYPRKEVN VRITLDDVNQ AIMVNPRNCY QTYAAATNSR EEKIYTYMGI LLPEYNNVHY SGAGQLNPLQ NDYNPETKSF NTIGIGTRIF LGGGIGYVIG EGTQHNPPFG TLMVKGDLKQ MNPKFIRAAT MPRYGSTLYV GIGIPIPVLN EKIAERCAIR DEDIEVPIYD YGFPRRDRPL IAKTNYKVLR SGKITLNVNI DGKDVEKTVK TGSVSSYKMA REVAETLKQW ILDGKFLLTE RVDTLGRAEN KPMKSPITLV KDILSKPPIT AHSNISIMEA AKILIKHNIN HLPIVDEHGK LVGIITSWDI AKALAQNKKT IEEIMTRNVI TAHEDEPVDH VAIKMSKYNI SGVPVVDDYR RVVGIVTSED ISRLFGGKK // ID Y1031_METJA Reviewed; 308 AA. AC Q58437; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized transporter MJ1031; GN OrderedLocusNames=MJ1031; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the auxin efflux carrier (TC 2.A.69) CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99035.1; -; Genomic_DNA. DR PIR; F64428; F64428. DR ProteinModelPortal; Q58437; -. DR STRING; 243232.MJ_1031; -. DR TCDB; 2.A.69.4.2; the auxin efflux carrier (aec) family. DR DNASU; 1451928; -. DR EnsemblBacteria; AAB99035; AAB99035; MJ_1031. DR KEGG; mja:MJ_1031; -. DR eggNOG; arCOG04756; Archaea. DR eggNOG; COG0679; LUCA. DR InParanoid; Q58437; -. DR KO; K07088; -. DR OMA; AMPSTIF; -. DR PhylomeDB; Q58437; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR004776; Auxin_eff. DR InterPro; IPR014024; Auxin_eff_plant. DR Pfam; PF03547; Mem_trans; 2. DR TIGRFAMs; TIGR00946; 2a69; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 308 Uncharacterized transporter MJ1031. FT /FTId=PRO_0000123803. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 221 241 Helical. {ECO:0000255}. FT TRANSMEM 257 277 Helical. {ECO:0000255}. FT TRANSMEM 287 307 Helical. {ECO:0000255}. SQ SEQUENCE 308 AA; 33770 MW; 02A915806E4441AE CRC64; MIPMDVVLIV LILVLVGYFS KIFGILKEEH AKILNNIVIY IAMPSTIFLT ISKNVSSSQI LEFLKLPVVI FLCCLFVGIL AYLLGKHIFK LKDEKLGGLI LVSMLGNTGF LGYPVALGMF GEEGLARAIF CDLGGVFATM LLGTYVGIRF GKGRDKSILK DMAKFPPLIT GILSIILVFF GFKLNYIPSF ILKSLNYLSS ATVPLIMMSL GLSLSPKALK FGVFWGIIAS IFRFIVSPAT AFTLSELINI KGLEKNVLLV ESSMPSAMMT LVLGTLYELD IKLIASSIFI TTTFSLLVIA LWGWILLN // ID Y1051_METJA Reviewed; 513 AA. AC Q58451; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1051; GN OrderedLocusNames=MJ1051; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the NodU/CmcH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99054.1; -; Genomic_DNA. DR PIR; B64431; B64431. DR ProteinModelPortal; Q58451; -. DR STRING; 243232.MJ_1051; -. DR EnsemblBacteria; AAB99054; AAB99054; MJ_1051. DR KEGG; mja:MJ_1051; -. DR eggNOG; arCOG01188; Archaea. DR eggNOG; COG2192; LUCA. DR InParanoid; Q58451; -. DR KO; K00612; -. DR OMA; HECHALG; -. DR PhylomeDB; Q58451; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR InterPro; IPR031730; Carbam_trans_C. DR InterPro; IPR003696; Carbtransf_dom. DR Pfam; PF16861; Carbam_trans_C; 1. DR Pfam; PF02543; Carbam_trans_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 513 Uncharacterized protein MJ1051. FT /FTId=PRO_0000207857. SQ SEQUENCE 513 AA; 58662 MW; C91414C702AE4A2B CRC64; MILGICDGHN ASSSLIKRDE ILFAMSEERF TRKKNQRGFP EKSVDYILNK VKPDEINYVS VGGVFRRGER IKKLKEFQNR INKKFLYFYH HISHSYLFKL SDFKEALVIS IDGGGDGLSF LASIANKNNL EIIAQSDLID SVGDFYASIT ELLGFKPMED EGKVMSLSSY EGEDDINLTT IDYIKELKSF KNYLGVIGYE ATKALKKLIV SDKSQLSFED KVRISKFAQR TLENIVLKAI DDLSNEYNID NIVFVGGVAQ NVKLNSKIAE KYNLFVPPFM GDEGLCLGAS LADKRIDRIN INNTYFGYEI ENERAEKILE ELKNKLNDYK IEFVEERDIP EVIGNLILDN KVVCLSRGKM EFGPRALGNR SVIALPTKEN KEKINKKLKR SWFMPFAPTI LYDFIDDYLI NPRYSPFMTQ IFKVKENKIK EIEGVIHVDK TTRPQTLKKD SNKTFYGIIR YIYDSIGIPV VLNTSFNLHG EPIVCNEKDA INSFLKADFD ALLLGNYLIS KVK // ID Y1053_METJA Reviewed; 163 AA. AC Q58453; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1053; GN OrderedLocusNames=MJ1053; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99060.1; -; Genomic_DNA. DR PIR; D64431; D64431. DR ProteinModelPortal; Q58453; -. DR STRING; 243232.MJ_1053; -. DR EnsemblBacteria; AAB99060; AAB99060; MJ_1053. DR KEGG; mja:MJ_1053; -. DR eggNOG; arCOG00921; Archaea. DR eggNOG; COG1318; LUCA. DR InParanoid; Q58453; -. DR KO; K07745; -. DR OMA; EKVTWVD; -. DR PhylomeDB; Q58453; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR022285; CHP03879_regulat_dom_put. DR InterPro; IPR009057; Homeodomain-like. DR TIGRFAMs; TIGR03879; near_KaiC_dom; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 163 Uncharacterized protein MJ1053. FT /FTId=PRO_0000107153. SQ SEQUENCE 163 AA; 18789 MW; F34029258C08497D CRC64; MIPLVPTSKT EIDKLEHVLI LGTLFRPEIL ELIKDPIEKV TWVDSLAIAA GALAREKAGY TIREIADELG RTEQTIRKHL KGETKAGKLV RETYEMMKRG ELNIEEVEKF LEAVVRKEEL EKITDIKKLE EEIEKLKKEN EELAAKLEKV KEKLKEVLSE LEK // ID Y1054_METJA Reviewed; 895 AA. AC Q58454; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 117. DE RecName: Full=Uncharacterized protein MJ1054; DE EC=1.1.1.-; DE Contains: DE RecName: Full=Mja UDPGD intein; GN OrderedLocusNames=MJ1054; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UDP-glucose/GDP-mannose dehydrogenase CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99056.1; -; Genomic_DNA. DR PIR; E64431; E64431. DR ProteinModelPortal; Q58454; -. DR STRING; 243232.MJ_1054; -. DR EnsemblBacteria; AAB99056; AAB99056; MJ_1054. DR KEGG; mja:MJ_1054; -. DR eggNOG; arCOG00253; Archaea. DR eggNOG; COG1004; LUCA. DR InParanoid; Q58454; -. DR KO; K00012; -. DR OMA; IKWEFLK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0003979; F:UDP-glucose 6-dehydrogenase activity; IBA:GO_Central. DR GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0000271; P:polysaccharide biosynthetic process; IEA:InterPro. DR GO; GO:0006065; P:UDP-glucuronate biosynthetic process; IBA:GO_Central. DR Gene3D; 2.170.16.10; -; 2. DR Gene3D; 3.10.28.10; -; 1. DR Gene3D; 3.40.50.720; -; 3. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR017476; UDP-Glc/GDP-Man. DR InterPro; IPR014027; UDP-Glc/GDP-Man_DH_C. DR InterPro; IPR014026; UDP-Glc/GDP-Man_DH_dimer. DR InterPro; IPR001732; UDP-Glc/GDP-Man_DH_N. DR InterPro; IPR028357; UDPglc_DH_bac. DR PANTHER; PTHR11374; PTHR11374; 2. DR Pfam; PF14528; LAGLIDADG_3; 2. DR Pfam; PF00984; UDPG_MGDP_dh; 1. DR Pfam; PF03720; UDPG_MGDP_dh_C; 1. DR Pfam; PF03721; UDPG_MGDP_dh_N; 1. DR PIRSF; PIRSF500134; UDPglc_DH_bac; 1. DR PIRSF; PIRSF000124; UDPglc_GDPman_dh; 1. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SMART; SM00984; UDPG_MGDP_dh_C; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51294; SSF51294; 2. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF52413; SSF52413; 1. DR SUPFAM; SSF55608; SSF55608; 2. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR TIGRFAMs; TIGR03026; NDP-sugDHase; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 3: Inferred from homology; KW Autocatalytic cleavage; Complete proteome; NAD; Oxidoreductase; KW Protein splicing; Reference proteome. FT CHAIN 1 260 Uncharacterized protein MJ1054, 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000035997. FT CHAIN 261 714 Mja UDPGD intein. {ECO:0000255}. FT /FTId=PRO_0000035998. FT CHAIN 715 895 Uncharacterized protein MJ1054, 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000035999. FT DOMAIN 468 614 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT NP_BIND 2 19 NAD. {ECO:0000255}. FT ACT_SITE 261 261 {ECO:0000250}. SQ SEQUENCE 895 AA; 102615 MW; B511AA68CCA41445 CRC64; MNISVIGTGY VGLIQAVGLA EFGFDVVGID IDESKVKALN RGECPLYEEG LEGLLKKHVN KNLTFTTSYK PIKDSDVIFL CVGTPQDKDG NADLRFLFSA VEKIKETIDK EDYKVIVIKS TVPVGTNRRV KELLKDYNVD VVSNPEFLRE GIAVYDFFNP ERVILGFENL NNKKPIEIME EVYKYFKDKN IPFVITNWET AELIKYASNA FLATKISFIN ELAKLSDKVK ADIKTISYAM GLDPRIGNKF LNAGIGYGGS CFHPDEVLFI DRGRGLECIT FKELFELEDK DNVKILSFDG EKLSLKKLKL ASKRYYNDDL ITLRFNLGRE IKITKDHPVV ILEDGELKIK LTSDVKEGDK VILPYGNFGE EREIEIDILE ELSKTDLIEK VWIHNKDLAT NEFNIIKPYL SNKYPHDVKR NGTIRAKDIL PIKEILDKYG SKNRLFTAKS KSTTIPYKIK IDKDFARLIG YYLSEGWISK DYGRNGVVRK RIGLCFGIHE EEYINDVKNI LNKLGIKYIE KIKDGSHSIL ISSKILAYVF ENILNCGINC YNKNIPPQMF NAKEEIKWEF LKGLFRGDGG IVRLNNNKNL NIEFATVSKK MAHSLLILLQ LLGIVASVKK CYNNKSTTMA YIIRINGLEQ VKKIGELFGK KWENYKDIAE SYKRNIEPLG YKKSDNFAIL EVKEIIKEHY SGYVYSVETE NSLLITSYGI LIHNCFPKDV KALIKQFENN NIEPILIKAT DIVNEEQIKW FFEKIKNYYG NLNGKTFAVL GLAFKPNTDD LRESRAIKLI DMLLESGAIV KGFDYVEKAR ENTINMYKLD KSKGFYGYNL YVLDDLYETV KNVDGIIITV EYDFNKEDWE KIGNLVKEKV VFDGRNILDV EKIKKLGFKY YGVGR // ID Y1069_METJA Reviewed; 392 AA. AC Q58469; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized glycosyltransferase MJ1069; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1069; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 4 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99071.1; -; Genomic_DNA. DR PIR; D64433; D64433. DR ProteinModelPortal; Q58469; -. DR STRING; 243232.MJ_1069; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR DNASU; 1451965; -. DR EnsemblBacteria; AAB99071; AAB99071; MJ_1069. DR KEGG; mja:MJ_1069; -. DR eggNOG; arCOG01403; Archaea. DR eggNOG; COG0438; LUCA. DR InParanoid; Q58469; -. DR OMA; ITFAGRV; -. DR PhylomeDB; Q58469; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 392 Uncharacterized glycosyltransferase FT MJ1069. FT /FTId=PRO_0000080322. SQ SEQUENCE 392 AA; 45820 MW; 264254846109A4E8 CRC64; MRKIKLIIFP GYYIPHIGGL ETHVDEFTKH LSEDENYDIY IFAPNIPKYK EFEIRHNNVK VYRYPAFEII PNYPVPNIFN IKFWRMFFNL YKIDFDIVMT RTRFFSNTLL GFIFAKLRFK KKKLIHVEHG SAFVKLESEF KNKLSYFYDK TIGKLIFKKA DYVVAISKAV KNFILENFVN DKDIPIIYRG LEIEKIESIG EDKKIKEKFK NKIKLCFVGR LYKWKGVENI IKAYVDLPKD LKEKIILIVV GYGEDLERLK KLAGNYLNNG IYFTGKVDFE KAIAIVKASD IYIHSSYKGG GLSSSLLQAM CCGKAIVASP YEGADEVVID GYNGILLKDN SPEEIKRGII KLIENNNLRK IYGENAKNFI KENFNWKKSV KEYKKIFERL VN // ID Y1092_METJA Reviewed; 214 AA. AC Q58492; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative nickel/cobalt efflux system MJ1092; GN OrderedLocusNames=MJ1092; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Efflux system for nickel and cobalt. {ECO:0000305}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the NiCoT transporter (TC 2.A.52) family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99093.1; -; Genomic_DNA. DR PIR; C64436; C64436. DR ProteinModelPortal; Q58492; -. DR STRING; 243232.MJ_1092; -. DR TCDB; 2.A.113.1.4; 2.a.113. the nickel/cobalt transporter (nico) family. DR EnsemblBacteria; AAB99093; AAB99093; MJ_1092. DR KEGG; mja:MJ_1092; -. DR eggNOG; arCOG03918; Archaea. DR eggNOG; COG2215; LUCA. DR InParanoid; Q58492; -. DR OMA; FILGMLH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0015099; F:nickel cation transmembrane transporter activity; IEA:InterPro. DR GO; GO:0006824; P:cobalt ion transport; IEA:UniProtKB-KW. DR InterPro; IPR011541; Ni/Co_transpt_high_affinity. DR InterPro; IPR017199; UCP037409_transporter. DR Pfam; PF09930; DUF2162; 1. DR Pfam; PF03824; NicO; 1. PE 3: Inferred from homology; KW Cell membrane; Cobalt; Cobalt transport; Complete proteome; KW Ion transport; Membrane; Nickel; Nickel transport; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 214 Putative nickel/cobalt efflux system FT MJ1092. FT /FTId=PRO_0000194015. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. SQ SEQUENCE 214 AA; 22704 MW; A21A318891B7891B CRC64; MVMIMELLYA ITAFILGMLH ALEPGHGKSV VAAYILGTKA DLKDAILLGT TITISHTAVI FLLGILSIYL LESLNVDVVH DMMSVVGGLI LIAVGIWIIR SYLHPHEHKV DTKKGVITLG LSAGLVPCPA ALAVLLLSIS SGNLIDGLIY VAIFSIGLAI SLTGLAVAFV ESKELIKKYV GNRKVSKLPL ISGSIIILIG LYTIAHPILE HAIV // ID Y1114_METJA Reviewed; 192 AA. AC Q58514; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1114; GN OrderedLocusNames=MJ1114; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99122.1; -; Genomic_DNA. DR PIR; A64439; A64439. DR ProteinModelPortal; Q58514; -. DR STRING; 243232.MJ_1114; -. DR EnsemblBacteria; AAB99122; AAB99122; MJ_1114. DR KEGG; mja:MJ_1114; -. DR eggNOG; arCOG05068; Archaea. DR eggNOG; ENOG410YMDG; LUCA. DR OMA; HYRSGFR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 192 Uncharacterized protein MJ1114. FT /FTId=PRO_0000107173. SQ SEQUENCE 192 AA; 21244 MW; AA414E24D0042C2A CRC64; MDIVEKVYKE GILKLKENIP QIIINLVVAG LIWVFGILVF IPIADMLGNP YLFGLTALKP IISAIITIAL IIVLLRVTKD FGELMDGIAD IIAVKLAGSR VNEEKLKKYR RGLRGLAYLI VAIIAYLFFL PVISGITPVL AGIVLIILVL WAVTVLINIG HIFSEEIEEG IRIATEKLEK ALEKSVKNEE NE // ID Y1132_METJA Reviewed; 118 AA. AC Q58532; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=UPF0058 protein MJ1132; GN OrderedLocusNames=MJ1132; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0058 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99134.1; -; Genomic_DNA. DR PIR; C64441; C64441. DR ProteinModelPortal; Q58532; -. DR STRING; 243232.MJ_1132; -. DR EnsemblBacteria; AAB99134; AAB99134; MJ_1132. DR KEGG; mja:MJ_1132; -. DR eggNOG; arCOG02254; Archaea. DR eggNOG; COG1745; LUCA. DR OMA; PHHIHRL; -. DR PhylomeDB; Q58532; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.1270.110; -; 1. DR InterPro; IPR002753; UPF0058. DR Pfam; PF01893; UPF0058; 1. DR SUPFAM; SSF140371; SSF140371; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 118 UPF0058 protein MJ1132. FT /FTId=PRO_0000135709. SQ SEQUENCE 118 AA; 13841 MW; EF55ED33865142B1 CRC64; MHKEQLMKLH QFFVYVVKEI MDDNLENTDN ECKKLFKIYE MLDIRPHHIH RLKSEQKAAI LLLSACVASY LANNMDNVPK NLAKKLEENA FKHLNSCKKN IIILEENENN GESAEKEE // ID Y1136_METJA Reviewed; 541 AA. AC Q58536; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Uncharacterized protein MJ1136; GN OrderedLocusNames=MJ1136; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99138.1; -; Genomic_DNA. DR PIR; G64441; G64441. DR ProteinModelPortal; Q58536; -. DR STRING; 243232.MJ_1136; -. DR DNASU; 1452032; -. DR EnsemblBacteria; AAB99138; AAB99138; MJ_1136. DR KEGG; mja:MJ_1136; -. DR eggNOG; arCOG01361; Archaea. DR eggNOG; COG1243; LUCA. DR InParanoid; Q58536; -. DR KO; K07739; -. DR OMA; CIETRPD; -. DR PhylomeDB; Q58536; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033588; C:Elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016573; P:histone acetylation; IBA:GOC. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR005910; Hist_AcTrfase_ELP3. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF13673; Acetyltransf_10; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR PIRSF; PIRSF005669; Hist_AcTrfase_ELP3; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR01211; ELP3; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 541 Uncharacterized protein MJ1136. FT /FTId=PRO_0000107183. FT DOMAIN 401 541 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 541 AA; 62443 MW; 31794B06F11E0BFD CRC64; MVIIMDEKAK LMRCIIERIL DEYNKGKTLD KKRIEQIKAE CLRIHRIGIG HPSNSEILQY ATEEEKKILI PILRKKPVRT ISGVAVVAVM TSPEKCPHGK CIFCPGGVGS VFGDVPQSYT GREPATMRGL MFNFDPYLQT KARIEQLEKV GHPTNKIELI IMGGTFPARD IEYQDWFIKR CLDAMNGVDA SSLEEAQKIN ETAEHRCVAL CIETRPDYCG EKEINQMLKL GATRVELGVQ TIYNEILEFC KRGHTVEDTI KATQLLKDSG LKVSYHLMPG MPGSDMEMDK KMFKEIFENP DFKPDMVKIY PCLVIEGTEL YEMWKRGEYK PYREEEAIEI ISYAKSIMPK WVRTSRIQRD IPATVIVDGV KKSNLGELVY KYMEKHGIKC KCIRCREVGH VMYKKGIMPD IEHIKLCREE YEASGGTEIF LSYEDVKNDI LIAFLRLREP YKPFRKEIDD NTMLVRQLHV CGQEKPLTKD LKEITWQHKG YGRKLLEEAE RIAKEEFGKK KILVTSGIGV REYYRKLGYE RVGAYMGKYL E // ID Y1138_METJA Reviewed; 174 AA. AC Q58538; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ1138; GN OrderedLocusNames=MJ1138; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99145.1; -; Genomic_DNA. DR PIR; A64442; A64442. DR ProteinModelPortal; Q58538; -. DR PRIDE; Q58538; -. DR EnsemblBacteria; AAB99145; AAB99145; MJ_1138. DR KEGG; mja:MJ_1138; -. DR eggNOG; arCOG03788; Archaea. DR eggNOG; ENOG410XUXB; LUCA. DR InParanoid; Q58538; -. DR OMA; SFDIYAL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR004864; LEA-14. DR InterPro; IPR013990; WHy-dom. DR Pfam; PF03168; LEA_2; 1. DR SMART; SM00769; WHy; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 174 Uncharacterized protein MJ1138. FT /FTId=PRO_0000107185. FT TRANSMEM 7 24 Helical. {ECO:0000255}. SQ SEQUENCE 174 AA; 18948 MW; CC03739B5FDF5764 CRC64; MKSVKKLLLL AFAVCLAVGF SGCLEQPKIE VVGQKIQKVD ADNTKIEIQV LVDNPNPIGI SIDKISFDIY ALVGGDKIYL GHGEQSNIKI TSGNTTFTLP VTISNKKLVE VALKEKSTKI PIEIKGDIAV NLFITKVNIP IDIQQEIDVS AIAKEEVLNQ LNNLNPNQIQ SIAQ // ID Y1147_METJA Reviewed; 462 AA. AC Q58547; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1147; GN OrderedLocusNames=MJ1147; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99156.1; -; Genomic_DNA. DR PIR; B64443; B64443. DR ProteinModelPortal; Q58547; -. DR STRING; 243232.MJ_1147; -. DR EnsemblBacteria; AAB99156; AAB99156; MJ_1147. DR KEGG; mja:MJ_1147; -. DR eggNOG; arCOG03128; Archaea. DR eggNOG; ENOG411279I; LUCA. DR OMA; IDRFVEC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001646; 5peptide_repeat. DR Pfam; PF13576; Pentapeptide_3; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 462 Uncharacterized protein MJ1147. FT /FTId=PRO_0000107188. FT TRANSMEM 381 401 Helical. {ECO:0000255}. FT TRANSMEM 433 453 Helical. {ECO:0000255}. SQ SEQUENCE 462 AA; 54433 MW; 91FF068862971776 CRC64; MFILIIKCGI MEKEVISSRE FIDRFVECLE KGEDFKLKDC VVEGNVDILN IYEMIKDKEL KGGYIEKKDD EIVVNINIKV DIYNVEFNGD FRFFVNMEYQ IVISVFNGNA YFRVITFKGS VYFIRTIFNG DVDFIDTIFE ENAYFSVTAF KGNIINFSGT IFNKESHFKS TTFEGNTYFS VTTFNIAEFY NSTFKSHVYF DDISFNLLSF TDCRFRDDVS FKKIDKENFK GLAIFLKTQF LNKHTTIENF QLSKTSFLKT DVREVLLCDV KKEEILSHKI LRIKEDSGNK DKDLENKLKE LLGLSYKYII DQFNYKSVLA EYRNLRISIE NNRTYIEASN LYKMEMELIK EFSNGRFEKF IIGAYGAISD YGESMEKTGK WILGSMILFT ILASILRFKG MEWDIFKIIE FWWISFWEVI RLFLQIGTED KSLWILEPII RVTSLILLGN LYIAVRRKLS RK // ID Y114_METJA Reviewed; 303 AA. AC Q57578; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0114; GN OrderedLocusNames=MJ0114; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98110.1; -; Genomic_DNA. DR PIR; B64314; B64314. DR ProteinModelPortal; Q57578; -. DR EnsemblBacteria; AAB98110; AAB98110; MJ_0114. DR KEGG; mja:MJ_0114; -. DR eggNOG; arCOG05023; Archaea. DR eggNOG; ENOG410YBFK; LUCA. DR OMA; NFCILNN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 303 Uncharacterized protein MJ0114. FT /FTId=PRO_0000106698. SQ SEQUENCE 303 AA; 34922 MW; D23B7C090A5837DA CRC64; MEKVYSKFGR IEDLKEIISG LVNFTGIIRI DNALLFYIDS KLISSKFNGR EKSLEEIFSQ IPDEFLIEIY QGNEKEVKSA LINFKPEESI VEISKLSLVF ENEVILNSYN DVYKYLTYIN KVIFMPKRFK NEKGIVVYKN KREVFAVYFG RKTLFGKKAI SKLKTTFAVS EIIAKIEKIS NEELNSLKNQ YPEGVLLFGD SINDVVKKII SSKKPIILEN VSLIDALSYG TCLIKIEGSE IGYIVAKDGK PVYAFLNDYD GEKSYRLLKS MCIVEDVKYS IYKLSKEEYD MFKTFQENKI PLS // ID Y1153_METJA Reviewed; 62 AA. AC Q58553; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1153; GN OrderedLocusNames=MJ1153; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99159.1; -; Genomic_DNA. DR PIR; H64443; H64443. DR STRING; 243232.MJ_1153; -. DR EnsemblBacteria; AAB99159; AAB99159; MJ_1153. DR KEGG; mja:MJ_1153; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 62 Uncharacterized protein MJ1153. FT /FTId=PRO_0000107191. SQ SEQUENCE 62 AA; 7619 MW; BE817CC65B3D3063 CRC64; MKENILKQKW AKIMKKHKYK KPKWLIKAEQ KAEKMTLEEE KEWIEKAIRV YKDKGIDGLF EI // ID Y1154_METJA Reviewed; 451 AA. AC Q58554; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Uncharacterized protein MJ1154; GN OrderedLocusNames=MJ1154; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HD domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99151.1; -; Genomic_DNA. DR PIR; A64444; A64444. DR ProteinModelPortal; Q58554; -. DR STRING; 243232.MJ_1154; -. DR PRIDE; Q58554; -. DR EnsemblBacteria; AAB99151; AAB99151; MJ_1154. DR KEGG; mja:MJ_1154; -. DR eggNOG; arCOG04430; Archaea. DR eggNOG; COG1078; LUCA. DR InParanoid; Q58554; -. DR KO; K06885; -. DR OMA; GKYHDDV; -. DR PhylomeDB; Q58554; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008832; F:dGTPase activity; IBA:GO_Central. DR GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 451 Uncharacterized protein MJ1154. FT /FTId=PRO_0000107192. FT DOMAIN 50 150 HD. SQ SEQUENCE 451 AA; 53001 MW; FA71589054E00C84 CRC64; MKVIRDSIHK DIYLDEKELE IIDSEEFQRL RNIKQTGLTY LVYPSANHTR FEHSLGTMFI ASKIAEKINA DVELTRVSAL LHDIGHPPFS HTLEICGYSH EVFGRKKIKH MNLDNFSKSE IIKTLNRKNL EGKIISGDVD ADRMDYLLRD SYHTGTAYGM IDLPRILRSI TTFESFGKVK IGILKKGIQA IESLLVARHQ MYSAVYMHPT VRIADTMIKR AVIKEIQEKN LDIKDLANMD DIALVSFLRI SENYLMERID RRNLYKNLIT YSYFDLNPIE KWIFVNLDEK QILSLESRFY EEFGWDIFID IYPIPKMEEH NVYIISDEGV KRLDEVSPLA QSLKPSEMRL WNISIYAPKE KIKELRENNV KDRINKILKE LDVKVESKLI DILKEYGTIT GKRRFLEIAK ERGISPKEFY NELHKLIFCG LIKERFNRRT YVYCLNNFVK L // ID Y1157_METJA Reviewed; 341 AA. AC Q58558; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=CTU1/ATPBD3 family protein MJ1157; GN OrderedLocusNames=MJ1157; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99161.1; -; Genomic_DNA. DR PIR; E64444; E64444. DR ProteinModelPortal; Q58558; -. DR STRING; 243232.MJ_1157; -. DR DNASU; 1452056; -. DR EnsemblBacteria; AAB99161; AAB99161; MJ_1157. DR KEGG; mja:MJ_1157; -. DR eggNOG; arCOG00042; Archaea. DR eggNOG; COG0037; LUCA. DR InParanoid; Q58558; -. DR OMA; QTILMNY; -. DR PhylomeDB; Q58558; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0034227; P:tRNA thio-modification; IEA:InterPro. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR020554; UPF0021_CS. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. DR TIGRFAMs; TIGR00269; TIGR00269; 1. DR PROSITE; PS01263; UPF0021; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 341 CTU1/ATPBD3 family protein MJ1157. FT /FTId=PRO_0000219891. SQ SEQUENCE 341 AA; 40094 MW; B87D2AC28D6C18C3 CRC64; MLDSPHNLYI KKFMLCYIIY YFLICHLYNH IFNLREIMLC SCGNEAFYYQ KYSNRHLCKE CFKKDIERRA KKVLGKDIIR NNVKIGIGIS GGKDSLVMAY ILKELFKHIP NAKLICFFVD EGIKGFRNIA EKYVKEFCKE YNLDLKIIKF EDEIGYTLDE IVKNDYLSKL NIGKPCSFCG VVRRYLLNKH ALKEGCDYLA IGHNLDDFCQ TILMNYVEGN IKNIIQFGKE FEGGGFVKRI KPLKLIPEEE VKLYAEINNI KYQREPCPYS SLSYRHRMKK VIEILEEEKP GVKFSILRGY EKLLKYLNVK EEIRRCEICG FPCSGNICKV CSWLIKLKEI K // ID Y1217_METJA Reviewed; 98 AA. AC Q58614; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1217; GN OrderedLocusNames=MJ1217; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99218.1; -; Genomic_DNA. DR PIR; H64451; H64451. DR ProteinModelPortal; Q58614; -. DR STRING; 243232.MJ_1217; -. DR EnsemblBacteria; AAB99218; AAB99218; MJ_1217. DR KEGG; mja:MJ_1217; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q58614; -. DR KO; K07075; -. DR OMA; YRIRSIA; -. DR PhylomeDB; Q58614; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein MJ1217. FT /FTId=PRO_0000107219. SQ SEQUENCE 98 AA; 11559 MW; 074E10CA476F74D1 CRC64; MKTLSEIKEI LRKHKKILKE KYKVKSIAIF GSYAREEQKE TSDIDILIDY YEPISLLKLI ELENYLSDLL GIKVDLITKN SIHNPYVKKS IEEDLIYI // ID Y1226_METJA Reviewed; 805 AA. AC Q58623; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 106. DE RecName: Full=Putative cation-transporting ATPase MJ1226; DE EC=3.6.3.-; GN OrderedLocusNames=MJ1226; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) CC (TC 3.A.3) family. Type IIIA subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99229.1; -; Genomic_DNA. DR PIR; A64453; A64453. DR ProteinModelPortal; Q58623; -. DR STRING; 243232.MJ_1226; -. DR TCDB; 3.A.3.3.4; the p-type atpase (p-atpase) superfamily. DR EnsemblBacteria; AAB99229; AAB99229; MJ_1226. DR KEGG; mja:MJ_1226; -. DR eggNOG; arCOG01578; Archaea. DR eggNOG; COG0474; LUCA. DR InParanoid; Q58623; -. DR KO; K01535; -. DR OMA; VGFWEEY; -. DR PhylomeDB; Q58623; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008553; F:hydrogen-exporting ATPase activity, phosphorylative mechanism; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0006754; P:ATP biosynthetic process; IEA:InterPro. DR GO; GO:1902600; P:hydrogen ion transmembrane transport; IBA:GOC. DR Gene3D; 1.20.1110.10; -; 2. DR Gene3D; 2.70.150.10; -; 2. DR Gene3D; 3.40.1110.10; -; 2. DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N. DR InterPro; IPR023299; ATPase_P-typ_cyto_domN. DR InterPro; IPR018303; ATPase_P-typ_P_site. DR InterPro; IPR023298; ATPase_P-typ_TM_dom. DR InterPro; IPR008250; ATPase_P-typ_transduc_dom_A. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006534; P-type_ATPase_IIIA. DR InterPro; IPR001757; P_typ_ATPase. DR Pfam; PF00690; Cation_ATPase_N; 1. DR Pfam; PF00122; E1-E2_ATPase; 1. DR PRINTS; PR00120; HATPASE. DR SMART; SM00831; Cation_ATPase_N; 1. DR SUPFAM; SSF56784; SSF56784; 2. DR SUPFAM; SSF81660; SSF81660; 1. DR TIGRFAMs; TIGR01647; ATPase-IIIA_H; 1. DR TIGRFAMs; TIGR01494; ATPase_P-type; 2. DR PROSITE; PS00154; ATPASE_E1_E2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Phosphoprotein; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 805 Putative cation-transporting ATPase FT MJ1226. FT /FTId=PRO_0000046427. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TRANSMEM 615 637 Helical. {ECO:0000255}. FT TRANSMEM 641 663 Helical. {ECO:0000255}. FT TRANSMEM 680 700 Helical. {ECO:0000255}. FT TRANSMEM 712 734 Helical. {ECO:0000255}. FT TRANSMEM 747 769 Helical. {ECO:0000255}. FT TRANSMEM 773 790 Helical. {ECO:0000255}. FT ACT_SITE 311 311 4-aspartylphosphate intermediate. FT {ECO:0000250}. SQ SEQUENCE 805 AA; 89618 MW; 8E63D3F7E47668CD CRC64; MWGVVMNVEE IEEEYKTSIK TGLSTEEAKK RLKIYGYNEI PEKKVHPIIK FLSYFWNPIA WMIEIAAILS AIIKHWVDFV IILILLLVNG VVGFWEEYKA ENVIEFLKQK MALNARVLRD GKWQIIPAKE LVPGDVVRIR IGDIVPADII LVDGDYLVVD ESALTGESLP VEKKIGDIAY SGSIVKKGEM TGIVKATGLN TYFGKTVKLV EKAEKVSSYQ KMIIKIGDYL IVLAVILIAI MVAVELFRGK SLIETAQFAL VLAVSAIPAA MPAVLSITMA IGALNLAKKD AIVKKLVAIE ELAGVDILCS DKTGTLTKNQ LVCGEIIALN GFSKEDVVLF AALASREEDA DAIDMAILNE AKKLGLMEKI KNYKIKKFIP FDPVIKRTEA EVTNDEEFKV SKGAPQVILD LCNADEELRR KVEEIVDKLA ENGYRALGVA VYKNGRWHFA GIIPLYDPPR EDAPLAVKKI KELGVIIKMV TGDHVAIAKN IARMLGIGDK IISISELLKK LKRGEIKEEK FDEIVEEADG FAEVFPEHKY KIVDSLQKRG HLVAMTGDGV NDAPALKKAD CGIAVSNATD AARAAADIVL LSPGISVIVD AIQEARRIFQ RMESYVIYRI TETIRILFFV ELCILILGIY PITALMIVLL AILNDIPILA IAYDNVVEPK SPVRWRMREI LMLSTALGLS GVVSSFLIFY ISDVFLHLTI AELQSFVFLK LILAGHATIF VTRIRDRLWK KPYPSKLLFW GVMGTNIIGT IVAAEGIFMA PIGWDLALFM WLYAHVWMLI NDEIKMILLK RLKID // ID Y1230_METJA Reviewed; 76 AA. AC Q58627; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1230; GN OrderedLocusNames=MJ1230; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99236.1; -; Genomic_DNA. DR PIR; E64453; E64453. DR STRING; 243232.MJ_1230; -. DR EnsemblBacteria; AAB99236; AAB99236; MJ_1230. DR KEGG; mja:MJ_1230; -. DR eggNOG; arCOG05073; Archaea. DR eggNOG; COG3478; LUCA. DR InParanoid; Q58627; -. DR KO; K07069; -. DR OMA; FDIQHNH; -. DR PhylomeDB; Q58627; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR018652; DUF2082_NA-bd_Znr. DR Pfam; PF09855; zinc_ribbon_13; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 76 Uncharacterized protein MJ1230. FT /FTId=PRO_0000107227. SQ SEQUENCE 76 AA; 8903 MW; 2C53E9EABEF0247C CRC64; MVIFMEKRWK CPKCGNTEFF EKEVAMTGTG LSKIFDIQHN EYIVITCKKC GYSEFYDKSI VKSKDNLMNI LDIFFG // ID Y1240_METJA Reviewed; 97 AA. AC Q58637; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ1240; GN OrderedLocusNames=MJ1240; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99245.1; -; Genomic_DNA. DR PIR; G64454; G64454. DR STRING; 243232.MJ_1240; -. DR EnsemblBacteria; AAB99245; AAB99245; MJ_1240. DR KEGG; mja:MJ_1240; -. DR eggNOG; arCOG01145; Archaea. DR eggNOG; COG2129; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ1240. FT /FTId=PRO_0000107233. SQ SEQUENCE 97 AA; 11401 MW; 2F4F613EA65576D7 CRC64; MEIKKSYKDY KKLVWNVSTE FTQALARIMF FYIVNDLETA KNLAKITSPY LPKVPSKLLK ELSEAIEEEI KAKSDIEKEK AKEKVKKAFV KLFYYTV // ID Y1241_METJA Reviewed; 71 AA. AC Q58638; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ1241; GN OrderedLocusNames=MJ1241; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99246.1; -; Genomic_DNA. DR PIR; H64454; H64454. DR ProteinModelPortal; Q58638; -. DR STRING; 243232.MJ_1241; -. DR EnsemblBacteria; AAB99246; AAB99246; MJ_1241. DR KEGG; mja:MJ_1241; -. DR eggNOG; arCOG01040; Archaea. DR eggNOG; COG0529; LUCA. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 71 Uncharacterized protein MJ1241. FT /FTId=PRO_0000107234. SQ SEQUENCE 71 AA; 8128 MW; 9D74BEE228F13AB4 CRC64; MVLKMEIKWY VKRGFEDNLI DALNTYGSAC VLGLAGMGKT TIARYIYTKL RREGVKVVYL TSDEESKTIK F // ID Y1252_METJA Reviewed; 251 AA. AC Q58648; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Uncharacterized protein MJ1252; GN OrderedLocusNames=MJ1252; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0638 and MJ1123 and M.tuberculosis CC Rv2003c. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99255.1; -; Genomic_DNA. DR PIR; B64456; B64456. DR ProteinModelPortal; Q58648; -. DR STRING; 243232.MJ_1252; -. DR EnsemblBacteria; AAB99255; AAB99255; MJ_1252. DR KEGG; mja:MJ_1252; -. DR eggNOG; arCOG01774; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q58648; -. DR OMA; FFGALNH; -. DR PhylomeDB; Q58648; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 251 Uncharacterized protein MJ1252. FT /FTId=PRO_0000107241. SQ SEQUENCE 251 AA; 29161 MW; BB12219F6E7201FF CRC64; MCKAFCSCYS YHYHHREKMG IKEYYDKLAK SYDKLYKNKY MRIVEREIIQ KEIKDGDFVL DIGCGTGEQL KILNNAVGLD ISLEMAKIAK NKTNKPVVVA NAEFLPFKNK SFDKAISFFG ALNHCNLKRA LREVNRVLKD DGIFIFTVAN IYDIKWIIKN ILKGNFKKVK NAMKKRKGTI TKVIDGEKIK VKTRFYDFKE VEDALKKEGF EVVYTFGTNI TNSPLDKFIY KSFLKNFASY IGFVAKKVKN R // ID Y1254_METJA Reviewed; 469 AA. AC Q58651; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1254; GN OrderedLocusNames=MJ1254; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99266.1; -; Genomic_DNA. DR PIR; E64456; E64456. DR ProteinModelPortal; Q58651; -. DR STRING; 243232.MJ_1254; -. DR PRIDE; Q58651; -. DR EnsemblBacteria; AAB99266; AAB99266; MJ_1254. DR KEGG; mja:MJ_1254; -. DR eggNOG; arCOG00391; Archaea. DR eggNOG; ENOG410Y1BI; LUCA. DR OMA; QVYIIVP; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 469 Uncharacterized protein MJ1254. FT /FTId=PRO_0000107242. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. SQ SEQUENCE 469 AA; 53926 MW; E4FBDDCA1C1E3453 CRC64; MIAFLFYKCF AKNYKINFLY KNSSYINTNT LWLKVIYIKT KDVIIFLLLF FVAFNVSSAY VIKNLNIDCI VTPDDTINET ISFVIYNNED KNLSHISYTI PQTIRNFTIN ASAGVKGYSA LYNEGVTEIA IEFEKPIPKG GYTNITINCF VNDAIWTKNG IKQLILSFPI TSKNATIKIV LPPGAVILSP QGTLLVTPSG YKITTDGKHQ IIVWDLSLNK EITFTITVKY TFISYPGQNI IEQPAINNNL KYLLIIAIFG TAIFGGLFVK EKISKRKIIE RTKNIKNELT SLKNKLKEKE EEIKNLAIKI KDLEDKLSKA NKNLLNKDEI ISVLNERISE YESQIQKLLD ENIIYKEKIE SLNKYIETLK KENDKLKDKV RELSDIAKKY MEEKRGVLWS FLTEDEKIII DLIKKHGHIT QKEIVEITGM SKPKVSRIIS ELEDRKIIRK EKIGRINKLT LTEESKKLL // ID Y1255_METJA Reviewed; 394 AA. AC Q58652; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 06-JUN-2003, sequence version 2. DT 11-MAY-2016, entry version 79. DE RecName: Full=Uncharacterized glycosyltransferase MJ1255; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1255; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase 28 family. CC {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99267.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99267.1; ALT_INIT; Genomic_DNA. DR PIR; F64456; F64456. DR ProteinModelPortal; Q58652; -. DR STRING; 243232.MJ_1255; -. DR CAZy; GT1; Glycosyltransferase Family 1. DR EnsemblBacteria; AAB99267; AAB99267; MJ_1255. DR KEGG; mja:MJ_1255; -. DR eggNOG; arCOG01393; Archaea. DR eggNOG; COG1819; LUCA. DR InParanoid; Q58652; -. DR OMA; FGHTTRC; -. DR PhylomeDB; Q58652; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043231; C:intracellular membrane-bounded organelle; IBA:GO_Central. DR GO; GO:0008194; F:UDP-glycosyltransferase activity; IBA:GO_Central. DR GO; GO:0009813; P:flavonoid biosynthetic process; IBA:GO_Central. DR GO; GO:0052696; P:flavonoid glucuronidation; IBA:GO_Central. DR InterPro; IPR005262; CHP00661. DR InterPro; IPR007235; Glyco_trans_28_C. DR Pfam; PF04101; Glyco_tran_28_C; 1. DR TIGRFAMs; TIGR00661; MJ1255; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 394 Uncharacterized glycosyltransferase FT MJ1255. FT /FTId=PRO_0000215619. SQ SEQUENCE 394 AA; 45637 MW; 9BAABAE2903328AD CRC64; MKILISVCGE GFGHTTRCVA IGEALKNDYE ISYIAYGKSK NFIEKYGFKV FETFPEIKLK GKDGKFDITS SILNKEYSPK KAIRREINII REYNPDLIIS DCKYSTVVAA KLLKKPVICI SNQNYTRYKL KTDLIVYPTM KALNIINERC ERFIVPDFPL PYTICEYNLK IIKNMEFIGP LIRYDVDDVD NYGEDYILSV IGGFEYRYKI LEELGKIALK NNLNVKLVCG SYEVAKKLMR DLNLNSYKNE NVEIIPITTN MKELIKNAEL IVSHGGHSTI MEALSFGKPL IVIPDLDHPE QGNNAKKVHD LGCGIALSYK ELYRLEEAIL DIRNMKMYKR NASKMKELAK KYDGKKNIKK IIDEFFETRK NIRKYYLTDR IANKLINKFK LKIR // ID Y127_METJA Reviewed; 121 AA. AC Q57591; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0331 protein MJ0127; GN OrderedLocusNames=MJ0127; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0331 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98107.1; -; Genomic_DNA. DR PIR; G64315; G64315. DR ProteinModelPortal; Q57591; -. DR STRING; 243232.MJ_0127; -. DR EnsemblBacteria; AAB98107; AAB98107; MJ_0127. DR KEGG; mja:MJ_0127; -. DR eggNOG; arCOG05024; Archaea. DR eggNOG; COG2361; LUCA. DR InParanoid; Q57591; -. DR OMA; DIVWDVI; -. DR PhylomeDB; Q57591; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 121 UPF0331 protein MJ0127. FT /FTId=PRO_0000158260. SQ SEQUENCE 121 AA; 14358 MW; FA3526010E173FEA CRC64; MPKKDVRAFL YDILENMKDI IDFTNDMTFD EFLKDKKTQK AVIRSLEVIG EAVKNLPEDF INKYPQVPWK GMARLRDKLI HHYFGINYEI IWDIVINKVP NDIKEIEEII KDIEGEDENS I // ID Y1292_METJA Reviewed; 552 AA. AC Q58688; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ1292; GN OrderedLocusNames=MJ1292; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99308.1; -; Genomic_DNA. DR ProteinModelPortal; Q58688; -. DR STRING; 243232.MJ_1292; -. DR EnsemblBacteria; AAB99308; AAB99308; MJ_1292. DR KEGG; mja:MJ_1292; -. DR eggNOG; arCOG05057; Archaea. DR eggNOG; ENOG410YACR; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 552 Uncharacterized protein MJ1292. FT /FTId=PRO_0000107258. SQ SEQUENCE 552 AA; 63978 MW; A4B5B14354B29159 CRC64; MKFKYIVLLF ALSLALITVN GLEIKDIDYS DSSQYLIITV SNPDNNINAN ISIIGYIDNK IDTQVEMFNY SIPKYSLMFI RKKMVFNEKG VHTVFVTIKS NNITYTFYKK INITYAYNSK VPVPEEEVTK KIEIEGLEFE ICPYPYPPFY DFVYVTIRNN DYVPHYVNIS FTASLQGTYY IIKDNKIIKS NPPSNGLIIK SWTPNVYVPP KSKIIIPIKV NFYYSGKYTI TVKAVSDNHY STEKTVKGNT VILKSLFGDE IKVYNVEIAC PLYVYNVRCE DEYGDYAYSN WFDVDVNNTV DYDVYGTLQV FLCKKEGDNY LILNNKTINK YFLAKEFNDG YSIPVKLNTS ALNPYDENFT IFVLCKTGNM ESFYYKTFTK PIKINSLEVK NYPEHYYFVD ESIFYDVYVN VTNNLNKKIY ANISIKDIYN KTYSKEVELN KSCVNIIKFS GLKINAKDLS HDGKIKLKFI VTAITPPYEK YYIIKKNISI NLSLIPTPPV YLCSNLNDEI FVGYPQNLSF SLKKVVGRCV ETRVYITVPD DIKKYTILKR SI // ID Y1370_METJA Reviewed; 328 AA. AC Q58765; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=UPF0285 protein MJ1370 {ECO:0000255|HAMAP-Rule:MF_01087}; GN OrderedLocusNames=MJ1370; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0285 family. {ECO:0000255|HAMAP- CC Rule:MF_01087}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99387.1; -; Genomic_DNA. DR PIR; A64471; A64471. DR ProteinModelPortal; Q58765; -. DR STRING; 243232.MJ_1370; -. DR PRIDE; Q58765; -. DR EnsemblBacteria; AAB99387; AAB99387; MJ_1370. DR KEGG; mja:MJ_1370; -. DR eggNOG; arCOG04885; Archaea. DR eggNOG; COG4020; LUCA. DR InParanoid; Q58765; -. DR OMA; DHGTSGI; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01087; UPF0285; 1. DR InterPro; IPR016735; UPF0285_methan. DR PIRSF; PIRSF018783; UCP018783; 1. DR TIGRFAMs; TIGR03281; methan_mark_12; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 328 UPF0285 protein MJ1370. FT /FTId=PRO_0000151262. SQ SEQUENCE 328 AA; 35980 MW; AC96B0820123FACF CRC64; MITVGIDHGT SGITTCIKDN DKKIIFKLKR TELKEKSYLE ELEKHISLED IDLIALTYSM GDGINKILPI EKVKNRGVLS IEGAGEKVGG GTKVYDEIKE SGLPAVVIPG LHRGIECLDE RFRALYSHIA SPEKVSIAYY AYKLFGFNDF VLSDISSNTV TLLIKDGKIF GGFDACIGAI GMLHGPIDLE MIRDIDAGKI TANEAFSKAG AVKIAKLYKG VENTKEEIIN NYFNDENCRL AVDSLILSVS MEINSLLPLL DKNKRRVVLA GSIGTLRNPI DIPKRIKEFV EAKIFVLYGE SGAIGGALIA EDILKGKRDI LGIEVEFK // ID Y1374_METJA Reviewed; 266 AA. AC Q58769; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 73. DE RecName: Full=Uncharacterized protein MJ1374; GN OrderedLocusNames=MJ1374; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99381.1; -; Genomic_DNA. DR PIR; E64471; E64471. DR ProteinModelPortal; Q58769; -. DR STRING; 243232.MJ_1374; -. DR EnsemblBacteria; AAB99381; AAB99381; MJ_1374. DR KEGG; mja:MJ_1374; -. DR eggNOG; arCOG00499; Archaea. DR eggNOG; COG1235; LUCA. DR InParanoid; Q58769; -. DR OMA; PTTIGFR; -. DR PhylomeDB; Q58769; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042781; F:3'-tRNA processing endoribonuclease activity; IBA:GO_Central. DR GO; GO:0034414; P:tRNA 3'-trailer cleavage, endonucleolytic; IBA:GOC. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF12706; Lactamase_B_2; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 266 Uncharacterized protein MJ1374. FT /FTId=PRO_0000107303. SQ SEQUENCE 266 AA; 29920 MW; 5B6831CA308F2426 CRC64; MRVEIIFLGC GGGRWATITQ KKATGGFRIH TNELRMHVDP GPGAIVRLNE LKISPWRTNA LFISHCHPDH YTDGEIIVEA ITQGMTKKRG VFLGSLSVVE GFGEYEYVVS KYHQSKLEEV RVLYPGDSAE LYDTTIKATH TKHGDPFGIG FRLSTIYGDI GYTSDTEFIP QLIEDFDGVR ILIANIVRKK NERIKGHLCS NDAIDLINSM NKKPELLIMN HMGVKMTNPQ IEAEYISQNT GIEVIPARLG LKVELLNGKY KYQLIK // ID Y1380_METJA Reviewed; 78 AA. AC Q58775; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=UPF0331 protein MJ1380; GN OrderedLocusNames=MJ1380; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0331 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99390.1; -; Genomic_DNA. DR PIR; C64472; C64472. DR STRING; 243232.MJ_1380; -. DR EnsemblBacteria; AAB99390; AAB99390; MJ_1380. DR KEGG; mja:MJ_1380; -. DR eggNOG; arCOG05024; Archaea. DR eggNOG; COG2361; LUCA. DR InParanoid; Q58775; -. DR OMA; PNVPWKE; -. DR PhylomeDB; Q58775; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 78 UPF0331 protein MJ1380. FT /FTId=PRO_0000158264. SQ SEQUENCE 78 AA; 9306 MW; 3FAC5FE9CED507C1 CRC64; MSKRDVKAFL YDILESANDV IEFTKDIDYN EFINNKMIRY AVIRALEIIG EASRYINNDF REKFPNVPWK EMVGLRNI // ID Y1410_METJA Reviewed; 159 AA. AC Q58805; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=UPF0113 protein MJ1410; GN OrderedLocusNames=MJ1410; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0113 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99417.1; -; Genomic_DNA. DR PIR; A64476; A64476. DR ProteinModelPortal; Q58805; -. DR STRING; 243232.MJ_1410; -. DR EnsemblBacteria; AAB99417; AAB99417; MJ_1410. DR KEGG; mja:MJ_1410; -. DR eggNOG; arCOG00993; Archaea. DR eggNOG; COG1374; LUCA. DR InParanoid; Q58805; -. DR KO; K07565; -. DR OMA; VFNKNRE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR005155; Rbsml_synth_fac_NIP7-like. DR Pfam; PF03657; UPF0113; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 159 UPF0113 protein MJ1410. FT /FTId=PRO_0000159748. SQ SEQUENCE 159 AA; 18506 MW; BFA9572469EFAAC1 CRC64; MKVRKLKNAE INLIEEELSK YTDKDFVKSF KYENLIVLEG KWLTVCYTNI ETIKKLNMFQ DIFSVGNVFG EIKRKFRLSL EGFTLISPNI INNYAIVNEK AEALFLYGRD IFKESIIEVK GFGRIAVFNK NREFLGIGLF DGKIIKNIKD KGWYLREGG // ID Y1416_METJA Reviewed; 452 AA. AC Q58811; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1416; GN OrderedLocusNames=MJ1416; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99426.1; -; Genomic_DNA. DR PIR; G64476; G64476. DR ProteinModelPortal; Q58811; -. DR STRING; 243232.MJ_1416; -. DR DNASU; 1452319; -. DR EnsemblBacteria; AAB99426; AAB99426; MJ_1416. DR KEGG; mja:MJ_1416; -. DR eggNOG; arCOG00637; Archaea. DR eggNOG; COG1973; LUCA. DR InParanoid; Q58811; -. DR KO; K07388; -. DR OMA; IGGDMVI; -. DR PhylomeDB; Q58811; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR009186; Ni_metllenz_mat. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR006283; ThiL. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF006346; Ni_metllenz_mat; 1. DR SUPFAM; SSF56042; SSF56042; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 452 Uncharacterized protein MJ1416. FT /FTId=PRO_0000201463. SQ SEQUENCE 452 AA; 50076 MW; 8B4C364CEDBABF92 CRC64; MMDLEGYVRR CLRKKIPENK IIEDGFKRIL EIKEDVDEEF AKKFIKAILE EVKTTEKFRE IDDENLKTLL KYPKSGVTMG RMGVGSRGEG DFFVHREIAR IVKSTKVKAY VSAEEQDDAG IVRADAKYIV AAIDGTHSRL SDFPFLGGFH VTRAALRDIY VMGAEAVALI SDVHLADDGD VGKIFDFTAG ICAVSEAVNV PLIGGSTLRV GGDMVIGDRL VSAVGAIGVI KEGEPTARRN AEVGDVILMT EGSGGGTITT TALYYGWFDV IYETLNVDFI KACQNLIRSG LIKKIHAMTD VTNGGLRGDA YEISKTAKVS LIFDKEKVYK TINPKVLEML EVLNIDPLGV STDSLMIICP EEYADDIKKV TGAIEVGYVE EGEESYLVDG NKKIPLKPMF RESAYTPVKK VVGERKPGDF EEMKEKVRRA CDEAIKKKDF VVELLKERKK KF // ID Y1433_METJA Reviewed; 247 AA. AC Q58828; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1433; GN OrderedLocusNames=MJ1433; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99443.1; -; Genomic_DNA. DR PIR; H64478; H64478. DR ProteinModelPortal; Q58828; -. DR STRING; 243232.MJ_1433; -. DR EnsemblBacteria; AAB99443; AAB99443; MJ_1433. DR KEGG; mja:MJ_1433; -. DR eggNOG; arCOG03165; Archaea. DR eggNOG; ENOG4111GI4; LUCA. DR OMA; LWAVFHL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 247 Uncharacterized protein MJ1433. FT /FTId=PRO_0000107325. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. SQ SEQUENCE 247 AA; 29480 MW; 1C88A2B8EB4B304D CRC64; MNDKRYMLII AICLIFLSIL VYSIHFLIFG KVDYILSYFL LHLAFVPIEV LLVSLIIEKI LDYREKKKIL EKLNMVVGSF FNSVGEELLK IILEGDVGNI RDYLKISDEW NDKTYEETKK LLMNYDCNID IEKIDLYKLK NLLERNKEFL LRLMENPLLL EHESFTELLL AVFHLADELH RREDLSNLPK SDLDHLKNDI IRVYKLLIIQ WLNYLMHLKD NYPYLYSLCL RANPFDNKSI IIEEDDK // ID Y1435_METJA Reviewed; 71 AA. AC Q58830; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 74. DE RecName: Full=Uncharacterized protein MJ1435; GN OrderedLocusNames=MJ1435; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99450.1; -; Genomic_DNA. DR PIR; B64479; B64479. DR PDB; 2QTX; X-ray; 2.50 A; A/B/C/D/E/F/G/H/I/J/K/L=1-71. DR PDB; 4X9C; X-ray; 1.40 A; A/B/C/D/E/F=1-71. DR PDB; 4X9D; X-ray; 1.50 A; A/B/C/D/E/F=1-71. DR PDBsum; 2QTX; -. DR PDBsum; 4X9C; -. DR PDBsum; 4X9D; -. DR ProteinModelPortal; Q58830; -. DR SMR; Q58830; 14-71. DR STRING; 243232.MJ_1435; -. DR EnsemblBacteria; AAB99450; AAB99450; MJ_1435. DR KEGG; mja:MJ_1435; -. DR eggNOG; arCOG08275; Archaea. DR eggNOG; COG1923; LUCA. DR KO; K03666; -. DR OMA; KHAIDYI; -. DR EvolutionaryTrace; Q58830; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR010920; LSM_dom. DR SUPFAM; SSF50182; SSF50182; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 71 Uncharacterized protein MJ1435. FT /FTId=PRO_0000107326. FT HELIX 20 23 {ECO:0000244|PDB:4X9C}. FT STRAND 27 32 {ECO:0000244|PDB:4X9C}. FT STRAND 37 45 {ECO:0000244|PDB:4X9C}. FT STRAND 47 54 {ECO:0000244|PDB:4X9C}. FT STRAND 57 62 {ECO:0000244|PDB:4X9C}. FT HELIX 63 65 {ECO:0000244|PDB:4X9C}. FT STRAND 66 71 {ECO:0000244|PDB:4X9C}. SQ SEQUENCE 71 AA; 8295 MW; AC1B6AF9651500EB CRC64; MNKPVKKQQP KKVIPNFEYA RRLNGKKVKI FLRNGEVLDA EVTGVSNYEI MVKVGDRNLL VFKHAIDYIE Y // ID Y1471_METJA Reviewed; 178 AA. AC Q58866; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1471; GN OrderedLocusNames=MJ1471; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99486.1; -; Genomic_DNA. DR PIR; F64483; F64483. DR ProteinModelPortal; Q58866; -. DR STRING; 243232.MJ_1471; -. DR EnsemblBacteria; AAB99486; AAB99486; MJ_1471. DR KEGG; mja:MJ_1471; -. DR eggNOG; arCOG05085; Archaea. DR eggNOG; ENOG410YJ0S; LUCA. DR OMA; NRSEGWY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 178 Uncharacterized protein MJ1471. FT /FTId=PRO_0000107357. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 178 AA; 20692 MW; 23B5B6625792B4EE CRC64; MINSVDLAIG TAILLIGMAY WTVSIVEHNN NYVDIVKSDY IFDKGISTME HLSEDGTLQD AVLLYYFDRV NDSKKLLEER IPLKHYLLYI DNNLLINKSN GVNNSNSVYI LTVLTLNRSE GWYVIYGNED FVNISKERFL DYDDAYNYLK YRNYDIHMPV YLSKNVSSSR VELYILGN // ID Y1477_METJA Reviewed; 346 AA. AC Q58872; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein MJ1477; GN OrderedLocusNames=MJ1477; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99489.1; -; Genomic_DNA. DR PIR; D64484; D64484. DR ProteinModelPortal; Q58872; -. DR SMR; Q58872; 70-339. DR STRING; 243232.MJ_1477; -. DR EnsemblBacteria; AAB99489; AAB99489; MJ_1477. DR KEGG; mja:MJ_1477; -. DR eggNOG; arCOG07957; Archaea. DR eggNOG; COG2342; LUCA. DR InParanoid; Q58872; -. DR KO; K01884; -. DR OMA; PIAYISI; -. DR PhylomeDB; Q58872; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR016063; Extracellular_prot. DR InterPro; IPR004352; GH114_TIM-barrel. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR InterPro; IPR016062; TM1410-rel. DR Pfam; PF03537; Glyco_hydro_114; 1. DR PRINTS; PR01545; THEMAYE10DUF. DR SUPFAM; SSF51445; SSF51445; 1. DR TIGRFAMs; TIGR01370; TIGR01370; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 346 Uncharacterized protein MJ1477. FT /FTId=PRO_0000107359. FT TRANSMEM 16 36 Helical. {ECO:0000255}. SQ SEQUENCE 346 AA; 40620 MW; A71B3D69A956BFCE CRC64; MHLNKIRGKN MKKSHILGII ICIILIVGFF ISFDSTFLDN PKMMSKSKNN IRNAENLTNI SKNSNNLKFL WAYQLQNADI DEIANSNFTL IVIDYSKDGT ENGKYSEEEI EKLKKAGKIP IAYISIGEAE DYRFYWDNEW LKNPPKWLGD ENPEWEGCYA VKYWHPEWKK IIFSYLDKII QQGFCGVYLD KVDEFEYWAE NGYDEDFTAK EMIKFIVEIS NYCRNKTNNS FIIIPQNGER LLEYDKHGKL LNTVSGWAVE DLFYDGVEQK TEEEINERIK LLDKVKDSGK FVLVVDYVDD GTKTNENLKR VEDFINKSLD KGYVPYVAKS DRELDELNTW WLKLIN // ID WECB_METJA Reviewed; 366 AA. AC Q58899; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 83. DE RecName: Full=UDP-N-acetylglucosamine 2-epimerase; DE EC=5.1.3.14; DE AltName: Full=UDP-GlcNAc-2-epimerase; GN Name=wecB; OrderedLocusNames=MJ1504; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Catalyzes the reversible epimerization at C-2 of UDP-N- CC acetylglucosamine (UDP-GlcNAc) to produce UDP-N-acetylmannosamine CC (UDP-ManNAc), the activated donor of ManNAc residues. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: UDP-N-acetyl-alpha-D-glucosamine = UDP-N- CC acetyl-alpha-D-mannosamine. CC -!- SUBUNIT: Homodimer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the UDP-N-acetylglucosamine 2-epimerase CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99517.1; -; Genomic_DNA. DR PIR; G64487; G64487. DR PDB; 4NEQ; X-ray; 2.85 A; A=1-366. DR PDB; 4NES; X-ray; 1.42 A; A=1-366. DR PDBsum; 4NEQ; -. DR PDBsum; 4NES; -. DR ProteinModelPortal; Q58899; -. DR STRING; 243232.MJ_1504; -. DR EnsemblBacteria; AAB99517; AAB99517; MJ_1504. DR KEGG; mja:MJ_1504; -. DR eggNOG; arCOG01392; Archaea. DR eggNOG; COG0381; LUCA. DR InParanoid; Q58899; -. DR KO; K01791; -. DR OMA; RTETEWV; -. DR PhylomeDB; Q58899; -. DR BRENDA; 5.1.3.14; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008761; F:UDP-N-acetylglucosamine 2-epimerase activity; IEA:UniProtKB-EC. DR InterPro; IPR003331; UDP_GlcNAc_Epimerase_2_dom. DR InterPro; IPR029767; WecB-like. DR Pfam; PF02350; Epimerase_2; 1. DR TIGRFAMs; TIGR00236; wecB; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Cytoplasm; Isomerase; KW Reference proteome. FT CHAIN 1 366 UDP-N-acetylglucosamine 2-epimerase. FT /FTId=PRO_0000208535. FT ACT_SITE 207 207 {ECO:0000250}. FT STRAND 3 7 {ECO:0000244|PDB:4NES}. FT HELIX 10 23 {ECO:0000244|PDB:4NES}. FT STRAND 30 34 {ECO:0000244|PDB:4NES}. FT HELIX 41 43 {ECO:0000244|PDB:4NES}. FT HELIX 45 50 {ECO:0000244|PDB:4NES}. FT STRAND 57 59 {ECO:0000244|PDB:4NES}. FT HELIX 67 85 {ECO:0000244|PDB:4NES}. FT STRAND 88 96 {ECO:0000244|PDB:4NES}. FT HELIX 97 108 {ECO:0000244|PDB:4NES}. FT STRAND 112 117 {ECO:0000244|PDB:4NES}. FT HELIX 128 138 {ECO:0000244|PDB:4NES}. FT STRAND 141 147 {ECO:0000244|PDB:4NES}. FT HELIX 148 156 {ECO:0000244|PDB:4NES}. FT HELIX 161 163 {ECO:0000244|PDB:4NES}. FT STRAND 164 166 {ECO:0000244|PDB:4NES}. FT HELIX 170 183 {ECO:0000244|PDB:4NES}. FT HELIX 186 195 {ECO:0000244|PDB:4NES}. FT STRAND 201 205 {ECO:0000244|PDB:4NES}. FT HELIX 209 212 {ECO:0000244|PDB:4NES}. FT HELIX 215 232 {ECO:0000244|PDB:4NES}. FT STRAND 235 239 {ECO:0000244|PDB:4NES}. FT HELIX 242 250 {ECO:0000244|PDB:4NES}. FT HELIX 254 259 {ECO:0000244|PDB:4NES}. FT STRAND 263 266 {ECO:0000244|PDB:4NES}. FT HELIX 271 280 {ECO:0000244|PDB:4NES}. FT STRAND 282 286 {ECO:0000244|PDB:4NES}. FT HELIX 289 298 {ECO:0000244|PDB:4NES}. FT STRAND 302 304 {ECO:0000244|PDB:4NES}. FT HELIX 313 316 {ECO:0000244|PDB:4NES}. FT STRAND 319 322 {ECO:0000244|PDB:4NES}. FT HELIX 327 338 {ECO:0000244|PDB:4NES}. FT HELIX 353 363 {ECO:0000244|PDB:4NES}. SQ SEQUENCE 366 AA; 41726 MW; E40DA8E87B835416 CRC64; MKLSIILGTR PEIIKLSPII RALEKTNIDW HIIHTNQHYS ENMDKIFFEE LNLPNPKYNL NIGSGTHGEQ TGKMLIEIEK VLLKEKPDVV VVQGDTNTVL AGALVASKLK IDVAHVEAGL RSFDRNMPEE INRVLTDHIS SYLFAPTEIA KNNLLREGIE ENKIFVVGNT IVDATLQNLK IAEKNENVRA FFNSVVIDDD YFLLTLHRAE NVDNKERLKN IVEGIFEIIE IYDKAIIFSI HPRTKKRLKE FNLFDKLKSN KKIKIIEPVG YLEFLMLEKN AELILTDSGG VQEEACILKV PCITLRDNTE RPETVEVGAN ILVGDNKEKL IKAVEIMLNK KRNWKNPFGN GKSGERIVRI LTYGKY // ID WTPB_METJA Reviewed; 249 AA. AC Q58763; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Molybdate/tungstate transport system permease protein WtpB; GN Name=wtpB; OrderedLocusNames=MJ1368; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in CC molybdate/tungstate import. Probably responsible for the CC translocation of the substrate across the membrane (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (WtpC), two transmembrane proteins (WtpB) and a solute-binding CC protein (WtpA). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99376.1; -; Genomic_DNA. DR PIR; G64470; G64470. DR ProteinModelPortal; Q58763; -. DR STRING; 243232.MJ_1368; -. DR TCDB; 3.A.1.6.9; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAB99376; AAB99376; MJ_1368. DR KEGG; mja:MJ_1368; -. DR eggNOG; arCOG00164; Archaea. DR eggNOG; COG0555; LUCA. DR InParanoid; Q58763; -. DR KO; K15496; -. DR OMA; IPFMINS; -. DR PhylomeDB; Q58763; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Molybdenum; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 249 Molybdate/tungstate transport system FT permease protein WtpB. FT /FTId=PRO_0000060308. FT TOPO_DOM 1 5 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 6 26 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 27 48 Extracellular. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 70 93 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 115 116 Extracellular. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 138 177 Cytoplasmic. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 199 223 Extracellular. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TOPO_DOM 245 249 Cytoplasmic. {ECO:0000255}. FT DOMAIN 45 240 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 249 AA; 27942 MW; 3359BC2A3EB48675 CRC64; MEKFDIAMTV FLVMIFLFIF LPIIYMLSNP GDLNQLLDKE VIEAFKTTLL AGAVATLIAL IFGIPTGYIL ARYDFKFKSF VEAVLDLPMA IPHSVIGIII LSFIYGIDII NFIGRYVVDN FWGIVTVYLF VGIPFMVNSI RDGFLSVDEE IEYVSRTLGA SKIRTFFEIS LPLIKNNIIS GIILSFARGI SEVGAILIIA YYPKTVPILI YERFMSFGLD ASKPISVGMI LISIALFALL RMFGRMRGR // ID WTPC_METJA Reviewed; 297 AA. AC Q58762; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 104. DE RecName: Full=Molybdate/tungstate import ATP-binding protein WtpC; DE EC=3.6.3.-; GN Name=wtpC; OrderedLocusNames=MJ1367; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in CC molybdate/tungstate import. Responsible for energy coupling to the CC transport system (By similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (WtpC), two transmembrane proteins (WtpB) and a solute-binding CC protein (WtpA). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC Sulfate/tungstate importer (TC 3.A.1.6) family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99375.1; -; Genomic_DNA. DR PIR; F64470; F64470. DR ProteinModelPortal; Q58762; -. DR SMR; Q58762; 1-228. DR STRING; 243232.MJ_1367; -. DR TCDB; 3.A.1.6.9; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAB99375; AAB99375; MJ_1367. DR KEGG; mja:MJ_1367; -. DR eggNOG; arCOG00175; Archaea. DR eggNOG; COG3839; LUCA. DR InParanoid; Q58762; -. DR KO; K15497; -. DR OMA; FGCTILF; -. DR PhylomeDB; Q58762; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0015412; F:molybdate transmembrane-transporting ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR030283; WtpC. DR PANTHER; PTHR24220:SF421; PTHR24220:SF421; 1. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Molybdenum; Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 297 Molybdate/tungstate import ATP-binding FT protein WtpC. FT /FTId=PRO_0000093225. FT DOMAIN 2 226 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 32 39 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 297 AA; 33266 MW; 710DB22733EEB122 CRC64; MLKVNNLSKI WKDFKLKNVS FEIDREYCVI LGPSGAGKSV LIKCIAGILK PDSGRIILNG EDITNLPPEK RNVGYVPQNY ALFPNKNVYK NIAYGLIIKK VNKLEIDRKV KEIAEFLNIS HLLNRDVKTL SGGEQQRVAL ARALILNPSI LLLDEPTSAV DIKIKESIIS ELKKIKHIPV LHITHDLAEA RTLGEKVGIF MNGELIAFGD KSILKKPKNK KVAEFLGFNI IDDKAIAPED VIIKDGNGGE VVNIIDYGKY KKVFVKYNGY IIKAFTERDL NIGDNVGLEF REQTKLT // ID Y002_METJA Reviewed; 243 AA. AC Q60312; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0002; GN OrderedLocusNames=MJ0002; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97989.1; -; Genomic_DNA. DR PIR; B64300; B64300. DR STRING; 243232.MJ_0002; -. DR EnsemblBacteria; AAB97989; AAB97989; MJ_0002. DR KEGG; mja:MJ_0002; -. DR eggNOG; COG3541; LUCA. DR InParanoid; Q60312; -. DR KO; K07074; -. DR OMA; CICKKLY; -. DR PhylomeDB; Q60312; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR018775; NucleotidylTrfase_prd. DR Pfam; PF10127; Nuc-transf; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 243 Uncharacterized protein MJ0002. FT /FTId=PRO_0000106645. SQ SEQUENCE 243 AA; 28492 MW; 2B1BE2C59F816CB9 CRC64; MEIFMEVPIF VVISGSDLYG IPNPSDVDIR GAHILDRELF IKNCLYKSKE EEVINKMFGK CDFVSFELGK FLRELLKPNA NFIEIALSDK VLYSSKYHED VKGIAYNCIC KKLYHHWKGF AKPLQKLCEK ESYNNPKTLL YILRAYYQGI LCLESGEFKS DFSSFRCLDC YDEDIVSYLF ECKVNKKPVD ESYKKKIKSY FYELGVLLDE SYKNSNLIDE PSETAKIKAI ELYKKLYFED VRE // ID Y003_METJA Reviewed; 156 AA. AC Q60313; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0003; GN OrderedLocusNames=MJ0003; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97990.1; -; Genomic_DNA. DR PIR; C64300; C64300. DR STRING; 243232.MJ_0003; -. DR EnsemblBacteria; AAB97990; AAB97990; MJ_0003. DR KEGG; mja:MJ_0003; -. DR eggNOG; arCOG02433; Archaea. DR eggNOG; COG5418; LUCA. DR InParanoid; Q60313; -. DR OMA; ELIYLGI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 156 Uncharacterized protein MJ0003. FT /FTId=PRO_0000106646. SQ SEQUENCE 156 AA; 18429 MW; 364797DB0EE38AB9 CRC64; MKGKRIAIVS HRILNQNSVV NGLERAEGAF NEVVEILLKN NYGIIQLPCP ELIYLGIDRE GKTKEEYDTK EYRELCKKLL EPIIKYLQEY KKDNYKFILI GIENSTTCDI FKNRGILMEE FFKEVEKLNI IIKAIEYPKN EKDYNKFVKT LEKMIK // ID Y009_METJA Reviewed; 276 AA. AC Q60320; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0009; GN OrderedLocusNames=MJ0009; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97998.1; -; Genomic_DNA. DR PIR; A64301; A64301. DR STRING; 243232.MJ_0009; -. DR EnsemblBacteria; AAB97998; AAB97998; MJ_0009. DR KEGG; mja:MJ_0009; -. DR eggNOG; arCOG05016; Archaea. DR eggNOG; ENOG410YJMK; LUCA. DR OMA; GCHAYLR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 276 Uncharacterized protein MJ0009. FT /FTId=PRO_0000106650. SQ SEQUENCE 276 AA; 32241 MW; D974214C75F1A39A CRC64; MIFNENTPNF IDFKESFKEL PLSDETFKII EENGIKLREI AIGEFSGRDS VAAIIKAIEE GIDFVLPVVA FTGTDYGNIN IFYKNWEIVN KRIKEIDKDK ILLPLHFMFE PKLWNALNGR WVVLSFKRYG YYRPCIGCHA YLRIIRIPLA KHLGGKIISG ERLYHNGDFK IDQIEEVLNV YSKICRDFDV ELILPIRYIR EGKKIKEIIG EEWEQGEKQF SCVFSGNYRD KDGKVIFDKE GILKMLNEFI YPASVEILKE GYKGNFNYLN IVKKLI // ID Y037_METJA Reviewed; 238 AA. AC Q60344; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein MJ0037; GN OrderedLocusNames=MJ0037; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98018.1; -; Genomic_DNA. DR PIR; E64304; E64304. DR ProteinModelPortal; Q60344; -. DR STRING; 243232.MJ_0037; -. DR EnsemblBacteria; AAB98018; AAB98018; MJ_0037. DR KEGG; mja:MJ_0037; -. DR eggNOG; arCOG01150; Archaea. DR eggNOG; COG1407; LUCA. DR InParanoid; Q60344; -. DR KO; K06953; -. DR OMA; INGDIKH; -. DR PhylomeDB; Q60344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR004376; CHP00024_Pesterase-like. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR024173; Pesterase_MJ0037. DR Pfam; PF00149; Metallophos; 1. DR PIRSF; PIRSF000887; Pesterase_MJ0037; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00024; SbcD_rel_arch; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 238 Uncharacterized protein MJ0037. FT /FTId=PRO_0000106661. SQ SEQUENCE 238 AA; 27684 MW; 164A1C90B8C7960B CRC64; MEERLKIKDF YITVDRCLVY KDYAIIADTH IGFDVFFGEG GANFPLLQKD EVIKRTLNII DKYKINNLII NGDIKHNFKP YPKEIKFLKE FIEFLREYIN VILIKGNHDT FISSAGYEIF DYFELGNYLI FHGDKEIKID RDLLKEKFWI LGHEHPSIKL RDDVGAILKF PTYLLNKNYI VLPAFNPLSP GNDLINNSAS SKIIKKSYLE AEVIAITDIG LLNFGTLRDL REFAKTHL // ID Y042_METJA Reviewed; 215 AA. AC Q60347; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0042; GN OrderedLocusNames=MJ0042; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98028.1; -; Genomic_DNA. DR PIR; B64305; B64305. DR ProteinModelPortal; Q60347; -. DR STRING; 243232.MJ_0042; -. DR EnsemblBacteria; AAB98028; AAB98028; MJ_0042. DR KEGG; mja:MJ_0042; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR011723; Znf/thioredoxin_put. DR TIGRFAMs; TIGR02098; MJ0042_CXXC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 215 Uncharacterized protein MJ0042. FT /FTId=PRO_0000106665. SQ SEQUENCE 215 AA; 24892 MW; D1F39FD383A3A0A1 CRC64; MNVKCPECGA WIYVVEEDSG GDAMEVKCPK CGTSIYVVKP MGEKMKNKRD KDFLDVKILE IEETKKTSPY KDTKSEDVLK ALRVKANING EIYEFRIWQI AKKPEYRGMV YVVKSVSHYC GSVKTKNFQV DEDNDIYVKQ KFGIIEGVNK SKIKLPKERM EEIAEKLGFE LKEGDEGLRL YLGEKYSENP PLSQRPELIE KLIKCWIAFW EPTMI // ID Y058_METJA Reviewed; 391 AA. AC Q60366; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative ammonium transporter MJ0058; GN OrderedLocusNames=MJ0058; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ammonia transporter channel CC (TC 1.A.11.2) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98038.1; -; Genomic_DNA. DR PIR; B64307; B64307. DR ProteinModelPortal; Q60366; -. DR STRING; 243232.MJ_0058; -. DR EnsemblBacteria; AAB98038; AAB98038; MJ_0058. DR KEGG; mja:MJ_0058; -. DR eggNOG; arCOG04397; Archaea. DR eggNOG; COG0004; LUCA. DR InParanoid; Q60366; -. DR KO; K03320; -. DR OMA; LYPIVEH; -. DR PhylomeDB; Q60366; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central. DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central. DR Gene3D; 1.10.3430.10; -; 1. DR InterPro; IPR029020; Ammonium/urea_transptr. DR InterPro; IPR001905; Ammonium_transpt. DR InterPro; IPR018047; Ammonium_transpt_CS. DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom. DR PANTHER; PTHR11730; PTHR11730; 1. DR Pfam; PF00909; Ammonium_transp; 1. DR SUPFAM; SSF111352; SSF111352; 1. DR TIGRFAMs; TIGR00836; amt; 1. DR PROSITE; PS01219; AMMONIUM_TRANSP; 1. PE 3: Inferred from homology; KW Ammonia transport; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 391 Putative ammonium transporter MJ0058. FT /FTId=PRO_0000139764. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 88 108 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 192 212 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 261 281 Helical. {ECO:0000255}. FT TRANSMEM 305 325 Helical. {ECO:0000255}. FT TRANSMEM 338 358 Helical. {ECO:0000255}. SQ SEQUENCE 391 AA; 41153 MW; 33632A73849E1C9A CRC64; MFEVKHMDGI DVFFFMWAAS LIFFMKAGFI ALEIGQFRAK NVSYHCVLKL LDLAAVFIAY LFIGYGISYG FENIMPLITG TFDADLGAWW MKMVMFAAAA VTIITGGVAE RIKILPYFIG ALIVGGILYP IVEHLVWGGG FANLGINFHD YAGSGAVHLF GGLVGLMAAY VLGPRIDKYI NGKPQAIPGH NIPIAVLGAF ILAFGWYGFN IGSASGIANG VELASVAMAT TMALAGGIIG GALSSRNDPL YTANGMCAGL VAVCSGVDLF TPIGAFIVGL LAGIQQPFTY KFIEEKLKID DVCAIGPVHA MSGLIGVICA GIPFLLKADA VSKVSITGQI IGAIVIALIA IVGGLIIYKG LDLTIGLRVS EEAEKVGLDT AILQTTAYSE E // ID Y059_METJA Reviewed; 112 AA. AC Q60381; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized nitrogen regulatory PII-like protein MJ0059; GN OrderedLocusNames=MJ0059; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- INTERACTION: CC Q58739:MJ1343; NbExp=2; IntAct=EBI-7201321, EBI-7201308; CC -!- SIMILARITY: Belongs to the P(II) protein family. CC {ECO:0000255|PROSITE-ProRule:PRU00675}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98041.1; -; Genomic_DNA. DR PIR; C64307; C64307. DR PDB; 2J9C; X-ray; 1.30 A; A/B/C=1-112. DR PDB; 2J9D; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I/J/K/L=1-112. DR PDB; 2J9E; X-ray; 1.62 A; A/B/C=1-112. DR PDBsum; 2J9C; -. DR PDBsum; 2J9D; -. DR PDBsum; 2J9E; -. DR ProteinModelPortal; Q60381; -. DR SMR; Q60381; 1-112. DR IntAct; Q60381; 1. DR MINT; MINT-4297928; -. DR STRING; 243232.MJ_0059; -. DR EnsemblBacteria; AAB98041; AAB98041; MJ_0059. DR KEGG; mja:MJ_0059; -. DR eggNOG; arCOG02305; Archaea. DR eggNOG; COG0347; LUCA. DR InParanoid; Q60381; -. DR KO; K04751; -. DR OMA; AIEVKGF; -. DR PhylomeDB; Q60381; -. DR EvolutionaryTrace; Q60381; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR002187; N-reg_PII. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR InterPro; IPR017918; N-reg_PII_CS. DR Pfam; PF00543; P-II; 1. DR PIRSF; PIRSF039144; GlnB; 1. DR PRINTS; PR00340; PIIGLNB. DR SMART; SM00938; P-II; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR PROSITE; PS00638; PII_GLNB_CTER; 1. DR PROSITE; PS51343; PII_GLNB_DOM; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 112 Uncharacterized nitrogen regulatory PII- FT like protein MJ0059. FT /FTId=PRO_0000139815. FT MOD_RES 51 51 O-UMP-tyrosine. {ECO:0000255|PROSITE- FT ProRule:PRU00675}. FT STRAND 1 8 {ECO:0000244|PDB:2J9C}. FT HELIX 10 12 {ECO:0000244|PDB:2J9C}. FT HELIX 13 22 {ECO:0000244|PDB:2J9C}. FT STRAND 28 36 {ECO:0000244|PDB:2J9C}. FT STRAND 39 42 {ECO:0000244|PDB:2J9C}. FT STRAND 52 54 {ECO:0000244|PDB:2J9C}. FT STRAND 56 66 {ECO:0000244|PDB:2J9C}. FT HELIX 67 69 {ECO:0000244|PDB:2J9C}. FT HELIX 70 81 {ECO:0000244|PDB:2J9C}. FT STRAND 89 96 {ECO:0000244|PDB:2J9C}. FT STRAND 98 101 {ECO:0000244|PDB:2J9C}. FT TURN 102 104 {ECO:0000244|PDB:2J9C}. FT HELIX 109 112 {ECO:0000244|PDB:2J9C}. SQ SEQUENCE 112 AA; 12490 MW; 3DC3F307C32FE9F3 CRC64; MKKVEAIIRP EKLEIVKKAL SDAGYVGMTV SEVKGRGVQG GIVERYRGRE YIVDLIPKVK IELVVKEEDV DNVIDIICEN ARTGNPGDGK IFVIPVERVV RVRTKEEGKE AL // ID Y067_METJA Reviewed; 103 AA. AC Q60371; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0067; GN OrderedLocusNames=MJ0067; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the FUN14 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98052.1; -; Genomic_DNA. DR PIR; C64308; C64308. DR STRING; 243232.MJ_0067; -. DR DNASU; 1450906; -. DR EnsemblBacteria; AAB98052; AAB98052; MJ_0067. DR KEGG; mja:MJ_0067; -. DR eggNOG; arCOG04811; Archaea. DR eggNOG; COG2383; LUCA. DR InParanoid; Q60371; -. DR OMA; ITGYALK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007014; FUN14. DR Pfam; PF04930; FUN14; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 103 Uncharacterized protein MJ0067. FT /FTId=PRO_0000106677. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. SQ SEQUENCE 103 AA; 11059 MW; 94DCD5C2F9394D53 CRC64; MIILDFSQFL PDIGSGFIIG FVIGWAAKKA IKVVAFLIGI YILSLLYLAK IGVISINKEA FSALLGNLEN SLLVFGDKII GLIHSFSFGT SFLIGFGLGF KKG // ID Y080_METJA Reviewed; 127 AA. AC Q60386; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized transcriptional regulator MJ0080; GN OrderedLocusNames=MJ0080; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98060.1; -; Genomic_DNA. DR PIR; H64309; H64309. DR ProteinModelPortal; Q60386; -. DR STRING; 243232.MJ_0080; -. DR EnsemblBacteria; AAB98060; AAB98060; MJ_0080. DR KEGG; mja:MJ_0080; -. DR eggNOG; arCOG01008; Archaea. DR eggNOG; COG0864; LUCA. DR KO; K07722; -. DR OMA; YDWLSRI; -. DR PhylomeDB; Q60386; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.1220.10; -; 1. DR InterPro; IPR013321; Arc_rbn_hlx_hlx. DR InterPro; IPR002145; CopG. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR014864; TF_NikR_Ni-bd_C. DR Pfam; PF08753; NikR_C; 1. DR Pfam; PF01402; RHH_1; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 127 Uncharacterized transcriptional regulator FT MJ0080. FT /FTId=PRO_0000139318. SQ SEQUENCE 127 AA; 14892 MW; BB57018575CF9AE4 CRC64; MERISLTIEK NLLKEVDEII NKERISRSEF IRRALEYYVK KYDWLSRIES KIGEITVIYN SKAVEDIVKL ESQYKDIVII SLEIPFEGKI IRMIAIKGQR DRIIEFTNKL KGISSVELAQ LTTISIE // ID Y091_METJA Reviewed; 302 AA. AC Q57556; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Uncharacterized membrane protein MJ0091; GN OrderedLocusNames=MJ0091; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the sodium/potassium/calcium exchanger CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98072.1; -; Genomic_DNA. DR PIR; C64311; C64311. DR PDB; 3V5S; X-ray; 3.50 A; A=1-302. DR PDB; 3V5U; X-ray; 1.90 A; A=1-302. DR PDBsum; 3V5S; -. DR PDBsum; 3V5U; -. DR ProteinModelPortal; Q57556; -. DR STRING; 243232.MJ_0091; -. DR TCDB; 2.A.19.5.3; the ca(2+):cation antiporter (caca) family. DR DNASU; 1450930; -. DR EnsemblBacteria; AAB98072; AAB98072; MJ_0091. DR KEGG; mja:MJ_0091; -. DR eggNOG; arCOG02881; Archaea. DR eggNOG; COG0530; LUCA. DR InParanoid; Q57556; -. DR KO; K07301; -. DR OMA; EQMAELP; -. DR PhylomeDB; Q57556; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005262; F:calcium channel activity; IBA:GO_Central. DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central. DR GO; GO:0008273; F:calcium, potassium:sodium antiporter activity; IBA:GO_Central. DR GO; GO:0030955; F:potassium ion binding; IBA:GO_Central. DR GO; GO:0031402; F:sodium ion binding; IBA:GO_Central. DR GO; GO:0070588; P:calcium ion transmembrane transport; IBA:GOC. DR GO; GO:0006874; P:cellular calcium ion homeostasis; IBA:GO_Central. DR GO; GO:0035725; P:sodium ion transmembrane transport; IBA:GOC. DR InterPro; IPR004481; K/Na/Ca-exchanger. DR InterPro; IPR004837; NaCa_Exmemb. DR PANTHER; PTHR10846; PTHR10846; 1. DR Pfam; PF01699; Na_Ca_ex; 2. DR TIGRFAMs; TIGR00367; TIGR00367; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 302 Uncharacterized membrane protein MJ0091. FT /FTId=PRO_0000209509. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 77 97 Helical. {ECO:0000255}. FT TRANSMEM 106 126 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 227 247 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT HELIX 2 34 {ECO:0000244|PDB:3V5U}. FT HELIX 38 43 {ECO:0000244|PDB:3V5U}. FT HELIX 45 63 {ECO:0000244|PDB:3V5U}. FT HELIX 67 83 {ECO:0000244|PDB:3V5U}. FT HELIX 85 92 {ECO:0000244|PDB:3V5U}. FT HELIX 99 118 {ECO:0000244|PDB:3V5U}. FT TURN 119 121 {ECO:0000244|PDB:3V5U}. FT HELIX 125 145 {ECO:0000244|PDB:3V5U}. FT HELIX 159 192 {ECO:0000244|PDB:3V5U}. FT HELIX 198 203 {ECO:0000244|PDB:3V5U}. FT HELIX 205 209 {ECO:0000244|PDB:3V5U}. FT HELIX 211 222 {ECO:0000244|PDB:3V5U}. FT HELIX 226 242 {ECO:0000244|PDB:3V5U}. FT HELIX 244 251 {ECO:0000244|PDB:3V5U}. FT HELIX 258 277 {ECO:0000244|PDB:3V5U}. FT HELIX 282 298 {ECO:0000244|PDB:3V5U}. SQ SEQUENCE 302 AA; 32213 MW; 3D4F8373ED375879 CRC64; MLILGVGYFL LGLILLYYGS DWFVLGSERI ARHFNVSNFV IGATVMAIGT SLPEILTSAY ASYMHAPGIS IGNAIGSCIC NIGLVLGLSA IISPIIVDKN LQKNILVYLL FVIFAAVIGI DGFSWIDGVV LLILFIIYLR WTVKNGSAEI EENNDKNNPS VVFSLVLLII GLIGVLVGAE LFVDGAKKIA LALDISDKVI GFTLVAFGTS LPELMVSLAA AKRNLGGMVL GNVIGSNIAD IGGALAVGSL FMHLPAENVQ MAVLVIMSLL LYLFAKYSKI GRWQGILFLA LYIIAIASLR MG // ID Y094_METJA Reviewed; 310 AA. AC Q57559; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0094; GN OrderedLocusNames=MJ0094; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98074.1; -; Genomic_DNA. DR PIR; F64311; F64311. DR ProteinModelPortal; Q57559; -. DR STRING; 243232.MJ_0094; -. DR EnsemblBacteria; AAB98074; AAB98074; MJ_0094. DR KEGG; mja:MJ_0094; -. DR eggNOG; arCOG03226; Archaea. DR eggNOG; COG4052; LUCA. DR InParanoid; Q57559; -. DR OMA; AKPNMIG; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR026327; Me_CoM_Rdtase_prot-C-like. DR InterPro; IPR011312; UCP019164_menthan. DR Pfam; PF04609; MCR_C; 1. DR PIRSF; PIRSF019164; UCP019164; 1. DR TIGRFAMs; TIGR03274; methan_mark_7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 310 Uncharacterized protein MJ0094. FT /FTId=PRO_0000106690. SQ SEQUENCE 310 AA; 35866 MW; 8D2F64D524CE2EB1 CRC64; MVILMYEIVR YEGGVYKNNI FKEWIEDIGG FVIQEHVMQL DVYMTLAIPQ NELENIKEEA KKYKGKIIET PLAGTEIAVV APSLSRHHLP HTACDISEYL RRFGAKPNMI GLARGVGRDI AQLREKERRL IEEHDLAVYV MGNFEDCIKN KTHLFDVDIP VVVTGGPEKI DIPYPYVGNL GRRSHRLRHG EEIRALRKMV EVITELINER RRELSYDPPI VPPVVVKDEI EKQVEEVYSI LSPMPIVTQL DGLRVKLDYD KYADKIREVK VKNYTLGDIA DIKRSEMKNY ILIKIKPKSE VEFEMHKDKA // ID Y1006_METJA Reviewed; 359 AA. AC Q58412; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Uncharacterized ATP-binding protein MJ1006; GN OrderedLocusNames=MJ1006; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99014.1; -; Genomic_DNA. DR PIR; E64425; E64425. DR ProteinModelPortal; Q58412; -. DR STRING; 243232.MJ_1006; -. DR DNASU; 1451903; -. DR EnsemblBacteria; AAB99014; AAB99014; MJ_1006. DR KEGG; mja:MJ_1006; -. DR eggNOG; ENOG4102U6X; Archaea. DR eggNOG; ENOG410Z1ZF; LUCA. DR InParanoid; Q58412; -. DR KO; K06921; -. DR OMA; FENKIKV; -. DR PhylomeDB; Q58412; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 359 Uncharacterized ATP-binding protein FT MJ1006. FT /FTId=PRO_0000184672. FT NP_BIND 46 53 ATP. {ECO:0000255}. SQ SEQUENCE 359 AA; 42777 MW; 7D2F72172C6E8BC4 CRC64; MAIQNGLRNR ILFLVIFMKF YNREKELNYL KNYVQLEPNS ILFVYGPKSS GKSTVMLRVI EELSKKDDLV FFYYDLREYA TPTKEEFLEI FFEKGDKKYL LNRFEINLKI FKFGIEEKFD FDNIKLNDVF SKMKESINAV IKDGKKPILI IDELQKLKSI YFNGEGKGDK SLLNELFNLF VHLTKVRHLC HVICLTSDTL FIEEIYRNST LENTSEYYLI DWLRKESIRN ILKEEGFSEE EVDYCLKYLS LPYEISQLIN NKKLGLSVEQ TIKQWINIER DKILYLISTQ KEFEMGKLID ALKLFENKIK VDIKEIIRDN LMDEVKFLIK NEILFYDVMN GIIKPTSVKK WYAIKEVIE // ID Y1010_METJA Reviewed; 377 AA. AC Q58416; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Uncharacterized ATP-binding protein MJ1010; GN OrderedLocusNames=MJ1010; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99015.1; -; Genomic_DNA. DR PIR; A64426; A64426. DR PDB; 3BJO; X-ray; 2.05 A; A=278-377. DR PDBsum; 3BJO; -. DR ProteinModelPortal; Q58416; -. DR SMR; Q58416; 278-377. DR STRING; 243232.MJ_1010; -. DR EnsemblBacteria; AAB99015; AAB99015; MJ_1010. DR KEGG; mja:MJ_1010; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q58416; -. DR KO; K06921; -. DR OMA; NIFDYIT; -. DR PhylomeDB; Q58416; -. DR EvolutionaryTrace; Q58416; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 377 Uncharacterized ATP-binding protein FT MJ1010. FT /FTId=PRO_0000184673. FT NP_BIND 32 39 ATP. {ECO:0000255}. FT HELIX 278 298 {ECO:0000244|PDB:3BJO}. FT TURN 299 302 {ECO:0000244|PDB:3BJO}. FT STRAND 306 309 {ECO:0000244|PDB:3BJO}. FT STRAND 312 315 {ECO:0000244|PDB:3BJO}. FT HELIX 318 326 {ECO:0000244|PDB:3BJO}. FT HELIX 327 329 {ECO:0000244|PDB:3BJO}. FT STRAND 332 335 {ECO:0000244|PDB:3BJO}. FT HELIX 336 338 {ECO:0000244|PDB:3BJO}. FT HELIX 341 349 {ECO:0000244|PDB:3BJO}. FT STRAND 352 356 {ECO:0000244|PDB:3BJO}. FT TURN 357 360 {ECO:0000244|PDB:3BJO}. FT STRAND 361 366 {ECO:0000244|PDB:3BJO}. FT HELIX 367 376 {ECO:0000244|PDB:3BJO}. SQ SEQUENCE 377 AA; 44463 MW; 50AC996D843166A5 CRC64; MINMKFFNRV EEIKEILSIL EEEPNLIYFI YGPINSGKTA LINEIINNRL DKNKYVVFYI DLREIFISKY DEFEAKLRAT KTFGFRLIIE VLFEEYEDDK KPIEIIRSLI KDAPSLCGIP TPKNTLEEIL KKKTTKNVFK YITNILMDIK REGKQPIIII DELQKIGDMK INGFLIYELF NYFVSLTKHK HLCHVFCLSS DSLFIERVYN EAMLKERVDY ILVDDFDKET ALKFIDFLSE EILNKKLSDE DKELIYSYVG GKPILIINVI GKLKHKNLKD VLNILLMDEI SKLKDFLSNL DYIKPKVNIE EEIIEIRKED IINALKLFKG KYEIEVDKIP KAVYVYLVKK NILFLYPQRG TLKPQSFLVW NAIKRVL // ID Y1052_METJA Reviewed; 100 AA. AC Q58452; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=UPF0045 protein MJ1052; GN OrderedLocusNames=MJ1052; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0045 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99055.1; -; Genomic_DNA. DR PIR; C64431; C64431. DR PDB; 2EKY; X-ray; 1.80 A; A/B/C/D/E/F/G/H=1-100. DR PDB; 2EPI; X-ray; 1.70 A; A/B/C/D=1-100. DR PDBsum; 2EKY; -. DR PDBsum; 2EPI; -. DR ProteinModelPortal; Q58452; -. DR SMR; Q58452; 1-100. DR STRING; 243232.MJ_1052; -. DR EnsemblBacteria; AAB99055; AAB99055; MJ_1052. DR KEGG; mja:MJ_1052; -. DR eggNOG; arCOG04373; Archaea. DR eggNOG; COG0011; LUCA. DR InParanoid; Q58452; -. DR OMA; SVSKYVK; -. DR PhylomeDB; Q58452; -. DR EvolutionaryTrace; Q58452; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.70.930; -; 1. DR InterPro; IPR029756; MTH1187/YkoF-like. DR InterPro; IPR002767; Thiamine_BP. DR Pfam; PF01910; Thiamine_BP; 1. DR SUPFAM; SSF89957; SSF89957; 1. DR TIGRFAMs; TIGR00106; TIGR00106; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 100 UPF0045 protein MJ1052. FT /FTId=PRO_0000147628. FT STRAND 6 16 {ECO:0000244|PDB:2EPI}. FT STRAND 18 20 {ECO:0000244|PDB:2EPI}. FT HELIX 23 33 {ECO:0000244|PDB:2EPI}. FT STRAND 39 43 {ECO:0000244|PDB:2EPI}. FT STRAND 46 52 {ECO:0000244|PDB:2EPI}. FT HELIX 53 68 {ECO:0000244|PDB:2EPI}. FT STRAND 71 86 {ECO:0000244|PDB:2EPI}. FT HELIX 90 96 {ECO:0000244|PDB:2EPI}. SQ SEQUENCE 100 AA; 11223 MW; EDD51BF797B85AE2 CRC64; MIFMRKVVAE VSIIPLGKGA SVSKYVKKAI EVFKKYDLKV ETNAMGTVLE GDLDEILKAF KEAHSTVLND VDRVVSSLKI DERKDKENTI ERKLKAIGEL // ID Y1057_METJA Reviewed; 290 AA. AC Q58457; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized glycosyltransferase MJ1057; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1057; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase 2 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99061.1; -; Genomic_DNA. DR PIR; H64431; H64431. DR ProteinModelPortal; Q58457; -. DR STRING; 243232.MJ_1057; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB99061; AAB99061; MJ_1057. DR KEGG; mja:MJ_1057; -. DR eggNOG; arCOG01381; Archaea. DR eggNOG; COG0463; LUCA. DR InParanoid; Q58457; -. DR OMA; FGSDDIM; -. DR PhylomeDB; Q58457; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 290 Uncharacterized glycosyltransferase FT MJ1057. FT /FTId=PRO_0000059252. SQ SEQUENCE 290 AA; 35103 MW; 3F6A1B221C420D74 CRC64; MVGEMDKPLV SVVMATYNEP EKYLKESIES IXNQTXKDFX FIIVLDNPNN KKAEEIIKEY QQKDKRIIFI KNERNLGRGA SRNKAVNIAR GKYIAILDAD DIALPKRLEK QFKYMENNRD IDLLFSWVYF IDENGNILKE FKPEKYKFKE IKKYFFKEHL TVHPSMMVKS KILKKLKYDE KLIRSQDYDF WIRCIANDYK FDIIEEFLLK YRIPNRDNYL SRIKKQKLYS YYTLKTHWKN KKHFCNNVYF WKVFFYSLVV YLFIVLTPTF ILKILIDIKD KKTEISTKGH // ID Y1072_METJA Reviewed; 116 AA. AC Q58472; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1072; GN OrderedLocusNames=MJ1072; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99079.1; -; Genomic_DNA. DR PIR; G64433; G64433. DR STRING; 243232.MJ_1072; -. DR EnsemblBacteria; AAB99079; AAB99079; MJ_1072. DR KEGG; mja:MJ_1072; -. DR eggNOG; arCOG09652; Archaea. DR eggNOG; ENOG4110ZR7; LUCA. DR OMA; NQLDKKM; -. DR PhylomeDB; Q58472; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 116 Uncharacterized protein MJ1072. FT /FTId=PRO_0000107158. FT TRANSMEM 89 109 Helical. {ECO:0000255}. SQ SEQUENCE 116 AA; 13595 MW; 68BBDBEE2A56BC78 CRC64; MIYFGGIMAI AYAKLYEIIA KYIKDEKRAE ELYNAVVEVI KEEKIIVKHE LKDELKNELA TKEDIMLAEE RILRYVDNRF NQLDKKMTVG FVILILLYIL TNPNAIELIK LLFGVK // ID Y1093_METJA Reviewed; 300 AA. AC Q58493; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ1093; GN OrderedLocusNames=MJ1093; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC -!- SIMILARITY: Belongs to the MoaA/NifB/PqqE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99096.1; -; Genomic_DNA. DR PIR; D64436; D64436. DR ProteinModelPortal; Q58493; -. DR STRING; 243232.MJ_1093; -. DR EnsemblBacteria; AAB99096; AAB99096; MJ_1093. DR KEGG; mja:MJ_1093; -. DR eggNOG; arCOG00956; Archaea. DR eggNOG; COG0535; LUCA. DR InParanoid; Q58493; -. DR KO; K02585; -. DR OMA; PKCNIAC; -. DR PhylomeDB; Q58493; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 300 Uncharacterized protein MJ1093. FT /FTId=PRO_0000153050. FT METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 42 42 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 300 AA; 34568 MW; 5EEA1B14CA4CF1E0 CRC64; MDKNKMSKFA HITKVHPCFN EKIHDKVGRV HLPVAPRCNI ACKFCRRSLG KEACEHRPGV ALSVLKPEDV ESYLNKVLKE IPNIKVVGIA GPGDSLFNKE TFETLKIIDE KFPNLIKCLS TNGLLLNKYY KKLADLNVKT VTVTVNAIDP EILKEIVEWV YYDKKVHYGI EGAKILIENQ IDGIKKAYDE DLIIKINTVL IPEINMNHVV DIAKELKDFV YIQNIIPLIP LYKMSHLRPP TCEELKKVRE ECEKYIPQFR ACGQCRADAV GLIKERKILE EFFKEKNKKL NVFELKHFSH // ID Y1115_METJA Reviewed; 261 AA. AC Q58515; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1115; GN OrderedLocusNames=MJ1115; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the BtpA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99116.1; -; Genomic_DNA. DR PIR; B64439; B64439. DR ProteinModelPortal; Q58515; -. DR STRING; 243232.MJ_1115; -. DR DNASU; 1452011; -. DR EnsemblBacteria; AAB99116; AAB99116; MJ_1115. DR KEGG; mja:MJ_1115; -. DR eggNOG; arCOG01982; Archaea. DR eggNOG; COG0434; LUCA. DR InParanoid; Q58515; -. DR KO; K06971; -. DR OMA; ENFFDAP; -. DR PhylomeDB; Q58515; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005137; PSI_BtpA. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR PANTHER; PTHR21381; PTHR21381; 1. DR Pfam; PF03437; BtpA; 1. DR PIRSF; PIRSF005956; BtpA; 1. DR ProDom; PD011184; PSI_BtpA; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00259; thylakoid_BtpA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein MJ1115. FT /FTId=PRO_0000159331. SQ SEQUENCE 261 AA; 28939 MW; D831E2F79BD69517 CRC64; MIPMFKKKPL IGMVHLKPLP GSYHYNDNFD DIVDFAIKEA KKLEEAGFDA VMIENFGDAP FKKEADKITI ASMAVIAKAI KEEVSLPLGI NILRNDAIGA YSIAYVVKAD FIRVNVLSGV AFTDQGIIEG KAYELAKLKK LLPSKIKVFA DVHVKHAYHF IDFESSLLDT VERGLADAVI ISGKRTGKEV DIEKLKLAKE LVDVPVIVGS GTNYNNLRIL WSYADGFIIG TWIKKDGKAN NEIDIDRAKK IVNLANKLKM C // ID Y1125_METJA Reviewed; 60 AA. AC Q58525; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ1125; GN OrderedLocusNames=MJ1125; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99127.1; -; Genomic_DNA. DR PIR; D64440; D64440. DR STRING; 243232.MJ_1125; -. DR EnsemblBacteria; AAB99127; AAB99127; MJ_1125. DR KEGG; mja:MJ_1125; -. DR eggNOG; arCOG03445; Archaea. DR eggNOG; ENOG4111GIP; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 60 Uncharacterized protein MJ1125. FT /FTId=PRO_0000107179. SQ SEQUENCE 60 AA; 6905 MW; 7393670630AC1E63 CRC64; MMVKNTIDVK EILRELDTTR IKDYPLMSGK EILLRTNFKG CCGMPSQISQ LNLKEQLESC // ID Y1127_METJA Reviewed; 280 AA. AC Q58527; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ1127; GN OrderedLocusNames=MJ1127; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99129.1; -; Genomic_DNA. DR PIR; F64440; F64440. DR ProteinModelPortal; Q58527; -. DR STRING; 243232.MJ_1127; -. DR DNASU; 1452023; -. DR EnsemblBacteria; AAB99129; AAB99129; MJ_1127. DR KEGG; mja:MJ_1127; -. DR eggNOG; arCOG00893; Archaea. DR eggNOG; COG1831; LUCA. DR InParanoid; Q58527; -. DR KO; K07049; -. DR OMA; CAVQLHT; -. DR PhylomeDB; Q58527; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR InterPro; IPR011589; UCP004961. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF004961; UCP004961_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 280 Uncharacterized protein MJ1127. FT /FTId=PRO_0000107180. SQ SEQUENCE 280 AA; 31672 MW; 6FC7CD2F0E85C959 CRC64; MDVLKSLPVT DNHIHVDDKH GYGAEKVAKT FYNAGGKVMI VLNKPTFDGN LTASMDILVR DVEIINKNTP VKAFGLVGVH PAELTYLMKF MSLEEAKQRI VDALNYAKKL VEEYDFIVGI GEVGRPHYPV SEDVWKASNE ILKYCMELAK DIGCAIQIHA ESSTEEQFKE FSEMAKEVGL NPEKVVKHHC GNMVLEGERY GIFPSILASR VNEDVVKKSL RFVMETDYID DLKRPGVALG IKTVPRVTRR LIEKGVLDEE GVYKIHKENI ERIYDMDLEL // ID Y1183_METJA Reviewed; 161 AA. AC Q58583; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1183; GN OrderedLocusNames=MJ1183; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH862. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99184.1; -; Genomic_DNA. DR PIR; F64447; F64447. DR ProteinModelPortal; Q58583; -. DR STRING; 243232.MJ_1183; -. DR EnsemblBacteria; AAB99184; AAB99184; MJ_1183. DR KEGG; mja:MJ_1183; -. DR eggNOG; arCOG04847; Archaea. DR eggNOG; COG4090; LUCA. DR InParanoid; Q58583; -. DR OMA; AMPKIGV; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR009183; UCP004962. DR Pfam; PF09897; DUF2124; 1. DR PIRSF; PIRSF004962; UCP004962; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 161 Uncharacterized protein MJ1183. FT /FTId=PRO_0000107206. SQ SEQUENCE 161 AA; 18310 MW; B1214A1F0AEC5678 CRC64; MGDIMTLKLL KEENGLSPML REFRTLVRDS NIEKVAFVGS VGVCQPFAEL FGYAIRDKEC YFIPDGDLNK VKKLVIKDIG MQMEDFENLN KVDAIVLFGG LAMPKYGVEV DKIKELINKL SPKKVIGVCF MSIFQKAGWD KEIDFDYLMD GFIKVSIYCK D // ID Y1205_METJA Reviewed; 103 AA. AC Q58602; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=UPF0058 protein MJ1205; GN OrderedLocusNames=MJ1205; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0058 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99209.1; -; Genomic_DNA. DR PIR; D64450; D64450. DR ProteinModelPortal; Q58602; -. DR STRING; 243232.MJ_1205; -. DR EnsemblBacteria; AAB99209; AAB99209; MJ_1205. DR KEGG; mja:MJ_1205; -. DR eggNOG; arCOG02254; Archaea. DR eggNOG; COG1745; LUCA. DR InParanoid; Q58602; -. DR OMA; HRSKAEH; -. DR PhylomeDB; Q58602; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.1270.110; -; 1. DR InterPro; IPR002753; UPF0058. DR Pfam; PF01893; UPF0058; 1. DR SUPFAM; SSF140371; SSF140371; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 103 UPF0058 protein MJ1205. FT /FTId=PRO_0000135710. SQ SEQUENCE 103 AA; 12378 MW; A7EEE4737597499E CRC64; MHKDELIQLH QLLIYLRKYI EKKYNCDNNE FKEYDELNIY PHHIHRTKAE HIYTIFLLSS IIAKILSDNG KIPRSVSNLL RVSGEKIKKE IQRKRCKIKN TNT // ID Y1223_METJA Reviewed; 92 AA. AC Q58620; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1223; GN OrderedLocusNames=MJ1223; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.thermoautotrophicum MTH1250. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99235.1; -; Genomic_DNA. DR PIR; F64452; F64452. DR STRING; 243232.MJ_1223; -. DR EnsemblBacteria; AAB99235; AAB99235; MJ_1223. DR KEGG; mja:MJ_1223; -. DR eggNOG; arCOG04878; Archaea. DR eggNOG; COG2212; LUCA. DR KO; K14111; -. DR OMA; AFCKVIG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 92 Uncharacterized protein MJ1223. FT /FTId=PRO_0000107224. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. SQ SEQUENCE 92 AA; 9739 MW; DDBCA78E28CCF164 CRC64; MNIYVWLFAI IALSFSALVG LRLSFKKGTA NVLVGESIIT VVAGTLIVVI SQKYNLAFAD TIALAIFICG VVGAFAFCKV IGGDNEKAKQ PN // ID Y1248_METJA Reviewed; 154 AA. AC Q58645; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1248; GN OrderedLocusNames=MJ1248; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99258.1; -; Genomic_DNA. DR PIR; G64455; G64455. DR ProteinModelPortal; Q58645; -. DR STRING; 243232.MJ_1248; -. DR EnsemblBacteria; AAB99258; AAB99258; MJ_1248. DR KEGG; mja:MJ_1248; -. DR eggNOG; arCOG09678; Archaea. DR eggNOG; ENOG411106R; LUCA. DR OMA; DHEIEGF; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 154 Uncharacterized protein MJ1248. FT /FTId=PRO_0000107239. SQ SEQUENCE 154 AA; 18006 MW; 219316E7F5A7E585 CRC64; MKMEVIEKLS ELSGIDKKSL RRILIILEFS LRKKDGSPTS FAEKFNIKSF GDLYNYIRDV KSNLKRDHEI EGFNGLTEMW KSVAPRAQYW IMDTFGEENP RDALFSASVF TMRTFGIMLD NLLLLKKIIK TLDEYQKEVT EYVSAQKFEA EDLE // ID Y125_METJA Reviewed; 116 AA. AC Q57589; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=UPF0331 protein MJ0125; GN OrderedLocusNames=MJ0125; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0331 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98105.1; -; Genomic_DNA. DR PIR; E64315; E64315. DR ProteinModelPortal; Q57589; -. DR STRING; 243232.MJ_0125; -. DR EnsemblBacteria; AAB98105; AAB98105; MJ_0125. DR KEGG; mja:MJ_0125; -. DR eggNOG; arCOG05024; Archaea. DR eggNOG; COG2361; LUCA. DR InParanoid; Q57589; -. DR OMA; FKADLRT; -. DR PhylomeDB; Q57589; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 116 UPF0331 protein MJ0125. FT /FTId=PRO_0000158259. SQ SEQUENCE 116 AA; 13970 MW; 7A77740A495160EF CRC64; MPKRDIKAFL YDILSYMDDI INFTKDMDYE EFINNKAIKY AVIRCLEVIG EAVKKIPKDI REKYPHIPFK ELAGMRDKLI HQYFGVDYLT VWETAKYEIP EIKKEFEKII KDLEEK // ID Y1284_METJA Reviewed; 121 AA. AC Q58680; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1284; DE Flags: Precursor; GN OrderedLocusNames=MJ1284; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To B.burgdorferi BB0465 N-terminal region. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99293.1; -; Genomic_DNA. DR PIR; C64460; C64460. DR STRING; 243232.MJ_1284; -. DR EnsemblBacteria; AAB99293; AAB99293; MJ_1284. DR KEGG; mja:MJ_1284; -. DR eggNOG; arCOG08269; Archaea. DR eggNOG; ENOG41110SX; LUCA. DR OMA; RNFIFEN; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 31 {ECO:0000255}. FT CHAIN 32 121 Uncharacterized protein MJ1284. FT /FTId=PRO_0000014011. SQ SEQUENCE 121 AA; 14084 MW; 51E484F654BF6712 CRC64; MILNNKGFIR ILEATIAGIM VILVFSYLVM SQNFDYNLSL EFIGYNALYS AHIEEGDFEN ISSLYKKIEL PSNVGYGFEI YKNGNLIYSD AKNGVVVERN FIFENNTSVN FYKLRLILWW R // ID Y1310_METJA Reviewed; 128 AA. AC Q58706; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1310; GN OrderedLocusNames=MJ1310; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99317.1; -; Genomic_DNA. DR PIR; E64463; E64463. DR ProteinModelPortal; Q58706; -. DR STRING; 243232.MJ_1310; -. DR EnsemblBacteria; AAB99317; AAB99317; MJ_1310. DR KEGG; mja:MJ_1310; -. DR eggNOG; arCOG03072; Archaea. DR eggNOG; COG1006; LUCA. DR InParanoid; Q58706; -. DR KO; K14114; -. DR OMA; HAGMIKP; -. DR PhylomeDB; Q58706; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0042773; P:ATP synthesis coupled electron transport; IEA:InterPro. DR InterPro; IPR001133; NADH_UbQ_OxRdtase_chain4L/K. DR Pfam; PF00420; Oxidored_q2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 128 Uncharacterized protein MJ1310. FT /FTId=PRO_0000107268. FT TRANSMEM 13 35 Helical. {ECO:0000255}. FT TRANSMEM 42 64 Helical. {ECO:0000255}. FT TRANSMEM 90 112 Helical. {ECO:0000255}. SQ SEQUENCE 128 AA; 13938 MW; 8A7166717236008C CRC64; MIMINYLVNR MDFQMASFIT SGLLVIIGLY GVFFVDNVLK KIIALEILGS GVNLALIAIG YNGGTIPIKL PGVSVEVFAK ESAYPLTHAL VLTNIVIEAS MLAVMLGVSI ILYKKYKTLR SSVILKED // ID Y1333_METJA Reviewed; 84 AA. AC Q58729; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1333; GN OrderedLocusNames=MJ1333; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99345.1; -; Genomic_DNA. DR PIR; D64466; D64466. DR STRING; 243232.MJ_1333; -. DR EnsemblBacteria; AAB99345; AAB99345; MJ_1333. DR KEGG; mja:MJ_1333; -. DR eggNOG; arCOG05077; Archaea. DR eggNOG; ENOG410YW7N; LUCA. DR OMA; DSRYIEL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Coiled coil; Complete proteome; Reference proteome. FT CHAIN 1 84 Uncharacterized protein MJ1333. FT /FTId=PRO_0000107278. FT COILED 5 31 {ECO:0000255}. SQ SEQUENCE 84 AA; 9871 MW; 7C9F1E5079BBCF88 CRC64; MPSPKIQEII NELDNLMNRE RKYIELVATV EYLLNLIEPS KREKFKEALY DAETVEDVYE LIKAIKLQLG MQGARRYLLT LEGQ // ID Y1336_METJA Reviewed; 148 AA. AC Q58732; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1336; GN OrderedLocusNames=MJ1336; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99346.1; -; Genomic_DNA. DR PIR; G64466; G64466. DR ProteinModelPortal; Q58732; -. DR STRING; 243232.MJ_1336; -. DR EnsemblBacteria; AAB99346; AAB99346; MJ_1336. DR KEGG; mja:MJ_1336; -. DR eggNOG; ENOG4102TPF; Archaea. DR eggNOG; COG2870; LUCA. DR PhylomeDB; Q58732; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 148 Uncharacterized protein MJ1336. FT /FTId=PRO_0000107280. SQ SEQUENCE 148 AA; 17013 MW; 5A036EDED081B76B CRC64; MGYNQQLLRV DYEKIYPIND ELSSKILGVI KNLNGKSDIL VISDYAKGLI TKELMDDIKK EFKGKILIDP KPKNDFYKDV YLIKPNLKEA SQILGREIEN KDDELEKSGL ESVDKYNSNF VITRGEKGAT LITVDEIFTM FQQKSKRS // ID Y1337_METJA Reviewed; 231 AA. AC Q58733; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1337; GN OrderedLocusNames=MJ1337; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99358.1; -; Genomic_DNA. DR PIR; H64466; H64466. DR ProteinModelPortal; Q58733; -. DR STRING; 243232.MJ_1337; -. DR EnsemblBacteria; AAB99358; AAB99358; MJ_1337. DR KEGG; mja:MJ_1337; -. DR eggNOG; arCOG05078; Archaea. DR eggNOG; COG0063; LUCA. DR InParanoid; Q58733; -. DR OMA; CIGGTGD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0052855; F:ADP-dependent NAD(P)H-hydrate dehydratase activity; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR000631; CARKD. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF01256; Carb_kinase; 1. DR SUPFAM; SSF53613; SSF53613; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 231 Uncharacterized protein MJ1337. FT /FTId=PRO_0000107281. SQ SEQUENCE 231 AA; 25675 MW; 203926DBCD472FAE CRC64; MIGAVLKTLE YFDEKDVKVI TTGDIGEGDG SLKIYDALKE IDDDLVIIHY IKPKISKIRE INFSPKIIAD AGGMYAAKAA NIGDKFYLFL PDVGELAFLA DEKASHPAYV RGFISEIDDN EVPKLIERDY KLKMPKYMVV KGETDYTIRE EKIIDKIKEP KIKAMECIGG TGDTLTEIVS SLISVDFKTE EALSLGCKIN RKLGEIANVN PNTQITEIIN AIPKALENTL K // ID Y1344_METJA Reviewed; 112 AA. AC Q58740; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized nitrogen regulatory PII-like protein MJ1344; GN OrderedLocusNames=MJ1344; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the P(II) protein family. CC {ECO:0000255|PROSITE-ProRule:PRU00675}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99353.1; -; Genomic_DNA. DR PIR; G64467; G64467. DR ProteinModelPortal; Q58740; -. DR SMR; Q58740; 1-112. DR STRING; 243232.MJ_1344; -. DR EnsemblBacteria; AAB99353; AAB99353; MJ_1344. DR KEGG; mja:MJ_1344; -. DR eggNOG; arCOG02305; Archaea. DR eggNOG; COG0347; LUCA. DR InParanoid; Q58740; -. DR KO; K04751; -. DR OMA; QVESCIN; -. DR PhylomeDB; Q58740; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030234; F:enzyme regulator activity; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW. DR GO; GO:0006808; P:regulation of nitrogen utilization; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR002187; N-reg_PII. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR InterPro; IPR017918; N-reg_PII_CS. DR Pfam; PF00543; P-II; 1. DR PRINTS; PR00340; PIIGLNB. DR SMART; SM00938; P-II; 1. DR SUPFAM; SSF54913; SSF54913; 1. DR PROSITE; PS00638; PII_GLNB_CTER; 1. DR PROSITE; PS51343; PII_GLNB_DOM; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotide-binding; Phosphoprotein; KW Reference proteome; Transcription; Transcription regulation. FT CHAIN 1 112 Uncharacterized nitrogen regulatory PII- FT like protein MJ1344. FT /FTId=PRO_0000139816. FT MOD_RES 51 51 O-UMP-tyrosine. {ECO:0000255|PROSITE- FT ProRule:PRU00675}. SQ SEQUENCE 112 AA; 12532 MW; 3DDCE2A0F32FE9F3 CRC64; MKKVEAIIRP EKLEIVKKAL SDAGYVGMTV SEVKGRGVQG GIVERYRGRE YIVDLIPKVK IELVVKEEDV DNVIDIICEN ARTGNPGDGK IFVIPVERVV RVRTKEEGRD VL // ID Y1369_METJA Reviewed; 155 AA. AC Q58764; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1369; GN OrderedLocusNames=MJ1369; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99386.1; -; Genomic_DNA. DR PIR; H64470; H64470. DR ProteinModelPortal; Q58764; -. DR STRING; 243232.MJ_1369; -. DR EnsemblBacteria; AAB99386; AAB99386; MJ_1369. DR KEGG; mja:MJ_1369; -. DR eggNOG; arCOG02727; Archaea. DR eggNOG; COG1673; LUCA. DR OMA; RNIEICY; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.10.590.10; -; 1. DR InterPro; IPR002740; EVE_domain. DR InterPro; IPR015947; PUA-like_domain. DR SUPFAM; SSF88697; SSF88697; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein MJ1369. FT /FTId=PRO_0000107301. SQ SEQUENCE 155 AA; 18595 MW; CC47AC47A0A684EB CRC64; MRDIVMTYWL FSSNNIRNIE ICYNHMIWGF WDRNAGEKQK KNWRSFIRKY NQIKPFDVAV FQIAKTGEIH AIGVIKETYY DDQTPIWDNE INLNKVTFPW RVSFSVIIFS KEAVIKRFIK IQDYIDGYGL GELEHHDFNE ILKAFQKKFG MISIK // ID Y13A_METJA Reviewed; 100 AA. AC P81330; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0139.1; GN OrderedLocusNames=MJ0139.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98131.1; -; Genomic_DNA. DR STRING; 243232.MJ_0139.1; -. DR EnsemblBacteria; AAB98131; AAB98131; MJ_0139.1. DR KEGG; mja:MJ_0139.1; -. DR eggNOG; arCOG02134; Archaea. DR eggNOG; COG3316; LUCA. DR PhylomeDB; P81330; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MJ0139.1. FT /FTId=PRO_0000106715. SQ SEQUENCE 100 AA; 12094 MW; 8C7C2C24E8FEC1F3 CRC64; MRLTIEVIKE RIVERKLFKR NRKSIEVKIL AGLLYYLGLS LRKVSLFLSQ FEDISHESVR IYYHKIKEVL NRFPSNSKFD TVVSWIKSFM MFYNWVKSLT // ID Y1402_METJA Reviewed; 346 AA. AC Q58797; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ1402; DE Flags: Precursor; GN OrderedLocusNames=MJ1402; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99412.1; -; Genomic_DNA. DR PIR; A64475; A64475. DR ProteinModelPortal; Q58797; -. DR EnsemblBacteria; AAB99412; AAB99412; MJ_1402. DR KEGG; mja:MJ_1402; -. DR eggNOG; arCOG05987; Archaea. DR eggNOG; ENOG410YSPP; LUCA. DR OMA; YAGGFNN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR013373; Flagellin/pilin_N. DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 346 Uncharacterized protein MJ1402. FT /FTId=PRO_0000014015. SQ SEQUENCE 346 AA; 38064 MW; 46034EA32D0F69DF CRC64; MFEWMKNKKA ISPILALLIV LGVTIVVGAV FYAWGSGLFN NSQQSTQSAL EGTTSTITYA AGAIGVGVPK EIDVEGDLDL TYPTPDYKLS HLTTTDYGSY DERLIVPVPL TLENYYDSTL TNVKIESDGA TEVAGLTLKK ITLNYNGQNY DAYLLCTNDG TPFKGILNRT GIYPDATWTG DDGNNYTSVY YILAPNSVTG VAAVDGSKDL SVTTAKKWPY SQNDVQSMRL YAGGFNNMWY ACAVNGSYSS WTNTLTATKF IGWNTAQAFY KYKTPIDAKF YTSEWDVGTL HKGEKVSKEI FFFFGSSMGF QEEPSGETTV KIPVKVVSDQ GVYKQVDVNI VLKDRL // ID Y1404_METJA Reviewed; 421 AA. AC Q58799; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ1404; GN OrderedLocusNames=MJ1404; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 4 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99421.1; -; Genomic_DNA. DR PIR; C64475; C64475. DR ProteinModelPortal; Q58799; -. DR STRING; 243232.MJ_1404; -. DR EnsemblBacteria; AAB99421; AAB99421; MJ_1404. DR KEGG; mja:MJ_1404; -. DR eggNOG; arCOG00601; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q58799; -. DR OMA; LGIMEEN; -. DR PhylomeDB; Q58799; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR014651; UCP036983_2CBS_MJ1404. DR Pfam; PF00571; CBS; 4. DR PIRSF; PIRSF036983; UCP_2CBS_MJ1404; 1. DR SMART; SM00116; CBS; 4. DR PROSITE; PS51371; CBS; 4. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 421 Uncharacterized protein MJ1404. FT /FTId=PRO_0000107313. FT DOMAIN 13 74 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 74 133 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 139 195 CBS 3. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 217 274 CBS 4. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 421 AA; 47609 MW; FF89C9E64060202F CRC64; MRLMLNEPVK EIMTKDVVTV TPDTPVSKAL GIMEENGFHH LIVVDKKDGK EEYYLISMRD LLLASSTDEE VRSLMYKAHC VHEDTPFLDA VCEMLDSGQR AAPIVNNVGK MVGIITDYDI MARAAKSKIM KDTKVTKIMT RNVITINEND SIGKARALMR DNNIGRLVVV DDEGNPVGMV TEVDILKKVF KPKKKMTAGE FKGEKVPRMG QPVRLIMNTP LITVDVDASA ADAARVMQEY DIRGVPVVKG KSLRGIVTRL DIIKYIADLK KGAMIEIELH GMLDPEFKDL AERIIATEVK KMVKHAGKIH WIKITIKKER DKGGVPYYRI TTYVKTPNKL YVGEGRPKAS LPNKLEAEGE DIAYVSEHER WEFIDVLKES LESVLRQLEA DYDKYHPKHA GKVVKGQFPE EFNPEEFKKE E // ID Y1409_METJA Reviewed; 268 AA. AC Q58804; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1409; GN OrderedLocusNames=MJ1409; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99423.1; -; Genomic_DNA. DR PIR; H64475; H64475. DR ProteinModelPortal; Q58804; -. DR EnsemblBacteria; AAB99423; AAB99423; MJ_1409. DR KEGG; mja:MJ_1409; -. DR eggNOG; arCOG05083; Archaea. DR eggNOG; ENOG410YCGB; LUCA. DR OMA; VYIDVFM; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Coiled coil; Complete proteome; Reference proteome. FT CHAIN 1 268 Uncharacterized protein MJ1409. FT /FTId=PRO_0000107314. FT COILED 132 159 {ECO:0000255}. SQ SEQUENCE 268 AA; 31970 MW; 0FB410E4D603ECDC CRC64; METMKAKELA QKILLDIYRN LDEFSKDIIR GDLADIEFKG FYLKGKNGEK AYIRNLDDFE NLKDFDVEMR KYKLKSINLK NLDEGLMIIN LSSRVSKEYK FEANEYSIIY PSNNTTIEFK ERVLKWMELE DDELDEKIIE FDTKMNEILE ELLEDVEVEE EISVYIDVFM DVNKIENFVE KDDERIIIWI HPVFLFSNDD VLRGLLAYEL SRFKSRFLEV GYKDIIKYCR ELKKLTNKKP KVLEKIKDIA NKYGDIDSLN LINEIENE // ID Y1412_METJA Reviewed; 498 AA. AC Q58807; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0288 protein MJ1412 {ECO:0000255|HAMAP-Rule:MF_01089}; GN OrderedLocusNames=MJ1412; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0288 family. {ECO:0000255|HAMAP- CC Rule:MF_01089}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99419.1; -; Genomic_DNA. DR PIR; C64476; C64476. DR ProteinModelPortal; Q58807; -. DR STRING; 243232.MJ_1412; -. DR EnsemblBacteria; AAB99419; AAB99419; MJ_1412. DR KEGG; mja:MJ_1412; -. DR eggNOG; arCOG04900; Archaea. DR eggNOG; COG4070; LUCA. DR InParanoid; Q58807; -. DR OMA; FKKWDVV; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01089; UPF0288; 1. DR InterPro; IPR016466; UPF0288_methan. DR PIRSF; PIRSF005852; UCP005852; 1. DR TIGRFAMs; TIGR03268; methan_mark_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 498 UPF0288 protein MJ1412. FT /FTId=PRO_0000156051. SQ SEQUENCE 498 AA; 56317 MW; D8D1DA4D2B86B166 CRC64; MAKVIVNGKE KVGETLREVI KDEYYNEGAN IVIIKGVKRE AEKIPKKFLI KTTKGNITIA ITENNETAKF FINNYKDFVK KLRWVSGMDV AFGSTTIDLE ISTEPKEFKK WDVVLSISGL DKDEGHIVFI KKKTEGVYGL KDPKIGIVVG GKWVIDRLEV GDKIIDIEPI REEKEAVDYL VTTDLDLKLE DGWRIFTYFT AEFDGTPSAV EHCLALMEDG IFEITENTNT YVADCRLQTL KIEEGNLIDR ERGFITVRNY GVGEGKVYIY RESRSSSLSH TVVGRVKEGI ELIDFSDSGV LSVKXVPERL CAIGLTIEEA EEMFKKYNIE VEKEGDLENA IVVEQEPEYT LDVLKEKKVK IRGLDKNKII VIELFEDKAP ITAWYFRKTT GLTTKRVGKL HVYFKHKDIV MFKGNPEYAK GLLPENIPTD KVEPCSIGVT NMVSRYKGMI GVRLGESDKF GPTGESFEKT NIVGGIVENA EYLKNVKTGD DVYVLLKK // ID Y1419_METJA Reviewed; 93 AA. AC Q58814; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 2. DT 09-DEC-2015, entry version 81. DE RecName: Full=UPF0147 protein MJ1419; GN OrderedLocusNames=MJ1419; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0147 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99429.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99429.1; ALT_INIT; Genomic_DNA. DR PIR; B64477; B64477. DR ProteinModelPortal; Q58814; -. DR SMR; Q58814; 6-93. DR STRING; 243232.MJ_1419; -. DR EnsemblBacteria; AAB99429; AAB99429; MJ_1419. DR KEGG; mja:MJ_1419; -. DR eggNOG; arCOG04308; Archaea. DR eggNOG; COG1698; LUCA. DR InParanoid; Q58814; -. DR KO; K09721; -. DR OMA; ANDNSVP; -. DR PhylomeDB; Q58814; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.1440.50; -; 1. DR HAMAP; MF_00342; UPF0147; 1. DR InterPro; IPR023130; Ta0600-like_domain. DR InterPro; IPR005354; UPF0147. DR Pfam; PF03685; UPF0147; 1. DR ProDom; PD029943; UPF0147; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 93 UPF0147 protein MJ1419. FT /FTId=PRO_0000150908. SQ SEQUENCE 93 AA; 10278 MW; 87088824EB02CD8C CRC64; MVFGSAASEK TPEEILKGVA LMLDEIINDT TVPRNIRAAA EKAKEAVLKE GEEPIVRSAT AIHILDEISN DPNMPLHTRT QIWSIVSELE RVK // ID Y1450_METJA Reviewed; 371 AA. AC Q58845; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 77. DE RecName: Full=Uncharacterized protein MJ1450; GN OrderedLocusNames=MJ1450; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99458.1; -; Genomic_DNA. DR PIR; A64481; A64481. DR ProteinModelPortal; Q58845; -. DR STRING; 243232.MJ_1450; -. DR EnsemblBacteria; AAB99458; AAB99458; MJ_1450. DR KEGG; mja:MJ_1450; -. DR eggNOG; arCOG02232; Archaea. DR eggNOG; COG2303; LUCA. DR InParanoid; Q58845; -. DR OMA; ATHYSKL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR SUPFAM; SSF51905; SSF51905; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 371 Uncharacterized protein MJ1450. FT /FTId=PRO_0000107337. FT DOMAIN 110 140 4Fe-4S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. SQ SEQUENCE 371 AA; 42027 MW; 8B76588950AF5992 CRC64; MYDFAIIGSG VAGATLAKEL RYRYKVAVIE KGKKPSYASE GKNVEINYVY GLGGSGVYSL GNAIKTEIKG YKIDKDIYKE IWEELKIKAP KDDFLNDIDK AFIELGFEKM EKFIDFDRCN KCGECARKIC KAKWTPLNYL KESNANIITE FNIKAINYSN YYEILDDKGR KIKAKNLIIS AGGINSPRIL KKMIDDENIG KNLFIDTFVT VGGILEDSYL NKDISMLVYK KYKNFMLATH YSKLLINEIK KDYKDVKEKD IVGIMIKIKD ENNGVVLDND VKKEITKEDF KTLARGICKA TKYLYKLGVD DIYTTIPRGS HPGGSLSLVV DEFEVREGLY VCDASLFKEA LGVPPIVSII ALSKKFVREI L // ID Y1463_METJA Reviewed; 233 AA. AC Q58858; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=UPF0128 protein MJ1463; GN OrderedLocusNames=MJ1463; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0128 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99477.1; -; Genomic_DNA. DR PIR; F64482; F64482. DR ProteinModelPortal; Q58858; -. DR STRING; 243232.MJ_1463; -. DR EnsemblBacteria; AAB99477; AAB99477; MJ_1463. DR KEGG; mja:MJ_1463; -. DR eggNOG; arCOG05084; Archaea. DR eggNOG; COG1851; LUCA. DR InParanoid; Q58858; -. DR KO; K09130; -. DR OMA; EYPPKVR; -. DR PhylomeDB; Q58858; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00264; UPF0128; 1. DR InterPro; IPR005266; UPF0128. DR Pfam; PF03673; UPF0128; 1. DR PIRSF; PIRSF016179; UCP016179; 1. DR ProDom; PD023377; CHP00703; 1. DR TIGRFAMs; TIGR00703; TIGR00703; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 233 UPF0128 protein MJ1463. FT /FTId=PRO_0000185225. SQ SEQUENCE 233 AA; 26609 MW; DDB46A3B1D893999 CRC64; MVVDAKEVEM INTLVFETLG NPEKEREFKL KSLKRWGFDL IFGKVDGKET YFTVELDERK AGDKFSKDGK EYEVIEVLQE LPKNTELYAH IEMEMGKAYI VCQLRDEDGK NTEVLRVPAA TLLLAFLKKN KLANIIKAIK NVGISLELSM QNGVGGKPLS YEELPNVARR FIRSARKVEK ETGFGRLSFA YYGETKDGEP RYRFSWLLPT IALFDLDIAK KVEQTLGILK VSE // ID Y1537_METJA Reviewed; 343 AA. AC Q58932; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1537; GN OrderedLocusNames=MJ1537; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99559.1; -; Genomic_DNA. DR PIR; H64491; H64491. DR ProteinModelPortal; Q58932; -. DR STRING; 243232.MJ_1537; -. DR EnsemblBacteria; AAB99559; AAB99559; MJ_1537. DR KEGG; mja:MJ_1537; -. DR eggNOG; arCOG05089; Archaea. DR eggNOG; ENOG410YDQH; LUCA. DR OMA; PEESTWL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 343 Uncharacterized protein MJ1537. FT /FTId=PRO_0000107395. SQ SEQUENCE 343 AA; 40505 MW; 839521737D113FD6 CRC64; MWHNQGDAMS LSMNLKLCNY HNCNCNIGEE YYNHTYPQFW NRIIEKYKLN KIISYDFTSL PYYRFVGMVG DFISKNITTG PCLLTPKEIR KLNPNIDFEE VKKMFLRHPT FEDYVSVAIE TNKGYKNHII IETYEYAKLV EYKTNIPFEE ALKLTKLSAK NFKKYYKKKV KAKYYLTHKK SFDRRLRELC NEHYKYYLEN ANISKKGKEI IKNNPEESTW LRIKVSFLPE AINKDDSTIV EPVSSIEGML LANKISEVSG IVVRSPPTLN LKPIMNEGNE NEIFYLNNDI EKEIKKLTYR TRTKWGCSLY HNLLFLNSPI CCNKNCEECL EIFINKIKIL KMG // ID Y1540_METJA Reviewed; 136 AA. AC Q58935; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1540; GN OrderedLocusNames=MJ1540; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99569.1; -; Genomic_DNA. DR PIR; C64492; C64492. DR ProteinModelPortal; Q58935; -. DR STRING; 243232.MJ_1540; -. DR EnsemblBacteria; AAB99569; AAB99569; MJ_1540. DR KEGG; mja:MJ_1540; -. DR eggNOG; arCOG08298; Archaea. DR eggNOG; ENOG41111FN; LUCA. DR OMA; TITIESH; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 136 Uncharacterized protein MJ1540. FT /FTId=PRO_0000107398. SQ SEQUENCE 136 AA; 15633 MW; 0590C8C629EAFE04 CRC64; MLKELNYLFL FQRLIKNGSL EIALTNIFSL GISRDYITIN IENIKTLKEI MEAVSSKSAN KKLKSFLEKI EDLKIFLSEA SKIAEILVNN RKTFILKYKG KEVLIVGYDA RGGIFLKNIK ITDKLALIKM LNEFKN // ID Y1552_METJA Reviewed; 141 AA. AC Q58947; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1552; GN OrderedLocusNames=MJ1552; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99572.1; -; Genomic_DNA. DR PIR; G64493; G64493. DR ProteinModelPortal; Q58947; -. DR STRING; 243232.MJ_1552; -. DR DNASU; 1452460; -. DR EnsemblBacteria; AAB99572; AAB99572; MJ_1552. DR KEGG; mja:MJ_1552; -. DR eggNOG; arCOG01285; Archaea. DR eggNOG; COG1545; LUCA. DR InParanoid; Q58947; -. DR KO; K07068; -. DR OMA; TVYFPPR; -. DR PhylomeDB; Q58947; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002878; DUF35_OB-fold_C. DR InterPro; IPR022002; DUF35_Znr_N. DR InterPro; IPR012340; NA-bd_OB-fold. DR Pfam; PF12172; DUF35_N; 1. DR Pfam; PF01796; OB_aCoA_assoc; 1. DR SUPFAM; SSF50249; SSF50249; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 141 Uncharacterized protein MJ1552. FT /FTId=PRO_0000107408. SQ SEQUENCE 141 AA; 16390 MW; 11690E4E7922D751 CRC64; MGIKYLLRDK MVVRSWRHIK ERYCLIGVRC KNCGTVYFPS REICPKCRRK TEFEEIKLSG KGKVYTYSVV HVAPKDFEKQ APYVIAIIEL EEGARITGQI VDCKPEDVYI GMQVEAVFRR IKEDGDDGVI TYGYKFKPIE N // ID Y1563_METJA Reviewed; 152 AA. AC Q58958; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 107. DE RecName: Full=Putative HTH-type transcriptional regulator MJ1563; DE AltName: Full=DNA-binding protein MJ1563; GN OrderedLocusNames=MJ1563; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS). RX PubMed=12471609; DOI=10.1002/prot.10272; RA Ray S.S., Bonanno J.B., Chen H., de Lencastre H., Wu S., Tomasz A., RA Burley S.K.; RT "X-ray structure of an M.jannaschii DNA-binding protein: implications RT for antibiotic resistance in S. aureus."; RL Proteins 50:170-173(2003). CC -!- SIMILARITY: Belongs to the GbsR family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99584.1; -; Genomic_DNA. DR PIR; B64495; B64495. DR PDB; 1KU9; X-ray; 2.80 A; A/B=1-152. DR PDBsum; 1KU9; -. DR ProteinModelPortal; Q58958; -. DR SMR; Q58958; 1-151. DR STRING; 243232.MJ_1563; -. DR EnsemblBacteria; AAB99584; AAB99584; MJ_1563. DR KEGG; mja:MJ_1563; -. DR eggNOG; arCOG02795; Archaea. DR eggNOG; COG1510; LUCA. DR InParanoid; Q58958; -. DR OMA; HGLNKSV; -. DR PhylomeDB; Q58958; -. DR EvolutionaryTrace; Q58958; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR026282; MJ1563. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PIRSF; PIRSF006707; MJ1563; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; DNA-binding; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 152 Putative HTH-type transcriptional FT regulator MJ1563. FT /FTId=PRO_0000160637. FT DOMAIN 7 106 HTH arsR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. FT DNA_BIND 44 68 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. FT HELIX 3 21 {ECO:0000244|PDB:1KU9}. FT HELIX 26 37 {ECO:0000244|PDB:1KU9}. FT HELIX 44 51 {ECO:0000244|PDB:1KU9}. FT HELIX 55 67 {ECO:0000244|PDB:1KU9}. FT STRAND 70 74 {ECO:0000244|PDB:1KU9}. FT STRAND 83 86 {ECO:0000244|PDB:1KU9}. FT HELIX 89 117 {ECO:0000244|PDB:1KU9}. FT HELIX 123 133 {ECO:0000244|PDB:1KU9}. FT HELIX 135 145 {ECO:0000244|PDB:1KU9}. FT HELIX 146 149 {ECO:0000244|PDB:1KU9}. SQ SEQUENCE 152 AA; 17609 MW; ABD121B907F4271A CRC64; MIIMEEAKKL IIELFSELAK IHGLNKSVGA VYAILYLSDK PLTISDIMEE LKISKGNVSM SLKKLEELGF VRKVWIKGER KNYYEAVDGF SSIKDIAKRK HDLIAKTYED LKKLEEKCNE EEKEFIKQKI KGIERMKKIS EKILEALNDL DN // ID Y1617_METJA Reviewed; 93 AA. AC Q59012; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1617; GN OrderedLocusNames=MJ1617; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99646.1; -; Genomic_DNA. DR PIR; H64501; H64501. DR ProteinModelPortal; Q59012; -. DR STRING; 243232.MJ_1617; -. DR EnsemblBacteria; AAB99646; AAB99646; MJ_1617. DR KEGG; mja:MJ_1617; -. DR eggNOG; arCOG02717; Archaea. DR eggNOG; COG2034; LUCA. DR InParanoid; Q59012; -. DR OMA; FFMITLG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002849; DUF131. DR Pfam; PF01998; DUF131; 1. DR TIGRFAMs; TIGR00304; TIGR00304; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein MJ1617. FT /FTId=PRO_0000107439. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. SQ SEQUENCE 93 AA; 10461 MW; 589E72AC270850A9 CRC64; MIMKPILIFL GIILMFIGFF MITLGMILPS SQENYEKPET EKTESSVEYS GIVMIGPIPI VFGNSPGLMI LSVLIAILMI IWMFLFAFGI RIK // ID Y1625_METJA Reviewed; 671 AA. AC Q59020; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ1625; GN OrderedLocusNames=MJ1625; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99643.1; -; Genomic_DNA. DR PIR; H64502; H64502. DR ProteinModelPortal; Q59020; -. DR STRING; 243232.MJ_1625; -. DR EnsemblBacteria; AAB99643; AAB99643; MJ_1625. DR KEGG; mja:MJ_1625; -. DR eggNOG; arCOG01695; Archaea. DR eggNOG; COG1293; LUCA. DR InParanoid; Q59020; -. DR OMA; MVYGKRN; -. DR PhylomeDB; Q59020; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR008532; DUF814. DR InterPro; IPR010979; Ribosomal_S13-like_H2TH. DR Pfam; PF05670; DUF814; 1. DR SUPFAM; SSF46946; SSF46946; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 671 Uncharacterized protein MJ1625. FT /FTId=PRO_0000107445. SQ SEQUENCE 671 AA; 78616 MW; 49BB5EE873CF6A86 CRC64; MKSEITNVDV CCVVDELQNL INGRLDKAFL IDNEQNRELI LKIHVPEGGS RELVISIGKY KYITLTNYER EKPKLPPSFA MLLRKYLKNA KLIKIEQVNF DRVVIFHFET RDGIYKLVAE LFGDGNIIFL NNEDTIIAPL RVERWSTRNI VPKEKYKFPP QKPLNPYNLE FSIAYEVFKD YFLNNKGVEC VRLISRVFGI GGLYAEEICE RAEIDKKKRD LSEEEIKKLF EASKNLFDEI FNNRKPQIVL KDNEYFDVVP IDLKKYKGLE KKYYNSFLEA VDDYFAKFLT KVVVKKEKSK IEKEIERQEN ILRRQLETLK KYKEDAEKNQ IKGDLIYANY QIVEELLNAI RQAREKMDWA RIKKIIRENK EHPILGLIEN INENIGEIII RLKSEVDDKV IEERVSLDIR KNAFENAESY YEKAKKLRNK IEGIENAIEL TKKKIEELKK KGEEELKEKE SMQMKKKIRK ERKWYEKFKW TVINGFLVIA GKDAITNEII IKKYTDKDDI VFHADIQGAP FTVIKTQGKE VDEETLEEVA KFSVSHSRAW KLGYGAIDTY WVKPEQISKT AESGEYLKRG AFVIRGERHY YRNTPLELGV GVIEYDGDVK ITTAPPKTLQ KSFIKWVLLK PSNKEKGKVV KELKEIFKDY GIDDEDILRV LPPGGCEIVK K // ID Y1627_METJA Reviewed; 151 AA. AC Q59021; DT 05-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=UPF0179 protein MJ1627; GN OrderedLocusNames=MJ1627; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0179 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99644.1; -; Genomic_DNA. DR PIR; A64503; A64503. DR STRING; 243232.MJ_1627; -. DR EnsemblBacteria; AAB99644; AAB99644; MJ_1627. DR KEGG; mja:MJ_1627; -. DR eggNOG; arCOG04477; Archaea. DR eggNOG; COG1860; LUCA. DR InParanoid; Q59021; -. DR KO; K09730; -. DR OMA; CPSHEYC; -. DR PhylomeDB; Q59021; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00498; UPF0179; 1. DR InterPro; IPR005369; UPF0179. DR Pfam; PF03684; UPF0179; 1. DR PIRSF; PIRSF006595; UCP006595; 1. DR ProDom; PD016182; UPF0179; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 151 UPF0179 protein MJ1627. FT /FTId=PRO_0000156870. SQ SEQUENCE 151 AA; 16941 MW; 2E18EB717F4E779E CRC64; MSKESKITLI GSKLAKTGGE FIYLGEIEEC KNCKFKRLCH GNLEVGRKYK IVSVRSANHP CIVHEGGVKV VEVVLADLTI MIESKKALEG VVLNHEPITC DNFDCEYYSF CNSEGIKEGE KYKIKQVLNE KINCPFGNSL KKVIVELVEN K // ID Y1635_METJA Reviewed; 414 AA. AC Q59029; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Putative transposase MJ1635; GN OrderedLocusNames=MJ1635; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: In the N-terminal section; belongs to the transposase CC 2 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transposase CC 35 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99664.1; -; Genomic_DNA. DR PIR; A64504; A64504. DR STRING; 243232.MJ_1635; -. DR EnsemblBacteria; AAB99664; AAB99664; MJ_1635. DR KEGG; mja:MJ_1635; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR InParanoid; Q59029; -. DR KO; K07496; -. DR OMA; YSILNSW; -. DR PhylomeDB; Q59029; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR InterPro; IPR001959; Transposase_2. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF01385; OrfB_IS605; 1. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Metal-binding; KW Reference proteome; Transposable element; Transposition; Zinc. FT CHAIN 1 414 Putative transposase MJ1635. FT /FTId=PRO_0000107451. FT METAL 329 329 Zinc. {ECO:0000255}. FT METAL 332 332 Zinc. {ECO:0000255}. FT METAL 346 346 Zinc. {ECO:0000255}. FT METAL 349 349 Zinc. {ECO:0000255}. SQ SEQUENCE 414 AA; 49003 MW; 031FC33EC1D4F277 CRC64; MSNKTKLKDN KELLYQVVLS YKVSHNYPLK AFLIECKNKL NECIDMIWNN IKYTKKDNPK LPKSNEFKRE LRNKLLENWN YASHYIDGII KTSYSILQSW ASNYKRGYRT KTKPIAKRLF VRVKTTLIKY DKEKGEIRIT IKPRKDYLIL NIKNEWFFDK VKNLTIGEII LKEKETFLTF KDNLNYSDKG MIVGVDSNLR SLDLFHPIEG WTRVDLTELH RIKEVYDRKI DFLKKLLKKF PLRAMRKINR LFERRRNRVK DFLHKLTIQL SRLFPDAIFV FEDLNKRRMY KSKYFNRKID RVNWNGLIEK ISYKTIVILV NPAYTSTICP ICGSRMESQE GQVVYCSNCL NSFNRQLVGC YNIFKRGLGN IKEIMGGSGV TTTGVEVSFG KLMTPNPNVI YIVDYNGKYF NEIA // ID Y1639_METJA Reviewed; 154 AA. AC Q59033; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MJ1639; GN OrderedLocusNames=MJ1639; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99665.1; -; Genomic_DNA. DR PIR; E64504; E64504. DR ProteinModelPortal; Q59033; -. DR EnsemblBacteria; AAB99665; AAB99665; MJ_1639. DR KEGG; mja:MJ_1639; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 154 Uncharacterized protein MJ1639. FT /FTId=PRO_0000107453. SQ SEQUENCE 154 AA; 17584 MW; 594DBEA256F4EDA7 CRC64; MYFVIKGDSI MYFVLRLGGD LSLYIPAKYR PFFEPLDKNS PYNIKVNLEN SSGDIVVDNV LDDKKIDERN SEITKLGGLI NELRRKKENG DNINIIEIRL KLKDDSIITH NLNTPNIEDY DDNKLVINSG TLVINGKTTI DLNNIEEITL KLDI // ID Y1673_METJA Reviewed; 129 AA. AC Q59067; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1673; GN OrderedLocusNames=MJ1673; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99695.1; -; Genomic_DNA. DR PIR; G64508; G64508. DR STRING; 243232.MJ_1673; -. DR EnsemblBacteria; AAB99695; AAB99695; MJ_1673. DR KEGG; mja:MJ_1673; -. DR eggNOG; arCOG09685; Archaea. DR eggNOG; ENOG4111VKP; LUCA. DR OMA; VSWCFKN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MJ1673. FT /FTId=PRO_0000107471. SQ SEQUENCE 129 AA; 15418 MW; 06277ED71FD85C3E CRC64; MPKMFLLFSH KLTDDQINDA RKNLKVDEFI YLPKELQELW SNIPPDVDDI DNYLKPIKEF LEKHAKPNDY VLIQGDFGAT YKMVNFAIDK NLIPIYSTTK RIAKDIYKDG KIITIRKFKH CRFRKYNPY // ID Y1676_METJA Reviewed; 238 AA. AC Q59070; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1676; GN OrderedLocusNames=MJ1676; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH564. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99698.1; -; Genomic_DNA. DR PIR; B64509; B64509. DR ProteinModelPortal; Q59070; -. DR STRING; 243232.MJ_1676; -. DR EnsemblBacteria; AAB99698; AAB99698; MJ_1676. DR KEGG; mja:MJ_1676; -. DR eggNOG; arCOG04839; Archaea. DR eggNOG; COG4053; LUCA. DR OMA; IYTMTAF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR012021; UCP005278. DR PIRSF; PIRSF005278; UCP005278; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 238 Uncharacterized protein MJ1676. FT /FTId=PRO_0000107473. SQ SEQUENCE 238 AA; 26085 MW; 4A2656C01EAF76C1 CRC64; MKKYIVSIGV DISDNDVKTN PKVNELVNKE IKKRLSKLGI KATISNITGD DIVITSFVPE NLIEKNNKII FEVLNKYAEG FDDLRGISED KDKAGEGLSY AIAESISEYG DAIIIAFDTY GGESFVDEMA LFVKEIGEKF GYDVGCSVSN EPIEIPGIGY TGAESDDPVV VITVEELDDI PKLAGLIYGG LLSFDKLYFV KNGDEVNILP PGVIYTMTAF LNGNVIDLYG GIRRKIKF // ID Y1679_METJA Reviewed; 97 AA. AC Q59073; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1679; GN OrderedLocusNames=MJ1679; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99704.1; -; Genomic_DNA. DR PIR; E64509; E64509. DR ProteinModelPortal; Q59073; -. DR STRING; 243232.MJ_1679; -. DR EnsemblBacteria; AAB99704; AAB99704; MJ_1679. DR KEGG; mja:MJ_1679; -. DR eggNOG; arCOG01011; Archaea. DR eggNOG; COG3609; LUCA. DR InParanoid; Q59073; -. DR OMA; RERRIPQ; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.1220.10; -; 1. DR InterPro; IPR013321; Arc_rbn_hlx_hlx. DR InterPro; IPR002145; CopG. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR016748; Tscrpt_reg_CopG_prd. DR Pfam; PF01402; RHH_1; 1. DR PIRSF; PIRSF019108; Txn_reg_CopG_prd; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ1679. FT /FTId=PRO_0000107479. SQ SEQUENCE 97 AA; 11880 MW; 64C59303B9101FE0 CRC64; MIEEEITLKI PKSIVNQIDE LIKEGYFSSR DEFVRYAVRE SLTEIAISKK MSREECKKIW EEYKIRKKDI KIDEKEIEEL LDEVDKEWKK WKKLKLK // ID WTPA_METJA Reviewed; 346 AA. AC Q58586; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 99. DE RecName: Full=Molybdate/tungstate-binding protein WtpA; DE Flags: Precursor; GN Name=wtpA; OrderedLocusNames=MJ1186; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Part of the ABC transporter complex WtpABC involved in CC molybdate/tungstate import. Binds tungstate and molybdate (By CC similarity). {ECO:0000250}. CC -!- SUBUNIT: The complex is composed of two ATP-binding proteins CC (WtpC), two transmembrane proteins (WtpB) and a solute-binding CC protein (WtpA). {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Peripheral membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the bacterial solute-binding protein 1 CC family. WtpA subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99190.1; -; Genomic_DNA. DR PIR; A64448; A64448. DR PDB; 3CFZ; X-ray; 1.70 A; A=37-325. DR PDBsum; 3CFZ; -. DR ProteinModelPortal; Q58586; -. DR SMR; Q58586; 38-344. DR STRING; 243232.MJ_1186; -. DR TCDB; 3.A.1.6.9; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAB99190; AAB99190; MJ_1186. DR KEGG; mja:MJ_1186; -. DR eggNOG; arCOG00219; Archaea. DR eggNOG; COG0725; LUCA. DR InParanoid; Q58586; -. DR KO; K15495; -. DR OMA; SPNDDPC; -. DR PhylomeDB; Q58586; -. DR EvolutionaryTrace; Q58586; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:1901359; F:tungstate binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR022498; ABC_trnspt_W-bd_WtpA. DR TIGRFAMs; TIGR03730; tungstate_WtpA; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Metal-binding; Molybdenum; Reference proteome; Signal; Transport. FT SIGNAL 1 19 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 20 346 Molybdate/tungstate-binding protein WtpA. FT /FTId=PRO_0000159720. FT METAL 46 46 Molybdate or tungstate; via amide FT nitrogen. {ECO:0000250}. FT METAL 47 47 Molybdate or tungstate. {ECO:0000250}. FT METAL 75 75 Molybdate or tungstate. {ECO:0000250}. FT METAL 158 158 Molybdate or tungstate. {ECO:0000250}. FT METAL 160 160 Molybdate or tungstate; via amide FT nitrogen. {ECO:0000250}. FT METAL 221 221 Molybdate or tungstate. {ECO:0000250}. FT METAL 239 239 Molybdate or tungstate. {ECO:0000250}. FT STRAND 38 45 {ECO:0000244|PDB:3CFZ}. FT HELIX 46 48 {ECO:0000244|PDB:3CFZ}. FT HELIX 49 62 {ECO:0000244|PDB:3CFZ}. FT STRAND 66 73 {ECO:0000244|PDB:3CFZ}. FT HELIX 75 83 {ECO:0000244|PDB:3CFZ}. FT STRAND 90 96 {ECO:0000244|PDB:3CFZ}. FT HELIX 99 103 {ECO:0000244|PDB:3CFZ}. FT TURN 104 108 {ECO:0000244|PDB:3CFZ}. FT STRAND 113 117 {ECO:0000244|PDB:3CFZ}. FT STRAND 120 124 {ECO:0000244|PDB:3CFZ}. FT TURN 129 133 {ECO:0000244|PDB:3CFZ}. FT TURN 136 138 {ECO:0000244|PDB:3CFZ}. FT HELIX 139 142 {ECO:0000244|PDB:3CFZ}. FT STRAND 150 153 {ECO:0000244|PDB:3CFZ}. FT TURN 155 157 {ECO:0000244|PDB:3CFZ}. FT HELIX 159 175 {ECO:0000244|PDB:3CFZ}. FT HELIX 180 184 {ECO:0000244|PDB:3CFZ}. FT HELIX 186 188 {ECO:0000244|PDB:3CFZ}. FT STRAND 192 196 {ECO:0000244|PDB:3CFZ}. FT STRAND 199 204 {ECO:0000244|PDB:3CFZ}. FT TURN 212 214 {ECO:0000244|PDB:3CFZ}. FT STRAND 215 220 {ECO:0000244|PDB:3CFZ}. FT HELIX 221 224 {ECO:0000244|PDB:3CFZ}. FT HELIX 225 229 {ECO:0000244|PDB:3CFZ}. FT STRAND 232 239 {ECO:0000244|PDB:3CFZ}. FT HELIX 240 245 {ECO:0000244|PDB:3CFZ}. FT STRAND 249 251 {ECO:0000244|PDB:3CFZ}. FT TURN 255 257 {ECO:0000244|PDB:3CFZ}. FT HELIX 262 264 {ECO:0000244|PDB:3CFZ}. FT HELIX 265 268 {ECO:0000244|PDB:3CFZ}. FT STRAND 271 275 {ECO:0000244|PDB:3CFZ}. FT HELIX 276 278 {ECO:0000244|PDB:3CFZ}. FT STRAND 280 283 {ECO:0000244|PDB:3CFZ}. FT STRAND 288 292 {ECO:0000244|PDB:3CFZ}. FT HELIX 300 312 {ECO:0000244|PDB:3CFZ}. FT HELIX 315 318 {ECO:0000244|PDB:3CFZ}. FT TURN 319 321 {ECO:0000244|PDB:3CFZ}. SQ SEQUENCE 346 AA; 39445 MW; 85009C2115769C40 CRC64; MIKRLIVISI LLIVGTVLCG CMEQENVGQQ NSEAQEKIVL KIFHAGSLSV PFEEYEKMFE KEHPNVDVER EPAGSVACVR KIIDLGKKAD ILASADYSLI PQMMMPKYAD WYVMFARNEI VLAYTDKSKY KDEINSTNWY KILQRPDVKI GFSNPNDDPC GYRTQMVLQL AELYYKDPTI YDNLVLKHSN IKVEENNGTY LILVPKELDV DTNKLFVRSK ETDLLAPLEA GAFDYLFIYK SVANQHHLKY IELPKEINLG YYEYADTYKK VALKIIAKNK TINAKPIVYG MTVPTNAPHK KEAIEFVKFV LGHPEVLENN GQPAIIPAVA YGNVPEELKD LVKIEK // ID Y007_METJA Reviewed; 373 AA. AC Q60318; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Uncharacterized protein MJ0007; GN OrderedLocusNames=MJ0007; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the FldB/FldC dehydratase beta subunit CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97988.1; -; Genomic_DNA. DR PIR; G64300; G64300. DR STRING; 243232.MJ_0007; -. DR EnsemblBacteria; AAB97988; AAB97988; MJ_0007. DR KEGG; mja:MJ_0007; -. DR eggNOG; arCOG04464; Archaea. DR eggNOG; COG1775; LUCA. DR InParanoid; Q60318; -. DR OMA; MAVPNWK; -. DR PhylomeDB; Q60318; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010327; FldB/FldC_alpha/beta. DR Pfam; PF06050; HGD-D; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 373 Uncharacterized protein MJ0007. FT /FTId=PRO_0000106648. FT TRANSMEM 32 52 Helical. {ECO:0000255}. SQ SEQUENCE 373 AA; 42984 MW; BA370B62EB70202D CRC64; MMKLKAIEKL MQKFASRKEQ LYKQKEEGRK VFGMFCAYVP IEIILAANAI PVGLCGGKND TIPIAEEDLP RNLCPLIKSS YGFKKAKTCP YFEASDIVIG ETTCEGKKKM FELMERLVPM HIMHLPHMKD EDSLKIWIKE VEKLKELVEK ETGNKITEEK LKETVDKVNK VRELFYKLYE LRKNKPAPIK GLDVLKLFQF AYLLDIDDTI GILEDLIEEL EERVKKGEGY EGKRILITGC PMVAGNNKIV EIIEEVGGVV VGEESCTGTR FFENFVEGYS VEDIAKRYFK IPCACRFKND ERVENIKRLV KELDVDGVVY YTLQYCHTFN IEGAKVEEAL KEEGIPIIRI ETDYSESDRE QLKTRLEAFI EMI // ID Y015_METJA Reviewed; 98 AA. AC Q60330; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0015; GN OrderedLocusNames=MJ0015; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97993.1; -; Genomic_DNA. DR PIR; G64301; G64301. DR ProteinModelPortal; Q60330; -. DR STRING; 243232.MJ_0015; -. DR EnsemblBacteria; AAB97993; AAB97993; MJ_0015. DR KEGG; mja:MJ_0015; -. DR eggNOG; arCOG07384; Archaea. DR eggNOG; COG0241; LUCA. DR PhylomeDB; Q60330; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.1000; -; 1. DR InterPro; IPR023214; HAD-like_dom. DR InterPro; IPR006549; HAD-SF_hydro_IIIA. DR SUPFAM; SSF56784; SSF56784; 1. DR TIGRFAMs; TIGR01662; HAD-SF-IIIA; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein MJ0015. FT /FTId=PRO_0000106655. SQ SEQUENCE 98 AA; 11733 MW; 428760FF9D57D475 CRC64; MMRLNWQIRQ VQLLLERLGL QQLVWMDCLV MMLNKAIFLD RDGVINKRLI GDYVKKIEEF ELLPNVREAL IEFKKMGYLL IVVTNQQGSK QFLIFYNL // ID Y047_METJA Reviewed; 428 AA. AC Q60355; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0047; GN OrderedLocusNames=MJ0047; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC RNA-metabolizing metallo-beta-lactamase-like family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98027.1; -; Genomic_DNA. DR ProteinModelPortal; Q60355; -. DR STRING; 243232.MJ_0047; -. DR EnsemblBacteria; AAB98027; AAB98027; MJ_0047. DR KEGG; mja:MJ_0047; -. DR eggNOG; arCOG00541; Archaea. DR eggNOG; COG1236; LUCA. DR InParanoid; Q60355; -. DR KO; K07577; -. DR OMA; QATILRN; -. DR PhylomeDB; Q60355; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR022712; Beta_Casp. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR Pfam; PF10996; Beta-Casp; 1. DR Pfam; PF16661; Lactamase_B_6; 1. DR Pfam; PF07521; RMMBL; 1. DR SMART; SM01027; Beta-Casp; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 428 Uncharacterized protein MJ0047. FT /FTId=PRO_0000106668. SQ SEQUENCE 428 AA; 48492 MW; A649ED66705AA01B CRC64; MEIIFRGAAL EVGRSCIEIK TDKSKILLDC GVKLGKEIEY PILDNSIRDV DKVFISHAHL DHSGALPVLF HRKMDVPVIT TELSKKLIKV LLKDMVKIAE TENKKIPYNN HDVKEAIRHT IPLNYNDKKY YKDFSYELFS AGHIPGSASI LLNYQNNKTI LYTGDVKLRD TRLTKGADLS YTKDDIDILI IESTYGNSIH PDRKAVELSF IEKIKEILFR GGVALIPVFA VDRAQEILLI LNDYNIDAPI YLDGMAVEVT KLMLNYKHML NESSQLEKAL KNVKIIEKSE DRIKAIENLS KNGGIVVTTA GMLDGGPILY YLKLFMHNPK NALLLTGYQV RDSNGRHLIE TGKIFIGKDE IKPNLEVCMY NFSCHAGMDE LHEIIKKVNP ELLIIQHGEE VQATILRNWA LEHGFDAITP KLGEKIRI // ID Y064_METJA Reviewed; 189 AA. AC Q60376; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0064; GN OrderedLocusNames=MJ0064; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98051.1; -; Genomic_DNA. DR PIR; H64307; H64307. DR ProteinModelPortal; Q60376; -. DR STRING; 243232.MJ_0064; -. DR EnsemblBacteria; AAB98051; AAB98051; MJ_0064. DR KEGG; mja:MJ_0064; -. DR eggNOG; arCOG03876; Archaea. DR eggNOG; ENOG4111Z73; LUCA. DR OMA; EIHYGLK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 189 Uncharacterized protein MJ0064. FT /FTId=PRO_0000106675. SQ SEQUENCE 189 AA; 21635 MW; BC45A1FC9AD8DB58 CRC64; MIKMNDKQAD WLNKLIEELD KSSSSVLETE IVLDEIITKL NNLISEINNY ITEIHYGLRI TNERINLSVS ELDELEKKLK EYLDFAENMK KSVENTHNAI IAVKNEMRDI KHSLEESSLK ISNRYNLMED TLKHHSKKIE SLSNSIKSLS KTQESIINSI NSTKMLLYIT IALTVVNLII SLKTSGIIG // ID Y072_METJA Reviewed; 44 AA. AC Q60378; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0072; GN OrderedLocusNames=MJ0072; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98054.1; -; Genomic_DNA. DR PIR; H64308; H64308. DR STRING; 243232.MJ_0072; -. DR EnsemblBacteria; AAB98054; AAB98054; MJ_0072. DR KEGG; mja:MJ_0072; -. DR eggNOG; arCOG05114; Archaea. DR eggNOG; COG4087; LUCA. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR023214; HAD-like_dom. DR SUPFAM; SSF56784; SSF56784; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 44 Uncharacterized protein MJ0072. FT /FTId=PRO_0000106680. SQ SEQUENCE 44 AA; 4889 MW; C742DB9EBBC1F451 CRC64; MIILLDLNGT IATDGKIKEG VKERLTILKE RAEIYILSAD TSEL // ID Y076_METJA Reviewed; 113 AA. AC Q60383; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MJ0076; GN OrderedLocusNames=MJ0076; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98057.1; -; Genomic_DNA. DR PIR; E64309; E64309. DR STRING; 243232.MJ_0076; -. DR EnsemblBacteria; AAB98057; AAB98057; MJ_0076. DR KEGG; mja:MJ_0076; -. DR eggNOG; arCOG08279; Archaea. DR eggNOG; ENOG410Y63Y; LUCA. DR OMA; QFRIEEN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 113 Uncharacterized protein MJ0076. FT /FTId=PRO_0000106682. SQ SEQUENCE 113 AA; 12949 MW; 1669DA93CD1F2F5C CRC64; MEVNLLSISI KPPIKIPKNK TVELDVDWNI EYKKLDAKKF NFVCNIKAYG DFSFEANIEG EISTENDYDN IPDFISVSIV ENLMKSLPKL VSYAQQFRIE ENVFVNQPLS LAS // ID Y086_METJA Reviewed; 372 AA. AC Q57551; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 74. DE RecName: Full=Uncharacterized protein MJ0086; DE EC=2.1.1.-; GN OrderedLocusNames=MJ0086; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the class I-like SAM-binding CC methyltransferase superfamily. Cation-independent O- CC methyltransferase family. {ECO:0000255|PROSITE-ProRule:PRU01020}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98068.1; -; Genomic_DNA. DR PIR; F64310; F64310. DR ProteinModelPortal; Q57551; -. DR STRING; 243232.MJ_0086; -. DR EnsemblBacteria; AAB98068; AAB98068; MJ_0086. DR KEGG; mja:MJ_0086; -. DR eggNOG; arCOG03411; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q57551; -. DR OMA; CKCWELQ; -. DR PhylomeDB; Q57551; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008171; F:O-methyltransferase activity; IBA:GO_Central. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0019438; P:aromatic compound biosynthetic process; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR031725; ASMT_dimerisation. DR InterPro; IPR016461; O-MeTrfase_COMT. DR InterPro; IPR001077; O_MeTrfase_2. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF16864; Dimerisation2; 1. DR Pfam; PF00891; Methyltransf_2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51683; SAM_OMT_II; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 372 Uncharacterized protein MJ0086. FT /FTId=PRO_0000106687. FT REGION 227 229 S-adenosyl-L-methionine binding. FT {ECO:0000255|PROSITE-ProRule:PRU01020}. FT BINDING 202 202 S-adenosyl-L-methionine. FT {ECO:0000255|PROSITE-ProRule:PRU01020}. SQ SEQUENCE 372 AA; 43285 MW; E2665D92DE83E317 CRC64; MLLKSPDKSP EKILKLFDEV YSKARIFYLL RTAIDLNLFE YLSSFKTAKE LAEILDADLI LMEYMLKILN ELDLIESKVV SERIYYKNAE ITNIYLKKDS NYSIINPIYS YFENIKNWEN LADILKNKSN CSNMDVDNFF PKVVRRMADE CKCWELQKVL NYMAKYEEFK NAKKLLDLAG GHGLYAIGFS MLNRNLKCYV FDLPNVIEET KKFIKKYNAK NVFTITGDFY KDDIGKGYDI IFCSYNPGGK NPKIAEKVYN ALNEGGLFIN KQFFPDKEEG IEDYINNMEW NFSKPEGLKK GKIRYTFEGD LNLNDYLKYL EDLGFKILEV VDMSELLGLD ENSSSFRKSA NPSDSLRFKD NSPAKMIVAK KL // ID Y1002_METJA Reviewed; 309 AA. AC Q58408; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=Uncharacterized protein MJ1002; GN OrderedLocusNames=MJ1002; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 DAC domain. {ECO:0000255|PROSITE- CC ProRule:PRU01130}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99005.1; -; Genomic_DNA. DR PIR; A64425; A64425. DR ProteinModelPortal; Q58408; -. DR STRING; 243232.MJ_1002; -. DR PRIDE; Q58408; -. DR EnsemblBacteria; AAB99005; AAB99005; MJ_1002. DR KEGG; mja:MJ_1002; -. DR eggNOG; arCOG04453; Archaea. DR eggNOG; COG1624; LUCA. DR InParanoid; Q58408; -. DR OMA; CAGRYIS; -. DR PhylomeDB; Q58408; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030955; F:potassium ion binding; IEA:InterPro. DR GO; GO:0004743; F:pyruvate kinase activity; IEA:InterPro. DR Gene3D; 3.40.1380.20; -; 1. DR InterPro; IPR003390; DNA_integrity_scan_DisA_N. DR InterPro; IPR015794; Pyrv_Knase_a/b. DR InterPro; IPR015795; Pyrv_Knase_C. DR InterPro; IPR014499; UCP019073. DR Pfam; PF02457; DisA_N; 1. DR Pfam; PF02887; PK_C; 1. DR PIRSF; PIRSF019073; UCP019073; 1. DR SUPFAM; SSF52935; SSF52935; 1. DR PROSITE; PS51794; DAC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 309 Uncharacterized protein MJ1002. FT /FTId=PRO_0000107138. FT DOMAIN 144 301 DAC. {ECO:0000255|PROSITE- FT ProRule:PRU01130}. SQ SEQUENCE 309 AA; 34380 MW; 382D44A261C76907 CRC64; MIAKYIIKHG LELAYDIKAD AFMIFTETGK SYELLKSFLK KDEHSGIIKI LDKISHKNVK IIVATPNQVT YKKISSENEE NIYPIFIKHR EDNRCMIISS GIVHALKMKI LKENNKIVAV VGEPKTPGKL DTIMVVNVKE HVKTITLYEL FETLDEKQKR TLKEIIKLAM EIGREGREGE YVGTIFVMGD TLNVMSMSKP LILNPFAGHN ASIFDENVKG TIKELSSIDG AFIITDEGKV VSAGRFLEIK GDVNIPKGLG ARHLAAASIS KNTNAIAVTV SQSGGIVRVF KDGKIVFETD PRANILFFD // ID Y1023_METJA Reviewed; 262 AA. AC Q58429; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ1023; GN OrderedLocusNames=MJ1023; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99027.1; -; Genomic_DNA. DR PIR; F64427; F64427. DR ProteinModelPortal; Q58429; -. DR STRING; 243232.MJ_1023; -. DR EnsemblBacteria; AAB99027; AAB99027; MJ_1023. DR KEGG; mja:MJ_1023; -. DR eggNOG; arCOG00197; Archaea. DR eggNOG; COG4152; LUCA. DR InParanoid; Q58429; -. DR KO; K01990; -. DR OMA; WCARIDV; -. DR PhylomeDB; Q58429; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 262 Uncharacterized ABC transporter ATP- FT binding protein MJ1023. FT /FTId=PRO_0000093223. FT DOMAIN 5 223 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 37 44 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 262 AA; 30316 MW; B195338E6ACED777 CRC64; MKPKIKVENL TKYFGDKKVL DEISFEVYEG EIFGLLGHNG AGKTTTLRIL AGIIEEYTGY VEVNGKIGYL PEERGLYRDE KVVDVLKFFG ELAGMKKEEI AKSIDYWLNK LKISNYKYSK IKELSKGNQQ KVQFIVSVIH NPDIVILDEP FSGLDVVNVR LLRDIIFELK EEGKTIILST HQLEKIERLC DRVLILKKGK AVHYGKIEDI CRKMAYIEYL DNGKLIKKEI PYEEAVLILK EKAEDVIKFE VRYSLEDLFL DE // ID Y1032_METJA Reviewed; 366 AA. AC Q58438; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1032; GN OrderedLocusNames=MJ1032; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To A.fulgidus AF2058. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99036.1; -; Genomic_DNA. DR PIR; G64428; G64428. DR ProteinModelPortal; Q58438; -. DR STRING; 243232.MJ_1032; -. DR EnsemblBacteria; AAB99036; AAB99036; MJ_1032. DR KEGG; mja:MJ_1032; -. DR eggNOG; arCOG04151; Archaea. DR eggNOG; COG2237; LUCA. DR InParanoid; Q58438; -. DR KO; K08975; -. DR OMA; TYYLIQE; -. DR PhylomeDB; Q58438; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007254; DUF373. DR Pfam; PF04123; DUF373; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 366 Uncharacterized protein MJ1032. FT /FTId=PRO_0000107149. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 256 276 Helical. {ECO:0000255}. FT TRANSMEM 299 319 Helical. {ECO:0000255}. FT TRANSMEM 325 345 Helical. {ECO:0000255}. SQ SEQUENCE 366 AA; 41470 MW; 86D639A1A69BB9B2 CRC64; MEKEGVKNYL VLVVDIDDDI GRKAGLNTPI LGREENIKAL IKLGLADPGD SDVNAILGGV KIYDELKASG KDVEIATISG DVDVESEKCA LRIKEQIDFL LYLYNPDFIY LVSDGKEDEM ILKYLESKNI FVWKKRVIVK QSETLESTYY LIQEFIKKTM EEYIPLILTF IGFSLILYAI FADIGWRIVV GIIGLYILSE GVGVRKLLME KIKKKEEFDV GRVFPISASI SIFILIIGLI YSLSSINKTS STLTEFIGEF LLHFVDSLTL SLLILMVGKF VDTIINSEKD LLEILKKYFF CLICIFISRE LIISGGEYLL KKISFIMFVM CVIIYISIVI ILSVILFTKS SKEDKFKKLK NSITKG // ID Y1055_METJA Reviewed; 326 AA. AC Q58455; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ1055; GN OrderedLocusNames=MJ1055; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the NAD(P)-dependent epimerase/dehydratase CC family. dTDP-glucose dehydratase subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99057.1; -; Genomic_DNA. DR PIR; F64431; F64431. DR ProteinModelPortal; Q58455; -. DR STRING; 243232.MJ_1055; -. DR EnsemblBacteria; AAB99057; AAB99057; MJ_1055. DR KEGG; mja:MJ_1055; -. DR eggNOG; arCOG01369; Archaea. DR eggNOG; COG0451; LUCA. DR InParanoid; Q58455; -. DR KO; K08679; -. DR OMA; YGANETM; -. DR PhylomeDB; Q58455; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0050662; F:coenzyme binding; IEA:InterPro. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001509; Epimerase_deHydtase_N. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR008089; Nuc_sugar_epim. DR Pfam; PF01370; Epimerase; 1. DR PRINTS; PR01713; NUCEPIMERASE. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; NAD; Reference proteome. FT CHAIN 1 326 Uncharacterized protein MJ1055. FT /FTId=PRO_0000183264. FT ACT_SITE 157 157 Proton acceptor. {ECO:0000250}. FT BINDING 132 132 Substrate. {ECO:0000250}. SQ SEQUENCE 326 AA; 38369 MW; 4A45A975ECC0FB78 CRC64; MKYKNILVTG SAGFIGFHLS KYLMDNYEDL KVIGIDNLNN YYNPVLKEKR NEILKNYENY TFIKLDFSDW DDLVENLKDK EIDLIVHLGA QAGVRYSLQN PWAYIKSNEM GTLNIFEFAR RFDIEKVVYA SSSSVYGGNR KIPFSEDDRV DKPISLYAST KRSNELMAHV YHHLYGIKMI GLRFFTVYGE YGRPDMAYFK FAKNILLGKE IEVYNYGNME RDFTYISDVV DGILRAIKKD FDYEIFNLGN SKPVKLMYFI ELIEKYLNKK AKKKFLPMQD GDVLRTYADL SKSEKLLGYK PKVTIEEGLK RFCNWFLENK DWLLRL // ID Y1058_METJA Reviewed; 609 AA. AC Q58458; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ1058; GN OrderedLocusNames=MJ1058; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the NodU/CmcH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99062.1; -; Genomic_DNA. DR PIR; A64432; A64432. DR ProteinModelPortal; Q58458; -. DR STRING; 243232.MJ_1058; -. DR EnsemblBacteria; AAB99062; AAB99062; MJ_1058. DR KEGG; mja:MJ_1058; -. DR eggNOG; arCOG01188; Archaea. DR eggNOG; COG2192; LUCA. DR InParanoid; Q58458; -. DR KO; K00612; -. DR OMA; SPYMERT; -. DR PhylomeDB; Q58458; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR InterPro; IPR031730; Carbam_trans_C. DR InterPro; IPR003696; Carbtransf_dom. DR Pfam; PF16861; Carbam_trans_C; 1. DR Pfam; PF02543; Carbam_trans_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Transferase. FT CHAIN 1 609 Uncharacterized protein MJ1058. FT /FTId=PRO_0000207858. SQ SEQUENCE 609 AA; 71733 MW; C91899CF01CB84EA CRC64; MVKILGVKYF LHDSGVFYID TKNKEIFGIL TERVTRIKHD GGTVIPILNE YPKLKNIDYV AYPFEQTNLD FILFKHIDDY IKRTYKPKYI KEYAKYKKEL SQNKTKFVLN NIYRPFIWEI LAVYGLRKLL FKRFNNIYNK LGNLAIKREL KKIFRKDVSL YEHHLCHAAS AYYFSPFFPK ETLVFTLDGI GDWKYHSLWL FKEYDYRLVS YSSFDIICYD DVEGIFKGAS IGHIYSLFTE ILGFTPNSDE GKTEALAAYG KPNGELYNLL KKGYKINKEK LRWEHDINIL KKLHNKQYLQ KWKEKIGDEN FAATIQRWLE DTVVEYLNIV YEKFKIQRLA MAGGVVANVI MNLNIFERTP FEELYIFPAM GDDGVAAGAA ILKAVELGED ISWLKDLEMP YWGPNYSRED VEKELKKDKW KDKITYEYIG EKWPEIAAEM IAKGNIIAVY QGKMEFGPRA LGNRSILADP RDPKTRDKIN STVKRRPWFQ PFCPSVLEEE RERLFEKSYK HKHMAIAFRM KKEFWDKLPS AMHIDGTARP QFVEEKDNPN YYRLLKKFKE ITGYGIVINT SFNLHGRTIV RTPEDAITDF IDCNIDAMFI EGYLVKRKI // ID Y105_METJA Reviewed; 152 AA. AC Q57569; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0105; GN OrderedLocusNames=MJ0105; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98085.1; -; Genomic_DNA. DR PIR; A64313; A64313. DR STRING; 243232.MJ_0105; -. DR EnsemblBacteria; AAB98085; AAB98085; MJ_0105. DR KEGG; mja:MJ_0105; -. DR eggNOG; arCOG04420; Archaea. DR eggNOG; COG1935; LUCA. DR InParanoid; Q57569; -. DR KO; K09135; -. DR OMA; SICRVQL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007417; DUF473. DR Pfam; PF04322; DUF473; 1. DR ProDom; PD020987; DUF473; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 152 Uncharacterized protein MJ0105. FT /FTId=PRO_0000106694. SQ SEQUENCE 152 AA; 17506 MW; CB08D268DAA85897 CRC64; MDTTRPLSWD FQSQLMSNLK ILYCLNMLKL SNWYFGGIMK VYGLFGINEN AINDFIENHI KTFTIINALN LETVKNLKEG DLVFITSTLR EDLRNGTEGI LGRVINVSLV PQMINGFEEK EIIAGRVQLE MLGFAKCVKY ESIHVEITFR MY // ID Y1061_METJA Reviewed; 333 AA. AC Q58461; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Uncharacterized membrane protein MJ1061; GN OrderedLocusNames=MJ1061; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the polysaccharide synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99064.1; -; Genomic_DNA. DR PIR; D64432; D64432. DR ProteinModelPortal; Q58461; -. DR STRING; 243232.MJ_1061; -. DR EnsemblBacteria; AAB99064; AAB99064; MJ_1061. DR KEGG; mja:MJ_1061; -. DR eggNOG; arCOG01375; Archaea. DR eggNOG; COG1086; LUCA. DR InParanoid; Q58461; -. DR OMA; ICIHAAA; -. DR PhylomeDB; Q58461; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003869; Polysac_CapD-like. DR Pfam; PF02719; Polysacc_synt_2; 1. DR SUPFAM; SSF51735; SSF51735; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 333 Uncharacterized membrane protein MJ1061. FT /FTId=PRO_0000166459. SQ SEQUENCE 333 AA; 37846 MW; DA8F3AB5129344B6 CRC64; MFQDISNFYK DKTILVTGGT GSIGKEIVKT LLKFNPKTIR VLDINETALF ELEHELNSEK IRCFIGDVRD KDRLKRAIEE VDVVFHAAAL KHVPLCEYNP FEAVKTNVIG TQNLIEVAMD EEVEKFITIS TDKAVNPVNV MGATKLLAER LTISANLYKG KRKTAFSVVR FGNVLNSRGS ILPLLKEQIK KGGPVTLTHP DMTRFIMSIN EAVKLVLKAC YLAKGGEIFI LKMPSVRIKD LIEVVIEELA PKYGYKPEDI EIKIIGKRPG EKLYEELIIE EEIYNLEELE DMFVVYPYGV DGNKNNKIIY NSKDAKFLNK EKIKKILKEI SYL // ID Y1086_METJA Reviewed; 340 AA. AC Q58486; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1086; GN OrderedLocusNames=MJ1086; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99087.1; -; Genomic_DNA. DR PIR; E64435; E64435. DR ProteinModelPortal; Q58486; -. DR STRING; 243232.MJ_1086; -. DR DNASU; 1451982; -. DR EnsemblBacteria; AAB99087; AAB99087; MJ_1086. DR KEGG; mja:MJ_1086; -. DR eggNOG; arCOG01831; Archaea. DR eggNOG; COG1665; LUCA. DR InParanoid; Q58486; -. DR KO; K09717; -. DR OMA; FDNPAVY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 340 Uncharacterized protein MJ1086. FT /FTId=PRO_0000107164. SQ SEQUENCE 340 AA; 40555 MW; CC82FB3F988358C1 CRC64; MKVRIRDFIE TTEGLYFAVN TYAHPKNKFF AFLRYVPYEF VDFKIEDNNI REINGRKYIK MAESKIAYKF LEEKFSKYLY YDETINVLMH AIPKEDVKRI LRPKERLNEI INEENNLNEL EEKCRKLALI LEDYGVPIKS MGVSGSLLLK LNNKNSDIDF VIYGKDMHKK AREALKQAFE DNKLKPLSDD FWKIAYKKRI KDKTLTYEEF VFYEKRKYNR GIVDNTMFDL LFTREWDEIT EKYGDKRYKN LGFAKIEGRV LNDDFAFDNP AVYKIECYND EDIKEVVSFT HTYAGQCFNG EEIVARGKLE EVIDKSGERY KRIVVGTTRE AFNEYIKIKR // ID Y1094_METJA Reviewed; 385 AA. AC Q58494; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1094; GN OrderedLocusNames=MJ1094; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 YcaO domain. {ECO:0000255|PROSITE- CC ProRule:PRU00999}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99097.1; -; Genomic_DNA. DR PIR; E64436; E64436. DR STRING; 243232.MJ_1094; -. DR EnsemblBacteria; AAB99097; AAB99097; MJ_1094. DR KEGG; mja:MJ_1094; -. DR eggNOG; arCOG02882; Archaea. DR eggNOG; COG1944; LUCA. DR InParanoid; Q58494; -. DR KO; K09136; -. DR OMA; VYAGKGA; -. DR PhylomeDB; Q58494; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR017667; Methan_mark_1. DR InterPro; IPR003776; YcaO-like_dom. DR Pfam; PF02624; YcaO; 1. DR TIGRFAMs; TIGR03266; methan_mark_1; 1. DR TIGRFAMs; TIGR00702; TIGR00702; 1. DR PROSITE; PS51664; YCAO; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 385 Uncharacterized protein MJ1094. FT /FTId=PRO_0000144980. FT DOMAIN 67 385 YcaO. {ECO:0000255|PROSITE- FT ProRule:PRU00999}. SQ SEQUENCE 385 AA; 44159 MW; 22E404017BE43946 CRC64; MDIKYKLASY RICSPEETFE KIQEALKKIE TVEIKNIQHL DKVNIPVYYL KRRVVVDGKE GIAIHYGKGA NDIQAKVSAC MEAIERFSAS YDKNKVKEKP DNPINVEDLI LPQYADKNVK EWVEGIDIIN NETIDVPADA VFYPTSGKLF RGNTNGLASG NNLDEAILHA TLEIIERDAW SLADLARKIP TKINPEDAKN PLIHELIEKY EKAGVKIILK DLTSEFEIPV VAAISDDLSK NPLMLCVGVG CHLHPEIAIL RALTEVAQSR ASQLHGFRRD AKLREEFTSK IPYERLKRIH RKWFEFEGEI NIADMPNNAR YDLKKDLKFI KDKLSEFGFD KLIYVDLNKV GVDAVRVIIP KMEVYTIDRD RLSRRAFERV KKLYY // ID Y1120_METJA Reviewed; 279 AA. AC Q58520; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 85. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ1120; GN OrderedLocusNames=MJ1120; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99121.1; -; Genomic_DNA. DR PIR; G64439; G64439. DR ProteinModelPortal; Q58520; -. DR STRING; 243232.MJ_1120; -. DR EnsemblBacteria; AAB99121; AAB99121; MJ_1120. DR KEGG; mja:MJ_1120; -. DR eggNOG; arCOG00225; Archaea. DR eggNOG; COG0583; LUCA. DR OMA; AHRIVWK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 279 Uncharacterized HTH-type transcriptional FT regulator MJ1120. FT /FTId=PRO_0000105832. FT DOMAIN 14 71 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 31 50 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 279 AA; 32209 MW; 2F15753B5BAB4952 CRC64; MKVDLTIEYR GKLITPNQIK LLIALHKTKS QNEAAKLLNI KPSSFNIQLK RLENKLGVKL YYSSPNGTVL TDAGLEILET YNSYSKRLKN HFFTVSGFVS GEIAKILFGN PIITSFDNAL KLLKMGFVDV LGVDDSYWIY RLGDERFLKS EIGSCDFNIF LIAYDNFVMV SKKEFNYKNL VGIRFSSQRI VYNILKKEGI KFKVKVRVKN PFRAIELVNE GYSLFLNESL LRYIDGDFNV IYPNFYEKTV HAINFISFGK DIEIDKKEIK KIKKLGFKI // ID Y1151_METJA Reviewed; 113 AA. AC Q58551; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ1151; GN OrderedLocusNames=MJ1151; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99157.1; -; Genomic_DNA. DR PIR; F64443; F64443. DR STRING; 243232.MJ_1151; -. DR EnsemblBacteria; AAB99157; AAB99157; MJ_1151. DR KEGG; mja:MJ_1151; -. DR eggNOG; arCOG10934; Archaea. DR eggNOG; ENOG411102U; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 113 Uncharacterized protein MJ1151. FT /FTId=PRO_0000107189. FT COMPBIAS 5 110 Lys-rich. SQ SEQUENCE 113 AA; 14013 MW; EDC0A02B7BA09293 CRC64; MIIMKPRNKR NKKFKKPEWL IEVEDKIEKM ADEEFDKLFE EIYEKLNRGG LREVLNVHKT DKSKYKKYKK PKWLIEAEKE LEKAIETGEY FKWLKEQGEK YRKQKKEIKK NNF // ID Y1158_METJA Reviewed; 129 AA. AC Q58557; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1158; GN OrderedLocusNames=MJ1158; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99174.1; -; Genomic_DNA. DR PIR; D64444; D64444. DR ProteinModelPortal; Q58557; -. DR STRING; 243232.MJ_1158; -. DR EnsemblBacteria; AAB99174; AAB99174; MJ_1158. DR KEGG; mja:MJ_1158; -. DR eggNOG; arCOG05070; Archaea. DR eggNOG; ENOG410XZEP; LUCA. DR OMA; RNCGFTR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MJ1158. FT /FTId=PRO_0000107196. SQ SEQUENCE 129 AA; 15359 MW; FFD2D590CCC5C7B0 CRC64; MWGIQHFGDF MEKWELKKLA VCFNCKKEAD QIIEIYTNQA FVKCSNCGAT RYYILRRVGI EDESIIEDEK NKKHKYEPWF LEKTAVCFNC KKEATQDIAI TETKMIVRCR NCGFTRVYQF HILDIPENK // ID Y115_METJA Reviewed; 155 AA. AC Q57579; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0115; GN OrderedLocusNames=MJ0115; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98096.1; -; Genomic_DNA. DR PIR; C64314; C64314. DR STRING; 243232.MJ_0115; -. DR EnsemblBacteria; AAB98096; AAB98096; MJ_0115. DR KEGG; mja:MJ_0115; -. DR eggNOG; arCOG04853; Archaea. DR eggNOG; COG4008; LUCA. DR OMA; MGEDEYM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR017671; Methan_mark_9. DR TIGRFAMs; TIGR03277; methan_mark_9; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein MJ0115. FT /FTId=PRO_0000106699. SQ SEQUENCE 155 AA; 17727 MW; E28BB0FD12CB1745 CRC64; MGWENAPSHI CRGGDLRGLA FCCPPIKYCP IHKALAVLKM SPEEFIRIKE EFGKRTKLGL GENTCFGSLV WCCKITKPCP YRDYELAKNN ISPDEYMELK KQLAEEIIRN SQFFKEAVEV FVKKGIPKDI AEKCILETGD LKKAYEMAIK MIDKD // ID Y1162_METJA Reviewed; 218 AA. AC Q58562; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Uncharacterized protein MJ1162; GN OrderedLocusNames=MJ1162; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99164.1; -; Genomic_DNA. DR PIR; A64445; A64445. DR ProteinModelPortal; Q58562; -. DR STRING; 243232.MJ_1162; -. DR EnsemblBacteria; AAB99164; AAB99164; MJ_1162. DR KEGG; mja:MJ_1162; -. DR eggNOG; arCOG01145; Archaea. DR eggNOG; COG2129; LUCA. DR InParanoid; Q58562; -. DR KO; K07096; -. DR OMA; VPGNCDP; -. DR PhylomeDB; Q58562; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MJ1162. FT /FTId=PRO_0000107198. SQ SEQUENCE 218 AA; 24676 MW; 2F9D763416039EE4 CRC64; MVKYMKIVGI TDLHGKLPPA VREFKDFADV LVVCGDITHF GKGIEVIEKL AELSDYMEVL CVPGNCDTKE VIDELNSFKL NIDRKVKKIE NINFVGIGGS NKTPFNTPNE YTEEEIYNKL INVVKNLKNI FLVSHAPPYN TMADIVDLDK DIHVGSKSIR KIIEDFNENI RFCACGHIHE SRCIDKIGNT IVVNPSPKSY FVYDTKKNMV VLDDFNGF // ID Y1164_METJA Reviewed; 318 AA. AC Q58564; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative HTH-type transcriptional regulatory protein MJ1164 {ECO:0000255|HAMAP-Rule:MF_00584}; GN OrderedLocusNames=MJ1164; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|HAMAP-Rule:MF_00584}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99166.1; -; Genomic_DNA. DR PIR; C64445; C64445. DR ProteinModelPortal; Q58564; -. DR STRING; 243232.MJ_1164; -. DR EnsemblBacteria; AAB99166; AAB99166; MJ_1164. DR KEGG; mja:MJ_1164; -. DR eggNOG; arCOG04152; Archaea. DR eggNOG; COG1395; LUCA. DR InParanoid; Q58564; -. DR KO; K07728; -. DR OMA; GVVYFRH; -. DR PhylomeDB; Q58564; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR HAMAP; MF_00584; HTH_type_cro_C1; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR020886; Tscrpt_reg_HTH_Cro/C1. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 318 Putative HTH-type transcriptional FT regulatory protein MJ1164. FT /FTId=PRO_0000144856. FT DOMAIN 131 189 HTH cro/C1-type. {ECO:0000255|HAMAP- FT Rule:MF_00584}. FT DNA_BIND 142 161 H-T-H motif. {ECO:0000255|HAMAP- FT Rule:MF_00584}. SQ SEQUENCE 318 AA; 36530 MW; F7E61B67F09263CD CRC64; MMIMREILIS ECIELLRSHK FIVSKPLGRS CFDMVASKED IRLILKILKN IDSLSRDQSK ELKKISKILH GTPLIIGIRT RNAPMEHGVV YDRYNIKAVT FETFRDYLEG SPPMVYANRG GFFVKIDGKV LKEVREAMGI SVGKLAEVAG VSRKAIYKYE TQMANPSVDV ALKIEEFLDV PLVKGIDLFE PVDDEDVENK LENLEDFKKE AINFLNELGF KSFVVEKAPF DAVAEKDMDN NLNILLTNIE EKDNEEVKRK ALFVRELSRL LDGYSLLILE EKEKEYKNLP VVSIEELKKM DDALELIEHI KSMLRDIR // ID Y1219_METJA Reviewed; 104 AA. AC Q58616; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1219; GN OrderedLocusNames=MJ1219; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99224.1; -; Genomic_DNA. DR PIR; B64452; B64452. DR STRING; 243232.MJ_1219; -. DR EnsemblBacteria; AAB99224; AAB99224; MJ_1219. DR KEGG; mja:MJ_1219; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 104 Uncharacterized protein MJ1219. FT /FTId=PRO_0000107221. FT TRANSMEM 53 73 Helical. {ECO:0000255}. FT TRANSMEM 74 94 Helical. {ECO:0000255}. SQ SEQUENCE 104 AA; 11505 MW; 3306B9A4AC3C0E72 CRC64; MVNMAPNTNF ASLVAVAGCV LLGYNYYTGN IFCGVIGSLL LFGALWSLNG GKIWGIISFI ISASIFCYIN WDFILNLLFY SIIAFIVMSI LILIFGNNRG GYYY // ID Y1232_METJA Reviewed; 296 AA. AC Q58629; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 90. DE RecName: Full=Uncharacterized protein MJ1232; GN OrderedLocusNames=MJ1232; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99237.1; -; Genomic_DNA. DR PIR; G64453; G64453. DR ProteinModelPortal; Q58629; -. DR STRING; 243232.MJ_1232; -. DR EnsemblBacteria; AAB99237; AAB99237; MJ_1232. DR KEGG; mja:MJ_1232; -. DR eggNOG; arCOG00610; Archaea. DR eggNOG; COG2524; LUCA. DR InParanoid; Q58629; -. DR KO; K07744; -. DR OMA; PKGGYKA; -. DR PhylomeDB; Q58629; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016436; UCP005063_CBS. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR InterPro; IPR005104; WHTH_HrcA_DNA-bd. DR Pfam; PF00571; CBS; 2. DR Pfam; PF03444; HrcA_DNA-bdg; 1. DR PIRSF; PIRSF005063; UCP005063_CBS_MJ1232; 1. DR SMART; SM00116; CBS; 2. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 296 Uncharacterized protein MJ1232. FT /FTId=PRO_0000107228. FT DOMAIN 176 232 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 236 292 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 296 AA; 33205 MW; 7A4CDB4858A9719C CRC64; MELTVVQREI LQELINLYRE KNRPIKGTEI ALRLNRNPGT IRNQMQALRA LDLVDGVPGP KGGYVPTSKA YRALGLEDEG EIIVPIYKDG KKVEGVKVVK IEFDTVSHEK CCSSKIHIEG DTKHFNIGDI IRVGPTYHNK IIINGKIIGR DDIHRILLID VLGVSSIPNI KVGDVGIKEV WTINPNCTLR ETAKLFAEKY ISGAPVVDND KLVGVISLHD IAENIDNIDK KVKEVMRRDV ITIHKDEKIY DALKIMNKNN VGRLVIVDDN NKIVGIITRT DILKIISGKF PENFHT // ID Y1236_METJA Reviewed; 634 AA. AC Q58633; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 92. DE RecName: Full=Uncharacterized protein MJ1236; GN OrderedLocusNames=MJ1236; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99240.1; -; Genomic_DNA. DR PIR; C64454; C64454. DR ProteinModelPortal; Q58633; -. DR STRING; 243232.MJ_1236; -. DR EnsemblBacteria; AAB99240; AAB99240; MJ_1236. DR KEGG; mja:MJ_1236; -. DR eggNOG; arCOG00543; Archaea. DR eggNOG; COG1782; LUCA. DR InParanoid; Q58633; -. DR KO; K07041; -. DR OMA; HVHIDHC; -. DR PhylomeDB; Q58633; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR022712; Beta_Casp. DR InterPro; IPR019975; KH-dom/beta-lactamase-dom_arc. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004044; KH_dom_type_2. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR Pfam; PF10996; Beta-Casp; 1. DR Pfam; PF07650; KH_2; 1. DR Pfam; PF00753; Lactamase_B; 1. DR Pfam; PF07521; RMMBL; 1. DR SMART; SM01027; Beta-Casp; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR TIGRFAMs; TIGR03675; arCOG00543; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 634 Uncharacterized protein MJ1236. FT /FTId=PRO_0000107231. SQ SEQUENCE 634 AA; 71761 MW; F6FB9D6C07732A15 CRC64; MSAEEVLENI RKEIIKKSPK EAKIVDVQFE GPEVVVYVKN PEIFTNEIIK SLAKDLRKRI SIRPDPSVLV EPEIAKQKIL EIVPEEAEIT NFVFDANTGE VIIESKKPGL VIGKEGKTLE MIKKAIRWAP KPVRTPPIQS ETIKAIRATL YRERHEVKEI LRRIGRRIHR DIVVRGDYWI RVSFLGGARE VGRSCLYVQT PDTRVLIDCG INVACEDKAF PHFDAPEFSI EDLDAVIVTH AHLDHCGFIP GLFRYGYDGP VYCTRPTRDL MTLLQKDYLE IAKKEGKEVP YTSKDIKTCV KHTIPIDYGV TTDISPTIKL TLHNAGHVLG SAIAHLHIGE GLYNLAYTGD IKFETSRLLE PAVCQFPRLE TLIIESTYGA YDDVLPEREE AERELLRVVS ETTDRGGKVL IPVFGVGRAQ ELMLVLEEGY NQGIFNAPVY LDGMIWEATA IHTAYPEYLS KEMRQKIFHE GDNPFLSEVF KRVGSTNERR KVIDSDEPCV ILATSGMLTG GPSVEYLKHL APDEKNAIIF VGYQAEGTLG RKVQSGWKEI PIITRNGKTK SIPINLQVYT IEGFSGHSDR KQLIKYIRRL KPSPEKIIMV HGEESKCLDF ADTVRRLFKK QTYVPMNLDA IRVK // ID Y1281_METJA Reviewed; 1048 AA. AC Q58677; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ1281; GN OrderedLocusNames=MJ1281; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99287.1; -; Genomic_DNA. DR PIR; H64459; H64459. DR ProteinModelPortal; Q58677; -. DR STRING; 243232.MJ_1281; -. DR EnsemblBacteria; AAB99287; AAB99287; MJ_1281. DR KEGG; mja:MJ_1281; -. DR eggNOG; arCOG08205; Archaea. DR eggNOG; arCOG09753; Archaea. DR eggNOG; ENOG411106P; LUCA. DR eggNOG; ENOG41110WX; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 1048 Uncharacterized protein MJ1281. FT /FTId=PRO_0000107249. FT COMPBIAS 598 601 Poly-Glu. SQ SEQUENCE 1048 AA; 121015 MW; 14138CFDCE6A8A76 CRC64; MMILWKRQRT LLKMLLMTLI MEETTTIKEE VFFMKKFVII LTISIAVLFA GCVSEEGSYE ESKISEKSIS SPLDIVPKSS EKVVYTKTEG FVDLLGENSE IVNAYKELIG KYGLSVDDIE YTIQADNTYV LKGYGLDEYK FMDELGLDYK EEKYNGANML INENHNYAVA KYKNYLIHGN TEDVKRVIDT IKGDYPSITE KKEIKDMLSK VDDDYVIANI GRNYKGYYGA FIYLKGRNVE FDVVAVYNDV DDAKEQYEYV KEELEDELDN GNIKDYDIDR DGNIVVAKVI MSKEEFLGDY ANKLGLNFGN EIKYNTENEY NTQTKEKSEF NHDNTNKVNK NINLEEPYNL IPNVFWASYV DVGKFSKVVK GKGVYDELNS ILKCYGLSPD DVEFYMNLET ANLIKTDKLT AKEYLKKLGY SYNEEYYGGA TLLVYTTEVS DMVGKFAATN YKGYFIFGLK GGVEKVIDAI NGKNNLVTED ENIREIINEM PKGYFAFKLY NQFDADGGEF YYDEGDKIVI KGLWICIDDE YAKKRKYIIE NDYENYGYTD YNIEVDGNRV TTTLTIDKDE FGEYDGYTLV SSDWIGLKKL ENCENVNEEE ENQINEEQQT NVENEQQTEQ QFENEDKETN TYELPLTWKE LEVAGMDGVM FDFGNKKVTF EDWKYSPCEF RNPIIIDGNK IWCFGFSGGE YGYFTYNDNM GFDADVDDII LIEMPYNVKA VCDDFYGAGW FIEDDNGKLH HVIFDCPKET IMDKTGNVEI DLAKIKKDVV VANVDVDELM AGAEDNKNNY KIVIGWKGNK LYLITMEKDK FEDWAYNSKY EDGFDEPFPP VQIKEFEFNG NIIDARSDFR NYIIVATENG LYIITVYKRE PDEFKITDSL KTNIECYAFD TGSGLLVYYD GSKVYYTDIK IKSESDNSDI YYIARNYEGG LNIDGVTGLS ICHNYNWLGT QVEVAGDGWI KTYNIEFEAK KDAEGNSVYD ENGNSIYIVK FEPKNVYYDE IYDKYYSISV PFAGKYIYRG DSGDSKNGRV EFRVYTTNNK LYLFGTNW // ID Y1287_METJA Reviewed; 270 AA. AC Q58683; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1287; GN OrderedLocusNames=MJ1287; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99289.1; -; Genomic_DNA. DR PIR; F64460; F64460. DR ProteinModelPortal; Q58683; -. DR STRING; 243232.MJ_1287; -. DR EnsemblBacteria; AAB99289; AAB99289; MJ_1287. DR KEGG; mja:MJ_1287; -. DR eggNOG; arCOG01817; Archaea. DR eggNOG; COG0630; LUCA. DR InParanoid; Q58683; -. DR KO; K07332; -. DR PhylomeDB; Q58683; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 270 Uncharacterized protein MJ1287. FT /FTId=PRO_0000207311. SQ SEQUENCE 270 AA; 31254 MW; 4DDE275588363C6B CRC64; MPTDLIRYGS ISPEMLAYLW LLIEYKNSIM VAGEVATGKT TLLNAFSLFI PPQMKIVSIE DTPEIRLYHE NWIAGTTRSG FGGEEYEITM MDLLKAALRQ RPDYLIVGEV RGEEAKILFQ AITTGHLALS TIHAKSPEAV IRRLNAEPMN IPKIMLEQLN AICMQVRLIY KGRFVRRTKS ITEIVEYDPK IDDIILHDVF RWNPEDDTFE FSGESYLLRR IAEFIGISEK EIINELHSRA EFLRNLCKTK PNFEEFVKKI CEYKEYHKGD // ID Y128_METJA Reviewed; 98 AA. AC Q57592; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0128; GN OrderedLocusNames=MJ0128; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98108.1; -; Genomic_DNA. DR PIR; H64315; H64315. DR ProteinModelPortal; Q57592; -. DR STRING; 243232.MJ_0128; -. DR EnsemblBacteria; AAB98108; AAB98108; MJ_0128. DR KEGG; mja:MJ_0128; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q57592; -. DR KO; K07075; -. DR OMA; IASEIIY; -. DR PhylomeDB; Q57592; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein MJ0128. FT /FTId=PRO_0000106706. SQ SEQUENCE 98 AA; 11565 MW; 02ED1E679CBDA3AC CRC64; MKTISEIKDI LRKHKKILKE KYKVKSIAIF GSYARNEQTE KSDIDILVEF YETPDYLKFF ELEDYLSDLL GIKVDLVIKG AIKNPYIKKS IEEDLIYV // ID Y1290_METJA Reviewed; 312 AA. AC Q58686; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1290; GN OrderedLocusNames=MJ1290; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99296.1; -; Genomic_DNA. DR PIR; A64461; A64461. DR ProteinModelPortal; Q58686; -. DR STRING; 243232.MJ_1290; -. DR EnsemblBacteria; AAB99296; AAB99296; MJ_1290. DR KEGG; mja:MJ_1290; -. DR eggNOG; arCOG08273; Archaea. DR eggNOG; ENOG41110JJ; LUCA. DR OMA; GKYILEY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 312 Uncharacterized protein MJ1290. FT /FTId=PRO_0000107257. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 286 306 Helical. {ECO:0000255}. SQ SEQUENCE 312 AA; 35823 MW; 0E36803803E7605B CRC64; MKKAIYLLIL CIFGLFSVYF TYAENISDIS NTTSKNISSS NISHNNIIYS NINYNEILYI IVKNNTAYVK DVINGTNNPY HIKSAGIILY EKIYGYNYSN LLYRNSSNSL IFYYNFSVDK INYTINITIP QIEDYVGSLG GPIRMRIPPN NVKIIIVAEN KLAETNGKYI LEYNKTDKKV ISLIYLDNVS SICNIYYTKF FNSSEFYGYA VANVTSITEN RTSYTIKNPK GTFTFDRKYN VFVSNKTAYL KEPYLYVKLY NSTIDDIIIL ENNKISENST KFMSNYLLSF IGIIIGFGII GLAIYLSKRG RK // ID Y1293_METJA Reviewed; 231 AA. AC Q58689; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1293; GN OrderedLocusNames=MJ1293; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99309.1; -; Genomic_DNA. DR PIR; D64461; D64461. DR ProteinModelPortal; Q58689; -. DR STRING; 243232.MJ_1293; -. DR EnsemblBacteria; AAB99309; AAB99309; MJ_1293. DR KEGG; mja:MJ_1293; -. DR eggNOG; arCOG05057; Archaea. DR eggNOG; ENOG410YACR; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 231 Uncharacterized protein MJ1293. FT /FTId=PRO_0000107260. FT TRANSMEM 86 106 Helical. {ECO:0000255}. SQ SEQUENCE 231 AA; 26686 MW; D7D34948088BC95A CRC64; MTNKTRKETN EIKNNITLPP NIKTEVNRTS KYDFTNLSKD LEIVYALIKI TGFDEYLPFN IENLNKIFIK EKISPYPYLL NLIKDLIILF VIGLIITIIG LLMYEPTRPK VISIIASILY KLKIKEKPKP KKKETIKLPK PPKIYISDVI YSLGDTVRIE ISSEIDIGNN LYILSPTNKK YKIELIKTGK NKYLGLFKIP ENEVPGQYFI IYKPENLSIG GFLVVDIKKE M // ID Y1301_METJA Reviewed; 400 AA. AC Q58697; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Uncharacterized ATP-binding protein MJ1301; GN OrderedLocusNames=MJ1301; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99326.1; -; Genomic_DNA. DR PIR; D64462; D64462. DR ProteinModelPortal; Q58697; -. DR STRING; 243232.MJ_1301; -. DR DNASU; 1452203; -. DR EnsemblBacteria; AAB99326; AAB99326; MJ_1301. DR KEGG; mja:MJ_1301; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q58697; -. DR KO; K06921; -. DR OMA; REKEIHK; -. DR PhylomeDB; Q58697; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 2. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 400 Uncharacterized ATP-binding protein FT MJ1301. FT /FTId=PRO_0000184675. FT NP_BIND 36 43 ATP. {ECO:0000255}. SQ SEQUENCE 400 AA; 46904 MW; EE9460CAD791D049 CRC64; MGILVIFMKF FNREKEIHKI LSIIEGEPNL IYFIYGSINS GKTALINEII NNRLDKNKYI VFYFDLREIF ISKYDDFIEV LFEEYEGDKS PIEVIKAIIN DLPSLYGIPI PKNTLNEIFK KKTTKNVFRY ITNVLMDIKR EGKQPIIIID ELQKIGDMKI NGFLIYELFN YFVSLTKHKH LCHVFCLSSD SLFIERVYNE AMLEDRVDYI LVDDHRGGYA PSIGILPQIE SGVAFGNPAL EYSNRGFASM RGEYILVDDF DKETALKFMD FLAKENNMSL TNEDKELIYN YVGGKPVLII KVIDKLRYEN LNDILDFMLK DATQKLKYFL EDVKEEDEEL YKKVVDALKL FKEDYEIEDI KIPKKIREFL IKRNILFLNP IEGILKPQSF LVWNAIKKVL // ID Y1302_METJA Reviewed; 168 AA. AC Q58698; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ1302; GN OrderedLocusNames=MJ1302; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99311.1; -; Genomic_DNA. DR PIR; E64462; E64462. DR ProteinModelPortal; Q58698; -. DR STRING; 243232.MJ_1302; -. DR EnsemblBacteria; AAB99311; AAB99311; MJ_1302. DR KEGG; mja:MJ_1302; -. DR eggNOG; arCOG01543; Archaea. DR eggNOG; COG1143; LUCA. DR InParanoid; Q58698; -. DR KO; K14121; -. DR OMA; CHDFCPV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 168 Uncharacterized polyferredoxin-like FT protein MJ1302. FT /FTId=PRO_0000159152. FT DOMAIN 48 78 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 91 122 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 58 58 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 61 61 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 64 64 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 68 68 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 100 100 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 103 103 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 106 106 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 110 110 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 168 AA; 19169 MW; 6BBC523D3DB9AD03 CRC64; MVIELAELKN FAKIFLTGIY ENLERIIFGS GRYTSLEMRN AILTGTVKIP KTVIEELCIG CEGCANVCPT KAIEMIPIEP VKITDNYVKD KIPKINPEKC VYCLYCHDFC PVFSVFNEIS PIHPRDVGEE YIEIDISKLL QKKIEISEEQ INKISSLLSI NLRRIIKD // ID Y1304_METJA Reviewed; 152 AA. AC Q58700; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1304; GN OrderedLocusNames=MJ1304; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HEPN domain. {ECO:0000255|PROSITE- CC ProRule:PRU00105}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99313.1; -; Genomic_DNA. DR PIR; G64462; G64462. DR ProteinModelPortal; Q58700; -. DR STRING; 243232.MJ_1304; -. DR EnsemblBacteria; AAB99313; AAB99313; MJ_1304. DR KEGG; mja:MJ_1304; -. DR eggNOG; arCOG01191; Archaea. DR eggNOG; COG2250; LUCA. DR InParanoid; Q58700; -. DR OMA; WNPLEEY; -. DR PhylomeDB; Q58700; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007842; HEPN_dom. DR Pfam; PF05168; HEPN; 1. DR SMART; SM00748; HEPN; 1. DR PROSITE; PS50910; HEPN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 152 Uncharacterized protein MJ1304. FT /FTId=PRO_0000107262. FT DOMAIN 15 135 HEPN. {ECO:0000255|PROSITE- FT ProRule:PRU00105}. SQ SEQUENCE 152 AA; 18008 MW; 1B234DC43E5D3C84 CRC64; MEDSGFNIKY AKLFIKRAEE DLEVAKVLLK TNHYPDSVYH SQQCVEKAVK AVLILNGIIF RRHVVSGVFR NVIYEMKIED SWKEKLLNLI PKIESLEEHW VMPRYPEPYF GELWNPLEEY TKEDAEECLK DAENVLEVIK DFLKEKYGLK QI // ID Y1306_METJA Reviewed; 83 AA. AC Q58702; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1306; GN OrderedLocusNames=MJ1306; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99314.1; -; Genomic_DNA. DR PIR; A64463; A64463. DR STRING; 243232.MJ_1306; -. DR DNASU; 1452208; -. DR EnsemblBacteria; AAB99314; AAB99314; MJ_1306. DR KEGG; mja:MJ_1306; -. DR eggNOG; arCOG06490; Archaea. DR eggNOG; ENOG410ZC9S; LUCA. DR KO; K14119; -. DR OMA; NYLYYPS; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 83 Uncharacterized protein MJ1306. FT /FTId=PRO_0000107264. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. SQ SEQUENCE 83 AA; 9337 MW; 0D413F375A61DEA4 CRC64; MLDAILSNYL YYPSILAFLF GVLMGAKYRH KIGNIFGYLI LTVVIAYFLK AFPYYDLLPL SCSYLSAVIG IIIGNRLFGG KMI // ID Y1313_METJA Reviewed; 403 AA. AC Q58709; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1313; GN OrderedLocusNames=MJ1313; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH1421. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99320.1; -; Genomic_DNA. DR PIR; H64463; H64463. DR ProteinModelPortal; Q58709; -. DR STRING; 243232.MJ_1313; -. DR EnsemblBacteria; AAB99320; AAB99320; MJ_1313. DR KEGG; mja:MJ_1313; -. DR eggNOG; arCOG04278; Archaea. DR eggNOG; COG1679; LUCA. DR InParanoid; Q58709; -. DR KO; K09123; -. DR OMA; ICIGCPH; -. DR PhylomeDB; Q58709; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR007506; DUF521. DR Pfam; PF04412; DUF521; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 403 Uncharacterized protein MJ1313. FT /FTId=PRO_0000107270. FT NP_BIND 163 176 ATP. {ECO:0000255}. SQ SEQUENCE 403 AA; 44601 MW; DDA9EB7CA167F348 CRC64; MYLTKEEEKI LDGEYGEVLR RCMNLLVSLG DIYGADKLIP ISSAQISGVS YKTIKDIGLE FLEDFAKEDV KVKVYATLNP AGMDLDIWRE LGIDEKFAKK QLRIIEAFKK MEVEISCTCT PYLTGNLPRF GEHISWAESS AVSFANSVLG AKTNREGGPS ALAAAIIGKT PYYGYHLDEN RKTTHIIELD GQLISNFKYG ESFYGALGYL VGKIVKNGIP YFENLYKLNP NNDNLKSLGA AMAASGGIAL YHAKNLTAEC RVKEVVNDKI EKISIGVEEI KEAYEKLNTT NEEPDLICIG CPHCSLMEIK KIAELLKNKK LNADLWVCCS LHIKAIADRM GYTKIIEKAG GKVVKDTCMV VSPIEDLGYK RVATNSGKAA VYLPSFCKSE VIFGDIEELL KGR // ID Y131_METJA Reviewed; 103 AA. AC Q57595; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0131; GN OrderedLocusNames=MJ0131; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98119.1; -; Genomic_DNA. DR PIR; C64316; C64316. DR STRING; 243232.MJ_0131; -. DR EnsemblBacteria; AAB98119; AAB98119; MJ_0131. DR KEGG; mja:MJ_0131; -. DR eggNOG; arCOG06571; Archaea. DR eggNOG; ENOG411111D; LUCA. DR OMA; WIIVNTI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 103 Uncharacterized protein MJ0131. FT /FTId=PRO_0000106709. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. SQ SEQUENCE 103 AA; 11861 MW; F028E0050D09F9A6 CRC64; MPGVIFWTIF IIQFMIWVFL STTKIGRVIA FIWGTMPFLA LYLKYTGYFP TIFENPDVNL FANLLSNFVV EWSYLVVQTT VPSWIGLLFG LKLSGNNDTP QII // ID Y1321_METJA Reviewed; 713 AA. AC Q58717; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1321; GN OrderedLocusNames=MJ1321; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 Piwi domain. {ECO:0000255|PROSITE- CC ProRule:PRU00150}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99334.1; -; Genomic_DNA. DR PIR; H64464; H64464. DR ProteinModelPortal; Q58717; -. DR STRING; 243232.MJ_1321; -. DR EnsemblBacteria; AAB99334; AAB99334; MJ_1321. DR KEGG; mja:MJ_1321; -. DR eggNOG; arCOG03890; Archaea. DR eggNOG; COG1431; LUCA. DR KO; K07578; -. DR OMA; IEVISIR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR003100; PAZ_dom. DR InterPro; IPR003165; Piwi. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF02171; Piwi; 1. DR SMART; SM00950; Piwi; 1. DR SUPFAM; SSF101690; SSF101690; 1. DR SUPFAM; SSF53098; SSF53098; 1. DR PROSITE; PS50822; PIWI; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 713 Uncharacterized protein MJ1321. FT /FTId=PRO_0000107275. FT DOMAIN 426 699 Piwi. {ECO:0000255|PROSITE- FT ProRule:PRU00150}. SQ SEQUENCE 713 AA; 84583 MW; EB0B3265C600DF2D CRC64; MVLNKVTYKI NAYKIKEEFI PKEVHFYRIK SFVNEAFNFY RFVNFYGGMI INKKDKSFVL PYKVDNKVLK YKDGNNEIPI DIEYIKSLKL EYVKPEIAEK LVRGYLKSVH KIEPELSRII KNIRKHKVVE NIKVESYCEY EVKKHDGDYY LILNFRHTAS ITKHLWDFVN RDKALLEEYV GKKIIFKPNP KVRYTISLVD APNPQKIEEI MSHIIKYYKW SEDMVKSTFG EIDYNQPIMY CEEILEPFAP QFCNLVFYMD ELDSYILKEL QSYWRLSNEN KGKIINEIAK KLRFIDNTPK ELEFMKFNNT PLLVKDVNKN PTKIYSTNTL FTWIYNQNAK IYLPYDVPEI IRNKNLLTYI LIDEEIKDEL KAIKDKVNKM FRNYNKIANK TELPKFNYAN RWKYFSTDDI RGIIKEIKSE FNDEICFALI IGKEKYKDND YYEILKKQLF DLKIISQNIL WENWRKDDKG YMTNNLLIQI MGKLGIKYFI LDSKTPYDYI MGLDTGLGIF GNHRVGGCTV VYDSEGKIRR IQPIETPAPG ERLHLPYVIE YLENKANIDM ENKNILFLRD GFIQNSERND LKEISKELNS NIEVISIRKN NKYKVFTSDY RIGSVFGNDG IFLPHKTPFG SNPVKLSTWL RFNCGNEEGL KINESIMQLL YDLTKMNYSA LYGEGRYLRI PAPIHYADKF VKALGKNWKI DEELLKHGFL YFI // ID Y1331_METJA Reviewed; 144 AA. AC Q58727; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Acylphosphatase-like protein MJ1331; GN OrderedLocusNames=MJ1331; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99344.1; -; Genomic_DNA. DR PIR; B64466; B64466. DR ProteinModelPortal; Q58727; -. DR STRING; 243232.MJ_1331; -. DR EnsemblBacteria; AAB99344; AAB99344; MJ_1331. DR KEGG; mja:MJ_1331; -. DR eggNOG; arCOG01674; Archaea. DR eggNOG; COG1254; LUCA. DR InParanoid; Q58727; -. DR OMA; PNEKKRQ; -. DR PhylomeDB; Q58727; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR Pfam; PF00708; Acylphosphatase; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 144 Acylphosphatase-like protein MJ1331. FT /FTId=PRO_0000158564. FT DOMAIN 8 100 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. SQ SEQUENCE 144 AA; 16726 MW; FE4C4BFF88D54D2D CRC64; MVASMATTYE LRIYGNVECA EFIDKVESLG KLLDVNGVVY VYKDSVRILA NFPNEKKRQL FKEIIKDLED DGGLIKVERI EERDLNTYIE FPNGLNKIST NELKEINKKL DKTISYLENI FNALEKQIKV SEEIRDILKD TFEV // ID Y1332_METJA Reviewed; 393 AA. AC Q58728; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized GTP-binding protein MJ1332; GN OrderedLocusNames=MJ1332; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01047}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01047}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99340.1; -; Genomic_DNA. DR PIR; C64466; C64466. DR ProteinModelPortal; Q58728; -. DR STRING; 243232.MJ_1332; -. DR EnsemblBacteria; AAB99340; AAB99340; MJ_1332. DR KEGG; mja:MJ_1332; -. DR eggNOG; arCOG00357; Archaea. DR eggNOG; COG0012; LUCA. DR InParanoid; Q58728; -. DR KO; K06942; -. DR OMA; KQGYIKY; -. DR PhylomeDB; Q58728; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR013646; MMR_HSR1_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004095; TGS. DR InterPro; IPR012676; TGS-like. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF08438; MMR_HSR1_C; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF81271; SSF81271; 1. DR PROSITE; PS51710; G_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 393 Uncharacterized GTP-binding protein FT MJ1332. FT /FTId=PRO_0000205446. FT DOMAIN 2 266 OBG-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 8 15 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 78 82 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. SQ SEQUENCE 393 AA; 44267 MW; 5213CD351907BEC5 CRC64; MAMIGLVGKP NVGKSTMFNA LTEKPAEIGN YPFTTIQPNK GIAYITSPCP CKELGVKCNP RNSKCIDGIR HIPVEVIDVA GLVPGAHEGR GMGNKFLDDL RQADAFILVV DASGKTDAEG NPTENYDPVE DVKFLLNEID MWIYSILTKN WDKLARRAQQ EKNIVKALKD QLSGLNIDED DIKMAIRDMD ESPIKWTEED LLNLAKKLRK ISKPMIIAAN KADHPDAEKN IERLKKEFKD YIVIPTSAEI ELALKRAEKA GIIKRKENDF EIIDESKVNE QMRRAFDYIK DFLKKYGGTG VQECINKAYF DLLDMIVVYP VEDENKFSDK QGNVLPDAFL VKKGSTARDL AYKVHTELGE KFIYAIDAKK KIRVGADYEL KHNDIIKIVS AAK // ID Y1334_METJA Reviewed; 283 AA. AC Q58730; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative UTP--glucose-1-phosphate uridylyltransferase; DE EC=2.7.7.9; DE AltName: Full=Alpha-D-glucosyl-1-phosphate uridylyltransferase; DE AltName: Full=UDP-glucose pyrophosphorylase; DE Short=UDPGP; DE AltName: Full=Uridine diphosphoglucose pyrophosphorylase; GN OrderedLocusNames=MJ1334; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: UTP + alpha-D-glucose 1-phosphate = CC diphosphate + UDP-glucose. CC -!- SIMILARITY: Belongs to the UDPGP type 2 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99341.1; -; Genomic_DNA. DR PIR; E64466; E64466. DR ProteinModelPortal; Q58730; -. DR STRING; 243232.MJ_1334; -. DR EnsemblBacteria; AAB99341; AAB99341; MJ_1334. DR KEGG; mja:MJ_1334; -. DR eggNOG; arCOG00665; Archaea. DR eggNOG; COG1210; LUCA. DR InParanoid; Q58730; -. DR KO; K00963; -. DR OMA; PDDLHFG; -. DR PhylomeDB; Q58730; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003983; F:UTP:glucose-1-phosphate uridylyltransferase activity; IEA:UniProtKB-EC. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR GO; GO:0006011; P:UDP-glucose metabolic process; IEA:InterPro. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR005771; GalU_uridylyltTrfase_bac/arc. DR InterPro; IPR005835; NTP_transferase_dom. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00483; NTP_transferase; 1. DR SUPFAM; SSF53448; SSF53448; 1. DR TIGRFAMs; TIGR01099; galU; 1. PE 3: Inferred from homology; KW Complete proteome; Nucleotidyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 283 Putative UTP--glucose-1-phosphate FT uridylyltransferase. FT /FTId=PRO_0000201377. SQ SEQUENCE 283 AA; 32090 MW; A98C684C9940F127 CRC64; MIRKAVIPVA GFGTRLLPIT KAQPKEMLPV VNKPIVQYVV EDLVEAGVKD ILFVTGKGKQ AIENHFDVNY ELECKLEKSG KYELLKIIKE IDRLGNIFYV RQKEQKGLGD AILYGEEFVG EEYFIAMVGD TIYSKNIVKD LIKAHEKYGC SVIALERVPK EDVYKYGVID GEEIEKGVYK IKNMVEKPKV EEAPSNLIIT GAYLLSPKIF EKIRETPPGR GGEIQITDAM NLLLKEEDII GVEINCKRYD IGDALGWLKA NVEIGAERFP EFREFLKEFV KNL // ID Y1343_METJA Reviewed; 420 AA. AC Q58739; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Putative ammonium transporter MJ1343; GN OrderedLocusNames=MJ1343; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- INTERACTION: CC Q60381:MJ0059; NbExp=2; IntAct=EBI-7201308, EBI-7201321; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ammonia transporter channel CC (TC 1.A.11.2) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99352.1; -; Genomic_DNA. DR PIR; F64467; F64467. DR ProteinModelPortal; Q58739; -. DR IntAct; Q58739; 1. DR MINT; MINT-4297916; -. DR STRING; 243232.MJ_1343; -. DR EnsemblBacteria; AAB99352; AAB99352; MJ_1343. DR KEGG; mja:MJ_1343; -. DR eggNOG; arCOG04397; Archaea. DR eggNOG; COG0004; LUCA. DR InParanoid; Q58739; -. DR KO; K03320; -. DR OMA; KFFFLMT; -. DR PhylomeDB; Q58739; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0008519; F:ammonium transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0072488; P:ammonium transmembrane transport; IBA:GO_Central. DR GO; GO:0006995; P:cellular response to nitrogen starvation; IBA:GO_Central. DR GO; GO:0019740; P:nitrogen utilization; IBA:GO_Central. DR GO; GO:0015695; P:organic cation transport; IBA:GO_Central. DR Gene3D; 1.10.3430.10; -; 1. DR InterPro; IPR029020; Ammonium/urea_transptr. DR InterPro; IPR001905; Ammonium_transpt. DR InterPro; IPR018047; Ammonium_transpt_CS. DR InterPro; IPR024041; NH4_transpt_AmtB-like_dom. DR PANTHER; PTHR11730; PTHR11730; 1. DR Pfam; PF00909; Ammonium_transp; 1. DR SUPFAM; SSF111352; SSF111352; 1. DR TIGRFAMs; TIGR00836; amt; 1. DR PROSITE; PS01219; AMMONIUM_TRANSP; 1. PE 1: Evidence at protein level; KW Ammonia transport; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 420 Putative ammonium transporter MJ1343. FT /FTId=PRO_0000139765. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 250 270 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TRANSMEM 339 359 Helical. {ECO:0000255}. FT TRANSMEM 365 385 Helical. {ECO:0000255}. SQ SEQUENCE 420 AA; 43786 MW; F7AE2554D19DACA2 CRC64; MWGENIATAD LFANATDIHS IVQALTTLAN ASDVFFLVVM GVLVFMMQWG FAMLEGGQVR KKNVNNVMMK NMVDWLIGCV AWLFIGGILC SKGFDLSAFI DWWKQILGTN WPNNGLDLAS WFFGLVFCAT AATIVSGGVA ERIKFSAYVL ISLIITGLLY PLFVYLGPWG ASIVPWHDYA GSLVVHGLGG FLALGAIAAL GPRIGRFVDG RPVPILGHNI PMAVFGAFAL AIGWYGFNVG SSLALGDISG LVCATTTMAM AGGGIGALIA SRNDVLFTAN GIVAGLVAIC SGTDVVSPIG GLIIGLIAGL QVPIVYKLVE KAGLDDVCGV VPVHGTAGVI GAILTGILGL KIFGGAGGVS LIDQIIGAVF CIIYGTGLGY ILAKIVGIAL GGLRVSEEEE KMGLDMAEHK MPAYPEETVI // ID Y1345_METJA Reviewed; 314 AA. AC Q58741; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=TPR repeat-containing protein MJ1345; GN OrderedLocusNames=MJ1345; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9697413; DOI=10.1016/S0968-0004(98)01228-6; RA Kyrpides N.C., Woese C.R.; RT "Tetratrico-peptide-repeat proteins in the archaeon Methanococcus RT jannaschii."; RL Trends Biochem. Sci. 23:245-247(1998). CC -!- SIMILARITY: Contains 9 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99354.1; -; Genomic_DNA. DR PIR; H64467; H64467. DR ProteinModelPortal; Q58741; -. DR STRING; 243232.MJ_1345; -. DR EnsemblBacteria; AAB99354; AAB99354; MJ_1345. DR KEGG; mja:MJ_1345; -. DR eggNOG; arCOG03038; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q58741; -. DR OMA; ALHCKKA; -. DR PhylomeDB; Q58741; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00515; TPR_1; 2. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 8. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 8. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 314 TPR repeat-containing protein MJ1345. FT /FTId=PRO_0000106460. FT REPEAT 12 45 TPR 1. FT REPEAT 46 78 TPR 2. FT REPEAT 80 112 TPR 3. FT REPEAT 114 146 TPR 4. FT REPEAT 147 180 TPR 5. FT REPEAT 182 214 TPR 6. FT REPEAT 215 248 TPR 7. FT REPEAT 249 282 TPR 8. FT REPEAT 284 313 TPR 9. SQ SEQUENCE 314 AA; 36518 MW; F58D35315E854E12 CRC64; MGEGVNMEIY NESILWDEYF DALEKRNYEK ALLLIDKILE VRESPDVYVR KARILRTLGE NDKALEYFDK ALKLKPKYIL ANFLKGALLV SLGKLEEAKE VFLKLCRLEK SDLPVKYVTA FILKKLGEYD YALKIIDKIL KKYPKSAIAW AEKGEILYRE GKLKKSLECF DNALKINPKD CQSLLYKGEI LFKLGRYGEA LKCLKKVFER NNKDIRALMY IIQILIYLGR LNQALEYTKK ALKLNPDDPL LYLYKGIILN KLGKYNEAIK YFDKVLEINP NIPDAWNGKA IALEKLGKIN EAIECYNRAL DIYE // ID Y1358_METJA Reviewed; 152 AA. AC Q58753; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1358; GN OrderedLocusNames=MJ1358; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99377.1; -; Genomic_DNA. DR PIR; E64469; E64469. DR ProteinModelPortal; Q58753; -. DR STRING; 243232.MJ_1358; -. DR DNASU; 1452260; -. DR EnsemblBacteria; AAB99377; AAB99377; MJ_1358. DR KEGG; mja:MJ_1358; -. DR OMA; EHNIASP; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 152 Uncharacterized protein MJ1358. FT /FTId=PRO_0000107296. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. SQ SEQUENCE 152 AA; 18007 MW; 0FB45F8E0C4378FC CRC64; MGVVFAFGFY LIFIKLTGLK LMDYFPRFKE NRLKMIFSIL SVILAFLINW LIMKNFSFLI EIIHPIASVW IFIILIYLLL RFLFLKRVPL SNYEKKFMGN MSAIAIFLEL LKIIEYVDEH NIASPITVAL VFFIPVVVFF NCKYFYEMEL SS // ID Y1383_METJA Reviewed; 256 AA. AC Q58778; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 90. DE RecName: Full=Uncharacterized protein MJ1383; DE Flags: Precursor; GN OrderedLocusNames=MJ1383; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0761. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99393.1; -; Genomic_DNA. DR PIR; F64472; F64472. DR ProteinModelPortal; Q58778; -. DR STRING; 243232.MJ_1383; -. DR DNASU; 1452286; -. DR EnsemblBacteria; AAB99393; AAB99393; MJ_1383. DR KEGG; mja:MJ_1383; -. DR eggNOG; arCOG00892; Archaea. DR eggNOG; COG1099; LUCA. DR InParanoid; Q58778; -. DR KO; K07051; -. DR OMA; IKSYINY; -. DR PhylomeDB; Q58778; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:InterPro. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR InterPro; IPR012022; UCP005295. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005295; UCP005295_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 256 Uncharacterized protein MJ1383. FT /FTId=PRO_0000014013. SQ SEQUENCE 256 AA; 29036 MW; 6D26F427EAB54675 CRC64; MIDTHIHSDT RGLEDLELMA MCLDGVITLA HDPFEMKNIK VWEAHVEKLL INELERAKKV GLNLFICVGM HPRAIPPEID EALDKIKSYI NYNSRVVGIG EIGLEKATKE EKEVFIKQLL LAEELNMPAV VHTPRRNKEE VTKIILDEIS TLNLKNRDIV IEHCNKETTK WVLDEEFYVG LTIQPGKLTP LEAVEIVKEY KDFADKILLN SDCSSNASDV LAVPRTVLKM KINGIEKDVI YKVAHKNAVN LFGLDI // ID Y1386_METJA Reviewed; 74 AA. AC Q58781; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1386; GN OrderedLocusNames=MJ1386; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99399.1; -; Genomic_DNA. DR PIR; A64473; A64473. DR STRING; 243232.MJ_1386; -. DR EnsemblBacteria; AAB99399; AAB99399; MJ_1386. DR KEGG; mja:MJ_1386; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 74 Uncharacterized protein MJ1386. FT /FTId=PRO_0000107305. FT TRANSMEM 52 72 Helical. {ECO:0000255}. SQ SEQUENCE 74 AA; 8517 MW; 03F777FB41325531 CRC64; MKIYDAVVKT TFQISTSIFF DYIYFFDYKG MKMAEIFAVN NYTELKKIRR MITFGFTVLG LGIGMIFGDA GLDV // ID Y1393_METJA Reviewed; 608 AA. AC Q58788; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1393; GN OrderedLocusNames=MJ1393; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1394 and A.fulgidus AF2028. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99403.1; -; Genomic_DNA. DR PIR; H64473; H64473. DR ProteinModelPortal; Q58788; -. DR STRING; 243232.MJ_1393; -. DR EnsemblBacteria; AAB99403; AAB99403; MJ_1393. DR KEGG; mja:MJ_1393; -. DR eggNOG; arCOG06147; Archaea. DR eggNOG; ENOG4111G40; LUCA. DR InParanoid; Q58788; -. DR OMA; VVWANCT; -. DR PhylomeDB; Q58788; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 608 Uncharacterized protein MJ1393. FT /FTId=PRO_0000107307. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 608 AA; 66768 MW; 010FAF1C29F8C73C CRC64; MRKLIFMALL MSLLFIGTVF GYGDNGPLYV AYYEKYNITG NTTGDGLVSS TIESITGYIV INNTGTTIND TLYDVWVAVN ISNNITGPEV YVNGTPKGVF IESSAPAYTN LPNANTYIHI PILPNNSYVI IKFAIDKSIT GVPLIINETY SDTKIPSERL SNWSVYLNIS RNVSALPATD TPVSVIMTKY LSNDPNNYGS DTWNFLNITG AIANEGSITL WDGPYFLPGY NDSLTWTGVV INTTKNATIT INITGNNTYT NRTGTLMKYG FAVIFFEFNG TKSGTKIEGI YATGYGGVSA TKEGPFLNAS SGKYEIWYES ANVSNKASSY YFNLTHVTIW AVNGSNPVIL DPFNITLLIP NSKQTSSPNE ILSPGSVWSS TKYAFTFDGI PVVWANCTFK VADENITLIN RSINEYSTKY GSSYVVVEEI YVVGSYLIKV TKHIVPDADG TYDIYIVVEN IGSVKTPEYV YVYDLIPKNF TVSDEWVNQS SMLIAEGNHT ITTNPRYNLS MWWALHAIYP GADGDGNWND TAEILANKTV VIHYKLNGTG EFYPSDAFIV GIDPTNSLLP TTSPKITTVA GTVENNSEPF LALLTLLVGL GIIIRRVM // ID Y1398_METJA Reviewed; 391 AA. AC Q58793; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ1398; GN OrderedLocusNames=MJ1398; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99407.1; -; Genomic_DNA. DR PIR; E64474; E64474. DR ProteinModelPortal; Q58793; -. DR STRING; 243232.MJ_1398; -. DR EnsemblBacteria; AAB99407; AAB99407; MJ_1398. DR KEGG; mja:MJ_1398; -. DR eggNOG; arCOG02611; Archaea. DR eggNOG; COG3398; LUCA. DR OMA; WHLRILE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 2. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR SMART; SM00418; HTH_ARSR; 2. DR SUPFAM; SSF46785; SSF46785; 2. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 391 Uncharacterized HTH-type transcriptional FT regulator MJ1398. FT /FTId=PRO_0000160635. FT DOMAIN 235 330 HTH arsR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. SQ SEQUENCE 391 AA; 45530 MW; 68FE5DF4B1418989 CRC64; MKKDTLLLII LILFCIVHVY GIYVHIYGIN VSLENVSQYL YNTTVYLSYE NGTPCFYIGE KKEFVIIPPY IKVDRDIAPL IKKLRFKIEN KSYNLIITKK NVNTNKMAII FTSINGSREV NGNKTIIWIK DPLKLKQSEV EALYELPEKG EVIARYKDGK PAAIKINNKI YVGFKPDEDV LANLIYIHIV KKTSNPLPYI LFTVFLTLAS LMLTFQETLK KKFLELISAL ASVKVFILSR INLLDEEKVL LNDTRREIYN YILDNPGCHL RELSKNLNKP VSTLTWHLRI LEKANLIKSK KFGNRLIYYP ADMDMRDLPL LYLKNETQKS IFEYLLKSPA HLRKIAKDLN LNVETVRYNL KKLENLGIVK SKEEGNRIVY YINESILKFH K // ID Y1414_METJA Reviewed; 241 AA. AC Q58809; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1414; GN OrderedLocusNames=MJ1414; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99424.1; -; Genomic_DNA. DR PIR; E64476; E64476. DR ProteinModelPortal; Q58809; -. DR STRING; 243232.MJ_1414; -. DR EnsemblBacteria; AAB99424; AAB99424; MJ_1414. DR KEGG; mja:MJ_1414; -. DR eggNOG; arCOG07627; Archaea. DR eggNOG; ENOG41111JQ; LUCA. DR InParanoid; Q58809; -. DR OMA; INTFSYN; -. DR Proteomes; UP000000805; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 241 Uncharacterized protein MJ1414. FT /FTId=PRO_0000107315. SQ SEQUENCE 241 AA; 27861 MW; 27936638E39481E2 CRC64; MSPMRWAIFL VLLTITFSGC LNKEISKEEI IKKIDEINTF SYNAKVFINL SVSNPAINKV NMKMDIDGYS DGKLSKGIIH VYYTVRYFNG RNETIPFYVN EEGTFIKLEG KWQKITNNDL SNHTWNILAY IKDLIEKNDI KIEEENNHYI IRLKDENAEK QLNPFFYRGI KIPGINLKIS EEEVVIILDK YGTPIKVIKK GKLYGTSSKG NLDGVIVIET EIKDINKDFD FSIPEDLSIY N // ID Y141_METJA Reviewed; 99 AA. AC Q57606; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0141; GN OrderedLocusNames=MJ0141; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98124.1; -; Genomic_DNA. DR PIR; F64317; F64317. DR ProteinModelPortal; Q57606; -. DR STRING; 243232.MJ_0141; -. DR EnsemblBacteria; AAB98124; AAB98124; MJ_0141. DR KEGG; mja:MJ_0141; -. DR eggNOG; arCOG01201; Archaea. DR eggNOG; COG1708; LUCA. DR InParanoid; Q57606; -. DR KO; K07076; -. DR OMA; PIIYKKT; -. DR PhylomeDB; Q57606; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 99 Uncharacterized protein MJ0141. FT /FTId=PRO_0000106717. SQ SEQUENCE 99 AA; 11578 MW; 2199CE924EE8FADD CRC64; MEIIEIIKEF KKDISTILKD KLDRVILFGS YARGDYDEES DVDVLILVKE MPTLKEKQKI IKIASRYSLK YDILISPIIY KKTIKTSFID EVENYGVEV // ID Y1432_METJA Reviewed; 162 AA. AC Q58827; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1432; GN OrderedLocusNames=MJ1432; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99442.1; -; Genomic_DNA. DR PIR; G64478; G64478. DR ProteinModelPortal; Q58827; -. DR STRING; 243232.MJ_1432; -. DR EnsemblBacteria; AAB99442; AAB99442; MJ_1432. DR KEGG; mja:MJ_1432; -. DR eggNOG; arCOG00985; Archaea. DR eggNOG; COG2016; LUCA. DR InParanoid; Q58827; -. DR KO; K07575; -. DR OMA; MELKVKH; -. DR PhylomeDB; Q58827; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 2.30.130.10; -; 1. DR InterPro; IPR022430; CHP03684. DR InterPro; IPR015266; DUF1947. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR016437; Transl_RNA-bd_prd. DR InterPro; IPR004521; Uncharacterised_CHP00451. DR PANTHER; PTHR22798; PTHR22798; 1. DR Pfam; PF09183; DUF1947; 1. DR Pfam; PF01472; PUA; 1. DR PIRSF; PIRSF005067; Tma_RNA-bind_prd; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR TIGRFAMs; TIGR03684; arCOG00985; 1. DR TIGRFAMs; TIGR00451; unchar_dom_2; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 162 Uncharacterized protein MJ1432. FT /FTId=PRO_0000107324. FT DOMAIN 78 154 PUA. {ECO:0000255|PROSITE- FT ProRule:PRU00161}. SQ SEQUENCE 162 AA; 18365 MW; C67CF3638B2024BD CRC64; MEIRKRYFLS KKDVKKIKKE LEVFFENVDE IIPKKGNVEI AITDDFEIIL VDKEPIAFKK DDKVIPTLKL LLKSLPDKNL VVVDIGAIKF LINGADVMAP GIVDADENIK EEDVVFVVDE NHKKPICVGI ALMNGKEMKE ADKGKAIKNL HYVGDKIWNF KG // ID Y1439_METJA Reviewed; 207 AA. AC Q58834; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1439; GN OrderedLocusNames=MJ1439; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the thermonuclease family. CC {ECO:0000255|PROSITE-ProRule:PRU00272}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99448.1; -; Genomic_DNA. DR PIR; F64479; F64479. DR ProteinModelPortal; Q58834; -. DR STRING; 243232.MJ_1439; -. DR EnsemblBacteria; AAB99448; AAB99448; MJ_1439. DR KEGG; mja:MJ_1439; -. DR eggNOG; arCOG03192; Archaea. DR eggNOG; COG1525; LUCA. DR InParanoid; Q58834; -. DR KO; K01174; -. DR OMA; AYIFINN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 2.40.50.90; -; 1. DR InterPro; IPR016071; Staphylococal_nuclease_OB-fold. DR InterPro; IPR002071; Thermonucl_AS. DR Pfam; PF00565; SNase; 1. DR SMART; SM00318; SNc; 1. DR SUPFAM; SSF50199; SSF50199; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. DR PROSITE; PS01123; TNASE_1; 1. DR PROSITE; PS01284; TNASE_2; 1. DR PROSITE; PS50830; TNASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Endonuclease; Hydrolase; Nuclease; KW Reference proteome. FT CHAIN 1 207 Uncharacterized protein MJ1439. FT /FTId=PRO_0000215283. FT ACT_SITE 80 80 {ECO:0000250}. FT ACT_SITE 88 88 {ECO:0000250}. FT ACT_SITE 148 148 {ECO:0000250}. SQ SEQUENCE 207 AA; 24547 MW; 4866BC9AAB498906 CRC64; MIRGRIMRKF LILSMLIFTT LCGCVDFSSS NSNGYYHDSW SYNNYTSFVD THEHYYGKVV KVVDGDTVYV EVNGELWKIR LLGVDTPEIH KRNNPYEYYL LNGTPITDTK YLKEWGYKAK HFAEKELKNK TVIIVFDNEA PKKDKYGRYL AYIFINNSNN LINFNEELLK YGYARVYISN FELKDEFLNV EREAKENRVG LWNWSNN // ID Y1442_METJA Reviewed; 202 AA. AC Q58837; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1442; GN OrderedLocusNames=MJ1442; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99459.1; -; Genomic_DNA. DR PIR; A64480; A64480. DR ProteinModelPortal; Q58837; -. DR STRING; 243232.MJ_1442; -. DR EnsemblBacteria; AAB99459; AAB99459; MJ_1442. DR KEGG; mja:MJ_1442; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 202 Uncharacterized protein MJ1442. FT /FTId=PRO_0000107335. FT TRANSMEM 18 38 Helical. {ECO:0000255}. SQ SEQUENCE 202 AA; 22658 MW; B9158361B5E6D9FC CRC64; MTSIRIFIKF YGGTMRKFLI FLIFLSVLGC GITISGCIGG KNVEEIQNMQ EQVVQQQQNE NQEEYQNEDE GVDYNSIRDV QPIGTAKEAD EKIRPILNEV FGEVKLMEYV STGKQNEGES IVLTYVPKRK ITTNDFEKLN EAIKKSGYFE SSGGIAGGGQ SGEGMVLWYV SKDNKSAIQI ILYPDTNEIV VGYYKGKIYS SQ // ID Y1445_METJA Reviewed; 176 AA. AC Q58840; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Uncharacterized protein MJ1445; GN OrderedLocusNames=MJ1445; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99460.1; -; Genomic_DNA. DR PIR; D64480; D64480. DR ProteinModelPortal; Q58840; -. DR STRING; 243232.MJ_1445; -. DR EnsemblBacteria; AAB99460; AAB99460; MJ_1445. DR KEGG; mja:MJ_1445; -. DR eggNOG; arCOG01154; Archaea. DR eggNOG; COG4186; LUCA. DR InParanoid; Q58840; -. DR OMA; WIIHGHH; -. DR PhylomeDB; Q58840; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR004843; Calcineurin-like_PHP_apaH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR Pfam; PF00149; Metallophos; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 176 Uncharacterized protein MJ1445. FT /FTId=PRO_0000107336. FT COMPBIAS 122 129 His-rich. SQ SEQUENCE 176 AA; 20713 MW; B5D5F69B2896A38B CRC64; MSMRKIYLIS DTHFNHANII KYCNRPFSNV EEMNKTLIKN WNNVVRDKDI VYFLGDLILS KNKAKKAREL LELLNGEIVF IRGNHDKFGE KFRVIEYNGY KFMLIHNPDS SYTLNFDGWI IHGHHHANHL DEYPFINPKR KSINVSVEVI NYKPVSLDLI VKLIEKGKVV RTINDL // ID Y1451_METJA Reviewed; 484 AA. AC Q58846; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1451; GN OrderedLocusNames=MJ1451; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH1153. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99462.1; -; Genomic_DNA. DR PIR; B64481; B64481. DR ProteinModelPortal; Q58846; -. DR STRING; 243232.MJ_1451; -. DR EnsemblBacteria; AAB99462; AAB99462; MJ_1451. DR KEGG; mja:MJ_1451; -. DR eggNOG; arCOG04866; Archaea. DR eggNOG; COG4065; LUCA. DR InParanoid; Q58846; -. DR OMA; VMARCMN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008303; Methan_mark_14. DR Pfam; PF09887; DUF2114; 1. DR PIRSF; PIRSF016937; UCP016937; 1. DR TIGRFAMs; TIGR03285; methan_mark_14; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 484 Uncharacterized protein MJ1451. FT /FTId=PRO_0000107338. SQ SEQUENCE 484 AA; 52432 MW; BA63804FEB0A0CB5 CRC64; MGIFDVISGL FKKKPKIAYA KSQSVDLIEL KRNPYYIVAS VELGNTTTKS IITATNMDTG KTYIVSKHVK MTRDVRKPKK GEEVFGETLW GVELTREAVA DMVKEVLLES LKKAGLTVDD LHFVVRSTGV TAGFASPEEV GEMIIALAQG CMKAGVPPAK MTPAMTKEQI PKPFDKYSFL DKIIFDGAVT GVLPPTGKEV VANEMEGELV TAGIKVGSKW TDVDFRNPCM SIDFGTTLAG RITNDTLPYA KVIGNLCGLA GAIADAIARG SGKIDEKTGA ALDLANIKGK PNEELAKEYA EEMHKYIIIK EVPKDVDRFG TVPVDPKSAE KAGTTLIGCD VGKNGSDLIK LEELGRELVE KSDIPTLMCC LDYVMSEVVR RLVELAYKKG LISEKSAVGI TGRAGITGRK PELIIEKLKT LEIWDKVEEN VVFVEDGLAL GASVMARCMN CLGTPQVPIG GVRGGGCILG LRRKWQKERG MIRD // ID Y1452_METJA Reviewed; 259 AA. AC Q58847; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ1452; GN OrderedLocusNames=MJ1452; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH738. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99463.1; -; Genomic_DNA. DR PIR; C64481; C64481. DR ProteinModelPortal; Q58847; -. DR STRING; 243232.MJ_1452; -. DR EnsemblBacteria; AAB99463; AAB99463; MJ_1452. DR KEGG; mja:MJ_1452; -. DR eggNOG; arCOG04843; Archaea. DR eggNOG; COG4076; LUCA. DR InParanoid; Q58847; -. DR OMA; LITEPQV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0008469; F:histone-arginine N-methyltransferase activity; IBA:GO_Central. DR GO; GO:0035242; F:protein-arginine omega-N asymmetric methyltransferase activity; IBA:GO_Central. DR GO; GO:0034969; P:histone arginine methylation; IBA:GOC. DR GO; GO:0019919; P:peptidyl-arginine methylation, to asymmetrical-dimethyl arginine; IBA:GOC. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR025799; Arg_MeTrfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR021172; UCP006607_RNA_methylase-rel. DR PANTHER; PTHR11006; PTHR11006; 1. DR PIRSF; PIRSF006607; RNAmts_UCP006607; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 259 Uncharacterized protein MJ1452. FT /FTId=PRO_0000107340. SQ SEQUENCE 259 AA; 29428 MW; F1EC01380F09376E CRC64; MKLRLKVPQW HYSLLTDYER LAIFKNAIER VVDEDDVVFD LGTGSGILAM IAAKKAKKVY AIELDPFTYD YAKENIKVNG FNNIEIIEGD ASTYNFKEKA DVVIAELLDT ALIIEPQVKV MNSIIERGFL KEDVKIIPAK AISTIQLVEA KMSHIYYDED IKSEEVSEEV IYEEVDFHKT NPIEVSYNIE LELEKSCENL GIKLRTYTIL DDKHVAGQTS MLNPPLVIPL NKKVDKGRVK INLSYRRGGD LESIKVNLG // ID Y1455_METJA Reviewed; 305 AA. AC Q58850; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1455; GN OrderedLocusNames=MJ1455; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99469.1; -; Genomic_DNA. DR PIR; F64481; F64481. DR ProteinModelPortal; Q58850; -. DR STRING; 243232.MJ_1455; -. DR DNASU; 1452359; -. DR EnsemblBacteria; AAB99469; AAB99469; MJ_1455. DR KEGG; mja:MJ_1455; -. DR eggNOG; ENOG4102U3B; Archaea. DR eggNOG; ENOG4111GQV; LUCA. DR OMA; NIGEFGT; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 305 Uncharacterized protein MJ1455. FT /FTId=PRO_0000107344. SQ SEQUENCE 305 AA; 35009 MW; BA911EEC3B248C40 CRC64; MILFEWGTYN ALSTLKQAAL LGTRITEIPP AVLSRRLPSG YYESYKKLGG EYFTSILAHG PYYSLSSEKG LKGHLSAIEK ATLCGAEIYN YHLGKRVGDD LNYHLEVLKK FSEVNNEMIY SPEPATNIGE FGTLDELEEL IKAAKEEDIK IIPSLQLENI FLNELGVYEK DDLDEAAEKA DVDWWLKIFR RMDKISDYIM HFRFSQVIGL KYGKRFYKKR VPLGKGYPPV EPLTEALATY LVDNATRGGF KKVLFVYTGL PEVKYRDLID LYAMIMKKSI DKLMSRESQV EYGDFYKVMS SEEEE // ID Y1472_METJA Reviewed; 544 AA. AC Q58867; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1472; DE Flags: Precursor; GN OrderedLocusNames=MJ1472; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99487.1; -; Genomic_DNA. DR PIR; G64483; G64483. DR ProteinModelPortal; Q58867; -. DR STRING; 243232.MJ_1472; -. DR EnsemblBacteria; AAB99487; AAB99487; MJ_1472. DR KEGG; mja:MJ_1472; -. DR eggNOG; arCOG03508; Archaea. DR eggNOG; COG5306; LUCA. DR OMA; LPYWVQT; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR018765; DUF2341. DR Pfam; PF10102; DUF2341; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 22 {ECO:0000255}. FT CHAIN 23 544 Uncharacterized protein MJ1472. FT /FTId=PRO_0000014016. SQ SEQUENCE 544 AA; 63400 MW; A3E93AD51C94EBF0 CRC64; MYFSQNAIIL VMLMFVISAV FYATIDYKTK EVEDEIKIKE VSLYEKNLIN TIDRNIDKIV EDAFVNASYK IMKERKFFTA SSEAVAYITS YIKNETKESL NNVNYGYSNI SYNISSVKIS PTYDPLVVHL YCEIDIKYSK KLNNGELIAL KPIVINRDIK LSRIPDPYVY LNKFYYTWGY EKKINIYNFP NDNYNRTFCI ILNSSNFNYS EMHNPQSPTE LRVIGWDSVS NKIILLPYWV QTWREGNNDV SVIWVRANKN EIYNYNNGQG YIYILYNSTT PVDRQDPEHT FIFFDDFNYF NPDKWDSVGY FIINNSKITV IAGAGSSVYT KQTYGTRYEL IFRANFTPSH AQTIGFFTQL SDNDGVGWDM YDWTGNNPEL YMRVGYSGSD IGDYVPNSNK YLNKFYIYDL KRISTTDLNF TIFNDTLDIE YSNSFTNGNK GNNYPISITA LINLNTNVTV DWIFLKDIND ITTTVPPIGV DEYPNLDYKE EKPKTFTGTI YYGEPGKYIL VYNSTYSIIG LYTNKTDYWL YPNMPGYKPL IEEN // ID Y1488_METJA Reviewed; 393 AA. AC Q58883; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 63. DE RecName: Full=Uncharacterized protein MJ1488; GN OrderedLocusNames=MJ1488; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99500.1; -; Genomic_DNA. DR PIR; G64485; G64485. DR ProteinModelPortal; Q58883; -. DR STRING; 243232.MJ_1488; -. DR EnsemblBacteria; AAB99500; AAB99500; MJ_1488. DR KEGG; mja:MJ_1488; -. DR eggNOG; arCOG01521; Archaea. DR eggNOG; COG1233; LUCA. DR InParanoid; Q58883; -. DR OMA; ALHMIPH; -. DR PhylomeDB; Q58883; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 393 Uncharacterized protein MJ1488. FT /FTId=PRO_0000107372. SQ SEQUENCE 393 AA; 43396 MW; AEE623668282B340 CRC64; MRIGIVGAGL GGLLAGALLS KNHEVVVFEK LPFLGGRFTN LKYEGFQLTT GALHMIPHGN DGYLAQALRK AGANVKIINS KPDGTFLING KEYLYKELFS LLGFKEKAKA FKLATKLKLG KVDKNISFGE FLEEIDLALK VGNAFTGWAL SLTAYETPMS EIIEIAKNYH KFGGPGIPIG GCKAVTDELS RIIKKNNGKI IKEYEVKRIE IDEKAYIDDY EFDVVISNIS PIETQKICNI KFLKSKPKPS KGIKISIATK EGIIKHGGVL FTPECERING LNQVTNVDKS LAPEGWHLVM THQTQLTNNV KKEIDLGLED IENLFKGKDY KILHIQSYRD DWPVNHASNG TDIDNIVNDR FYLVGDGAKG RGGIEVEGIA MGVLKVVNYI NSL // ID Y1515_METJA Reviewed; 355 AA. AC Q58910; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1515; GN OrderedLocusNames=MJ1515; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99533.1; -; Genomic_DNA. DR PIR; B64489; B64489. DR ProteinModelPortal; Q58910; -. DR STRING; 243232.MJ_1515; -. DR EnsemblBacteria; AAB99533; AAB99533; MJ_1515. DR KEGG; mja:MJ_1515; -. DR eggNOG; arCOG03639; Archaea. DR eggNOG; arCOG07614; Archaea. DR eggNOG; COG0121; LUCA. DR InParanoid; Q58910; -. DR KO; K07008; -. DR OMA; YWVFAHN; -. DR PhylomeDB; Q58910; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR029055; Ntn_hydrolases_N. DR InterPro; IPR026869; Put_GATase_2. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF13230; GATase_4; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 355 Uncharacterized protein MJ1515. FT /FTId=PRO_0000107386. FT DOMAIN 2 248 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT ACT_SITE 2 2 For GATase activity. {ECO:0000250}. SQ SEQUENCE 355 AA; 41888 MW; 55921898CC90E304 CRC64; MCELLGICFN KKVNVELSLN SFKHRSEDHP NGWGIAFYPD GFVRVIKEPI KMNEALLAEC VRWTKIKSNI FIAHIRKASA GSESYVNTHP FVRKLEDKEI AFAHNGTLLG YEDLELDGYY PIGETDSEYV FCYLLSQIEK REIEWNKEGF DEMLDILLDI NYYGAFNCLF SDGEYLFAYK DYRGRRELHF LKRKPPYGRI RLEDEDYIIN LGDVKSVREE GFIIATNPLT NEDWKSFENG ELMVFKNGEM IYSNKRLTDL ELKILKILRE SPHRVSLKKI IENLEYLSRN IRHDASVVRI GIRSLLDKGY IKQDSRDTVN WDDLEATFYT KPEKRVEIDK RLKGFRWRRN RIIMS // ID Y1516_METJA Reviewed; 99 AA. AC Q58911; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1516; GN OrderedLocusNames=MJ1516; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99536.1; -; Genomic_DNA. DR PIR; C64489; C64489. DR STRING; 243232.MJ_1516; -. DR EnsemblBacteria; AAB99536; AAB99536; MJ_1516. DR KEGG; mja:MJ_1516; -. DR eggNOG; arCOG03293; Archaea. DR eggNOG; COG2314; LUCA. DR InParanoid; Q58911; -. DR OMA; RIVYYEQ; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007829; TM2. DR Pfam; PF05154; TM2; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 99 Uncharacterized protein MJ1516. FT /FTId=PRO_0000107387. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. SQ SEQUENCE 99 AA; 11483 MW; B837A92FA94002FB CRC64; MMAMNEIELM QIKDFVKDMD KNQRIVYYEQ KKKSVGIAVL LSFIIPGAGQ MYLGRVGKGI ILLLTCWLII PWIYSIYDAY KSAKDYNAQL YSIIFSKDD // ID Y1518_METJA Reviewed; 374 AA. AC Q58913; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ1518; GN OrderedLocusNames=MJ1518; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99549.1; -; Genomic_DNA. DR PIR; E64489; E64489. DR ProteinModelPortal; Q58913; -. DR STRING; 243232.MJ_1518; -. DR EnsemblBacteria; AAB99549; AAB99549; MJ_1518. DR KEGG; mja:MJ_1518; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 374 Uncharacterized protein MJ1518. FT /FTId=PRO_0000107390. SQ SEQUENCE 374 AA; 44817 MW; 6D678115913A8BFA CRC64; MLSIIFGSKP REDEIDSVDR YMTKLFLRII FIPDYTNKIH DLSENVSKNI KNLIMELKSG NIFEINKILD DLEYNIYTID DESLTIKERV YNAVEIIFKV VSNEILRTES IDDKELEIIK KLHELVVLTD KVLRITYNSL NRSLEDINSY RRIIANNNLP DDIIRRLNII NAYIEKIKSD ILSMRENEQR VLIICLSKFY NLYLSKDKKE REKLADEIKN LIEYLYFDWY YDFIDNIGEY EFKFIKNIAA MCLLYDYTKE LEKDGSKEMF NHVIFKILRN GGFKVKEYDI IETLLNIREN LPKSSKIDVR YFDKELIKII RGIVRESKKD VFYNNMKRLK EFVEELREME KKLSEANNIT LHDLRKLGFN DMFL // ID Y1526_METJA Reviewed; 244 AA. AC Q58921; DT 19-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=UPF0280 protein MJ1526 {ECO:0000255|HAMAP-Rule:MF_01079}; GN OrderedLocusNames=MJ1526; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0280 family. {ECO:0000255|HAMAP- CC Rule:MF_01079}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99544.1; -; Genomic_DNA. DR PIR; E64490; E64490. DR ProteinModelPortal; Q58921; -. DR STRING; 243232.MJ_1526; -. DR EnsemblBacteria; AAB99544; AAB99544; MJ_1526. DR KEGG; mja:MJ_1526; -. DR eggNOG; arCOG04376; Archaea. DR eggNOG; COG2122; LUCA. DR InParanoid; Q58921; -. DR KO; K09740; -. DR OMA; NTIINER; -. DR PhylomeDB; Q58921; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.10.520.10; -; 1. DR HAMAP; MF_01079; UPF0280; 1. DR InterPro; IPR003374; ApbE-like. DR InterPro; IPR007183; UPF0280. DR PIRSF; PIRSF006421; UCP006421; 1. DR SUPFAM; SSF143631; SSF143631; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 244 UPF0280 protein MJ1526. FT /FTId=PRO_0000140486. SQ SEQUENCE 244 AA; 26804 MW; 051C70F1D9C6E3D4 CRC64; MWFKKRIIIK ETNILLKVDD KGYFKKAEEI ILKNRLELER YILKNPYFLT SYFPVDVEDD APEIVRLMAI AGEIANVGPM ASVAGAIAEM LIKNLNAKNI IAENGGDICL RAKKDVIIGL YAGNSKITGE VGFRLKKEKI KNIYGVCTSS ATVGHSVSFG EADAVTVFAK SSAIADAAAT AICNASRGRD EEEMINNALE KADEIKKIDG IFVVVKDKVG IKGKIPELVK TDKRITLGEL FDIY // ID Y1549_METJA Reviewed; 392 AA. AC Q58944; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MJ1549; GN OrderedLocusNames=MJ1549; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99567.1; -; Genomic_DNA. DR PIR; D64493; D64493. DR ProteinModelPortal; Q58944; -. DR STRING; 243232.MJ_1549; -. DR EnsemblBacteria; AAB99567; AAB99567; MJ_1549. DR KEGG; mja:MJ_1549; -. DR eggNOG; arCOG01278; Archaea. DR eggNOG; COG0183; LUCA. DR InParanoid; Q58944; -. DR KO; K00626; -. DR OMA; IDAMYVG; -. DR PhylomeDB; Q58944; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016747; F:transferase activity, transferring acyl groups other than amino-acyl groups; IEA:InterPro. DR Gene3D; 3.40.47.10; -; 4. DR InterPro; IPR002155; Thiolase. DR InterPro; IPR016039; Thiolase-like. DR InterPro; IPR020617; Thiolase_C. DR InterPro; IPR020616; Thiolase_N. DR Pfam; PF02803; Thiolase_C; 1. DR Pfam; PF00108; Thiolase_N; 1. DR PIRSF; PIRSF000429; Ac-CoA_Ac_transf; 1. DR SUPFAM; SSF53901; SSF53901; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 392 Uncharacterized protein MJ1549. FT /FTId=PRO_0000107402. SQ SEQUENCE 392 AA; 42148 MW; 06150891366789BA CRC64; MRDVAIIGYG QTKFGELWER SFRSLIVEAG VKAVEAAGID GKDIDEMYVG NMSAGLFVGQ EHIASLIAEH AGLNPIPSTR VEAACASGSL ALRQAVLNVA SGASDVVLVG GVEKMTDVVD ATSAISSASD QEWEALFGAT FPSLYAMMAQ RYMYEYGLTL EELSMWSVIM HENASKNRYA QFPFKVTLEQ VLNSSPVAEP LRLLHCSPVS DGAAALIVCE AEKAKEFVNK DDIIYIKASV QASDTIALHS RESITSLKAA KVASEKAYKM ANIEPKDVDV AEVHDCFAIN GLILMEELGF CKKGEAGKIV YDKKIAIDYD GFPAVNPSGG LKAAGHALGA TGIRQVGEIY WQLKQDKEVK DRQVEIKNGY GITVNVGGTG GTVCIHILSD KR // ID Y1553_METJA Reviewed; 157 AA. AC Q58948; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 105. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ1553; GN OrderedLocusNames=MJ1553; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99573.1; -; Genomic_DNA. DR PIR; H64493; H64493. DR ProteinModelPortal; Q58948; -. DR STRING; 243232.MJ_1553; -. DR EnsemblBacteria; AAB99573; AAB99573; MJ_1553. DR KEGG; mja:MJ_1553; -. DR eggNOG; arCOG01683; Archaea. DR eggNOG; COG0640; LUCA. DR InParanoid; Q58948; -. DR OMA; VYYKITN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PRINTS; PR00778; HTHARSR. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; DNA-binding; Membrane; KW Reference proteome; Transcription; Transcription regulation; KW Transmembrane; Transmembrane helix. FT CHAIN 1 157 Uncharacterized HTH-type transcriptional FT regulator MJ1553. FT /FTId=PRO_0000160636. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT DOMAIN 1 85 HTH arsR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. SQ SEQUENCE 157 AA; 18563 MW; 30F558E964AF8294 CRC64; MKFLFSKTKI EILKKLNERN YTISELSKIL GKSKSTISEH LNALYEMGLV DKENYSKWVY YKITNKGKKV LENLEALILM VSSIFALIGL WIYYIFKQIK YQAREVVLSK TVVERGIYTT YKGSTTFQKE PLFLIFLIIS TFLIIFIVYL VYKIIRR // ID Y1556_METJA Reviewed; 312 AA. AC Q58951; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1556; GN OrderedLocusNames=MJ1556; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99576.1; -; Genomic_DNA. DR PIR; C64494; C64494. DR ProteinModelPortal; Q58951; -. DR STRING; 243232.MJ_1556; -. DR DNASU; 1452464; -. DR EnsemblBacteria; AAB99576; AAB99576; MJ_1556. DR KEGG; mja:MJ_1556; -. DR eggNOG; arCOG00360; Archaea. DR eggNOG; COG3366; LUCA. DR InParanoid; Q58951; -. DR OMA; PRMANIM; -. DR PhylomeDB; Q58951; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 312 Uncharacterized protein MJ1556. FT /FTId=PRO_0000107410. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 264 284 Helical. {ECO:0000255}. FT TRANSMEM 292 312 Helical. {ECO:0000255}. SQ SEQUENCE 312 AA; 35563 MW; 3185414AE35B24D1 CRC64; MMDKIIQTLT LTFTFLYYSI PMLIVGLFIS QILIESNIIK KIYFIGKIFT RLANLPEECG IAITTSFIEP RMANIMLVDF YKKGIINKKE LYISSLIDAF PAMLRHWDSL LPILLATLGF FGIIYFIILV LIGFIQTLIF MAIGKITLKN REYKEDNTDK KIKLNKDVVY TAFKNTIKYG IPIIRDITIA SIITSFLIEF GFFDYITEII KNKAYYLPLS VEEITVAVTQ PINYIGAFVL AGEFLNRGIL DEIEVVRALL LGSILSSIPA LRFLAPYYIG IYGFKDGFNL MMISTLVRIL ITALFVIITL IL // ID Y1560_METJA Reviewed; 386 AA. AC Q58955; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized MFS-type transporter MJ1560; GN OrderedLocusNames=MJ1560; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99579.1; -; Genomic_DNA. DR PIR; G64494; G64494. DR ProteinModelPortal; Q58955; -. DR STRING; 243232.MJ_1560; -. DR EnsemblBacteria; AAB99579; AAB99579; MJ_1560. DR KEGG; mja:MJ_1560; -. DR eggNOG; arCOG00130; Archaea. DR eggNOG; COG0477; LUCA. DR InParanoid; Q58955; -. DR OMA; NSIAIRD; -. DR PhylomeDB; Q58955; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR InterPro; IPR001958; Tet-R_TetA/multi-R_MdtG. DR Pfam; PF07690; MFS_1; 1. DR PRINTS; PR01035; TCRTETA. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 386 Uncharacterized MFS-type transporter FT MJ1560. FT /FTId=PRO_0000084887. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 102 122 Helical. {ECO:0000255}. FT TRANSMEM 134 154 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 272 292 Helical. {ECO:0000255}. FT TRANSMEM 297 317 Helical. {ECO:0000255}. FT TRANSMEM 342 362 Helical. {ECO:0000255}. FT TRANSMEM 365 385 Helical. {ECO:0000255}. SQ SEQUENCE 386 AA; 42068 MW; 2B928E8E56D1BFC1 CRC64; MGKLEKNVFV IWITTFTTML GVGFIAPIMA IYAQTLGATN LEIGLIFGSF ALARTVAQIP VGVLSDIYGK KFFIVCGTFF YGVSTLMYNF VSTVLGFLIV RIFTGIFSAF VTPVAGSYIA AIAPKTRLGE YMGIFNSAIT LGFGIGPFIG GILADMYGIK MPFYFCGFLG ILAAIISYMK LEDIVFNKNK EKIDVKKIST LFSFEFLKNR NFSSSFIINV SNVMINAGIY AYLALYAINY NITISQVGFM IALTNILMAL LQRSFGKLYD KLGNIMIIIG IFIISFGMYL LSTSTTFLTI LASLTIIAVG SSISSTATTS LAVKDIPTHR KGEAMGLFTT SINIGMFIGA VSFGFLADIL GIANMYKFSA IFSIVVGIIS YLRIER // ID Y1566_METJA Reviewed; 447 AA. AC Q58961; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1566; GN OrderedLocusNames=MJ1566; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99592.1; -; Genomic_DNA. DR PIR; E64495; E64495. DR ProteinModelPortal; Q58961; -. DR STRING; 243232.MJ_1566; -. DR EnsemblBacteria; AAB99592; AAB99592; MJ_1566. DR KEGG; mja:MJ_1566; -. DR eggNOG; arCOG08283; Archaea. DR eggNOG; ENOG410Z0TH; LUCA. DR InParanoid; Q58961; -. DR OMA; EWIPFGK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 447 Uncharacterized protein MJ1566. FT /FTId=PRO_0000107414. FT TRANSMEM 380 400 Helical. {ECO:0000255}. FT TRANSMEM 412 432 Helical. {ECO:0000255}. SQ SEQUENCE 447 AA; 51527 MW; 1643E9D3633E4378 CRC64; MGFKYLKIKN PKVILTEWIP FGKNYMTEFI DRITLKEYQR KRIKYFTASE RRDIRYKAVF ETSEYQTTVN IIEFIPETSV KFTAEIIGER KKDVFIYVDY LGRCIYSSEI TKAGDEEEIV SLDNLSFVIP DLILDSSRIM SHLISPPQRY LLETLYGEIK VYKHVTVLTE TVVNIDENTI LEISQVIGAV KNIIEIDDGL IIFGDFGIFI SHKNPEKFEK FIYYYPFIRS ITGVSRDLFF KLNNIASKLE VISNTLASGV DLEDITEIRG ELSRIDRELA VIEIVCGYLK EIVEFLNSSY PPNFGDFDLM ILEKVEAERK LRRLIYRIAE IENILKSNDS LATSLTRLLT TISEDLERKI ANQLAENTKY QVAIGEAMEV LEIGIFGVYA LEAAHILLLT SGKDEILHHI KILGFPLEFW IILVVTILGV YVGKIVIEYR KKKVLGE // ID Y1570_METJA Reviewed; 115 AA. AC Q58965; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1570; GN OrderedLocusNames=MJ1570; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.thermoautotrophicum MTH1706. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99594.1; -; Genomic_DNA. DR PIR; A64496; A64496. DR ProteinModelPortal; Q58965; -. DR STRING; 243232.MJ_1570; -. DR EnsemblBacteria; AAB99594; AAB99594; MJ_1570. DR KEGG; mja:MJ_1570; -. DR eggNOG; arCOG03159; Archaea. DR eggNOG; COG0310; LUCA. DR InParanoid; Q58965; -. DR KO; K02009; -. DR OMA; NYGDAWG; -. DR PhylomeDB; Q58965; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR025937; PDGLE_dom. DR InterPro; IPR020486; Uncharacterised_MJ1570. DR Pfam; PF13190; PDGLE; 1. DR ProDom; PD074023; Uncharacterised_MJ1570; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 115 Uncharacterized protein MJ1570. FT /FTId=PRO_0000107417. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. SQ SEQUENCE 115 AA; 12632 MW; 7DEA63DE6131C6A8 CRC64; MNWQDPLVKK FLYLIVAMVI LCPLGILLVW NYGDAWGEWG PEDVAEKVGE DKVSGLLHLA DIWSYAPLPD YDIPGWDDPF HASIGYIISA IVGVILCVGA YYALIKIVNP KAAAG // ID Y1573_METJA Reviewed; 61 AA. AC Q58968; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ1573; GN OrderedLocusNames=MJ1573; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99595.1; -; Genomic_DNA. DR PIR; D64496; D64496. DR STRING; 243232.MJ_1573; -. DR EnsemblBacteria; AAB99595; AAB99595; MJ_1573. DR KEGG; mja:MJ_1573; -. DR eggNOG; arCOG00555; Archaea. DR eggNOG; COG1205; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 61 Uncharacterized protein MJ1573. FT /FTId=PRO_0000107421. SQ SEQUENCE 61 AA; 7298 MW; 11F1BD4328B6BF5A CRC64; MVMLFPDYIR DVNQMKSSLS FLDKIEEDDL AISIYRDRKL SRKELFPIYL GATTHLHKEC Y // ID Y1574_METJA Reviewed; 684 AA. AC Q58969; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Uncharacterized ATP-dependent helicase MJ1574; DE EC=3.6.4.-; GN OrderedLocusNames=MJ1574; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the helicase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99590.1; -; Genomic_DNA. DR PIR; E64496; E64496. DR ProteinModelPortal; Q58969; -. DR STRING; 243232.MJ_1574; -. DR EnsemblBacteria; AAB99590; AAB99590; MJ_1574. DR KEGG; mja:MJ_1574; -. DR eggNOG; arCOG00555; Archaea. DR eggNOG; COG1205; LUCA. DR InParanoid; Q58969; -. DR KO; K06877; -. DR OMA; YPTRALI; -. DR PhylomeDB; Q58969; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004004; F:ATP-dependent RNA helicase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0010501; P:RNA secondary structure unwinding; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 684 Uncharacterized ATP-dependent helicase FT MJ1574. FT /FTId=PRO_0000102200. FT DOMAIN 54 239 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 264 419 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 67 74 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 181 184 DEVH box. SQ SEQUENCE 684 AA; 81280 MW; B60E8AFC0C6A49AE CRC64; MEDVFKGIEK EIIKIYKIPE RKGRFSNFKF KNKEINELID ALGFKLYLHQ VKALKYLYNK KDVVVTTSTA SGKSEIFRLA IFDNFLSNPD DRYLLIYPTR ALINNQYEKF SMENELFYKI TNKRVKAEIL TGDVGLEKRR EILKDKPNVL FTTPDMLHYQ ILKNHNNYLW LLKNLKLLVV DELHVYRGVF GTNMVYVFKR LLKLLKRLNN NLQILCLSAT LKNPKEFVKL LFNRDFEVVD KSYNPSSRKY LAILEPKNLD NKQLLRRLIE NLVDNNIKTL VFFDTRKETE KLMRFLLNSK VFYKLSTYKG TLPKYVREEI EEKFKNGEIL ALLTTNALEL GIDIGDLDAV INYGIPPDGI FSLIQRFGRA GRRDKEALNI IVLRKDGLDY YYKEHLNELY ERIRKGIIEY MPVNIKNRFV TKKHLHYLIS ELKIVDFDEL NDFEKEIVKE LEREGKIKIY KNPITNKTEI RNVKQPIYSS IRTASDESYY LILDKPWIKS KLLNKTQSEI LSFINWLKIK GYVIEEVDKD EYYRSLITGM PYFSRGKLFI AKDKIGIRKF HFIFADELDM FWDVEALQKK EEEIDILDIY DKKSYKDIDI YYGRLRVRKI YEGFIVRGVD VDKYYQELLA LKDNGILDAE IDLFKDFFGL NFISVKFNKK IIRDFETDGI WLCYFQIILG MLTK // ID Y1595_METJA Reviewed; 336 AA. AC Q58990; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=UPF0104 membrane protein MJ1595; GN OrderedLocusNames=MJ1595; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0104 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99613.1; -; Genomic_DNA. DR PIR; B64499; B64499. DR ProteinModelPortal; Q58990; -. DR STRING; 243232.MJ_1595; -. DR EnsemblBacteria; AAB99613; AAB99613; MJ_1595. DR KEGG; mja:MJ_1595; -. DR eggNOG; arCOG00899; Archaea. DR eggNOG; COG0392; LUCA. DR InParanoid; Q58990; -. DR KO; K07027; -. DR OMA; EAFRAYY; -. DR PhylomeDB; Q58990; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR022791; L-PG_synthase/AglD. DR Pfam; PF03706; LPG_synthase_TM; 1. DR TIGRFAMs; TIGR00374; TIGR00374; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 336 UPF0104 membrane protein MJ1595. FT /FTId=PRO_0000138105. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 127 147 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 285 305 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. SQ SEQUENCE 336 AA; 38163 MW; 282DC6E6C983198D CRC64; MMKIKITKST ILLIISFLFI LAIMAYIGLD KIIKVLINTN PEYVILAFIL QILVSVILSA RWKFIIKILG YSANFKNIFL LVLMGLFINN ITPSMRGGGE AFRAYYLSKL EEIPKGLAFS TVVVERVLDT AIFLFFTLFV IGYFVVTGFK YLEYLILSWI FLFSLTAIII YLIANKGLLI KTVTKISKFI CKYCSYNYDE TKILQSIEEF YNSMKFFKNK RGWEVVVAIF LSVMRYIFDI LKLWLLFLSL SYVVSVICVS AVYLITLLSG VLSITPSGFG TADTVMILSF SAFNIPPSVA AAVTLLDRLV SYILPTILGY IAMLIIKREI DKKKGK // ID Y1598_METJA Reviewed; 350 AA. AC Q58993; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=UPF0284 protein MJ1598 {ECO:0000255|HAMAP-Rule:MF_01086}; GN OrderedLocusNames=MJ1598; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0284 family. {ECO:0000255|HAMAP- CC Rule:MF_01086}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99619.1; -; Genomic_DNA. DR PIR; E64499; E64499. DR PDB; 3L0Z; X-ray; 2.65 A; A/B/C=1-350. DR PDBsum; 3L0Z; -. DR ProteinModelPortal; Q58993; -. DR STRING; 243232.MJ_1598; -. DR EnsemblBacteria; AAB99619; AAB99619; MJ_1598. DR KEGG; mja:MJ_1598; -. DR eggNOG; arCOG04272; Archaea. DR eggNOG; COG2038; LUCA. DR InParanoid; Q58993; -. DR OMA; VGDKMMP; -. DR PhylomeDB; Q58993; -. DR EvolutionaryTrace; Q58993; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008939; F:nicotinate-nucleotide-dimethylbenzimidazole phosphoribosyltransferase activity; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro. DR HAMAP; MF_01086; UPF0284; 1. DR InterPro; IPR003200; Nict_dMeBzImd_PRibTrfase-like. DR InterPro; IPR002805; Nict_dMeBzImd_PRibTrfase_put. DR Pfam; PF02277; DBI_PRT; 1. DR SUPFAM; SSF52733; SSF52733; 1. DR TIGRFAMs; TIGR00303; TIGR00303; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 350 UPF0284 protein MJ1598. FT /FTId=PRO_0000151051. FT STRAND 3 7 {ECO:0000244|PDB:3L0Z}. FT HELIX 11 14 {ECO:0000244|PDB:3L0Z}. FT STRAND 20 26 {ECO:0000244|PDB:3L0Z}. FT HELIX 31 33 {ECO:0000244|PDB:3L0Z}. FT STRAND 38 40 {ECO:0000244|PDB:3L0Z}. FT HELIX 42 45 {ECO:0000244|PDB:3L0Z}. FT HELIX 48 58 {ECO:0000244|PDB:3L0Z}. FT STRAND 62 64 {ECO:0000244|PDB:3L0Z}. FT HELIX 71 73 {ECO:0000244|PDB:3L0Z}. FT HELIX 78 88 {ECO:0000244|PDB:3L0Z}. FT STRAND 95 98 {ECO:0000244|PDB:3L0Z}. FT STRAND 108 111 {ECO:0000244|PDB:3L0Z}. FT HELIX 118 120 {ECO:0000244|PDB:3L0Z}. FT HELIX 127 139 {ECO:0000244|PDB:3L0Z}. FT STRAND 144 151 {ECO:0000244|PDB:3L0Z}. FT HELIX 155 165 {ECO:0000244|PDB:3L0Z}. FT TURN 171 173 {ECO:0000244|PDB:3L0Z}. FT STRAND 177 179 {ECO:0000244|PDB:3L0Z}. FT HELIX 183 197 {ECO:0000244|PDB:3L0Z}. FT HELIX 205 212 {ECO:0000244|PDB:3L0Z}. FT HELIX 216 229 {ECO:0000244|PDB:3L0Z}. FT STRAND 234 239 {ECO:0000244|PDB:3L0Z}. FT HELIX 240 252 {ECO:0000244|PDB:3L0Z}. FT HELIX 254 256 {ECO:0000244|PDB:3L0Z}. FT STRAND 262 267 {ECO:0000244|PDB:3L0Z}. FT HELIX 268 271 {ECO:0000244|PDB:3L0Z}. FT HELIX 278 285 {ECO:0000244|PDB:3L0Z}. FT STRAND 290 293 {ECO:0000244|PDB:3L0Z}. FT HELIX 297 299 {ECO:0000244|PDB:3L0Z}. FT HELIX 303 310 {ECO:0000244|PDB:3L0Z}. FT HELIX 319 328 {ECO:0000244|PDB:3L0Z}. FT HELIX 334 343 {ECO:0000244|PDB:3L0Z}. SQ SEQUENCE 350 AA; 37800 MW; 0A7B711273B71C2F CRC64; MSIIAINENG FLDKIKGRNP LFTCVISSIE TTLSIPISGV HRDVIKYTPS ADVELVFYGK SLTLKTPPID ATGSPTPATI TRACVELKNI KNLHIDAGAF VKPKIPFIEI DEKPTGRIEE GKAMNNSKEL YMKGYLLGKN LDAELLIVGE SVPGGTTTAL GVLLGLGYDA EGKVSSGSIN NPHELKIKVV REGLKKAGIN EKSSVFDVLN AVGDKMMPVV AGLAISFAER NKPVILAGGT QMSAVLAVIK EINKKVLDKN LIAIGTTEFV LNDKKGDLKG IVEQIGNVPV LASKFYFEKA KIEGLKNYCK GSVKEGVGAG GIAVYSIVND LEPTKIREFI ENKFYEWYKE // ID Y1601_METJA Reviewed; 160 AA. AC Q58996; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1601; GN OrderedLocusNames=MJ1601; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99621.1; -; Genomic_DNA. DR PIR; H64499; H64499. DR ProteinModelPortal; Q58996; -. DR STRING; 243232.MJ_1601; -. DR EnsemblBacteria; AAB99621; AAB99621; MJ_1601. DR KEGG; mja:MJ_1601; -. DR eggNOG; arCOG04396; Archaea. DR eggNOG; COG2061; LUCA. DR InParanoid; Q58996; -. DR OMA; MRVSMDI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR002912; ACT_dom. DR Pfam; PF01842; ACT; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 160 Uncharacterized protein MJ1601. FT /FTId=PRO_0000107434. FT DOMAIN 3 80 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 160 AA; 18337 MW; 0886905973D1D0EA CRC64; MITIDIELKD KPGELLRVLT PISKYGANVI SIIHSREEKR GGKVPVRIVI DVDDKDKLKK ILEDLEKEGA IIKKIDGKDK KVYLDVVVIG HVVDTNVRDT IDRINEIGLV EDLDLIMPHP DKESSAMMRI IVDEDKIEEL FYLFEELEKE KGLLFIKSIF // ID Y1610_METJA Reviewed; 615 AA. AC Q59005; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=Uncharacterized glycosyl hydrolase MJ1610; DE EC=3.2.1.-; GN OrderedLocusNames=MJ1610; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 15 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99630.1; -; Genomic_DNA. DR PIR; A64501; A64501. DR ProteinModelPortal; Q59005; -. DR STRING; 243232.MJ_1610; -. DR CAZy; GH15; Glycoside Hydrolase Family 15. DR EnsemblBacteria; AAB99630; AAB99630; MJ_1610. DR KEGG; mja:MJ_1610; -. DR eggNOG; arCOG03285; Archaea. DR eggNOG; COG3387; LUCA. DR InParanoid; Q59005; -. DR OMA; SNAMFLI; -. DR PhylomeDB; Q59005; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004339; F:glucan 1,4-alpha-glucosidase activity; IEA:InterPro. DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IBA:GO_Central. DR GO; GO:0016052; P:carbohydrate catabolic process; IBA:GO_Central. DR GO; GO:0005976; P:polysaccharide metabolic process; IEA:InterPro. DR Gene3D; 1.50.10.10; -; 1. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR012341; 6hp_glycosidase. DR InterPro; IPR000165; Glucoamylase. DR InterPro; IPR006465; Oligosac_amylase. DR SUPFAM; SSF48208; SSF48208; 1. DR TIGRFAMs; TIGR01577; oligosac_amyl; 1. DR PROSITE; PS00820; GLUCOAMYLASE; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosidase; Hydrolase; Reference proteome. FT CHAIN 1 615 Uncharacterized glycosyl hydrolase FT MJ1610. FT /FTId=PRO_0000186121. FT ACT_SITE 403 403 Proton acceptor. {ECO:0000255|PROSITE- FT ProRule:PRU10051}. FT ACT_SITE 406 406 Proton donor. {ECO:0000255|PROSITE- FT ProRule:PRU10051}. SQ SEQUENCE 615 AA; 72008 MW; 2B37EB89F0357BE5 CRC64; MIYMGGIVGN NSLLAKIGDY GEIEYLFYPQ VGYETHFFDS ALAVYDKKVK WHWDDDWDIT QKYIEETNIF KTILEDDKII LTIKDFVPVS HNVLIRRVYI KNKLDKKLNF KLFFYENLRI GENPITNTVK FLEDGCIVKY NGKYIFCIGS DKRIDSFQCG NRYSKTSAYI DIENGILKEH KESSGLLTDS AISWNIKIDE KRSLAFNIYI LPQRFDGDFS IITEQLKIIM NNSENIKNLS MNYWKHIIGE INRFIHPELR QNNKIYSITK RALMTLLMLC DKEGGIIAAP SLHPDYRYVW GRDGSYISIA LDLFGIRNIP DRFFEFMSKI QNADGSWLQN YYVNGKPRLT AIQTDQIGSI LWAMDVHYRL TGDRKFVERY WNTIEKAANY LRLVALNFTP CFDLWEERFG VFAYTMGATY AGLKCAYSMS KAVNKRDKVK DWGKTIEFLK HEVPKRFYLE DEERFAKSIN PLDKTIDTSI LGLSYPFNLI DVDDERMIKT AEAIEKAFKY KVGGIGRYPE DIYFGGNPWI ITTLWLSLYY RRLYKVLKEK DDNGADIYLQ KSKKLFNWVM KYSFDGLFPE QIHKELGVPM SAMPLGWSNA MFLIYVYEND KVIIP // ID Y1621_METJA Reviewed; 57 AA. AC Q59016; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ1621; GN OrderedLocusNames=MJ1621; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99647.1; -; Genomic_DNA. DR PIR; D64502; D64502. DR STRING; 243232.MJ_1621; -. DR EnsemblBacteria; AAB99647; AAB99647; MJ_1621. DR KEGG; mja:MJ_1621; -. DR eggNOG; arCOG02209; Archaea. DR eggNOG; COG2244; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 57 Uncharacterized protein MJ1621. FT /FTId=PRO_0000107443. FT TRANSMEM 4 26 Helical. {ECO:0000255}. FT TRANSMEM 33 55 Helical. {ECO:0000255}. SQ SEQUENCE 57 AA; 6422 MW; 076F438483AED617 CRC64; MPTVNILSYF AFSVEAVLFP MSSELWEKGY REALGYGVEK ICLYSFVLVL PIAILMA // ID Y1628_METJA Reviewed; 448 AA. AC Q59022; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1628; GN OrderedLocusNames=MJ1628; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99655.1; -; Genomic_DNA. DR PIR; B64503; B64503. DR ProteinModelPortal; Q59022; -. DR STRING; 243232.MJ_1628; -. DR EnsemblBacteria; AAB99655; AAB99655; MJ_1628. DR KEGG; mja:MJ_1628; -. DR eggNOG; arCOG01746; Archaea. DR eggNOG; COG3044; LUCA. DR InParanoid; Q59022; -. DR KO; K06924; -. DR OMA; RHYRIAG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR019195; ABC_ATPase_put. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF09818; ABC_ATPase; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 448 Uncharacterized protein MJ1628. FT /FTId=PRO_0000107447. FT NP_BIND 257 264 ATP. {ECO:0000255}. SQ SEQUENCE 448 AA; 51262 MW; 122A0233DFEFFDA2 CRC64; MFVDEVINNL KGNEFLNTTL LTKSNKNKLY YAVKQPDGNI KVVLPFVFEN KNFLKLSEYK DGIEGATQRV IEEIKQEIIK KKRFLPLAGY FGRIYKALYE PLTVVNCNLN LGYDLWKVDK YNYIEGDKIY LMLRMIFKEK DSKEIVKQIN ELCNDLDKFI KKIPIDLLID EAKNIINQKY LRDKLDELGL VCFIANNSKP ARKYTEVRRH YRIAGPKDVN IPFECPEELE PIEIELKYGK KVKGLGIKKK EIFIITGRNA QGKTTLLQAI DSGRDDHLIG DGREFIITTK SLSKASTGSM EMSGQDISLF FQKLPPGIKG SPKAVYGTAS GSMYMAYQIQ RAIKNKTKLI LIDEDNSAVN LLVSGVLSKW FEGVKSLAEI IMEDREKLGD SSFIIVTSSL DLLTALGDRA IYLEDHKAKY LDLTYFREEL GRYYLELASK FIGVKIRE // ID Y1656_METJA Reviewed; 237 AA. AC Q59050; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1656; GN OrderedLocusNames=MJ1656; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FAH family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99677.1; -; Genomic_DNA. DR PIR; F64506; F64506. DR ProteinModelPortal; Q59050; -. DR STRING; 243232.MJ_1656; -. DR EnsemblBacteria; AAB99677; AAB99677; MJ_1656. DR KEGG; mja:MJ_1656; -. DR eggNOG; arCOG00235; Archaea. DR eggNOG; COG0179; LUCA. DR InParanoid; Q59050; -. DR OMA; PCKDVSA; -. DR PhylomeDB; Q59050; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.90.850.10; -; 1. DR InterPro; IPR011234; Fumarylacetoacetase_C-rel. DR Pfam; PF01557; FAA_hydrolase; 1. DR SUPFAM; SSF56529; SSF56529; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJ1656. FT /FTId=PRO_0000156838. FT METAL 91 91 Divalent metal cation. {ECO:0000250}. FT METAL 93 93 Divalent metal cation. {ECO:0000250}. FT METAL 122 122 Divalent metal cation. {ECO:0000250}. SQ SEQUENCE 237 AA; 26985 MW; E88847ECDD94DD7C CRC64; MIISFEKLGE KYKIIDLNLN SIKQKIGDSL NIKEIKPTKI ICVGLNYIDH AKELNMEIPE YPIIFLKPTS AIIYNEDYII RPRISKRVDY EVELAIVIGK KCKNIKKDEA NDYIMGYTIL NDVTARDLQQ KDGQWTRAKS FDTFCPIGPR IVKDIDPMNL NIECRVNGEI KQKSNTKNMI FDVYELVEFV ASIMTLYPGD IISTGTPPGV GELKAGDVVE CEIEGIGILR NYVKDEE // ID Y1662_METJA Reviewed; 555 AA. AC Q59056; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ1662; GN OrderedLocusNames=MJ1662; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99680.1; -; Genomic_DNA. DR ProteinModelPortal; Q59056; -. DR STRING; 243232.MJ_1662; -. DR EnsemblBacteria; AAB99680; AAB99680; MJ_1662. DR KEGG; mja:MJ_1662; -. DR eggNOG; arCOG00185; Archaea. DR eggNOG; COG1123; LUCA. DR InParanoid; Q59056; -. DR KO; K00400; -. DR OMA; GKRVNSY; -. DR PhylomeDB; Q59056; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 3. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 555 Uncharacterized ABC transporter ATP- FT binding protein MJ1662. FT /FTId=PRO_0000093227. FT DOMAIN 4 244 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 255 547 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 292 299 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 555 AA; 63040 MW; 18BBF0BB89E037E1 CRC64; MITVKVKNLT KKYGDFKALD KVSFEAKKGE ILGIVGKSGA GKSTLIRILR GSLDYDEGEV EILGRKDNFK EITAIHLQRN FALWAEPVIN NIIRKLYAIR NNADEQLPLE EEWEEYEKTA IEILKLVGLE HKKDAFANIL SGGEKQRLIL GRQIAKIYEK GEGVLLLDEP ATMACPASKQ KLLDVIKNIR DKLGITVIIT SHLPEIHRYL CDRLILLENG KVKMDGDVEE VLNEFLKKMK PPYKRTPNIK DNAIIQVRNV SKRYYVVHGG ETLNLRNVSF DVKEGEILSI IGPSGVGKTV IMRLMAGLEL PDEGKIIVDG IDITNYGWER IELRKRIGIM HQEFSLPYYQ TVENLLKYRL GLKGEKAIAH AKAKAEELGL SPKIVDALYQ LIDVPESERI SKLQKMGLTE DIIYKLFPPV VESFEPEEIL EALDLGKDIL KKKVIELSGG QKVRVAMALQ LITKPKILFL DEPFGDLDPI TLRDVANYLK IINERFGTTI VLVSHCVEFI KEISDRAILL DENRLVMEGN PEEVCEEFIR RSNARFMKEE LKCKN // ID Y1665_METJA Reviewed; 458 AA. AC Q59059; DT 19-SEP-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=UPF0210 protein MJ1665 {ECO:0000255|HAMAP-Rule:MF_01221}; GN OrderedLocusNames=MJ1665; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0210 family. {ECO:0000255|HAMAP- CC Rule:MF_01221}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99687.1; -; Genomic_DNA. DR PIR; G64507; G64507. DR ProteinModelPortal; Q59059; -. DR STRING; 243232.MJ_1665; -. DR EnsemblBacteria; AAB99687; AAB99687; MJ_1665. DR KEGG; mja:MJ_1665; -. DR eggNOG; arCOG04321; Archaea. DR eggNOG; COG2848; LUCA. DR InParanoid; Q59059; -. DR KO; K09157; -. DR OMA; EAMTSVC; -. DR PhylomeDB; Q59059; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01221; UPF0210; 1. DR InterPro; IPR007841; UPF0210. DR Pfam; PF05167; DUF711; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 458 UPF0210 protein MJ1665. FT /FTId=PRO_0000070564. SQ SEQUENCE 458 AA; 48599 MW; 2B7DECC92BB06501 CRC64; MFRPEEIIET IKMIKMENLD LRTVTLGLSL RDCVSKDLDE LKENIYNKIT SSAENLVETA ERISEKYGIP IVNKRIAVTP ISLVIGGAIK DLDKEEQIKA CVEVGEVLDK AAKKVRVDFL GGYSALVHKD ATKEDRALID SIPFMMEKTE RVCSSVNVAS TKTGINMDAV KRMGEIIKET AFRTEKAIGC AKLVVFANAP EDNPFMAGAF HGVGEGDKVI NVGVSGPGVV RAVIEKLPDA DFGTLANEIK KVAFKITRVG ELIGREVSKE LGVKFGVVDL SLAPTPARGD SIANILEAMG LEKCGTHGST AALALLNDAV KKGGAMATSY VGGLSGAFIP VSEDSGMVEA VEAGALTLEK LEAMTCVCSV GIDMVAIPGD TPASTISAII ADEMAIGVIN NKTTAVRIIP VPGKKAGEYV DYGGLLGKAP IMEVNKYSSE KFIKRGGRIP APLQALTN // ID Y1681_METJA Reviewed; 380 AA. AC Q59075; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 84. DE RecName: Full=Uncharacterized protein MJ1681; GN OrderedLocusNames=MJ1681; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99702.1; -; Genomic_DNA. DR PIR; G64509; G64509. DR ProteinModelPortal; Q59075; -. DR STRING; 243232.MJ_1681; -. DR EnsemblBacteria; AAB99702; AAB99702; MJ_1681. DR KEGG; mja:MJ_1681; -. DR eggNOG; arCOG00621; Archaea. DR eggNOG; COG1146; LUCA. DR eggNOG; COG1900; LUCA. DR InParanoid; Q59075; -. DR OMA; TCRQSDR; -. DR PhylomeDB; Q59075; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR002708; HcyBio. DR InterPro; IPR017677; Methan_mark_16. DR Pfam; PF01837; HcyBio; 1. DR ProDom; PD011569; DUF39; 1. DR TIGRFAMs; TIGR03287; methan_mark_16; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 380 Uncharacterized protein MJ1681. FT /FTId=PRO_0000107481. FT DOMAIN 287 318 4Fe-4S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. SQ SEQUENCE 380 AA; 42581 MW; D362219799F4796A CRC64; MEKELKVITI DELKKYIRNN EEDKIEEVDV VTSATCGIMS GTAGIFHIPF NEVFKRAEEI YLNDIKGVVG ICPNEFLGKV DAIFYGEVGF LFKDLVKGKV VEAKAISEGK IYKNEITIDD LPTAKMIGTR MAFKNYTAIT NLSDEEVNTI FHRLPLKKGE ASFSGCGMLN PLENMVIKDE KDVVGKKALL NGAEAIILGF GTRASIEKPN LMMSADMKDM DAYYLGGFVT SNGIEIYNTI AVPIKVDEHK EALKKLDKDI TLPLVNIFGR EIIDIGSYAE VWENVDLRPK IYQDKCKNCR ECLVEKYCPT FAIKRENGKI KITEDCFGCG VCNICPYGVF KTKLGSVCGI PITCRQSDRK RALKLAKELK KKIERGEFKI // ID Y198_METJA Reviewed; 314 AA. AC Q57651; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Uncharacterized protein MJ0198; GN OrderedLocusNames=MJ0198; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98193.1; -; Genomic_DNA. DR PIR; G64324; G64324. DR ProteinModelPortal; Q57651; -. DR STRING; 243232.MJ_0198; -. DR EnsemblBacteria; AAB98193; AAB98193; MJ_0198. DR KEGG; mja:MJ_0198; -. DR eggNOG; arCOG01170; Archaea. DR eggNOG; COG0148; LUCA. DR OMA; IKVMITT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000015; C:phosphopyruvate hydratase complex; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0004634; F:phosphopyruvate hydratase activity; IEA:InterPro. DR GO; GO:0006096; P:glycolytic process; IEA:InterPro. DR Gene3D; 3.30.390.10; -; 1. DR InterPro; IPR020811; Enolase_N. DR InterPro; IPR029017; Enolase_N-like. DR Pfam; PF03952; Enolase_N; 1. DR SMART; SM01193; Enolase_N; 1. DR SUPFAM; SSF54826; SSF54826; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 314 Uncharacterized protein MJ0198. FT /FTId=PRO_0000106737. SQ SEQUENCE 314 AA; 35242 MW; 439FC94A7DAEDDEA CRC64; MTNVIIEKIS AKEVFKGAKI KVMITTMTNI SIGYDIIEVN NPEEAIADVE NVIAPELIGY PATDIDFIDS LICETSVNNP TVAMGISISV ARAASNSLDI PLFKFLGGAL TTELPIVASG ILVDKDKNEL IPIVMADSIE DIVNLYLKLT DVLSHDYSIV NIDGAYTCKD IFNEIPKIRN LIDEIKEDED LDILLGLSSK KETVKDKDLS QIDYLEVEEP VEFDGFLCTD SIYEESDFVK VFPYEMGTIT EMYYYINYIM DKGLYPVIFG NNSSFAHIAV SFKVPFLRPK LSSNVLNEVW NIERTIMNPN IRRF // ID Y202_METJA Reviewed; 304 AA. AC Q57655; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0202; GN OrderedLocusNames=MJ0202; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98186.1; -; Genomic_DNA. DR PIR; C64325; C64325. DR ProteinModelPortal; Q57655; -. DR STRING; 243232.MJ_0202; -. DR EnsemblBacteria; AAB98186; AAB98186; MJ_0202. DR KEGG; mja:MJ_0202; -. DR eggNOG; arCOG04410; Archaea. DR eggNOG; COG1578; LUCA. DR InParanoid; Q57655; -. DR KO; K09116; -. DR OMA; YILKAKC; -. DR PhylomeDB; Q57655; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002791; DUF89. DR InterPro; IPR014444; UCP006593. DR Pfam; PF01937; DUF89; 1. DR PIRSF; PIRSF006593; UCP006593; 1. DR SUPFAM; SSF111321; SSF111321; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 304 Uncharacterized protein MJ0202. FT /FTId=PRO_0000106739. SQ SEQUENCE 304 AA; 34419 MW; 8A3FA78D5085CA8C CRC64; MVLLILKFHG ESVKIKPECA ICIIRQVVDA ANEITDDERE QFRLIKSTME VIKDVYGESA VPAWMGTVVH RYLKKISNNN DPYKNLKEKA NKIALQYLDK VREMSNTDDE LERLRKKVLA TIAGNVIDFG AYSTGINIEK LIEDTLNGEL KIDNSRKLLN DLKDKNIKKI LYICDNAGEI IFDRVLMEEI KKYDKDIVAV VKGKPILNDA TLEDAKIAKI DEIAKVITTG SDIIGIILEE CSEEFLKEFE SADLIIAKGM GNYESLTEYE DKIDKPIYYI LKAKCKPVAE NIGVDVGDNV LLKR // ID Y006_METJA Reviewed; 378 AA. AC Q60314; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized oxidoreductase MJ0006; DE EC=1.-.-.-; GN OrderedLocusNames=MJ0006; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000250}; CC -!- COFACTOR: CC Name=Mo-bis(molybdopterin guanine dinucleotide); CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000250}; CC Note=Binds 1 molybdenum-bis(molybdopterin guanine dinucleotide) CC (Mo-bis-MGD) cofactor per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S Mo/W bis-MGD-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU01004}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97987.1; -; Genomic_DNA. DR PIR; F64300; F64300. DR ProteinModelPortal; Q60314; -. DR STRING; 243232.MJ_0006; -. DR EnsemblBacteria; AAB97987; AAB97987; MJ_0006. DR KEGG; mja:MJ_0006; -. DR eggNOG; arCOG04862; Archaea. DR eggNOG; COG0243; LUCA. DR InParanoid; Q60314; -. DR KO; K00123; -. DR OMA; GHCICNS; -. DR PhylomeDB; Q60314; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003954; F:NADH dehydrogenase activity; IBA:GO_Central. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 2. DR SMART; SM00926; Molybdop_Fe4S4; 1. DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Molybdenum; Oxidoreductase; Reference proteome. FT CHAIN 1 378 Uncharacterized oxidoreductase MJ0006. FT /FTId=PRO_0000063231. FT DOMAIN 1 57 4Fe-4S Mo/W bis-MGD-type. FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 8 8 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 11 11 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 15 15 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. FT METAL 43 43 Iron-sulfur (4Fe-4S). FT {ECO:0000255|PROSITE-ProRule:PRU01004}. SQ SEQUENCE 378 AA; 42051 MW; E0C13060FF2609AA CRC64; MKVVHTICPG CSVGCGIDLI VKDDKVVGTY PYKRHPINEG KNCSNGKNSY KIIYHEKRLK KPLIKKNGKL VEATWDEALS FIAEKLKNYN ADDITFIASG KCTNEDNYAL KKLVDSLKAK IGHCICNSPK VNYAEVSTTI DDIENAKNII IIGDVFSEHA LIGRKVIKAK EKGSKVTIFN TEEKEILKLN ADEFVKVDSY LGVDLSNVDK NTIIIINAPV NVDEIIKTAK ENKAKVLPVA KHCNTVGATL IGIPALNKDE YFELLKNSKF LYIMGENPAL VDKDVLKNVE FLVVQDIIMT ETAEMADVVL PSTCWAEKDG TFINTDKRIQ KINKAVNPPG DAMDDWLIIK SLAEKLGSDL GFNSLEDIQQ DIHRNKLL // ID Y077_METJA Reviewed; 382 AA. AC Q60384; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0077; GN OrderedLocusNames=MJ0077; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98058.1; -; Genomic_DNA. DR PIR; D64309; D64309. DR ProteinModelPortal; Q60384; -. DR STRING; 243232.MJ_0077; -. DR EnsemblBacteria; AAB98058; AAB98058; MJ_0077. DR KEGG; mja:MJ_0077; -. DR eggNOG; arCOG00442; Archaea. DR eggNOG; COG2425; LUCA. DR InParanoid; Q60384; -. DR OMA; FFKYEVE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002035; VWF_A. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF53300; SSF53300; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 382 Uncharacterized protein MJ0077. FT /FTId=PRO_0000106683. SQ SEQUENCE 382 AA; 44917 MW; EC9C2F7C4EBEA695 CRC64; MIRYDKYDKM VWEGCKNKIT FHLSERETEI VFYLFFKYEV EILTETDLIK KIVRDRRFKN VKSITTLDEN YSLIATEFFC EKLKELKEKG REEDISELLD ELESYMENIT SSFSSFGSGE GYKSYTDPKK KLELTEKLLK NNKLKEFMKV LGKFKRMAIK KYKTKIKHFS GEKYSINLGN NLINLLSSEY KNFAEEILFV DLLRRYNENK PLNYKILENN ENCGDFVVCL DLSGSMRGNK EIWAKAIALC LMDISLKRNK RYISILFDDG VRDIKIYEKK VSFDEILEFA SVFYGGGTNF EKPLREALKF NGDIVFITDG ECEVSLEFLE KIKEEKQRRK IKIYSICINT KPTVSLRQIS DVSVTIYELT SKTAEKVFDM LI // ID Y084_METJA Reviewed; 249 AA. AC Q60392; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized ATP-binding protein MJ0084; GN OrderedLocusNames=MJ0084; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98064.1; -; Genomic_DNA. DR PIR; D64310; D64310. DR ProteinModelPortal; Q60392; -. DR STRING; 243232.MJ_0084; -. DR EnsemblBacteria; AAB98064; AAB98064; MJ_0084. DR KEGG; mja:MJ_0084; -. DR eggNOG; arCOG00588; Archaea. DR eggNOG; COG3640; LUCA. DR InParanoid; Q60392; -. DR KO; K07321; -. DR OMA; MKISICG; -. DR PhylomeDB; Q60392; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR014433; CooC. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF005647; CooC; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 249 Uncharacterized ATP-binding protein FT MJ0084. FT /FTId=PRO_0000106686. FT NP_BIND 7 14 ATP. {ECO:0000255}. SQ SEQUENCE 249 AA; 27655 MW; C84434BC1913D023 CRC64; MKISICGKGG CGKSSITTLL AKEFAKKGHN VLVIDGDESN LSLHKLLGMD LPKDFIEYLG GRKEFMKKLR EKMDGKEVEL FEGEISIDSL PKEYLVEKDN IKLLAIGKIH DFGEGCACPM GALLREFLKS LKLKDKEVVI VDTEAGIEHF GRGVEGGCDV IIAIIDPTYE SIRLSKKIEE IGEKLGKKVY FIVNKVDDET KDLILENVNK DKVIAVIPNN KEIMKCGLMG EELNAELSEI KDVVEILTK // ID Y095_METJA Reviewed; 126 AA. AC Q57560; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0095; GN OrderedLocusNames=MJ0095; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98086.1; -; Genomic_DNA. DR PIR; G64311; G64311. DR STRING; 243232.MJ_0095; -. DR EnsemblBacteria; AAB98086; AAB98086; MJ_0095. DR KEGG; mja:MJ_0095; -. DR eggNOG; arCOG05010; Archaea. DR eggNOG; COG4921; LUCA. DR InParanoid; Q57560; -. DR OMA; DISGRHR; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014514; UCP021940. DR Pfam; PF09974; DUF2209; 1. DR PIRSF; PIRSF021940; UCP021940; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 126 Uncharacterized protein MJ0095. FT /FTId=PRO_0000106691. SQ SEQUENCE 126 AA; 14709 MW; D41D24ABDD043E9B CRC64; MAIDISGRHH ENDIFFRVYA GVLVEIKADR IVHVEKIDVM VKEEETQKLR DIVKEVKELI DKVGDEFDYI LCERGEFFNI SKDIISAILK KEVIFPKTRG ELEAINIAHH VSYSVRKLLI EEKRKS // ID Y096_METJA Reviewed; 262 AA. AC Q57561; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0096; GN OrderedLocusNames=MJ0096; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98087.1; -; Genomic_DNA. DR PIR; H64311; H64311. DR ProteinModelPortal; Q57561; -. DR STRING; 243232.MJ_0096; -. DR EnsemblBacteria; AAB98087; AAB98087; MJ_0096. DR KEGG; mja:MJ_0096; -. DR eggNOG; arCOG05021; Archaea. DR eggNOG; ENOG410YS84; LUCA. DR OMA; SIWYSYF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 262 Uncharacterized protein MJ0096. FT /FTId=PRO_0000106692. FT TRANSMEM 21 41 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 205 225 Helical. {ECO:0000255}. FT TRANSMEM 240 260 Helical. {ECO:0000255}. SQ SEQUENCE 262 AA; 29463 MW; 47329C0221DDCFA2 CRC64; MEVKAMEIFK KYLSLNIPKK ILITYFLCWA GFLFSFSVGK FLLYLSSILK SNFISEPAKL AQSVGTAKFN AVSSAVSNTV GVKNAYLTYA LSYIVSNFMG CLIIMFALGA LAYLYKKDLE KAKTLEEKEE LFKCYQKYLL ILFIFTVINP LTGLIGVNLQ YSDLIAVLPH GFFEFFGFAT AVVVGVELSN KILPIVKREI TSKKIVILIA CSFIFIFIAG MLEPIDWFIY SYAKAYGIPL LAAFATGYKN LFLYLISMLF KS // ID Y1004_METJA Reviewed; 214 AA. AC Q58410; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1004; GN OrderedLocusNames=MJ1004; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99008.1; -; Genomic_DNA. DR PIR; C64425; C64425. DR ProteinModelPortal; Q58410; -. DR STRING; 243232.MJ_1004; -. DR EnsemblBacteria; AAB99008; AAB99008; MJ_1004. DR KEGG; mja:MJ_1004; -. DR eggNOG; arCOG00628; Archaea. DR eggNOG; ENOG4111KJJ; LUCA. DR OMA; CGGLEKF; -. DR PhylomeDB; Q58410; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR016486; UCP006591_CBS. DR Pfam; PF00571; CBS; 2. DR PIRSF; PIRSF006591; UCP006591_CBS_MJ1004; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 214 Uncharacterized protein MJ1004. FT /FTId=PRO_0000107139. FT DOMAIN 7 65 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 69 129 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 214 AA; 24585 MW; 7D259934229043E7 CRC64; MKVRDLMDKN FAKIYVDETV EDAINLLKKK KRFSAPIVDK EDRLVGWVTT LELLGISEKD FKKPITEFMR PVEEVITVYE DDEARNVVLK FVKYKVVSIP VLTRDGRVIG MVRNCDVVKT LAKLYEIPVY KIFKELHNHI GDISWEELME AAAVVTKRMT GEDITPQEYE ERIKKTTFGK AIWACGGLEK FFVGLIEIGM VALARKLAKR RKGG // ID Y1036_METJA Reviewed; 233 AA. AC Q58442; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1036; GN OrderedLocusNames=MJ1036; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99045.1; -; Genomic_DNA. DR PIR; C64429; C64429. DR ProteinModelPortal; Q58442; -. DR STRING; 243232.MJ_1036; -. DR EnsemblBacteria; AAB99045; AAB99045; MJ_1036. DR KEGG; mja:MJ_1036; -. DR eggNOG; arCOG00576; Archaea. DR eggNOG; COG0428; LUCA. DR InParanoid; Q58442; -. DR KO; K07238; -. DR OMA; ISFFIHT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003689; ZIP. DR Pfam; PF02535; Zip; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 233 Uncharacterized protein MJ1036. FT /FTId=PRO_0000107151. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 119 139 Helical. {ECO:0000255}. FT TRANSMEM 159 179 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. SQ SEQUENCE 233 AA; 26171 MW; D2D82ACF6200DB58 CRC64; MSNMVEVPIF IAILSFIVMC IGELLAYYSV SLKYKYEFEA ISFGFIFGVA TLILIPKSYS NMFVLYVILG MITVYLIEKY LAYCPLSKKY CVECDNLEEN RIKFIYPISF FIHTFIDGLI IAVSYISEIG LPLYLAILMH KLPAGFVLIS PLKGVYKNPL YPGVFVSFGT VLGTIVGLVT LKDVSTKILL AFSGGVFLGA FLMLAPHIYE HKEEKTFLYI LLGYILVGII ALH // ID Y104_METJA Reviewed; 663 AA. AC Q57568; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized ATP-dependent helicase MJ0104; DE EC=3.6.4.-; GN OrderedLocusNames=MJ0104; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98084.1; -; Genomic_DNA. DR PIR; H64312; H64312. DR ProteinModelPortal; Q57568; -. DR STRING; 243232.MJ_0104; -. DR EnsemblBacteria; AAB98084; AAB98084; MJ_0104. DR KEGG; mja:MJ_0104; -. DR eggNOG; arCOG00792; Archaea. DR eggNOG; COG1112; LUCA. DR InParanoid; Q57568; -. DR OMA; DFFLIHG; -. DR PhylomeDB; Q57568; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR004483; SMUBP-2/Hcs1-like. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00376; TIGR00376; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 663 Uncharacterized ATP-dependent helicase FT MJ0104. FT /FTId=PRO_0000080730. FT NP_BIND 207 214 ATP. {ECO:0000250}. SQ SEQUENCE 663 AA; 77573 MW; 590C64A66AB4DE4F CRC64; MQNWFKSGDS LNLVDLYVKK FMDLIEIERR CEMDFHKNEI IKLGKKRENV GRAILNLKGK FLGESLGCTI VRFGRKKPFK TEISPGDVVL VSKENPLQSD LYANVIYVGK NFIDVAFDVD VPKWVYKERV RVDLYVNDIT FKRMKEALRE FARKRDKLAY IILGIEHPEK PLREDIKLEF YDKNLNESQK LAVKKAVLSR DLYLIHGPPG TGKTRTITEV IVQEVKFNKH KVLATADSNI AADNILEYLI KKYPDLKVVR VGHPTRISKD LIQHSLPYLI ENHEKYQEIL ALREKIKEIK EQRDKFLKPS PRWRRGMSDE QILKVAKRKK SYRGIPKEKI VSMAEWIIRN KKIKRIINNL DEITEKIMNE ILAEADVIVA TNSMAGSEIL KGWEFDVIVI DEGSQAMEPS CLIPIVKGRK LIMAGDHKQL PPTVLSENEE LKKTLFERLI KKYPEFSSIL EIQYRMNEKI MEFPNKMFYN NKLKADESVK NITLLDLVKE EEIDEVDRDI INEIPVQFIN VEGIERKDKE SPSYYNIEEA EKVLEIVKKL VKYKIPTNVI TPYDAQVRYL RRLFEEHNID IEVNTVDGFQ GRENEAIVIS FVRTKNFGFL KDLRRLNVAI TRAKRKLILI GNENLLKQDK VYNEMIKWAK SVEEEHKNKI IQK // ID Y1060_METJA Reviewed; 537 AA. AC Q58460; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1060; GN OrderedLocusNames=MJ1060; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99072.1; -; Genomic_DNA. DR PIR; C64432; C64432. DR ProteinModelPortal; Q58460; -. DR STRING; 243232.MJ_1060; -. DR EnsemblBacteria; AAB99072; AAB99072; MJ_1060. DR KEGG; mja:MJ_1060; -. DR eggNOG; arCOG06580; Archaea. DR eggNOG; ENOG411115R; LUCA. DR OMA; TIAFSHE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 537 Uncharacterized protein MJ1060. FT /FTId=PRO_0000107154. SQ SEQUENCE 537 AA; 65990 MW; 83E8A0C63B6D0837 CRC64; MIVEIYNFNF IRINEKEIKL FYNTYPPLKK LECYLDFIKE LVSNSYKNNK FIKKDEFEHL VYNTFLYFLI NWDNLYHTNQ MPFYIWYNFK ERVDDILKSE KDITFILNQK YVNIDYFGKY LKKFTNNIKS KNKNRIVDYI MENFQGNLIM LYFLVRKIIM NKNNNYRFDI LFITDYDRYY GNNRFFGNHL FKNEEFKKLL KNFDINLTDK NYSILFTKYN FINLPKYIKD YYKKRQDYLF IEDILNLKLG FDILLNSSKI FKKVNLTNYN DEHEKFIHTM FNIFLKHKLP FVLWFYLSIK DYISKTNIKC IVGDSERNFM FYLCNIYRLW RKNIKTIAFS HEVINNNYIH LPISEKYSCI PDCKLVWNEN IKKLLIDKYN FPKDKVIVFP DPRFLYWKKY PKKEKTILFV SQGYPEFYEE IFNTFRDKKL INTLIEHGYS FYFKPHPGEY LNDFSIRELE KLKNIKEIKI INGLNFVPEY TIGMSSTMIY ELLNAGSKSF FLESNAKETF MMDDKEFKKY FRKNLKEIFF EILNKQL // ID Y106_METJA Reviewed; 238 AA. AC Q57570; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 97. DE RecName: Full=Uncharacterized protein MJ0106; GN OrderedLocusNames=MJ0106; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98088.1; -; Genomic_DNA. DR PIR; B64313; B64313. DR ProteinModelPortal; Q57570; -. DR STRING; 243232.MJ_0106; -. DR PRIDE; Q57570; -. DR DNASU; 1450947; -. DR EnsemblBacteria; AAB98088; AAB98088; MJ_0106. DR KEGG; mja:MJ_0106; -. DR eggNOG; arCOG00347; Archaea. DR eggNOG; COG1938; LUCA. DR InParanoid; Q57570; -. DR KO; K06869; -. DR OMA; ETVGIRP; -. DR PhylomeDB; Q57570; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004425; CHP00061. DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2. DR Pfam; PF09754; PAC2; 1. DR TIGRFAMs; TIGR00161; TIGR00161; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 238 Uncharacterized protein MJ0106. FT /FTId=PRO_0000106695. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. SQ SEQUENCE 238 AA; 26473 MW; CF30383FF83551DB CRC64; MVDSMKFVEK AKIEFENPIV IEAFPGTGLV GSIAGFQIIK DLNLKYFGYF EVDGILPLTT IEKGIPYPPV RAYANKDFII LFSDIIISPF KINGLAEFIV KTFSNKNPKL FVSLGGIMAG KSEKVFGIAN KEELIEDLKN YVEIFDFGVV GGMGGNLLIK CHDNGFDAIG LLAETVGIRP DPRGGANLLE VLNKMFNLNV NIENLIKEAE AIENKLKELA EQHLKMMSKS RKEYPMYI // ID Y1079_METJA Reviewed; 397 AA. AC Q58479; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ1079; GN OrderedLocusNames=MJ1079; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99076.1; -; Genomic_DNA. DR PIR; F64434; F64434. DR ProteinModelPortal; Q58479; -. DR STRING; 243232.MJ_1079; -. DR EnsemblBacteria; AAB99076; AAB99076; MJ_1079. DR KEGG; mja:MJ_1079; -. DR eggNOG; arCOG04469; Archaea. DR eggNOG; COG1784; LUCA. DR InParanoid; Q58479; -. DR KO; K08971; -. DR OMA; MALGVPD; -. DR PhylomeDB; Q58479; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002823; DUF112_TM. DR Pfam; PF01970; TctA; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 397 Uncharacterized protein MJ1079. FT /FTId=PRO_0000107160. FT TRANSMEM 2 24 Helical. {ECO:0000255}. FT TRANSMEM 44 66 Helical. {ECO:0000255}. FT TRANSMEM 92 114 Helical. {ECO:0000255}. FT TRANSMEM 124 143 Helical. {ECO:0000255}. FT TRANSMEM 150 169 Helical. {ECO:0000255}. FT TRANSMEM 173 195 Helical. {ECO:0000255}. FT TRANSMEM 255 277 Helical. {ECO:0000255}. FT TRANSMEM 297 319 Helical. {ECO:0000255}. FT TRANSMEM 331 350 Helical. {ECO:0000255}. FT TRANSMEM 354 373 Helical. {ECO:0000255}. SQ SEQUENCE 397 AA; 44268 MW; D6AC13687ED1FB54 CRC64; MLNLLYLILG IICGTITGLF PGIHPNNIVA LSFLILPYFG LDNYIPFLIG LVITHYFINF IPSAFLGVPD DETAVSALPM HKLTLNGNGY EAIVLAGFGS YLGVVFSILI SLFLMSILHF DVRAFYCSIK IFIPFILIAF ILYQIFTAKS VWEVLVIFLS GIFGIAVLYC SEAFNITLTA IFTGMFGIPL LINNLKTYKI KSQMMAFPDF ELKFLKSSFF ASVAGFFRIF LPGISGAQLN YILSKILNER DLKNFIVSQG SIILSNEVFS LLAVIFIGVG RSGVARAIQL LNANININTA IFSILISSTI AIIILLNLSK YILLFIRKVN FKFLSLFFII FCSLVVIIGS YNTYLIYHII VYLTAIYIGL LAVKSNTNLS NMMNVLIFPT ILYFLRG // ID Y1080_METJA Reviewed; 135 AA. AC Q58480; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1080; GN OrderedLocusNames=MJ1080; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99094.1; -; Genomic_DNA. DR PIR; G64434; G64434. DR STRING; 243232.MJ_1080; -. DR EnsemblBacteria; AAB99094; AAB99094; MJ_1080. DR KEGG; mja:MJ_1080; -. DR eggNOG; arCOG00563; Archaea. DR eggNOG; COG5427; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 135 Uncharacterized protein MJ1080. FT /FTId=PRO_0000107161. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT COMPBIAS 15 23 Leu-rich. SQ SEQUENCE 135 AA; 15437 MW; DDDFA77B995865FA CRC64; MEGKIMNIKH KIPILLLVLY IALGVFIQYN GISEFKSLPS PIYGGDYYYQ MGVIWHIRDG GNPLESSSMI GGMPGYLPLY AYLCAKFCDL LNLDTMKGIL YFSVVLFIMT SVIWFYLFRV LFKDDWVALI EVVLA // ID Y1128_METJA Reviewed; 308 AA. AC Q58528; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1128; DE Flags: Precursor; GN OrderedLocusNames=MJ1128; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99130.1; -; Genomic_DNA. DR PIR; G64440; G64440. DR ProteinModelPortal; Q58528; -. DR STRING; 243232.MJ_1128; -. DR DNASU; 1452024; -. DR EnsemblBacteria; AAB99130; AAB99130; MJ_1128. DR KEGG; mja:MJ_1128; -. DR eggNOG; arCOG07790; Archaea. DR eggNOG; ENOG410XQJ3; LUCA. DR OMA; CQAGCLK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:InterPro. DR GO; GO:0016857; F:racemase and epimerase activity, acting on carbohydrates and derivatives; IEA:InterPro. DR GO; GO:0006024; P:glycosaminoglycan biosynthetic process; IEA:InterPro. DR InterPro; IPR008928; 6-hairpin_glycosidase-like. DR InterPro; IPR010598; C5-epim. DR Pfam; PF06662; C5-epim_C; 1. DR SUPFAM; SSF48208; SSF48208; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 28 {ECO:0000255}. FT CHAIN 29 308 Uncharacterized protein MJ1128. FT /FTId=PRO_0000014008. SQ SEQUENCE 308 AA; 36443 MW; 48FCB2EB001B5091 CRC64; MILMKKFEII LFLFIAVLIF VFGYFVGASQ PLYSENPVIQ YFKNPKPFTV ENVNMPVTYY GTICGKYIGY QITPHNVNEE ARKCFYKYFK LKDKNPKEAE RYLKRGLFLT EYLISQADKE TAEVDEKNIT FIVWRYNFEF PLYNLSKGWR GALCQAGCLK TLYLAYEATG DERYLNYANL AINAFKVPVE KGGLLKIRIY KNKSYYWFPE YASENPPYVL NGFITATLWI GDFGNKTGNA DALYLYKEGL KSIKTFLPMY DAGDWSYYDA LGHRCNKHYE HLHRLQMLWL YNKTGDEIYL KYYKKWRE // ID Y1129_METJA Reviewed; 95 AA. AC Q58529; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1129; GN OrderedLocusNames=MJ1129; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99131.1; -; Genomic_DNA. DR PIR; H64440; H64440. DR ProteinModelPortal; Q58529; -. DR STRING; 243232.MJ_1129; -. DR EnsemblBacteria; AAB99131; AAB99131; MJ_1129. DR KEGG; mja:MJ_1129; -. DR eggNOG; arCOG01845; Archaea. DR eggNOG; COG2151; LUCA. DR InParanoid; Q58529; -. DR OMA; MSVMAMA; -. DR PhylomeDB; Q58529; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002744; DUF59. DR Pfam; PF01883; DUF59; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 95 Uncharacterized protein MJ1129. FT /FTId=PRO_0000107181. SQ SEQUENCE 95 AA; 10580 MW; 99AAA7B868562AD0 CRC64; MVTKEDVLNA LKTVADPHMG ISIVDMGLIR DVEVDDEGNV KFKLIPTNPY CMSVMAMAFQ AKEAVKSLEG VKKVEVTVEG HVMEKDINEM LKEKE // ID Y1133_METJA Reviewed; 421 AA. AC Q58533; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ1133; GN OrderedLocusNames=MJ1133; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UbiD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99135.1; -; Genomic_DNA. DR PIR; D64441; D64441. DR ProteinModelPortal; Q58533; -. DR STRING; 243232.MJ_1133; -. DR EnsemblBacteria; AAB99135; AAB99135; MJ_1133. DR KEGG; mja:MJ_1133; -. DR eggNOG; arCOG01671; Archaea. DR eggNOG; COG0043; LUCA. DR InParanoid; Q58533; -. DR OMA; MPQEPRI; -. DR PhylomeDB; Q58533; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016831; F:carboxy-lyase activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR InterPro; IPR002830; UbiD. DR Pfam; PF01977; UbiD; 1. DR SUPFAM; SSF50475; SSF50475; 1. DR TIGRFAMs; TIGR00148; TIGR00148; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 421 Uncharacterized protein MJ1133. FT /FTId=PRO_0000157383. SQ SEQUENCE 421 AA; 47215 MW; 867974520F489996 CRC64; MREIINKLNP IIIDKADKKF GVSRILKKYD GKPVYIKDVN GFEVVGNLCS RETLSKIFNV KKEDFIFFML DAMEKEKEGK LKINNKLKEK YIVEIPENIK NWPIPIYYEK DAGAYITSGV VVVYDKDYGY NLSIHRILVK DDYLVIRMVE QRHLHFLYNK ALKEKGYLDV AIVIGVHPAV LLAGSTSADI TFDELKFAAA LLGGEIGVFE LDNGLLVPEA EFIIEGKILP EVDDEGPFVD ITGTYDIVRK QPIIKIEKLY RKEKPIFHAL LPGGIEHKTL MGMPQEPRIL KGVRNTVPTV KNIVLTEGGC CWLHAVVQIE KRTEGDGKNA ILAAFASHPS LKHVIVVDDD INIFDINDVE YAIATRVQGD KDIVIISGAK GSSLDPSSDL KNKLTAKVGV DATMSLIKGR EHFERAKIPD K // ID Y1137_METJA Reviewed; 191 AA. AC Q58537; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 86. DE RecName: Full=Uncharacterized protein MJ1137; GN OrderedLocusNames=MJ1137; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99139.1; -; Genomic_DNA. DR PIR; H64441; H64441. DR ProteinModelPortal; Q58537; -. DR STRING; 243232.MJ_1137; -. DR EnsemblBacteria; AAB99139; AAB99139; MJ_1137. DR KEGG; mja:MJ_1137; -. DR eggNOG; arCOG01880; Archaea. DR eggNOG; COG0170; LUCA. DR InParanoid; Q58537; -. DR OMA; CKREKED; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR032974; Polypren_kinase. DR PANTHER; PTHR13205; PTHR13205; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 191 Uncharacterized protein MJ1137. FT /FTId=PRO_0000107184. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. SQ SEQUENCE 191 AA; 21688 MW; EB041414C9E41310 CRC64; MREIYRQTIH LVFGVLIAFS VLIFKKQLII PLIVSIVIGI CLYFLCKRYY IPIVSDLLNL CKREKEDGKG AIYFAIGMLI SLILIDDIKA VFFGILVFAV GDSLATIIGI RGKLKIKYFG KTVEGFLAFF ISASLILYPF YGTYGIFVAL ISAFIEFVSK KIRIDDNLYL PFIVAFIINH QINICSLMNF I // ID Y1152_METJA Reviewed; 73 AA. AC Q58552; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ1152; GN OrderedLocusNames=MJ1152; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99158.1; -; Genomic_DNA. DR PIR; G64443; G64443. DR STRING; 243232.MJ_1152; -. DR EnsemblBacteria; AAB99158; AAB99158; MJ_1152. DR KEGG; mja:MJ_1152; -. DR eggNOG; arCOG09567; Archaea. DR eggNOG; ENOG41110W1; LUCA. DR OMA; IESMGHE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 73 Uncharacterized protein MJ1152. FT /FTId=PRO_0000107190. SQ SEQUENCE 73 AA; 8760 MW; C7116019D1CE55E7 CRC64; MVIMKKHVKR IVKKYLGSKK AESEEEDILP DWIVKVKNEI ENITYEEYVK DVDKFFNEVK KKGIEKVLFD DIK // ID Y1163_METJA Reviewed; 217 AA. AC Q58563; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=UPF0173 metal-dependent hydrolase MJ1163 {ECO:0000255|HAMAP-Rule:MF_00457}; GN OrderedLocusNames=MJ1163; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0173 family. {ECO:0000255|HAMAP- CC Rule:MF_00457}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99165.1; -; Genomic_DNA. DR PIR; B64445; B64445. DR ProteinModelPortal; Q58563; -. DR STRING; 243232.MJ_1163; -. DR EnsemblBacteria; AAB99165; AAB99165; MJ_1163. DR KEGG; mja:MJ_1163; -. DR eggNOG; arCOG00497; Archaea. DR eggNOG; COG2220; LUCA. DR InParanoid; Q58563; -. DR OMA; IGMNIGG; -. DR PhylomeDB; Q58563; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-HAMAP. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_00457; UPF0173; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR022877; UPF0173. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 217 UPF0173 metal-dependent hydrolase MJ1163. FT /FTId=PRO_0000156393. SQ SEQUENCE 217 AA; 23516 MW; A2FE84E38D9BC616 CRC64; MITWYGHACF KVDNVLIDPF VPNPLCDLPY DEIMEGVEVI AVTHGHADHL GNAEELAKTY NVPVVTNHEI SVYLSERGVC AEGMNIGGTI EINGAKLTMV KAEHSSDISP TISGGVAAGF IINDRVYHAG DTGLFGDMEL IGEIYAPQIA LLPIGGRYTM GIDEALVAIE LIYPEIVIPM HYNTFPLIEV DVNEFVKKAE ALGVEVIVPK IGEPLEL // ID Y1178_METJA Reviewed; 351 AA. AC Q58577; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized glycosyltransferase MJ1178; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1178; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 4 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99181.1; -; Genomic_DNA. DR PIR; H64446; H64446. DR ProteinModelPortal; Q58577; -. DR STRING; 243232.MJ_1178; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAB99181; AAB99181; MJ_1178. DR KEGG; mja:MJ_1178; -. DR eggNOG; arCOG01403; Archaea. DR eggNOG; COG0438; LUCA. DR InParanoid; Q58577; -. DR OMA; YEENEYK; -. DR PhylomeDB; Q58577; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 351 Uncharacterized glycosyltransferase FT MJ1178. FT /FTId=PRO_0000080323. SQ SEQUENCE 351 AA; 39863 MW; 49998FDC44523FFA CRC64; MIIMKVLMPS IYYPYIGGIT LHVENLVKRL KDIEFHILTY DSYEENEYKN VIIHNVPHLK KFRGISYLIN AYKIGKNIIE SEGIDLIHSH YAFPQGCVGA LLKNKLSIPH ILTLHGSDAL ILKNSIKGRY FFKYATTNSD KIICVSKYIK NQLDENLKNR AIVIYNGVNK EILYNEGDYN FGLFVGAFVP QKGVDILIDA IKDIDFNFKL IGDGKLYKKI ENFVVKNNLS HIELLGRKSF DEVASFMRKC SFLVVPSRSE GFGMVAVEGM ACSKPVIATR VGGLGEIVID GYNGLLAEKN NPNDLKEKIL ELINNEELRK TLGENGKEFS KKFSWEKCVM GVRKVYEELS D // ID Y1189_METJA Reviewed; 283 AA. AC Q58589; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1189; GN OrderedLocusNames=MJ1189; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0233. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99198.1; -; Genomic_DNA. DR PIR; D64448; D64448. DR ProteinModelPortal; Q58589; -. DR EnsemblBacteria; AAB99198; AAB99198; MJ_1189. DR KEGG; mja:MJ_1189; -. DR eggNOG; arCOG02880; Archaea. DR eggNOG; ENOG410Z0NF; LUCA. DR OMA; MPFLQMF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR025098; DUF4013. DR Pfam; PF13197; DUF4013; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 283 Uncharacterized protein MJ1189. FT /FTId=PRO_0000107210. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 113 133 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 200 220 Helical. {ECO:0000255}. FT TRANSMEM 246 266 Helical. {ECO:0000255}. SQ SEQUENCE 283 AA; 31673 MW; 90D0EA63A28BE128 CRC64; MKKLEYYLKD AFYYVLSDVK KGIVGGLLSS TSGAIGAIFG IILSILLIHN INPNDVVGLD NNILLTSLIV ASFGFLIALI IGFILDGYYV RVMKTTVENY DVLPDWDDIA ELLKRGFLYW IGNIILSIIF MIVPILFIIF GVFLIFLPLV GIVFIGIGFL LLFVSTIALL IYEGLAEVNY SVKGFSGFFE FKEIFRMINL NYIILLIIVG VIVIVINFVV QLPFILLKIF AISPARYSTF SSSETIVDVI SAVISAFVGF YTAVFAKRAI ALYYKDRVEE LKK // ID Y1198_METJA Reviewed; 761 AA. AC Q58598; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Uncharacterized protein MJ1198; GN OrderedLocusNames=MJ1198; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 CR-type zinc finger. {ECO:0000255|PROSITE- CC ProRule:PRU00546}. CC -!- SIMILARITY: Contains 1 S1 motif domain. {ECO:0000255|PROSITE- CC ProRule:PRU00180}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99202.1; -; Genomic_DNA. DR PIR; E64449; E64449. DR PDB; 2K52; NMR; -; A=131-202. DR PDBsum; 2K52; -. DR ProteinModelPortal; Q58598; -. DR SMR; Q58598; 131-202. DR STRING; 243232.MJ_1198; -. DR EnsemblBacteria; AAB99202; AAB99202; MJ_1198. DR KEGG; mja:MJ_1198; -. DR eggNOG; arCOG00429; Archaea. DR eggNOG; COG1107; LUCA. DR InParanoid; Q58598; -. DR KO; K07463; -. DR OMA; GYGPDFA; -. DR PhylomeDB; Q58598; -. DR EvolutionaryTrace; Q58598; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR Gene3D; 2.10.230.10; -; 1. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR001305; HSP_DnaJ_Cys-rich_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR022967; S1_dom. DR InterPro; IPR003029; S1_domain. DR Pfam; PF00684; DnaJ_CXXCXGXG; 1. DR Pfam; PF00575; S1; 1. DR SMART; SM00316; S1; 1. DR SUPFAM; SSF50249; SSF50249; 2. DR SUPFAM; SSF57938; SSF57938; 1. DR PROSITE; PS50126; S1; 1. DR PROSITE; PS51188; ZF_CR; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Metal-binding; Reference proteome; KW Zinc; Zinc-finger. FT CHAIN 1 761 Uncharacterized protein MJ1198. FT /FTId=PRO_0000107211. FT DOMAIN 135 200 S1 motif. {ECO:0000255|PROSITE- FT ProRule:PRU00180}. FT ZN_FING 1 84 CR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00546}. FT STRAND 137 146 {ECO:0000244|PDB:2K52}. FT STRAND 149 155 {ECO:0000244|PDB:2K52}. FT STRAND 158 162 {ECO:0000244|PDB:2K52}. FT HELIX 164 166 {ECO:0000244|PDB:2K52}. FT HELIX 172 174 {ECO:0000244|PDB:2K52}. FT STRAND 180 188 {ECO:0000244|PDB:2K52}. FT TURN 190 192 {ECO:0000244|PDB:2K52}. FT STRAND 194 199 {ECO:0000244|PDB:2K52}. SQ SEQUENCE 761 AA; 85939 MW; FB8C3D16923E2E12 CRC64; MIVKCPICDG TGKKVVKYKT CPVCEGTGFI DEFSPKQHMK RVSKRATYDL DYGEIPCPKC KGTGKVPVYA KCDFCGGSGK VVKCDRCGAI IGKYPDFKDR TLCDKCLKEE EERKKGLRNV YVFDELATFY DVEPGKFYKG VVTRIEKYGA FINLNEQVRG LLRPRDMISL RLENLNVGDE IIVQAIDVRP EKREIDFKYI PLTTYDLVKY EKEVPLSQIK DISQNLVEMR DQVVHIRGEV VQIVQTPGPT VFTITDGTDF AWVAALEIAG LRAHPDVKVG DIVDVIGRVT IRDGRLQIER IKLQKLEGDE AEEIRKKIEE EIDRRAEPAK DIPFLVKSEV LERLRPKMAD VAKRIRKAVL DGRPIIIRHH ADTDGYCGGI ALEKAILPII DKFAIDVDAI WHFFKRRPSK APFYELEDVT KDLVFSIEDA LKFGQKLPLI VLIDNGSTDE DIPAISKAKA YGIEVIVIDH HFPGEVVDGK VEVDDYVDAH VNPYLVGGDS NLTAGVLGTE IARMINPDVE DEIKHIPGIA VVGDHAKGEE AEQYVKIALD RLNELSKKYG KGRTYDREYL EKIALCMDFE AFYLRFMDGK GIVDDILATN IKEFGRHEEL IDILYEQAMK MVERQMKAVI PALKTEFLEN GIILNTLDVE KYAHKFTFPA PGKTTGFAHD YIVQKYGEDK PIITLSYGPD FGVVRATDAV HEKYNFNLNL IVEQLMEEIP EASLDGGGHE CAGSLKFVEG LRDKVIGRFI EIIKNMKPKE Q // ID Y119_METJA Reviewed; 224 AA. AC Q57583; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0119; GN OrderedLocusNames=MJ0119; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 4Fe-4S domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98100.1; -; Genomic_DNA. DR PIR; G64314; G64314. DR ProteinModelPortal; Q57583; -. DR STRING; 243232.MJ_0119; -. DR EnsemblBacteria; AAB98100; AAB98100; MJ_0119. DR KEGG; mja:MJ_0119; -. DR eggNOG; arCOG00295; Archaea. DR eggNOG; COG2000; LUCA. DR KO; K06939; -. DR OMA; LLPGYNC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR InterPro; IPR007202; 4Fe-4S_dom. DR Pfam; PF04060; FeS; 1. DR PROSITE; PS51656; 4FE4S; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 224 Uncharacterized protein MJ0119. FT /FTId=PRO_0000106701. FT DOMAIN 9 68 4Fe-4S. SQ SEQUENCE 224 AA; 25680 MW; 572D7C9260859992 CRC64; MDSWNMKGSK MVDVNEITKY LPGFNCGACG YKRCDLFAEA LLNKDVKLED CPFLLRERFK ENYEKLKEIL KIKGKIKKEE KYIGVIDGYE ADFLLKPLPN ECSCRETLLI MDKKELKVGD YIRYRPLGCP IPHFAKIIDE YHGFYIIHVV GPSHRITGEK IEYKDVGIAI VVAFEGIVEG KVPEVGKTVK FIPKHCMMQK VHSGVVVQVE GKRVYIEGID LKVF // ID Y1210_METJA Reviewed; 258 AA. AC Q58607; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Uncharacterized protein MJ1210; GN OrderedLocusNames=MJ1210; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99213.1; -; Genomic_DNA. DR PIR; A64451; A64451. DR ProteinModelPortal; Q58607; -. DR STRING; 243232.MJ_1210; -. DR DNASU; 1452106; -. DR EnsemblBacteria; AAB99213; AAB99213; MJ_1210. DR KEGG; mja:MJ_1210; -. DR eggNOG; arCOG00348; Archaea. DR eggNOG; COG2047; LUCA. DR InParanoid; Q58607; -. DR KO; K07159; -. DR OMA; IWREDEG; -. DR PhylomeDB; Q58607; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004426; CHP00062. DR InterPro; IPR019151; Proteasome_assmbl_chaperone_2. DR Pfam; PF09754; PAC2; 1. DR TIGRFAMs; TIGR00162; TIGR00162; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 258 Uncharacterized protein MJ1210. FT /FTId=PRO_0000107214. FT TRANSMEM 163 187 Helical. {ECO:0000255}. SQ SEQUENCE 258 AA; 28708 MW; 62E71561D4950050 CRC64; MMFMVKIITR KVKDIEPLEN ALLIEGLPGI GHVGRLAAEH LVHEFKGEKF LELFCYDFPP QVLVKDDGTI EYMCAEFYAI REPKPMIVVL GNTQALSPIG QYHLAEEIVK IGIEYGANFV YTLGGFGVGK LCEEVKVYGA TTSKELAKKL KEHDILFRTD GGGIVGAAGL MLMFADLNGI PGICLMGETP GYLIDPNAAK AVLEKFCKLE NIEINMEELE KRAKGMEQFI EKIKKFEEEM LKAAQAKPPS EEDLRYIG // ID Y1227_METJA Reviewed; 240 AA. AC Q58624; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 98. DE RecName: Full=Putative glycyl-radical enzyme activating enzyme MJ1227 {ECO:0000305}; DE Short=GRE activating enzyme MJ1227 {ECO:0000305}; DE EC=1.97.1.- {ECO:0000305}; GN OrderedLocusNames=MJ1227; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0A9N4}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:P0A9N4}; CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99230.1; -; Genomic_DNA. DR PIR; B64453; B64453. DR ProteinModelPortal; Q58624; -. DR STRING; 243232.MJ_1227; -. DR DNASU; 1452123; -. DR EnsemblBacteria; AAB99230; AAB99230; MJ_1227. DR KEGG; mja:MJ_1227; -. DR eggNOG; arCOG00952; Archaea. DR eggNOG; COG1180; LUCA. DR InParanoid; Q58624; -. DR KO; K04069; -. DR OMA; CNFSCPF; -. DR PhylomeDB; Q58624; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR012840; NrdG2. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR TIGRFAMs; TIGR02495; NrdG2; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 240 Putative glycyl-radical enzyme activating FT enzyme MJ1227. FT /FTId=PRO_0000200545. FT REGION 35 37 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT REGION 126 128 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 29 29 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 33 33 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 36 36 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 71 71 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 240 AA; 27682 MW; 362C14E1F761E57A CRC64; MKALVSGIVD LSTIDYPKKA SAVIFLYGCN MKCPYCHNLK FMLEHKRGMT VEEIFNDIDF LFADAIVISG GEPTLQKDAV IEIARYAKEK GFPVKIDTNG THPEVIEELI KNKLIDYVAI DVKCRFDKYK EFVKCREDGE EIKNKILKII DLCKKNNVFV ECRTTFVPKV MDEEDIEDIA KTVKDCDLYA IQQFEPKDAY DEEFKKLPMP KENELRELGK IAKKYIDNVV IRTINGTFEI // ID Y1243_METJA Reviewed; 123 AA. AC Q58640; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=UPF0251 protein MJ1243; GN OrderedLocusNames=MJ1243; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0251 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99248.1; -; Genomic_DNA. DR PIR; B64455; B64455. DR ProteinModelPortal; Q58640; -. DR STRING; 243232.MJ_1243; -. DR EnsemblBacteria; AAB99248; AAB99248; MJ_1243. DR KEGG; mja:MJ_1243; -. DR eggNOG; arCOG02238; Archaea. DR eggNOG; COG1342; LUCA. DR InParanoid; Q58640; -. DR KO; K06933; -. DR OMA; KIRECGF; -. DR PhylomeDB; Q58640; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IEA:InterPro. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR HAMAP; MF_00674; UPF0251; 1. DR InterPro; IPR013324; RNA_pol_sigma_r3_r4. DR InterPro; IPR002852; UPF0251. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02001; DUF134; 1. DR SUPFAM; SSF88659; SSF88659; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 123 UPF0251 protein MJ1243. FT /FTId=PRO_0000147576. SQ SEQUENCE 123 AA; 14391 MW; 2DC553451B5E1F19 CRC64; MSRRGRPKIP RFISEEPKFR IFKPHGVSLT EVDKVILSVD ELEAIRLVDY LDYTQEEASK LMGISRRVLW SLLTEGRKKI ADALINGKAI VIEGGEYKIR ECGFCMRHRF GIKKHCRTWR EEL // ID Y129_METJA Reviewed; 170 AA. AC Q57593; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0129; GN OrderedLocusNames=MJ0129; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0554 and MJ0587. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98118.1; -; Genomic_DNA. DR PIR; A64316; A64316. DR ProteinModelPortal; Q57593; -. DR STRING; 243232.MJ_0129; -. DR DNASU; 1450971; -. DR EnsemblBacteria; AAB98118; AAB98118; MJ_0129. DR KEGG; mja:MJ_0129; -. DR PhylomeDB; Q57593; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 170 Uncharacterized protein MJ0129. FT /FTId=PRO_0000106707. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. SQ SEQUENCE 170 AA; 19621 MW; 4F3B62C7DDA89D9A CRC64; MLSFVVMSFL IFVIVMVNEH KAHLSVIQKM ILAVVNGSIT IILSIIVFYI FYPQNISLFL ITAGILTVFV FLYGLLLFLF GFTHRELSYL SKYDKYKFLC KFTIEMFSSL TNHAFLTISA IVLYQIQHPK PTIDFIVMIG MITISVIVVM LLFLKTYSII IKQLKKLENN // ID Y1305_METJA Reviewed; 147 AA. AC Q58701; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1305; GN OrderedLocusNames=MJ1305; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99327.1; -; Genomic_DNA. DR PIR; H64462; H64462. DR ProteinModelPortal; Q58701; -. DR STRING; 243232.MJ_1305; -. DR EnsemblBacteria; AAB99327; AAB99327; MJ_1305. DR KEGG; mja:MJ_1305; -. DR eggNOG; arCOG01202; Archaea. DR eggNOG; COG1708; LUCA. DR InParanoid; Q58701; -. DR KO; K07076; -. DR OMA; PIFIDEE; -. DR PhylomeDB; Q58701; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MJ1305. FT /FTId=PRO_0000107263. SQ SEQUENCE 147 AA; 17388 MW; 7E19C52F45D4065D CRC64; MDEKMLNNIL DEFLQKCKQK FGDDLISIIL FGSYARGTAV EYSDVDLLVI AKNLPKRRID RHKVLRDIVL EFIYRYGINI SPILVEPRDL SLKSINPLIC GILTGYKIIY DRDNFWKNYL ERIKPIIKRI KPIFIDEEKE WKIADLI // ID Y1307_METJA Reviewed; 262 AA. AC Q58703; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ1307; GN OrderedLocusNames=MJ1307; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99315.1; -; Genomic_DNA. DR PIR; B64463; B64463. DR ProteinModelPortal; Q58703; -. DR STRING; 243232.MJ_1307; -. DR EnsemblBacteria; AAB99315; AAB99315; MJ_1307. DR KEGG; mja:MJ_1307; -. DR eggNOG; arCOG03079; Archaea. DR eggNOG; COG2111; LUCA. DR InParanoid; Q58703; -. DR KO; K14118; -. DR OMA; SIVVNYR; -. DR PhylomeDB; Q58703; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007182; MnhB. DR Pfam; PF04039; MnhB; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 262 Uncharacterized protein MJ1307. FT /FTId=PRO_0000107265. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 179 199 Helical. {ECO:0000255}. FT TRANSMEM 216 236 Helical. {ECO:0000255}. SQ SEQUENCE 262 AA; 28591 MW; EBA52610F60F90AB CRC64; MNSKRDLAVA ISFFVFGASV LYSLAHMQIS PGVNEVYLTH YIIPNYVCAV IFDWRAYDTL GECLVLVVAV MVSWIVFGKS LYDNTYLKEL FHAPESDDYI TLQGWGEYTP IIKFLAFPMS VLMVALGIIT VLGGHITPGG GFQGGALIAA AFILSVIAFG SNSPLWFDHK FLEKLEALGA LGYLLLGVAG MFIGGYYLFN FTEINGFTIF PAPKEIITAG IIPYLNIAVG LKVLAGLSTA AFLLSCEKVI IEKISKSEEK LE // ID Y1309_METJA Reviewed; 481 AA. AC Q58705; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MJ1309; GN OrderedLocusNames=MJ1309; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99316.1; -; Genomic_DNA. DR PIR; D64463; D64463. DR ProteinModelPortal; Q58705; -. DR STRING; 243232.MJ_1309; -. DR DNASU; 1452211; -. DR EnsemblBacteria; AAB99316; AAB99316; MJ_1309. DR KEGG; mja:MJ_1309; -. DR eggNOG; arCOG01537; Archaea. DR eggNOG; COG0651; LUCA. DR InParanoid; Q58705; -. DR KO; K14115; -. DR OMA; PSVAFMV; -. DR PhylomeDB; Q58705; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR001750; ND/Mrp_mem. DR Pfam; PF00361; Proton_antipo_M; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 481 Uncharacterized protein MJ1309. FT /FTId=PRO_0000107267. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 264 284 Helical. {ECO:0000255}. FT TRANSMEM 303 323 Helical. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. FT TRANSMEM 400 420 Helical. {ECO:0000255}. FT TRANSMEM 443 463 Helical. {ECO:0000255}. SQ SEQUENCE 481 AA; 52543 MW; 1D04E5902DB25AE9 CRC64; MNYLPMMIVF PLIMAIIMNL LHGKEKAVKY ITFITAAILI ILPFISQYGY YYFGGHGVVN GWVSGIAYLY NPAKQAIIVT LSLIASLVLI TGMGEKLKNN MFVTLSLMGF ASIAAIVLAD DIFNLYVFFE IVSIVQAGLV FLSGTEEAYK AGLRYMIMGN VAAALMLLGI AFLLASTGTL NITDMKHYLL VDNPMIYGGL LLLIVGLAYG AGLPPFHNVK ADLYARSKGF ISAMLQTYSK FVLVGLMIII LKLFNGLDYF ASAHAVLIAL GVLAMVFGVV MALLQSDYKK LLAYHAISQG GYVATGLALG TPLGIVAGIF HAINHVIYKS ALFLGAYIVS CKRGSNLHKL GGLLPLMPSV AFMVLCAKLA ISGIPPFNGF QSKWMLAQAA MQVNMPEIAI IMIIVSIGTF VSMMKAFYLI YLKPVDEETL KEYQNKEVPK LAVFSLFVLT ALCIIIGLYP DIVTNYLWDY AKELGVNYYL K // ID Y1318_METJA Reviewed; 602 AA. AC Q58714; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized protein MJ1318; GN OrderedLocusNames=MJ1318; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase S16 family. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. CC -!- SIMILARITY: Contains 1 Lon proteolytic domain. CC {ECO:0000255|PROSITE-ProRule:PRU01122}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99325.1; -; Genomic_DNA. DR PIR; E64464; E64464. DR ProteinModelPortal; Q58714; -. DR STRING; 243232.MJ_1318; -. DR MEROPS; S16.A12; -. DR EnsemblBacteria; AAB99325; AAB99325; MJ_1318. DR KEGG; mja:MJ_1318; -. DR eggNOG; arCOG01937; Archaea. DR eggNOG; COG1750; LUCA. DR InParanoid; Q58714; -. DR KO; K06870; -. DR OMA; DMQASAR; -. DR PhylomeDB; Q58714; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0004176; F:ATP-dependent peptidase activity; IEA:InterPro. DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro. DR GO; GO:0030163; P:protein catabolic process; IEA:InterPro. DR Gene3D; 3.30.230.10; -; 1. DR InterPro; IPR027065; Lon_Prtase. DR InterPro; IPR008269; Pept_S16_C. DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold. DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr. DR PANTHER; PTHR10046; PTHR10046; 1. DR Pfam; PF05362; Lon_C; 1. DR SUPFAM; SSF54211; SSF54211; 1. DR PROSITE; PS51786; LON_PROTEOLYTIC; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 602 Uncharacterized protein MJ1318. FT /FTId=PRO_0000107273. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 103 123 Helical. {ECO:0000255}. FT TRANSMEM 577 597 Helical. {ECO:0000255}. FT DOMAIN 25 210 Lon proteolytic. {ECO:0000255|PROSITE- FT ProRule:PRU01122}. FT ACT_SITE 110 110 {ECO:0000255|PROSITE-ProRule:PRU01122}. FT ACT_SITE 153 153 {ECO:0000255|PROSITE-ProRule:PRU01122}. SQ SEQUENCE 602 AA; 67257 MW; A5FBE1C388160AA3 CRC64; MKTWRENMKK ILTLLLITFL LNSAFAVIIK APAVSLTDRG YVGVPINIQI NVTKGDGHVF MDTMPLTELD MQGSARIAAK VAGEVTGKDM SKYNVYITVR SDVPVVGGPS AGGTMTIGII CELMNWSLNK HVMMTGTINP DGSIGPVGGI LEKIEAAKKA NCTIMLIPKG QRYVEVEGNK VDAVEFGKKL GIKVIEVGSI YEAIPYFTNK KIIMKEYPEN PLIEEKYKDI MKELSENVLK TANEKYENLS KELSNSYVGY EYQKALLNEL TTSKSLLEKA NDEYLKNKYY SATCSAFNAL IKLETIEHTL KYLTGEEDVK TFLTEVQNKI SHDKEIVYSK NVTTNNFEEI LAGRIRIAEA EKLLDNAWKS YYLGNYDEAI KYGSFAKLRG DSAIWWVSLK ENDNNGKIIN EAKLKSLAQQ YLDNAETILT YVETLFPNLP TDDLENDLES AKEAYKDGDY LLTIAESIDT CVKAEIPLVI FGDIEYSKKY ARNKINLAEN LGITPISALG YYEYANSLND TISKIMYYKY SSYYAQMDID VIKELNKSIS ENISSEINIV TNENVNIEET TTKENNVGIM ISAIIGGLIG FAGGYLARRV SA // ID Y1326_METJA Reviewed; 391 AA. AC Q58722; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized GTP-binding protein MJ1326; GN OrderedLocusNames=MJ1326; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. {ECO:0000255|PROSITE- CC ProRule:PRU01047}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01047}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99336.1; -; Genomic_DNA. DR PIR; E64465; E64465. DR ProteinModelPortal; Q58722; -. DR STRING; 243232.MJ_1326; -. DR EnsemblBacteria; AAB99336; AAB99336; MJ_1326. DR KEGG; mja:MJ_1326; -. DR eggNOG; arCOG00358; Archaea. DR eggNOG; COG1163; LUCA. DR InParanoid; Q58722; -. DR KO; K06944; -. DR OMA; AAWLKVM; -. DR PhylomeDB; Q58722; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR Gene3D; 3.10.20.30; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR031662; GTP-binding_2. DR InterPro; IPR006074; GTP1-OBG_CS. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR004095; TGS. DR Pfam; PF01926; MMR_HSR1; 1. DR Pfam; PF16897; MMR_HSR1_Xtn; 1. DR Pfam; PF02824; TGS; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51710; G_OBG; 1. DR PROSITE; PS00905; GTP1_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 391 Uncharacterized GTP-binding protein FT MJ1326. FT /FTId=PRO_0000205445. FT DOMAIN 85 314 OBG-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 91 98 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 137 141 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 267 270 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT COMPBIAS 69 76 Poly-Gly. SQ SEQUENCE 391 AA; 43649 MW; 1926F930A16FDD96 CRC64; MLFLLSLKRI FIFRNHKFNI VGDVMGIEEE IRRIEEELKK TPYNKATQKH IGRLKAKLAK LREQAQSRGG GGGGKGYAVK KSGDATAAFV GFPSVGKSTL LNKLTNAKSE VGAYAFTTLT IVPGILEYKG AKIQLLDAPG IIVGASSGKG RGTEVLSAVR SADLILLTVD IYTLDHLPVL EKELYNVGIR LDQTPPDVKI KVKERGGINV SSTVPLTHID EDTIEAILNE YRIHNADVVI REDITLEQFI DVVAGNRVYI PSLVVVNKID LADEEYLKYI KQKLEEFGKD YILVSGNKGI NLDLLKEKIY EKLGFIKIYL KPQGKKPDFD EPLIMRRGAT VKDVCEKLHK DFVRNFRYAQ VWGKSAKHPG QRVGLDHKLE DGDILTIVIK R // ID Y132_METJA Reviewed; 220 AA. AC Q57596; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0132; GN OrderedLocusNames=MJ0132; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the N4/N6-methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98113.1; -; Genomic_DNA. DR PIR; D64316; D64316. DR ProteinModelPortal; Q57596; -. DR STRING; 243232.MJ_0132; -. DR REBASE; 3902; M.MjaORF132P. DR EnsemblBacteria; AAB98113; AAB98113; MJ_0132. DR KEGG; mja:MJ_0132; -. DR eggNOG; arCOG02632; Archaea. DR eggNOG; COG0286; LUCA. DR KO; K03427; -. DR OMA; IDASNEY; -. DR PhylomeDB; Q57596; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0006306; P:DNA methylation; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 220 Uncharacterized protein MJ0132. FT /FTId=PRO_0000106710. SQ SEQUENCE 220 AA; 25767 MW; 710DDAE4C7A47954 CRC64; MDGYNEDVLK ENPDVRRIYN TFVRGGYPPK QSADWAWVQL MLYFARKKVG IVLDSGALFR GGKEKKIRKE IVEKDLIEAI ILLPEKLFYN VTAPGIVMIL NKNKPEERKG KILFINASLE FEKHPEVRRL NRLGEENIDK IVDVYENWED IEGFSRVVDL EEIRKNDYNL NVSLYVFPVE EKEDIDLRKE LEEFKEIEKK EKEVLDEVIG YVEGILRAGS // ID Y1342_METJA Reviewed; 114 AA. AC Q58738; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1342; GN OrderedLocusNames=MJ1342; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99359.1; -; Genomic_DNA. DR PIR; E64467; E64467. DR EnsemblBacteria; AAB99359; AAB99359; MJ_1342. DR KEGG; mja:MJ_1342; -. DR eggNOG; arCOG07626; Archaea. DR eggNOG; ENOG410Y55T; LUCA. DR OMA; EIPGSAC; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJ1342. FT /FTId=PRO_0000107286. SQ SEQUENCE 114 AA; 13134 MW; 73DB2C0F38AA616A CRC64; MLWVLGGKKI AKCLKETVNP KEIEDKELIK FLINFCDMCN DFVIDDEKIG IKIDKCKYCP KQIGEAEIPG SACPIPSILA SCMRELTKKD YKINLWDGNK VIIKENGYCW FRIK // ID Y1354_METJA Reviewed; 145 AA. AC Q58749; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1354; GN OrderedLocusNames=MJ1354; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99366.1; -; Genomic_DNA. DR PIR; A64469; A64469. DR STRING; 243232.MJ_1354; -. DR EnsemblBacteria; AAB99366; AAB99366; MJ_1354. DR KEGG; mja:MJ_1354; -. DR eggNOG; arCOG09680; Archaea. DR eggNOG; ENOG41111B6; LUCA. DR OMA; VGYMVLF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 145 Uncharacterized protein MJ1354. FT /FTId=PRO_0000107293. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 83 103 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. SQ SEQUENCE 145 AA; 16713 MW; 15EFEE71C5262B37 CRC64; MDVGIILGIL SAMGFLVFLG IGGHILIGYE IIRKISKAYE KGEDVKELEN KIINKSHLTN TLEKITTFTL TSIFLFEMEK YRYVIDVGYS ILFLVTLTLY LVPNLSLLVW VTFFGATVFM IMLWILRFRA IKEFNKAFIE ELTTQ // ID Y1355_METJA Reviewed; 571 AA. AC Q58750; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1355; GN OrderedLocusNames=MJ1355; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99364.1; -; Genomic_DNA. DR PIR; B64469; B64469. DR ProteinModelPortal; Q58750; -. DR STRING; 243232.MJ_1355; -. DR EnsemblBacteria; AAB99364; AAB99364; MJ_1355. DR KEGG; mja:MJ_1355; -. DR eggNOG; arCOG05079; Archaea. DR eggNOG; COG1542; LUCA. DR InParanoid; Q58750; -. DR KO; K09010; -. DR OMA; YIHRDEL; -. DR PhylomeDB; Q58750; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007548; DUF505. DR Pfam; PF04458; DUF505; 2. DR PIRSF; PIRSF029056; DUF505; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 571 Uncharacterized protein MJ1355. FT /FTId=PRO_0000107294. SQ SEQUENCE 571 AA; 65700 MW; 72DFE8C090E14C62 CRC64; MFLKKRHLEI LKKMKETEMQ NEIEKALPEE FKTRALELFI LGFAELKGDK IIFTEAGKKL MEIVDKIDLE KIPDIFVDSE IIKIMELLEE TGNVPEDWML MLKERFLADE NGLTEIGKEI LKIYRETHPV VYLTPELLAF IKDMPKIGVY DELITYKNTK EYGDNIINAL QAMRLLLISP KTESGKAFST TKALNYVLKV ASLVPNLSRA LILRKEDFEI LERGETTEEM TESGFYAEGK VTELGQAMMD TYKEMGKVEE KTLPIYVLED EIKVLKAIEE IKEKYETNPE IIPTYDEIKK RTNIDDLGAV LHTLESKELI KREVVKNKDT YWMTEFGEKV KDLGEVSTDG MKAITYPESG DVPIAEWVIK GKEEGTVKRG ITEKGKYLIK LSKTIKRKPY LTKYDISTLI KIPRKRYIHR DELVKLIQGH VGGDEKEIIK SLGEAESKGF IKELQNKMIK LTELGEEVKT AIEMAKIQEL LATKFAVTPT TFNILKTIYD HKEEFDKVWK EKSEGKEHKE NEIVLLAKYL SLTPEEIKKN LVILKNVGFI GKKGLTDAGV KLVEAYLNFY Q // ID Y1379_METJA Reviewed; 100 AA. AC Q58774; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1379; GN OrderedLocusNames=MJ1379; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99389.1; -; Genomic_DNA. DR PIR; B64472; B64472. DR ProteinModelPortal; Q58774; -. DR STRING; 243232.MJ_1379; -. DR EnsemblBacteria; AAB99389; AAB99389; MJ_1379. DR KEGG; mja:MJ_1379; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q58774; -. DR KO; K07075; -. DR OMA; ENNYPSF; -. DR PhylomeDB; Q58774; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MJ1379. FT /FTId=PRO_0000107304. SQ SEQUENCE 100 AA; 11819 MW; E20512C0CFE1019F CRC64; MKTLSEIKEI LRKHKKILKD KYKVKSIALF GSYARGEQTE ESDIDIMVEF DENNYPSFSE YLELIEYLEK ILGLKVDLIT KKSIHNPYVK KSIEEDLIYV // ID Y1389_METJA Reviewed; 134 AA. AC Q58784; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1389; GN OrderedLocusNames=MJ1389; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99400.1; -; Genomic_DNA. DR PIR; D64473; D64473. DR ProteinModelPortal; Q58784; -. DR STRING; 243232.MJ_1389; -. DR EnsemblBacteria; AAB99400; AAB99400; MJ_1389. DR KEGG; mja:MJ_1389; -. DR eggNOG; arCOG02603; Archaea. DR eggNOG; COG2018; LUCA. DR KO; K07131; -. DR OMA; SEMLYKR; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 134 Uncharacterized protein MJ1389. FT /FTId=PRO_0000107306. SQ SEQUENCE 134 AA; 15253 MW; 0620AE6F7AA49E35 CRC64; MKATENRKVN EINEILLPLS KNLKNVEGFV IVSKDSLVKV GNIDGEDLEI ISRHMAVVMG SSEMLYKRFN DEVEYIEIKG KKHKIILYNL DDFIFAVVGN IKADEIKDKV MELKFKVNNI DGLTAENIIE EIAL // ID Y138_METJA Reviewed; 482 AA. AC Q57602; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 78. DE RecName: Full=Putative glutamine amidotransferase-like protein MJ0138; GN OrderedLocusNames=MJ0138; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00605}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98121.1; -; Genomic_DNA. DR PIR; B64317; B64317. DR ProteinModelPortal; Q57602; -. DR STRING; 243232.MJ_0138; -. DR DNASU; 1450979; -. DR EnsemblBacteria; AAB98121; AAB98121; MJ_0138. DR KEGG; mja:MJ_0138; -. DR eggNOG; arCOG00107; Archaea. DR eggNOG; COG1492; LUCA. DR OMA; EGVMGAF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:1903600; C:glutaminase complex; IBA:GO_Central. DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0042823; P:pyridoxal phosphate biosynthetic process; IBA:GO_Central. DR GO; GO:0008614; P:pyridoxine metabolic process; IBA:GO_Central. DR GO; GO:0042819; P:vitamin B6 biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR017926; GATASE. DR InterPro; IPR011698; GATase_3. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF07685; GATase_3; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51273; GATASE_TYPE_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Reference proteome; KW Transferase. FT CHAIN 1 482 Putative glutamine amidotransferase-like FT protein MJ0138. FT /FTId=PRO_0000106714. FT DOMAIN 1 203 Glutamine amidotransferase type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00605}. SQ SEQUENCE 482 AA; 54464 MW; 60598EEE7C120409 CRC64; MEIGILDIKG SLPLFEDFGN LPTKIITENN YKEIKDLDAL IIPGGSLIES KSLNDDLKKE IINFNGYIIG ICSGFQILAK KIDIGRKSSV PIIKEGLGLL DVEFSPLVCT DRVEFEVKKS IFGEGKGEGF HCHTYGNIEV VDKETKILTV SKVKKLNYKL GAEKEIISGA FKGKVFGTMV HNFLDNEFVR DNFLKHLGVT EDEKEEIFEK NKIIKDELKK RALKYRLNPK LLKENNKKDV NKKRGIILLA TSSNSGKTFL TTALSSKLNG RVFVAKIGGD VRDIVPALYL LREKMTKYNS IKIGERGWVD VSKFLDYIKK SDYDYIIVEG VMGAFTAALK NISSYQIAKK LGFPVYIVSA CNISGIEGAF VEAMAYYSLL KDIGIKVEGV ILNKVYDWNS FNKLKSLAEK HNIKLYGVGK IANESRGLIP EVEIDYESFC RNAFNVDLEI EIPEVEINNH IKDEEDNFLE RLDNWMENIN KY // ID Y1395_METJA Reviewed; 132 AA. AC Q58790; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1395; GN OrderedLocusNames=MJ1395; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99405.1; -; Genomic_DNA. DR PIR; B64474; B64474. DR ProteinModelPortal; Q58790; -. DR STRING; 243232.MJ_1395; -. DR EnsemblBacteria; AAB99405; AAB99405; MJ_1395. DR KEGG; mja:MJ_1395; -. DR eggNOG; arCOG07532; Archaea. DR eggNOG; ENOG4111VJ8; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 132 Uncharacterized protein MJ1395. FT /FTId=PRO_0000107310. FT TRANSMEM 105 125 Helical. {ECO:0000255}. SQ SEQUENCE 132 AA; 15215 MW; FB202241F54A7318 CRC64; MDVNVSYKDT YSVITYQVWE PIDGGKNITL IIEYDADIVD NGILFKTVSI PIGGDLNIKN FHINFVSPYY LTYQEPDGNN FQIPKKTLLI INAEFSILPL PKLPVHGYVV FWLSILCILI IIFVYTELRR KK // ID Y142_METJA Reviewed; 147 AA. AC Q57607; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0332 protein MJ0142; GN OrderedLocusNames=MJ0142; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0332 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98125.1; -; Genomic_DNA. DR PIR; G64317; G64317. DR ProteinModelPortal; Q57607; -. DR STRING; 243232.MJ_0142; -. DR EnsemblBacteria; AAB98125; AAB98125; MJ_0142. DR KEGG; mja:MJ_0142; -. DR eggNOG; arCOG02123; Archaea. DR eggNOG; COG1895; LUCA. DR InParanoid; Q57607; -. DR OMA; YYTMFYC; -. DR PhylomeDB; Q57607; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007842; HEPN_dom. DR Pfam; PF05168; HEPN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 147 UPF0332 protein MJ0142. FT /FTId=PRO_0000159639. SQ SEQUENCE 147 AA; 17592 MW; 707D67BF058E065C CRC64; MRLKIMELRY KRELEKLIEK AEKSLEASEN LYNSEFYDFA VSRIYYSMFY CVKALLLTKE INPKKHSGVL KMFAKEFIKT NELDVELFEY INEAYNYRQT ADYDATIEIK KEEAEYLLHK GHIFLNKTKK YLISKNILKG ENDNTKS // ID Y1434_METJA Reviewed; 220 AA. AC Q58829; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Putative endonuclease MJ1434; GN OrderedLocusNames=MJ1434; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the Nth/MutY family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99444.1; -; Genomic_DNA. DR PIR; A64479; A64479. DR ProteinModelPortal; Q58829; -. DR STRING; 243232.MJ_1434; -. DR EnsemblBacteria; AAB99444; AAB99444; MJ_1434. DR KEGG; mja:MJ_1434; -. DR eggNOG; arCOG00461; Archaea. DR eggNOG; COG2231; LUCA. DR InParanoid; Q58829; -. DR KO; K07457; -. DR OMA; WWPADTP; -. DR PhylomeDB; Q58829; -. DR BRENDA; 3.2.2.27; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006284; P:base-excision repair; IEA:InterPro. DR Gene3D; 1.10.1670.10; -; 1. DR Gene3D; 1.10.340.30; -; 1. DR InterPro; IPR011257; DNA_glycosylase. DR InterPro; IPR003651; Endouclease3_FeS-loop_motif. DR InterPro; IPR003265; HhH-GPD_domain. DR InterPro; IPR023170; HTH_base_excis_C. DR InterPro; IPR005759; Nth. DR Pfam; PF00730; HhH-GPD; 1. DR PIRSF; PIRSF001435; Nth; 1. DR SMART; SM00478; ENDO3c; 1. DR SMART; SM00525; FES; 1. DR SUPFAM; SSF48150; SSF48150; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 220 Putative endonuclease MJ1434. FT /FTId=PRO_0000102244. FT METAL 202 202 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 208 208 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 211 211 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 217 217 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 220 AA; 25938 MW; BB3188BE152995F6 CRC64; MKENKFEMIY KIYKILLDYY GHQNWWPAET RYEVVVGAIL TQNTSWKNVE RAINNLKMED LLEEVKILNV DEDKLKELIR PAGFYNLKAK RLKNVTKFIV ENYGNTEEMA KTDKDTLILR AELLSINGVG KETADSILLY ALDRESFVVD AYTKRMFSRL GVINEKAKYD EIKEIFEKNL PKDLEIYKEY HALIVEHCKK FCRKKALCDN CPIKEFCLSK // ID Y1443_METJA Reviewed; 110 AA. AC Q58838; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=UPF0132 membrane protein MJ1443; GN OrderedLocusNames=MJ1443; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0132 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99453.1; -; Genomic_DNA. DR PIR; B64480; B64480. DR ProteinModelPortal; Q58838; -. DR STRING; 243232.MJ_1443; -. DR EnsemblBacteria; AAB99453; AAB99453; MJ_1443. DR KEGG; mja:MJ_1443; -. DR eggNOG; arCOG04344; Archaea. DR eggNOG; COG4818; LUCA. DR InParanoid; Q58838; -. DR OMA; FVKFHAM; -. DR PhylomeDB; Q58838; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 110 UPF0132 membrane protein MJ1443. FT /FTId=PRO_0000158602. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. SQ SEQUENCE 110 AA; 12411 MW; 0D162443D7741796 CRC64; MIFMGKTSLG LDENIEGALC YLFGVITGIL FYILEKESKF VKFHAVQSII LFGGLWVLSI ILAFIPYGWM LSGLVNLAAF ILWIVCMYKA YKGEKFKLPV IGDIAEQYSQ // ID Y1462_METJA Reviewed; 83 AA. AC Q58857; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1462; GN OrderedLocusNames=MJ1462; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99476.1; -; Genomic_DNA. DR PIR; E64482; E64482. DR STRING; 243232.MJ_1462; -. DR EnsemblBacteria; AAB99476; AAB99476; MJ_1462. DR KEGG; mja:MJ_1462; -. DR eggNOG; arCOG08274; Archaea. DR eggNOG; ENOG410YYSA; LUCA. DR OMA; ARGDILS; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 83 Uncharacterized protein MJ1462. FT /FTId=PRO_0000107351. SQ SEQUENCE 83 AA; 9511 MW; F1BD6B842BA834CD CRC64; MMIYGILLNI PEKHATKYED LIRRIIGEGI ARGDILSFTE ARYKGDVAFV MLARSRRAAE KVYQQLKEHP IHVKVIEIEG KGD // ID Y1468_METJA Reviewed; 1009 AA. AC Q58863; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein MJ1468; GN OrderedLocusNames=MJ1468; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 5 PKD domains. {ECO:0000255|PROSITE- CC ProRule:PRU00151}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99478.1; -; Genomic_DNA. DR PIR; C64483; C64483. DR ProteinModelPortal; Q58863; -. DR STRING; 243232.MJ_1468; -. DR EnsemblBacteria; AAB99478; AAB99478; MJ_1468. DR KEGG; mja:MJ_1468; -. DR eggNOG; arCOG02508; Archaea. DR eggNOG; arCOG03991; Archaea. DR eggNOG; COG3291; LUCA. DR InParanoid; Q58863; -. DR OMA; WCGYLNN; -. DR PhylomeDB; Q58863; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 2.60.40.670; -; 5. DR InterPro; IPR026495; PIP_CTERM. DR InterPro; IPR022409; PKD/Chitinase_dom. DR InterPro; IPR000601; PKD_dom. DR Pfam; PF00801; PKD; 3. DR SMART; SM00089; PKD; 7. DR SUPFAM; SSF49299; SSF49299; 5. DR TIGRFAMs; TIGR04173; PIP_CTERM; 1. DR PROSITE; PS50093; PKD; 5. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Repeat; Transmembrane; Transmembrane helix. FT CHAIN 1 1009 Uncharacterized protein MJ1468. FT /FTId=PRO_0000107354. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 985 1005 Helical. {ECO:0000255}. FT DOMAIN 213 247 PKD 1. {ECO:0000255|PROSITE- FT ProRule:PRU00151}. FT DOMAIN 436 503 PKD 2. {ECO:0000255|PROSITE- FT ProRule:PRU00151}. FT DOMAIN 724 806 PKD 3. {ECO:0000255|PROSITE- FT ProRule:PRU00151}. FT DOMAIN 822 886 PKD 4. {ECO:0000255|PROSITE- FT ProRule:PRU00151}. FT DOMAIN 925 962 PKD 5. {ECO:0000255|PROSITE- FT ProRule:PRU00151}. FT COMPBIAS 293 298 Poly-Asn. SQ SEQUENCE 1009 AA; 115120 MW; 13E9B4933EAB7972 CRC64; MKLLKILMPL IILGIISIVN GYVIVIHPNT MNITNSSGVY NTDPNIIAYN VNDTITFEAL APDSVAQDIL DNGVVKWDFG DLTETDYGNY RTTTHTYTFP FPYPVAWCGY LNNTGYSKAL TYNWLVVGDV ANTKYVFNGS PLNSKTSWEV YYNSTNNTVI IKYYSETPVD REFNGLSVDT TSVTVNVSRD EIVEGDTVKF NFSVSRNIIF CVWSFGDGTF SFEKFPEHTY TKSGLYYPRV LVVDDSGRVM VGYLDEGIEV KRARGGYIYW VTGPSHYDGE AYTYVYNSSG DDNNNNGNAY TDPYKITYKV NDTIKFEMSG AWGEYWKWDF GDGTETPYTY KSYFTPSYHQ YKFPFMWPFF WMSYGWGSWW KSDTLNFIVV DDVENTRYNF YPSSAHDKTY YDYEYNKENH TVNLYYYSDV ISTPKFNVKL RDGYYIDITA TADKTQVSVN ENVRFDCSPY GNPIFIMWCF GDGTCSFEKS PTHRYSSSGL YYPHVFVIDD NGNIEVGIPP PIGVGGYSSY PQIYASPTIA PTYYPINITI VEPASWTWYW HHIYFGDGGS VWIKPKKSPY TFTHTYTSEG VYPIYMKVYT AENMKTVYVI DNKNPIAKLY IYPNPASYKD TISFSPINSY DPDANRMIPE YNYYGTLIGY YPISPNSPMA RIYGFNLTVY DSNGNVAWNY SSNELTIISK SFPIGNYTAK LVVWDGMGGV NSTTVKFSVI NRPPVAQFIY YPDKPEPNED VEFVSQSYDP EGEIAYYIWN FGDGTVINTT DTIVHHKYER PGYYTVTLTV FDKYNASSSI SKQIVVGGIL ANFTYEIINE NTVRFEDTSV VAPGKIISWH WDFGDGSTST EQNPIHTYSK EGAYFVTLTV KSDTNLTDSV TKIVIISPPP KYPPVADFTY KVINGTTVEF NANLSYDEDG YIKYYIWDFG DGTPANTTTN PIIIHKYKKE GVYPVTLTVI DNDNLSDSRT KLINIGESFI HSVPIPPYIE ILIVISTIFC FFQIIRGLK // ID Y147_METJA Reviewed; 371 AA. AC Q57611; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Uncharacterized ATP-binding protein MJ0147; GN OrderedLocusNames=MJ0147; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98139.1; -; Genomic_DNA. DR PIR; D64318; D64318. DR ProteinModelPortal; Q57611; -. DR SMR; Q57611; 269-368. DR STRING; 243232.MJ_0147; -. DR DNASU; 1450991; -. DR EnsemblBacteria; AAB98139; AAB98139; MJ_0147. DR KEGG; mja:MJ_0147; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q57611; -. DR KO; K06921; -. DR OMA; DEMRYKE; -. DR PhylomeDB; Q57611; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 371 Uncharacterized ATP-binding protein FT MJ0147. FT /FTId=PRO_0000184667. FT NP_BIND 33 40 ATP. {ECO:0000255}. SQ SEQUENCE 371 AA; 43859 MW; 088E8FC7D414F8BE CRC64; MVIQMKFFNR EKEIHEILSI LEGEPNIIYF IYGPLNSGKT ALIKHIIENK LSDDYKVFYI NFRTYLISEK REFIEAIFTT KKDDFFEKIK DKSEVLNLIT KGAKILTGIP IPEVEFDKLF EEKINDAFQY LNSILLEVKK SGKQPVLILD ELQMIKDVVL NWQKYLLKEL FQFLVSLTKE QHLCHVFCLS SDSLFIEYVY SAGELEGRAK YLLVDDFDKE TALKFMDFLA KEILNKKLSD EDKELIYNYV GGKPVYIYSV IDEMRYRKLE DILNLMLKEE TQKLKYFLKE LDYIKPKVEL KDEIIEIKKD DIINALKLFK ENYEVSDDDI PEPVYIYLVK KNILFLNPIE GILKPQSFLI WNAIKKLLNG H // ID Y1487_METJA Reviewed; 426 AA. AC Q58882; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Uncharacterized methyltransferase MJ1487; DE EC=2.1.1.-; GN OrderedLocusNames=MJ1487; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 B12-binding domain. {ECO:0000255|PROSITE- CC ProRule:PRU00666}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99497.1; -; Genomic_DNA. DR PIR; F64485; F64485. DR ProteinModelPortal; Q58882; -. DR STRING; 243232.MJ_1487; -. DR EnsemblBacteria; AAB99497; AAB99497; MJ_1487. DR KEGG; mja:MJ_1487; -. DR eggNOG; arCOG01356; Archaea. DR eggNOG; COG1032; LUCA. DR InParanoid; Q58882; -. DR OMA; DFIFGFP; -. DR PhylomeDB; Q58882; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR023980; CHP04013_B12-bd/rSAM. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04013; B12_SAM_MJ_1487; 1. DR PROSITE; PS51332; B12_BINDING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Methyltransferase; Reference proteome; S-adenosyl-L-methionine; KW Transferase. FT CHAIN 1 426 Uncharacterized methyltransferase MJ1487. FT /FTId=PRO_0000107371. FT DOMAIN 1 137 B12-binding. {ECO:0000255|PROSITE- FT ProRule:PRU00666}. FT METAL 183 183 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 187 187 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 190 190 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 426 AA; 48962 MW; 44C59FD3C9397351 CRC64; MEENTALVVY YTKLHKNSFN ALIGALEIDE YFDNLPIYFA NKKDIFNLKE VLKKYDKVVI AISFFTTELW KTYELINELK AKYQSYRNKI IYLAGGPHPT GDPKGTLKLG FDVVCIGEGE ETFPEFIKAV NEDEDYKKVK GIAYLNDNEF IYTGRRKPVD LNKYPPFPVK HNKFGHIEIT RGCPYKCYFC QTPRIFGKKI RHRDVENIYK YVEIMAERNL KDIRFITPNA FGYGSKDGKT LNIDKIEKLL ESIREILGNN GRIFFGTFPS EVRPEHVNIE TVDLILRYAD NKNLVIGAQS GSEKVLELCH RGHTVEDVYN AVRVARKAGL GVDVDFIFGL PGETEEDVEK TIKVMKDLIK MGAKIHAHTF MPLPQTPFAK ANPGKVDKKI IRAMRYEIPK GIFHGTWHNQ EIIAQKISKY LKTGKL // ID Y1530_METJA Reviewed; 156 AA. AC Q58925; DT 11-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Uncharacterized N-acetyltransferase MJ1530; DE EC=2.3.1.-; GN OrderedLocusNames=MJ1530; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the acetyltransferase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99551.1; -; Genomic_DNA. DR PIR; A64491; A64491. DR ProteinModelPortal; Q58925; -. DR STRING; 243232.MJ_1530; -. DR EnsemblBacteria; AAB99551; AAB99551; MJ_1530. DR KEGG; mja:MJ_1530; -. DR eggNOG; arCOG00833; Archaea. DR eggNOG; COG0456; LUCA. DR InParanoid; Q58925; -. DR KO; K03789; -. DR OMA; SAENEGH; -. DR PhylomeDB; Q58925; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR InterPro; IPR006464; Rbsml_AcTrfase. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR TIGRFAMs; TIGR01575; rimI; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Cytoplasm; Reference proteome; KW Transferase. FT CHAIN 1 156 Uncharacterized N-acetyltransferase FT MJ1530. FT /FTId=PRO_0000074632. FT DOMAIN 1 145 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 156 AA; 18052 MW; 298FE51AC69E88CD CRC64; MIIRKFSSKD LDAVEEIERE AFKTPYPTSL ILGFWSMYPN CFYVAEIDGR VVGYILGSMD WGNGHIISLA VKKECRGLGI GTALLKTLEN YYFNIANCNY IVLEVRVSNV LARRFYYRMG YRDRKLLPKY YEDGEDAILM IKKKPNAKGP LIITLW // ID Y1545_METJA Reviewed; 241 AA. AC Q58940; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ1545; GN OrderedLocusNames=MJ1545; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99563.1; -; Genomic_DNA. DR PIR; H64492; H64492. DR ProteinModelPortal; Q58940; -. DR STRING; 243232.MJ_1545; -. DR EnsemblBacteria; AAB99563; AAB99563; MJ_1545. DR KEGG; mja:MJ_1545; -. DR eggNOG; arCOG04060; Archaea. DR eggNOG; COG1709; LUCA. DR InParanoid; Q58940; -. DR KO; K07731; -. DR OMA; YESGRRK; -. DR PhylomeDB; Q58940; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR017271; Tscrpt_reg_HTH_MJ1545_prd. DR Pfam; PF01381; HTH_3; 1. DR PIRSF; PIRSF037724; TF_HTH_MJ1545_prd; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 241 Uncharacterized HTH-type transcriptional FT regulator MJ1545. FT /FTId=PRO_0000149793. FT DOMAIN 32 86 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 43 62 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 241 AA; 27274 MW; F4898E3F80842591 CRC64; MTFYFYFVIN MEKVAIYIIG DIVLAENTGK ALKKWRNLFN IQQIELAKYL NVSPSVISDY EVGRRKNPGV NIIKKYVLAL IEIDKEKGGQ TIKALKRILD KSPSMKAILS IKEYENPITL NEFVNIIDGE IAVGDNSDTP IYGHTVVDSI KAILEMTGDD FYHLYGWTTE RALIFTNVST GRSPMVAVRV SIMKPRVVVL QGINKDKIDS LALKLAEIDN IPLITTHLDT KELIKRLNEI K // ID Y1554_METJA Reviewed; 622 AA. AC Q58949; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1554; DE Flags: Precursor; GN OrderedLocusNames=MJ1554; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99574.1; -; Genomic_DNA. DR PIR; A64494; A64494. DR ProteinModelPortal; Q58949; -. DR STRING; 243232.MJ_1554; -. DR EnsemblBacteria; AAB99574; AAB99574; MJ_1554. DR KEGG; mja:MJ_1554; -. DR eggNOG; arCOG02284; Archaea. DR eggNOG; COG4880; LUCA. DR InParanoid; Q58949; -. DR OMA; TYLHPIG; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019198; Beta_propeller_containing. DR InterPro; IPR011044; Quino_amine_DH_bsu. DR InterPro; IPR014441; UCP006425_b-propeller. DR Pfam; PF09826; Beta_propel; 1. DR PIRSF; PIRSF006425; UCP006425_WD40; 1. DR SUPFAM; SSF50969; SSF50969; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 622 Uncharacterized protein MJ1554. FT /FTId=PRO_0000014017. SQ SEQUENCE 622 AA; 72283 MW; 86CAA62F3854D73F CRC64; MKIKAVAIFL SLLMIISLFS GCVENEKPIK EGSNDFKLIP VNSKSNFEEF KNTVENSIGN YIYVGHSYAS REVQITSTVK SSNVETSTEP ERFSKTNVQV KGVDEADILK TNGNIIAFSQ NKIYLIKPLP PKYAKIIKNI SECGYLYLTN NTLIVISWNK ITSYNVSNPE MPKIIWQMDL NGSYVDSRLY NGTLYLVVRK NSIDCPIVWN NYKIGYDKYY IPELPPIYSM DFDTTYIISR INIKSGKVEN SIAIVGNYKT TLYMSKNNLY FAYNLKINEK KLMLNFLNES ADKYFPTEVA DKIKRVIENE DFGDNAKFVE ITETIERYLS SLPSEKRHNL MKKLQNDFEN YLEEHWEEFE YTGIAKINLD SFEVKSGKVS GHLLNNFAMD EYNGYLRVAT TIGDWRFRDK MTNNIYILDS DLNVVGKLTG LEKGERIYAV RFMGDKAYIV TYKETDPLLV IDLKNPKNPK VLGELKIPGY STYLHPIGNN LFIGIGKDDD GKLKISLFNI SDLNNPKEVD KYKLNVWWSP AFRDYHAFLW DEKYKIFFLP AYNHAYVFKV EDNKIEMVKD DEHKTNVLRA LFINNYLYTF SLSEMHILDE NNWQLVKKIE FENYLPYGYG FK // ID Y1558_METJA Reviewed; 90 AA. AC Q58953; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 80. DE RecName: Full=UPF0237 protein MJ1558 {ECO:0000255|HAMAP-Rule:MF_01054}; GN OrderedLocusNames=MJ1558; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0237 family. {ECO:0000255|HAMAP- CC Rule:MF_01054}. CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|HAMAP- CC Rule:MF_01054}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99581.1; -; Genomic_DNA. DR PIR; E64494; E64494. DR ProteinModelPortal; Q58953; -. DR STRING; 243232.MJ_1558; -. DR EnsemblBacteria; AAB99581; AAB99581; MJ_1558. DR KEGG; mja:MJ_1558; -. DR eggNOG; arCOG04941; Archaea. DR eggNOG; COG3830; LUCA. DR InParanoid; Q58953; -. DR KO; K07166; -. DR OMA; IFKYMHR; -. DR PhylomeDB; Q58953; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR HAMAP; MF_01054; UPF0237; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR022986; UPF0237_ACT. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 90 UPF0237 protein MJ1558. FT /FTId=PRO_0000219910. FT DOMAIN 5 79 ACT. {ECO:0000255|HAMAP-Rule:MF_01054}. SQ SEQUENCE 90 AA; 9988 MW; A477B9511CBED489 CRC64; MSRVVVSVIG QDRTGIVAGI SKVLAENNAN ILDISQTIMD NLFAMIMLVD ISNAKVDFAT LKKELEKAGE ELGVQVIVQH EDIFKYMHRI // ID Y1561_METJA Reviewed; 553 AA. AC Q58956; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1561; GN OrderedLocusNames=MJ1561; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0795 and MJ1506. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99582.1; -; Genomic_DNA. DR PIR; H64494; H64494. DR ProteinModelPortal; Q58956; -. DR STRING; 243232.MJ_1561; -. DR PRIDE; Q58956; -. DR EnsemblBacteria; AAB99582; AAB99582; MJ_1561. DR KEGG; mja:MJ_1561; -. DR eggNOG; arCOG02079; Archaea. DR eggNOG; COG1361; LUCA. DR InParanoid; Q58956; -. DR OMA; FKDSWSN; -. DR PhylomeDB; Q58956; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 553 Uncharacterized protein MJ1561. FT /FTId=PRO_0000107412. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 524 544 Helical. {ECO:0000255}. SQ SEQUENCE 553 AA; 61713 MW; 86CA1E67C5A0AA01 CRC64; MITNKIKIFL ISLIFISGVY ALQVDAPQYQ PNVIHPGDDV DLWIKITNDN YDNEVKNIVV EVSPHYPFEL RQVNPIKGKA TISHLNPGES DTVYFKLHVD ENAPSRDYEI DVKVSYDEIN KEDGKETIHH YEITKIYYLH VYGIASFEIN GNFSLIPSKT QTVPIEIINT GTGTAKEVNL YIGYSLNSVN AGSESVEVSA YGTTKTQEKT IYYPTAVPIS NLPISPVGET KFYLGALKPD NSRVINLKLY TASNLVEGCY QIPAVITWID EDGTKRAEQI TIGAYVKGDI LLGISNVVTD PKEIKPGTTY VRIDVTITNN GHAEAKDVKL KLITNKPFKD SWSNCNIKDV GNLLPGVSKT VSFYVDVDKY ASAKHYKLPI EISYLDTANN KYKTEKFIDI YVKPKPLFEI ITKEVNVTAG KENTVYITIK NVGSEKAERV KISAIRNSGQ PFDYPIKSDT IGTLYPNQTG TGVIVIDVDK NAESKPYIIT IEIRCAGDSD EGDNNVYVYQ EPLKVVVNNS NSKSYWILGI IVVIAIVLVV GYVFKRKNSK DKE // ID Y1571_METJA Reviewed; 292 AA. AC Q58966; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1571; GN OrderedLocusNames=MJ1571; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99588.1; -; Genomic_DNA. DR PIR; B64496; B64496. DR ProteinModelPortal; Q58966; -. DR STRING; 243232.MJ_1571; -. DR EnsemblBacteria; AAB99588; AAB99588; MJ_1571. DR KEGG; mja:MJ_1571; -. DR eggNOG; arCOG02250; Archaea. DR eggNOG; COG0619; LUCA. DR InParanoid; Q58966; -. DR KO; K02008; -. DR OMA; MCYRYIF; -. DR PhylomeDB; Q58966; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro. DR InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane. DR InterPro; IPR012809; ECF_CbiQ. DR Pfam; PF02361; CbiQ; 1. DR TIGRFAMs; TIGR02454; ECF_T_CbiQ; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 292 Uncharacterized protein MJ1571. FT /FTId=PRO_0000107419. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 184 204 Helical. {ECO:0000255}. FT TRANSMEM 271 291 Helical. {ECO:0000255}. SQ SEQUENCE 292 AA; 33670 MW; 28E02654E07163A7 CRC64; MFKIYNIKSR IIRENMNNKL FDKTIEHVIK YLNENIFFEK YTRISGLLQN IESRIKIISL VIFLVGSVLS KHILTLIIFN SIALILAYLS NIPLLQYLKR VYVFIPIFAG IIAIPVMFNF MTPGKDVFVI LNNPHISITY EGLIYAITFT LRVATCVSFA VLIPITTQWN KVTSAIHKLG VPEVVITITN LAYRYIFLLL NFVLDMMYSR KSRVVNKLGM VESWKEAGKA IGALFIKTYQ MGEDXYYAML SRGYNGEIKH IYREEIKIKD IAFLLFSIII TALLVLFDRG IL // ID Y1582_METJA Reviewed; 249 AA. AC Q58977; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Uncharacterized metal-dependent hydrolase MJ1582 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=MJ1582; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P0AFQ7}; CC Note=Binds 2 divalent metal cations per subunit. CC {ECO:0000250|UniProtKB:P0AFQ7}; CC -!- SIMILARITY: Belongs to the TatD-type hydrolase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99602.1; -; Genomic_DNA. DR PIR; E64497; E64497. DR ProteinModelPortal; Q58977; -. DR STRING; 243232.MJ_1582; -. DR EnsemblBacteria; AAB99602; AAB99602; MJ_1582. DR KEGG; mja:MJ_1582; -. DR eggNOG; arCOG00891; Archaea. DR eggNOG; COG0084; LUCA. DR InParanoid; Q58977; -. DR KO; K03424; -. DR OMA; DEHAEKC; -. DR PhylomeDB; Q58977; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR018228; DNase_TatD-rel_CS. DR InterPro; IPR015991; DNase_TatD-type. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005902; DNase_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR TIGRFAMs; TIGR00010; TIGR00010; 1. DR PROSITE; PS01091; TATD_3; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome. FT CHAIN 1 249 Uncharacterized metal-dependent hydrolase FT MJ1582. FT /FTId=PRO_0000202012. FT METAL 10 10 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 12 12 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 95 95 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 95 95 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 129 129 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 150 150 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 198 198 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 249 AA; 28900 MW; C83FC884683F0361 CRC64; MRDVKYVDAH CHIEDKAFNK NRDEVIERAK KEDVIIVTSG ASLGGCLRAL ELRKKYNIYL TLGYHPSRVK ADDKVIEKVY NLIKNNEYEI LAIGEIGMDI KDENYKRQEE IFKKFLSLAE ELNKPIVVHA RGFERKIFDI AKDKVDIMFH CYSGDVELAK EIGKEGHLIS ISTLVCFSEH HKKLVESLDL EYLTTETDSP YLSPIKGTKN EPKNVKLVIE EIAKIKEMEV EEVKDVIYKN TCKFFKRRL // ID Y1584_METJA Reviewed; 151 AA. AC Q58979; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ1584; GN OrderedLocusNames=MJ1584; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99608.1; -; Genomic_DNA. DR PIR; G64497; G64497. DR STRING; 243232.MJ_1584; -. DR EnsemblBacteria; AAB99608; AAB99608; MJ_1584. DR KEGG; mja:MJ_1584; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 151 Uncharacterized protein MJ1584. FT /FTId=PRO_0000107427. SQ SEQUENCE 151 AA; 17270 MW; EC712881545F28F4 CRC64; MEIGNKVMEM KNDISKWKLI KTLYKVLKLK CWYDDENYAW SGGLSAYADG LRLLSKVGLF KIESEYCRSV TGKFKELKAS AVNLNAVDED ELIETLYRVL RQSCIMNIDD NIGESFGKKV YASGLRLLSK LGLFEIESEQ GDYIIGKFKE I // ID Y1620_METJA Reviewed; 505 AA. AC Q59015; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized protein MJ1620; GN OrderedLocusNames=MJ1620; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99641.1; -; Genomic_DNA. DR PIR; C64502; C64502. DR ProteinModelPortal; Q59015; -. DR STRING; 243232.MJ_1620; -. DR EnsemblBacteria; AAB99641; AAB99641; MJ_1620. DR KEGG; mja:MJ_1620; -. DR eggNOG; arCOG01356; Archaea. DR eggNOG; COG1032; LUCA. DR InParanoid; Q59015; -. DR OMA; GLRPYVY; -. DR PhylomeDB; Q59015; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 2. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF01938; TRAM; 1. DR SMART; SM00729; Elp3; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 505 Uncharacterized protein MJ1620. FT /FTId=PRO_0000107441. FT DOMAIN 435 499 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. SQ SEQUENCE 505 AA; 57466 MW; 949F2318DF8D7404 CRC64; MKALIIDCLA SGDGKRILAR DVIGAGPRTV KGILQSEGIE AKITPVEDLD IKDIKKYNLI FISAMTSDFK CVKKLVERIR LKTDSKIIVG GPIANDINIL EKIEADISIV GEGEITIREL IKKDFDAEDV KGTTYWDYNE DELKINPLRE ILTDLKLITP STEIKDYKNY FSARVYVEVV RGCSNFKRPL LLCTNKKCNL CENGTLKCPL NINPGCGFCS VPSVFGYARS RDEEDILKEV EALLKEGVNR IVLSAPDFLD YKRGEKLINP YFPEPNYEAI ESLLSKCKDL ADKYNANVLI ENIKANLFNE KVAEIFSKYL KTPIYIGCES GDKNHCKLLG RPTTPDDVLK AVKIAKKYNL KAQVYFIYGL PGENEETAKN TVNFMHKIKN YIDKITVYKF RPLPMSAFQN FKPNITKYSL LIRETANKIN LEIKKKYIGR VLEVIISERH FRNKRDAIGY LPDSGLMVVV KDGAKFIGKT KKVKIIKAYE KYLEGRILKT WLCKY // ID Y1624_METJA Reviewed; 128 AA. AC Q59018; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 28-NOV-2003, sequence version 2. DT 11-NOV-2015, entry version 81. DE RecName: Full=UPF0292 protein MJ1624 {ECO:0000255|HAMAP-Rule:MF_01095}; GN OrderedLocusNames=MJ1624; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000255|HAMAP-Rule:MF_01095}; CC Note=Binds two Mg(2+) per subunit. {ECO:0000255|HAMAP- CC Rule:MF_01095}; CC -!- SIMILARITY: Belongs to the UPF0292 family. {ECO:0000255|HAMAP- CC Rule:MF_01095}. CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|HAMAP- CC Rule:MF_01095}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99642.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99642.1; ALT_INIT; Genomic_DNA. DR PIR; F64502; F64502. DR ProteinModelPortal; Q59018; -. DR STRING; 243232.MJ_1624; -. DR EnsemblBacteria; AAB99642; AAB99642; MJ_1624. DR KEGG; mja:MJ_1624; -. DR eggNOG; arCOG01486; Archaea. DR eggNOG; COG1658; LUCA. DR InParanoid; Q59018; -. DR OMA; MYAENYK; -. DR PhylomeDB; Q59018; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000287; F:magnesium ion binding; IEA:UniProtKB-HAMAP. DR HAMAP; MF_01095; UPF0292; 1. DR InterPro; IPR006171; Toprim_domain. DR InterPro; IPR022972; UPF0292. DR Pfam; PF13662; Toprim_4; 1. DR SMART; SM00493; TOPRIM; 1. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Magnesium; Metal-binding; Reference proteome. FT CHAIN 1 128 UPF0292 protein MJ1624. FT /FTId=PRO_0000143951. FT DOMAIN 23 105 Toprim. {ECO:0000255|HAMAP- FT Rule:MF_01095}. FT METAL 29 29 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01095}. FT METAL 74 74 Magnesium 1; catalytic. FT {ECO:0000255|HAMAP-Rule:MF_01095}. FT METAL 74 74 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01095}. FT METAL 76 76 Magnesium 2. {ECO:0000255|HAMAP- FT Rule:MF_01095}. SQ SEQUENCE 128 AA; 15196 MW; 157D50F40100229F CRC64; MRRDEYFEKL LEVIEELKIE AEEKPIIVEG KRDVESLEKL GVEGTFIIIA KTPIYLIADE LVRKRVKEVI LLTDFDRRGR MLAKAIIEEF RHRGIKVNTK IRHEIFIYTN SGIRDIESLF SYVNKRLF // ID Y162_METJA Reviewed; 421 AA. AC Q57626; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0162; GN OrderedLocusNames=MJ0162; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC RNA-metabolizing metallo-beta-lactamase-like family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98146.1; -; Genomic_DNA. DR PIR; C64320; C64320. DR ProteinModelPortal; Q57626; -. DR STRING; 243232.MJ_0162; -. DR EnsemblBacteria; AAB98146; AAB98146; MJ_0162. DR KEGG; mja:MJ_0162; -. DR eggNOG; arCOG00544; Archaea. DR eggNOG; COG1236; LUCA. DR InParanoid; Q57626; -. DR OMA; SIMDNAY; -. DR PhylomeDB; Q57626; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR022712; Beta_Casp. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR011108; RMMBL. DR Pfam; PF10996; Beta-Casp; 1. DR Pfam; PF00753; Lactamase_B; 1. DR Pfam; PF07521; RMMBL; 1. DR SMART; SM01027; Beta-Casp; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 421 Uncharacterized protein MJ0162. FT /FTId=PRO_0000106724. SQ SEQUENCE 421 AA; 47477 MW; 5F5643116A67BABB CRC64; MVLLKFHGGC QQIGMSCVEV ETQKGRVLLD CGMSPDTGEI PKVDDKAVDA VIVSHAHLDH CGAIPFYKFK KIYCTHPTAD LMFITWRDTL NLTKAYKEED IQHAMENIEC LNYYEERQIT ENIKFKFYNA GHILGSASIY LEVDGKKILY TGDINEGVSR TLLPADTDID EIDVLIIEST YGSPLDIKPA RKTLERQLIE EISETIENGG KVIIPVFAIG RAQEILLIIN NYIRSGKLRD VPIYTDGSLI HATAVYMSYI NWLNPKIKNM VENRINPFGE IKKADESLVF NKEPCIIVST SGMVQGGPVL KYLKLLKDPK NKLILTGYQA EGTLGRELEE GAKEIQPFKN KIPIRGKVVK IEFSAHGDYN SLVRYIKKIP KPEKAIVMHG ERYQSLSFAM TIWKTLKIPT FVPVRGTILP I // ID Y183_METJA Reviewed; 48 AA. AC Q57642; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0183; GN OrderedLocusNames=MJ0183; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98180.1; -; Genomic_DNA. DR PIR; H64322; H64322. DR STRING; 243232.MJ_0183; -. DR EnsemblBacteria; AAB98180; AAB98180; MJ_0183. DR KEGG; mja:MJ_0183; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 48 Uncharacterized protein MJ0183. FT /FTId=PRO_0000106732. SQ SEQUENCE 48 AA; 5688 MW; 19B753A15C69F8FB CRC64; MLSPDMPLKN LDEYDRLGIK KKADAIARFI ENRWDYLQKN NMIALYGN // ID Y184_METJA Reviewed; 77 AA. AC Q57643; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0184; GN OrderedLocusNames=MJ0184; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98181.1; -; Genomic_DNA. DR PIR; A64323; A64323. DR STRING; 243232.MJ_0184; -. DR EnsemblBacteria; AAB98181; AAB98181; MJ_0184. DR KEGG; mja:MJ_0184; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 77 Uncharacterized protein MJ0184. FT /FTId=PRO_0000106733. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. SQ SEQUENCE 77 AA; 9150 MW; A5164FA166378C68 CRC64; MNIMITKQFD RHLKYYTTIV KVFANGIILI TAYYLVFELP VGYLIGLYII MFVVWLLVSM FFLGRLLDFM AKMDLKK // ID Y235_METJA Reviewed; 82 AA. AC Q57687; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0235; GN OrderedLocusNames=MJ0235; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98227.1; -; Genomic_DNA. DR PIR; D64329; D64329. DR STRING; 243232.MJ_0235; -. DR EnsemblBacteria; AAB98227; AAB98227; MJ_0235. DR KEGG; mja:MJ_0235; -. DR eggNOG; arCOG05025; Archaea. DR eggNOG; ENOG410Z21C; LUCA. DR OMA; MKCLREI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 82 Uncharacterized protein MJ0235. FT /FTId=PRO_0000106754. SQ SEQUENCE 82 AA; 9899 MW; CB23BFE0DA7F4E9F CRC64; MEKLIINSMK KVFLEELKDL ENELNQIFKK YNVKSKDELK KKIANGEIKE EQIKDDLERI EFLEENIERV MKCLREINVK SL // ID Y259_METJA Reviewed; 202 AA. AC Q57707; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0259; GN OrderedLocusNames=MJ0259; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98250.1; -; Genomic_DNA. DR PIR; D64332; D64332. DR ProteinModelPortal; Q57707; -. DR STRING; 243232.MJ_0259; -. DR EnsemblBacteria; AAB98250; AAB98250; MJ_0259. DR KEGG; mja:MJ_0259; -. DR eggNOG; arCOG05028; Archaea. DR eggNOG; ENOG410YPUN; LUCA. DR OMA; SSFCLCT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 202 Uncharacterized protein MJ0259. FT /FTId=PRO_0000106761. SQ SEQUENCE 202 AA; 22872 MW; 208E43AF60241A7E CRC64; MKKLLLIIGI ISLMTSMSMC LNNNNLNNLD LKKSILVEVN GTPIEIPLRA TVGEAKEVKL INTTDREIYN YYHSKILIYI KGDMNISVKE GGVSIVDLVT KLEWFNQFYP HNIVVELNRT NSTVTVKSIF ANGKTSITEL KVNESEYLMH NNKTMVIEIL KTHNTATITK INNTFIIEGN SLKELDNAET RFVIDMFKGS IT // ID Y012_METJA Reviewed; 208 AA. AC Q60328; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Putative transposase MJ0012; GN OrderedLocusNames=MJ0012; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the transposase 35 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; D64301; D64301. DR InParanoid; Q60328; -. DR PhylomeDB; Q60328; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Metal-binding; KW Reference proteome; Transposable element; Transposition; Zinc. FT CHAIN 1 208 Putative transposase MJ0012. FT /FTId=PRO_0000106652. FT METAL 83 83 Zinc. {ECO:0000255}. FT METAL 86 86 Zinc. {ECO:0000255}. FT METAL 100 100 Zinc. {ECO:0000255}. FT METAL 103 103 Zinc. {ECO:0000255}. SQ SEQUENCE 208 AA; 24347 MW; 4C824F93015561B4 CRC64; MKKYWNRRKN RVEDFINKLT SQLSKLFPDA IFIFEDLDKF NMYDKNSNFN RNLDRTNWRK IAKKLEYKSV VLYVNPHYTS KTCPVCGSKM KSQEGQVVKC DKCGIFDRQF VRCYNIFKRG VELAKKLLGG VGVPVAGAEV DDLLSNEPRG ELRLVKPNPN VEAKLPVRKS NRRFELQNPK DFVQIFDFPL MVYTVDLNGK YLKIYNCP // ID Y039_METJA Reviewed; 115 AA. AC Q60351; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized protein MJ0039; GN OrderedLocusNames=MJ0039; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98020.1; -; Genomic_DNA. DR PIR; G64304; G64304. DR PDB; 1GO3; X-ray; 1.75 A; F/N=9-115. DR PDBsum; 1GO3; -. DR ProteinModelPortal; Q60351; -. DR SMR; Q60351; 9-115. DR IntAct; Q60351; 1. DR STRING; 243232.MJ_0039; -. DR EnsemblBacteria; AAB98020; AAB98020; MJ_0039. DR KEGG; mja:MJ_0039; -. DR eggNOG; arCOG01016; Archaea. DR eggNOG; COG1460; LUCA. DR InParanoid; Q60351; -. DR KO; K03051; -. DR OMA; CALDYLQ; -. DR PhylomeDB; Q60351; -. DR EvolutionaryTrace; Q60351; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IEA:InterPro. DR GO; GO:0003899; F:DNA-directed RNA polymerase activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0000166; F:nucleotide binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.150.80; -; 1. DR InterPro; IPR010997; HRDC-like. DR InterPro; IPR002121; HRDC_dom. DR InterPro; IPR005574; RNA_pol_II_Rpb4. DR InterPro; IPR010924; RNAP_F. DR Pfam; PF03874; RNA_pol_Rpb4; 1. DR PIRSF; PIRSF005053; RNA_pol_F_arch; 1. DR SUPFAM; SSF47819; SSF47819; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 115 Uncharacterized protein MJ0039. FT /FTId=PRO_0000106663. FT STRAND 11 20 {ECO:0000244|PDB:1GO3}. FT HELIX 22 35 {ECO:0000244|PDB:1GO3}. FT HELIX 40 52 {ECO:0000244|PDB:1GO3}. FT HELIX 57 69 {ECO:0000244|PDB:1GO3}. FT HELIX 74 83 {ECO:0000244|PDB:1GO3}. FT HELIX 88 94 {ECO:0000244|PDB:1GO3}. FT HELIX 104 111 {ECO:0000244|PDB:1GO3}. SQ SEQUENCE 115 AA; 13389 MW; 898CE40770B73730 CRC64; MYQAKRERMI GKKILGERYV TVSEAAEIMY NRAQIGELSY EQGCALDYLQ KFAKLDKEEA KKLVEELISL GIDEKTAVKI ADILPEDLDD LRAIYYKREL PENAEEILEI VRKYI // ID Y052_METJA Reviewed; 222 AA. AC Q60359; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0052; GN OrderedLocusNames=MJ0052; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 rhodanese domain. {ECO:0000255|PROSITE- CC ProRule:PRU00173}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98033.1; -; Genomic_DNA. DR PIR; D64306; D64306. DR ProteinModelPortal; Q60359; -. DR STRING; 243232.MJ_0052; -. DR DNASU; 1450891; -. DR EnsemblBacteria; AAB98033; AAB98033; MJ_0052. DR KEGG; mja:MJ_0052; -. DR eggNOG; arCOG02020; Archaea. DR eggNOG; COG2603; LUCA. DR InParanoid; Q60359; -. DR KO; K06917; -. DR OMA; IVVFCAR; -. DR PhylomeDB; Q60359; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.250.10; -; 1. DR InterPro; IPR030818; Arch_SelU_Nterm. DR InterPro; IPR001763; Rhodanese-like_dom. DR Pfam; PF00581; Rhodanese; 1. DR SMART; SM00450; RHOD; 1. DR SUPFAM; SSF52821; SSF52821; 1. DR TIGRFAMs; TIGR04568; arch_SelU_Nterm; 1. DR PROSITE; PS50206; RHODANESE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 222 Uncharacterized protein MJ0052. FT /FTId=PRO_0000106670. FT DOMAIN 104 221 Rhodanese. {ECO:0000255|PROSITE- FT ProRule:PRU00173}. SQ SEQUENCE 222 AA; 25151 MW; 61991060852008A6 CRC64; MDEGILARLI TFTEDVVLCI VLNDGRKMIT NGKKILAGKI EGELASFILS ASKEFLEDKK VGVKKFKDYD IYFERIDINK FLKSIGGEFV KNTITVSELL ELIKKEDVII VDTRSPREFK EETLPGAINI PLFLDDEHAL IGKTYKQESR EKAIEIATDI VEKSLKRILN EAKKLDRDKL IVVFCARGGM RSQTMALILQ LLGFKVKRLI GGFKAFKHAV DK // ID Y053_METJA Reviewed; 227 AA. AC Q60360; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0053; GN OrderedLocusNames=MJ0053; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98039.1; -; Genomic_DNA. DR PIR; E64306; E64306. DR STRING; 243232.MJ_0053; -. DR EnsemblBacteria; AAB98039; AAB98039; MJ_0053. DR KEGG; mja:MJ_0053; -. DR eggNOG; arCOG05019; Archaea. DR eggNOG; COG2603; LUCA. DR InParanoid; Q60360; -. DR OMA; CPYECQI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR030815; Arch_SelU_Cterm. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR04569; arch_SelU_Cterm; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 227 Uncharacterized protein MJ0053. FT /FTId=PRO_0000106671. FT NP_BIND 17 24 ATP. {ECO:0000255}. SQ SEQUENCE 227 AA; 26722 MW; A10A48D331225665 CRC64; MGLSFNGENM IIFGLFGKTG CGKTEILNEL KKHHPVIDIE EIARTRGSIL GDLYHLSMRS QEEFDYLINK EIEKAKKFGY AVVEYEGRKI GGEKKLKIPE LLADIKNYTY KILIDCPYEC QINRLVSIYK PKNEKEKEIL INKFLILKES FKKPEMIEAV DNIIELIKQD KYYEAAKLIE EKLYREHYMR NVKKIKPDLI VYNEDVKKSA KIIDEFIKKK LKEHNLI // ID Y063_METJA Reviewed; 181 AA. AC Q60375; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0063; GN OrderedLocusNames=MJ0063; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98050.1; -; Genomic_DNA. DR PIR; G64307; G64307. DR ProteinModelPortal; Q60375; -. DR STRING; 243232.MJ_0063; -. DR EnsemblBacteria; AAB98050; AAB98050; MJ_0063. DR KEGG; mja:MJ_0063; -. DR eggNOG; arCOG08289; Archaea. DR eggNOG; ENOG41110SW; LUCA. DR OMA; NCASSIP; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 181 Uncharacterized protein MJ0063. FT /FTId=PRO_0000106674. SQ SEQUENCE 181 AA; 21173 MW; E007B9432CB52053 CRC64; MFQMENRNDE LFIKLDSSIK SLLRSAREFK KENESISNVL LQLAEMLDNI DKTLEIIEKN FQIILKNRES GKFSNNEIIQ KFVKPLENLI KVIENIESTS NNLKNEIENC ASSIPTLKEI TDKLKIINME SATQAIEEFK IAYDMLEDNR KNLDELIEKT KILKDKLKNL LLQIDNFLNE H // ID Y078_METJA Reviewed; 207 AA. AC Q60385; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0078; GN OrderedLocusNames=MJ0078; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98066.1; -; Genomic_DNA. DR PIR; F64309; F64309. DR ProteinModelPortal; Q60385; -. DR STRING; 243232.MJ_0078; -. DR EnsemblBacteria; AAB98066; AAB98066; MJ_0078. DR KEGG; mja:MJ_0078; -. DR eggNOG; arCOG08278; Archaea. DR eggNOG; ENOG41110P5; LUCA. DR OMA; TKERGFE; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.10.10; -; 1. DR InterPro; IPR011989; ARM-like. DR InterPro; IPR016024; ARM-type_fold. DR SUPFAM; SSF48371; SSF48371; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 207 Uncharacterized protein MJ0078. FT /FTId=PRO_0000106684. SQ SEQUENCE 207 AA; 24563 MW; 571955A95E51DAF1 CRC64; MNCEEYRKKL KLNYGNREKL KVLKELYQME VDEITKLNIL DDVFELLTST KERGFEDIIS THYTSDSKNK AIIYYCIKII EKVGIKYPNL VYIYIPYLIK LLDSEFECIR FASAEALANI PSKLTIYAYP KLIKKLDNEV YAKVLVKLIM KSDNKEAILL KLFENFNEYS LYVIKELYKY DKELVYEFIP LILKEFGNNG LYSFLQK // ID Y085_METJA Reviewed; 373 AA. AC Q57550; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized lipoprotein MJ0085; DE Flags: Precursor; GN OrderedLocusNames=MJ0085; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98067.1; -; Genomic_DNA. DR PIR; E64310; E64310. DR ProteinModelPortal; Q57550; -. DR SMR; Q57550; 44-366. DR STRING; 243232.MJ_0085; -. DR EnsemblBacteria; AAB98067; AAB98067; MJ_0085. DR KEGG; mja:MJ_0085; -. DR eggNOG; arCOG03303; Archaea. DR eggNOG; COG0614; LUCA. DR InParanoid; Q57550; -. DR KO; K02016; -. DR OMA; CLRLLTY; -. DR PhylomeDB; Q57550; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 373 Uncharacterized lipoprotein MJ0085. FT /FTId=PRO_0000013991. FT DOMAIN 58 333 Fe/B12 periplasmic-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00344}. FT LIPID 21 21 S-archaeol cysteine. {ECO:0000255}. SQ SEQUENCE 373 AA; 41812 MW; 8E64F5683E830878 CRC64; MLKKLIGLLT ILIIAVGFCG CMEQNIEKQT PTASEAPNTI KVVDLYGREV EVPKEVNRIV CCGPGCLRLI VYLNATDKVV GVEDTEKKWT PWTRPYRIAH PELANLPTIG QGGPCPKPNP EAIIQVKPDV IFVTYMPKDE VDALQQKTGI PVVVLSYGQL ATFNNEDLFK SLELAGKILG KEERAKEVIE FIKNCQNDLN ERTKDIPDDK KPSVYVGGIG YKGLHGIDST ECKYPPFVAV NAKNVADELG KEGHVFVTKE QILKWNPDII FIDEGGLKLV VEDYKRNKEF YNSLKAFKNG DVYGLLPYNF YTTNIGTALA DAYYIGKVVY PDRFKDIDPE QKADEIFTFL VGKPVYKEMK EKLGGFKKLE FSS // ID Y090_METJA Reviewed; 407 AA. AC Q57555; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized protease MJ0090; DE EC=3.4.-.-; GN OrderedLocusNames=MJ0090; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98071.1; -; Genomic_DNA. DR PIR; B64311; B64311. DR ProteinModelPortal; Q57555; -. DR STRING; 243232.MJ_0090; -. DR DNASU; 1450929; -. DR EnsemblBacteria; AAB98071; AAB98071; MJ_0090. DR KEGG; mja:MJ_0090; -. DR eggNOG; arCOG03202; Archaea. DR eggNOG; COG0826; LUCA. DR InParanoid; Q57555; -. DR KO; K08303; -. DR OMA; NTIIYDH; -. DR PhylomeDB; Q57555; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001539; Peptidase_U32. DR InterPro; IPR009000; Transl_B-barrel. DR Pfam; PF01136; Peptidase_U32; 1. DR SUPFAM; SSF50447; SSF50447; 1. DR PROSITE; PS01276; PEPTIDASE_U32; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome. FT CHAIN 1 407 Uncharacterized protease MJ0090. FT /FTId=PRO_0000079186. SQ SEQUENCE 407 AA; 46775 MW; 74FC8503D3A028DB CRC64; MMVMVELLSP ANDLTCLKTA IDYGADAVYC GLKELNMRAN AKNFTREELI EGIKYAHDNN KKVYLCTNTV VYENDLKKVE EILDFANSAE VDAVIVSDLG TMQLANELGL RVHASVQCNV TNSLTAKFYS KFAKRVILSR ELTLNQIKEI RENLKKDKVD LELEGFVHGA LCVAISGRCF LSSYLFGRHA NCGDCLQPCR RKWKLINEHH DGTYEIVCEG KYLLSPKDLC MIEHIPELME VFDSFKIEGR AKNADYVMRT TKIYREAIDS VLDGSYYDKL EYFKKELQKV YNRSYDTGFY FRDINKNHDF QYEIEGNASK YRKIEIGRVV NFYKKVSVAE IELWHDLKIG DTILIIGKTT GCVEEVVKSM QINHKDVEIA KKGERVGVKL NHLVREGDRV YLLKETI // ID Y1005_METJA Reviewed; 131 AA. AC Q58411; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1005; GN OrderedLocusNames=MJ1005; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99013.1; -; Genomic_DNA. DR PIR; D64425; D64425. DR ProteinModelPortal; Q58411; -. DR STRING; 243232.MJ_1005; -. DR EnsemblBacteria; AAB99013; AAB99013; MJ_1005. DR KEGG; mja:MJ_1005; -. DR eggNOG; arCOG05062; Archaea. DR eggNOG; ENOG4111W6D; LUCA. DR OMA; DIGHFIL; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR013196; HTH_11. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF08279; HTH_11; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 131 Uncharacterized protein MJ1005. FT /FTId=PRO_0000107140. SQ SEQUENCE 131 AA; 15579 MW; 3417CF17A408481E CRC64; MRIEDEIKNI IEKKDYDFWE FLKKAYENNI KLDIGHFILL NILIGVNDLY HKLSEKFGEE EARKILERNK IFAKNSDFIS GEFLKDYIDR KSRVAVHNRI KDLKTLGFKI ESKSGPFGGY KIVGYPEWFK K // ID Y1017_METJA Reviewed; 203 AA. AC Q58423; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1017; GN OrderedLocusNames=MJ1017; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99023.1; -; Genomic_DNA. DR PIR; H64426; H64426. DR ProteinModelPortal; Q58423; -. DR STRING; 243232.MJ_1017; -. DR EnsemblBacteria; AAB99023; AAB99023; MJ_1017. DR KEGG; mja:MJ_1017; -. DR eggNOG; arCOG05063; Archaea. DR eggNOG; ENOG410YNQT; LUCA. DR OMA; PIFWIFL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 203 Uncharacterized protein MJ1017. FT /FTId=PRO_0000107143. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. SQ SEQUENCE 203 AA; 23749 MW; DA69129BA5C2CA1D CRC64; MKVKVYRVGG ITGIFLIFLI LLLLIILAIV ALPIFLILMA IFGGYILLKY KIKSFFRKVW YNIRKKKIKI EDTSTNGEVK INFAKRIEIE DGKIETNNIN TLLDYLDENT KSFAYYLKNI GAEFRDDGIY FKGYKIYPIF KKSYPINEII SLRYPENIDA VVLGLKGEPY DPKFLYLIPK EFLKDRMSIS ELKRFEIGDM VLK // ID Y1020_METJA Reviewed; 259 AA. AC Q58426; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1020; GN OrderedLocusNames=MJ1020; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99024.1; -; Genomic_DNA. DR PIR; C64427; C64427. DR ProteinModelPortal; Q58426; -. DR STRING; 243232.MJ_1020; -. DR DNASU; 1451917; -. DR EnsemblBacteria; AAB99024; AAB99024; MJ_1020. DR KEGG; mja:MJ_1020; -. DR eggNOG; arCOG04230; Archaea. DR eggNOG; COG3294; LUCA. DR InParanoid; Q58426; -. DR KO; K09163; -. DR OMA; NDHGPVH; -. DR PhylomeDB; Q58426; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 259 Uncharacterized protein MJ1020. FT /FTId=PRO_0000107144. SQ SEQUENCE 259 AA; 29218 MW; 1CACA2E63B82592B CRC64; MGRDMDFEEL NSLQGIPKMI YDELIKNKKV NTFLKMSNIM AVGRLGYNDH GKTHAKIVAN NAIKMLKILY KKGIEPSFVK DCKGSFEDSL VITLLGAYLH DIGNSVHRDI HHLHSAYLAL DIVENILKKY YKEEKAYQMT TEVLHAIYSH SEGIMGLTIE AGVIAVADGT DMTKGRSRIP ICKKCYDIHS VSAASIERVE IKEGDEKPIQ IEVILSNEAG IFQIQEVLGE KIKWSGIKNY VSVYARVEKE KPVFEEITI // ID Y1027_METJA Reviewed; 377 AA. AC Q58433; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized protein MJ1027; GN OrderedLocusNames=MJ1027; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99031.1; -; Genomic_DNA. DR PIR; B64428; B64428. DR ProteinModelPortal; Q58433; -. DR STRING; 243232.MJ_1027; -. DR EnsemblBacteria; AAB99031; AAB99031; MJ_1027. DR KEGG; mja:MJ_1027; -. DR eggNOG; arCOG01547; Archaea. DR eggNOG; COG3261; LUCA. DR InParanoid; Q58433; -. DR KO; K14123; -. DR OMA; HIHLWSA; -. DR PhylomeDB; Q58433; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 2. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00346; Complex1_49kDa; 2. DR Pfam; PF00374; NiFeSe_Hases; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 377 Uncharacterized protein MJ1027. FT /FTId=PRO_0000118628. SQ SEQUENCE 377 AA; 43175 MW; 913C3C1A6BE0332C CRC64; MLFMKYEGEI AIGPVHPTML EPHRLRLFIE DEIIKEAELV IGVNYRGIEL IMEGLPPEKI SILSEKICGI CSHIHVWCNV TVTERGCDIE VPERAEYIRA IVEELERLHS HMLLFGHAFE VLGFETMAFR AFMIREPIMQ ILGEITGGRA QYSCPIIGGI RPRCNIKESK IPALLERLEK FEENLKKLLE RTVNDPMIMS RIKDVGVLDK KTAKKLHALG PTARGSGIHS DMRKMGQVPV YDNFEFEEIV FDDGDVFSRL AVRFYECFES VKIIRQGLKD LPNLDKRIYN PNYELKEFKP IDVYNEAQRG QVYYSYGLDE NGRVRQVKIR TPTATNLACM EAILPGHHVS DAELIIASCD PCFTCTDRMI VVKENKI // ID Y1049_METJA Reviewed; 161 AA. AC Q58449; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1049; GN OrderedLocusNames=MJ1049; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99059.1; -; Genomic_DNA. DR PIR; H64430; H64430. DR ProteinModelPortal; Q58449; -. DR EnsemblBacteria; AAB99059; AAB99059; MJ_1049. DR KEGG; mja:MJ_1049; -. DR eggNOG; arCOG05066; Archaea. DR eggNOG; ENOG410YS66; LUCA. DR OMA; NVLLAYR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 161 Uncharacterized protein MJ1049. FT /FTId=PRO_0000107152. SQ SEQUENCE 161 AA; 18880 MW; DFD39C9FA1514D22 CRC64; MVIKKIIKKI RGNKDLPKPI EVPDEEYIVI GEEKPAYILE EESETESEVL GLEHKEKEEV KEVEEVVRVE KILPKLYVVR IKHPLDFENI KDKIPEYDVV IVNFEEVPFE SILKELNEFR DYMSILNFKL GFVAENVLLA YRDDVILDKY VSNITDDAEN V // ID Y1082_METJA Reviewed; 120 AA. AC Q58482; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1082; GN OrderedLocusNames=MJ1082; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1503. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99084.1; -; Genomic_DNA. DR PIR; A64435; A64435. DR ProteinModelPortal; Q58482; -. DR STRING; 243232.MJ_1082; -. DR EnsemblBacteria; AAB99084; AAB99084; MJ_1082. DR KEGG; mja:MJ_1082; -. DR eggNOG; arCOG02242; Archaea. DR eggNOG; COG3355; LUCA. DR InParanoid; Q58482; -. DR OMA; EDLMRCI; -. DR PhylomeDB; Q58482; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002831; Tscrpt_reg_TrmB_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01978; TrmB; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 120 Uncharacterized protein MJ1082. FT /FTId=PRO_0000107162. SQ SEQUENCE 120 AA; 14455 MW; F40E066CD5198029 CRC64; MKEFIINRLK KFTIEDLMRC ILGLQEIEIR VYFDLLENGE GSVLEIAERV NRDRTTVQKA LRSLMNCGLV DRRKVTEKVG YKYIYNAVDL DRVSDIIEEL LDDWYQNVKK WLTYFRENRK // ID Y1085_METJA Reviewed; 509 AA. AC Q58485; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 66. DE RecName: Full=Uncharacterized protein MJ1085; GN OrderedLocusNames=MJ1085; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99095.1; -; Genomic_DNA. DR PIR; D64435; D64435. DR ProteinModelPortal; Q58485; -. DR STRING; 243232.MJ_1085; -. DR DNASU; 1451981; -. DR EnsemblBacteria; AAB99095; AAB99095; MJ_1085. DR KEGG; mja:MJ_1085; -. DR eggNOG; arCOG09556; Archaea. DR eggNOG; ENOG41110ZS; LUCA. DR OMA; DAYEYND; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR021869; RNase_Zc3h12_NYN. DR Pfam; PF11977; RNase_Zc3h12a; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 509 Uncharacterized protein MJ1085. FT /FTId=PRO_0000107163. SQ SEQUENCE 509 AA; 59471 MW; 8ACF7C4B045D6049 CRC64; MDNMGKDKNI LKIRANLIKY IDVDEIEELP KVKVKNVEEF LEAHRVLGKH VICRYKDNLE DIFFFVDNGV IFYIPSDGFK TLEDLIEAKS LGLSAEEYYE YLEFGDINEY KKYKSSGFKS IEEYKKAKDL GFIGGLEELV KEGIAQRLDD KYIIEYLYYG ILENREFSND AELYYFAIEK GFSDFDELKN ALKAGFGDAN EYKDALNRGF KDAYEYNDAL SKGFRDADEY KIAKAIGVNS KKELEEYMEL KRICENFGLE TFEEGYLLKV LMDLKIDEEI TLKELYNKLK EKERLMKIKK DVLNKLANLS SPSWYSTRFT TVDDLEEYLV DSEIVSYLGE YIKEEKIFRR IYPPKPSRRI VIIDAISVLN NMHNLSPNSI ENLIKKIKNA GFKNIITVMD TVTYYKIKGK DICRFLANEC NIKVSKSKDE AYKLIIEYIK NFGALVISNA SFKDYIIKDS KLFYKDIKEY IIPFIVENGE INLDIELLRK LYTEVVTKRI EKIKSNVVS // ID Y1089_METJA Reviewed; 268 AA. AC Q58489; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1089; GN OrderedLocusNames=MJ1089; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiQ family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99090.1; -; Genomic_DNA. DR PIR; H64435; H64435. DR STRING; 243232.MJ_1089; -. DR EnsemblBacteria; AAB99090; AAB99090; MJ_1089. DR KEGG; mja:MJ_1089; -. DR eggNOG; arCOG02249; Archaea. DR eggNOG; COG0619; LUCA. DR InParanoid; Q58489; -. DR KO; K02008; -. DR OMA; NRWIAYS; -. DR PhylomeDB; Q58489; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro. DR GO; GO:0005887; C:integral component of plasma membrane; IEA:InterPro. DR GO; GO:0006824; P:cobalt ion transport; IEA:InterPro. DR InterPro; IPR003339; ABC/ECF_trnsptr_transmembrane. DR InterPro; IPR012809; ECF_CbiQ. DR Pfam; PF02361; CbiQ; 1. DR TIGRFAMs; TIGR02454; ECF_T_CbiQ; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 268 Uncharacterized protein MJ1089. FT /FTId=PRO_0000107165. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. SQ SEQUENCE 268 AA; 30904 MW; B9483380C8EC325E CRC64; MGFMKHNIVD NVAFSNKLRH VNPKLKVIFA LSLLLISVFS TSFIVPLIIF FINSILLLFK AKVPKKIYAV FVGIPLGFGI LNLVIFAFLF GTVEWFKINV FGFEIPVYKD GIELGLLLFG RMLGGVSSML FLAFTTPMVE LFYIFRELKM PDVLVDMMML IYRYIFVLYE EYEKMKFAQE SRLGTSNLKS TYKSLGALAA HLFIRAWEKG EKLNITMMSR CYDGKIKLLQ TIENPSIKYI LFIAIFDIFL IILAYLTKDF TLTSYIKI // ID Y1098_METJA Reviewed; 254 AA. AC Q58498; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1098; GN OrderedLocusNames=MJ1098; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99101.1; -; Genomic_DNA. DR PIR; A64437; A64437. DR ProteinModelPortal; Q58498; -. DR STRING; 243232.MJ_1098; -. DR EnsemblBacteria; AAB99101; AAB99101; MJ_1098. DR KEGG; mja:MJ_1098; -. DR eggNOG; ENOG4111JZH; LUCA. DR InParanoid; Q58498; -. DR OMA; LAWWYQD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR Gene3D; 3.10.28.10; -; 2. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR004860; LAGLIDADG_2. DR Pfam; PF03161; LAGLIDADG_2; 1. DR SUPFAM; SSF55608; SSF55608; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 254 Uncharacterized protein MJ1098. FT /FTId=PRO_0000107167. SQ SEQUENCE 254 AA; 30440 MW; E98B050B1340BF34 CRC64; MYEKYIVEGL SDREIAYLIG CGKATVVRAR QKHGIYREDV KMCDDYTLDN ISEDLRTFID GLLLGDACIT EKGNLLITQN KRYDWLEYVK HRFQQFGLNV YFHCYKYKRR TSEVIADLYV LSTSRYELFR QLRERWYPDG IKRIPNDLVI NDEGLAQWYL GDGSLTKQKN GYKLELSTHG FTLDENKFLQ QKLKLLYGFD FRISKKHQYR YLRLFKSKQV HAFCSIVEPF IPPSYRNKVR CLHDYQWLKS WDVI // ID Y1106_METJA Reviewed; 185 AA. AC Q58506; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1106; GN OrderedLocusNames=MJ1106; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH236. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99109.1; -; Genomic_DNA. DR PIR; A64438; A64438. DR STRING; 243232.MJ_1106; -. DR EnsemblBacteria; AAB99109; AAB99109; MJ_1106. DR KEGG; mja:MJ_1106; -. DR eggNOG; arCOG04822; Archaea. DR eggNOG; COG1790; LUCA. DR OMA; ELGIYRR; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007556; DUF483. DR Pfam; PF04467; DUF483; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 185 Uncharacterized protein MJ1106. FT /FTId=PRO_0000107169. SQ SEQUENCE 185 AA; 22110 MW; E991917F84DC6E36 CRC64; MLKNLLYKIE KLRSGELEGF EVLKEHIQSL DEFQYQQIVE RLKFQIELVE KYKPKVRPAI DPMVSTELGI YRRLDDFEIG KLLDYPECCI KSFVEDVRVA IDREHLKEVE EMKEELKNKG IYAIVLPSGF IPCSLKCEEA IKRGFIGYLT KEEFDKILEL EKELKEKIRH WHFGYDEYYE KIILP // ID Y1110_METJA Reviewed; 486 AA. AC Q58510; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1110; GN OrderedLocusNames=MJ1110; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99113.1; -; Genomic_DNA. DR PIR; E64438; E64438. DR ProteinModelPortal; Q58510; -. DR STRING; 243232.MJ_1110; -. DR EnsemblBacteria; AAB99113; AAB99113; MJ_1110. DR KEGG; mja:MJ_1110; -. DR eggNOG; arCOG03198; Archaea. DR eggNOG; COG1771; LUCA. DR InParanoid; Q58510; -. DR KO; K09724; -. DR OMA; RMVDEKK; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007503; DUF530. DR Pfam; PF04409; DUF530; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 486 Uncharacterized protein MJ1110. FT /FTId=PRO_0000107172. SQ SEQUENCE 486 AA; 56596 MW; EC8007EAAEFFF977 CRC64; MESTSNLIKN ANEFLDSLNE INDKLKEVVG KIKNKTIDKT KLSDIILTLE KNLEILQDLK SKMEFLEFDS PYKNVGKLKG GYDSEGLQEI ASYSTYLRRI ASEKKGILER VRHALVAHKI ALAHLTEDIG NINLPPNLPL DGSYKKIMFE FPPYLVTTYK EFLDILEPKG RGILTSYTIS LIVIDKGKRE FKRIKVEDKN YEKYIKEKFG NAIITSIKRN FSKNKIIDDQ YVRRVLAIGY LNTYKDEIEK AINEKIDKLL NEEEKKYLNR YLELCLLFRE EADISGGILD VRCMEERKLK ELELKEILEK EGLYRDGEPI EPLKKAIKIK NELSKKISKD ILIKRFSEDV FKFYLYKTPD ERARSNLFPS IMITPQRGFL SWMSVDGINC VDVLDLKFKL EEELPKYQIP LKNIGGVALY LIHDWDAVER FNFKKKDIED LLKKIALIEP IKEILKDKNV DVSKLEKFGK VKKEKTKKFL DLLSGL // ID Y1113_METJA Reviewed; 301 AA. AC Q58513; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative glycosyltransferase MJ1113; DE EC=2.-.-.-; GN OrderedLocusNames=MJ1113; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the glycosyltransferase 4 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99115.1; -; Genomic_DNA. DR PIR; H64438; H64438. DR ProteinModelPortal; Q58513; -. DR STRING; 243232.MJ_1113; -. DR EnsemblBacteria; AAB99115; AAB99115; MJ_1113. DR KEGG; mja:MJ_1113; -. DR eggNOG; arCOG03199; Archaea. DR eggNOG; COG0472; LUCA. DR InParanoid; Q58513; -. DR KO; K01001; -. DR OMA; KYGYDLH; -. DR PhylomeDB; Q58513; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008963; F:phospho-N-acetylmuramoyl-pentapeptide-transferase activity; IEA:InterPro. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR000715; Glycosyl_transferase_4. DR PANTHER; PTHR22926; PTHR22926; 1. DR Pfam; PF00953; Glycos_transf_4; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Glycosyltransferase; Membrane; KW Reference proteome; Transferase; Transmembrane; Transmembrane helix. FT CHAIN 1 301 Putative glycosyltransferase MJ1113. FT /FTId=PRO_0000108952. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT TRANSMEM 164 184 Helical. {ECO:0000255}. FT TRANSMEM 191 211 Helical. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. SQ SEQUENCE 301 AA; 33363 MW; B94D45ED1EED81A5 CRC64; MGHYFINLFT YTIIAFIFSA VLCKFLMKKM INYKFGYDLH KKEKIKVPEM GGLAVLFSNA LFIPFVNPIF VLPIITAGII GIVDDIAKLS PKEKLILLFI SGLIIGILFY NNSYVNLIEI LIIALGIMIS SNLTNMLAGF NGLEIGMGVI ASISLALVLF LDNYTTGFLS ALIFSASYLG LLIFNKYPAK VFPGDVGTLP IGAFLAVLAV VYKEYIPFLV IMMPYVIDAS LKYLSAGVMS RDEHKPTTLK EDGKLYYIGG YLSLPRLILK YKPMREPHLV TVLWIIGIFF GIVGILISLI A // ID Y1118_METJA Reviewed; 89 AA. AC Q58518; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1118; GN OrderedLocusNames=MJ1118; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99119.1; -; Genomic_DNA. DR PIR; E64439; E64439. DR ProteinModelPortal; Q58518; -. DR STRING; 243232.MJ_1118; -. DR EnsemblBacteria; AAB99119; AAB99119; MJ_1118. DR KEGG; mja:MJ_1118; -. DR eggNOG; arCOG02155; Archaea. DR eggNOG; COG1873; LUCA. DR InParanoid; Q58518; -. DR OMA; LIPYKLV; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR027275; PRC-brl_dom. DR InterPro; IPR011033; PRC_barrel-like. DR Pfam; PF05239; PRC; 1. DR SUPFAM; SSF50346; SSF50346; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 89 Uncharacterized protein MJ1118. FT /FTId=PRO_0000107175. SQ SEQUENCE 89 AA; 10034 MW; 7C21C2CCFE6D477D CRC64; MEKMPAKLLF ERSIIGNKGS VIGKVKDIVF DEKVGRLVSL EVEPAEHSPI MREEGRNVLI PYKLVVAIKD VVVIDETNLN RVNIRVAEH // ID Y1123_METJA Reviewed; 205 AA. AC Q58523; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Uncharacterized protein MJ1123; GN OrderedLocusNames=MJ1123; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0638 and MJ1252 and M.tuberculosis CC Rv2003c. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99125.1; -; Genomic_DNA. DR PIR; B64440; B64440. DR ProteinModelPortal; Q58523; -. DR STRING; 243232.MJ_1123; -. DR EnsemblBacteria; AAB99125; AAB99125; MJ_1123. DR KEGG; mja:MJ_1123; -. DR eggNOG; arCOG01773; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q58523; -. DR OMA; AENPKKM; -. DR PhylomeDB; Q58523; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 205 Uncharacterized protein MJ1123. FT /FTId=PRO_0000107178. SQ SEQUENCE 205 AA; 23560 MW; 21791B51CEA3E2B6 CRC64; MNVFDKYAEE YDKWFDENEI IYKSEIEALK RHIPKGRGLE IGVGTGRFAK PFNIKIGVDI SKEMAKIAEK RGIKVIIAKG EDLPFKDEEF DFFLINTVLE FAENPKKMIE EAKRVLKRGG KIIIGIIDRD SFLGKMYEEK KQKSKFYKDA NFLSAKEVIE MLKELGFKNI KATQTIFKEI DKVDKVEVKE GYGEGGFVAI SAEKI // ID Y1141_METJA Reviewed; 214 AA. AC Q58541; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ1141; GN OrderedLocusNames=MJ1141; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99141.1; -; Genomic_DNA. DR PIR; D64442; D64442. DR STRING; 243232.MJ_1141; -. DR EnsemblBacteria; AAB99141; AAB99141; MJ_1141. DR KEGG; mja:MJ_1141; -. DR eggNOG; arCOG02078; Archaea. DR eggNOG; COG1852; LUCA. DR InParanoid; Q58541; -. DR KO; K09729; -. DR OMA; CLRDLKC; -. DR PhylomeDB; Q58541; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002829; DUF116. DR InterPro; IPR017446; Polyprenyl_synth-rel. DR PANTHER; PTHR12001; PTHR12001; 1. DR Pfam; PF01976; DUF116; 1. DR PIRSF; PIRSF006594; UCP006594; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 214 Uncharacterized protein MJ1141. FT /FTId=PRO_0000107186. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. SQ SEQUENCE 214 AA; 24430 MW; AC0C4D0301F95228 CRC64; MISILGLDGF LQLVGMITIA IFALAFISFI LILIISYILL KKNKLIFPSL ALFLMDNLYS ILLKIFLLIG TEDTFYRVGI EFYNKYYEDR FKKAKKRVLI LPHCLRDTKC PAKLTPKGVE CIFCNRCRVG EIIKVAEEKG YKVYIVPGST FLKRILKEEK PEAVFGVACN RDLFYGMNML SRKGIPSQGQ PLLRDGCINT LVDVDELITR LKSL // ID Y1155_METJA Reviewed; 603 AA. AC Q58555; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=UPF0313 protein MJ1155; GN OrderedLocusNames=MJ1155; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC -!- SIMILARITY: Belongs to the UPF0313 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99152.1; -; Genomic_DNA. DR PIR; B64444; B64444. DR ProteinModelPortal; Q58555; -. DR STRING; 243232.MJ_1155; -. DR EnsemblBacteria; AAB99152; AAB99152; MJ_1155. DR KEGG; mja:MJ_1155; -. DR eggNOG; arCOG04984; Archaea. DR eggNOG; COG1032; LUCA. DR InParanoid; Q58555; -. DR OMA; NLNTDHS; -. DR PhylomeDB; Q58555; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0005506; F:iron ion binding; IEA:UniProtKB-HAMAP. DR Gene3D; 3.80.30.20; -; 1. DR HAMAP; MF_01251; UPF0313; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR022946; UPF0313. DR InterPro; IPR024560; UPF0313_C. DR InterPro; IPR013704; UPF0313_N. DR Pfam; PF11842; DUF3362; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF08497; Radical_SAM_N; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03904; SAM_YgiQ; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 603 UPF0313 protein MJ1155. FT /FTId=PRO_0000076404. FT METAL 299 299 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 303 303 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 306 306 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 603 AA; 70425 MW; B3AB76483FEE6444 CRC64; MFLPTTKEEM DEWGWEELDI IIVTGDAYID HYLFGASVVG RYLVEHGYRV GIIAQPDWKN LDDIKRLGKP NYFFAVTAGN LDSMLAHYTP QKRLRDFDSM SNEGIRKRPD RATIVYTNLI KRAFKGVPIA LGGIEASLRR FSHYDYWDNK VRKSVLIDSK ADILMYGMGE KSILAITKAL ESGENIKDLE INGTVVRVNE RKIGDIKERY ETKELPSHEE VVNSKEKYAE MHRKLMTMDK VIYQKVGNQY LVQFPPIYLT EKEMDEIYEM PFERRAHPSY SYVPGIVPVQ FSVVTHRGCF GGCSFCSILH HQGKVIQNRS ERSILKEIRK LLNHEDFKGV IQDIGAPTAN MYRMGCKKGL ADRCPKNCLY PEPCENLIIN HKPLIKLYRK IRDIVGDDVR VYVRSGVRYD LIMYDEEYGE DYIKELSKYH VSGRLKVAPE HISKKVCKAI QKPDGRLFKK FLEKYREIAE KVGGIKEVLP YWLIAHPNCS IKEMIELAEF IHKNNCYSRQ VQVFTPTPMT LSTTMYHTGI NPITNEKVYV PYTYREKKIQ KAICLYREEE NWEKALEGFK MVGYKGVIYR WIMEQMEKKK KQKKDKNKKN RLN // ID Y1170_METJA Reviewed; 89 AA. AC Q58570; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0145 protein MJ1170; GN OrderedLocusNames=MJ1170; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0145 family. Highly divergent. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99172.1; -; Genomic_DNA. DR PIR; A64446; A64446. DR ProteinModelPortal; Q58570; -. DR STRING; 243232.MJ_1170; -. DR EnsemblBacteria; AAB99172; AAB99172; MJ_1170. DR KEGG; mja:MJ_1170; -. DR eggNOG; arCOG02287; Archaea. DR eggNOG; COG0393; LUCA. DR OMA; NYAVPEL; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.110.70; -; 1. DR InterPro; IPR002765; UPF0145. DR Pfam; PF01906; YbjQ_1; 1. DR SUPFAM; SSF117782; SSF117782; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 89 UPF0145 protein MJ1170. FT /FTId=PRO_0000138507. SQ SEQUENCE 89 AA; 9722 MW; 29FAE10A172BABEA CRC64; MILMITSTTD NLEGFKIVKY LGVVIGYGDD PDDALEDLID VAEDMGANAV IGIRISNELT TEIISDENYA VPELTYYAYG TAVIVEKID // ID Y1180_METJA Reviewed; 145 AA. AC Q58580; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1180; GN OrderedLocusNames=MJ1180; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99188.1; -; Genomic_DNA. DR PIR; C64447; C64447. DR ProteinModelPortal; Q58580; -. DR STRING; 243232.MJ_1180; -. DR EnsemblBacteria; AAB99188; AAB99188; MJ_1180. DR KEGG; mja:MJ_1180; -. DR eggNOG; arCOG01803; Archaea. DR eggNOG; COG0715; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 145 Uncharacterized protein MJ1180. FT /FTId=PRO_0000107203. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 145 AA; 16167 MW; 3431CAA205CD66D0 CRC64; MKKIYMLVAL LISSLVLFAG CVQNETSEVP TLTVAYLPTD HHASLFVACD NPDLFKDKYG ICLKAVKDKE EYELYKGNKK IANVKVVKVT EGGASIMNLM TQGQVDVALL GYPPVIFYID KGTKAKVIMN LHTEVLQLLL ERIFQ // ID Y1196_METJA Reviewed; 366 AA. AC Q58596; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Putative amino-acid transporter MJ1196; GN OrderedLocusNames=MJ1196; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC) CC superfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99200.1; -; Genomic_DNA. DR PIR; C64449; C64449. DR ProteinModelPortal; Q58596; -. DR STRING; 243232.MJ_1196; -. DR EnsemblBacteria; AAB99200; AAB99200; MJ_1196. DR KEGG; mja:MJ_1196; -. DR eggNOG; arCOG00009; Archaea. DR eggNOG; COG0531; LUCA. DR InParanoid; Q58596; -. DR OMA; SCAFSVL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015655; F:alanine:sodium symporter activity; IEA:InterPro. DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IBA:GOC. DR GO; GO:0015807; P:L-amino acid transport; IBA:GOC. DR InterPro; IPR002293; AA/rel_permease1. DR InterPro; IPR001463; Na/Ala_symport. DR PANTHER; PTHR11785; PTHR11785; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. DR PRINTS; PR00175; NAALASMPORT. PE 3: Inferred from homology; KW Amino-acid transport; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 366 Putative amino-acid transporter MJ1196. FT /FTId=PRO_0000054254. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. FT TRANSMEM 173 193 Helical. {ECO:0000255}. FT TRANSMEM 205 225 Helical. {ECO:0000255}. FT TRANSMEM 247 267 Helical. {ECO:0000255}. FT TRANSMEM 291 311 Helical. {ECO:0000255}. FT TRANSMEM 314 334 Helical. {ECO:0000255}. FT TRANSMEM 346 366 Helical. {ECO:0000255}. SQ SEQUENCE 366 AA; 40470 MW; 450E9B5DC8EF4C80 CRC64; MGHLTLKDAV FLTITSIVGG GIFVLSPLTY LLFGKSIIWG WALLIFVSLI MASPFAYAST KISESGGVYK FVMKILGREI GVFSAYILWL SGVFALSGVV SFFEIVFNTK FNVSYVGLCL IVILTALILG GLRIVGNFVR IFGILTITII LYIVFSNGIK IDSIGEFNLK NAILTIYFGL WTATGWEGIT MPLSAFKNQK AIAYGLLVGT FIIGVLYLLF SLTIVSLNVK TNNLDEILKI LIGDNLFLLA GMLLIISSCA FSVLFTLSYM PYGMGKDRIF PKAFIKLRKE IPYYGVILNT LLVIILLIFD AKTLVDMSMF STLIAYFLLY LAVFKESSGK IKAISLISML ITGLLILFRV YNFIIL // ID Y120_METJA Reviewed; 233 AA. AC Q57584; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0120; GN OrderedLocusNames=MJ0120; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98101.1; -; Genomic_DNA. DR PIR; H64314; H64314. DR ProteinModelPortal; Q57584; -. DR STRING; 243232.MJ_0120; -. DR EnsemblBacteria; AAB98101; AAB98101; MJ_0120. DR KEGG; mja:MJ_0120; -. DR eggNOG; arCOG01231; Archaea. DR eggNOG; COG0378; LUCA. DR InParanoid; Q57584; -. DR OMA; LSKDMCP; -. DR PhylomeDB; Q57584; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0016151; F:nickel cation binding; IBA:GO_Central. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003495; CobW/HypB/UreG_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF02492; cobW; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 233 Uncharacterized protein MJ0120. FT /FTId=PRO_0000106702. SQ SEQUENCE 233 AA; 25933 MW; 0FE4552D596E0937 CRC64; MKVAIVAGTP GAGKTSVLIH TIRTLINEGY KPVVVKIDCL YTDDDVRYKK LGIPVLVGLS KDMCPDHFAI YNFEEMVDWA KDKGDILLIE TAGLCHRCAP YTKNSLGICV IDATSGPNTP RKVGPFLTSA DIVVITKGDI ISQAEREVFR ERVLEMNPNC RIYEVNGLTG QGCVEIAKEI IESKDIKDLE NEELRHNAPL CICTLCVGET RVSKKYHRGI LRRIDGFMEY EGE // ID Y1216_METJA Reviewed; 121 AA. AC Q58613; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=UPF0331 protein MJ1216; GN OrderedLocusNames=MJ1216; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0331 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99217.1; -; Genomic_DNA. DR PIR; G64451; G64451. DR ProteinModelPortal; Q58613; -. DR STRING; 243232.MJ_1216; -. DR EnsemblBacteria; AAB99217; AAB99217; MJ_1216. DR KEGG; mja:MJ_1216; -. DR eggNOG; arCOG05024; Archaea. DR eggNOG; COG2361; LUCA. DR InParanoid; Q58613; -. DR OMA; WRNIAGM; -. DR PhylomeDB; Q58613; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 121 UPF0331 protein MJ1216. FT /FTId=PRO_0000158263. SQ SEQUENCE 121 AA; 14498 MW; F95805B623D85298 CRC64; MPKRDIKAFL YDILEYMDDI INFTKNMEYE EFINNKAIKY AVVRCLEVIG EAVKKIPKDI REKYPHIPFK ELAGMRDKLI HQYFGVDYLT VWETAKYEIP EIKKEFEKII KDIEGKDENS L // ID Y1218_METJA Reviewed; 425 AA. AC Q58615; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1218; GN OrderedLocusNames=MJ1218; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99219.1; -; Genomic_DNA. DR PIR; A64452; A64452. DR ProteinModelPortal; Q58615; -. DR STRING; 243232.MJ_1218; -. DR REBASE; 3904; S.MjaORF1220P. DR EnsemblBacteria; AAB99219; AAB99219; MJ_1218. DR KEGG; mja:MJ_1218; -. DR eggNOG; arCOG02626; Archaea. DR eggNOG; COG0732; LUCA. DR InParanoid; Q58615; -. DR KO; K01154; -. DR OMA; RIPREWE; -. DR PhylomeDB; Q58615; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 425 Uncharacterized protein MJ1218. FT /FTId=PRO_0000107220. SQ SEQUENCE 425 AA; 49410 MW; 5681C338F957C49F CRC64; MVIIMQFYKE ENFKEMHGLR VPEDWEVVRI GDFIKYIKGK KPAVMVDEEL EGYYPYLSTE YLRDGIASKF VKITNKEIIV NENDILLLWD GSNAGEIFLG KKGILSSTMV KLEQKNKIMD DLYLFYSLKL KESFLKSQTK GTGIPHVDKK IFENIKIPLP PLEEQKQIAK ILSDFDNLIG TINKQIEVLN KAKKGMMKKL FTKGVFEHKS FKKSEIGEIP EDWEVVKLKE VVDIQSGKYF KYSEFCENGV KCLKIDNVGF GKIFWETVSF LPEDYLNKYP QLVLKSGDIV LALNRPIIGG KIKIGILKDI DEPAILYQRV GRFIFKSEKI DKQFLFYLLM SEYFKKELSK LLIGTDQPYI RTPVLLNIKI PLPHLEEQKA MAERLKSIDN LIEIKRKEKE QIEKAKKKIM NLLLTGKIRV KNLNF // ID Y121_METJA Reviewed; 261 AA. AC Q57585; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0121; GN OrderedLocusNames=MJ0121; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98102.1; -; Genomic_DNA. DR PIR; A64315; A64315. DR ProteinModelPortal; Q57585; -. DR STRING; 243232.MJ_0121; -. DR EnsemblBacteria; AAB98102; AAB98102; MJ_0121. DR KEGG; mja:MJ_0121; -. DR eggNOG; arCOG03228; Archaea. DR eggNOG; COG1136; LUCA. DR InParanoid; Q57585; -. DR OMA; DIECMAQ; -. DR PhylomeDB; Q57585; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 261 Uncharacterized ABC transporter ATP- FT binding protein MJ0121. FT /FTId=PRO_0000093218. FT DOMAIN 1 236 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 36 43 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 261 AA; 29262 MW; 6C26F1CBEB2FE5A2 CRC64; MEIKEITIIG GYDKNGNPEP VREVTIKRGE IVGVVGPTGS GKSNLISDIE QLAQGDTISK RRILVNGEVP PIEMRRDPKK RRIAQLSQNM NFLADMTVEE FILMHAKSRG VYRENIVDEV IELANRLTGE PIKKDYNLTI LSGGQSRSLM VADVAVISDS PIVLIDEIEN AGIKKHEALE LLAGYGKIVL VITHDPVLAL MTDRRIVMRN GGMQKIIETT EEEKEISRKI NEVDNWLLSL REKIRFGERL THEDISLMVK G // ID Y1220_METJA Reviewed; 578 AA. AC Q58617; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized adenine-specific methylase MJ1220; DE EC=2.1.1.72; GN OrderedLocusNames=MJ1220; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99225.1; -; Genomic_DNA. DR PIR; C64452; C64452. DR ProteinModelPortal; Q58617; -. DR STRING; 243232.MJ_1220; -. DR REBASE; 3905; M.MjaORF1220P. DR PRIDE; Q58617; -. DR EnsemblBacteria; AAB99225; AAB99225; MJ_1220. DR KEGG; mja:MJ_1220; -. DR eggNOG; arCOG02632; Archaea. DR eggNOG; COG0286; LUCA. DR InParanoid; Q58617; -. DR KO; K03427; -. DR OMA; ELAKGDM; -. DR PhylomeDB; Q58617; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR022749; D12N6_MeTrfase_N. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF12161; HsdM_N; 1. DR Pfam; PF02384; N6_Mtase; 1. DR SUPFAM; SSF53335; SSF53335; 2. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 578 Uncharacterized adenine-specific FT methylase MJ1220. FT /FTId=PRO_0000088001. FT REGION 280 282 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 303 303 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 578 AA; 66638 MW; 5339ED873EF8E9E2 CRC64; MKLRNVEPRF LKAYNILMDK FGLFPFTYDM AEKVLKDNYE NVNEVLSKLA DAGLLEKTAK KEDKRKKIYK IKPLTTEKIE KVSKDKLIGL LKQGADLIRT QVDYKVLLLF LFFKAISDKY LLKVEELKKE FEDLDEEDIY VLANEEILEL YDVEGKKLYV WHEVANNPED FINALNKIVE MNKEKLSGLD ELIKRTGLPT LFENENRHIV QHLINLFSRA DFSEASYDIL GDAYEWTLNY FAPTKAKEGE VYTPIEVSKL IAHLVEPKDD EVILDPACGS GSMLIEQYRF AGSNPNIVLV GQERNDVTAV LAKLNFILHG INLKDAKVFI GDSLLNPKFE SFIXEVKGTG KADKVVANPP WNQDGYDENT LKVNEKYKDI YMYGFPNKNS ADWAWVQLIN YYTEKKAGIV LDSGALFRGG KEKTIRKRFV DDDLIEAVVL LPEKLFYNCP APGIILILNK NKPEERKGKI LFINASNEYI KHPEVKKLNK LSDENIEKIA KAYKEFKDVD GFCKVVDIEE IRKNDYNLNV SLYISPIEED EDVDLGEVYE ELNKLHNEYL EKFEVVKGYL EEINGLIK // ID Y1233_METJA Reviewed; 288 AA. AC Q58630; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ1233; GN OrderedLocusNames=MJ1233; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99243.1; -; Genomic_DNA. DR PIR; H64453; H64453. DR ProteinModelPortal; Q58630; -. DR STRING; 243232.MJ_1233; -. DR EnsemblBacteria; AAB99243; AAB99243; MJ_1233. DR KEGG; mja:MJ_1233; -. DR eggNOG; arCOG00054; Archaea. DR eggNOG; COG2521; LUCA. DR InParanoid; Q58630; -. DR KO; K06983; -. DR OMA; GIRMHRT; -. DR PhylomeDB; Q58630; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008757; F:S-adenosylmethionine-dependent methyltransferase activity; IBA:GO_Central. DR GO; GO:0032259; P:methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 288 Uncharacterized protein MJ1233. FT /FTId=PRO_0000107229. SQ SEQUENCE 288 AA; 32912 MW; E8050E04ECF009DA CRC64; MSKITLVLTM NYITSKIAKE ILNSQSEEIF LNLDLNKTEK KEKILIDREK KIAKFPEGDV SFDILKKIAK DEGHIYFIKD GEVFKAAISN NGYYKLVPTI PPTIEINGIR MHRTKEVNPY EDTLNKINAV KVKKGEKVLD TCMGLGYTAI EAYRRGAEVI TIEKNPNVLE LAKINPYSEE LFKGGIKIIL GDAYDVIKRF KDEEFDVVIH DPPRFSLAGH LYSEEFYKEI FRVLKPGGRL FHYVGNPGKK YRGKDLQKGV MERLRKVGFV NVKRVEEALG VVAVKPRD // ID Y1257_METJA Reviewed; 349 AA. AC Q58654; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1257; GN OrderedLocusNames=MJ1257; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00529}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99268.1; -; Genomic_DNA. DR PIR; H64456; H64456. DR ProteinModelPortal; Q58654; -. DR STRING; 243232.MJ_1257; -. DR EnsemblBacteria; AAB99268; AAB99268; MJ_1257. DR KEGG; mja:MJ_1257; -. DR eggNOG; arCOG00056; Archaea. DR eggNOG; COG0293; LUCA. DR eggNOG; COG1818; LUCA. DR InParanoid; Q58654; -. DR KO; K06963; -. DR OMA; IIHIKKR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002877; rRNA_MeTrfase_FtsJ_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF01728; FtsJ; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 349 Uncharacterized protein MJ1257. FT /FTId=PRO_0000107243. FT DOMAIN 51 160 THUMP. {ECO:0000255|PROSITE- FT ProRule:PRU00529}. SQ SEQUENCE 349 AA; 41198 MW; D0A061A05D8CA5C7 CRC64; MKPVALVTTK PGFEPQLREE LNKLPIKKKI LWTPFRGILK VLSQNPYEFL NIIKENKNNL KFSLRIIPLE IGCQTDINEI KKAISFLINK KKEKLKNKSF VVRCNRRGNH EFTSEELERI IGEYVLENFK DLNLRVNLKD WDFKINIEIL QDESYISIFQ DEFNELVIEE NIKNLKNLKR YIERPLNRSE RKMQELMEKF PFIFENINCV VDIGSSPGGW AKMLSKKAKK VYAIDTGELK IKANNIIHIK KRAENVDFEK DINEEIDLIT NDTNLYPDES LFLTLKFAKH LKTNGYIIHT LKARNLKTKK EDLEKVLKIL SYYRNIKIFK IINLRANTKN ELTLILKKV // ID Y126_METJA Reviewed; 98 AA. AC Q57590; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0126; GN OrderedLocusNames=MJ0126; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98106.1; -; Genomic_DNA. DR ProteinModelPortal; Q57590; -. DR STRING; 243232.MJ_0126; -. DR EnsemblBacteria; AAB98106; AAB98106; MJ_0126. DR KEGG; mja:MJ_0126; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q57590; -. DR KO; K07075; -. DR OMA; YTEPPSL; -. DR PhylomeDB; Q57590; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein MJ0126. FT /FTId=PRO_0000106705. SQ SEQUENCE 98 AA; 11605 MW; 0748F07131F29685 CRC64; MKTLSEIKEI LRKHKKELKE KYKVKSIAIF GSYARNEQTE TSDIDILIDY YEPISLLKLI ELENYLSDLL EIKVDLITKN SIHNPYVKKS IEEDLIYI // ID Y1286_METJA Reviewed; 595 AA. AC Q58682; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1286; GN OrderedLocusNames=MJ1286; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii FlaJ. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99288.1; -; Genomic_DNA. DR PIR; E64460; E64460. DR STRING; 243232.MJ_1286; -. DR PRIDE; Q58682; -. DR EnsemblBacteria; AAB99288; AAB99288; MJ_1286. DR KEGG; mja:MJ_1286; -. DR eggNOG; arCOG01808; Archaea. DR eggNOG; COG2064; LUCA. DR InParanoid; Q58682; -. DR KO; K07333; -. DR OMA; IFVFYPE; -. DR PhylomeDB; Q58682; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR018076; T2SS_F. DR Pfam; PF00482; T2SSF; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 595 Uncharacterized protein MJ1286. FT /FTId=PRO_0000107254. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 239 259 Helical. {ECO:0000255}. FT TRANSMEM 281 301 Helical. {ECO:0000255}. FT TRANSMEM 334 354 Helical. {ECO:0000255}. FT TRANSMEM 368 388 Helical. {ECO:0000255}. FT TRANSMEM 504 524 Helical. {ECO:0000255}. FT TRANSMEM 547 567 Helical. {ECO:0000255}. FT TRANSMEM 571 591 Helical. {ECO:0000255}. SQ SEQUENCE 595 AA; 68277 MW; 9008BF01EECAC3DC CRC64; MKNLLKRYVS IKNIIKVIEL DFFANLKLRY YKLAMKLFKI EDEKFDEILL KAGMNAVSST YLPVVFLTSI ILGLIIFIIF LIVFNIFYAI FGLIGGIFIV ILIGVLYPYV LAEEKAKSID ENLPYAFAFI SALSSANIPV VEIFTSLSKE DIYGGMSKEA KEIVKDTKVF NYDIITTFLR RARITPSKKL SSVYYNIVAS LIVGAEMKNI FHEIYERLME DRKLELFEAI EKVEILSEFY VIACGMIPLF VVMTVPVASS ISAILQTASL FGDPKLLPLT FYLWVPIASI IFMGLVYGIL PKDFKLNVSL LDVLKEFDEP EIEGIKMKFK WKPVHFITLF FWMLSIISFM LFFIRKSIFK FHGTDFLMFG ILFLILPFIL TSYWHFIIEN QKERYYPIFL NDLTMAVRSG MDIIRAMQVC ARTNYGPLTK IVKKMAIQMS WGRPVNEVFA DLERTEKSLI AKRIASILKE CAVSGGDVKD ILTSVTVHAY KLSEMKREIS ARQFIYVVVI YLSFFLYIGT SYIMVHSLLP TLLKNIHGLS VEFYKNYLFQ GILIYSIFSG ASLGILTERS IIAGIKHILL MLIVGYMLFK FYIGG // ID Y1289_METJA Reviewed; 165 AA. AC Q58685; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1289; GN OrderedLocusNames=MJ1289; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99295.1; -; Genomic_DNA. DR PIR; H64460; H64460. DR STRING; 243232.MJ_1289; -. DR EnsemblBacteria; AAB99295; AAB99295; MJ_1289. DR KEGG; mja:MJ_1289; -. DR eggNOG; arCOG08272; Archaea. DR eggNOG; ENOG411114S; LUCA. DR OMA; LINDVIC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 165 Uncharacterized protein MJ1289. FT /FTId=PRO_0000107256. FT TRANSMEM 9 29 Helical. {ECO:0000255}. SQ SEQUENCE 165 AA; 19092 MW; 8D4833D9C8DDB10D CRC64; MNTYLSTLLV LTTIFALSII AYEWGINIID TTLNQVSKEK EKNRIEIIKN LINDVIYSGV DSERTFDETK ITLKENNVKI SNGTKYVSFN ITTIEGIDYD VYLEKGTLYI FIYNISAQCP NVYYIKYTNL SIYEFGGNIT INYSDNLRHF YVNNSKVYVY SLLMG // ID Y1317_METJA Reviewed; 398 AA. AC Q58713; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized MFS-type transporter MJ1317; GN OrderedLocusNames=MJ1317; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the major facilitator superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99324.1; -; Genomic_DNA. DR PIR; D64464; D64464. DR ProteinModelPortal; Q58713; -. DR STRING; 243232.MJ_1317; -. DR EnsemblBacteria; AAB99324; AAB99324; MJ_1317. DR KEGG; mja:MJ_1317; -. DR eggNOG; arCOG00130; Archaea. DR eggNOG; COG0477; LUCA. DR InParanoid; Q58713; -. DR OMA; TESKIVQ; -. DR PhylomeDB; Q58713; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011701; MFS. DR InterPro; IPR020846; MFS_dom. DR Pfam; PF07690; MFS_1; 1. DR SUPFAM; SSF103473; SSF103473; 1. DR PROSITE; PS50850; MFS; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 398 Uncharacterized MFS-type transporter FT MJ1317. FT /FTId=PRO_0000084886. FT TRANSMEM 43 65 Helical. {ECO:0000255}. FT TRANSMEM 89 108 Helical. {ECO:0000255}. FT TRANSMEM 156 173 Helical. {ECO:0000255}. FT TRANSMEM 180 198 Helical. {ECO:0000255}. FT TRANSMEM 224 246 Helical. {ECO:0000255}. FT TRANSMEM 259 281 Helical. {ECO:0000255}. FT TRANSMEM 291 311 Helical. {ECO:0000255}. FT TRANSMEM 316 338 Helical. {ECO:0000255}. FT TRANSMEM 351 373 Helical. {ECO:0000255}. FT TRANSMEM 380 397 Helical. {ECO:0000255}. SQ SEQUENCE 398 AA; 44097 MW; 99CBE61675FD7D06 CRC64; MVRKVAEQNL QKNNENDREL SKNVYLLGFT SFLNDMSSEM IMPILPMLIT SVGGGSLSIG LVGGLREFIS NILMVLIGYC SDKVRKRKIF VVLGYLTSSM FKLLLGLSKS WLGAVIFSSL ERMGKGIRTA PRDAIISESM PKTLGKGFGI QRAFDTAGAI LGSTLSLLFI LYLQYSFNQI ILIAAVIGFL TLIPLYFVKE KPSPSNNKIT FRVGIKNLPK ELKLFILISA IFTLSNFSYM FYILRAQEFL MIVDEKMAII IPIALYILYN IFYATFSIPF GILSDKIGRK SVLTIGYIVY GIVSLGFAYF ISQKSLILLF ALYGIAYALF AGNQKAYVSD LSSEDIRATA LGLFYTVVGL TSLPASLIAG YLWKISPEMT FLYGSVLAII SGLLLLFI // ID Y1319_METJA Reviewed; 492 AA. AC Q58715; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized sodium-dependent transporter MJ1319; GN OrderedLocusNames=MJ1319; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative sodium-dependent transporter. CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein. CC -!- SIMILARITY: Belongs to the sodium:neurotransmitter symporter (SNF) CC (TC 2.A.22) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99329.1; -; Genomic_DNA. DR PIR; F64464; F64464. DR ProteinModelPortal; Q58715; -. DR STRING; 243232.MJ_1319; -. DR TCDB; 2.A.22.5.1; the neurotransmitter:sodium symporter (nss) family. DR EnsemblBacteria; AAB99329; AAB99329; MJ_1319. DR KEGG; mja:MJ_1319; -. DR eggNOG; arCOG04466; Archaea. DR eggNOG; COG0733; LUCA. DR InParanoid; Q58715; -. DR KO; K03308; -. DR OMA; SKWGFIL; -. DR PhylomeDB; Q58715; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005328; F:neurotransmitter:sodium symporter activity; IEA:InterPro. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR000175; Na/ntran_symport. DR PANTHER; PTHR11616; PTHR11616; 2. DR Pfam; PF00209; SNF; 2. DR PRINTS; PR00176; NANEUSMPORT. DR PROSITE; PS00610; NA_NEUROTRAN_SYMP_1; 1. DR PROSITE; PS50267; NA_NEUROTRAN_SYMP_3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Symport; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 492 Uncharacterized sodium-dependent FT transporter MJ1319. FT /FTId=PRO_0000214820. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 97 117 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 222 242 Helical. {ECO:0000255}. FT TRANSMEM 258 278 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 359 379 Helical. {ECO:0000255}. FT TRANSMEM 391 411 Helical. {ECO:0000255}. FT TRANSMEM 428 448 Helical. {ECO:0000255}. FT TRANSMEM 463 483 Helical. {ECO:0000255}. SQ SEQUENCE 492 AA; 53468 MW; A4CEF33AC40D4DB9 CRC64; MSYMERESWS SNLGFILASV GSAIGLGNIW RFGYMVYTNG GGAFLIPYIV ALLCVGIPLM ILEFAIGHYT KKSAPLALEK LHKGSEWTGW FAVISGFIIT SYYVVIIAWC LYYLIILVIY GYPSDPNAYF FHNILQISSG VEDIGGVSYG ILVSTLAVWG IVALILSAGI KNGLEKANKI MIPFLLFLII LLVLNALTLP GALTGIEWYL TPDFSALFNY NVWLSAFSQI FFSLSLGFGI LIAYASYLPK KSDLTINAVT VSLLNCGFSF LAGFAVFGTL GYMSYTSGIP LDKAVSEGIG LAFVTFPKAL SLLPFASRLF GIVFFLALVF AGISSAVSIV EASVSAIIDK FSLSRKKALL AVLALFIIIS PIFTTGAGLY YLDIIDHFAS GYLLPIAAIL EIIIAIWLFG GDKLREHVNK LSEIKLGVWW KYLAGVVSPI ILTAVVFLDA SNVLTSGYGG YKTTYVIFGA LIIPLAFVVS VILQKMKTIK GW // ID Y1325_METJA Reviewed; 89 AA. AC Q58721; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ1325; GN OrderedLocusNames=MJ1325; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99335.1; -; Genomic_DNA. DR PIR; D64465; D64465. DR ProteinModelPortal; Q58721; -. DR STRING; 243232.MJ_1325; -. DR EnsemblBacteria; AAB99335; AAB99335; MJ_1325. DR KEGG; mja:MJ_1325; -. DR eggNOG; arCOG01681; Archaea. DR eggNOG; COG0640; LUCA. DR InParanoid; Q58721; -. DR KO; K03892; -. DR OMA; WNYYYIV; -. DR PhylomeDB; Q58721; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR PRINTS; PR00778; HTHARSR. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 89 Uncharacterized HTH-type transcriptional FT regulator MJ1325. FT /FTId=PRO_0000160634. FT DOMAIN 1 89 HTH arsR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. SQ SEQUENCE 89 AA; 10292 MW; 33AFC876DCD861F9 CRC64; MEKYEKAAEI FKAFGDPTRL MILKLLAENG SMCVCKIIDE LKKPQPTISH HLNILKKAGI VKARKEGTWN FYYIVDDRVK EIIKLVDEL // ID Y1341_METJA Reviewed; 312 AA. AC Q58737; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1341; GN OrderedLocusNames=MJ1341; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99351.1; -; Genomic_DNA. DR PIR; D64467; D64467. DR ProteinModelPortal; Q58737; -. DR EnsemblBacteria; AAB99351; AAB99351; MJ_1341. DR KEGG; mja:MJ_1341; -. DR eggNOG; arCOG00116; Archaea. DR eggNOG; ENOG4111GHT; LUCA. DR OMA; IINCEYG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR SUPFAM; SSF53383; SSF53383; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 312 Uncharacterized protein MJ1341. FT /FTId=PRO_0000107285. SQ SEQUENCE 312 AA; 35425 MW; 8D01DAB275CDB249 CRC64; MILKHRRPNI YGLMNKEGNK EEVEMIINEL LNRDYKITFL PSGSSAVFLS MWIAKIYSNE ISIPDMGGWQ GFLKFPKLLN LKNNMIETNL GIIDLEKLDE SLKENSSLIL TSLAGYLAPQ PLKEIKKLCE EREVLFIEDI SGKIGGDCGY GDIVVCSTGT PKILNCEYGG FLGISKEIEE KLGNALNDIK ILSKTYKTIN YFGLLKEELL NAKKTYKKYV EASKIIKDEI ENAYFREFEG ISVFIECDNP KNISKKINSL IKLDNRKSIT TICPNYDRIL KNGIVFETKK IDISELNREV INEIIIALSS IL // ID Y1349_METJA Reviewed; 360 AA. AC Q58744; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized protein MJ1349; GN OrderedLocusNames=MJ1349; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 4Fe-4S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99357.1; -; Genomic_DNA. DR PIR; D64468; D64468. DR ProteinModelPortal; Q58744; -. DR STRING; 243232.MJ_1349; -. DR EnsemblBacteria; AAB99357; AAB99357; MJ_1349. DR KEGG; mja:MJ_1349; -. DR eggNOG; arCOG02650; Archaea. DR eggNOG; COG1035; LUCA. DR InParanoid; Q58744; -. DR KO; K00441; -. DR OMA; PCGACYE; -. DR PhylomeDB; Q58744; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR007525; FrhB_FdhB_C. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 360 Uncharacterized protein MJ1349. FT /FTId=PRO_0000159228. FT DOMAIN 11 40 4Fe-4S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. SQ SEQUENCE 360 AA; 40099 MW; 4F0046D70AA3482F CRC64; MRLMKSYKNL KEEVWDTNRC SGCGACVAVC PVNNLYFREE SPVKFECDEC SCIIVPADIV EHPISAEFCK TVVYDVPCGA CYDACPRIKK SAIPKPKGLG NILKAVRAKA SIEIKNAQNG GVVTAILANA FDEGLIDGAI VMMDDKWTLE PESYLALSKE DVLKSAGSKY LWKGPILKAL KTAVMEKKLK KLAVVGTPCV INAIYQILSS DNDLLKPFRE AIRLKIALFC FETYDYSKMI KKLNEDGIEP WEVKKMDIES GKLKITLING NTVEYKLKDV ESAMRNGCKV CGDFTGLTSD ISVGNVGTEK GYSTVLIRNK WGEGFFKRAV YNGYITYDEN VDLEAVEKLV ELKKKRVKKD // ID Y1362_METJA Reviewed; 322 AA. AC Q58757; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ1362; GN OrderedLocusNames=MJ1362; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99370.1; -; Genomic_DNA. DR PIR; A64470; A64470. DR ProteinModelPortal; Q58757; -. DR STRING; 243232.MJ_1362; -. DR EnsemblBacteria; AAB99370; AAB99370; MJ_1362. DR KEGG; mja:MJ_1362; -. DR eggNOG; arCOG01545; Archaea. DR eggNOG; COG0650; LUCA. DR KO; K14124; -. DR OMA; FPFYLAT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR Pfam; PF00146; NADHdh; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 322 Uncharacterized protein MJ1362. FT /FTId=PRO_0000107299. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 189 209 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 268 288 Helical. {ECO:0000255}. FT TRANSMEM 300 320 Helical. {ECO:0000255}. SQ SEQUENCE 322 AA; 35835 MW; CDF313E6C717C90A CRC64; MIDELISIIG IPALAFAIST YIPGIQRKIE ARIQQRIGPS ILAPGFWAFF KFLFKETKAP DANLPKLYNL LPLLSIVVLW ALLSITSLTS FHILSNEIGI VGLLKLEEMM YVILGSLAFS IMGWKMPFID ECKGTPFIKT LKLSLEQLGA VRSFKMITIG SFPFYLATFL PFVQKKSIFL KDIVGEPFLF SLAGIFGAAC YFIGYVIMIK EYPFSITHTK ADVIEGPTME LIAKYRALYL ASKELLLIAL GSLFATLYLG IAPDIENPIT IVENFAIALI FPILATFVRA FSPVLLFKQI YPISYVATLI GVIGFIFALL GW // ID Y1384_METJA Reviewed; 198 AA. AC Q58779; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Putative nitroreductase MJ1384; DE EC=1.-.-.-; GN OrderedLocusNames=MJ1384; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=FMN; Xref=ChEBI:CHEBI:58210; Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the nitroreductase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99394.1; -; Genomic_DNA. DR PIR; G64472; G64472. DR ProteinModelPortal; Q58779; -. DR STRING; 243232.MJ_1384; -. DR EnsemblBacteria; AAB99394; AAB99394; MJ_1384. DR KEGG; mja:MJ_1384; -. DR eggNOG; arCOG00288; Archaea. DR eggNOG; COG0778; LUCA. DR InParanoid; Q58779; -. DR OMA; RYVHMEV; -. DR PhylomeDB; Q58779; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.109.10; -; 1. DR InterPro; IPR029479; Nitroreductase. DR InterPro; IPR000415; Nitroreductase-like. DR InterPro; IPR020051; SagB-type_dehydrogenase. DR Pfam; PF00881; Nitroreductase; 1. DR SUPFAM; SSF55469; SSF55469; 1. DR TIGRFAMs; TIGR03605; antibiot_sagB; 1. PE 3: Inferred from homology; KW Complete proteome; Flavoprotein; FMN; Oxidoreductase; KW Reference proteome. FT CHAIN 1 198 Putative nitroreductase MJ1384. FT /FTId=PRO_0000072720. SQ SEQUENCE 198 AA; 22403 MW; 7737D2E2DED8E8A6 CRC64; MGDTMEIQLP DIEEIKLEDV LIKRRSVREY CSSPLTLREL SHILFAAYGV TDERGFKTVP SAGATYPLEI YVNVRDVVGV EEGVYKYIPE RHSIVRILDE EVGHELALAA LKQMFIAIAP IVLIIAANYE RTTRVYGDRG FRYVHMEVGH VAQNVYLMAT SLGLGTVSVG AFYDNEIREI LKIKEYPLLL MPVGRKIE // ID Y1387_METJA Reviewed; 379 AA. AC Q58782; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0272 protein MJ1387 {ECO:0000255|HAMAP-Rule:MF_01074}; GN OrderedLocusNames=MJ1387; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0272 family. {ECO:0000255|HAMAP- CC Rule:MF_01074}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99396.1; -; Genomic_DNA. DR PIR; B64473; B64473. DR ProteinModelPortal; Q58782; -. DR STRING; 243232.MJ_1387; -. DR EnsemblBacteria; AAB99396; AAB99396; MJ_1387. DR KEGG; mja:MJ_1387; -. DR eggNOG; arCOG02701; Archaea. DR eggNOG; COG1641; LUCA. DR InParanoid; Q58782; -. DR KO; K09121; -. DR OMA; EVAKIIM; -. DR PhylomeDB; Q58782; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01074; UPF0272; 1. DR InterPro; IPR002822; UPF0272. DR Pfam; PF01969; DUF111; 1. DR TIGRFAMs; TIGR00299; TIGR00299; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 379 UPF0272 protein MJ1387. FT /FTId=PRO_0000146860. SQ SEQUENCE 379 AA; 42868 MW; 9BDB73BE619B4EFD CRC64; MFLLDPFSGI SGDMFLSAMI DFVDKEDFIN TIKKVIDVEI EIKKVKKCHI LANKVNIIPK CINCNANTYK DIKNVIKSSD IQEDIKITAL EILKILAEAE SKVHNVDVEN VHFHEVGNYD TIADIVGAAY IINKLNLKNN CLYKPINVGN GFVRTEHGLL PVPAPATAEI LKGLKIFFSD INEELTTPTG SAIIKYINPK LAKGAFIIKE VSYGAGDKDL NLLNALRVFR VEDIKREDIV LLETNVDDIS AEILGYLYEV LDGKVRDLHF IPTYMKKNRP AYTIRAIVDR DIAEEVAKII MRETGSLGVR IFDIERITAD REFKTIKLFD ESVRLKVGRV NDEIISQKPE FEDLKNIAKK YGIPLKDLYK LINISQIKN // ID Y1413_METJA Reviewed; 103 AA. AC Q58808; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=UPF0145 protein MJ1413; GN OrderedLocusNames=MJ1413; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0145 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99420.1; -; Genomic_DNA. DR PIR; D64476; D64476. DR ProteinModelPortal; Q58808; -. DR STRING; 243232.MJ_1413; -. DR EnsemblBacteria; AAB99420; AAB99420; MJ_1413. DR KEGG; mja:MJ_1413; -. DR eggNOG; arCOG02287; Archaea. DR eggNOG; COG0393; LUCA. DR InParanoid; Q58808; -. DR OMA; RVGAYES; -. DR PhylomeDB; Q58808; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.110.70; -; 1. DR HAMAP; MF_00338; UPF0145; 1. DR InterPro; IPR002765; UPF0145. DR Pfam; PF01906; YbjQ_1; 1. DR SUPFAM; SSF117782; SSF117782; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 103 UPF0145 protein MJ1413. FT /FTId=PRO_0000138495. SQ SEQUENCE 103 AA; 11233 MW; 77029876B2B94E17 CRC64; MGGMITTTTP YIEGKKIIKY LGFVHGVASV YVTVKYYEDV KDAYERALRE SEDTALIRMV DNAKKLGANA IIGINSNYAM VGEKGDMIMV GIYGTAVVVE EDG // ID Y1436_METJA Reviewed; 97 AA. AC Q58831; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1436; GN OrderedLocusNames=MJ1436; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH1236. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99445.1; -; Genomic_DNA. DR PIR; C64479; C64479. DR STRING; 243232.MJ_1436; -. DR EnsemblBacteria; AAB99445; AAB99445; MJ_1436. DR KEGG; mja:MJ_1436; -. DR eggNOG; arCOG04876; Archaea. DR eggNOG; ENOG41123J5; LUCA. DR KO; K14125; -. DR OMA; DDFVGLF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019597; Energy-convert_hydgase-B_suP. DR Pfam; PF10622; Ehbp; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ1436. FT /FTId=PRO_0000107327. SQ SEQUENCE 97 AA; 11265 MW; FD1065C09E68AB4D CRC64; MPKMVLLPRM TMALGGYIRE TTFPYEEDDE VKPFPYRNVI VGNPTDEPIK IEVPAYNEGW IERHKKLGLI VVPVNEDDDF VGLFQMVKEK VKNAKRE // ID Y1457_METJA Reviewed; 135 AA. AC Q58852; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1457; GN OrderedLocusNames=MJ1457; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99470.1; -; Genomic_DNA. DR PIR; H64481; H64481. DR STRING; 243232.MJ_1457; -. DR EnsemblBacteria; AAB99470; AAB99470; MJ_1457. DR KEGG; mja:MJ_1457; -. DR eggNOG; arCOG11086; Archaea. DR eggNOG; ENOG41111R0; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 135 Uncharacterized protein MJ1457. FT /FTId=PRO_0000107345. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. SQ SEQUENCE 135 AA; 14508 MW; E69A4F18B630A92D CRC64; MMVMTALTLL ILFFGLAFIL VGFGLILGYL IFSRKNKTVN GTANRTVVVE RDSSNLLGTA AAVAGGVIAG ELITDAIEDV INNNENNEAD GYNSEGIETT IEDTIEEIDK GVDNVIEDIT DEIDNITNDI GDSFF // ID Y1461_METJA Reviewed; 199 AA. AC Q58856; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ1461; GN OrderedLocusNames=MJ1461; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1356. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99475.1; -; Genomic_DNA. DR PIR; D64482; D64482. DR STRING; 243232.MJ_1461; -. DR EnsemblBacteria; AAB99475; AAB99475; MJ_1461. DR KEGG; mja:MJ_1461; -. DR eggNOG; arCOG09682; Archaea. DR eggNOG; ENOG4110ZR4; LUCA. DR OMA; FERMGIN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 199 Uncharacterized protein MJ1461. FT /FTId=PRO_0000107350. SQ SEQUENCE 199 AA; 23821 MW; B2E07FCE421FF069 CRC64; MEQFDFDSIF NNAVGNMKYF IKKVKKYEEI KKHEDILKKD LLNAVNVFIE RFRNNPCICK NRNNHSSCTT NACGEIENRM KNWVEKLFEY SDDEEKLNEF FKIIAKDAMK FVELDFEPLY ILCGLEEIRE TAEEKLKEEL PTEEYLKVME EFDDLIERMS LVATAVYMEF EDRVFERMGI NKNLKYNIIK LGLKKMNIN // ID Y1464_METJA Reviewed; 373 AA. AC Q58859; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized GTP-binding protein MJ1464; GN OrderedLocusNames=MJ1464; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TRAFAC class YlqF/YawG GTPase family. CC {ECO:0000255|PROSITE-ProRule:PRU01058}. CC -!- SIMILARITY: Contains 1 CP-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01058}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99472.1; -; Genomic_DNA. DR PIR; G64482; G64482. DR ProteinModelPortal; Q58859; -. DR STRING; 243232.MJ_1464; -. DR EnsemblBacteria; AAB99472; AAB99472; MJ_1464. DR KEGG; mja:MJ_1464; -. DR eggNOG; arCOG00350; Archaea. DR eggNOG; COG1161; LUCA. DR InParanoid; Q58859; -. DR OMA; FPFINDA; -. DR PhylomeDB; Q58859; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR GO; GO:0003924; F:GTPase activity; IBA:GO_Central. DR GO; GO:0042254; P:ribosome biogenesis; IBA:GO_Central. DR Gene3D; 1.10.1580.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR030378; G_CP_dom. DR InterPro; IPR023179; GTP-bd_ortho_bundle. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01926; MMR_HSR1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51721; G_CP; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 373 Uncharacterized GTP-binding protein FT MJ1464. FT /FTId=PRO_0000205447. FT DOMAIN 14 168 CP-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01058}. FT NP_BIND 117 124 GTP. {ECO:0000255}. SQ SEQUENCE 373 AA; 42635 MW; 469F4A1FF9111640 CRC64; MMVRVMRYKK VPVKKIVNKI IDECDVILLV LDARDPEMTR NRELEKKIKA KGKKLIYVLN KADLVPKDIL EKWKEVFGEN TVFVSAKRRL GTKILREMIK QSLKEMGKKE GKVGIVGYPN VGKSSIINAL TGKRKALTGS VAGLTKGEQW VRLTKNIKLM DTPGVLEMRD EDDLVISGAL RLEKVENPIP PALKILSRIN NFDNSIIKEY FGVDYEEVDE ELLKKIGNKR SYLTKGGEVD LVRTAKTIIK EYQDGKLNYY KVDLKKYGQD RERDISFITK YLKDFPFIED AKMIVTHLKD FDGLYKKIKK PVLGSEEIDG NIVVVSFGEK TKDACRKKVE NLCRERNIEV LSKFGDKIGA NNIYVAVGKR VKE // ID Y1467_METJA Reviewed; 184 AA. AC Q58862; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1467; GN OrderedLocusNames=MJ1467; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99483.1; -; Genomic_DNA. DR PIR; B64483; B64483. DR ProteinModelPortal; Q58862; -. DR STRING; 243232.MJ_1467; -. DR EnsemblBacteria; AAB99483; AAB99483; MJ_1467. DR KEGG; mja:MJ_1467; -. DR eggNOG; arCOG06584; Archaea. DR eggNOG; ENOG410YJRP; LUCA. DR OMA; NITICKE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 184 Uncharacterized protein MJ1467. FT /FTId=PRO_0000107353. SQ SEQUENCE 184 AA; 20993 MW; 5659B7F6E9401828 CRC64; MEKYKLRKNN TILLYDYSIN FSIKDNVKLE KKRFNMNKNK IKKRGQLSVD FVLAILFLML VSLFIYYNAL TFTNNTTDAL IVDRMYSIAD TFENYAILSY TKNETIVLKL KPIGDLGYVI HVSNKIINVS YKTLIVFTPT DNGVIISGSN IETAPVDIGK NISITVTIDK NNITICKELT INIT // ID Y1493_METJA Reviewed; 231 AA. AC Q58888; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1493; GN OrderedLocusNames=MJ1493; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 SWIM-type zinc finger. CC {ECO:0000255|PROSITE-ProRule:PRU00325}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99511.1; -; Genomic_DNA. DR PIR; D64486; D64486. DR ProteinModelPortal; Q58888; -. DR STRING; 243232.MJ_1493; -. DR EnsemblBacteria; AAB99511; AAB99511; MJ_1493. DR KEGG; mja:MJ_1493; -. DR eggNOG; arCOG03430; Archaea. DR eggNOG; ENOG410Y5I8; LUCA. DR OMA; CKHAYAL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR007527; Znf_SWIM. DR Pfam; PF04434; SWIM; 1. DR PROSITE; PS50966; ZF_SWIM; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 231 Uncharacterized protein MJ1493. FT /FTId=PRO_0000107377. FT ZN_FING 43 76 SWIM-type. {ECO:0000255|PROSITE- FT ProRule:PRU00325}. SQ SEQUENCE 231 AA; 27883 MW; 173F6F3D7F1402AC CRC64; MITMNYDPKI IERGKLYYRN NLVKYCIKYK NFLFGEVVGS DTYKVKVDLD NNYFGLCTCQ YKYNCKHAYA LIEAYENNNY VDAEEIFKEI EDKPKEEILK ILKNLVVKYY LWDEFLNTDS LLNKAIGLIK LIPLERKNIY TFKSFLRNQF VKNADDEELI KVIDEMIRAD LDFNNSDIIE ALTIILDEIF RRENKEAIKK LINLYRKHKK ELWIVGDYLI EYYDNYFDYE D // ID Y1506_METJA Reviewed; 437 AA. AC Q58901; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1506; GN OrderedLocusNames=MJ1506; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99522.1; -; Genomic_DNA. DR PIR; A64488; A64488. DR ProteinModelPortal; Q58901; -. DR STRING; 243232.MJ_1506; -. DR EnsemblBacteria; AAB99522; AAB99522; MJ_1506. DR KEGG; mja:MJ_1506; -. DR eggNOG; arCOG02080; Archaea. DR eggNOG; COG1361; LUCA. DR InParanoid; Q58901; -. DR OMA; NIVGPTT; -. DR PhylomeDB; Q58901; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 437 Uncharacterized protein MJ1506. FT /FTId=PRO_0000107381. FT TRANSMEM 47 67 Helical. {ECO:0000255}. SQ SEQUENCE 437 AA; 50390 MW; 97E6EA7694971D32 CRC64; MLYILKCKSN YIINFHRLPQ KTSKALYTNI SLSFIYRFMW GIMMKKLLII LIGFILLSSI SAIQIDAPQY QPNVIHPGDD VDLWIKINND NYDNEVKNIV VEVTPHYPFE LRQVNPIKGK ATISHLNPGE SDTVYFKLHV DENAPSRDYR IDVKVSYDEV DKEDGKETSH HYEITKIYYL HVYGIASFEI NIDDTSIIPG KTKTIKLDIK NVGTGNAKYL NLYLIGNDKI NILGGSLIFV GCLKANNQYI IPIKIYAVPE IEDGIYSINA NLFWVGEDGK QYNSTIPLNI RVVKKIYANQ PYIYLDDVKN KGDYIEITIG IANRGTTKIK HCVMTLTANG RNYTKYIGDL DEDDYDTSIF EIKEFGDIPI KVTVTYFDDY HNPYNATETF NIHVEKVKKE ESLSPMYIIG GVIVVIIIIL YIRKRKRHQE FEEFEEI // ID Y1508_METJA Reviewed; 224 AA. AC Q58903; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ1508; GN OrderedLocusNames=MJ1508; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99520.1; -; Genomic_DNA. DR PIR; C64488; C64488. DR ProteinModelPortal; Q58903; -. DR SMR; Q58903; 1-221. DR STRING; 243232.MJ_1508; -. DR EnsemblBacteria; AAB99520; AAB99520; MJ_1508. DR KEGG; mja:MJ_1508; -. DR eggNOG; arCOG00922; Archaea. DR eggNOG; COG1136; LUCA. DR InParanoid; Q58903; -. DR KO; K02003; -. DR OMA; YGRNIIH; -. DR PhylomeDB; Q58903; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 224 Uncharacterized ABC transporter ATP- FT binding protein MJ1508. FT /FTId=PRO_0000093226. FT DOMAIN 2 221 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 224 AA; 25264 MW; CF0B72742D24921E CRC64; MIEAKNVWKI YGKGEAKTIA LKNINLKIEE GEFVMIMGPS GCGKSTLLNI LALLDTPTKG EVYYKGRRTS SMSENERAIF RRKISGFIFQ QFHLIKTLTA LENVELPMML DERDKSYRRK RAKKLLEMVG LGDRLNHYPH QLSGGQQQRV AIARALANNP KIIFADEPTG NLDSKSGMAV MSILKGLNEK GITIIMVTHE QELTKYASKI IKLRDGEIVE IINK // ID Y1517_METJA Reviewed; 278 AA. AC Q58912; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ1517; GN OrderedLocusNames=MJ1517; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99548.1; -; Genomic_DNA. DR PIR; D64489; D64489. DR ProteinModelPortal; Q58912; -. DR STRING; 243232.MJ_1517; -. DR EnsemblBacteria; AAB99548; AAB99548; MJ_1517. DR KEGG; mja:MJ_1517; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 278 Uncharacterized protein MJ1517. FT /FTId=PRO_0000107389. SQ SEQUENCE 278 AA; 32685 MW; 800A0DA2A0A6D022 CRC64; MVKLMNLWSE RIKDREVVEV IGCERVPLNE TLNEIVVLFD EYTKRGDYKV EIFDDVFNYY HNRILTNDEF IDGVARIKLG LDTRNHAKEW LLEVVNWFAG NRYNLRDEEI KLGNRLRDWM NIGVSLVIPK ELKPKFDEFY KMAKKFDWQV EIRNEMIFKT TLNGKEVYTF ILMGDVVNER LDNILDGGGV FDLGKRVVCD DEWFSGWLVR DIDVNKNIME VLGMLSLKSQ EILDISVESA LIRRKNIKTK SMVVKLVKVK NLIQLLKRKK KSGLNCLV // ID Y1520_METJA Reviewed; 387 AA. AC Q58915; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1520; GN OrderedLocusNames=MJ1520; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. ChlP CC subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99539.1; -; Genomic_DNA. DR PIR; G64489; G64489. DR ProteinModelPortal; Q58915; -. DR STRING; 243232.MJ_1520; -. DR EnsemblBacteria; AAB99539; AAB99539; MJ_1520. DR KEGG; mja:MJ_1520; -. DR eggNOG; arCOG00570; Archaea. DR eggNOG; COG0644; LUCA. DR InParanoid; Q58915; -. DR OMA; EFTEDAR; -. DR PhylomeDB; Q58915; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0071949; F:FAD binding; IEA:InterPro. DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 1. DR InterPro; IPR002938; FAD-bd. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR011777; Geranylgeranyl_Rdtase_fam. DR Pfam; PF01494; FAD_binding_3; 1. DR SUPFAM; SSF51905; SSF51905; 2. DR TIGRFAMs; TIGR02032; GG-red-SF; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 387 Uncharacterized protein MJ1520. FT /FTId=PRO_0000219666. SQ SEQUENCE 387 AA; 43299 MW; E0796DA99B4A9734 CRC64; MNRNDYDVVI IGGGPVGCIT GEYIKNGRVL IVEEHQSIGV PLQCAGLISK NGVKELGNPK GVVNKVRGAY IYSKNSMVKI GNEGIRAYIF ERKVMDKDIA IRAAKKCDFL LKAYGKIEKD KNGYKVEITH LGEKITLNPK IIVGADGAKT ITGKKLGLVN NKNREILSSC QFEMVNAEVD DDFVYIFLDR KYSERFFTWI IPMGKDRVRV GLIDRGNCYN KLIRFINENK IAKEILKNAT ITEFSTGSLP IGYLDKTFKD NVLLVGDAAC HVKPLSGGGL YFGAMGGKIA GEVISKYLNE DIENLELYDK RWKETFGSEI KNGLRVRKLF LKLGNDTLDK IIEKLSKSDL IDYINKHGDM DRQASLSIKV LKSLDIGLGF RILRDLL // ID Y1544_METJA Reviewed; 441 AA. AC Q58939; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1544; GN OrderedLocusNames=MJ1544; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99562.1; -; Genomic_DNA. DR PIR; G64492; G64492. DR ProteinModelPortal; Q58939; -. DR STRING; 243232.MJ_1544; -. DR EnsemblBacteria; AAB99562; AAB99562; MJ_1544. DR KEGG; mja:MJ_1544; -. DR eggNOG; arCOG03167; Archaea. DR eggNOG; COG1373; LUCA. DR InParanoid; Q58939; -. DR KO; K07133; -. DR OMA; VSISHNT; -. DR PhylomeDB; Q58939; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR InterPro; IPR025420; DUF4143. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13635; DUF4143; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 441 Uncharacterized protein MJ1544. FT /FTId=PRO_0000107400. FT NP_BIND 57 64 ATP. {ECO:0000255}. SQ SEQUENCE 441 AA; 52563 MW; AA0B23729523BCE2 CRC64; MSNILDIKIL RVSSMIDKKI LFEEVILDNL EIAKKAKVIN RDIEIKLIPN KIKVIYGVRR GGKTYFLFQI INKHFKDDFI YINFEDERLI NIALDELNEL LKIALSIKNT KNLFFDEIQS VDNWDKFVRR LNDSGFNIFI TGSSSKLLSK EIATSLRGRN LKTEILPLNF KEFLKFKNFN VKKRYSTIEK AELLKYLNEF IKFGGFPEIT LIDDENIKKE ILKEYLDGIF YRDVVERHSI RNIKEIKVLR NILINLFANE ISIKKIANLL KEFNTKISRE CIYNYLEYFS DAYLIFLLNN FSYKTKTISY SKLYVIDGMW NFSLSFSKNK GRILENLVFL ELRRRGFVEN ENLFYVKRKN YEVDFLIFGE NKELIQVCYE LNETNKEREI KAYEKAIKDL KLDNVNLKII TYNDEGFEKI TVDDKEHLIE IVPFWKWSLT Y // ID Y1550_METJA Reviewed; 61 AA. AC Q58945; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ1550; GN OrderedLocusNames=MJ1550; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99580.1; -; Genomic_DNA. DR PIR; E64493; E64493. DR STRING; 243232.MJ_1550; -. DR EnsemblBacteria; AAB99580; AAB99580; MJ_1550. DR KEGG; mja:MJ_1550; -. DR eggNOG; arCOG08299; Archaea. DR eggNOG; ENOG4111181; LUCA. DR OMA; CPFIKDI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 61 Uncharacterized protein MJ1550. FT /FTId=PRO_0000107404. SQ SEQUENCE 61 AA; 7106 MW; 52C0B8011E728F12 CRC64; MDKFCPFIKD ICKKDKCVMW VGGECRLIML IDLYISSKIY ELYGYENGTL EVEDVDEDEA S // ID Y1569_METJA Reviewed; 222 AA. AC Q58964; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Putative metal transport protein MJ1569; GN OrderedLocusNames=MJ1569; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: May be involved in metal transport. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CbiM family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99587.1; -; Genomic_DNA. DR PIR; H64495; H64495. DR ProteinModelPortal; Q58964; -. DR STRING; 243232.MJ_1569; -. DR EnsemblBacteria; AAB99587; AAB99587; MJ_1569. DR KEGG; mja:MJ_1569; -. DR eggNOG; arCOG02248; Archaea. DR eggNOG; COG0310; LUCA. DR InParanoid; Q58964; -. DR KO; K02007; -. DR OMA; TAIVVWY; -. DR PhylomeDB; Q58964; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0000041; P:transition metal ion transport; IEA:InterPro. DR InterPro; IPR002751; CbiM_fam. DR Pfam; PF01891; CbiM; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 222 Putative metal transport protein MJ1569. FT /FTId=PRO_0000107416. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 102 122 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. SQ SEQUENCE 222 AA; 23948 MW; 69AEE7C6D44C112B CRC64; MHIPDGYLGP ITCAFFYLIM IPIWYKSIKE LKKLDPRKLP LLGVLTAFSF LVMMFNLPVP DGTTAHMVGG TLIAILMDNP WVATIAISIV LIIQAIFFGD GGITCIGANC FNMGVVLPFV GYYVYKFLRD KVGEVIASGI GAYVGIVAAA IVAGFEFGLQ PFIEPGYCPY PFTVSVPAMA FAHLITAGPA AAVVTAIVVW YVKKVRPDLF TSKEQQVSGV NA // ID Y1579_METJA Reviewed; 70 AA. AC Q58974; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ1579; GN OrderedLocusNames=MJ1579; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99607.1; -; Genomic_DNA. DR PIR; B64497; B64497. DR ProteinModelPortal; Q58974; -. DR STRING; 243232.MJ_1579; -. DR EnsemblBacteria; AAB99607; AAB99607; MJ_1579. DR KEGG; mja:MJ_1579; -. DR eggNOG; arCOG05091; Archaea. DR eggNOG; ENOG410Z3EC; LUCA. DR OMA; ETAPYVQ; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 70 Uncharacterized protein MJ1579. FT /FTId=PRO_0000107424. FT COMPBIAS 53 70 Lys-rich. SQ SEQUENCE 70 AA; 8483 MW; A485930C4F232461 CRC64; MNQRKEIELL MFDVLPYMAN MEFIKELLES VNSLEELEQK VRELLEKETD ITKKTDLKIL LEKIEERKNK // ID Y1599_METJA Reviewed; 277 AA. AC Q58994; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1599; GN OrderedLocusNames=MJ1599; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99626.1; -; Genomic_DNA. DR PIR; F64499; F64499. DR ProteinModelPortal; Q58994; -. DR STRING; 243232.MJ_1599; -. DR DNASU; 1452508; -. DR EnsemblBacteria; AAB99626; AAB99626; MJ_1599. DR KEGG; mja:MJ_1599; -. DR eggNOG; arCOG00046; Archaea. DR eggNOG; COG0037; LUCA. DR InParanoid; Q58994; -. DR OMA; LNPLCVM; -. DR PhylomeDB; Q58994; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012121; ATPase_PP-loop_MJ1599. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01507; PAPS_reduct; 1. DR PIRSF; PIRSF036668; ATPase_UCP036668; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 277 Uncharacterized protein MJ1599. FT /FTId=PRO_0000107433. SQ SEQUENCE 277 AA; 32340 MW; F59EF4A2485D3BAE CRC64; MKCSICVHTS KTKKIINYEG KPICVDCLTM LKYPPNFEKM KKEVEEILYN LKKEGGKYHC ILAFSGGKDS VLALKLLKEK FKLNPLCVMV DNKYMAKEAI ENALNVTKHY QVDLMILNRD YTDLFEDAIK RGESPCRRCS RLILREVWRV TKLLGLKYII TGHELPFGHS AIREMKEGIK MIRLLAPYKF KEEEKYKMLE DLPWKKPDLG GYTTNCLVLG VALERFYDKY GFSFEIDRIA TLVRLGLLSK EKAKKELEKP KVPKEIYEEL RRRGLKI // ID Y1607_METJA Reviewed; 390 AA. AC Q59002; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 79. DE RecName: Full=Uncharacterized glycosyltransferase MJ1607; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1607; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 4 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99629.1; -; Genomic_DNA. DR PIR; F64500; F64500. DR ProteinModelPortal; Q59002; -. DR STRING; 243232.MJ_1607; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAB99629; AAB99629; MJ_1607. DR KEGG; mja:MJ_1607; -. DR eggNOG; arCOG01403; Archaea. DR eggNOG; COG0438; LUCA. DR InParanoid; Q59002; -. DR OMA; EYPPRIV; -. DR PhylomeDB; Q59002; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13439; Glyco_transf_4; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 390 Uncharacterized glycosyltransferase FT MJ1607. FT /FTId=PRO_0000080324. SQ SEQUENCE 390 AA; 44446 MW; 17C12B7BF7B06556 CRC64; MKIAMVTWEY PPRIVGGLAI HCKGLAEGLV RNGHEVDVIT VGYDLPEYEN INGVNVYRVR PISHPHFLTW AMFMAEEMEK KLGILGVDKY DVIHCHDWMT HFVGANLKHI CRMPYVQSIH STEIGRCGGL YSDDSKAIHA MEYLSTYESC QVITVSKSLK EEVCSIFNTP EDKVKVIYNG INPWEFDINL SWEEKINFRR SIGVQDDEKM ILFVGRLTYQ KGIEYLIRAM PKILERHNAK LVIAGSGDMR DYLEDLCYQL GVRHKVVFLG FVNGDTLKKL YKSADVVVIP SVYEPFGIVA LEAMAAGTPV VVSSVGGLME IIKHEVNGIW VYPKNPDSIA WGVDRVLSDW GFREYIVNNA KKDVYEKYSW DNIAKETVNV YKIAMEMMGR // ID Y1608_METJA Reviewed; 70 AA. AC Q59003; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1608; GN OrderedLocusNames=MJ1608; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99635.1; -; Genomic_DNA. DR PIR; G64500; G64500. DR ProteinModelPortal; Q59003; -. DR STRING; 243232.MJ_1608; -. DR EnsemblBacteria; AAB99635; AAB99635; MJ_1608. DR KEGG; mja:MJ_1608; -. DR eggNOG; arCOG05093; Archaea. DR eggNOG; ENOG410XYR3; LUCA. DR InParanoid; Q59003; -. DR OMA; KMAIGWL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019707; DUF2582. DR Pfam; PF10771; DUF2582; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 70 Uncharacterized protein MJ1608. FT /FTId=PRO_0000107435. SQ SEQUENCE 70 AA; 8122 MW; BDC6BE5A1A47AF57 CRC64; MEDMWGKIGE TAGKIYHLLE GGEKSLSQIE KILRKEGYNS NIVKMAIGWL AREDKIFVLK DDKKWVIKLK // ID Y1653_METJA Reviewed; 385 AA. AC Q59047; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative ribosomal RNA large subunit methyltransferase MJ1653; DE EC=2.1.1.-; GN OrderedLocusNames=MJ1653; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L- CC homocysteine + rRNA containing C(5)-methylcytosine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99674.1; -; Genomic_DNA. DR PIR; C64506; C64506. DR ProteinModelPortal; Q59047; -. DR STRING; 243232.MJ_1653; -. DR EnsemblBacteria; AAB99674; AAB99674; MJ_1653. DR KEGG; mja:MJ_1653; -. DR eggNOG; arCOG00032; Archaea. DR eggNOG; COG1092; LUCA. DR InParanoid; Q59047; -. DR KO; K06969; -. DR OMA; DCFCHTG; -. DR PhylomeDB; Q59047; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10672; Methyltrans_SAM; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 385 Putative ribosomal RNA large subunit FT methyltransferase MJ1653. FT /FTId=PRO_0000213171. FT DOMAIN 2 81 PUA. {ECO:0000255|PROSITE- FT ProRule:PRU00161}. SQ SEQUENCE 385 AA; 43763 MW; 27EC604EC4A435ED CRC64; MTTKLYVDFG GYSAIEKGNL IIPRDNILNK EDFDSIEIGE VVDIYSKRGK FLGRGFKNPK EVRIMTLRKE DLDENYIREK IIKANEYRLK LGFKDTYRMV YTQSDWLNGL VIDKYNDIAT VQIFNYGIEK MKDVVVETLL DLGIDSIYEK SSGRNRKRAG LPEVEGILAG EKTETIIQEG EAKFKVTFDG QKTGFFLDQR ENRLELEKFI KEGDRVLDIC CYTGGFSVHA AIRGAEVVGV DLSKKALKLA EENMELNNIP KDRYEFIEGN AFKVMEEFIE DGEKFDVVIL DPPAFAQSKK ALKSAIKGYH MLNRFGAKLA DRLLVTCSCS QPLEPDAFKA LVIDACLKAK KWAKIIKYGS QSPDHPITSK GTEYLKCLFL SVEEI // ID Y165_METJA Reviewed; 256 AA. AC Q57629; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized protein MJ0165; GN OrderedLocusNames=MJ0165; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98147.1; -; Genomic_DNA. DR PIR; F64320; F64320. DR ProteinModelPortal; Q57629; -. DR STRING; 243232.MJ_0165; -. DR EnsemblBacteria; AAB98147; AAB98147; MJ_0165. DR KEGG; mja:MJ_0165; -. DR eggNOG; arCOG02465; Archaea. DR eggNOG; COG1691; LUCA. DR InParanoid; Q57629; -. DR KO; K06898; -. DR OMA; MIEEDVC; -. DR PhylomeDB; Q57629; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006189; P:'de novo' IMP biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.50.7700; -; 1. DR InterPro; IPR000031; PurE_dom. DR Pfam; PF00731; AIRC; 1. DR SMART; SM01001; AIRC; 1. DR SUPFAM; SSF52255; SSF52255; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 256 Uncharacterized protein MJ0165. FT /FTId=PRO_0000106727. FT TRANSMEM 181 201 Helical. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. SQ SEQUENCE 256 AA; 28107 MW; AB9DE5847D62D928 CRC64; MGKNLRDLLL AFKNGDISLD EIEKQIKLNY YEEIEERLKL DINRQFRTGV PEVVYGKGKD IDEIIKATLK LVEKNGIALA TKIEDIEKLS DEIRKWNLKN YDIKINKKAK TLIIKNKNYE VKKIGKVGIL TAGTSDIPVA EEAKDTLEIM GVEAITAYDV GIAGIHRLFP ALKRMIEEDV CCIIVVAGME GALPSVIASM VDIPVIGVPT STSYGIKITP LLTMLHSCSP GIAVVNIDNG FGAGVFAGLI AKIMHK // ID Y1677_METJA Reviewed; 205 AA. AC Q59071; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=UPF0056 membrane protein MJ1677; GN OrderedLocusNames=MJ1677; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0056 (MarC) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99699.1; -; Genomic_DNA. DR PIR; C64509; C64509. DR ProteinModelPortal; Q59071; -. DR STRING; 243232.MJ_1677; -. DR EnsemblBacteria; AAB99699; AAB99699; MJ_1677. DR KEGG; mja:MJ_1677; -. DR eggNOG; arCOG01997; Archaea. DR eggNOG; COG2095; LUCA. DR InParanoid; Q59071; -. DR KO; K05595; -. DR OMA; AIILWTS; -. DR PhylomeDB; Q59071; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002771; Multi_antbiot-R_MarC. DR Pfam; PF01914; MarC; 1. DR TIGRFAMs; TIGR00427; TIGR00427; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 205 UPF0056 membrane protein MJ1677. FT /FTId=PRO_0000156918. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 112 132 Helical. {ECO:0000255}. FT TRANSMEM 145 165 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. SQ SEQUENCE 205 AA; 22304 MW; 3C68D938EFA689AC CRC64; MDLQYFILAF SSIFSILNPF GAVPVFITLT ESYPKKERDL VAKKTVIYAL AILLAFALFG EWILKFFGIS LDAFKIAGGI LLLLISLDMV RGQQEAKIHR KEIEAAYEID EIALMPLATP LLAGPGSITA CMVAMAEASD IGDKFLVILA ILLSLGITYL TLLSAESVLD RIGRLGIRIL TRMMGLILTA IAVQMIVNGI RGALL // ID Y169_METJA Reviewed; 263 AA. AC Q57633; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized ATP-binding protein MJ0169; GN OrderedLocusNames=MJ0169; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98154.1; -; Genomic_DNA. DR PIR; B64321; B64321. DR ProteinModelPortal; Q57633; -. DR STRING; 243232.MJ_0169; -. DR PRIDE; Q57633; -. DR EnsemblBacteria; AAB98154; AAB98154; MJ_0169. DR KEGG; mja:MJ_0169; -. DR eggNOG; arCOG00589; Archaea. DR eggNOG; COG0455; LUCA. DR InParanoid; Q57633; -. DR KO; K03609; -. DR OMA; KDMAIHL; -. DR PhylomeDB; Q57633; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR025501; MinD. DR InterPro; IPR010224; MinD_archaea. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF003092; MinD; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01969; minD_arch; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 263 Uncharacterized ATP-binding protein FT MJ0169. FT /FTId=PRO_0000106728. FT NP_BIND 10 17 ATP. {ECO:0000255}. SQ SEQUENCE 263 AA; 28950 MW; 292FBE38EE72ACF4 CRC64; MIFMIITIAS GKGGVGKTTT SASLAVALAK LGKKVLAIDG DISMANLGIL FNMEKKKPSL HEVLSEEADV RDAIYKHKTG VYVLPTSLSL EGYKKSDIDL LPDVVNEVAD DFDYVIIDAP AGLNREMATH LAIADKLLLV VTPEMFSIID AVRLKESAEM AGTPLMGVVL NRVGRDFGEM GRDEIEMLIK GKVLVEVPED ENVRSAALKK MSVIEYRKNS PASQAYMKLA SIIAGVPIYI EDEIKIIRKE SFIDKIKRLF RMY // ID Y206_METJA Reviewed; 135 AA. AC Q57659; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0206; GN OrderedLocusNames=MJ0206; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98190.1; -; Genomic_DNA. DR PIR; G64325; G64325. DR ProteinModelPortal; Q57659; -. DR STRING; 243232.MJ_0206; -. DR EnsemblBacteria; AAB98190; AAB98190; MJ_0206. DR KEGG; mja:MJ_0206; -. DR eggNOG; arCOG04171; Archaea. DR eggNOG; COG2090; LUCA. DR InParanoid; Q57659; -. DR KO; K09738; -. DR OMA; PRGDCII; -. DR PhylomeDB; Q57659; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.60.120.630; -; 1. DR InterPro; IPR007171; DUF371. DR InterPro; IPR023131; Mth639-like_domain. DR Pfam; PF04027; DUF371; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 135 Uncharacterized protein MJ0206. FT /FTId=PRO_0000106740. SQ SEQUENCE 135 AA; 15376 MW; BBF1243507DE8A01 CRC64; MEFIIKAKGH KNVSATHKTT LEITKEDYLT PTGHCIIGID ADKSMTDFSE EFKEKLRNAK KIIVEIEVEG IKDTIIGEGH KDLILNHPTD MVIRKSNYIC PRTLMINANK SAKDINREIV KKLKEGKELI FKIIV // ID Y215_METJA Reviewed; 159 AA. AC Q57668; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0215; GN OrderedLocusNames=MJ0215; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJECL20. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98205.1; -; Genomic_DNA. DR PIR; H64326; H64326. DR ProteinModelPortal; Q57668; -. DR STRING; 243232.MJ_0215; -. DR EnsemblBacteria; AAB98205; AAB98205; MJ_0215. DR KEGG; mja:MJ_0215; -. DR eggNOG; arCOG03413; Archaea. DR eggNOG; COG2453; LUCA. DR InParanoid; Q57668; -. DR OMA; RERYCEC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GOC. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR SUPFAM; SSF52799; SSF52799; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 159 Uncharacterized protein MJ0215. FT /FTId=PRO_0000106745. SQ SEQUENCE 159 AA; 18397 MW; 5FAD7EB90DE3A8D3 CRC64; MYIAILKCES MGRCKHNGEV SIFGVRPASF PNFPFHLMDK IGGFVILDEL WLRRWCEIIE YPMRIPTLYV PIEDYGIPTV EDMDLIVDFI KYHVSKEKEV VVSCIGGHGR TGTVLAVWAG LNGIKNPIEY VRERYCECAV ETEEQEEFVI EYLKMKKRG // ID Y22A_METJA Reviewed; 193 AA. AC P81304; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0226.1; GN OrderedLocusNames=MJ0226.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98217.1; -; Genomic_DNA. DR STRING; 243232.MJ_0226.1; -. DR EnsemblBacteria; AAB98217; AAB98217; MJ_0226.1. DR KEGG; mja:MJ_0226.1; -. DR eggNOG; arCOG10447; Archaea. DR eggNOG; ENOG41111HY; LUCA. DR OMA; WHYITST; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 193 Uncharacterized protein MJ0226.1. FT /FTId=PRO_0000106748. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. SQ SEQUENCE 193 AA; 22933 MW; C981628CFF211079 CRC64; MDIELILLIV VLFLTPYLIA LFIIFNPPYC ILDYLLYKKY RKAKEEWHYI TSTNMGMNRS RWIFILIVEI IALCSGFYIL ININRPHDEI LTFSLIFLFI AIIYDKLTPA SGTVEIYKEG IAVYIKIFNT LKPFLNRYIV LPWKFFKGYK IKSKNNTKYV ILVPKSRLFF SIYLIDRDGN VEKTIRNHLN PIQ // ID Y298_METJA Reviewed; 150 AA. AC Q57746; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 81. DE RecName: Full=Uncharacterized protein MJ0298; GN OrderedLocusNames=MJ0298; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98297.1; -; Genomic_DNA. DR PIR; C64337; C64337. DR ProteinModelPortal; Q57746; -. DR STRING; 243232.MJ_0298; -. DR EnsemblBacteria; AAB98297; AAB98297; MJ_0298. DR KEGG; mja:MJ_0298; -. DR eggNOG; arCOG00519; Archaea. DR eggNOG; COG0716; LUCA. DR InParanoid; Q57746; -. DR OMA; FGSGIYF; -. DR PhylomeDB; Q57746; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR Gene3D; 3.40.50.360; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR026816; Flavodoxin_dom. DR InterPro; IPR029039; Flavoprotein-like_dom. DR Pfam; PF12724; Flavodoxin_5; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 150 Uncharacterized protein MJ0298. FT /FTId=PRO_0000106781. FT DOMAIN 4 148 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. SQ SEQUENCE 150 AA; 17228 MW; F0655E356CBDB828 CRC64; MKALILYKSI HHKNTEKIAK TIADELNADI YNIDKVSPDI IENYDLIGFG SGIYFGKHHK SIFKFLDKIS KTNKKAFIFS TAGFPFLKSM FHKELRDKLK SKGFEILGEF CCKGYHTYGI FKLFGGLNKN HPNEDDIKKA KEFAKSILKN // ID Y300_METJA Reviewed; 296 AA. AC Q57748; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 91. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0300; GN OrderedLocusNames=MJ0300; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH lysR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00253}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98287.1; -; Genomic_DNA. DR PIR; E64337; E64337. DR ProteinModelPortal; Q57748; -. DR STRING; 243232.MJ_0300; -. DR DNASU; 1451155; -. DR EnsemblBacteria; AAB98287; AAB98287; MJ_0300. DR KEGG; mja:MJ_0300; -. DR eggNOG; arCOG00224; Archaea. DR eggNOG; COG0583; LUCA. DR InParanoid; Q57748; -. DR OMA; SAVKSFW; -. DR PhylomeDB; Q57748; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005119; LysR_subst-bd. DR InterPro; IPR000847; Tscrpt_reg_HTH_LysR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF00126; HTH_1; 1. DR Pfam; PF03466; LysR_substrate; 1. DR PRINTS; PR00039; HTHLYSR. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50931; HTH_LYSR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 296 Uncharacterized HTH-type transcriptional FT regulator MJ0300. FT /FTId=PRO_0000105831. FT DOMAIN 1 60 HTH lysR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. FT DNA_BIND 20 39 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00253}. SQ SEQUENCE 296 AA; 33111 MW; 13474BFF48985038 CRC64; MDPKISYFQT FIVASKTKSF SKAAKRLGIT QGTVSNHISA LEKYFDAQLF LRTPEGVDLT PEGKIFYERA EKILDLLNEA KLLMRAIHEN PEGIIRIYAS TTPGEHILPS IIKEYKSSYK NVDFEITITD SERCFKALDE GLADIAAVGY LKNKNYEYTI IGKDRLVLIV PPNHPLAEKG TAKLEDILKE DYIDREEGSG TREAFIKALN DKGYSIMDLN VVMRLGSHSA VITAVSEGYG VSVVSEIPAK KAEDAGLIKI VPVVDLDVVR YLYLVKSRRP KNPSAVKSFW EFVTKV // ID Y325_METJA Reviewed; 308 AA. AC Q57771; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0325; GN OrderedLocusNames=MJ0325; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98313.1; -; Genomic_DNA. DR PIR; E64340; E64340. DR ProteinModelPortal; Q57771; -. DR STRING; 243232.MJ_0325; -. DR EnsemblBacteria; AAB98313; AAB98313; MJ_0325. DR KEGG; mja:MJ_0325; -. DR eggNOG; arCOG01564; Archaea. DR eggNOG; COG3276; LUCA. DR InParanoid; Q57771; -. DR OMA; ISNTSMK; -. DR PhylomeDB; Q57771; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR InterPro; IPR009000; Transl_B-barrel. DR InterPro; IPR004161; Transl_elong_EFTu/EF1A_2. DR Pfam; PF03144; GTP_EFTU_D2; 1. DR SUPFAM; SSF50447; SSF50447; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 308 Uncharacterized protein MJ0325. FT /FTId=PRO_0000106794. SQ SEQUENCE 308 AA; 34597 MW; 7195B94307F3E60A CRC64; MEGLTVGLFG HVEGVGKELG KKGTSTDITL YNYKQGDKAV CYVEPTRYPD RINPLIYEIN MMDYALVFID EITGELGETL LALDMFGINN GAFVVGEYVD LDMLKNIISQ TSMKDFEILE RDFINIREKM INLNIERDYN GFVKIPIDHY FTVRSVGTVI LGKVESGTVR VHDNLRVYPT DKMAMVRSIQ IHDNDFKEAK AGNRVGLALK GITTDELDRG MILSNGELKV AKEIEININW NPFMQKTVKE GENYQIIVGL QSVSCVVEEV NKNKIKLSLQ KEIAYDVGDK LCLIDGSAKI RILGVGKL // ID Y326_METJA Reviewed; 436 AA. AC Q57772; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Putative permease MJ0326; GN OrderedLocusNames=MJ0326; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the xanthine/uracil permease family. AzgA CC purine transporter (TC 2.A.1.40) subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98314.1; -; Genomic_DNA. DR PIR; F64340; F64340. DR ProteinModelPortal; Q57772; -. DR STRING; 243232.MJ_0326; -. DR EnsemblBacteria; AAB98314; AAB98314; MJ_0326. DR KEGG; mja:MJ_0326; -. DR eggNOG; arCOG02807; Archaea. DR eggNOG; COG2252; LUCA. DR InParanoid; Q57772; -. DR KO; K06901; -. DR OMA; MVDFFDT; -. DR PhylomeDB; Q57772; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR026033; Pur_Permease_PbuG-like. DR InterPro; IPR006043; Xant/urac/vitC. DR PANTHER; PTHR11119; PTHR11119; 1. DR Pfam; PF00860; Xan_ur_permease; 1. DR PIRSF; PIRSF005353; PbuG; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 436 Putative permease MJ0326. FT /FTId=PRO_0000106795. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 103 123 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 194 214 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TRANSMEM 322 342 Helical. {ECO:0000255}. FT TRANSMEM 345 365 Helical. {ECO:0000255}. FT TRANSMEM 381 401 Helical. {ECO:0000255}. FT TRANSMEM 416 436 Helical. {ECO:0000255}. SQ SEQUENCE 436 AA; 46723 MW; 409B4075F6D70891 CRC64; MIMKFVEKYF EFEKYGTNLK VETLAGITTF MTMAYIIFVN PQILSTAGMD FGAVMVATCI ASAIATLVMG LYARYPFALA PGMGLNAYFT YGVCLGMGID WRVALGAVFI SGVLFIILTL TKIRTWIFNV IPNAIKYGTA VGIGLFIAFI GLKSAGIIVS SKATLVTLGN LMEPSTLLAL FGIFLTSILV SRNVIGAILI GIIVTSLIGM ILGISPFPEG IFSMPPSIAP TFLQLDIMGA LNLGLLTIVL AFFFVDMFDT LGTLSALASQ AGYLDKDGKL PRVEKALMAD ATGTVVGSLL GTSTVTTYIE SASGIALGGR TGFVSVVVAM LFLLSLFFYP VVKAIPPYAT AAALVIVGAL MMRSVKYIDF DDYTEAIPAF ITLLTIPLTF SIATGLALGF ITYPILKVFT GRWKEVHWLV YVLAVIFALR FVYLSG // ID Y333_METJA Reviewed; 96 AA. AC Q57779; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0333; GN OrderedLocusNames=MJ0333; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98321.1; -; Genomic_DNA. DR PIR; E64341; E64341. DR STRING; 243232.MJ_0333; -. DR EnsemblBacteria; AAB98321; AAB98321; MJ_0333. DR KEGG; mja:MJ_0333; -. DR eggNOG; arCOG09640; Archaea. DR eggNOG; ENOG411103R; LUCA. DR OMA; SIYRYSK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR010982; Lambda_DNA-bd_dom. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 96 Uncharacterized protein MJ0333. FT /FTId=PRO_0000106803. SQ SEQUENCE 96 AA; 10927 MW; A4EB1A265B52EB99 CRC64; MNKEKYGDNM MTDSDSKQAI FIIGVQGKEI KNVEQLMQEL SKIVNEGSIY RYSKETGLGK GTLHKIKNNE LQDPRISTVL KLLKASGKRL VIIDEW // ID Y335_METJA Reviewed; 247 AA. AC Q57781; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0335; GN OrderedLocusNames=MJ0335; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98323.1; -; Genomic_DNA. DR PIR; G64341; G64341. DR ProteinModelPortal; Q57781; -. DR STRING; 243232.MJ_0335; -. DR EnsemblBacteria; AAB98323; AAB98323; MJ_0335. DR KEGG; mja:MJ_0335; -. DR eggNOG; ENOG4102SUV; Archaea. DR eggNOG; ENOG410YZ7P; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 247 Uncharacterized protein MJ0335. FT /FTId=PRO_0000106805. SQ SEQUENCE 247 AA; 27881 MW; 9972F8BC3FA792DF CRC64; MQSIFLPVLN PTTIDGQEIT EEWIKKYGPT LRGKPVNIDH NYYSNGNLAV GDVVDVYFNP EGNLYAHIRI FDEIYWRLVD NGIKIKGVSF EFNDDGVGEE GIMKGLALCL ESDPKVDFAR LVEGNYVLEV LASIKRDSMD TKTQEKTEPK KIKDMTEEEF EKFLHEKIEQ ILASHKKENE DKDKSDNEDD KVVEILASKM DELVAVNKSV LKQLEEIRKA QKEILASAPV PPSGSGNSGH RRANLGL // ID Y3403_METJA Reviewed; 108 AA. AC Q60302; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJECS03; GN OrderedLocusNames=MJECS03; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37061.1; -; Genomic_DNA. DR PIR; C64516; C64516. DR EnsemblBacteria; AAC37061; AAC37061; MJ_ECS03. DR KEGG; mja:MJECS03; -. DR HOGENOM; HOG000244911; -. DR InParanoid; Q60302; -. DR OMA; IFYASRE; -. DR Proteomes; UP000000805; Plasmid small ECE. DR InterPro; IPR007176; DUF365. DR Pfam; PF04033; DUF365; 1. DR PIRSF; PIRSF006031; UCP006031; 1. DR ProDom; PD020174; DUF365; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 108 Uncharacterized protein MJECS03. FT /FTId=PRO_0000107484. FT COMPBIAS 31 107 Lys-rich. SQ SEQUENCE 108 AA; 13210 MW; 478DFC06482D0CDE CRC64; MKIIFYASRE EQGFYGEAEI EEVEFFENPM KILEKYKNNL FLTEEEFKKY IEDSNKKWGY GKKKKKPWIV IILKNIRKYP KVVKPKRFIP VCGKYVKEDE YEQILKKL // ID Y3405_METJA Reviewed; 144 AA. AC Q60304; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJECS05; GN OrderedLocusNames=MJECS05; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37063.1; -; Genomic_DNA. DR PIR; E64516; E64516. DR ProteinModelPortal; Q60304; -. DR EnsemblBacteria; AAC37063; AAC37063; MJ_ECS05. DR KEGG; mja:MJECS05; -. DR Proteomes; UP000000805; Plasmid small ECE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Plasmid; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 144 Uncharacterized protein MJECS05. FT /FTId=PRO_0000107486. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 120 140 Helical. {ECO:0000255}. SQ SEQUENCE 144 AA; 16357 MW; 24E5A15EDE7F451A CRC64; MESKEYRKLE YNYKAFLIFS KVAMLTFLTV GIGAIFTPQT YPIMPTIGFI VVAGIVSLIG MTIGALIIHQ QYETLPANEK LEFKQKLLPE AYYICIELFG YGSLVLLYNT FTSNNPTLCV MSLLMAGLFI LVVLVIWYFG YKSY // ID Y3406_METJA Reviewed; 140 AA. AC Q60305; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJECS06; GN OrderedLocusNames=MJECS06; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJECL27. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37064.1; -; Genomic_DNA. DR PIR; F64516; F64516. DR ProteinModelPortal; Q60305; -. DR EnsemblBacteria; AAC37064; AAC37064; MJ_ECS06. DR KEGG; mja:MJECS06; -. DR HOGENOM; HOG000155253; -. DR Proteomes; UP000000805; Plasmid small ECE. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR015880; Znf_C2H2-like. DR SMART; SM00355; ZnF_C2H2; 1. PE 4: Predicted; KW Complete proteome; Metal-binding; Plasmid; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 140 Uncharacterized protein MJECS06. FT /FTId=PRO_0000107487. FT ZN_FING 21 42 C2H2-type. SQ SEQUENCE 140 AA; 16592 MW; DDD50F3AEC9A690E CRC64; MNIDDYIEKL EIQKEGFFYK CPYCNYTNAD VKAIKKHIKS KHYDIIAKEV ENLNKQNKPQ RKPMKKQPKK KDDDYKDYML LFAHKKKCKI YLDNGMIVEG TVKAKDRFNI MVLDAKVDDK EVERIIIQKG HIVALIPLEE // ID Y011_METJA Reviewed; 197 AA. AC Q60327; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0011; GN OrderedLocusNames=MJ0011; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB97999.1; -; Genomic_DNA. DR PIR; C64301; C64301. DR ProteinModelPortal; Q60327; -. DR STRING; 243232.MJ_0011; -. DR EnsemblBacteria; AAB97999; AAB97999; MJ_0011. DR KEGG; mja:MJ_0011; -. DR eggNOG; arCOG05017; Archaea. DR eggNOG; ENOG4111IW8; LUCA. DR InParanoid; Q60327; -. DR OMA; GCPDVPY; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR021778; DUF3343. DR Pfam; PF11823; DUF3343; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 197 Uncharacterized protein MJ0011. FT /FTId=PRO_0000106651. SQ SEQUENCE 197 AA; 22142 MW; 7B710A00956E71F8 CRC64; MIGKLKNLFK LGKGKKEEKA KKSLEGKGLI IFENTKDAMR AESILKDKYK IKVVAPPPEI REGCDLAIEY ELIDEFGIKR ELESNDIKPL KFISLNDYSL KPLELIKVKE VDGFILVRCG NMKITIDKEG NIVNISGGGC PDVPYLALKL KGRNIKDIKE EETPKNLGFT LCAYILNKGS SQRGHSWTII DFEVLSI // ID Y013_METJA Reviewed; 162 AA. AC Q60321; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0013; GN OrderedLocusNames=MJ0013; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98000.1; -; Genomic_DNA. DR PIR; E64301; E64301. DR STRING; 243232.MJ_0013; -. DR EnsemblBacteria; AAB98000; AAB98000; MJ_0013. DR KEGG; mja:MJ_0013; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR PhylomeDB; Q60321; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 162 Uncharacterized protein MJ0013. FT /FTId=PRO_0000106653. SQ SEQUENCE 162 AA; 19588 MW; 8C53C3D9F88AFFBB CRC64; MPKKKNKLPT EIVLTYKVKH NHDLKNLPDE FIKISQRAID IIWENINWKE KVVKHRYKIG KKKYKYYTTT RLIPKIPKDN DFKRELRNRL LEGWEFASHY VDGAIKTAYS AIESWKSNYL NVNRKKNKPI FKRPFVRVKT TLMKYDRKNG IIRITIKPRK SI // ID Y023_METJA Reviewed; 118 AA. AC Q60333; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0023; GN OrderedLocusNames=MJ0023; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98012.1; -; Genomic_DNA. DR PIR; G64302; G64302. DR ProteinModelPortal; Q60333; -. DR EnsemblBacteria; AAB98012; AAB98012; MJ_0023. DR KEGG; mja:MJ_0023; -. DR eggNOG; arCOG09652; Archaea. DR eggNOG; ENOG4110ZR7; LUCA. DR OMA; AMYAPEI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 118 Uncharacterized protein MJ0023. FT /FTId=PRO_0000106659. FT TRANSMEM 95 115 Helical. {ECO:0000255}. SQ SEQUENCE 118 AA; 13938 MW; E00CAF8EA0E72809 CRC64; MKSIRISSDY RAKRDNASCF DETFLKSFAE ELYNAIIEII KENKTIIKNE VRDELRNELA TKEDILLVEE RLGKKIELLN QKIEREIKLV RRDMIIINLV IILAMYAPEI IGKLLIFR // ID Y034_METJA Reviewed; 316 AA. AC Q60349; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=UPF0051 protein MJ0034; GN OrderedLocusNames=MJ0034; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0051 (ycf24) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98015.1; -; Genomic_DNA. DR PIR; B64304; B64304. DR ProteinModelPortal; Q60349; -. DR STRING; 243232.MJ_0034; -. DR EnsemblBacteria; AAB98015; AAB98015; MJ_0034. DR KEGG; mja:MJ_0034; -. DR eggNOG; arCOG01715; Archaea. DR eggNOG; COG0719; LUCA. DR InParanoid; Q60349; -. DR KO; K07033; -. DR OMA; PVHLCFG; -. DR PhylomeDB; Q60349; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016226; P:iron-sulfur cluster assembly; IEA:InterPro. DR InterPro; IPR000825; SUF_FeS_clus_asmbl_SufBD. DR Pfam; PF01458; UPF0051; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 316 UPF0051 protein MJ0034. FT /FTId=PRO_0000147379. SQ SEQUENCE 316 AA; 35022 MW; 3657AC25CBE473D1 CRC64; MSIKEELMEI IEAIKYTSEK PEEIVHGKGP RIIVKESRII DVQGDEGIIL EGKEEDGKIK AKIIVKKGYK FKYPIHMCFG ITEENISQII DVEIILEEDS SISLMSHCSF PKGKGIKHIM NGIIKIGKNA KFSYNEFHYH GMDGDILVKP TVKVEIDEGG IYISNFTLTK GRIGTLDIEQ EIIAKKDAII DITTRTYAIK EDVVKVNEVV KLNGENAKCI IKSRGAAMDN SKISLKLKIE GNAPYSKGHI DCAEIVKGNA EVESIPIVVV RDDKARITHE AAIGSVDKKQ LETLMAKGLD EDEATEIIVK GMIGDL // ID Y035_METJA Reviewed; 250 AA. AC Q60350; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0035; GN OrderedLocusNames=MJ0035; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98016.1; -; Genomic_DNA. DR PIR; C64304; C64304. DR ProteinModelPortal; Q60350; -. DR STRING; 243232.MJ_0035; -. DR EnsemblBacteria; AAB98016; AAB98016; MJ_0035. DR KEGG; mja:MJ_0035; -. DR eggNOG; arCOG04236; Archaea. DR eggNOG; COG0396; LUCA. DR InParanoid; Q60350; -. DR KO; K09013; -. DR OMA; PARYDGI; -. DR PhylomeDB; Q60350; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 250 Uncharacterized ABC transporter ATP- FT binding protein MJ0035. FT /FTId=PRO_0000093216. FT DOMAIN 7 244 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 39 46 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 250 AA; 28258 MW; B49671A4698ABED1 CRC64; MVSIMLLKVE DLHVYRGNRE ILKGVNLTVE ENEIHAIIGP NGAGKSTLAY TIMGISGYKP TKGRIIFKGV DIIDKNITER ARMGMTLAWQ EPARFEGIKV KNYLMLGMNE KYKKDKEIAE EKIREALKLV NLDPDKYLDR YVDETLSGGE RKRIELASII CMEPDLAILD EPDSGIDIVS FDEIKRVFDY LKDKGCSLLV ITHREELAEH ADRVSLICAG EVIKSGDPKE VGEFYKKECG KCYKKVPDGK // ID Y046_METJA Reviewed; 261 AA. AC Q60354; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=Putative methyltransferase MJ0046; DE EC=2.1.1.-; GN OrderedLocusNames=MJ0046; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98026.1; -; Genomic_DNA. DR PIR; F64305; F64305. DR ProteinModelPortal; Q60354; -. DR STRING; 243232.MJ_0046; -. DR EnsemblBacteria; AAB98026; AAB98026; MJ_0046. DR KEGG; mja:MJ_0046; -. DR eggNOG; arCOG00111; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q60354; -. DR OMA; TPINRYL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0052907; F:23S rRNA (adenine(1618)-N(6))-methyltransferase activity; IBA:GO_Central. DR GO; GO:0070475; P:rRNA base methylation; IBA:GO_Central. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR010286; rRNA_lsu_MeTfrase_F-like. DR InterPro; IPR029063; SAM-dependent_MTases. DR PANTHER; PTHR13393; PTHR13393; 1. DR Pfam; PF05971; Methyltransf_10; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 261 Putative methyltransferase MJ0046. FT /FTId=PRO_0000218022. SQ SEQUENCE 261 AA; 29931 MW; E46C39551D2C34CF CRC64; MLGLKIEDAI KYNEKLKKYV YKKGDKLRIN FKDKEALIEY NKTVLKVLFD LDIEFHKNGL IPTPINRYLF IKSTFETLKE LGIEKPTVLE IGTGHSAIIS LLIKKFYNAE VYATEVDEEF IDFAKRNIEK NKLDIKIINS KGRAIEGIEE LKDKKFDLII SYPPFYSKNS VASGRKFGGA LAKNVELIGG GKFGEEFSFK IIEEGINFLN KKGVISLMMP KKPEKRRELI IKKMKEVGLD VEVDEIKTGN RLRYIIKGIK G // ID Y054_METJA Reviewed; 281 AA. AC Q60361; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0054; GN OrderedLocusNames=MJ0054; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98034.1; -; Genomic_DNA. DR PIR; F64306; F64306. DR ProteinModelPortal; Q60361; -. DR STRING; 243232.MJ_0054; -. DR EnsemblBacteria; AAB98034; AAB98034; MJ_0054. DR KEGG; mja:MJ_0054; -. DR eggNOG; arCOG04893; Archaea. DR eggNOG; COG4022; LUCA. DR InParanoid; Q60361; -. DR OMA; QGLCGRI; -. DR PhylomeDB; Q60361; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR009181; UCP004929_methan. DR Pfam; PF09872; DUF2099; 1. DR PIRSF; PIRSF004929; UCP004929; 1. DR TIGRFAMs; TIGR03275; methan_mark_8; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 281 Uncharacterized protein MJ0054. FT /FTId=PRO_0000106672. SQ SEQUENCE 281 AA; 31169 MW; ABDB1F83C578B7B3 CRC64; MDRHVMEALG KARVVVENGR VVEVTEPKIK YCPLFAKHRG IKEITKESIK ENIEFRIKDF GLFTKNRVVE ESRYIVPFGA SEILMSALKR KAIDVAVIVA DCAGTIITSN PNLVQGLCGR ISGIIETSPI LEVIEKIEKA GGVVLNKKTA EINQFEGVKK AIELDYKKIA VTVTNLEDAK RCKSLENDEI KILTFGVHLT GIEGSEEIAK YFDLVTACAS KVLREKLKGK IKAQIGKTIP IFALSDFGKE ILLERAKDLD KVLISIENLP VLNDNQPKPL I // ID Y065_METJA Reviewed; 363 AA. AC Q60370; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0065; GN OrderedLocusNames=MJ0065; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98045.1; -; Genomic_DNA. DR PIR; A64308; A64308. DR ProteinModelPortal; Q60370; -. DR STRING; 243232.MJ_0065; -. DR EnsemblBacteria; AAB98045; AAB98045; MJ_0065. DR KEGG; mja:MJ_0065; -. DR eggNOG; arCOG03231; Archaea. DR eggNOG; COG4069; LUCA. DR InParanoid; Q60370; -. DR OMA; KSKITGH; -. DR PhylomeDB; Q60370; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR012032; UCP006598. DR Pfam; PF09890; DUF2117; 1. DR PIRSF; PIRSF006598; UCP006598; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 363 Uncharacterized protein MJ0065. FT /FTId=PRO_0000106676. SQ SEQUENCE 363 AA; 40405 MW; F56B42C9C1F4D5C5 CRC64; MRIGVVIHGP EIIDSGYALK IINLLKKFGE VKAKLGGTMG RVAVIDNNLQ DIIDISEKLM PSQSLKKLAN NDILILMNYG KSKITGHTFG KIVVERANLN KPIIQIERPG EEDGTIIIWN DDNSKIVKEI ANYLSKELNL KIEKCISNGL EVWEKEGRVF RKVHGVDVGE AILVNGIVVG KAKSNEVILI AENGKLVDII GGELKEGGIE KLKNVDLKKA VIKTGILRRH PTNPKIESKE IDEGYTIIIN HAGEDVIEMI KNKGVVAVIT IGDDTTTICG DILARFGIKI IGITDGDRDE ILKNPVILKG SVIFLIKNMR DDDVGRILEK NLNLNKKYCY QELLDEVKKI FNDNNICYEE FVY // ID Y074_METJA Reviewed; 358 AA. AC Q60380; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Uncharacterized ATP-binding protein MJ0074; GN OrderedLocusNames=MJ0074; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98056.1; -; Genomic_DNA. DR PIR; B64309; B64309. DR ProteinModelPortal; Q60380; -. DR SMR; Q60380; 259-358. DR STRING; 243232.MJ_0074; -. DR EnsemblBacteria; AAB98056; AAB98056; MJ_0074. DR KEGG; mja:MJ_0074; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q60380; -. DR KO; K06921; -. DR OMA; YVIEECK; -. DR PhylomeDB; Q60380; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 358 Uncharacterized ATP-binding protein FT MJ0074. FT /FTId=PRO_0000184665. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 358 AA; 42310 MW; 34BBAEF2DFCF4876 CRC64; MKFFDREKEI AEILHILNRE PDDVYFIYGP INSGKTALIN EIINNRLDKD KYVVFYFDLR EIFISKYDDF IEVLFEEYEG NKKPVEIIKS LIKDVPSLCG IPAPKNTLEE ILKKKTTKNV FRYITKVLMD IKKEGKQPIL IIDELQKIGD MKINGFLIYE LFNYFVSLTK HKHLCHVFCL SSDSLFIERV YNEAMLDGRA KYLLVDDFDK ETALKFMDFL AKENNISLTN EDKELIYNYV GGKPKDIKYV VEESNFKDLK EVLDYLLNDE ISKLDMFLEI LDYSKPRVEV GNEVIEINKE DIIKALRLFK DKYEIPKKDI PTPVYVYLVK ENILFLNPQK RILKPQSYLV WNAIKRLL // ID Y075_METJA Reviewed; 365 AA. AC Q60388; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Uncharacterized ATP-binding protein MJ0075; GN OrderedLocusNames=MJ0075; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98065.1; -; Genomic_DNA. DR PIR; C64309; C64309. DR ProteinModelPortal; Q60388; -. DR SMR; Q60388; 271-362. DR STRING; 243232.MJ_0075; -. DR DNASU; 1450914; -. DR EnsemblBacteria; AAB98065; AAB98065; MJ_0075. DR KEGG; mja:MJ_0075; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q60388; -. DR KO; K06921; -. DR PhylomeDB; Q60388; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 365 Uncharacterized ATP-binding protein FT MJ0075. FT /FTId=PRO_0000184666. FT NP_BIND 31 38 ATP. {ECO:0000255}. SQ SEQUENCE 365 AA; 43328 MW; DDE2574318A3E099 CRC64; MIMKFFDRER EINEILGILD ETPDNIYFIY GPINSGKTTL MMEIINRLKD DKKYRIFYYN LRGVRISSYS DFFDIMFEIR EDNKFKQMVK DADVLVEGIK FIEKTAKLFN ESIILPSDLA KVILSKQKGF DVFRYLERVF REMNKKGLKP VIIIDELQRL KGLKSNGELI DDLFNFFVRL TKELHITHCF CLSSDSLFIE YVYDRAELRG RADYILVDDF DKETALKFMD FLSEDILGRK LSEDEKELIY SYVGGKPKDV YDVIIKLKLG KELKDILEFM LKEEIQKLKY FLEDVKEDDE ELYNKIVDAL KIFKENYEIE DIKIPKNIRE FLVKKNILFL NPIEGTLKPQ SFLVWNAIKK LLNGH // ID Y079_METJA Reviewed; 380 AA. AC Q60389; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0079; GN OrderedLocusNames=MJ0079; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98059.1; -; Genomic_DNA. DR PIR; G64309; G64309. DR ProteinModelPortal; Q60389; -. DR STRING; 243232.MJ_0079; -. DR EnsemblBacteria; AAB98059; AAB98059; MJ_0079. DR KEGG; mja:MJ_0079; -. DR eggNOG; arCOG00436; Archaea. DR eggNOG; COG0714; LUCA. DR InParanoid; Q60389; -. DR KO; K03924; -. DR OMA; IEILCKM; -. DR PhylomeDB; Q60389; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011704; ATPase_dyneun-rel_AAA. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07728; AAA_5; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 380 Uncharacterized protein MJ0079. FT /FTId=PRO_0000106685. SQ SEQUENCE 380 AA; 44550 MW; E81A7A8C5365AE59 CRC64; MSEIMHKLEK IREELNSYFL ERREEIDIAL TSILANEHTV FLGNPGVAKS QLIRAIASHI NANYFEKLIT RFTTEDELFG PLSIKELKDN DRFVRKTSGY LPTAEIAFLD EVFKANSSIL NALLSIINER IYHNGDKIEK VPLISLFGAS NELPEENELL AFYDRFLFRK VVRGIRSCEN LVKLIKLDEE YKPKTTISIK ELRKMQEKAN EVDIENIIGY LVDIKKKLSQ NHIYISDRRF KKSVKAIKCF AYLNGRREAE IEDLEILRHI FWDDIDDILI VSKVIFDITN KYAEQVLDKA EIIKNLKNEL KYIDIKKIGE CKKDYNKLIE ILCKMAYIRL ELKKIRNEAI INKRKTDFID EVIKETDEFN NYIEGILNEL // ID Y088_METJA Reviewed; 180 AA. AC Q57553; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0088; GN OrderedLocusNames=MJ0088; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98075.1; -; Genomic_DNA. DR PIR; H64310; H64310. DR STRING; 243232.MJ_0088; -. DR EnsemblBacteria; AAB98075; AAB98075; MJ_0088. DR KEGG; mja:MJ_0088; -. DR OMA; IMGYIRR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 180 Uncharacterized protein MJ0088. FT /FTId=PRO_0000106688. SQ SEQUENCE 180 AA; 21797 MW; CD2C47D358C5649F CRC64; MPNIWGGMLE KTVKITFIFE SEKRLNWEGY VNYLIFAHYF KLIYILLRNN KELLERILKD SLDNKEDYHK LGKYLHHDIM GYIRRHGYLS FLPFTPLPFY KELCEKFMTK IPEKPIIDYK CIERIENNKI IFEFEGEEEC LRCLMYLKDS SIDESIKVIK SEEMVVKILE ILLYILHNLL // ID Y089_METJA Reviewed; 254 AA. AC Q57554; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0089; GN OrderedLocusNames=MJ0089; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98070.1; -; Genomic_DNA. DR PIR; A64311; A64311. DR ProteinModelPortal; Q57554; -. DR STRING; 243232.MJ_0089; -. DR EnsemblBacteria; AAB98070; AAB98070; MJ_0089. DR KEGG; mja:MJ_0089; -. DR eggNOG; arCOG00198; Archaea. DR eggNOG; COG1120; LUCA. DR InParanoid; Q57554; -. DR KO; K02013; -. DR OMA; DRTIFER; -. DR PhylomeDB; Q57554; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 254 Uncharacterized ABC transporter ATP- FT binding protein MJ0089. FT /FTId=PRO_0000093217. FT DOMAIN 6 239 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 254 AA; 28528 MW; 379CB9A38BA787FA CRC64; MSLMILSVDG VEFAYKSRQI LNNIKFEVKR GEVVSILGVN GAGKSTLLKC INKILKPKRG TILIDNFDIK NLDNLELAKK VGYVPQRAEG NYMTVFDAVL LGRKPHIKWE VSDRDIEITH KVLKLLNLED YALRYTNELS GGELQKVIIA RALVQEPQIL LLDEPTNNLD LKNQLEVMKI IMDISKSQNI ASIVVMHDLN LALRYSDKFI MLKDGVIYAE GGREVINPEN IKAVYGVDAY IENVRGIPVV VPIG // ID Y092_METJA Reviewed; 489 AA. AC Q57557; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 98. DE RecName: Full=Uncharacterized iron-sulfur protein MJ0092; GN OrderedLocusNames=MJ0092; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the succinate dehydrogenase/fumarate CC reductase iron-sulfur protein family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 2Fe-2S ferredoxin-type domain. CC {ECO:0000255|PROSITE-ProRule:PRU00465}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98073.1; -; Genomic_DNA. DR PIR; D64311; D64311. DR ProteinModelPortal; Q57557; -. DR STRING; 243232.MJ_0092; -. DR EnsemblBacteria; AAB98073; AAB98073; MJ_0092. DR KEGG; mja:MJ_0092; -. DR eggNOG; arCOG00333; Archaea. DR eggNOG; COG0247; LUCA. DR eggNOG; COG0479; LUCA. DR InParanoid; Q57557; -. DR KO; K18210; -. DR OMA; STECENI; -. DR PhylomeDB; Q57557; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:InterPro. DR Gene3D; 3.10.20.30; -; 1. DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type. DR InterPro; IPR006058; 2Fe2S_fd_BS. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR012675; Beta-grasp_dom. DR InterPro; IPR004017; Cys_rich_dom. DR InterPro; IPR009051; Helical_ferredxn. DR InterPro; IPR004489; Succ_DH/fum_Rdtase_Fe-S. DR InterPro; IPR025192; Succ_DH/fum_Rdtase_N. DR Pfam; PF02754; CCG; 2. DR Pfam; PF13085; Fer2_3; 1. DR Pfam; PF13183; Fer4_8; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR SUPFAM; SSF54292; SSF54292; 1. DR TIGRFAMs; TIGR00384; dhsB; 1. DR PROSITE; PS00197; 2FE2S_FER_1; 1. DR PROSITE; PS51085; 2FE2S_FER_2; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 2Fe-2S; 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; Repeat. FT CHAIN 1 489 Uncharacterized iron-sulfur protein FT MJ0092. FT /FTId=PRO_0000158709. FT DOMAIN 2 84 2Fe-2S ferredoxin-type. FT {ECO:0000255|PROSITE-ProRule:PRU00465}. FT DOMAIN 123 155 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 177 205 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 48 48 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 53 53 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 56 56 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 68 68 Iron-sulfur 1 (2Fe-2S). {ECO:0000250}. FT METAL 134 134 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 137 137 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 140 140 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 144 144 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 186 186 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 189 189 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 192 192 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 196 196 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 489 AA; 56128 MW; A634315770434C3D CRC64; MIKITVKRFN GEKEYLESYE VPENITVLEA LEYINKHYEA NILFRASCRN AQCGSCAVTI NGEPRLACET KVEDGMIIEP LRGFKVIRDL IVDREPYYKK LLGIKNYLIR KNYPEELEIL IPKYVEENKE LRGCIDCLSC LSVCPAREVS DYPGPTFMRQ LARFAFDKRD EDGREITAYF ENIYNCTTCA KCVEVCPKEI DIVHRAIEKL RALAFSKGYY IENHLKVREN VLKYNRSVVE EELPLLKQVA DFYPAESEKL RVAFFTGCLV DFRLQNVGKD AIKVLNAHGV SVVIPKNQVC CGSPFFRTGQ RDVAEMLKRK NLEIFNKLDV DCVVTICAGC GSTLKNDYKE RKFEVKDITE VLTEVGLLKY KPLKMRITYH DPCHLRRGQK IYKQPREILK SIPELEFIDI EARCCGAGGG VRSGKPDIAN LIGKSRARMI YDANVDAVIT VCPFCEYHIR DSLKRFKEEN KIDKEIDVMN IVSLLAKVI // ID Y1011_METJA Reviewed; 130 AA. AC Q58417; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1011; GN OrderedLocusNames=MJ1011; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99012.1; -; Genomic_DNA. DR PIR; B64426; B64426. DR ProteinModelPortal; Q58417; -. DR STRING; 243232.MJ_1011; -. DR DNASU; 1451908; -. DR EnsemblBacteria; AAB99012; AAB99012; MJ_1011. DR KEGG; mja:MJ_1011; -. DR eggNOG; arCOG00232; Archaea. DR eggNOG; COG0704; LUCA. DR PhylomeDB; Q58417; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR026022; PhoU_dom. DR Pfam; PF01895; PhoU; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 130 Uncharacterized protein MJ1011. FT /FTId=PRO_0000107141. SQ SEQUENCE 130 AA; 15278 MW; 377FCAAB4F027635 CRC64; MPKKFDDIVN EMDRKIELLG EEIIKNLNLS VEGYCTNKKD ICNLVIYKNN NIIKNLESLE MYSVKALCLY RPVSKDLRKL LTIIKLCSML EKIEECAVKI SFVLLNSKFN FDRNDKYIKR MASLTEEIIY // ID Y1059_METJA Reviewed; 406 AA. AC Q58459; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized glycosyltransferase MJ1059; DE EC=2.4.-.-; GN OrderedLocusNames=MJ1059; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family. CC Glycosyltransferase 4 subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99063.1; -; Genomic_DNA. DR PIR; B64432; B64432. DR ProteinModelPortal; Q58459; -. DR STRING; 243232.MJ_1059; -. DR CAZy; GT4; Glycosyltransferase Family 4. DR EnsemblBacteria; AAB99063; AAB99063; MJ_1059. DR KEGG; mja:MJ_1059; -. DR eggNOG; arCOG01403; Archaea. DR eggNOG; COG0438; LUCA. DR InParanoid; Q58459; -. DR OMA; HEWFENN; -. DR PhylomeDB; Q58459; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016757; F:transferase activity, transferring glycosyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001296; Glyco_trans_1. DR InterPro; IPR028098; Glyco_trans_4-like_N. DR Pfam; PF13477; Glyco_trans_4_2; 1. DR Pfam; PF00534; Glycos_transf_1; 1. PE 3: Inferred from homology; KW Complete proteome; Glycosyltransferase; Reference proteome; KW Transferase. FT CHAIN 1 406 Uncharacterized glycosyltransferase FT MJ1059. FT /FTId=PRO_0000080321. SQ SEQUENCE 406 AA; 48270 MW; 7CB71CDDB02C7F9D CRC64; MSNKKKQLTV MGTVWDFWSV LKMFDKLYES KYISFYEPWL KGEIDKEKII LFNEKSKNPL LWPFKILKRT YKILKIIREF KPDLVITHHD DANVSIIPVI LLNKIFKISN NTKFILWVRN NPIESYKEGL YSKIIILAYK YFYKYADIII VQTQENKKII ESHFKSLKNK TKIVPNVYEI DKLQQLSNEP LEKQYRNIFK DSFVFINIGR LTEQKGQWFL IRSFKRVTEK YPNAKLIILG DGELKNKLQE LINKLNLQNN VYLLGMQKNP FKFLKHSNCF VFSSLWEGLP NTVIEALSLN LPVISTDCKT GPREILCPEL NISDKIDYPY YGKYGILTKP FSREFIWQDL NEKPLIEEEK MLADLMIKMI EDEDLRKRYS NGLERAKDFD IEKIIKEWKL LIEGTI // ID Y1063_METJA Reviewed; 243 AA. AC Q58463; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ1063; GN OrderedLocusNames=MJ1063; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99066.1; -; Genomic_DNA. DR PIR; F64432; F64432. DR ProteinModelPortal; Q58463; -. DR STRING; 243232.MJ_1063; -. DR EnsemblBacteria; AAB99066; AAB99066; MJ_1063. DR KEGG; mja:MJ_1063; -. DR eggNOG; ENOG4102TT4; Archaea. DR eggNOG; COG1861; LUCA. DR InParanoid; Q58463; -. DR KO; K07257; -. DR OMA; SHRFTID; -. DR PhylomeDB; Q58463; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR003329; Cytidylyl_trans. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF02348; CTP_transf_3; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 243 Uncharacterized protein MJ1063. FT /FTId=PRO_0000213212. SQ SEQUENCE 243 AA; 28442 MW; EA93C730AD962980 CRC64; MKIIGIIQAR TGSKRLKNKV LLKLGDRCIL EILLERLKKS KKLDDIIVAT TIKKEDNAIV ELCNSLGVNV FRGSEKDVLD RFYNASKFYS GDVIVRITGD NPLTSIELID KQVEYLLKNN FDYVSTKNII LGLSSEVFTF DALEKAWKNA KEKYQREHVT PYIYENPNLF KVFYLEPPEY LKREGIRLTI DTIKDFKLYL ELQKHFDLIN VDIRQIIDFL DKNPQIKNIN SNVRQKSYRE VEE // ID Y1064_METJA Reviewed; 214 AA. AC Q58464; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized acetyltransferase MJ1064; DE EC=2.3.1.-; GN OrderedLocusNames=MJ1064; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the transferase hexapeptide repeat family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99067.1; -; Genomic_DNA. DR PIR; G64432; G64432. DR ProteinModelPortal; Q58464; -. DR STRING; 243232.MJ_1064; -. DR EnsemblBacteria; AAB99067; AAB99067; MJ_1064. DR KEGG; mja:MJ_1064; -. DR eggNOG; arCOG01854; Archaea. DR eggNOG; COG0110; LUCA. DR InParanoid; Q58464; -. DR OMA; YTHEPVI; -. DR PhylomeDB; Q58464; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR018357; Hexapep_transf_CS. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 1. DR Pfam; PF14602; Hexapep_2; 1. DR SUPFAM; SSF51161; SSF51161; 1. DR PROSITE; PS00101; HEXAPEP_TRANSFERASES; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Reference proteome; Repeat; KW Transferase. FT CHAIN 1 214 Uncharacterized acetyltransferase MJ1064. FT /FTId=PRO_0000068760. SQ SEQUENCE 214 AA; 23402 MW; 908D40935BC72E76 CRC64; MSMIKLLKNT LKDPKKIMRA LEFAPSFVFG KIYLSIFGIN PLKVHNFGKI HIRKYDSSTI IIKSGILLRD VEIAARGNGK IIIGENFHCE PYVRLNVFEE GILEIGDNCG IGSFSIINAT KKITIGSNVL ISSHVHIIDG DHGFKKGELI RNQKMVSEPI EIGDDVWIGT GVKILKGVKI GEGAVIGAGS VVTRDIPPYS VAVGVPARVI KKRE // ID Y1068_METJA Reviewed; 507 AA. AC Q58467; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 89. DE RecName: Full=Uncharacterized membrane protein MJ1068; GN OrderedLocusNames=MJ1068; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polysaccharide synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99070.1; -; Genomic_DNA. DR PIR; B64433; B64433. DR ProteinModelPortal; Q58467; -. DR STRING; 243232.MJ_1068; -. DR EnsemblBacteria; AAB99070; AAB99070; MJ_1068. DR KEGG; mja:MJ_1068; -. DR eggNOG; arCOG02209; Archaea. DR eggNOG; COG2244; LUCA. DR InParanoid; Q58467; -. DR OMA; GYLDGIC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR029303; Polysacc_synt_C. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. DR Pfam; PF14667; Polysacc_synt_C; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 507 Uncharacterized membrane protein MJ1068. FT /FTId=PRO_0000166460. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 86 106 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 193 213 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TRANSMEM 275 295 Helical. {ECO:0000255}. FT TRANSMEM 323 343 Helical. {ECO:0000255}. FT TRANSMEM 355 375 Helical. {ECO:0000255}. FT TRANSMEM 387 407 Helical. {ECO:0000255}. FT TRANSMEM 408 428 Helical. {ECO:0000255}. FT TRANSMEM 444 464 Helical. {ECO:0000255}. FT TRANSMEM 467 487 Helical. {ECO:0000255}. SQ SEQUENCE 507 AA; 57664 MW; A345A38772278235 CRC64; MSYKEKAVKG VSWHLLSYFL AAPIAYLVRV LYANEIPKLD VGLFYAVLDF FSMLVVFRAF GLDQALIRYI PKYLAENRLD MLKSSIVFVG ILQTILAFIV AFLVVIFAPY IAEFYINNQG QFTGRLDLVI NILIIMAMGY YFLDSIVAFF SNILTGFQLQ NYASSTRVVR ILSVFIFSLI FIYLFNVHNA YVPSVSYLLM AVVMIIIYGY IVVKKIFPKF AKEKVIFSRK LIRNLFSYGM YVMIGYAGSL ILGYLDGICL TYFTGLNAVA DYRNVAMPTV NILSYFAFSV GAVLFPMSSE LWEKGYKKAL SYGVEKVFLY SLIIVTPLAI LMAYFPTVII NILFNPKYLS AAPAIQILSF GAMFLTFNSI GFNILNGIGR PNISTKILYI GASFNLIFNI LLIPKFGIIG AAITTVFGYF IMWIFQIWFL NKLLEHQFLN KKWILVILVG IFSLIPVMFI KDLIDNVILQ LFVCGVVYFG IYILGIFGLK IINIYEVKDI ISKIIKR // ID Y110_METJA Reviewed; 93 AA. AC Q57574; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0110; GN OrderedLocusNames=MJ0110; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98095.1; -; Genomic_DNA. DR PIR; F64313; F64313. DR STRING; 243232.MJ_0110; -. DR EnsemblBacteria; AAB98095; AAB98095; MJ_0110. DR KEGG; mja:MJ_0110; -. DR eggNOG; arCOG05022; Archaea. DR eggNOG; COG4095; LUCA. DR InParanoid; Q57574; -. DR KO; K15383; -. DR OMA; RDISIWQ; -. DR PhylomeDB; Q57574; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR006603; PQ-loop_rpt. DR Pfam; PF04193; PQ-loop; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein MJ0110. FT /FTId=PRO_0000106697. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. SQ SEQUENCE 93 AA; 10727 MW; 5BD1158C16D3D0D8 CRC64; MVINMDFDIT VIGYIAGTLT TFASLPQLIK SLKEKDMSNI SLAFVITFTT GLTLWLIYGI LRNDYPIIVF NILSLMFWIP ITYLKIRDEM RKS // ID Y1145_METJA Reviewed; 65 AA. AC Q58545; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1145; DE Flags: Precursor; GN OrderedLocusNames=MJ1145; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99155.1; -; Genomic_DNA. DR PIR; H64442; H64442. DR STRING; 243232.MJ_1145; -. DR EnsemblBacteria; AAB99155; AAB99155; MJ_1145. DR KEGG; mja:MJ_1145; -. DR eggNOG; arCOG05069; Archaea. DR eggNOG; ENOG410Z4EC; LUCA. DR OMA; YWACQAY; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 65 Uncharacterized protein MJ1145. FT /FTId=PRO_0000014009. SQ SEQUENCE 65 AA; 7693 MW; 1DD7EF92E847F51F CRC64; MDDIDRKAIS LLMDATLMSE DEIERTLKIL RNMARIKKRK EKNLKSIRDV LDYWACQAYK SSMKA // ID Y1161_METJA Reviewed; 167 AA. AC Q58561; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1161; GN OrderedLocusNames=MJ1161; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99175.1; -; Genomic_DNA. DR PIR; H64444; H64444. DR STRING; 243232.MJ_1161; -. DR EnsemblBacteria; AAB99175; AAB99175; MJ_1161. DR KEGG; mja:MJ_1161; -. DR eggNOG; arCOG09677; Archaea. DR eggNOG; ENOG41110F3; LUCA. DR OMA; DYQVING; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 167 Uncharacterized protein MJ1161. FT /FTId=PRO_0000107197. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 143 162 Helical. {ECO:0000255}. SQ SEQUENCE 167 AA; 18977 MW; 7A3CA6409CCC6640 CRC64; MRDNIRSINK LLIYLVLILS AMFLCQNVFA EDYNAIEITV KNISSGEILY QKIFPKDEAF SDYQVINGFT IDIHYNPNYP GMVYKVHQSN NHFIFNVSGE LNWGSYQQSG DIACIVDVIH YDFPPPSNTT SNTTTTSSSS TKAPIPLSVY LAITAFFTYI IYRKSKT // ID Y1182_METJA Reviewed; 366 AA. AC Q58582; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 68. DE RecName: Full=Uncharacterized protein MJ1182; GN OrderedLocusNames=MJ1182; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99183.1; -; Genomic_DNA. DR PIR; E64447; E64447. DR ProteinModelPortal; Q58582; -. DR STRING; 243232.MJ_1182; -. DR EnsemblBacteria; AAB99183; AAB99183; MJ_1182. DR KEGG; mja:MJ_1182; -. DR eggNOG; arCOG00570; Archaea. DR eggNOG; COG0644; LUCA. DR InParanoid; Q58582; -. DR OMA; CAYYKND; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR SUPFAM; SSF51905; SSF51905; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 366 Uncharacterized protein MJ1182. FT /FTId=PRO_0000107205. SQ SEQUENCE 366 AA; 42216 MW; FECB31A9BE771A51 CRC64; MQVCIIGAGL SGSILYRLLS EDGFYINIYD HVLVRGCKSM NFIFSNKNEI LTVKKVLKTV NINIKDYIIR EIKEVNIGGD NYYPNKKIYV INKSKLIEDL VPRTVVTNRE FNPVIRRYTT KVIDTGVIVR EFNTEAETKF YDLVVDASGC AKVLQLGNVY DKYKNDIKTC QFLIAYENEE SPEKFDKFFI DEIKIHKGKP MIGYTWITPI DDGLYHVGCA YYKNDHELWT YLTKYTKKMF GSDYVRVCGC TSKINGNLIS ESFIGGIYEK RCVAGVGESI GLTTPLGHGN IYAIISAYIL SRFIKKYDLN EAVLKYKDYI PKKFAELDKE KKAVRNFNVL RITKLLRDYY NIPAHESMKI ILKSLY // ID Y1185_METJA Reviewed; 622 AA. AC Q58585; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ1185; GN OrderedLocusNames=MJ1185; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the AOR/FOR family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99186.1; -; Genomic_DNA. DR PIR; H64447; H64447. DR ProteinModelPortal; Q58585; -. DR STRING; 243232.MJ_1185; -. DR EnsemblBacteria; AAB99186; AAB99186; MJ_1185. DR KEGG; mja:MJ_1185; -. DR eggNOG; arCOG05072; Archaea. DR eggNOG; COG2414; LUCA. DR InParanoid; Q58585; -. DR KO; K11389; -. DR OMA; CRFHRGW; -. DR PhylomeDB; Q58585; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016625; F:oxidoreductase activity, acting on the aldehyde or oxo group of donors, iron-sulfur protein as acceptor; IEA:InterPro. DR Gene3D; 1.10.569.10; -; 1. DR Gene3D; 3.60.9.10; -; 1. DR InterPro; IPR013984; Ald_Fedxn_OxRdtase_2. DR InterPro; IPR013983; Ald_Fedxn_OxRdtase_N. DR InterPro; IPR001203; OxRdtase_Ald_Fedxn_C. DR Pfam; PF01314; AFOR_C; 1. DR Pfam; PF02730; AFOR_N; 1. DR SMART; SM00790; AFOR_N; 1. DR SUPFAM; SSF48310; SSF48310; 1. DR SUPFAM; SSF56228; SSF56228; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 622 Uncharacterized protein MJ1185. FT /FTId=PRO_0000107208. SQ SEQUENCE 622 AA; 72499 MW; 6DD910C20DC47678 CRC64; MKNALINATT KKFEIIEKTV LPITWGLYWH NKFETWKYDA YDEKNVFCFG SGVLPVIGGH RLIFSFRSPL WDGFYFSSMG GAGYQFKSTG LNNVAIIGRC ENPSILVIEN DGQLRIDFIE VKEELKTVYE VSKYILELYK DKNLRSVVVG EAAKRTNMGG LFSQTVRNGK FVEGSEDWAA RGGGGSVLYR AHNIMGIVFF GDEKEDKEEK EKAKKIIESY YKKPMSKVVL EHTKKYRYDE ETKTGGTFGN NWLLYKEKVP IFNWRMPYID KEDRKKILEK ILKFYLEIFN KETIEPKRWA NCGEPCPVLC KKYRNKNKVD YEPYASNGTL LGIFDLYEAD RVVKTADALG FDAIEIGNLT AWVFELLDVG LLKEEELNIK KPIFDYKKIT NDDDEEIREI SKHNAEQAIK FMHNLAENSN DLYKILSLGK RKAAKILNER FKSRVNKIGK KFNDFAVYVP FGDWGEIAPN LYWTPGFFMP FVIQGRYLTY YKPEFNEPEK LAELVVESIK LELPIENLGI CRFHRKWLKP VLKELVKELL GIEDIVEDSI NLYREICEYN KKIGYPAKIE SERVKDLIIA MAKEFGNEEW TKKFENKENV DEYVKRVLNK YSELLGIDWR IS // ID Y1188_METJA Reviewed; 270 AA. AC Q58587; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1188; GN OrderedLocusNames=MJ1188; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99192.1; -; Genomic_DNA. DR PIR; B64448; B64448. DR ProteinModelPortal; Q58587; -. DR STRING; 243232.MJ_1188; -. DR EnsemblBacteria; AAB99192; AAB99192; MJ_1188. DR KEGG; mja:MJ_1188; -. DR eggNOG; arCOG01897; Archaea. DR eggNOG; COG1082; LUCA. DR InParanoid; Q58587; -. DR OMA; SLFFWEY; -. DR PhylomeDB; Q58587; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 270 Uncharacterized protein MJ1188. FT /FTId=PRO_0000107209. SQ SEQUENCE 270 AA; 32467 MW; 74DBB2C154B943A7 CRC64; MMKIGVSTLF FWEYPMVEIF DIFRDIGIKC MEFFPENPDF WDNRFDLDYI ADLRKEFLKF DVALHNPHIE LNPSSLNPYV REAVIKETLW SIELAKFYRC KLITIHPGKR PTNRSPTDEE YEAFFKYLDR TLEVAINKNI TICVENMPER INRIGWSPEE MEWILKRYDE LLYMTLDFAH AKEYMEEFLE SVIDYIKHTH ISGVVNRKDH FPLRKSEIDF SPYIKALLDY GYNGMFNLEL DDRRLEKNPV TKEEKIEEVI KDIEFLESII // ID Y1199_METJA Reviewed; 146 AA. AC Q58599; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1199; GN OrderedLocusNames=MJ1199; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To A.pernix APE2001. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99204.1; -; Genomic_DNA. DR PIR; F64449; F64449. DR ProteinModelPortal; Q58599; -. DR STRING; 243232.MJ_1199; -. DR REBASE; 4871; MjaORF1200P. DR EnsemblBacteria; AAB99204; AAB99204; MJ_1199. DR KEGG; mja:MJ_1199; -. DR eggNOG; arCOG01019; Archaea. DR eggNOG; COG4080; LUCA. DR InParanoid; Q58599; -. DR OMA; MHILENN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR018665; DUF2122_RecB-nuclease-rel. DR Pfam; PF09895; DUF2122; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Uncharacterized protein MJ1199. FT /FTId=PRO_0000107212. SQ SEQUENCE 146 AA; 16296 MW; 9934CB449198D85C CRC64; MRKMFICLHN TYSAKQVEEF GRIAYGFDIN TIVVTKATAS AAQSGIPTLH KMAYKLGKNV LFFEELDDAI EVLRPEKVFL IGNKSICDEK VDFNEVGEND LVVFCGASTG FTKLELEKGL GRYIVENEIG ALGNLAIFLY EMSKKI // ID Y1207_METJA Reviewed; 226 AA. AC Q58604; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized N-acetyltransferase MJ1207; DE EC=2.3.1.-; GN OrderedLocusNames=MJ1207; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the acetyltransferase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 N-acetyltransferase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00532}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99211.1; -; Genomic_DNA. DR PIR; F64450; F64450. DR ProteinModelPortal; Q58604; -. DR STRING; 243232.MJ_1207; -. DR DNASU; 1452104; -. DR EnsemblBacteria; AAB99211; AAB99211; MJ_1207. DR KEGG; mja:MJ_1207; -. DR eggNOG; arCOG00826; Archaea. DR eggNOG; arCOG01354; Archaea. DR eggNOG; COG0454; LUCA. DR InParanoid; Q58604; -. DR OMA; IHEFVVD; -. DR PhylomeDB; Q58604; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0031248; C:protein acetyltransferase complex; IBA:GO_Central. DR GO; GO:0004596; F:peptide alpha-N-acetyltransferase activity; IBA:GO_Central. DR GO; GO:0006474; P:N-terminal protein amino acid acetylation; IBA:GO_Central. DR Gene3D; 3.40.630.30; -; 1. DR InterPro; IPR016181; Acyl_CoA_acyltransferase. DR InterPro; IPR000182; GNAT_dom. DR Pfam; PF00583; Acetyltransf_1; 1. DR SUPFAM; SSF55729; SSF55729; 1. DR PROSITE; PS51186; GNAT; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 226 Uncharacterized N-acetyltransferase FT MJ1207. FT /FTId=PRO_0000074630. FT DOMAIN 75 226 N-acetyltransferase. FT {ECO:0000255|PROSITE-ProRule:PRU00532}. SQ SEQUENCE 226 AA; 26939 MW; 376E718D3509E2DA CRC64; MRVQLILHLE IPKEVCRSLE VDNYINNSIE INLKCEKKPT LYIKTHSIGS LKSILDDFFR CQNAAMEVYN LIKTYTIRNV TKDDLDDFLE LYFKAYRGFD KYYYKKKKWA RWYFKWLMKR DEDGFFVCEV NGKPVGFVAC DCNWISNIEK REVAEIHEIF VDPDFRGRGI GTALINKAIE YAKKRGRRIV ELWVGVENKG AIEFYKRLGF EEKEVVKGWL RMVKRI // ID Y1239_METJA Reviewed; 225 AA. AC Q58636; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ1239; GN OrderedLocusNames=MJ1239; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99244.1; -; Genomic_DNA. DR PIR; F64454; F64454. DR ProteinModelPortal; Q58636; -. DR STRING; 243232.MJ_1239; -. DR EnsemblBacteria; AAB99244; AAB99244; MJ_1239. DR KEGG; mja:MJ_1239; -. DR eggNOG; arCOG05074; Archaea. DR eggNOG; ENOG410XY3D; LUCA. DR OMA; DYHVIDA; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MJ1239. FT /FTId=PRO_0000107232. SQ SEQUENCE 225 AA; 26424 MW; FD0677EE457AB5AF CRC64; MIGIAIKPSK INEDIVDFGH FIGRYFDYYI IDAENEVIKD EEILERLEKI SKVVMTVQAK RVDAFELLEL YASYGFDLCV VLGNKQYLTE KERKFKNYRI LDVIKEAMRC SRDIWVGIEG VESLVKDIVE EHNLIAYYLY GQECSINSKR AIYVPYATKI NENALESMKG YLNRRKNYRG NWRDFILSLN DEESIERIKN NDIVVGYPII PNKEEILNFV RCFSV // ID Y123_METJA Reviewed; 110 AA. AC Q57587; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0123; GN OrderedLocusNames=MJ0123; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1213 and A.aeolicus AA15. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98111.1; -; Genomic_DNA. DR PIR; C64315; C64315. DR PDB; 4JIX; X-ray; 2.00 A; A/B=1-110. DR PDBsum; 4JIX; -. DR STRING; 243232.MJ_0123; -. DR EnsemblBacteria; AAB98111; AAB98111; MJ_0123. DR KEGG; mja:MJ_0123; -. DR eggNOG; arCOG02625; Archaea. DR eggNOG; COG1451; LUCA. DR KO; K07043; -. DR OMA; NECDEIE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002725; DUF45. DR Pfam; PF01863; DUF45; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 110 Uncharacterized protein MJ0123. FT /FTId=PRO_0000106703. FT HELIX 10 20 {ECO:0000244|PDB:4JIX}. FT STRAND 28 32 {ECO:0000244|PDB:4JIX}. FT STRAND 38 42 {ECO:0000244|PDB:4JIX}. FT TURN 43 46 {ECO:0000244|PDB:4JIX}. FT STRAND 47 51 {ECO:0000244|PDB:4JIX}. FT HELIX 52 57 {ECO:0000244|PDB:4JIX}. FT HELIX 60 76 {ECO:0000244|PDB:4JIX}. FT HELIX 83 89 {ECO:0000244|PDB:4JIX}. FT TURN 90 92 {ECO:0000244|PDB:4JIX}. FT HELIX 95 109 {ECO:0000244|PDB:4JIX}. SQ SEQUENCE 110 AA; 13187 MW; B905F6BBFBF207DF CRC64; MKINENKKDI KDIVNEILIS LNINESINIE IKPMKQKIAS FSFKTKTLRL NKYVVENFDE ELLHYIILHE LIHFKIKSIN HGIKFENELR NYFSKNECDE IELKIIQKLI // ID Y1242_METJA Reviewed; 539 AA. AC Q58639; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ1242; GN OrderedLocusNames=MJ1242; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99247.1; -; Genomic_DNA. DR PIR; A64455; A64455. DR ProteinModelPortal; Q58639; -. DR STRING; 243232.MJ_1242; -. DR EnsemblBacteria; AAB99247; AAB99247; MJ_1242. DR KEGG; mja:MJ_1242; -. DR eggNOG; arCOG00185; Archaea. DR eggNOG; COG1123; LUCA. DR InParanoid; Q58639; -. DR KO; K00400; -. DR OMA; EHRIAHI; -. DR PhylomeDB; Q58639; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR017669; Me_Coenz_M_Rdtase_A2. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 2. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR TIGRFAMs; TIGR03269; met_CoM_red_A2; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 539 Uncharacterized ABC transporter ATP- FT binding protein MJ1242. FT /FTId=PRO_0000093224. FT DOMAIN 9 276 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 288 536 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 41 48 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 325 332 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 539 AA; 60707 MW; 26E5A58A897FE952 CRC64; MEGGAMMLLE VKNVTKKFGD KVVLKNISFT LEEGESLGIL GKSGAGKSVL LHMLRGMDGY EPTEGQIIYH VSYCEKCGYV DVPSKAGTPC KKCGNELKKI EVDFWNDKKY TYNLKRKIAI MLQRTFALYG EKTVLENILE ALHQAGYEGK EAIDMALKLI KMVKLEHRIT HIARDLSGGE KQRVVLARQI AKEPFIFLAD EPTGTLDPQT AKLVHSALKE LVIKNKISLI LTSHWPEVIA ELTEKAIWLD KGEIIMEGTS EEVVNKFMET VKEFKKPETE VEIKEDIIKL ENVSKHYCSV ERGVIKAVDN VTLNIREREI FGLVGTSGAG KTTLAKIIAG VLPPSKGKYW FRVGDEWVDM TKPGPMGRGR AKRYIGILFQ EYALYPHRTI LENLTEAIGL ELPDEFARMK AVYTLVSVGF SEEEAEEILD KYPHELSVGE RHRCALAQVL IKEPRVVILD EPTGTMDPIT RNTVAESIHK SRIELEQTYI IVSHDMDFVL NVCDRAGLMR NGKLIKVGKP EEIVALLTEE EKQEMFGQK // ID Y1251_METJA Reviewed; 167 AA. AC Q58649; DT 06-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=UPF0254 protein MJ1251; GN OrderedLocusNames=MJ1251; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0254 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99254.1; -; Genomic_DNA. DR PIR; C64456; C64456. DR PDB; 3WVA; X-ray; 1.40 A; A/B=1-167. DR PDB; 3WVB; X-ray; 1.70 A; A/B=1-167. DR PDB; 3WVC; X-ray; 2.00 A; A/B=1-167. DR PDBsum; 3WVA; -. DR PDBsum; 3WVB; -. DR PDBsum; 3WVC; -. DR STRING; 243232.MJ_1251; -. DR EnsemblBacteria; AAB99254; AAB99254; MJ_1251. DR KEGG; mja:MJ_1251; -. DR eggNOG; arCOG04865; Archaea. DR eggNOG; COG4016; LUCA. DR OMA; ECFTHGK; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00673; UPF0254; 1. DR InterPro; IPR009625; UPF0254. DR Pfam; PF06787; UPF0254; 1. DR PIRSF; PIRSF018786; UPF0254; 1. DR ProDom; PD021915; UPF0254; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 167 UPF0254 protein MJ1251. FT /FTId=PRO_0000147367. FT STRAND 2 9 {ECO:0000244|PDB:3WVA}. FT TURN 10 13 {ECO:0000244|PDB:3WVA}. FT HELIX 14 24 {ECO:0000244|PDB:3WVA}. FT HELIX 32 34 {ECO:0000244|PDB:3WVA}. FT HELIX 37 43 {ECO:0000244|PDB:3WVA}. FT STRAND 46 53 {ECO:0000244|PDB:3WVA}. FT HELIX 57 64 {ECO:0000244|PDB:3WVA}. FT STRAND 72 75 {ECO:0000244|PDB:3WVC}. FT STRAND 76 78 {ECO:0000244|PDB:3WVA}. FT HELIX 83 101 {ECO:0000244|PDB:3WVA}. FT STRAND 104 110 {ECO:0000244|PDB:3WVA}. FT STRAND 112 115 {ECO:0000244|PDB:3WVA}. FT STRAND 117 121 {ECO:0000244|PDB:3WVA}. FT STRAND 126 129 {ECO:0000244|PDB:3WVA}. FT TURN 137 139 {ECO:0000244|PDB:3WVA}. FT HELIX 143 166 {ECO:0000244|PDB:3WVA}. SQ SEQUENCE 167 AA; 18946 MW; B41FFDCFFEA89F86 CRC64; MITVATAECF THANIGLTIH KAAAGYEDFE FKYLFSEEDL KLMKNVRVIS AMFVPSIIGV EKLLDIKLPE PDFNYKYAKA YSEEKDLEVA KLMAEGLKKK LNVNISIGST AGVGRGAICI LTDNNRYLFT SDVYANLITF ENIKERQKNG IEKGIKRFLE ILKKEYF // ID Y1279_METJA Reviewed; 185 AA. AC Q58675; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1279; GN OrderedLocusNames=MJ1279; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99285.1; -; Genomic_DNA. DR PIR; F64459; F64459. DR ProteinModelPortal; Q58675; -. DR STRING; 243232.MJ_1279; -. DR EnsemblBacteria; AAB99285; AAB99285; MJ_1279. DR KEGG; mja:MJ_1279; -. DR eggNOG; arCOG10917; Archaea. DR eggNOG; ENOG41110MD; LUCA. DR OMA; NCATYLL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 185 Uncharacterized protein MJ1279. FT /FTId=PRO_0000107247. SQ SEQUENCE 185 AA; 21379 MW; 8727A0497D57DDC1 CRC64; MVILMDKRFI ELIKKGWKLK NEENKATYID EVFLGAIITT LTDNGYVLMD IASNGNFHYF MFEHLESWDR IKIVAEVLPH SLTDVKVIGA RMFIEFSYGV MIKGIPPSLF GLGLKGYLSQ MLSNIGSIRY EYDGYYTFVN CATYLLINDY IDFDTLTIDW EKLNNDINAI ISSLAKYLEI HKKVE // ID Y1285_METJA Reviewed; 184 AA. AC Q58681; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1285; GN OrderedLocusNames=MJ1285; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99294.1; -; Genomic_DNA. DR PIR; D64460; D64460. DR STRING; 243232.MJ_1285; -. DR EnsemblBacteria; AAB99294; AAB99294; MJ_1285. DR KEGG; mja:MJ_1285; -. DR eggNOG; arCOG08270; Archaea. DR eggNOG; ENOG41111P0; LUCA. DR OMA; KEFLMYY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 184 Uncharacterized protein MJ1285. FT /FTId=PRO_0000107253. FT TRANSMEM 5 27 Helical. {ECO:0000255}. SQ SEQUENCE 184 AA; 21715 MW; 1C1605916DC36DE4 CRC64; MELDYLLATA MFLIVCVYVI SETVNLHSVY DIEEAKKEFL MYYNDLKYNY SISKGDLIFN FKVNKIGYVI EGFVFKDTSE SRELIKYLEN LNGSYIIAYS PSKDEFIITK NHEFLRIIGH YNISAKYKKG EYGDIEIIYP KNYSINYREF QGISCNKLFE VPFYIVDKNE NITLKYYGIL EVGR // ID Y1288_METJA Reviewed; 252 AA. AC Q58684; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ1288; GN OrderedLocusNames=MJ1288; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99290.1; -; Genomic_DNA. DR PIR; G64460; G64460. DR ProteinModelPortal; Q58684; -. DR STRING; 243232.MJ_1288; -. DR EnsemblBacteria; AAB99290; AAB99290; MJ_1288. DR KEGG; mja:MJ_1288; -. DR eggNOG; arCOG01817; Archaea. DR eggNOG; COG0630; LUCA. DR InParanoid; Q58684; -. DR KO; K07332; -. DR PhylomeDB; Q58684; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 252 Uncharacterized protein MJ1288. FT /FTId=PRO_0000207312. SQ SEQUENCE 252 AA; 29481 MW; F5418BCF81D510BC CRC64; MIFMVIKKIF GENFNFNKNI DIKKIFKLDK NVKKDREENE SYLDALKEIY EEIKNLEIYE KMTIGMAEII IGYDNVEKTK KYIVIEPILT KEEIKLFLKL RKVVQALLDV PVEEIDKEKL EDYLKEKIKE IFDDLKLTLD DVTRHKLIYF LIKYLIGYGK IDALMKDENL EDISCTGVGK PVYVFHRKYE HLKTNIKFET DEELDSFCIS LAQRCGKSLT LANPIVDGSL PDGSRLNVTL GRDISDMVQH LQ // ID Y1291_METJA Reviewed; 240 AA. AC Q58687; DT 18-OCT-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ1291; DE Flags: Precursor; GN OrderedLocusNames=MJ1291; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99297.1; -; Genomic_DNA. DR PIR; B64461; B64461. DR ProteinModelPortal; Q58687; -. DR STRING; 243232.MJ_1291; -. DR EnsemblBacteria; AAB99297; AAB99297; MJ_1291. DR KEGG; mja:MJ_1291; -. DR eggNOG; arCOG05987; Archaea. DR eggNOG; ENOG410YSPP; LUCA. DR OMA; WASVNID; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 30 {ECO:0000255}. FT CHAIN 31 240 Uncharacterized protein MJ1291. FT /FTId=PRO_0000014012. SQ SEQUENCE 240 AA; 27112 MW; CB527B46199362DC CRC64; MNKSGMSLII TMLLLIGTAI VIGAAYYAWS NKVFSDTTEK ITPTIKSSIG NIIKPIEIST IETYYFTNLD LNGDSRITNN PEERFIQTIK LEFINNIDED LNVNTRIYCL TPNVSWASVN IDDSSNNLLL DRDENPYNYS GQYVYFNGTV YYSSMKFYDE NGKLFYAAAS NGNALNTSNL LDLIDLNCPT ESFLLKGNSK TDINYYILIN NTKVPNTIIF EIIASTKYGD VEKKITFEIS // ID Y1295_METJA Reviewed; 218 AA. AC Q58691; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1295; GN OrderedLocusNames=MJ1295; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99302.1; -; Genomic_DNA. DR PIR; F64461; F64461. DR ProteinModelPortal; Q58691; -. DR STRING; 243232.MJ_1295; -. DR EnsemblBacteria; AAB99302; AAB99302; MJ_1295. DR KEGG; mja:MJ_1295; -. DR eggNOG; arCOG00304; Archaea. DR eggNOG; COG1387; LUCA. DR InParanoid; Q58691; -. DR OMA; VEITHVP; -. DR PhylomeDB; Q58691; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MJ1295. FT /FTId=PRO_0000107261. SQ SEQUENCE 218 AA; 24666 MW; 92C3E7FB2526D0AD CRC64; MRFDFHTHTV FSDGELIPAE LVRRARVLKH RAIAITDHAD FSNYKELIEK TTIAKEELKK YWDDIIVIVG VELTHIPPKS IPKMAKKAKD LGAEIVVVHG ETVVEPVEEK TNYYASISED VDILAHPGFI DKETAENLKE NDIFVEITSR RGHNITNGYV ANIAREFGLK TLINTDTHAP EDLIDDEFAK KVGLGAGLTN KELENTLLHY PKELLKRI // ID Y1303_METJA Reviewed; 501 AA. AC Q58699; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ1303; GN OrderedLocusNames=MJ1303; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 13 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99312.1; -; Genomic_DNA. DR PIR; F64462; F64462. DR ProteinModelPortal; Q58699; -. DR STRING; 243232.MJ_1303; -. DR EnsemblBacteria; AAB99312; AAB99312; MJ_1303. DR KEGG; mja:MJ_1303; -. DR eggNOG; arCOG02182; Archaea. DR eggNOG; ENOG410Y8PW; LUCA. DR InParanoid; Q58699; -. DR KO; K14120; -. DR OMA; CAIHCPR; -. DR PhylomeDB; Q58699; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR Pfam; PF13237; Fer4_10; 1. DR Pfam; PF12838; Fer4_7; 3. DR Pfam; PF13187; Fer4_9; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 13. DR PROSITE; PS51379; 4FE4S_FER_2; 13. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 501 Uncharacterized polyferredoxin-like FT protein MJ1303. FT /FTId=PRO_0000159153. FT DOMAIN 39 70 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 71 100 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 101 130 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 172 201 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 195 224 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 220 249 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 257 286 4Fe-4S ferredoxin-type 7. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 286 315 4Fe-4S ferredoxin-type 8. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 341 372 4Fe-4S ferredoxin-type 9. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 373 402 4Fe-4S ferredoxin-type 10. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 403 432 4Fe-4S ferredoxin-type 11. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 442 471 4Fe-4S ferredoxin-type 12. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 467 496 4Fe-4S ferredoxin-type 13. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 50 50 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 53 53 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 56 56 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 60 60 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 80 80 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 83 83 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 86 86 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 90 90 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 110 110 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 113 113 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 116 116 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 120 120 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 181 181 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 184 184 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 187 187 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 191 191 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 204 204 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 207 207 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 210 210 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 214 214 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 229 229 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 232 232 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 235 235 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 239 239 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 266 266 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 269 269 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 272 272 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 276 276 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 295 295 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 298 298 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 301 301 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 305 305 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 352 352 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 355 355 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 358 358 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 362 362 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 382 382 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 385 385 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 388 388 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 392 392 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 412 412 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 415 415 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 418 418 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 422 422 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 451 451 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 454 454 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 457 457 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 461 461 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 476 476 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 479 479 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 482 482 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 486 486 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 501 AA; 56297 MW; 46D5A1096224D0EE CRC64; MRGGRMIITI LDECRVEEKC QSCPFSQTSK CMEACPTDAI FLLNNKSFSC LTCGECARNC PNKAIKRNEF GGYYVDRRRC NGCGICANVC PIGIIKIVEK DGKKFPMGIC SMCGVCVEVC PYNARVSSYE LLNTKREGLA ERYLKVLENL MKVKLFRAEE KPGKVVEKVE RKSIKIDRDK CVGCLRCSYL CPRDTIVPDS IDACTSCNLC GENCPKDAIK DGEVDYNKCI LCLKCVEICP NDALKVENFK VIKVKEDKTS QPTSYCINCG LCAEHCPSGA LRFENGHLYY SPDVCWKCME CVKICPNDVR RIKQDFRRLY IHKGNLMPKA SMGNNKLYSC ESPVDDRVVG GCSLCEICIN NCPEEAISIT TVKLEKIKDE NCILCGTCSN VCPRDAIIID RSNGEVLFTD NCIACETCAI HCPRDVIPNT TGYKKVVDRE NSFIRTDMDF CIKCGLCNKV CPNNCIDYGV IDKERCEFCG ACYNICPTKA IYLHRKWKVK E // ID Y1340_METJA Reviewed; 114 AA. AC Q58736; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1340; GN OrderedLocusNames=MJ1340; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0310 and MJ0714. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99350.1; -; Genomic_DNA. DR PIR; C64467; C64467. DR ProteinModelPortal; Q58736; -. DR STRING; 243232.MJ_1340; -. DR EnsemblBacteria; AAB99350; AAB99350; MJ_1340. DR KEGG; mja:MJ_1340; -. DR eggNOG; arCOG02603; Archaea. DR eggNOG; COG2018; LUCA. DR InParanoid; Q58736; -. DR KO; K07131; -. DR OMA; MIRIEMK; -. DR PhylomeDB; Q58736; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJ1340. FT /FTId=PRO_0000107284. SQ SEQUENCE 114 AA; 11886 MW; 55030A1155D57BEE CRC64; MIDRVLLELN KTEGIKGSMV VGKDGLVIAS QLPGSVDAEL VGAMASAAFG AAERTAAEIG MGTLEQTMIE GEHGKTLMVD AGEGILVVLT DAKVNLGLIR ITMKRAAEKI KAMF // ID Y1365_METJA Reviewed; 397 AA. AC Q58760; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1365; GN OrderedLocusNames=MJ1365; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99373.1; -; Genomic_DNA. DR PIR; D64470; D64470. DR ProteinModelPortal; Q58760; -. DR STRING; 243232.MJ_1365; -. DR DNASU; 1452268; -. DR EnsemblBacteria; AAB99373; AAB99373; MJ_1365. DR KEGG; mja:MJ_1365; -. DR eggNOG; arCOG02142; Archaea. DR eggNOG; COG1916; LUCA. DR InParanoid; Q58760; -. DR OMA; WLTSLNP; -. DR PhylomeDB; Q58760; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002816; Pheromone_shutdown_TraB. DR InterPro; IPR005230; Pheromone_shutdown_TraB_bac. DR Pfam; PF01963; TraB; 1. DR TIGRFAMs; TIGR00261; traB; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 397 Uncharacterized protein MJ1365. FT /FTId=PRO_0000107300. FT TRANSMEM 255 275 Helical. {ECO:0000255}. FT TRANSMEM 284 304 Helical. {ECO:0000255}. FT TRANSMEM 308 328 Helical. {ECO:0000255}. FT TRANSMEM 370 390 Helical. {ECO:0000255}. SQ SEQUENCE 397 AA; 44777 MW; 1128105AFD1E8036 CRC64; MVIILRHVRV FNGVNECDIY LIGTAHVSKD SIEEVEKIIS SVSPEGIAVE LDDRRFFSLI TNEEKKVDLK KVLKEGNFLK FFIYLILANS QKKIGESFGI KPGSEMKKAI EIASKYGLPI YLIDRDIDIT LSRLMDRMTF KEKMKIFWEL LNSDEEDLEL DDDLLNDMVK NPEKFIKLLK EISPTIYEVL VDERDRFMAK RLFELSKNKN SLVAVVGAGH VEGIVRYLKK LENGNDIDLM ELIKVKKRKK SLKKLLTYGI SLTIISIFLY MICYALNNPE LLKMITFQWI LFTGGLSALG VLLARGKLIT ALVAFLSAPI TTLVPLPLAA VGTIAGLVEL KYREITDKDL VGIINAESIK ELLNNNLFRV LLVATLSNLG ASIGVFYCLG KFIGFLG // ID Y1371_METJA Reviewed; 244 AA. AC Q58766; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized methyltransferase MJ1371; DE EC=2.1.1.-; GN OrderedLocusNames=MJ1371; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MtxX family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99379.1; -; Genomic_DNA. DR PIR; B64471; B64471. DR ProteinModelPortal; Q58766; -. DR STRING; 243232.MJ_1371; -. DR EnsemblBacteria; AAB99379; AAB99379; MJ_1371. DR KEGG; mja:MJ_1371; -. DR eggNOG; arCOG00854; Archaea. DR eggNOG; COG4002; LUCA. DR InParanoid; Q58766; -. DR OMA; GVDEGWT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR InterPro; IPR016764; MeTrfase_MtxX_xsu. DR PIRSF; PIRSF019709; Methyltransf_MtxX; 1. DR TIGRFAMs; TIGR03270; methan_mark_4; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 244 Uncharacterized methyltransferase MJ1371. FT /FTId=PRO_0000135933. SQ SEQUENCE 244 AA; 27353 MW; 1354A2D00731E2C3 CRC64; MIIMYAIGIG DNKEEVLKAY EKLKEEGIEV ELIDNPKLLV DKLLDGEIDG AVRGSLSSSK VILYLRERIG KFYRASILKN PFTNGIFLLS PVGIDDISED KNERIKDKIR IIEFASNFLK NYNIKAKVAV LSGGRLGDLG RNKVVDETIY EAEEIVEHFK GNVDIIHNGI LIEEYLKDGY NIIIAVDGIT GNLIFRCLGL ICKIPGYGAV ILSDKNVNFI DTSRNANWER YYNAIKFLIG GDFG // ID Y1373_METJA Reviewed; 162 AA. AC Q58768; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1373; GN OrderedLocusNames=MJ1373; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99388.1; -; Genomic_DNA. DR PIR; D64471; D64471. DR ProteinModelPortal; Q58768; -. DR STRING; 243232.MJ_1373; -. DR EnsemblBacteria; AAB99388; AAB99388; MJ_1373. DR KEGG; mja:MJ_1373; -. DR eggNOG; arCOG05081; Archaea. DR eggNOG; ENOG410Z5EJ; LUCA. DR OMA; EMPTAGY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR025748; PrcB_C_dom. DR Pfam; PF14343; PrcB_C; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 162 Uncharacterized protein MJ1373. FT /FTId=PRO_0000107302. FT TRANSMEM 5 25 Helical. {ECO:0000255}. SQ SEQUENCE 162 AA; 18533 MW; 0579724028411CE5 CRC64; MKKKIIILFL FTAILCSITL CGCISFEKTQ IGNYNIKNNS CINSNVSKNQ TIQNVSDKIV NNNTNILNTL NYEIIAYGAF GEKNRGYYYY YKDNKTIIVI NLEEMPTAGY KIKIINITET ANKITVYYKV IPPKEFAAMV VTYPYIKLSV NGTYNVECKE VR // ID Y1375_METJA Reviewed; 415 AA. AC Q58770; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 16-MAR-2016, entry version 95. DE RecName: Full=Uncharacterized membrane protein MJ1375; GN OrderedLocusNames=MJ1375; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the polysaccharide synthase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99382.1; -; Genomic_DNA. DR PIR; F64471; F64471. DR ProteinModelPortal; Q58770; -. DR STRING; 243232.MJ_1375; -. DR EnsemblBacteria; AAB99382; AAB99382; MJ_1375. DR KEGG; mja:MJ_1375; -. DR eggNOG; arCOG02209; Archaea. DR eggNOG; COG2244; LUCA. DR InParanoid; Q58770; -. DR OMA; LTWIVEY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR029303; Polysacc_synt_C. DR InterPro; IPR002797; Polysacc_synth. DR Pfam; PF01943; Polysacc_synt; 1. DR Pfam; PF14667; Polysacc_synt_C; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 415 Uncharacterized membrane protein MJ1375. FT /FTId=PRO_0000166461. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 78 98 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 155 175 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. FT TRANSMEM 300 320 Helical. {ECO:0000255}. FT TRANSMEM 328 348 Helical. {ECO:0000255}. FT TRANSMEM 360 380 Helical. {ECO:0000255}. FT TRANSMEM 388 408 Helical. {ECO:0000255}. SQ SEQUENCE 415 AA; 45989 MW; EC0EC85C65BA7865 CRC64; MSLCKDSIYI LMSNLYSKGM AYLFYFITAF LLGTEAFGIL KGLMPIADTL TIFFSSGIPP AIAKFLAEEK EVDINKYIPI LYLMILLSVV GFILTPYIKY ILGGHYLNLP NILYFAVGLC VVASTVIAFS RGILQGLLKM KYLSLTWIVE YTAKVILVFI LTLYLGIFGS LLSISLAYLV GGIFGLYLIY KALKGKFDFK KLIDIKNTTK NIFSNFNLDI LRYSIPIALT SSSYRLFGDI DNIVIMSIMG GFWSGIYGYS SLISRGIFMF ASAVSIPLLP RISKTKDLSL LKEGIIQNTI FSSIFVIGCL FFPEIPLIAF FKTANPEGIL CLRILAISSL FMSYYTLISS ALQGLGYAKI SFYIILFGLV LNIILNLILV NAYGIVGGSL ATLITSISVF LIGVFAILRI KKHII // ID Y137_METJA Reviewed; 286 AA. AC Q57601; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein MJ0137; GN OrderedLocusNames=MJ0137; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1495. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98120.1; -; Genomic_DNA. DR PIR; A64317; A64317. DR ProteinModelPortal; Q57601; -. DR STRING; 243232.MJ_0137; -. DR DNASU; 1450978; -. DR EnsemblBacteria; AAB98120; AAB98120; MJ_0137. DR KEGG; mja:MJ_0137; -. DR eggNOG; arCOG01911; Archaea. DR eggNOG; COG0616; LUCA. DR InParanoid; Q57601; -. DR OMA; FYLIMAP; -. DR PhylomeDB; Q57601; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002825; Pept_S49_ser-pept_pro. DR Pfam; PF01972; SDH_sah; 1. DR SUPFAM; SSF52096; SSF52096; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 286 Uncharacterized protein MJ0137. FT /FTId=PRO_0000106713. FT TRANSMEM 8 28 Helical. {ECO:0000255}. SQ SEQUENCE 286 AA; 32166 MW; A43DD345B569C55F CRC64; MWGEKMDPLS GFISSLIWWL LFFYLIMAPQ IQYKQLQLAR LKILRELSNK RNSTVITMIH RQESIGLFGI PVYKFITIED SEEILRAIRA APKDKPIDLI IHTPGGLVLA ATQIAKALKA HPAETRVIVP HYAMSGGTLI ALAADKIIMD ENAVLGPVDP QLGQYPAPSI VKAVEQKGAD KADDQTLILA DIAKKAINQV QNFVYNLLKD KYGEEKAKEL SKILTEGRWT HDYPITVEEA KELGLDVDTN VPEEVYTLME LYKQPVRQRG TVEFMPYPVK QENGAK // ID Y1382_METJA Reviewed; 146 AA. AC Q58777; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=UPF0310 protein MJ1382; GN OrderedLocusNames=MJ1382; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0310 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99392.1; -; Genomic_DNA. DR PIR; E64472; E64472. DR ProteinModelPortal; Q58777; -. DR SMR; Q58777; 1-142. DR STRING; 243232.MJ_1382; -. DR EnsemblBacteria; AAB99392; AAB99392; MJ_1382. DR KEGG; mja:MJ_1382; -. DR eggNOG; arCOG02727; Archaea. DR eggNOG; COG1673; LUCA. DR InParanoid; Q58777; -. DR OMA; YFLCITT; -. DR PhylomeDB; Q58777; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.10.590.10; -; 1. DR HAMAP; MF_00771; UPF0310; 1. DR InterPro; IPR002740; EVE_domain. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR022996; UPF0310. DR Pfam; PF01878; EVE; 1. DR SUPFAM; SSF88697; SSF88697; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 146 UPF0310 protein MJ1382. FT /FTId=PRO_0000059635. SQ SEQUENCE 146 AA; 17299 MW; DB51C30DE77A96D2 CRC64; MAYWLCITNE DNWKVIKDKK IWGVAERHKN TINKVKVGDK LIIYEIQRSG KDYKPPYIRG VYEVVSEVYK DSSKIFKPTP RNPNEKFPYR VKLKEVKVFV PPINFKDLIP KLKFITNKKK WSGHLMGKAM REIPEEDYKL IIEAKA // ID Y1396_METJA Reviewed; 2894 AA. AC Q58791; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein MJ1396; GN OrderedLocusNames=MJ1396; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Contains 20 PbH1 repeats. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99406.1; -; Genomic_DNA. DR PIR; C64474; C64474. DR ProteinModelPortal; Q58791; -. DR STRING; 243232.MJ_1396; -. DR EnsemblBacteria; AAB99406; AAB99406; MJ_1396. DR KEGG; mja:MJ_1396; -. DR eggNOG; arCOG07534; Archaea. DR eggNOG; ENOG411285U; LUCA. DR InParanoid; Q58791; -. DR OMA; TWNKDIT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 2.160.20.10; -; 1. DR Gene3D; 2.60.120.200; -; 2. DR Gene3D; 2.60.40.10; -; 1. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR013783; Ig-like_fold. DR InterPro; IPR006626; PbH1. DR InterPro; IPR012334; Pectin_lyas_fold. DR InterPro; IPR011050; Pectin_lyase_fold/virulence. DR SMART; SM00710; PbH1; 20. DR SUPFAM; SSF49899; SSF49899; 2. DR SUPFAM; SSF51126; SSF51126; 2. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix. FT CHAIN 1 2894 Uncharacterized protein MJ1396. FT /FTId=PRO_0000107311. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT REPEAT 543 567 PbH1 1. FT REPEAT 2085 2107 PbH1 2. FT REPEAT 2135 2156 PbH1 3. FT REPEAT 2158 2180 PbH1 4. FT REPEAT 2201 2223 PbH1 5. FT REPEAT 2224 2244 PbH1 6. FT REPEAT 2245 2266 PbH1 7. FT REPEAT 2267 2289 PbH1 8. FT REPEAT 2290 2311 PbH1 9. FT REPEAT 2341 2363 PbH1 10. FT REPEAT 2367 2389 PbH1 11. FT REPEAT 2390 2419 PbH1 12. FT REPEAT 2422 2444 PbH1 13. FT REPEAT 2455 2477 PbH1 14. FT REPEAT 2479 2501 PbH1 15. FT REPEAT 2512 2542 PbH1 16. FT REPEAT 2550 2582 PbH1 17. FT REPEAT 2589 2611 PbH1 18. FT REPEAT 2612 2633 PbH1 19. FT REPEAT 2638 2660 PbH1 20. SQ SEQUENCE 2894 AA; 322363 MW; 8B64F786537A16DF CRC64; MKSYLKNISI FVFTILLLSN VSLGLNVSTT NNNSNFELNN SLIYKLNNSL TNTTNNSGSI IINNTTDTNK EKNECYLNIT INGYRVIVKT NGEVFGFANK TPLKFIKIGD NEYIISPIVL NVPIEIYSKF NDKILHRTVI LNYTKPEKEK KETNIKKEEL HYLNVSFNNF KLIVKTNGKP YAKYLDLNIK VKTKKIKKHE YLVYPLILNK TIIIYAKFKN ETLNRTIFLN YSIEENTTTN KTVILKNVYF PSEKIVIKTN FKPHTAYIVT PNNKIIHLKV HKKGKFYILS TKLKKNVILG NYSVVVDGIK KTFAVDYYKI NAKLIDNRFI VGNVSYYVKE PKFITCIVDK KEINISLING AFEIPLDYLI PKLNISKPEK IKKIILICGN AKEKIKVKFK NKEEIKKLIS YDPVNKEIII KLEGSEKEIK KLLKRYEKRK KYKISKIVKI YNYSIVEIKL KADKEILKDY NLPENILNTT EIVKKISSNK IRVEVNNKVD GVWYRFSCKI PKGYRVKEIV GDDGRVIRNN ISINRLTGEV IGEVRWYIEN NTLYFYDDPI YGYDISLIPP APNHSIAVEL SYNGQDYGGC GQISAIVFPY NKEDDETTVA TYDHAGRTGD YNYANNIDAY AGSKIAIKYT SGALTRQYGV LGTAGSLGWW TYYYLSEINR TDIPLNTVPN GILESVIITD MYAPWNNNEL NITQKVIIRG NNKWFATIYY IKNPTTKTYT NLKFFQGMDW NFRGSWWGDD AYYNSIDDVV YGYDSNAPVG DIQYGGFKSN IPSYEHDVNL YWSTWSDIRY DNLNNDSSYE GDAGTALAWT KDSLKPGEIW VVPIIWGLGY NYTDMMNEIN MGLSQLYDTG VKSIDYPNNG DSFNPNIGPI IYINSTIALY GLVDAYNLNV SINITQINGT YIYTNSTLIN LSVPYEEEKL VSFPVNISNM PYGAYNITIK TNLPNDQNTS NDEKSIIIYI TSFSVQPNYQ EKTGNVGEEI FYNITLYNFG VGGRFDINIT YLTKGWTTKI YNNSILIAED ANGDGIWDYI NPNYDLNSNN LPDIYVPTGE INLTVSKTIP STAPLGEIDT TTLKFVNINN PSIFGKTTFQ TSTPYPPSVQ KTFYLHGDTL RTLNTSIPTT INNYTTINSN SLASWIQYPR FADNFTVVGK IPILLYINDP NVIFGTEMHK IVVSLMATNG IDSFTLGSDV EYLYLDDTIK SYIFNITLDS IITIPKNYYL VLRVENQISS NSINIYHNST YPSNITLNTT TYVNVYNIFS DKNVYLPNEN VTIFANITDP IGSYDISGAN ITVYYPNGSV YINSSMLLQE IDKNSPSLWK LYNYSFSLPE SGKYLITITG IESNGVISKK NYTIYCGYEI QGYVKEDFGT LGKEDSEDKG IYGVNVSLLE DSNNDGIPDI GDTIVNSTTT DIFGHYSFLV YNSSKTYFVV VNSRTVGTTR GLNPQYSKND IWAEETYQTV YTPINSSQWI ANGNASIFPD KLLLTTDDYG EAGSVWYYKP VNLSEDLVVE FYAYLGDNPD GADGITFTLQ SLGTNELGGT GGDLGYGGIS PSVAVEVDTW LNDFDAPATT DHIAIDVNGN INHTYNSLTY PTPNPYDLGN VEDGREHLIK IVWNATTKTL QVYFDGNLSL TWNKDITQII GNSAYFGFTG GTGGAKNLQY VKPIYVKNGD GYIINPTYGV VEMFGGRDPN EEDNWEDGKY EHYCLINLNS YSGKNITFGF SFDVITNTKS TGQGSFSQFI KNANAIYGKD ESYFRIPNID AKNGNHYIYT SGNKILDNLT IVNGSTQING TIILSGLQWI ANGNAYINNS NNLTLILTPD DYNQKGSVWY YKPVNLSEDL VVEFYAYLGD NPDGADGITF TLQSLGTNEL GGTGGDLGYG GISPSVAVEV DTWLNDFDSP ATTDHIAIDV DGNLNHTYNS LTYSTPNPYD LGNVEDGREH LIKIVWNATT KTLQVYFDGN LALTWNKDIT QIIGNSTYFG FTGGTGGAKN LQYVKPTYVK NGDNVLNLEE ISPNPIIDNV GADTYIGNIF FENVSVGILG NETGLNNLTL KSCGIYGKIL NAGVKLVDYD WSLQNYPLYI DNLTINASGG YGISMLNKIW AMLYNSQISL KNGVGIYWAN WAGGFGNITI YNITISSCNQ GLVLYKDGNG IKLINSQIKN SVYEGVYSKN STLEILNSSI INNSIGIYAN ISSILVNNSL IYKNRYEGLL LENSSSSILN SNIMNNSIGI YLKENYISKI QKSNISYNAY GIEIVNSSNV YINSSNIFNA STDGIAIFNG ENVSVENSLL YNNNYSILSY GNLSNLSVLN SLLRDSINNS IDIEVPSDGF LNNLKLYNSS VLNSGSYGLF IYSLGSASNV NISKSLINGS YKDGIYIYGV NAINIVNNNI TNNGLIGGDP AGSGIKISGN YTKGVLILNN NISHNLGNGI SLEGLWSRTL CDVKVENNII SNNGIEENSG NGIYIGGRVE NVSIFNNTIQ YSDAQAILIQ EANGWNSWDW IGTNISIINN TIQYNGLTVT IGNITAGITV GAYGVYNQDN GYIIIEGNKI INNNLCPNPT YGGKVGGIEV YGLNESWISL EFNISKNIIA NNSAYGILIG ASKDINIINN TIFNNEKGIT IPNWDFVPYN IIISKNSIYN NSLLGIDLDD DNVTLNDGLL NYNEANHGID YPIITYAELN GDNLTVKGYI GNGTGSSNFA NAVVEIYLVK NLSGGDNLIG NNISSDGTVL NDTYGESWIY LGSLIADSNG FFSGTINVSG KGVGDESLLT ATATIKGIGT SEFGRNYLLI KKFFNITGTI VMLPNGYNIT IKSYNTTRDV YVYWYKPDNI EVINISGDYD ENGTYGNTYW FKFNVINANE TMNISITTNI TTVEGLIIGI DPKK // ID Y1399_METJA Reviewed; 197 AA. AC Q58794; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=UPF0200 protein MJ1399 {ECO:0000255|HAMAP-Rule:MF_01111}; GN OrderedLocusNames=MJ1399; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0200 family. {ECO:0000255|HAMAP- CC Rule:MF_01111}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99408.1; -; Genomic_DNA. DR PIR; F64474; F64474. DR ProteinModelPortal; Q58794; -. DR STRING; 243232.MJ_1399; -. DR EnsemblBacteria; AAB99408; AAB99408; MJ_1399. DR KEGG; mja:MJ_1399; -. DR eggNOG; arCOG01045; Archaea. DR eggNOG; COG0237; LUCA. DR InParanoid; Q58794; -. DR OMA; IALADYM; -. DR PhylomeDB; Q58794; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0004140; F:dephospho-CoA kinase activity; IBA:GO_Central. DR GO; GO:0015937; P:coenzyme A biosynthetic process; IBA:GO_Central. DR GO; GO:0016310; P:phosphorylation; IBA:GOC. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01111; UPF0200; 1. DR InterPro; IPR022970; NTP_hydrolase-rel. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 197 UPF0200 protein MJ1399. FT /FTId=PRO_0000094525. FT NP_BIND 8 15 ATP. {ECO:0000255|HAMAP-Rule:MF_01111}. SQ SEQUENCE 197 AA; 22630 MW; A440F8259920F873 CRC64; MLLIGITGMP GAGKSSAYEI AKKYNLPIVS MGDVVRYETK KRGLELTPEN VGNTAIKLRE EFGNEAIAVA CLKYIEENLK DKEIVIVEGI RSLYEVNYFR KHKPLVLIAI HSSPLTRFER LKKRGREDDS ANWEVFVERD LRELGFSIGH AIALADFVVV NEKSFEDCLN QLDNILQEIL NNLEKYKKYN FIYETLR // ID Y1401_METJA Reviewed; 808 AA. AC Q58796; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Probable ATP-dependent helicase MJ1401; DE EC=3.6.4.-; GN OrderedLocusNames=MJ1401; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the DEAD box helicase family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99409.1; -; Genomic_DNA. DR PIR; H64474; H64474. DR ProteinModelPortal; Q58796; -. DR STRING; 243232.MJ_1401; -. DR EnsemblBacteria; AAB99409; AAB99409; MJ_1401. DR KEGG; mja:MJ_1401; -. DR eggNOG; arCOG00554; Archaea. DR eggNOG; COG1202; LUCA. DR InParanoid; Q58796; -. DR KO; K03725; -. DR OMA; VAIRVGM; -. DR PhylomeDB; Q58796; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011545; DEAD/DEAH_box_helicase_dom. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR014014; RNA_helicase_DEAD_Q_motif. DR Pfam; PF00270; DEAD; 1. DR Pfam; PF00271; Helicase_C; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00490; HELICc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. DR PROSITE; PS51195; Q_MOTIF; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 808 Probable ATP-dependent helicase MJ1401. FT /FTId=PRO_0000102014. FT DOMAIN 221 391 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 396 585 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 234 241 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 189 217 Q motif. FT MOTIF 336 339 DEIH box. SQ SEQUENCE 808 AA; 92933 MW; C4F0DD8299BC0F0C CRC64; MLIVRKPKKK KDEIEIVKVG GKIEDGIEVK NNQKIFANYK KVGDKYKLYR CRVGDKLIQP SKVLELLKSD KIFILKENEE EIEEVLKSYN LKFDYIELCP FCLLKNIYKR LTRNNRCRYG NLEICINCGI NEIKEEVKIS EEFIEKFLKR FKDVDKVLSL LRIRNPLDKP ELTRYDIITG SEEDKIENYK IDELDIPEEL KEIIKSRGIE ELLPVQTLSV KAGLLNGDDL LIISATSSGK TLIGELAGIK NLIKTGKKFL FLVPLVALAN QKYLEFKERY EKLGFKVSLR VGLGRIGKKV DVETSLDADI IVGTYEGIDY LIRTKRLKDI GTVVIDEIHS LNLEERGARL DGLIGRLRFL FKEAQKIYLS ATIGNPKELA KQLNAKLVLY NGRPVPLERH IIFCKNDFAK LNIIKEIVKR EWQNISKFGY RGQCLIFTYS RKRAEYLAKA LKSKGIKAEF YHGGMEYIKR RKVEDDFANQ KIQCVVTTAA LSAGVDFPAS TVILESLAMG ADWLNPAEFQ QMCGRAGRKG MHEIGKVYLL VEIGKKYHAK MENTEDEVAF KLLNAVPEDV KVEYNEDEEE EQILATISAG ITNRYDIDRV PYIGRAFSLN KILSNLESYG MIKANNDVKL TNYGSAVAIS FLYPKVAEKI KEGIIENKEI IKLITEIMPF ENVYLSNNLK IKLSKILNIN VPSRFFDALE VIREGMEKIK DKKLKEDLTL IIMEFEGVEV EEKILEMIIN LRISGKTPGQ ISKTLYEEFK IQTYSGDIYY YLEQLLNLLD ATERIARIFN KRYAEKVKEL KEKIENPK // ID Y1428_METJA Reviewed; 567 AA. AC Q58823; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=TPR repeat-containing protein MJ1428; GN OrderedLocusNames=MJ1428; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 13 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99438.1; -; Genomic_DNA. DR PIR; C64478; C64478. DR ProteinModelPortal; Q58823; -. DR STRING; 243232.MJ_1428; -. DR PRIDE; Q58823; -. DR EnsemblBacteria; AAB99438; AAB99438; MJ_1428. DR KEGG; mja:MJ_1428; -. DR eggNOG; arCOG03038; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q58823; -. DR OMA; GNSFRMQ; -. DR PhylomeDB; Q58823; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 6. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR013105; TPR_2. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00515; TPR_1; 1. DR Pfam; PF13414; TPR_11; 1. DR Pfam; PF07719; TPR_2; 1. DR Pfam; PF13174; TPR_6; 1. DR Pfam; PF13181; TPR_8; 2. DR SMART; SM00028; TPR; 10. DR SUPFAM; SSF48452; SSF48452; 2. DR PROSITE; PS50005; TPR; 9. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 567 TPR repeat-containing protein MJ1428. FT /FTId=PRO_0000106461. FT REPEAT 14 47 TPR 1. FT REPEAT 48 81 TPR 2. FT REPEAT 83 115 TPR 3. FT REPEAT 116 148 TPR 4. FT REPEAT 150 183 TPR 5. FT REPEAT 199 234 TPR 6. FT REPEAT 236 268 TPR 7. FT REPEAT 269 301 TPR 8. FT REPEAT 303 335 TPR 9. FT REPEAT 344 379 TPR 10. FT REPEAT 380 412 TPR 11. FT REPEAT 414 446 TPR 12. FT REPEAT 505 538 TPR 13. SQ SEQUENCE 567 AA; 66239 MW; 7CE4AC7210B7927E CRC64; MNLFRKISEK LKSYEDWVTE ANYYLDEGIY DKAVECYLKA LEKKNTNPID WFNLAYALYH LEKYDSALEA INEALKISPS NIYFAYLKGL IHYKRGEIIL AYKYLKKASE KIKNEELFEI LGDISVKYGR YEEALKYYLK SYKMANSKNL NALFKAGKIY LLFGDIDKAY DAFNEILQQN PSHECKKIVE CMENVVNAIN SYEDLNNGLT MIKNKDYIGA LKIFNKVLQI DENSDISYYY KSVIAEIFEE YKKALEYIDK SISIFNRSLY YAKKGDILYK LGDEEGAIEA YNKAIKLNSQ NPYAYFGLAI LYYRKGELEK SSNFFDKVLE TYLEELSEED ISALNLYSLI GKAETTGIPK YYHEAMKYVD NLINLENSSR WWYVKGYIYY KLGNYKDAYE SFMNALRVNP KDISTLKSLA IVLEKSGKID EAITTYTKIL KIVNSLQFTC EIDNILEKLR SRKPTNLEIP SVLFDIPVMY HKPNITCFYA SNLWKYMANN NPIGAYIYLS FIESYISLDE ISQMVNDIKS KLSLEMYRYC ELIDDYKSDE SVLMQIKELL QKLGCML // ID Y1441_METJA Reviewed; 1226 AA. AC Q58836; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1441; GN OrderedLocusNames=MJ1441; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99452.1; -; Genomic_DNA. DR PIR; H64479; H64479. DR STRING; 243232.MJ_1441; -. DR EnsemblBacteria; AAB99452; AAB99452; MJ_1441. DR KEGG; mja:MJ_1441; -. DR eggNOG; arCOG03022; Archaea. DR eggNOG; COG1429; LUCA. DR InParanoid; Q58836; -. DR KO; K02230; -. DR OMA; GGSIDII; -. DR PhylomeDB; Q58836; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR InterPro; IPR003672; CobN/Mg_chltase. DR Pfam; PF02514; CobN-Mg_chel; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 1226 Uncharacterized protein MJ1441. FT /FTId=PRO_0000219888. SQ SEQUENCE 1226 AA; 141328 MW; 8F7DDF4E36162AB9 CRC64; MKITFYMWAS YCSILKKALD ELKKEGVDVE YKIYSNRNPI DDEFLEDAKD YDLVFIYRTS SDDIDLEKIK KFNENVIVVA QDPNFWNSEK SAKCYLFITY GGLDNFKNMV LYLMGKDKDV VKHPFQGIYY RGKIYEELEE FLKDVEFNKK YTVGILFSRH YLVNDDMDVI EKLLNRLDKE FNVIPVFSYG AKCEDLNALG SGESVLKYFL KDDKPIIDAL INLLSFPLGT VKDKANLNKI SGVEILKKLD VPVFHPIMSY YKSYEDWKKD EQGLSADIGW TIALPEFEGV IEPIIIGTTE NENGLEKKFG IEERIDKVVR RIKRWIELKY KPKKDRKVIF ILHNNACASV EATVGSAAHL DSFQSVINIM KKLKEEGYYV ENIPENGEEL AQLIMQKKAI SEFRWTTVNE IIAKGGYLYL MDEEEYYEYF NTLPENVKNK ILETWGDLNG KDIPAGMIYK VNGKNKIVIT GLKFGNVYVC VQPKRGCAGA RCDGRVCKIL HDPYCPPTHQ YIASYKYFND IADIIIHVGT HGTLEFLPGK NVGLSNECYP DICIGDIPHL YIYNSDNPPE GTIAKRRSYA TIIDHMQTVM VDAFYEELET LDSYIEEYLK EMDASRRHQL EHLIVEEVKK TNLLKIKEKI EKIEKEGKIH ENFKEIFDEL RDILEMIKNS KCNDGMHIFG ELPSGEKRVE FIKSILEAIF IQNNTMNSKR RGIAERSEAM HPGYPNRGLP PMEFEYKDKN LKKKVSDVLN GKSIEDKKLE EKIKDINERI EKSDEIGSLL RGIDAKYIEP GPSGLITRGN YDILPTGRNF YSLDPYRIPT KSAYRVGVLL AEKLINRYLE EEGRYPENIA LYWMASDIMW ADGEGMGMIL YLLGVKPVYR GGRVVGLEVI PLEELGRPRI DVTIRVSGIT RDMFPNCIEL VDEAIMKVAN LDEPLEMNFV KKHVVENLNK GLSFRESTFR IFCSPPGTYG NGVKYAVYAS AWENDEDLKD AFIYWNSYAY GKDVYGKKAI NAFENILKTV DLTFNKVVTD EYDLFGCCCY FGTHGGLTNA ARVLKGEEVK AYYGDTRNPN NVEVRTLKEE IERVSLTKLL NPKWIEGMKR HGYKGAGDIA KRIGRVYGWS ATTKEVENWI FDEIFNTFVK NEENRKFFKE HNIYALEEIA RRLLEAYQRG LWKTTEGNIE ELKRAYLEIE GDIEETYSSI ADIGEFQGGS VDIDMIWKEK LMSNGR // ID Y1453_METJA Reviewed; 192 AA. AC Q58848; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1453; GN OrderedLocusNames=MJ1453; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH863. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99468.1; -; Genomic_DNA. DR PIR; D64481; D64481. DR ProteinModelPortal; Q58848; -. DR STRING; 243232.MJ_1453; -. DR EnsemblBacteria; AAB99468; AAB99468; MJ_1453. DR KEGG; mja:MJ_1453; -. DR eggNOG; arCOG04458; Archaea. DR eggNOG; COG2457; LUCA. DR InParanoid; Q58848; -. DR KO; K09154; -. DR OMA; CSPYLIA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR007386; DUF447. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR InterPro; IPR016733; UCP018747. DR Pfam; PF04289; DUF447; 1. DR PIRSF; PIRSF018747; UCP018747; 1. DR SUPFAM; SSF50475; SSF50475; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 192 Uncharacterized protein MJ1453. FT /FTId=PRO_0000107342. SQ SEQUENCE 192 AA; 22651 MW; 7026CC8CE6A24643 CRC64; MISEVVVTTR KNNRDNKAPI GVYFKDKKVI MHLFSGSHTY ENLLTEDYFS VNVVPPIEIA KAVLDDEDDY LYYNDIPYLK SSYYAIFYKV IERKFVDRED KFGKNRLMIL EGEEIKRIYL NNIPKPYNRA DGLLVEIAVI YSRLANKNIK INEDDKKEMI NDIRKYFSII KKVGGREHKQ LAEIMLRNLN LL // ID Y1466_METJA Reviewed; 214 AA. AC Q58861; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 77. DE RecName: Full=Uncharacterized protein MJ1466; GN OrderedLocusNames=MJ1466; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0017 and MJ0139.1. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99474.1; -; Genomic_DNA. DR PIR; A64483; A64483. DR STRING; 243232.MJ_1466; -. DR EnsemblBacteria; AAB99474; AAB99474; MJ_1466. DR KEGG; mja:MJ_1466; -. DR eggNOG; arCOG02134; Archaea. DR eggNOG; COG3316; LUCA. DR InParanoid; Q58861; -. DR OMA; INILHDG; -. DR PhylomeDB; Q58861; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 1. DR InterPro; IPR032874; DDE_dom. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13610; DDE_Tnp_IS240; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 214 Uncharacterized protein MJ1466. FT /FTId=PRO_0000107352. SQ SEQUENCE 214 AA; 25626 MW; 3C6D5A76051F17EB CRC64; MRLTIEVIKE RIVERKLFKR NRKSIEVKIL AGLLYYLGLS LRKVSLFLSQ FEDISHESVR IYYHKIKEVL NEPERKERNL IAIDETKLKV GDKYIYAWSA IDVETKECLG VYISKTRNYL DTILFVKSIL KFCSNKPKIL VDGGKWYPWA LRKLGLEFER VKFGLRNCVE SFFSVLKRRT KVFYNRFPNN SKFDTVISWI KSFMMFYNWM KSLT // ID Y1475_METJA Reviewed; 125 AA. AC Q58870; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1475; GN OrderedLocusNames=MJ1475; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99488.1; -; Genomic_DNA. DR PIR; B64484; B64484. DR ProteinModelPortal; Q58870; -. DR STRING; 243232.MJ_1475; -. DR EnsemblBacteria; AAB99488; AAB99488; MJ_1475. DR KEGG; mja:MJ_1475; -. DR eggNOG; arCOG03351; Archaea. DR eggNOG; COG1710; LUCA. DR InParanoid; Q58870; -. DR OMA; EYHYYKL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 125 Uncharacterized protein MJ1475. FT /FTId=PRO_0000107358. SQ SEQUENCE 125 AA; 14634 MW; AFB8CC9AFA1718DE CRC64; MKKLIAKTKE ELIEKIKECE NEEEIYINLE LDRDVAIALL ESCEPKKIYL PKSKYKRSSK KIIKALEGVD VEVIPIKAKT GRPTNVDKII KKYLDKKPKE IAEITGINIK TVEYHYYKLK KKEKQ // ID Y1476_METJA Reviewed; 230 AA. AC Q58871; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 77. DE RecName: Full=Uncharacterized tRNA/rRNA methyltransferase MJ1476; DE EC=2.1.1.-; GN OrderedLocusNames=MJ1476; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the class IV-like SAM-binding CC methyltransferase superfamily. RNA methyltransferase TrmH family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99481.1; -; Genomic_DNA. DR PIR; C64484; C64484. DR ProteinModelPortal; Q58871; -. DR STRING; 243232.MJ_1476; -. DR EnsemblBacteria; AAB99481; AAB99481; MJ_1476. DR KEGG; mja:MJ_1476; -. DR eggNOG; arCOG01018; Archaea. DR eggNOG; COG0565; LUCA. DR InParanoid; Q58871; -. DR OMA; IPEHKKE; -. DR PhylomeDB; Q58871; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0003723; F:RNA binding; IBA:GO_Central. DR GO; GO:0052666; F:tRNA (cytosine-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0052665; F:tRNA (uracil-2'-O-)-methyltransferase activity; IBA:GO_Central. DR GO; GO:0002128; P:tRNA nucleoside ribose methylation; IBA:GO_Central. DR Gene3D; 3.40.1280.10; -; 1. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR004384; rRNA_MeTrfase_TrmH_1. DR InterPro; IPR001537; SpoU_MeTrfase. DR InterPro; IPR029026; tRNA_m1G_MTases_N. DR Pfam; PF00588; SpoU_methylase; 1. DR PIRSF; PIRSF004808; LasT; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR TIGRFAMs; TIGR00050; rRNA_methyl_1; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; Transferase. FT CHAIN 1 230 Uncharacterized tRNA/rRNA FT methyltransferase MJ1476. FT /FTId=PRO_0000159843. SQ SEQUENCE 230 AA; 26280 MW; E9B6B9B31B3A146E CRC64; MIIMISVILV NPKYSGNVGS IARVMMNFGF EELRIVGDKS IINNEAYMMA VHAREILDNA KFYNTFDEAI GDLDFVIATS GARGGDRNLK RVPITPKELA DKILEVKGNI GIVFGREDDG LRNEEIDKCD LLVSIPTSEK YPIMNLSHAV AVILYEIYTK KVRNKFLDIN MREASKEDKE LLIRKFNEFI DKNEKIPEHK KELCKIIFKR LVNRAFISGK EAWTLMSAFK // ID Y1481_METJA Reviewed; 213 AA. AC Q58876; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1481; GN OrderedLocusNames=MJ1481; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99493.1; -; Genomic_DNA. DR PIR; H64484; H64484. DR PDB; 3WKR; X-ray; 2.80 A; C/D/G/H=1-213. DR PDB; 3WKS; X-ray; 3.03 A; C/D=1-103. DR PDBsum; 3WKR; -. DR PDBsum; 3WKS; -. DR ProteinModelPortal; Q58876; -. DR STRING; 243232.MJ_1481; -. DR EnsemblBacteria; AAB99493; AAB99493; MJ_1481. DR KEGG; mja:MJ_1481; -. DR eggNOG; arCOG04872; Archaea. DR eggNOG; COG4024; LUCA. DR OMA; GIEKKCK; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR016736; UCP018814. DR Pfam; PF09873; DUF2100; 1. DR PIRSF; PIRSF018814; UCP018814; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 213 Uncharacterized protein MJ1481. FT /FTId=PRO_0000107367. FT HELIX 36 38 {ECO:0000244|PDB:3WKR}. FT HELIX 46 58 {ECO:0000244|PDB:3WKR}. FT HELIX 61 65 {ECO:0000244|PDB:3WKR}. FT TURN 66 69 {ECO:0000244|PDB:3WKR}. FT HELIX 74 95 {ECO:0000244|PDB:3WKR}. FT HELIX 96 98 {ECO:0000244|PDB:3WKR}. SQ SEQUENCE 213 AA; 24903 MW; E51EDB3F72ECF733 CRC64; MRVEYSKDLI RKGISTISQL KKAKIRVEKD DKKISYKDAK PGKIDVNEFK KAIYLLIEAD DFLYKKAPKH ELNEEEAKEF CKLIIKCQEH LNKILANFGF EFEEKEIDEG ALYIVSNKKL FKKLKNKNPN LKVVCTEGML DIEDMRAIGV PEKALEGLKK KVEIARKNVE RFIEKYKPEK IFVVVEDDKD ELLYLRAKNL YNAEKLDADE ILD // ID Y1492_METJA Reviewed; 156 AA. AC Q58887; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1492; GN OrderedLocusNames=MJ1492; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99504.1; -; Genomic_DNA. DR PIR; C64486; C64486. DR ProteinModelPortal; Q58887; -. DR STRING; 243232.MJ_1492; -. DR EnsemblBacteria; AAB99504; AAB99504; MJ_1492. DR KEGG; mja:MJ_1492; -. DR eggNOG; arCOG03949; Archaea. DR eggNOG; COG3815; LUCA. DR OMA; GHKMAVC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019206; DUF2085_TM. DR Pfam; PF09858; DUF2085; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 156 Uncharacterized protein MJ1492. FT /FTId=PRO_0000107375. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 34 54 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. SQ SEQUENCE 156 AA; 18363 MW; CBDDBFC6F75A9CF2 CRC64; MKKYYLIVLI SFLIFYLSIF LAPYFAYLGE TSNFWKFISI CLYAVYSLIC HQMPQRSFFI FGHKMAVCAR CFGIYTGVLV GMIIYPFIKK LDDFKIPNKW YLIIALIPMA VDGTTQLIGL RESFNELRFI TGFIAGFTVV FYILPIFFEM IYKKFK // ID Y1496_METJA Reviewed; 114 AA. AC Q58891; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0127 protein MJ1496; GN OrderedLocusNames=MJ1496; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0127 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB99507.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99507.1; ALT_INIT; Genomic_DNA. DR PIR; G64486; G64486. DR STRING; 243232.MJ_1496; -. DR EnsemblBacteria; AAB99507; AAB99507; MJ_1496. DR KEGG; mja:MJ_1496; -. DR eggNOG; arCOG03113; Archaea. DR eggNOG; COG1430; LUCA. DR InParanoid; Q58891; -. DR KO; K09005; -. DR OMA; YPIDVIF; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00263; UPF0127; 1. DR InterPro; IPR003795; DUF192. DR InterPro; IPR022906; UPF0127. DR Pfam; PF02643; DUF192; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 114 UPF0127 protein MJ1496. FT /FTId=PRO_0000150050. SQ SEQUENCE 114 AA; 13605 MW; 59FFDE4D35F0BE01 CRC64; MQNKKIKKVK VGNLEFEVVL ADNFIKRAFG LMLRDIGDKA MLFLYKRRKI AMHTFFMLYP IDIIFIDKNR VVEAVRLKPW KTYKCKNYST AMLEFKCSDI DLNEIIGEKV EFMR // ID Y1499_METJA Reviewed; 160 AA. AC Q58894; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1499; GN OrderedLocusNames=MJ1499; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99512.1; -; Genomic_DNA. DR PIR; B64487; B64487. DR STRING; 243232.MJ_1499; -. DR REBASE; 3907; C.MjaVP. DR EnsemblBacteria; AAB99512; AAB99512; MJ_1499. DR KEGG; mja:MJ_1499; -. DR eggNOG; arCOG09627; Archaea. DR eggNOG; ENOG41111II; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 160 Uncharacterized protein MJ1499. FT /FTId=PRO_0000107379. SQ SEQUENCE 160 AA; 17963 MW; 70E0B08F3E8E8C3C CRC64; MSKSGNKNQN CPKCNNSPWI QRANNFIAQN QNVQTGTKEY YQVEAVKYLL NNGHCGIDCR AKISDIIKGI NYPKNREAFQ HEVLIPLKQY GIIATLVYPG RKGGVFIPCN NDEIKKVAKQ VFKRIESELE NLEGSATGVQ NIKNLANSLK TTVHNLKNTI // ID Y1551_METJA Reviewed; 57 AA. AC Q58946; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1551; GN OrderedLocusNames=MJ1551; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99571.1; -; Genomic_DNA. DR PIR; F64493; F64493. DR STRING; 243232.MJ_1551; -. DR EnsemblBacteria; AAB99571; AAB99571; MJ_1551. DR KEGG; mja:MJ_1551; -. DR eggNOG; arCOG04856; Archaea. DR eggNOG; COG1532; LUCA. DR KO; K06964; -. DR OMA; LVMEDVM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019300; RNA-binding_protein_predicted. DR Pfam; PF10133; RNA_bind_2; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Uncharacterized protein MJ1551. FT /FTId=PRO_0000107405. SQ SEQUENCE 57 AA; 6515 MW; 0B6F2B918406A96C CRC64; MCSCNLYFNG ELVMEDVMIV EKKGDKVIAI DLFGDKKEFV GEIKKIDLNE NKIFIEG // ID Y1572_METJA Reviewed; 278 AA. AC Q58967; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 105. DE RecName: Full=Putative ABC transporter ATP-binding protein MJ1572; DE EC=3.6.3.-; GN OrderedLocusNames=MJ1572; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably part of an ABC transporter complex. Responsible CC for energy coupling to the transport system (By similarity). CC {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral CC membrane protein {ECO:0000250}. CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99589.1; -; Genomic_DNA. DR PIR; C64496; C64496. DR ProteinModelPortal; Q58967; -. DR STRING; 243232.MJ_1572; -. DR EnsemblBacteria; AAB99589; AAB99589; MJ_1572. DR KEGG; mja:MJ_1572; -. DR eggNOG; arCOG00202; Archaea. DR eggNOG; COG1122; LUCA. DR InParanoid; Q58967; -. DR KO; K02006; -. DR OMA; VMISHNM; -. DR PhylomeDB; Q58967; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell membrane; Complete proteome; Hydrolase; Membrane; KW Nucleotide-binding; Reference proteome; Transport. FT CHAIN 1 278 Putative ABC transporter ATP-binding FT protein MJ1572. FT /FTId=PRO_0000092142. FT DOMAIN 5 242 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 278 AA; 31726 MW; E87C62B70AB114D2 CRC64; MKEIYRLVDV SYKYPNGSIA LDNVNLNIYK NEVVAILGPN GAGKTTLLKI LDGLVFPDKG EVYFEGKKLT DEILRDKELM KEFRRKVGFV FQNPDVMLFN PTVWDEVAFS PLHLYSKEKA IEVTDKTLKD MKIYHLKDRH PYNLSGGEKK KVSISCILSV EPEVILMDEP TSALDPKSRA EIMNLIKSFK ECGKTVVLVT HDLNLACLAD RCYVLNKKVI FEGKVKDLFS LNLDELNLDV PEISKLFIKL KNMGYNINEI PVTLDEAVNI ISKLFQKY // ID Y157_METJA Reviewed; 96 AA. AC Q57621; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0157; GN OrderedLocusNames=MJ0157; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98150.1; -; Genomic_DNA. DR PIR; F64319; F64319. DR EnsemblBacteria; AAB98150; AAB98150; MJ_0157. DR KEGG; mja:MJ_0157; -. DR eggNOG; arCOG04846; Archaea. DR eggNOG; COG4014; LUCA. DR InParanoid; Q57621; -. DR OMA; DNNLMYR; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019209; DUF2098. DR InterPro; IPR017099; UCP037053. DR Pfam; PF09871; DUF2098; 1. DR PIRSF; PIRSF037053; UCP037053; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 96 Uncharacterized protein MJ0157. FT /FTId=PRO_0000106721. FT COMPBIAS 15 40 Val-rich. FT COMPBIAS 57 83 Glu/Lys-rich. SQ SEQUENCE 96 AA; 10954 MW; C81160A577AB5272 CRC64; MGYMDEVNIK VGDYVVYINT GTKGRVVDIR KDENGDIWVV LDNNLMYRPH LLRVIDKSKI TERKEDIDEV VKKLEKEELE EGKLIDLDLG DACGAG // ID Y1580_METJA Reviewed; 124 AA. AC Q58975; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1580; GN OrderedLocusNames=MJ1580; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.thermoautotrophicum MTH137. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99600.1; -; Genomic_DNA. DR PIR; C64497; C64497. DR STRING; 243232.MJ_1580; -. DR EnsemblBacteria; AAB99600; AAB99600; MJ_1580. DR KEGG; mja:MJ_1580; -. DR eggNOG; arCOG05092; Archaea. DR eggNOG; COG2456; LUCA. DR InParanoid; Q58975; -. DR KO; K09153; -. DR OMA; EIAINER; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019277; DUF2304. DR Pfam; PF10066; DUF2304; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 124 Uncharacterized protein MJ1580. FT /FTId=PRO_0000107425. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 71 91 Helical. {ECO:0000255}. SQ SEQUENCE 124 AA; 14644 MW; B9F5B537435BCB62 CRC64; MLIKILEEKL MELIQIVGVI FALFALSRVV LQLKRRSISF NEGLFWIFVW GFVVIFLVFP EFFGYVAEVL GVGRGVDALI YISIVVLFYL IYRLYAKINN LERQITHIVR EIAIRDRYEP KKRD // ID Y1583_METJA Reviewed; 126 AA. AC Q58978; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 83. DE RecName: Full=Probable S-adenosyl-L-methionine-binding protein MJ1583; GN OrderedLocusNames=MJ1583; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 TsaA-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU01003}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99603.1; -; Genomic_DNA. DR PIR; F64497; F64497. DR ProteinModelPortal; Q58978; -. DR STRING; 243232.MJ_1583; -. DR EnsemblBacteria; AAB99603; AAB99603; MJ_1583. DR KEGG; mja:MJ_1583; -. DR eggNOG; arCOG00761; Archaea. DR eggNOG; COG1720; LUCA. DR InParanoid; Q58978; -. DR OMA; FATRFTQ; -. DR PhylomeDB; Q58978; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.40.30.70; -; 1. DR InterPro; IPR023370; TsaA-like. DR InterPro; IPR023368; UPF0066_cons_site. DR Pfam; PF01980; UPF0066; 1. DR SUPFAM; SSF118196; SSF118196; 1. DR TIGRFAMs; TIGR00104; tRNA_TsaA; 1. DR PROSITE; PS01318; TSAA_1; 1. DR PROSITE; PS51668; TSAA_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 126 Probable S-adenosyl-L-methionine-binding FT protein MJ1583. FT /FTId=PRO_0000155623. FT DOMAIN 4 126 TsaA-like. {ECO:0000255|PROSITE- FT ProRule:PRU01003}. FT REGION 45 46 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 106 109 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT BINDING 75 75 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 126 AA; 14800 MW; D707F0E57BBB2CF0 CRC64; MYYLKPIGVV EQNENYTVLN IFDEFVEGLD GLKEGDYIIV LVWFHKNDSE EKRKILKVHP RGDINNPLKG VFATRSPYRP NPIGKYTVKI HKIYRNKIFI DKIDAYNETP IIDIKIFSEK LDCPKI // ID Y1614_METJA Reviewed; 251 AA. AC Q59009; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ1614; GN OrderedLocusNames=MJ1614; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1311. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99634.1; -; Genomic_DNA. DR PIR; E64501; E64501. DR ProteinModelPortal; Q59009; -. DR STRING; 243232.MJ_1614; -. DR EnsemblBacteria; AAB99634; AAB99634; MJ_1614. DR KEGG; mja:MJ_1614; -. DR eggNOG; arCOG01895; Archaea. DR eggNOG; COG1082; LUCA. DR InParanoid; Q59009; -. DR OMA; ENMPSYD; -. DR PhylomeDB; Q59009; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 251 Uncharacterized protein MJ1614. FT /FTId=PRO_0000107437. SQ SEQUENCE 251 AA; 28930 MW; 7C1AFDABF506E26A CRC64; MKLGVSTSLF LDTDKNLSDA LEILEERVKY VELGCDGNLN VMSDGNIELA QSYDLKYTLH CPITDLNLSS YRERIRKVSL DFVRDVLEVA IKVDAKLIVL HPGYCVFKYD YEKALNSLIK SLNDLNNIQE EFGVQITIEN MPSYDMFMFR NPDKEIIENL GELKITLDIG HSFLNKNIEN FLKISDKIAH IHIHDNNGEF DEHLCIGKGK INFNNFKKDL KKINAIKMIE LQNKSIDDLD LCIDNLKEIL R // ID Y1618_METJA Reviewed; 125 AA. AC Q59013; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1618; GN OrderedLocusNames=MJ1618; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99639.1; -; Genomic_DNA. DR PIR; A64502; A64502. DR ProteinModelPortal; Q59013; -. DR STRING; 243232.MJ_1618; -. DR EnsemblBacteria; AAB99639; AAB99639; MJ_1618. DR KEGG; mja:MJ_1618; -. DR eggNOG; arCOG03003; Archaea. DR eggNOG; COG0662; LUCA. DR InParanoid; Q59013; -. DR OMA; YPPYSHE; -. DR PhylomeDB; Q59013; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR013096; Cupin_2. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF07883; Cupin_2; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 125 Uncharacterized protein MJ1618. FT /FTId=PRO_0000107440. SQ SEQUENCE 125 AA; 14376 MW; 5B8402B3BDAC2404 CRC64; MITMKIIKTE YDKIKPYITK DGSIIRELLH PNIYKGVKQS LAEAIVPVGS KTLLHKHYTS EEIYYILEGR GLMTLDNEKF EVKKGDTIYI PPKTPHKIEN IGNVPLKILC CSYPPYSHED TEILE // ID Y1629_METJA Reviewed; 292 AA. AC Q59023; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=UPF0282 protein MJ1629 {ECO:0000255|HAMAP-Rule:MF_01406}; GN OrderedLocusNames=MJ1629; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0282 family. {ECO:0000255|HAMAP- CC Rule:MF_01406}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99650.1; -; Genomic_DNA. DR PIR; C64503; C64503. DR ProteinModelPortal; Q59023; -. DR STRING; 243232.MJ_1629; -. DR EnsemblBacteria; AAB99650; AAB99650; MJ_1629. DR KEGG; mja:MJ_1629; -. DR eggNOG; arCOG00969; Archaea. DR eggNOG; COG2248; LUCA. DR InParanoid; Q59023; -. DR KO; K07022; -. DR OMA; HYHRDHF; -. DR PhylomeDB; Q59023; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.15.10; -; 1. DR HAMAP; MF_01406; UPF0282; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR014426; UPF0282_hydrls. DR PIRSF; PIRSF004944; UCP004944_hydrls; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 292 UPF0282 protein MJ1629. FT /FTId=PRO_0000057631. SQ SEQUENCE 292 AA; 34049 MW; 6F49BB5A3225E13F CRC64; MKVIPLASES LGVRSLATYV KTKDVGILID PGVALAPDRY GLKPNDIEFE KLREMRNKIN DYAKKSNVIT ISHYHYDHYT PFFDDIYLES KDYAKELYKD KILLIKHPTE FINKSQMNRA KKFLESVKDI AKKIEFADNK TFKFGKTEIK FSPPFPHGRD DKLGYVLITT VKEGKFKFMH TSDTQGIIFD DIRDYIIKEK PNLILMGGPP TYLMHRYGKK NLEKTNENLK YIVENTGAEL IIDHHLLRDK KFREKINVDF KTVAEFLGEK NLLLEAYRKE IKQGKDINEL FG // ID Y1637_METJA Reviewed; 473 AA. AC Q59031; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 91. DE RecName: Full=Uncharacterized protein MJ1637; DE Flags: Precursor; GN OrderedLocusNames=MJ1637; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99658.1; -; Genomic_DNA. DR PIR; C64504; C64504. DR ProteinModelPortal; Q59031; -. DR STRING; 243232.MJ_1637; -. DR DNASU; 1452546; -. DR EnsemblBacteria; AAB99658; AAB99658; MJ_1637. DR KEGG; mja:MJ_1637; -. DR eggNOG; arCOG03167; Archaea. DR eggNOG; COG1373; LUCA. DR InParanoid; Q59031; -. DR KO; K07133; -. DR OMA; PMTFREY; -. DR PhylomeDB; Q59031; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IBA:GO_Central. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 473 Uncharacterized protein MJ1637. FT /FTId=PRO_0000014019. SQ SEQUENCE 473 AA; 55322 MW; 08E8FA079D540C42 CRC64; MIRAFLVFPY LYILVQSNGY TGGIMVQLND YILNHIAKTP LILSRYNKEK KRFDYDILKE KVDKYIENDK KELILLYGLR GLGKTTLLSQ IYHYARLKIE PNRVLYFSMD ELKLNDIKLM DALKAYSEIF GINLYEEKII LLLDEIQYER HWDLVLKNLY DTTNIFIIAT GSSALKLRES PDLARRALHK PIYPMTFREY LYLTKNIKIE SLFEEVILNN NLDNFKKVYA KVYSQILEED VKKYLRIGSL PFALEDDELE VYNKIYTMLE RIIYKDVREV KEFDMETLDK AFKLLYLLAN PKGERYSYES LANTLEIAKG TLINLVDVLE KCELLFKIYP YGSMDKKVRK SQKIKFLPVP IKTALWHKMG VVIDDVCYGS LLEDVVAFYL YLFCKKKGYS LSYEPKKGGA DFILISPYME KIVIEVGLGK KSSKQVLKSM ERVKASKGII IGDELKVEGN ILYIPWKGFL LLI // ID Y1644_METJA Reviewed; 177 AA. AC Q59038; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1644; GN OrderedLocusNames=MJ1644; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99675.1; -; Genomic_DNA. DR PIR; B64505; B64505. DR ProteinModelPortal; Q59038; -. DR STRING; 243232.MJ_1644; -. DR DNASU; 1452553; -. DR EnsemblBacteria; AAB99675; AAB99675; MJ_1644. DR KEGG; mja:MJ_1644; -. DR eggNOG; arCOG01644; Archaea. DR eggNOG; COG2245; LUCA. DR InParanoid; Q59038; -. DR OMA; IIGAFEL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR010397; DUF996. DR Pfam; PF06195; DUF996; 1. DR PIRSF; PIRSF019678; UCP019678; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 177 Uncharacterized protein MJ1644. FT /FTId=PRO_0000107456. FT TRANSMEM 20 42 Helical. {ECO:0000255}. FT TRANSMEM 62 84 Helical. {ECO:0000255}. FT TRANSMEM 94 116 Helical. {ECO:0000255}. FT TRANSMEM 136 158 Helical. {ECO:0000255}. SQ SEQUENCE 177 AA; 19461 MW; A94D57AF68E2804C CRC64; MIKMELKEAK YLGGIGAVLN LVSYAVGGIL AIAGYVLILL ALNKISKIFN DDEVFKKYLY GVVLWIIAVL IVIFAVGISF VSLSFIPLDY GLTAMSSFLV GVILFYILSV IGGYFIKKSY EKVSYYTGVD SFRICGLLYF IGTLLLIVIV GIIVIIVAQI LEIVAYFSLP DDLKSEN // ID Y1658_METJA Reviewed; 119 AA. AC Q59052; DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1658; GN OrderedLocusNames=MJ1658; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99685.1; -; Genomic_DNA. DR PIR; H64506; H64506. DR STRING; 243232.MJ_1658; -. DR EnsemblBacteria; AAB99685; AAB99685; MJ_1658. DR KEGG; mja:MJ_1658; -. DR eggNOG; arCOG06554; Archaea. DR eggNOG; ENOG41125U9; LUCA. DR OMA; IFISEMD; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020380; Uncharacterised_MJ1658. DR ProDom; PD076426; Uncharacterised_MJ1658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein MJ1658. FT /FTId=PRO_0000107461. SQ SEQUENCE 119 AA; 14042 MW; 607B4444AB5FF512 CRC64; MKDKILKDRE EIEKFFIKLL GREIFISEMD IFASRCGCVG IMITVRGLFV DDVEIFKEKI LNKLEELAKS YDINADWIFV RVLPGSDDII NIGVREFCNI CREEYRFKKP RPDLISLKF // ID Y1659_METJA Reviewed; 361 AA. AC Q59053; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 89. DE RecName: Full=Uncharacterized ATP-binding protein MJ1659; GN OrderedLocusNames=MJ1659; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99686.1; -; Genomic_DNA. DR PIR; A64507; A64507. DR ProteinModelPortal; Q59053; -. DR STRING; 243232.MJ_1659; -. DR EnsemblBacteria; AAB99686; AAB99686; MJ_1659. DR KEGG; mja:MJ_1659; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q59053; -. DR KO; K06921; -. DR OMA; RDEIFYE; -. DR PhylomeDB; Q59053; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 361 Uncharacterized ATP-binding protein FT MJ1659. FT /FTId=PRO_0000184677. FT NP_BIND 33 40 ATP. {ECO:0000255}. SQ SEQUENCE 361 AA; 43147 MW; AE223418058A8286 CRC64; MVDSMEFFDR EKEINYLVKV LSFEPNLIYF IYGPINSGKT TLIKHIIENK LDRDKYVVFY INLREHFISK YEDFIEVLFN TYEETFIEKL KKYLLSFIND LPKNIDVKST ILTGIPVPKN TLNEFLSTKN SENVFEYLTK IFEDIKKKGK QPILIIDELQ KIGDLKINGF LIYELFNFFI DLTKEKHLCH VLCLSSDSLF IERVYNEGTL KDRCKYYLVD DFDYKTTKAF LKKHNFNDEE IDIVWHYFGG KPIKLVEAIQ EKLLGEDVKE FCKKSLRVRK RQLKDLLYSL EDDNKELFER VIKLFENFKN RDEIFYEKIS EEIVWTVKKN ILFVNIEEGI LKPQSKLDLL AIREILDEIK T // ID Y1664_METJA Reviewed; 226 AA. AC Q59058; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1664; GN OrderedLocusNames=MJ1664; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99682.1; -; Genomic_DNA. DR PIR; F64507; F64507. DR ProteinModelPortal; Q59058; -. DR STRING; 243232.MJ_1664; -. DR EnsemblBacteria; AAB99682; AAB99682; MJ_1664. DR KEGG; mja:MJ_1664; -. DR eggNOG; arCOG09628; Archaea. DR eggNOG; ENOG41111EV; LUCA. DR OMA; EYNIYIL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 226 Uncharacterized protein MJ1664. FT /FTId=PRO_0000107462. SQ SEQUENCE 226 AA; 26892 MW; 7154EC06DBDF94C9 CRC64; MNKLKLKNEK EVRIKFGEYK LTGFSSDNGN NLYKLFNLTL SKIRYRKAML EHNFQLPKIK ESHKPKEITE KIKENDIYFL ELINEIKKDF KDFCSLDAGT LFELFMYYTL IEFFKENNID AKVIRNLDVS YKGNIFTEID LFVDVFGKNF IFECKNRHIS SNAILKLYGI MKILNINFGV LASTKGFYGN LKKEDIFKEY NIYILDKLIE KEKNKIFKEL KDIFNI // ID Y188_METJA Reviewed; 265 AA. AC Q57647; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0188; GN OrderedLocusNames=MJ0188; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98168.1; -; Genomic_DNA. DR PIR; E64323; E64323. DR ProteinModelPortal; Q57647; -. DR STRING; 243232.MJ_0188; -. DR EnsemblBacteria; AAB98168; AAB98168; MJ_0188. DR KEGG; mja:MJ_0188; -. DR eggNOG; arCOG00622; Archaea. DR eggNOG; arCOG00623; Archaea. DR eggNOG; COG0517; LUCA. DR eggNOG; COG1475; LUCA. DR InParanoid; Q57647; -. DR KO; K00088; -. DR OMA; GRIMFRT; -. DR PhylomeDB; Q57647; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR003115; ParB/Sulfiredoxin_dom. DR InterPro; IPR016427; UCP004699_CBS/ParB. DR Pfam; PF00571; CBS; 2. DR Pfam; PF02195; ParBc; 1. DR PIRSF; PIRSF004699; UCP004699_CBS_ParB; 1. DR SMART; SM00116; CBS; 2. DR SMART; SM00470; ParB; 1. DR SUPFAM; SSF110849; SSF110849; 1. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 265 Uncharacterized protein MJ0188. FT /FTId=PRO_0000106736. FT DOMAIN 9 64 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 67 126 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 265 AA; 29851 MW; B5D0CB9955F69F4A CRC64; MSVKVSEYMT KKVVTVSKDN TVKDVIKLLK ETGHNSFPVV ENGKLIGIVS VHDIVGKDDN EKVENVMTKR KDMVVTTPDA NIMDVGRIMF RTGFSKLPVV DEENNLVGII SNMDVIRSQI EKTTPKKLEN IIKTYKSLGY NLRVEKEEVD VNKLRPTQNK IHADELVGRM YELKKGLAEP IIAIKTKRGD YYILVDGHHR AVAAYKMGVP KLDAYVIYLD TDKKLGIEKT AEIMNLKSLE DVKIVDSDDE NSVKVIKYNK NGVLG // ID Y200_METJA Reviewed; 82 AA. AC Q57653; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized hydrogenase expression/formation protein MJ0200; GN OrderedLocusNames=MJ0200; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HupF/HypC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98184.1; -; Genomic_DNA. DR PIR; A64325; A64325. DR ProteinModelPortal; Q57653; -. DR STRING; 243232.MJ_0200; -. DR EnsemblBacteria; AAB98184; AAB98184; MJ_0200. DR KEGG; mja:MJ_0200; -. DR eggNOG; arCOG04427; Archaea. DR eggNOG; COG0298; LUCA. DR InParanoid; Q57653; -. DR KO; K04653; -. DR OMA; MCLAIPC; -. DR PhylomeDB; Q57653; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019812; Hydgase_assmbl_chp_CS. DR InterPro; IPR001109; Hydrogenase_HupF/HypC. DR Pfam; PF01455; HupF_HypC; 1. DR PRINTS; PR00445; HUPFHYPC. DR TIGRFAMs; TIGR00074; hypC_hupF; 1. DR PROSITE; PS01097; HUPF_HYPC; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 82 Uncharacterized hydrogenase FT expression/formation protein MJ0200. FT /FTId=PRO_0000201408. SQ SEQUENCE 82 AA; 9348 MW; 46C7C47A06FAB808 CRC64; MCLAIPCKVV EIIEEDGEKY AIAEYKGVKQ KAKLTLLDKE VKIGDYILIH TGYALEVLSE EDAKLSLEAW EELFKALEEM EQ // ID Y207_METJA Reviewed; 151 AA. AC Q57660; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0207; GN OrderedLocusNames=MJ0207; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98194.1; -; Genomic_DNA. DR PIR; H64325; H64325. DR ProteinModelPortal; Q57660; -. DR STRING; 243232.MJ_0207; -. DR EnsemblBacteria; AAB98194; AAB98194; MJ_0207. DR KEGG; mja:MJ_0207; -. DR eggNOG; arCOG07626; Archaea. DR eggNOG; ENOG410Y55T; LUCA. DR OMA; RICGYEF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR SUPFAM; SSF111126; SSF111126; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 151 Uncharacterized protein MJ0207. FT /FTId=PRO_0000106741. SQ SEQUENCE 151 AA; 16912 MW; 03F78A3F2EBCA189 CRC64; MVLYKIRRSK NDPCPSIPSA VIIGYSVGLK LITGHGAQSL SNMAGSYAGK ELGIYAMNNG YEFKDIKDIE RFLNQLDFAK IEMNEEEDEI IVKISKCNLC PKRICGYEFE GTACPWGGLL IGFISETLKY NLGYQMNLKP AETCIIKLKK K // ID Y21B_METJA Reviewed; 172 AA. AC P81232; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0210.1; GN OrderedLocusNames=MJ0210.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98206.1; -; Genomic_DNA. DR STRING; 243232.MJ_0210.1; -. DR DNASU; 1451060; -. DR EnsemblBacteria; AAB98206; AAB98206; MJ_0210.1. DR KEGG; mja:MJ_0210.1; -. DR eggNOG; arCOG09658; Archaea. DR eggNOG; ENOG41110F4; LUCA. DR OMA; YSWKEFK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 172 Uncharacterized protein MJ0210.1. FT /FTId=PRO_0000106743. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. SQ SEQUENCE 172 AA; 20084 MW; 510779FF2FE9817A CRC64; MFNKVAFMNI PMMDLIMIVI AIIITIGSFL FIAYLIFKYS KIKKQVKIIR EVKINLPKML KSNMIKNSFL IISLLCFYFG MLYIAGELVI SHILFIAICW IVVFLYIIIK GETRGYICEE GLLVSGVLYS WKEFKDVKIE DNYIILTTPI HKIVIKKEKG VENILKNYLK RN // ID Y264_METJA Reviewed; 153 AA. AC Q57712; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Uncharacterized protein MJ0264; GN OrderedLocusNames=MJ0264; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 4 [4Fe-4S] clusters. {ECO:0000250}; CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98251.1; -; Genomic_DNA. DR PIR; A64333; A64333. DR ProteinModelPortal; Q57712; -. DR STRING; 243232.MJ_0264; -. DR EnsemblBacteria; AAB98251; AAB98251; MJ_0264. DR KEGG; mja:MJ_0264; -. DR eggNOG; arCOG01502; Archaea. DR eggNOG; COG1142; LUCA. DR InParanoid; Q57712; -. DR KO; K00196; -. DR OMA; CLYACPE; -. DR PhylomeDB; Q57712; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF13247; Fer4_11; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 153 Uncharacterized protein MJ0264. FT /FTId=PRO_0000159309. FT DOMAIN 16 45 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 40 71 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 71 100 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 95 129 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 25 25 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 28 28 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 31 31 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 35 35 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 49 49 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 52 52 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 57 57 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 61 61 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 80 80 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 83 83 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 86 86 Iron-sulfur 4 (4Fe-4S). {ECO:0000250}. FT METAL 90 90 Iron-sulfur 3 (4Fe-4S). {ECO:0000250}. FT METAL 104 104 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 107 107 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 115 115 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 119 119 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 153 AA; 17013 MW; 8550F880E9FD487F CRC64; MHQVKSFLLL AIDGEKMVVV NVGSCIGCRR CERSCPINGI TFNEFPIKCM HCDRNPCLYA CPENAIERIN NKVVVIKDKC VGCGLCALAC PFGAIRIDGV AIKCNGCYKR DVEICKEVCP TGAINNLEEI LNNKIQNTVN KFNKLYYLYA NAK // ID Y271_METJA Reviewed; 180 AA. AC Q57719; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0271; GN OrderedLocusNames=MJ0271; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98260.1; -; Genomic_DNA. DR PIR; H64333; H64333. DR ProteinModelPortal; Q57719; -. DR DNASU; 1451125; -. DR EnsemblBacteria; AAB98260; AAB98260; MJ_0271. DR KEGG; mja:MJ_0271; -. DR OMA; ANMFIIE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 180 Uncharacterized protein MJ0271. FT /FTId=PRO_0000106764. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. SQ SEQUENCE 180 AA; 20813 MW; F306D3E4BC0ECFB6 CRC64; MDLKSNIKLI LATDLLAVLI LSLFIKNFKM VLAFLLAVFV IWLFIDKNNI NERLYENLLA MSVGFIEGIL IFLGIIYNEV FLDITLGIFA ILILIVMGIL FPKYKLIFEV FDEFVEHLKQ KSGFLTLISI FGMLLTIYVF LLILPSKEFC INAVDIIRTI MLVITANMFI IEFYTFKKFS // ID Y304_METJA Reviewed; 159 AA. AC Q57752; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0304; GN OrderedLocusNames=MJ0304; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the gamma-class carbonic anhydrase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98291.1; -; Genomic_DNA. DR PIR; A64338; A64338. DR ProteinModelPortal; Q57752; -. DR STRING; 243232.MJ_0304; -. DR EnsemblBacteria; AAB98291; AAB98291; MJ_0304. DR KEGG; mja:MJ_0304; -. DR eggNOG; arCOG01849; Archaea. DR eggNOG; COG0663; LUCA. DR InParanoid; Q57752; -. DR OMA; HACTVKD; -. DR PhylomeDB; Q57752; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR001451; Hexapep. DR InterPro; IPR011004; Trimer_LpxA-like. DR Pfam; PF00132; Hexapep; 2. DR SUPFAM; SSF51161; SSF51161; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 159 Uncharacterized protein MJ0304. FT /FTId=PRO_0000077472. SQ SEQUENCE 159 AA; 17174 MW; 8EBE072E411BCC94 CRC64; MISKNVRIAK GAVIVGDVTI GDYSSVWYNA VIRGDVDKII IGNYSNIQDC CVVHCSKGYP TIIGDYVSIG HGAVIHGCRI EDNVLVGMNA TILNGAKIGE NCIIGANALV TQNKEIPPNS LVLGVPGRVV RELTEEEIKS IKENALRYVK LSETLESYK // ID Y317_METJA Reviewed; 224 AA. AC Q57765; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0317; GN OrderedLocusNames=MJ0317; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98311.1; -; Genomic_DNA. DR PIR; F64339; F64339. DR ProteinModelPortal; Q57765; -. DR STRING; 243232.MJ_0317; -. DR EnsemblBacteria; AAB98311; AAB98311; MJ_0317. DR KEGG; mja:MJ_0317; -. DR eggNOG; arCOG05029; Archaea. DR eggNOG; ENOG410Y9GS; LUCA. DR OMA; RGVFSWT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 224 Uncharacterized protein MJ0317. FT /FTId=PRO_0000106790. SQ SEQUENCE 224 AA; 26112 MW; 1EBF400D80C4AAC1 CRC64; MKPKYALRKD MIGEFTLNKS FNTYRGKVLK ADFNGPIEGI VMKNKKEHIY FYPLLALHMV KPLNCVPINV IPKTSLPTNP KNVHIKEALS RIVGRTLKVY YETPKTSYLG RLLGFTRGVF SWTLVLEIHG EVVLLFNPDY IVYYGTKWKF LKNNPPYKPP RLMNITKTAN YLKRCLLEDV IIEPEYPRIN IEDKVFVYPY GVVSKDDYLG KTVEDILKEK EFLI // ID Y336_METJA Reviewed; 119 AA. AC Q57782; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0336; GN OrderedLocusNames=MJ0336; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98324.1; -; Genomic_DNA. DR PIR; H64341; H64341. DR STRING; 243232.MJ_0336; -. DR EnsemblBacteria; AAB98324; AAB98324; MJ_0336. DR KEGG; mja:MJ_0336; -. DR eggNOG; arCOG09641; Archaea. DR eggNOG; ENOG410Z9WP; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein MJ0336. FT /FTId=PRO_0000106806. SQ SEQUENCE 119 AA; 12393 MW; B27750A524DE2E5C CRC64; MTTENIISGI AIADLAPYRF GKITSTGIGF GTSTVSDDSI SIDADGVIIN SRAIYTAGMY VDLKVNGVQK VEIKEGESIA PGDYVIPSTD GSGKAVKSPI KAGFKVASVE GNYCTIILR // ID Y3402_METJA Reviewed; 1181 AA. AC Q60301; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized adenine-specific methylase MJECS02; DE EC=2.1.1.72; GN OrderedLocusNames=MJECS02; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + DNA adenine = S- CC adenosyl-L-homocysteine + DNA 6-methylaminopurine. CC -!- SIMILARITY: Belongs to the N(4)/N(6)-methyltransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37060.1; -; Genomic_DNA. DR PIR; B64516; B64516. DR ProteinModelPortal; Q60301; -. DR REBASE; 6813; MjaORFECS2P. DR EnsemblBacteria; AAC37060; AAC37060; MJ_ECS02. DR KEGG; mja:MJECS02; -. DR InParanoid; Q60301; -. DR OMA; NIEYNVR; -. DR Proteomes; UP000000805; Plasmid small ECE. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008170; F:N-methyltransferase activity; IEA:InterPro. DR GO; GO:0009007; F:site-specific DNA-methyltransferase (adenine-specific) activity; IEA:UniProtKB-EC. DR Gene3D; 3.40.50.150; -; 3. DR InterPro; IPR003356; DNA_methylase_A-5. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR011639; RM_methylase_Eco57I. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR025931; TaqI_C. DR Pfam; PF07669; Eco57I; 1. DR Pfam; PF02384; N6_Mtase; 1. DR Pfam; PF12950; TaqI_C; 1. DR SUPFAM; SSF53335; SSF53335; 3. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Plasmid; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 1181 Uncharacterized adenine-specific FT methylase MJECS02. FT /FTId=PRO_0000088002. SQ SEQUENCE 1181 AA; 138439 MW; 9F961D8F8C6A4BDD CRC64; MVVMAQTKLC SDIEIPKEVY NKWKDFIKLV GNIILSIKQI PELEGKFKEL LKKGRYNFKS DDFGGQLPEP FTRQKVIEPI LEFLGYEFTS EISKKSPLGD RKIPDYRVSV FNKEILIEAE PLGSDLNKKD SGIHQVKEWL IIKSYGVDTG IATNGLEWVL LHYDDTIKEI RTLKELNLKS IFEYVLENKK DKDLENELKQ VFSEFYYCFS KEYIEEYIEV ATKNIKHKKE EITNEFYKEF VKLVFGFEDV KDVKKKDKSS SEKDKGTKKC LYNCIEAPPN TSELDKKKFA VLLMNRLIFI KFLEDKGIVP RDLLRRTYED YKKSNVLINY YDAYLKPLFY EVLNTPEDER KENIRTNPYY KDIPYLNGGL FRSNNVPNEL SFTIKDNEII GEVINFLERY KFTLSTSEGS EEVELNPDIL GYVYEKLINI LAEKGQKGLG AYYTPDEITS YIAKNTIEPI VVERFKEIIK NWKINDINFS TLDEILNEDS KIAENKHILR AFLDELDKIR ILDPAVGSGH FLISALKELL QIKKRIYYLL REEMDIYKEK LGIILNNLYG VDIDDIAVEI AKLRLWLALI ENLDVEALKR GEVLLPNIEY NVRCGNSLVG WIDENLKQLS ISYLCDNVRI MCVLEGLIIN AHNSEERKKL KKAKELLEKR DGYVLDNYVE AYHLLYEVYR TSHGLKANLL KELLDEIRDS IYESVTPAYF AEIYQNGNNK KNNGKKSKKN RPRVEEFEKL KPFHWKIDFG WIIKEEGFDV IIGNPPYGNL LSPTEKEIMK RRDTPEFDIF VTFIVHSSKL LKNEGYLGFI IPSSFGTGVR YSNLRKELFT KMCLKKLIYL PFDVFSGAYV DNCIIILHKK PPKSEDLVLI YAFPKKTKKI SFEFKNDLFI EYSKILNDPK CRIFPKSPEI YIILDKIKQN CRESLTYLED LTESTIGILA SKYKFSDKKE NEYYLPYLEG NVYRYETKLK LKNYVDFSKH KNNEKLINLF MSPEKIFIRR IVNRQDRIMA SYGNIEGVVK KDLYVFVLKP DTPINYFYLL GILNSELISY IYIGKSAIAL KDDFRQTTLE ELRELPIVIP KNKNIINALT QLSKLRFELN DKLNENDRIF LENIIDSLVY GIYFQDLIPK EELNEICNEI NGIIKKYDEK SIDCLKYCQN IIKLLNTINT NELVRKIRNK N // ID Y3411_METJA Reviewed; 168 AA. AC Q60310; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 13-APR-2004, sequence version 2. DT 09-DEC-2015, entry version 73. DE RecName: Full=UPF0304 protein MJECS11 {ECO:0000255|HAMAP-Rule:MF_00762}; GN OrderedLocusNames=MJECS11; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0304 family. {ECO:0000255|HAMAP- CC Rule:MF_00762}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37069.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37069.1; ALT_INIT; Genomic_DNA. DR PIR; C64517; C64517. DR ProteinModelPortal; Q60310; -. DR EnsemblBacteria; AAC37069; AAC37069; MJ_ECS11. DR KEGG; mja:MJECS11; -. DR InParanoid; Q60310; -. DR KO; K09161; -. DR OMA; DKADHHF; -. DR Proteomes; UP000000805; Plasmid small ECE. DR Gene3D; 1.10.287.680; -; 1. DR Gene3D; 1.10.3190.10; -; 1. DR HAMAP; MF_00762; UPF0304; 1. DR InterPro; IPR005587; UPF0304_YfbU. DR InterPro; IPR023146; YfbU_alpha-helical. DR InterPro; IPR023145; YfbU_helix-hairpin. DR Pfam; PF03887; YfbU; 1. DR PIRSF; PIRSF006272; UCP006272; 1. DR ProDom; PD035118; YfbU; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 168 UPF0304 protein MJECS11. FT /FTId=PRO_0000218176. SQ SEQUENCE 168 AA; 20255 MW; 71AE55175D60F70F CRC64; MLSKIERLIL ANQYKILKIL ENTSEYDEII KILEEGYEIF YDEILGHIFD ELPESEGQFV LDILSFYDIV VEPYKQKNPN DHEIINHPYS YFKGFDGNSE TKYMAFVRFL IEDQKKFSFV AKYAKKTDNF NSHFPMLDKY RKMVELWESK YNKKYDLKRE EILDILNA // ID Y344_METJA Reviewed; 180 AA. AC Q57790; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0344; GN OrderedLocusNames=MJ0344; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98334.1; -; Genomic_DNA. DR PIR; H64342; H64342. DR STRING; 243232.MJ_0344; -. DR EnsemblBacteria; AAB98334; AAB98334; MJ_0344. DR KEGG; mja:MJ_0344; -. DR eggNOG; arCOG09648; Archaea. DR eggNOG; ENOG4110ZR8; LUCA. DR OMA; TIDESKH; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 180 Uncharacterized protein MJ0344. FT /FTId=PRO_0000106814. SQ SEQUENCE 180 AA; 19402 MW; 9EF646A626CDF3E2 CRC64; MAVLASSTEP EPTESLLQQT NELLIIGKGA IVYKEFTTGV DARIIDSQTI GIGIPFNYYP FMCMVLDDAG NGIPMQEFTS APGSLTVKVA ATLDSTKTYK IIAFLIGDSM KIITSIQSQS GTVTEIAPGF GIFKVIYNDT EGTDTLTINY DDGTSETITV DKSNLWTVLP MQLPDAERVA // ID Y348_METJA Reviewed; 795 AA. AC Q57794; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0348; GN OrderedLocusNames=MJ0348; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98337.1; -; Genomic_DNA. DR PIR; D64343; D64343. DR ProteinModelPortal; Q57794; -. DR STRING; 243232.MJ_0348; -. DR EnsemblBacteria; AAB98337; AAB98337; MJ_0348. DR KEGG; mja:MJ_0348; -. DR eggNOG; arCOG09651; Archaea. DR eggNOG; ENOG410YC6E; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 795 Uncharacterized protein MJ0348. FT /FTId=PRO_0000106819. SQ SEQUENCE 795 AA; 92391 MW; 2E782E6A74889639 CRC64; MVIMPFVHYI DEENFDDKLK EWTLGLNSDY VNPYDSGETQ YINSNYPWPA NINSLSSKIC EMGLIEMDGV EIRSVPLHWV STVSVPTAPS SSFVFNIPSM FQECMYECHI YNLPPDAGVT ATYNAYFDNN FPIPYKYTLT IQTSADDMFN NQDYKIWMNG TWGPSFHIPE SGTKILEFPI KYGKLNISFG ISGSSLTVTL MWIIENNNIN DFFDPDTEDY WQLIGRNINI VFGNFLPKHF PRGYINPIQN RTYLEKRILN TGDASNPTTI EYLWGSVTLL PDLESWQFYD DKGNSVDSKY ATISDDGYVS IYYEEMIKDG YFPKAIYLWT VHKESYLEAE PSIGTFERNE ESGVSERCDF DIIAFKKKYT GNLLTCVPLI VYFRPCEVPL GDINKWGWQP YIYYFDTYNV KPYCEKFIVR PKCICYRNSD PNEKTITFDI EYEINVDTKY LGWFQPELRL YYGGVLVDSK TGDVSNFTYT FRMPQNTIET YEMKLFIGGV EVAKEQIIVE RQKYCHSLSI EAKTYDKEGN ETDKFPHPTS ADYDENKHSE IIVKIKIKDE QGNYIDVPIE NIFINWQYPL NKINTGIYEV RIPNTADNAL NIQDYGIAIY IDKDWCDENG YYNKYNIEAE NVIINSDKIE RIGLWNFEGI TGYENGTTLL NQVYETVSGT FVNPICEFSV VEQLNEDRDL KQYSYCYRIY GSPMTLNLPT YTDDELKELA KAIVREMGQP RKIETFTILS KELQKINSSI TVDYNGQLIS MPVYSVRFSL ENSNIQIQIR NDQLKLLKDY LSLIK // ID Y3501_METJA Reviewed; 249 AA. AC Q60266; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Uncharacterized protein MJECL01; GN OrderedLocusNames=MJECL01; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37075.1; -; Genomic_DNA. DR PIR; A64510; A64510. DR ProteinModelPortal; Q60266; -. DR EnsemblBacteria; AAC37075; AAC37075; MJ_ECL01. DR KEGG; mja:MJECL01; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 249 Uncharacterized protein MJECL01. FT /FTId=PRO_0000107493. SQ SEQUENCE 249 AA; 29998 MW; 5420C6442CB84E31 CRC64; MMGEQLDYLL NIVKNDKKFL ETLKNMKIDV DSDEELSKIF FIIITFPFWL RCHDDIKNAL RLIDKITNKG SFTKVLDNSM KEYHVFYIYD VDKLSDLIAE ELKRLYLICK SEGKSYYENI FFRLDRKSIL KLFMKISPFK QLDVIKGKLK NQLDFFEEYF NNIEKIGYFS IRMENSRYNE HIKSLHPKLI ISLRVDKVHI RLEAQIDYYN INNENEEAYK KILELMKLNL LTIGYKAVEK FLEEIYEEV // ID Y351_METJA Reviewed; 150 AA. AC Q57797; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0351; GN OrderedLocusNames=MJ0351; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98340.1; -; Genomic_DNA. DR PIR; G64343; G64343. DR ProteinModelPortal; Q57797; -. DR STRING; 243232.MJ_0351; -. DR EnsemblBacteria; AAB98340; AAB98340; MJ_0351. DR KEGG; mja:MJ_0351; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 150 Uncharacterized protein MJ0351. FT /FTId=PRO_0000106822. SQ SEQUENCE 150 AA; 16810 MW; 8A82F7D62AA4D58B CRC64; MVEKMSPKTF GGEIMENSDI RAKLLEVLES GVVNGKWTIG IVRLNSELRR LLVNRCQCYI NDSETTKSKT KIIAEFCMDA AENGVRYSPD LVNAALTILK SMGYNIKDVQ CYYDVDFPAV ITVDGEVGVV IKPEHMEDLR VVGVKKLTEF // ID Y3520_METJA Reviewed; 147 AA. AC Q60280; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 69. DE RecName: Full=Uncharacterized protein MJECL20; GN OrderedLocusNames=MJECL20; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0215. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37091.1; -; Genomic_DNA. DR PIR; C64512; C64512. DR ProteinModelPortal; Q60280; -. DR EnsemblBacteria; AAC37091; AAC37091; MJ_ECL20. DR KEGG; mja:MJECL20; -. DR HOGENOM; HOG000155151; -. DR InParanoid; Q60280; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004725; F:protein tyrosine phosphatase activity; IBA:GO_Central. DR GO; GO:0035335; P:peptidyl-tyrosine dephosphorylation; IBA:GOC. DR Gene3D; 3.90.190.10; -; 1. DR InterPro; IPR029021; Prot-tyrosine_phosphatase-like. DR InterPro; IPR000387; TYR_PHOSPHATASE_dom. DR SUPFAM; SSF52799; SSF52799; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MJECL20. FT /FTId=PRO_0000107508. SQ SEQUENCE 147 AA; 16976 MW; 9F615C1406747570 CRC64; MGKCRHNGEV SIFGVRPASF PYFPFNLMDR IGGFVILDEL WLRRWCEIIE YPMKIPTLYV PIEDYGIPTV EDMDLIVDFI KYHVSNGREV VVSCIGGHGR TGTVLAIWAG LNGVENPIEY VRECYCECAV ETEEQEEFVM EYLKKRL // ID Y3523_METJA Reviewed; 827 AA. AC Q60282; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJECL23; GN OrderedLocusNames=MJECL23; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37094.1; -; Genomic_DNA. DR PIR; F64512; F64512. DR ProteinModelPortal; Q60282; -. DR EnsemblBacteria; AAC37094; AAC37094; MJ_ECL23. DR KEGG; mja:MJECL23; -. DR InParanoid; Q60282; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 2.140.10.10; -; 2. DR InterPro; IPR018391; PQQ_beta_propeller_repeat. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR027295; Quinoprotein_ADH-like_fam. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR Pfam; PF01011; PQQ; 3. DR Pfam; PF13360; PQQ_2; 2. DR SMART; SM00564; PQQ; 13. DR SUPFAM; SSF50998; SSF50998; 2. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 827 Uncharacterized protein MJECL23. FT /FTId=PRO_0000107511. SQ SEQUENCE 827 AA; 95203 MW; 6C0E929BAF645F1C CRC64; MVMRMVFVEN KINGVENIRQ EIDNLNVSNY KEIYDKFKNV FSKNRDIFNY YVDKLIELMK NLDDNELSLE IDKFMLCILK DSIIWEFKAG GSVWDLSIKD IKDNIIILGC SNHLFALDIK TGNKIWEYKV EHNVDSLFIK DNIVMLEYRG GHVCVLDVMT GDKIWESKVG ERMWGFSLKD NIVILGDGDK YIYAIDVRTG GKLWEFEAEW CVWELSIKDD KIILRCEDEY GCEYFYVLDI KTGEKILEFG GEWHVSDLLI SGDVTILADM WGCVYALDTN LYSKIQRVRP QLTNIMKEIV KIDLTLLKKS LNLNEWDELP IQITNKSLKD ITISKISIIN EEDILFKDIE PIKIRGRDTK VINLFINPKV KGKLPIDIVV EFEDEFNIRY KERFTEVLTI TKFKGDNVDD MRPEKIDKIL KQEIDNLNTS NYKEIYSRFK NIFNENRAVF NYYMNKLIEL VNNSNDELAI NVGKFILDIL GIKRVDELLW EFRAEGGVRL LSIKGDIVIL GCVSGHVYAI DIKTGKKLWE FKAEDTVWGL SIKDDIVVLG CGNIFESIVM LKNGKILEEG YAYALDINTG REIWRSKIKH DVRSLSIKDD IVVLGCKKGY ILALDINAGN MLWEFKAKSG KSIRNLSIKN DILLFGCDNY LYALDIDTGR ELWRFKAEGE VKSLSIKKDN VLLGCRGGYV YLLDINTGEK MERFKVVGSV LRLSIKDDIV ILGCNRECVY ALDINAGENL WAFKTDGDVN GLSIKNDAVL LGCDNYLYAL DINTGEEIWK FKTESAVLDL SIKDNIVISG CKRGHVYALD FNIIKNYSII QKIKQVL // ID Y3532_METJA Reviewed; 438 AA. AC Q60289; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MJECL32; GN OrderedLocusNames=MJECL32; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37101.1; -; Genomic_DNA. DR PIR; G64513; G64513. DR ProteinModelPortal; Q60289; -. DR EnsemblBacteria; AAC37101; AAC37101; MJ_ECL32. DR KEGG; mja:MJECL32; -. DR InParanoid; Q60289; -. DR OMA; TSISIID; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 438 Uncharacterized protein MJECL32. FT /FTId=PRO_0000107516. SQ SEQUENCE 438 AA; 50925 MW; DC8FB11505F5DEE3 CRC64; MGKELDNRTL DFYFEKYGKK KTSTEPSYKD IIEYITALIS ENLEDYQSQH TKLINIILNL VYPIKYFPHH LYDLGYRPKK GSTLGVRIVL DGIYYTKNGN PAEITPDVIL VNDNDTHVLI FECKSKSIKK EQLEKYLKLK ENLHVIINKG YISVTKNPRL YKSDVSYMSF DDLTTHPVLK DTEDIQILKV SPGEISLERG NYENQKLNKI FPITWGEKEK PSYDLLICDA ENDKEGSLFK ILILRELVSM ALSGHDEPEV GMVFSKKIIL PKGEYSLESL KEDDFKEIEN IIQKLCKKKC IIDKENKLLR VDKDIVILPE NKPLNANVLK LIDALNISIN MDSLVEKEFT VGTIMDALYR STSISIIDYF YKDYKNIVSK RIEETLKLFS NRNLKGYLKK VSRKWRIKVI KDKRMARKFK ESCKEEIGAI KSWQTTLD // ID Y3534_METJA Reviewed; 295 AA. AC Q60258; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 48. DE RecName: Full=Uncharacterized protein MJECL34; GN OrderedLocusNames=MJECL34; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37103.1; -; Genomic_DNA. DR PIR; A64514; A64514. DR ProteinModelPortal; Q60258; -. DR EnsemblBacteria; AAC37103; AAC37103; MJ_ECL34. DR KEGG; mja:MJECL34; -. DR HOGENOM; HOG000155271; -. DR OMA; DERYPYS; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 295 Uncharacterized protein MJECL34. FT /FTId=PRO_0000107518. SQ SEQUENCE 295 AA; 33624 MW; 191F9DA02F0D2151 CRC64; MKHMTPGLTE KKLYVYYDER YPYSWIPHNV AKHISKELEK YDFEVIDAPS LQRVLGEGSK DTNKEYVVVF AQDVVPDLVL DNPDNPTSNS LLRRFLNAGQ IIVWMGDSPQ YVGRADDNQK LNPPVMQNVL SMNPNYITTN KRISLTISGI VLSLPLWVGT KPHNKTPPHG VSGVSINPLA VAIDNVQYAH AFIISYKQSA SGFVRIYDFP INKEELVTKQ FIRGILGVAT RDVTTPIWNK IEILSEEVNK IDEKFDTKFN TLKSEIDTFK TTINEILKLE KEILEVIQKK CENKE // ID Y3538_METJA Reviewed; 259 AA. AC Q60293; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJECL38; GN OrderedLocusNames=MJECL38; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37107.1; -; Genomic_DNA. DR PIR; E64514; E64514. DR ProteinModelPortal; Q60293; -. DR DNASU; 1450820; -. DR EnsemblBacteria; AAC37107; AAC37107; MJ_ECL38. DR KEGG; mja:MJECL38; -. DR InParanoid; Q60293; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF10130; PIN_2; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. PE 4: Predicted; KW Complete proteome; Membrane; Plasmid; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 259 Uncharacterized protein MJECL38. FT /FTId=PRO_0000107521. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT COMPBIAS 123 163 Lys-rich. FT COMPBIAS 239 255 Ile-rich. SQ SEQUENCE 259 AA; 30076 MW; 00AEC07D21973C0A CRC64; MANMQSLTNI EVQRFHDCEW EYFKEFDDEF NKLWNEIEKT LGRDFINYLS AYFQKNLVYM LGKEFKLKLV VDTNIIFSQV LSYVTKGELP WILDFINNPF IELYAPQLIV DELKNKIENV LPKKCKKKNI DENKAKSKAI KIANIILSNI KIINDKKSNN WSKIAYNLIG HRDVKDIPFV TLALSLDTHG IITRDKDFKD QKIIKIWKVG EVKVVLTELS QGSFSFCIMN VTAPLAFKIC TSIIITILEI VTSIIKKTN // ID Y353_METJA Reviewed; 84 AA. AC O06918; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0353; GN OrderedLocusNames=MJ0353; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98342.1; -; Genomic_DNA. DR PIR; A64344; A64344. DR ProteinModelPortal; O06918; -. DR STRING; 243232.MJ_0353; -. DR EnsemblBacteria; AAB98342; AAB98342; MJ_0353. DR KEGG; mja:MJ_0353; -. DR eggNOG; arCOG08302; Archaea. DR eggNOG; ENOG4111180; LUCA. DR OMA; VNRRDLN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 84 Uncharacterized protein MJ0353. FT /FTId=PRO_0000106824. SQ SEQUENCE 84 AA; 9983 MW; 6ABE05448DB8A210 CRC64; MMRYSSNKIY FIVYLGGKPV SFGVAKDVDE FERRRENIEC LSDKIRVVKV GKKLFKRLRR QILEGEKKDF GMLKVNRRDL NVQV // ID Y354_METJA Reviewed; 58 AA. AC Q57800; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0354; GN OrderedLocusNames=MJ0354; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98343.1; -; Genomic_DNA. DR PIR; B64344; B64344. DR STRING; 243232.MJ_0354; -. DR EnsemblBacteria; AAB98343; AAB98343; MJ_0354. DR KEGG; mja:MJ_0354; -. DR eggNOG; arCOG09666; Archaea. DR eggNOG; ENOG41110IS; LUCA. DR OMA; DYNNGDT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 58 Uncharacterized protein MJ0354. FT /FTId=PRO_0000106825. SQ SEQUENCE 58 AA; 6781 MW; 354AC901F74A6500 CRC64; MQINKAIELL ERAWSDYNNG DTVGAILKLE EAEDLIRKLR VRLCSEIRRE GYDAIFIK // ID Y365_METJA Reviewed; 176 AA. AC Q57811; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0365; GN OrderedLocusNames=MJ0365; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98356.1; -; Genomic_DNA. DR PIR; E64345; E64345. DR ProteinModelPortal; Q57811; -. DR STRING; 243232.MJ_0365; -. DR PRIDE; Q57811; -. DR EnsemblBacteria; AAB98356; AAB98356; MJ_0365. DR KEGG; mja:MJ_0365; -. DR eggNOG; arCOG03130; Archaea. DR eggNOG; COG3359; LUCA. DR KO; K07502; -. DR OMA; DESEYYL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.30.420.10; -; 2. DR InterPro; IPR012337; RNaseH-like_dom. DR Pfam; PF13482; RNase_H_2; 1. DR SUPFAM; SSF53098; SSF53098; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 176 Uncharacterized protein MJ0365. FT /FTId=PRO_0000106834. SQ SEQUENCE 176 AA; 20784 MW; C62A30BD30321777 CRC64; MAKAIIDIET TGLNPMEHRI VAIGVKLGDR DIILMDESEY YLLVNFWDTV EKEGIEKIIG FNIDFDWQFL KLRSLYHRLK IKHFRKYQGR VDLRQILNGS GGQYRKGTKL VDYCRFLGID VPEDDANGSE IPELWEKFEE EGDEEAKRKI CEHLKRDLER TWELYKILVD CGLIEE // ID Y374_METJA Reviewed; 330 AA. AC Q57819; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 70. DE RecName: Full=Uncharacterized protein MJ0374; GN OrderedLocusNames=MJ0374; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98363.1; -; Genomic_DNA. DR PIR; F64346; F64346. DR ProteinModelPortal; Q57819; -. DR STRING; 243232.MJ_0374; -. DR EnsemblBacteria; AAB98363; AAB98363; MJ_0374. DR KEGG; mja:MJ_0374; -. DR eggNOG; arCOG03056; Archaea. DR eggNOG; arCOG03118; Archaea. DR eggNOG; COG0671; LUCA. DR eggNOG; COG1238; LUCA. DR InParanoid; Q57819; -. DR OMA; PYKVIAW; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.144.10; -; 1. DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase. DR InterPro; IPR032816; SNARE_assoc. DR Pfam; PF01569; PAP2; 1. DR Pfam; PF09335; SNARE_assoc; 1. DR SMART; SM00014; acidPPc; 1. DR SUPFAM; SSF48317; SSF48317; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 330 Uncharacterized protein MJ0374. FT /FTId=PRO_0000106837. SQ SEQUENCE 330 AA; 37018 MW; BA84B0170694C097 CRC64; MISGGYMDLY AMAEYLVNNY GYIGIFIISF TEAFIQPIPP DVFIIGASFF GLNPIISAIV ATIGTTLGGL FGYFLGDKLG HPIFIKLFGE KYLHKGEEFF NKYGVYGVVI AGFSPLPYKV IAWLSGIFEM HKLLFTVGTI IGRLPRFLAV AYFGDVLGNI NRLSDINIYL FYLINSHYNY IFDAIMPIIS KTAYPLIAIT SLIIFIKNRK FGMKLIFALF LAFMIAFSLK YLVNEPRPYL VLDNVHLLCN EGNEPSFPSG HTTLAFTLAT SLLFYSKKLG ILFLSWAIIV AYSRVYVGVH YPLDVLAGMI IGIFCGCLTR IDIYKLIDNI // ID Y410_METJA Reviewed; 264 AA. AC Q57853; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized ATP-binding protein MJ0410; GN OrderedLocusNames=MJ0410; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98399.1; -; Genomic_DNA. DR PIR; B64351; B64351. DR ProteinModelPortal; Q57853; -. DR STRING; 243232.MJ_0410; -. DR EnsemblBacteria; AAB98399; AAB98399; MJ_0410. DR KEGG; mja:MJ_0410; -. DR eggNOG; arCOG00589; Archaea. DR eggNOG; COG0455; LUCA. DR InParanoid; Q57853; -. DR OMA; PNITEGN; -. DR PhylomeDB; Q57853; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 264 Uncharacterized ATP-binding protein FT MJ0410. FT /FTId=PRO_0000106859. FT NP_BIND 8 15 ATP. {ECO:0000255}. SQ SEQUENCE 264 AA; 29512 MW; BC6D63DAF061B1EB CRC64; MKIGFYNIQG GTGKTTVAAN FAYILSQSVK TILIDCDIYG GTTAVLFGLE DKEHNLNTYL AGDSAIEDII YHYDDLAIIH TDVSSKVFGY KSDLNRFETL VKELEEEYDV IIYDFPPNIT EDNPLIGYVG EFELVNKVVV VGEDSIPSIV NSLKTIELIT DLGIGLTGII VNKYRGLTDI SEIIDDVIGV LPYDQNVERQ WVESTPIVKI KTKFTKEMTA LANEIASIYL EKDLASLRAL RLAKAISELT EVEKSEKDFE DYLE // ID Y412_METJA Reviewed; 267 AA. AC Q57855; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0412; GN OrderedLocusNames=MJ0412; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98401.1; -; Genomic_DNA. DR PIR; D64351; D64351. DR ProteinModelPortal; Q57855; -. DR STRING; 243232.MJ_0412; -. DR EnsemblBacteria; AAB98401; AAB98401; MJ_0412. DR KEGG; mja:MJ_0412; -. DR eggNOG; arCOG00193; Archaea. DR eggNOG; COG1116; LUCA. DR InParanoid; Q57855; -. DR KO; K02049; -. DR OMA; DIASDWR; -. DR PhylomeDB; Q57855; -. DR BioCyc; RETL1328306-WGS:GSTH-2052-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-3351-MONOMER; -. DR BioCyc; RETL1328306-WGS:GSTH-5971-MONOMER; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 267 Uncharacterized ABC transporter ATP- FT binding protein MJ0412. FT /FTId=PRO_0000093219. FT DOMAIN 17 248 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 53 60 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 267 AA; 30631 MW; 7FC75A5471AA00EA CRC64; MEKDDEVKKR DRMKVKLKVE NLTKIFEFNG NRVKALDNIN LEVYENEFLT VMGPSGCGKT TLLRIIAGLD YPTEGKVLLD GKEVKGPGAD RGVVFQQYTL MPWRTVLKNV TFGLELKGIP KNERIEIAKK FIKMVGLEGF EDAYPYQLSG GMQQRVAIAR TLANDPEIVL MDEPFAALDA QTRNILQNEL LKIWQKEKKT VFFVTHSVDE AVYLSDRVVV LTARPGRIKE IVKIDLERPR DRTSIEFLEY RKKILNILKD EVLKSLK // ID Y087_METJA Reviewed; 349 AA. AC Q57552; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Putative ABC transporter permease protein MJ0087; GN OrderedLocusNames=MJ0087; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98069.1; -; Genomic_DNA. DR PIR; G64310; G64310. DR ProteinModelPortal; Q57552; -. DR STRING; 243232.MJ_0087; -. DR EnsemblBacteria; AAB98069; AAB98069; MJ_0087. DR KEGG; mja:MJ_0087; -. DR eggNOG; arCOG01007; Archaea. DR eggNOG; COG0609; LUCA. DR InParanoid; Q57552; -. DR KO; K02015; -. DR OMA; KSTVHAG; -. DR PhylomeDB; Q57552; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 349 Putative ABC transporter permease protein FT MJ0087. FT /FTId=PRO_0000060304. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 166 186 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 254 274 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. FT TRANSMEM 318 338 Helical. {ECO:0000255}. SQ SEQUENCE 349 AA; 38201 MW; 6F43FC95F29FE870 CRC64; MDIPQKYKLY TKKKIIFGII LLITLFLSSI YALCVGDYKL TVNQVVNALM GYGKDDINLV IWNIRLPRIF AAIISGMSLA VAGAVMQCIL RNPLASPFTM GISHGAMFGA CFAIIMFGFG GAESTGRIFI NNPYMITIFA FLGALIGVVV ILLLAKLRGL TPEAMILAGV AMSSLFTAGT MLIQYFADDL QLAAMVYWTF GDLGRAIWTE IYIMAAVMIP SLIYFMYKRW DYNALEAGEE TAKSLGVNTE RTRLIGMLVA SLLTSVNVAF LGIIGFVGLI CPHIVRICIG GDYRFLIPIS ALFGAVLLLI ADTFARTIIA PIVLPVGILT SFLGAPMFLY LLLKMYKRV // ID Y1016_METJA Reviewed; 294 AA. AC Q58422; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1016; GN OrderedLocusNames=MJ1016; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99022.1; -; Genomic_DNA. DR PIR; G64426; G64426. DR ProteinModelPortal; Q58422; -. DR STRING; 243232.MJ_1016; -. DR DNASU; 1451913; -. DR EnsemblBacteria; AAB99022; AAB99022; MJ_1016. DR KEGG; mja:MJ_1016; -. DR eggNOG; arCOG00044; Archaea. DR eggNOG; COG0037; LUCA. DR InParanoid; Q58422; -. DR OMA; SICRICK; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012122; ATPase_PP-loop_MJ1016. DR InterPro; IPR018317; QueC. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF06508; QueC; 1. DR PIRSF; PIRSF036670; ATPase_UCP036670; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 294 Uncharacterized protein MJ1016. FT /FTId=PRO_0000107142. SQ SEQUENCE 294 AA; 34015 MW; 7037DB82C69CD041 CRC64; MEFSEWTKNK RKLNNLEELK RDIIEQFKEK NALDEGIVVM ASGGKDSSTA IALAKDLGLN IEYLIHFYHR WSWDVSKKMV EKLSKKFDIP VIFYNITDEL LKRTKGAKGS SICRICKNIM KDKAVDISKE KGIRIIMTGD SALEKVSGAV MNYLRDVYGE VVYNKMELTP VPQKYSKGKD KEVLFFRPLI RLACEDVLKL MDYYNIEIER AHEVGDKIGF WREGCCLQYA DENALLNEKL FNELYKYNKI ATEVAKKHGF RASIKLPSKK IMVVPKKDEY ITLIKNALRD VDES // ID Y1021_METJA Reviewed; 163 AA. AC Q58427; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ1021; GN OrderedLocusNames=MJ1021; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99025.1; -; Genomic_DNA. DR PIR; D64427; D64427. DR ProteinModelPortal; Q58427; -. DR STRING; 243232.MJ_1021; -. DR EnsemblBacteria; AAB99025; AAB99025; MJ_1021. DR KEGG; mja:MJ_1021; -. DR eggNOG; arCOG05064; Archaea. DR eggNOG; ENOG410YWMP; LUCA. DR OMA; MYNEICI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 163 Uncharacterized protein MJ1021. FT /FTId=PRO_0000107145. SQ SEQUENCE 163 AA; 19561 MW; 3D92438275C4330E CRC64; MEIERVAELI LLKDKNFKEK ERLRDLLREY IKTKDEISYL ENILEDFENL DVNLKHLKRD ADIIKSILPR LSKFTNIPVF MKIVKMLEAV EKIDTEDLES VRWNINKEIE ELNDKLKTLE NELRVIIINE ALSKIGTSNL EEFSKYLENL RYEEKNQKEE AYN // ID Y103_METJA Reviewed; 433 AA. AC Q57567; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=Uncharacterized protein MJ0103; GN OrderedLocusNames=MJ0103; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98083.1; -; Genomic_DNA. DR PIR; G64312; G64312. DR ProteinModelPortal; Q57567; -. DR STRING; 243232.MJ_0103; -. DR EnsemblBacteria; AAB98083; AAB98083; MJ_0103. DR KEGG; mja:MJ_0103; -. DR eggNOG; arCOG00951; Archaea. DR eggNOG; COG2100; LUCA. DR InParanoid; Q57567; -. DR KO; K06935; -. DR OMA; NCIFCSV; -. DR PhylomeDB; Q57567; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0061597; F:cyclic pyranopterin monophosphate synthase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR InterPro; IPR002792; TRAM_dom. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 433 Uncharacterized protein MJ0103. FT /FTId=PRO_0000171931. FT DOMAIN 370 433 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. FT REGION 171 172 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 236 238 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT METAL 118 118 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 122 122 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. FT METAL 125 125 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250}. SQ SEQUENCE 433 AA; 49866 MW; F82576531DF12142 CRC64; MVCLDLSQYR MITDVKNKDN TLILEINKIY EIEVEIPYEE VEIDGSIIKI NAHPKRAENI KVGILNLISY SIANNLKSKI TKRKTIYINE PIPLIGHTAF GLIERGRNII QVRGHCGCNL NCIFCSVDEG EFSKTRKNDY YVDLEYLIEN YKKIVDFKEN KFIEAHLDGQ GEPSLYYPLV DLVQELAEIN KKGNGIVSMQ TNGTVLNYKL IDELEEAGLH RINLSINALD EKMAKMLSGR RDYNIKKILD IAEYIKNSKI HLLIAPLLLP NINDEEFKRV IEYAVDLEQK NPQNIINPLT GKKDPILGCQ LCRVYQLGRR PKKMKVWDFE KFYYLLGKYE LEYKKKGIEV KLITSPKDFG THKRKRLPYP FKVGEVTKVK VVLDGRVKGE VLGVAKDRVI QIINCNNEQN LIGKTVKVRI LRNKDNIIVA ELV // ID Y1065_METJA Reviewed; 337 AA. AC Q58465; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ1065; GN OrderedLocusNames=MJ1065; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 AFP-like domain. {ECO:0000255|PROSITE- CC ProRule:PRU00021}. CC -!- SIMILARITY: To B.subtilis SpsE. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99068.1; -; Genomic_DNA. DR PIR; H64432; H64432. DR ProteinModelPortal; Q58465; -. DR STRING; 243232.MJ_1065; -. DR EnsemblBacteria; AAB99068; AAB99068; MJ_1065. DR KEGG; mja:MJ_1065; -. DR eggNOG; arCOG01050; Archaea. DR eggNOG; COG2089; LUCA. DR InParanoid; Q58465; -. DR KO; K01654; -. DR OMA; AYPSKIE; -. DR PhylomeDB; Q58465; -. DR BioCyc; RETL1328306-WGS:GSTH-773-MONOMER; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0016051; P:carbohydrate biosynthetic process; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR Gene3D; 3.90.1210.10; -; 1. DR InterPro; IPR006190; AFP_Neu5c_C. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR013132; Neu5Ac_N. DR InterPro; IPR013974; SAF. DR Pfam; PF03102; NeuB; 1. DR Pfam; PF08666; SAF; 1. DR SMART; SM00858; SAF; 1. DR SUPFAM; SSF51269; SSF51269; 1. DR PROSITE; PS50844; AFP_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 337 Uncharacterized protein MJ1065. FT /FTId=PRO_0000107156. FT DOMAIN 279 337 AFP-like. {ECO:0000255|PROSITE- FT ProRule:PRU00021}. SQ SEQUENCE 337 AA; 37977 MW; 790CCAFF48C1111B CRC64; MEKIKIGDRY VGKGEPTFII AEGGLNHNGD IDIGKELVKE AKKCGADAIK FQSYHTEDFI SKKSEYYELF KSLELSEEEF YELKEYAEKI GIMFISTPLD LKYVDILNKM NVPAFKIASG DLTFYPLLEK VAKTGKPVIL STGMSDIGEI WEAVKVLENN GCRDIILLHC ISSYPTPYED VNLNAIKTLK SIFNIPVGYS DHTLGILAPV VSVALGADVI EKHFTLDKNM EGPDHALSAD PEEFKEMVNN IRLVEKMLGS GEKIPMPSER DVIVEARRSI VAKRNIKKGE YLSVDNISFK RPGRGIETKY LSIILNRKIK NDKEEDDIIY WDDLLGD // ID Y1066_METJA Reviewed; 386 AA. AC Q58466; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized protein MJ1066; GN OrderedLocusNames=MJ1066; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000305}; CC -!- SIMILARITY: Belongs to the DegT/DnrJ/EryC1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99069.1; -; Genomic_DNA. DR PIR; A64433; A64433. DR ProteinModelPortal; Q58466; -. DR STRING; 243232.MJ_1066; -. DR EnsemblBacteria; AAB99069; AAB99069; MJ_1066. DR KEGG; mja:MJ_1066; -. DR eggNOG; arCOG00118; Archaea. DR eggNOG; COG0399; LUCA. DR InParanoid; Q58466; -. DR OMA; RANPVID; -. DR PhylomeDB; Q58466; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000653; DegT/StrS_aminotransferase. DR InterPro; IPR020026; PseC. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF01041; DegT_DnrJ_EryC1; 1. DR PIRSF; PIRSF000390; PLP_StrS; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03588; PseC; 1. PE 3: Inferred from homology; KW Complete proteome; Pyridoxal phosphate; Reference proteome. FT CHAIN 1 386 Uncharacterized protein MJ1066. FT /FTId=PRO_0000110032. FT MOD_RES 185 185 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 386 AA; 44501 MW; FE8F43C8D50CCB80 CRC64; MIRESFLPPF RPCIGEEEIN EVIDTLKSDW ITMGPKTLKF EELFRNYIGS KFAISLNSCT AGLHLSLVAL NIKDKDEVIT TPYTFAATGN VIVHQRAKPV FVDIDKETYN INVEEIENAI TERTKAIIPV HYAGHPCEMD EILKIARDYD LYVIEDAAHA LGAEYKGKKI GTIGDTTSFS FYATKNITTG EGGMVTTDNE EIAEKIKILR LHGISRDAWK RYSSEGSWYY EIIECGYKYN MTDIQASIGI HQLKKAEIMR KRREEIAKIY NEEFENLEGL ITPTIKKHVK HAWHLYPLLI NIDRLKINRT KFIEELKKQN IGTSVHFIPL HLHPFYRKTF GYKKGDFPNA EWVYEREISL PIYPKMTDDD VIDVVNAVKK IVSENR // ID Y1076_METJA Reviewed; 337 AA. AC Q58476; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Uncharacterized ATP-binding protein MJ1076; GN OrderedLocusNames=MJ1076; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99081.1; -; Genomic_DNA. DR PIR; C64434; C64434. DR ProteinModelPortal; Q58476; -. DR STRING; 243232.MJ_1076; -. DR EnsemblBacteria; AAB99081; AAB99081; MJ_1076. DR KEGG; mja:MJ_1076; -. DR eggNOG; ENOG4102U6X; Archaea. DR eggNOG; ENOG410Z1ZF; LUCA. DR InParanoid; Q58476; -. DR KO; K06921; -. DR OMA; RWINIEA; -. DR PhylomeDB; Q58476; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 337 Uncharacterized ATP-binding protein FT MJ1076. FT /FTId=PRO_0000184674. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 337 AA; 40093 MW; D83CAF90FA432B81 CRC64; MRFYNREKEL NYLKNYVQLE PNSILFVYGP KSSGKSTVMM RVIKELENSN IVFFYYNLRK YATPTKDEFL SIFFEKSDKK YLLNKLEINL KIFKFGIEEN FDFNNIKLND VFAKINESIN TVIKDGKRPV LVIDELQKLK NIYFNSGKSL LNELFNLFVS LTKMEHLCHV ICLTSDTLFI DNVYRNSSLS EASEYYLIDW LKKDDIKKIL KEEGFNKKEI DYCLNYLSLP YEISQLINNK KLGLSVEETI KRWINIEADG IKYLIDTSDL NEEEIYKVLS KFKDKIKINY KKDVKKEEMK YIKFLIENEI LFYDVINGII KPTSVKKWYA IKEILDK // ID Y1107_METJA Reviewed; 149 AA. AC Q58507; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1107; GN OrderedLocusNames=MJ1107; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99111.1; -; Genomic_DNA. DR PIR; B64438; B64438. DR ProteinModelPortal; Q58507; -. DR STRING; 243232.MJ_1107; -. DR PRIDE; Q58507; -. DR EnsemblBacteria; AAB99111; AAB99111; MJ_1107. DR KEGG; mja:MJ_1107; -. DR eggNOG; arCOG09652; Archaea. DR eggNOG; ENOG4110ZR7; LUCA. DR OMA; FEEQKPV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 149 Uncharacterized protein MJ1107. FT /FTId=PRO_0000107171. FT TRANSMEM 124 144 Helical. {ECO:0000255}. SQ SEQUENCE 149 AA; 17603 MW; 7DC7EC894464EF50 CRC64; MKFFVVFVMA VAYSKLYELI KNVKDEKEAE ELCKIIEEFF EKQCKENVSK KFEEQKPVLK LELKEELRKE LTTKEDLELI GEKILRYVDN KINQVIEKIN QLDKKIDEGF YQLDKKVDTL KRDIIIIALI IILANYAPSI IGKILSFLK // ID Y1181_METJA Reviewed; 199 AA. AC Q58581; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ1181; GN OrderedLocusNames=MJ1181; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99189.1; -; Genomic_DNA. DR PIR; D64447; D64447. DR ProteinModelPortal; Q58581; -. DR STRING; 243232.MJ_1181; -. DR EnsemblBacteria; AAB99189; AAB99189; MJ_1181. DR KEGG; mja:MJ_1181; -. DR eggNOG; arCOG01803; Archaea. DR eggNOG; COG0715; LUCA. DR KO; K02051; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 199 Uncharacterized protein MJ1181. FT /FTId=PRO_0000107204. SQ SEQUENCE 199 AA; 22093 MW; 699D1EBEDE274AB2 CRC64; MIEDALKAEG ITYTEDPNNK SAMVLLVNCK GQGTMPQMLA QKQLDAVIAW EPMPEIIKNK GIGKVIAHSE DLPSATGGTW ANHPCCCLAA SENALKNKRE AVITFAKLLK DATDEINKNR DLAVKASVRW LGTNENVEKD SIEHIKFDYR LEPVIPKVIK FVEAMKLQGL INGKLKDASS EEVKDIIFDL QTYNEIINN // ID Y1187_METJA Reviewed; 301 AA. AC Q58588; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized protein MJ1187; DE EC=3.2.2.-; GN OrderedLocusNames=MJ1187; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ADP-ribosylglycohydrolase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99191.1; -; Genomic_DNA. DR PIR; C64448; C64448. DR PDB; 1T5J; X-ray; 2.70 A; A=2-301. DR PDBsum; 1T5J; -. DR ProteinModelPortal; Q58588; -. DR SMR; Q58588; 1-301. DR STRING; 243232.MJ_1187; -. DR EnsemblBacteria; AAB99191; AAB99191; MJ_1187. DR KEGG; mja:MJ_1187; -. DR eggNOG; arCOG04448; Archaea. DR eggNOG; COG1397; LUCA. DR InParanoid; Q58588; -. DR OMA; NDEAIAG; -. DR PhylomeDB; Q58588; -. DR EvolutionaryTrace; Q58588; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR InterPro; IPR005502; Ribosyl_crysJ1. DR Pfam; PF03747; ADP_ribosyl_GH; 1. DR SUPFAM; SSF101478; SSF101478; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 301 Uncharacterized protein MJ1187. FT /FTId=PRO_0000157289. FT HELIX 2 22 {ECO:0000244|PDB:1T5J}. FT HELIX 23 25 {ECO:0000244|PDB:1T5J}. FT HELIX 30 36 {ECO:0000244|PDB:1T5J}. FT TURN 49 53 {ECO:0000244|PDB:1T5J}. FT HELIX 61 71 {ECO:0000244|PDB:1T5J}. FT HELIX 80 91 {ECO:0000244|PDB:1T5J}. FT HELIX 100 108 {ECO:0000244|PDB:1T5J}. FT TURN 109 112 {ECO:0000244|PDB:1T5J}. FT TURN 122 124 {ECO:0000244|PDB:1T5J}. FT HELIX 125 127 {ECO:0000244|PDB:1T5J}. FT HELIX 129 134 {ECO:0000244|PDB:1T5J}. FT HELIX 139 151 {ECO:0000244|PDB:1T5J}. FT HELIX 157 174 {ECO:0000244|PDB:1T5J}. FT HELIX 181 190 {ECO:0000244|PDB:1T5J}. FT TURN 191 193 {ECO:0000244|PDB:1T5J}. FT HELIX 195 201 {ECO:0000244|PDB:1T5J}. FT HELIX 202 206 {ECO:0000244|PDB:1T5J}. FT HELIX 210 217 {ECO:0000244|PDB:1T5J}. FT STRAND 220 222 {ECO:0000244|PDB:1T5J}. FT HELIX 223 236 {ECO:0000244|PDB:1T5J}. FT HELIX 240 248 {ECO:0000244|PDB:1T5J}. FT HELIX 254 269 {ECO:0000244|PDB:1T5J}. FT HELIX 271 273 {ECO:0000244|PDB:1T5J}. FT HELIX 276 280 {ECO:0000244|PDB:1T5J}. FT HELIX 285 299 {ECO:0000244|PDB:1T5J}. SQ SEQUENCE 301 AA; 33568 MW; 525E5CE4D369C201 CRC64; MVKMRDKILG SVFGAVIGDA LGMPTENLTK EEIKKLYGFV DSYVEPKNYL AGKLNKGEWT DDTEQAICLI KSLTKEGIDI KKFANCLIAW KNKNPPDIGL TSLMAIDKLE NNDYSGVDSS SCGAAMRIYP LGIVFHNNLK KLKEEVIKAS KITHNNKTAI AGALAIAFFV SSALKDRKDF SLLDECYNYI KDIDEEFAKK LLEIKNFNNL DYIYDYFGTG VKTDEVVPSA IATYLLTDNF KEGMLKCINA GGDTDSLASM YGAMAGAYYG FKNIPKEWID GLKNKEVIFE LAERLYHLAT E // ID Y1211_METJA Reviewed; 116 AA. AC Q58608; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ1211; GN OrderedLocusNames=MJ1211; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99222.1; -; Genomic_DNA. DR PIR; B64451; B64451. DR ProteinModelPortal; Q58608; -. DR STRING; 243232.MJ_1211; -. DR EnsemblBacteria; AAB99222; AAB99222; MJ_1211. DR KEGG; mja:MJ_1211; -. DR eggNOG; arCOG01182; Archaea. DR eggNOG; COG2112; LUCA. DR KO; K07176; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 116 Uncharacterized protein MJ1211. FT /FTId=PRO_0000107215. SQ SEQUENCE 116 AA; 13422 MW; 0EA661BCFC5EAA7C CRC64; MEFIDGEELK SAVDKLDKDR LLKVVEDILK ITLKLDILGI EHKEIQGGRH FLITNKKTYI IDFDKAKEKK TTKNFTGAIA LLFGEGRIAK TIRENLNIGI DEIKFIREFA KKYKKL // ID Y1213_METJA Reviewed; 110 AA. AC Q58610; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1213; GN OrderedLocusNames=MJ1213; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0123 and A.aeolicus AA15. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99223.1; -; Genomic_DNA. DR PIR; D64451; D64451. DR PDB; 4QHF; X-ray; 2.10 A; A=1-110. DR PDB; 4QHG; X-ray; 2.20 A; A=1-110. DR PDB; 4QHH; X-ray; 3.00 A; A=1-110. DR PDB; 4QHI; X-ray; 2.30 A; A/B/C/D=1-110. DR PDB; 4QHJ; X-ray; 1.75 A; A/B=1-110. DR PDBsum; 4QHF; -. DR PDBsum; 4QHG; -. DR PDBsum; 4QHH; -. DR PDBsum; 4QHI; -. DR PDBsum; 4QHJ; -. DR STRING; 243232.MJ_1213; -. DR EnsemblBacteria; AAB99223; AAB99223; MJ_1213. DR KEGG; mja:MJ_1213; -. DR eggNOG; arCOG09626; Archaea. DR eggNOG; COG1451; LUCA. DR InParanoid; Q58610; -. DR KO; K07043; -. DR OMA; KYHINEF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008756; Peptidase_M56. DR Pfam; PF05569; Peptidase_M56; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 110 Uncharacterized protein MJ1213. FT /FTId=PRO_0000107216. FT HELIX 4 17 {ECO:0000244|PDB:4QHJ}. FT HELIX 21 23 {ECO:0000244|PDB:4QHJ}. FT TURN 24 26 {ECO:0000244|PDB:4QHJ}. FT STRAND 28 32 {ECO:0000244|PDB:4QHJ}. FT STRAND 38 42 {ECO:0000244|PDB:4QHJ}. FT TURN 43 46 {ECO:0000244|PDB:4QHJ}. FT STRAND 47 51 {ECO:0000244|PDB:4QHJ}. FT TURN 52 54 {ECO:0000244|PDB:4QHJ}. FT HELIX 55 57 {ECO:0000244|PDB:4QHJ}. FT HELIX 60 76 {ECO:0000244|PDB:4QHJ}. FT HELIX 78 80 {ECO:0000244|PDB:4QHG}. FT HELIX 82 91 {ECO:0000244|PDB:4QHJ}. FT HELIX 95 106 {ECO:0000244|PDB:4QHJ}. SQ SEQUENCE 110 AA; 13080 MW; D94E9F492B28F24B CRC64; MKDRKILNEI LSNTINELNL NDKKANIKIK IKPLKRKIAS ISLTNKTIYI NKNILPYLSD EEIRFILAHE LLHLKYGKYH INEFEEELLF LFPNKEAILI NLINKLHQKK // ID Y1214_METJA Reviewed; 1018 AA. AC Q58611; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MJ1214; GN OrderedLocusNames=MJ1214; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99215.1; -; Genomic_DNA. DR PIR; E64451; E64451. DR ProteinModelPortal; Q58611; -. DR STRING; 243232.MJ_1214; -. DR REBASE; 3903; MjaORF1220P. DR EnsemblBacteria; AAB99215; AAB99215; MJ_1214. DR KEGG; mja:MJ_1214; -. DR eggNOG; arCOG00878; Archaea. DR eggNOG; COG0610; LUCA. DR InParanoid; Q58611; -. DR KO; K01153; -. DR OMA; QINRYER; -. DR PhylomeDB; Q58611; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:InterPro. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR. DR Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 3. DR TIGRFAMs; TIGR00348; hsdR; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 1018 Uncharacterized protein MJ1214. FT /FTId=PRO_0000107217. SQ SEQUENCE 1018 AA; 120993 MW; 97D383541BE128E2 CRC64; MNKMPIPEIY VHNDIEENLN KLGWKELEGY EGEAFSNYII KPILEEQLKI INDHIGEYKD EFIEKAINKL INEPKPEEIL DYIKNGILIT LDKGRKGQVS NRVKLIDYKN IEKNIFNYAH ELKFKGNDNI IPDFTLFING IPIIIIEAKR EFSEKETYEE AINQINRYER EAPKLFNYVQ FAIVYGDEKL YIPTYPNEEK EDRFKKPYKW KNEKKEEDIW DLLKRERVLD TIKNFIFFSK DRAGRKTKII PRYMQYWAVK KAYERITNYL NNKDYKNRGL VWHWQGSGKT FEILYLAELF YNEFKNKDPI VFIMVDRREL ETQFNDDIIA LQNANFKDCF KKINSVEELK GVLEDIKESE NNPNISEKGV YLVMMHKFDK NKLKDFIESF GSIDKKEILI LRDEAHRTES GKFATLRNKI LKNAIAIGFT GTPVHKKDMS TFKEYAYPQE GEFYLDRFFI EESIKEGFTL PLIWRVVKPE DIKDISEEEI KNIIEKLFVD EEDADKIVVS KKEIAEKIKL SDLLKSESSI KEASKYIAEH ILEDTENFKF KAMVVAQDRK SCILFKKYLD EYLKEKIKNY NENWTQVVIT YIHNDDVEIE NYKKEIEKKY GKNVDELNKK WTEDFINKEN PKILIVNKKL LTGFDAPILK TIYIHQFLKD YLLLQASARA NRPAKNKKYG LIVDLTGILI ENYKKAIENY NLYRDEAINK DILNNLFVET SKIWESFLTK LNEFKELFKL IVGIEFDDFI VNLKKQKNSK EFKKIISKII LSDKFDYFYA KLRELIQLFE AVGAYGEKLN YYETYEWLKI ISAGINKQMR PKSYKIPYNQ IKKEVIKYLE FDTYADIAST SINPQLLENL KNKDEINVIV ADMIYYALDT LQNKKEPIYR MIYDRINELK NAYISKTKKN EYVINELINC LNALKTYEEE EKTLSKSEKA IKNMLFYLKN VENCNIKKLP LTEKTLKNLE DKKLIKPSDF DKIKKFLFVD LKNAIKETEK RRKVSNKIVE EIIKPIFI // ID Y1222_METJA Reviewed; 243 AA. AC Q58619; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Uncharacterized protein MJ1222; GN OrderedLocusNames=MJ1222; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99226.1; -; Genomic_DNA. DR PIR; E64452; E64452. DR ProteinModelPortal; Q58619; -. DR STRING; 243232.MJ_1222; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB99226; AAB99226; MJ_1222. DR KEGG; mja:MJ_1222; -. DR eggNOG; arCOG00895; Archaea. DR eggNOG; COG0463; LUCA. DR InParanoid; Q58619; -. DR OMA; RYEVSSE; -. DR PhylomeDB; Q58619; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 243 Uncharacterized protein MJ1222. FT /FTId=PRO_0000107223. SQ SEQUENCE 243 AA; 27428 MW; 23BE405026EA5A44 CRC64; MEIMKKQNSQ INEINKDEIF VVVPAFNEEK MIGETLKNLK KEGYKNIVVV DDGSMDKTSE IAKKEGVIVC RHILNRGLGG ALGTGIKCAL LYKPKIIITF DADGQHHPKD VEKVVKPVLF EGYDMAIGSR MMDKNELKNM PLVKRIGNFG LNFITYLMGG YFVTDSQSGL RAFSYEAAKK IIGDLKSDRY EVSSEFIILA KKHGLKLKEV PIKTIYTEYS MSRGTNVITG FKILFKLIMQ KIF // ID Y1224_METJA Reviewed; 139 AA. AC Q58621; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=UPF0216 protein MJ1224 {ECO:0000255|HAMAP-Rule:MF_00585}; GN OrderedLocusNames=MJ1224; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0216 family. {ECO:0000255|HAMAP- CC Rule:MF_00585}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99227.1; -; Genomic_DNA. DR PIR; G64452; G64452. DR STRING; 243232.MJ_1224; -. DR EnsemblBacteria; AAB99227; AAB99227; MJ_1224. DR KEGG; mja:MJ_1224; -. DR eggNOG; arCOG01921; Archaea. DR eggNOG; COG2083; LUCA. DR InParanoid; Q58621; -. DR KO; K09737; -. DR OMA; LHNLKSN; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00585; UPF0216; 1. DR InterPro; IPR002746; UPF0216. DR Pfam; PF01886; DUF61; 1. DR PIRSF; PIRSF005264; UCP005264; 1. DR ProDom; PD016056; DUF61; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 139 UPF0216 protein MJ1224. FT /FTId=PRO_0000144224. SQ SEQUENCE 139 AA; 16202 MW; 6FB6D0CCC31F00E3 CRC64; MIILVMSMRD VEKIIKGIIK DMNPRFKRKT LRELLSEEKP HVIINGKRHR IKRRELEFLK EIASEDLKIP IVLEVDSSLG GAIKISGKEE VKVISKILGK EIDIFSEKDV MYIYKPELKI VRKELPTTTQ LIFKLSLFD // ID Y1225_METJA Reviewed; 280 AA. AC Q58622; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1225; GN OrderedLocusNames=MJ1225; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 4 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99228.1; -; Genomic_DNA. DR PIR; H64452; H64452. DR PDB; 3KH5; X-ray; 2.10 A; A=1-280. DR PDB; 3LFZ; X-ray; 2.20 A; A=1-280. DR PDBsum; 3KH5; -. DR PDBsum; 3LFZ; -. DR ProteinModelPortal; Q58622; -. DR STRING; 243232.MJ_1225; -. DR EnsemblBacteria; AAB99228; AAB99228; MJ_1225. DR KEGG; mja:MJ_1225; -. DR eggNOG; arCOG00600; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q58622; -. DR OMA; KDVARTM; -. DR PhylomeDB; Q58622; -. DR EvolutionaryTrace; Q58622; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 4. DR SMART; SM00116; CBS; 4. DR PROSITE; PS51371; CBS; 4. PE 1: Evidence at protein level; KW 3D-structure; CBS domain; Complete proteome; Reference proteome; KW Repeat. FT CHAIN 1 280 Uncharacterized protein MJ1225. FT /FTId=PRO_0000107226. FT DOMAIN 10 67 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 90 146 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 154 209 CBS 3. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 229 280 CBS 4. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT HELIX 5 7 {ECO:0000244|PDB:3KH5}. FT HELIX 23 33 {ECO:0000244|PDB:3KH5}. FT STRAND 37 41 {ECO:0000244|PDB:3KH5}. FT TURN 43 45 {ECO:0000244|PDB:3KH5}. FT STRAND 47 53 {ECO:0000244|PDB:3KH5}. FT HELIX 54 60 {ECO:0000244|PDB:3KH5}. FT TURN 61 63 {ECO:0000244|PDB:3KH5}. FT HELIX 65 67 {ECO:0000244|PDB:3KH5}. FT HELIX 68 71 {ECO:0000244|PDB:3KH5}. FT TURN 72 76 {ECO:0000244|PDB:3LFZ}. FT HELIX 78 81 {ECO:0000244|PDB:3KH5}. FT HELIX 86 88 {ECO:0000244|PDB:3KH5}. FT HELIX 103 112 {ECO:0000244|PDB:3KH5}. FT STRAND 116 121 {ECO:0000244|PDB:3KH5}. FT STRAND 126 132 {ECO:0000244|PDB:3KH5}. FT HELIX 133 140 {ECO:0000244|PDB:3KH5}. FT HELIX 141 143 {ECO:0000244|PDB:3KH5}. FT HELIX 151 153 {ECO:0000244|PDB:3KH5}. FT HELIX 167 177 {ECO:0000244|PDB:3KH5}. FT STRAND 180 186 {ECO:0000244|PDB:3KH5}. FT STRAND 189 195 {ECO:0000244|PDB:3KH5}. FT HELIX 196 203 {ECO:0000244|PDB:3KH5}. FT HELIX 206 213 {ECO:0000244|PDB:3KH5}. FT HELIX 218 222 {ECO:0000244|PDB:3KH5}. FT HELIX 225 228 {ECO:0000244|PDB:3KH5}. FT STRAND 229 232 {ECO:0000244|PDB:3KH5}. FT HELIX 242 251 {ECO:0000244|PDB:3KH5}. FT STRAND 256 260 {ECO:0000244|PDB:3KH5}. FT STRAND 265 271 {ECO:0000244|PDB:3KH5}. FT HELIX 272 275 {ECO:0000244|PDB:3KH5}. FT HELIX 276 279 {ECO:0000244|PDB:3KH5}. SQ SEQUENCE 280 AA; 31719 MW; 614AE160DC92E45F CRC64; MFVRVMKIAQ NKKIVTVYPT TTIRKALMTM NENKYRRLPV VNAGNNKVVG IITSMDIVDF MGGGSKYNLI REKHERNFLA AINEPVREIM EENVITLKEN ADIDEAIETF LTKNVGGAPI VNDENQLISL ITERDVIRAL LDKIDENEVI DDYITRDVIV ATPGERLKDV ARTMVRNGFR RLPVVSEGRL VGIITSTDFI KLLGSDWAFN HMQTGNVREI TNVRMEEIMK RDVITAKEGD KLKKIAEIMV TNDIGALPVV DENLRIKGII TEKDVLKYFA // ID Y1244_METJA Reviewed; 108 AA. AC Q58641; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ1244; GN OrderedLocusNames=MJ1244; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1245 and M.thermoautotrophicum CC MTH1110. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99249.1; -; Genomic_DNA. DR PIR; C64455; C64455. DR STRING; 243232.MJ_1244; -. DR EnsemblBacteria; AAB99249; AAB99249; MJ_1244. DR KEGG; mja:MJ_1244; -. DR eggNOG; arCOG03424; Archaea. DR eggNOG; COG4075; LUCA. DR OMA; KYTIIEI; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR024184; UCP005637. DR InterPro; IPR019296; Unchr_N-regulatory-PII-rel. DR Pfam; PF10126; Nit_Regul_Hom; 1. DR PIRSF; PIRSF005637; UCP005637; 1. DR SUPFAM; SSF54913; SSF54913; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 108 Uncharacterized protein MJ1244. FT /FTId=PRO_0000107235. SQ SEQUENCE 108 AA; 12029 MW; 098F29966DB174A0 CRC64; MKILLYLFVE SENVGKAINA LSEGGITGFF LYDYKGMSPQ DWQGFLLDED PEMAIKAVSD LAQNAVLIGT IVSENKLMEI EKLIDEKLAD CKYTIIEIPI EGIIVNMP // ID Y1278_METJA Reviewed; 179 AA. AC Q58674; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ1278; GN OrderedLocusNames=MJ1278; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99284.1; -; Genomic_DNA. DR PIR; E64459; E64459. DR ProteinModelPortal; Q58674; -. DR STRING; 243232.MJ_1278; -. DR EnsemblBacteria; AAB99284; AAB99284; MJ_1278. DR KEGG; mja:MJ_1278; -. DR eggNOG; arCOG10917; Archaea. DR eggNOG; ENOG41110MD; LUCA. DR OMA; HILRITV; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Coiled coil; Complete proteome; Reference proteome. FT CHAIN 1 179 Uncharacterized protein MJ1278. FT /FTId=PRO_0000107246. FT COILED 139 172 {ECO:0000255}. SQ SEQUENCE 179 AA; 20662 MW; CBC0BA276E7EC1A0 CRC64; MGIFDLAKKI THSREYTKSI DEIFVGELIN FMYKNGAVLT EINSPTESSH SLTFKFVNHP VLHILRITVD RKIEGMASKI LGSQSVLTFE AVIKNDLVEP NDVLVMYQTD FKNMFKIPIF GKVKINHDLN YIIATTTYIE DLGKYIKSDR IEKEALREEL EKILNTLVKH LEPLKKKFD // ID Y1282_METJA Reviewed; 352 AA. AC Q58678; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=UPF0252 protein MJ1282; GN OrderedLocusNames=MJ1282; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0252 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99291.1; -; Genomic_DNA. DR PIR; A64460; A64460. DR ProteinModelPortal; Q58678; -. DR DNASU; 1452180; -. DR EnsemblBacteria; AAB99291; AAB99291; MJ_1282. DR KEGG; mja:MJ_1282; -. DR eggNOG; arCOG02164; Archaea. DR eggNOG; COG1800; LUCA. DR KO; K07111; -. DR OMA; CLDYATL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR022651; S_layer_C. DR InterPro; IPR007562; Transglutaminase-like_domain. DR Pfam; PF04473; DUF553; 1. DR Pfam; PF05124; S_layer_C; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 352 UPF0252 protein MJ1282. FT /FTId=PRO_0000159555. SQ SEQUENCE 352 AA; 40310 MW; 41FF73286AB1FFA8 CRC64; MRKIILIFFI FLILQNIYAY EKIYDVNHVC YYTLTSVELQ KFVKTAEIIT PLNADNKTTI TKDTILVGNP EENPLTKKYI GFFKIKINKT FPGKNKGIIE KQIINGHTVI LLAGSDIQGT YASIITFANL NDIPENPIIC ETSNKVNIYS TSLNSEYFRD FIEKNILTPK EIEKVKSLSY KLKGKDKKAT IENIAKWVAN NIKYDYDKCK KIESGKFSWD EYNTPSETVK TKKGVCLDYA TLTSALLLND NIIPYMLDVA LYNTSSLKIS SYHASVAVKI DNTYFVIDQQ PYLIPINEYT AQTFEDNLRI ASIVMFRVVK ERDGIKLIKE KEVPGIAIYG DLINLLEMRF NN // ID Y1283_METJA Reviewed; 220 AA. AC Q58679; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1283; GN OrderedLocusNames=MJ1283; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99292.1; -; Genomic_DNA. DR PIR; B64460; B64460. DR ProteinModelPortal; Q58679; -. DR STRING; 243232.MJ_1283; -. DR EnsemblBacteria; AAB99292; AAB99292; MJ_1283. DR KEGG; mja:MJ_1283; -. DR eggNOG; arCOG08268; Archaea. DR eggNOG; ENOG411100Z; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 220 Uncharacterized protein MJ1283. FT /FTId=PRO_0000107252. FT TRANSMEM 10 30 Helical. {ECO:0000255}. SQ SEQUENCE 220 AA; 25277 MW; 037E6FD391C703B9 CRC64; MVEMNKRGQF FIIGGVILSI GLILFFLLGF NSYTSDGSYL TVFKMKDVKN SIESCLINSL TSNSNLSKNL DMLKNNYKDE GIEINYKKII FSNIRYEAKN LTFNFSLYNG NFSYNISNYG FGGAFNGSLN VSNYVFSKNL LLNISENGSV TGSFNITGSY VNVFVYDRFG NLILNETIYN NSNEKSLYYY ILNVSKEGIL LYLLWQRMFL TTHWQKMYPL // ID Y1311_METJA Reviewed; 293 AA. AC Q58707; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Uncharacterized protein MJ1311; GN OrderedLocusNames=MJ1311; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1614 and MJ0008. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99318.1; -; Genomic_DNA. DR PIR; F64463; F64463. DR PDB; 3WQO; X-ray; 2.64 A; A/B=1-293. DR PDBsum; 3WQO; -. DR ProteinModelPortal; Q58707; -. DR STRING; 243232.MJ_1311; -. DR DNASU; 1452213; -. DR EnsemblBacteria; AAB99318; AAB99318; MJ_1311. DR KEGG; mja:MJ_1311; -. DR eggNOG; arCOG01895; Archaea. DR eggNOG; COG1082; LUCA. DR InParanoid; Q58707; -. DR OMA; CCEIIYE; -. DR PhylomeDB; Q58707; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 293 Uncharacterized protein MJ1311. FT /FTId=PRO_0000107269. FT STRAND 18 22 {ECO:0000244|PDB:3WQO}. FT HELIX 23 25 {ECO:0000244|PDB:3WQO}. FT TURN 26 28 {ECO:0000244|PDB:3WQO}. FT HELIX 31 39 {ECO:0000244|PDB:3WQO}. FT STRAND 44 49 {ECO:0000244|PDB:3WQO}. FT HELIX 52 54 {ECO:0000244|PDB:3WQO}. FT HELIX 58 70 {ECO:0000244|PDB:3WQO}. FT STRAND 74 78 {ECO:0000244|PDB:3WQO}. FT HELIX 91 110 {ECO:0000244|PDB:3WQO}. FT STRAND 114 118 {ECO:0000244|PDB:3WQO}. FT HELIX 125 127 {ECO:0000244|PDB:3WQO}. FT HELIX 131 152 {ECO:0000244|PDB:3WQO}. FT STRAND 155 159 {ECO:0000244|PDB:3WQO}. FT HELIX 172 179 {ECO:0000244|PDB:3WQO}. FT STRAND 187 192 {ECO:0000244|PDB:3WQO}. FT HELIX 193 199 {ECO:0000244|PDB:3WQO}. FT HELIX 202 204 {ECO:0000244|PDB:3WQO}. FT HELIX 205 209 {ECO:0000244|PDB:3WQO}. FT STRAND 216 221 {ECO:0000244|PDB:3WQO}. FT STRAND 225 228 {ECO:0000244|PDB:3WQO}. FT STRAND 236 238 {ECO:0000244|PDB:3WQO}. FT HELIX 241 250 {ECO:0000244|PDB:3WQO}. FT STRAND 255 259 {ECO:0000244|PDB:3WQO}. FT HELIX 264 284 {ECO:0000244|PDB:3WQO}. SQ SEQUENCE 293 AA; 33260 MW; 0B30E5A286CE38F3 CRC64; MKRKTKLDKK SKWVLDMKFG VSSLVFLPES LTSSMEKIAE HNFDAWEIVC EGTHYLSPKN IKYLMELRDR YEVEIVVHAP FSDLNPASMN ERVRKLTVEC IRDAIEGAFE LDSEVVVVHP GYIPELWSNY VSEILDNNFS TLSEIVEIAE DYGIKIGLEN MPNFRGVLGI TPESLLEIVK DIDSKNLGIT FDIGHANTAG NPAEFVEKLQ NIGIGIIHVH AHDNNGYDDE HLKIGEGNIN FIEVLEKLKE IGYDGVISIE NKNIRDAVKS KEILKEYLEI VNEKVAEKEK IEE // ID Y1312_METJA Reviewed; 321 AA. AC Q58708; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=UPF0026 protein MJ1312; GN OrderedLocusNames=MJ1312; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC -!- SIMILARITY: Belongs to the UPF0026 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99319.1; -; Genomic_DNA. DR PIR; G64463; G64463. DR ProteinModelPortal; Q58708; -. DR STRING; 243232.MJ_1312; -. DR DNASU; 1452214; -. DR EnsemblBacteria; AAB99319; AAB99319; MJ_1312. DR KEGG; mja:MJ_1312; -. DR eggNOG; arCOG00953; Archaea. DR eggNOG; COG0731; LUCA. DR InParanoid; Q58708; -. DR OMA; IYCQLGR; -. DR PhylomeDB; Q58708; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 321 UPF0026 protein MJ1312. FT /FTId=PRO_0000217863. FT METAL 27 27 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 31 31 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 34 34 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 321 AA; 37131 MW; 0035C4E648DA607F CRC64; MTIAFGPVPS RRLGKSLGIN SIPCKFCSYD CVYCQVGRTI NKTIERREFY SPEDIFKSVE ERIGKLNNEK IDYLTFVADG EPTLDINLSK EVEMLRDFDI PIAIITNSSL IWREDVRNDI LNFDLVSFKV DSVDEKIWRE INRPHKDLVL DKILEGMIAF RDNYKGELIT ETMILGSIKY TEESIIKTAE FLKELNPNKC YLNTPIRPPS EKYIKPPKIE VITKILAIFN EIIGKNKIKL LGKFEGNEFI FSENVEEDIL AITSVHPMRE EVIKELLNKS NISFDIINKM VNEGKLIKLE YDGKVFYMKN IKSRDKNVSN P // ID Y1339_METJA Reviewed; 154 AA. AC Q58735; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein MJ1339; GN OrderedLocusNames=MJ1339; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain. CC {ECO:0000305}. CC -!- SIMILARITY: To M.thermoautotrophicum MTH765. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99349.1; -; Genomic_DNA. DR PIR; B64467; B64467. DR ProteinModelPortal; Q58735; -. DR STRING; 243232.MJ_1339; -. DR EnsemblBacteria; AAB99349; AAB99349; MJ_1339. DR KEGG; mja:MJ_1339; -. DR eggNOG; arCOG00362; Archaea. DR eggNOG; COG2229; LUCA. DR InParanoid; Q58735; -. DR KO; K06945; -. DR OMA; KRFEFMR; -. DR PhylomeDB; Q58735; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR InterPro; IPR016433; Small_GTPase_MJ1339. DR PIRSF; PIRSF004882; GTP_bind_MJ1339_prd; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 154 Uncharacterized protein MJ1339. FT /FTId=PRO_0000107282. FT DOMAIN 17 112 G. FT NP_BIND 12 19 GTP. {ECO:0000255}. SQ SEQUENCE 154 AA; 17196 MW; 94626C30C181107A CRC64; MKKDEVKVVV IGSSDVGKTT LMENLIDKIG KVEYKGITTA IDYGSLTIKD KKIHFFGTPG QKRFEFMREL ALKGTNFALV VLDASKGITK EDEEIIKLLE SKKIPYGIFI NKTDVGDIDT SEVYNFCNPK FIVKGCAVKK DGLDELINKI MSHT // ID Y1363_METJA Reviewed; 151 AA. AC Q58758; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized protein MJ1363; GN OrderedLocusNames=MJ1363; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99371.1; -; Genomic_DNA. DR PIR; B64470; B64470. DR ProteinModelPortal; Q58758; -. DR STRING; 243232.MJ_1363; -. DR EnsemblBacteria; AAB99371; AAB99371; MJ_1363. DR KEGG; mja:MJ_1363; -. DR eggNOG; arCOG01553; Archaea. DR eggNOG; COG3260; LUCA. DR InParanoid; Q58758; -. DR KO; K14122; -. DR OMA; NAIFSPF; -. DR PhylomeDB; Q58758; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:InterPro. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR Pfam; PF01058; Oxidored_q6; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 151 Uncharacterized protein MJ1363. FT /FTId=PRO_0000118784. FT METAL 24 24 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 27 27 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 92 92 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 129 129 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 151 AA; 16168 MW; 8A2910BB696F5F21 CRC64; MTVMIKKIAR KKCIHVMLVY TGGCNACDIE VVNAIFSPFY DAEQYNVFLT FNPREADILV VTGCVTKVVA ESLRKIYEKI PEPKAVVAVG ACALMGGVYK NIGGDLGTSD FVAGPVENII PVDVKVPGCA PRPEDIIAGI VKALPKVIEG K // ID Y1394_METJA Reviewed; 987 AA. AC Q58789; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1394; GN OrderedLocusNames=MJ1394; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1393 and A.fulgidus AF2028. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99404.1; -; Genomic_DNA. DR PIR; A64474; A64474. DR ProteinModelPortal; Q58789; -. DR STRING; 243232.MJ_1394; -. DR EnsemblBacteria; AAB99404; AAB99404; MJ_1394. DR KEGG; mja:MJ_1394; -. DR eggNOG; arCOG06147; Archaea. DR eggNOG; COG5306; LUCA. DR InParanoid; Q58789; -. DR OMA; DENFNGY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 987 Uncharacterized protein MJ1394. FT /FTId=PRO_0000107308. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 958 978 Helical. {ECO:0000255}. SQ SEQUENCE 987 AA; 112360 MW; D1E628FFB28CA86D CRC64; MMWGMPNIKL KFIYLCILLF VFMASMLNSV SGLKTIFYDD FENWSGWYNY SSGAVEQSSN YAHSGIYSLR KFLNDDPNGG YKLIGKEIGR DIVMEGWIYR PLPYVSGRWD RIGIEDENFN GYSIRIEHDY NKIAIETREN GIAVNTLVIT NWNPPENQWY YFKFYIYSNG TLRLEVYYEN GSLGATVSAI DNIYTKFDRV VVHGGQDYYV DDLRISDLYP PLRVRYIEEY NATATVDGTG KTNYSYGLTG HIIIENTAPY KEDTLNDVWV AVDIKNNASG LRLVYNGTPK GVFIESSAPA YTNLPNANTY IHIPILPNNS YVEYEFDIDA SQTLPILVNE TYDVTKIPAN KMSEWTVNLI VYLNKNLVPN GENVNVNVIK YLSNGQFYDN FENWTGWNQY KNGIVQWSSI QSHSGNYSLE KYGISTSLNN DPNGGYKLLP KEIGRDVVIS GWVYRPSNWG GGPIDRIGLE DENFDGYSFE VNHYSNYISI DRRTNGNPTE ISPEVYWNPP EDEWYYFELK IYSNGTITFS TYYQNGSLAA TVSTIDNTYT KFDRVVIHGG YVYYVDDLEV NSKNFDFYGD KNWKYLEITS ANSSEGTAVL FDGDYFKKDY NTSNLNAINW TNITLNWSND SATLVFNVLG NYSYSERDNI LAKYGFAKIL FNYNGTNTNT SIKGVYASGS YSISTDHGTT GEINIWIENV TFKNDAKSYS FNLTNLNIWA VNKSAYELYW NPFNKSIWID GSNYTITPNI DIPPGEVWNS KTYNFTFSGV PIVWANCSFT LSKKDYILLN EVSQIGSSYV VVEEIYVVGS YLIKVTKHIV PDADGTYDIY IVVENIGSVK TPEYVYVYDL IPKNFTVSDE WVNQSSMLIA EGNHTITTNP RYNLSMWWAL HAIYPGADGD GNWNDTAEIL ANKTVVIHYK LNGTGEFYPS DAFIVGIDPT NSLLPTTSPK ITTVAGTVEN NFEIFLILIN VIFGLGILTK RNIRNNK // ID Y1397_METJA Reviewed; 486 AA. AC Q58792; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1397; DE Flags: Precursor; GN OrderedLocusNames=MJ1397; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99410.1; -; Genomic_DNA. DR PIR; D64474; D64474. DR ProteinModelPortal; Q58792; -. DR STRING; 243232.MJ_1397; -. DR EnsemblBacteria; AAB99410; AAB99410; MJ_1397. DR KEGG; mja:MJ_1397; -. DR eggNOG; arCOG07531; Archaea. DR eggNOG; ENOG410YEI9; LUCA. DR OMA; VVFYPNG; -. DR Proteomes; UP000000805; Chromosome. DR PROSITE; PS00189; LIPOYL; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 25 {ECO:0000255}. FT CHAIN 26 486 Uncharacterized protein MJ1397. FT /FTId=PRO_0000014014. SQ SEQUENCE 486 AA; 55817 MW; 83BC9302A3D1240B CRC64; MGTMRSVYLI IIIILFFAFI SLSFGEIYEY RGVVFYPNGS QTVDVSKLHI DYENPDAFSI YISYRNSSFY LPYSKNITLN LPPKKFNISI TISASRISRD EWRVYYKIIN NYPYSILFNI SFPGGFNIKN ASVLVPAKSY KIITLSKIQN SNILYFGDSN ISFEVPAKLM IRYSLPIPFS IIKSNKILSN GSIEWTAIYI IKNDKNVSLN VNASYWAVVN NTKIDFGNYS YIIEPNENVS QSFNITSDYV PIFYLKFYAW RDVYETIKIK PAIKVDNSYI IGIGKVEGLS FNIPYYNYME REIKKKKEEK ENEESSKTIN QMQRHKKEEK SQTQETKKPS KNEMNKQEKE RKYPLIIEEK FKKVAAAIAT VTTTSITAML IPPIFRRRSY IVDKGIFSIK DLELLSGTVY VPEGCKLGNI LPGGITIIKL TDVEKDLARD LHEIYDIPLN SAKAIILGVK YGGRVFLSDK KAYDVAVEIG LEAYLF // ID Y1407_METJA Reviewed; 129 AA. AC Q58802; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=UPF0107 protein MJ1407; GN OrderedLocusNames=MJ1407; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0107 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99415.1; -; Genomic_DNA. DR PIR; F64475; F64475. DR ProteinModelPortal; Q58802; -. DR STRING; 243232.MJ_1407; -. DR EnsemblBacteria; AAB99415; AAB99415; MJ_1407. DR KEGG; mja:MJ_1407; -. DR eggNOG; arCOG04279; Archaea. DR eggNOG; COG1786; LUCA. DR InParanoid; Q58802; -. DR KO; K09128; -. DR OMA; FPYGKGS; -. DR PhylomeDB; Q58802; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016772; F:transferase activity, transferring phosphorus-containing groups; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:InterPro. DR Gene3D; 3.50.30.10; -; 1. DR HAMAP; MF_00078; UPF0107; 1. DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl. DR InterPro; IPR002840; DUF126. DR InterPro; IPR008279; PEP-util_enz_mobile_dom. DR InterPro; IPR012016; UPF0107. DR InterPro; IPR020794; UPF0107_arc. DR Pfam; PF01989; DUF126; 1. DR PIRSF; PIRSF004966; UCP004966; 1. DR SUPFAM; SSF52016; SSF52016; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 129 UPF0107 protein MJ1407. FT /FTId=PRO_0000152565. SQ SEQUENCE 129 AA; 13724 MW; 995D5A3F705C44D9 CRC64; MELKGRSISK GIIEGIAIVS KKPFSFLGGV DEEGNIIDKD SDLYGQSLKG KIFVFPYGRG STVGSYVIYG LAKRGILKGI VNKECEPIVA TGAILGGIPL VDKIDIEEIK TGDRIVVDGN TGVVKILNK // ID Y1408_METJA Reviewed; 350 AA. AC Q58803; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ1408; GN OrderedLocusNames=MJ1408; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TRAFAC class OBG-HflX-like GTPase CC superfamily. OBG GTPase family. NOG subfamily. CC {ECO:0000255|PROSITE-ProRule:PRU01047}. CC -!- SIMILARITY: Contains 1 OBG-type G (guanine nucleotide-binding) CC domain. {ECO:0000255|PROSITE-ProRule:PRU01047}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99416.1; -; Genomic_DNA. DR ProteinModelPortal; Q58803; -. DR SMR; Q58803; 5-332. DR STRING; 243232.MJ_1408; -. DR EnsemblBacteria; AAB99416; AAB99416; MJ_1408. DR KEGG; mja:MJ_1408; -. DR eggNOG; arCOG00352; Archaea. DR eggNOG; COG1084; LUCA. DR InParanoid; Q58803; -. DR KO; K06943; -. DR OMA; GINVGQF; -. DR PhylomeDB; Q58803; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031167; G_OBG. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR010674; NOG1_Rossman_fold_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF06858; NOG1; 1. DR PRINTS; PR00326; GTP1OBG. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. DR PROSITE; PS51710; G_OBG; 1. PE 3: Inferred from homology; KW Complete proteome; GTP-binding; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 350 Uncharacterized protein MJ1408. FT /FTId=PRO_0000195036. FT DOMAIN 171 334 OBG-type G. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 177 184 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 219 223 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. FT NP_BIND 286 289 GTP. {ECO:0000255|PROSITE- FT ProRule:PRU01047}. SQ SEQUENCE 350 AA; 40006 MW; C6B02B7B6965FE99 CRC64; MSREANPFKK MPTILMPDEL MAKALRRGEK VANEMRQKEL PWLLKARFVE EHKVRTIASV VADNLQKVID KTPPVRKLPK FYQEMVEVLV GIDDFKKSMG AFKWASELVR KLGNEYARKI RKARTPQQAG KLRKEFVGRV KSILEQIHPE MAFVAVAREK LKDLPTFKDL PTVVIAGYPN VGKSTLLKKL TGADVEINSY PFTTKGINVG YIGEIQMVDT PGLLDRPLYE RNDIELQAIL ALNYLANLIL FIIDASEFCG YTIEEQINLL KEIKDLFKAP IVVAINKIDL VDEERVKEIE EKLKEVGIEE ILKISADKDI GLDELKERLK KIAIKEFLKD KDAENKELEC // ID Y1426_METJA Reviewed; 168 AA. AC Q58821; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1426; GN OrderedLocusNames=MJ1426; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99437.1; -; Genomic_DNA. DR PIR; A64478; A64478. DR ProteinModelPortal; Q58821; -. DR STRING; 243232.MJ_1426; -. DR EnsemblBacteria; AAB99437; AAB99437; MJ_1426. DR KEGG; mja:MJ_1426; -. DR eggNOG; ENOG4102TZF; Archaea. DR eggNOG; ENOG4111TWY; LUCA. DR InParanoid; Q58821; -. DR OMA; PDMTIND; -. DR PhylomeDB; Q58821; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 168 Uncharacterized protein MJ1426. FT /FTId=PRO_0000107319. FT DOMAIN 20 77 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 117 168 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 168 AA; 18874 MW; 690A7A4B7902B300 CRC64; MRTILNKLNI NGEIMLIKDI MKKPIVVYED NDLIDVIRLF RKNKISGAPV LNKDGKLVGI ISESDIVKTI VTHNEDLNLI LPSPLDLIEL PLKTALKIEE FMEDLKNALK TKVRDVMTRK VIVAKPDMTI NDAAKLMVKN NIKRLPVVDD EGNLIGIVTR GDLIEALI // ID Y144_METJA Reviewed; 258 AA. AC Q57608; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ0144; GN OrderedLocusNames=MJ0144; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98127.1; -; Genomic_DNA. DR PIR; A64318; A64318. DR ProteinModelPortal; Q57608; -. DR STRING; 243232.MJ_0144; -. DR EnsemblBacteria; AAB98127; AAB98127; MJ_0144. DR KEGG; mja:MJ_0144; -. DR eggNOG; arCOG00605; Archaea. DR eggNOG; COG0042; LUCA. DR InParanoid; Q57608; -. DR OMA; ELNCHCR; -. DR PhylomeDB; Q57608; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro. DR GO; GO:0017150; F:tRNA dihydrouridine synthase activity; IBA:GO_Central. DR GO; GO:0002943; P:tRNA dihydrouridine synthesis; IBA:GOC. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR005270; tRNA_dU_NifR3-rel. DR InterPro; IPR001269; tRNA_hU_synthase. DR PANTHER; PTHR11082; PTHR11082; 1. DR Pfam; PF01207; Dus; 1. DR TIGRFAMs; TIGR00736; nifR3_rel_arch; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 258 Uncharacterized protein MJ0144. FT /FTId=PRO_0000106718. SQ SEQUENCE 258 AA; 29754 MW; F83AF4A8D7BF0836 CRC64; MNKKIEELNK LDKKVVLAPM AGITDGDFCR KFKDLFAIVT IGGYNLDSAT YKASRDIEKR GRKEFSINLE EFNSYIIEQI KKARESNALV SVNVRFVDID EAYDKLLTIA KHADIIELNC HCRQPEITSL GIGQELMKNK NLLKEFLTKM KELNKPIFLK IRLNCIPLKE LIDNLNYVRD YFDGLHVDCF YPGKPYADMD SLKILAEEFN DKIIIGNNSI DSIEKAKEML KYSDFVSVAR TILKGNVEWI KELNKENI // ID Y1469_METJA Reviewed; 75 AA. AC Q58864; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=UPF0333 protein MJ1469; GN OrderedLocusNames=MJ1469; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0333 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99484.1; -; Genomic_DNA. DR PIR; D64483; D64483. DR STRING; 243232.MJ_1469; -. DR EnsemblBacteria; AAB99484; AAB99484; MJ_1469. DR KEGG; mja:MJ_1469; -. DR eggNOG; arCOG09683; Archaea. DR eggNOG; COG1991; LUCA. DR OMA; SIVGFYY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR InterPro; IPR026451; ClassIII_w_PIP. DR Pfam; PF04021; Class_IIIsignal; 1. DR TIGRFAMs; TIGR04205; classIII_w_PIP; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 75 UPF0333 protein MJ1469. FT /FTId=PRO_0000218269. FT TRANSMEM 13 33 Helical. {ECO:0000255}. SQ SEQUENCE 75 AA; 8050 MW; 8F4FDE15923B9ED7 CRC64; MKPKKIISNK AQISLELALL LGALVVAASI VGFYYLKSVT RGTSTAESIS KNITLAAKNK ALDNIYKVKR ALNGQ // ID Y1478_METJA Reviewed; 303 AA. AC Q58873; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=CTU1/ATPBD3 family protein MJ1478; GN OrderedLocusNames=MJ1478; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99482.1; -; Genomic_DNA. DR PIR; E64484; E64484. DR ProteinModelPortal; Q58873; -. DR STRING; 243232.MJ_1478; -. DR EnsemblBacteria; AAB99482; AAB99482; MJ_1478. DR KEGG; mja:MJ_1478; -. DR eggNOG; arCOG00042; Archaea. DR eggNOG; COG0037; LUCA. DR InParanoid; Q58873; -. DR OMA; VKPLYEV; -. DR PhylomeDB; Q58873; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0034227; P:tRNA thio-modification; IEA:InterPro. DR GO; GO:0002098; P:tRNA wobble uridine modification; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR000541; Ncs6/Tuc1/Ctu1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR InterPro; IPR020554; UPF0021_CS. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. DR TIGRFAMs; TIGR00269; TIGR00269; 1. DR PROSITE; PS01263; UPF0021; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 303 CTU1/ATPBD3 family protein MJ1478. FT /FTId=PRO_0000219892. SQ SEQUENCE 303 AA; 35543 MW; D62272DDA060A40D CRC64; MVKTMKCKFC DKKSYIKLKS PKMYLCKEHF VEYFENKVKK SIDKYKMLSK DEKILVAVSG GKDGHAAAWV LKKLGYNIEL FHINLGIEGF SEESLKAVKE LAEKLEVPLH VVNLKDITGK TMEDIRGKKC SICGTTKRYL MNKFGYENGF DVIVTGHNLD DEVSFILNNL FNWNIRYLAK HEPVLPAHDK FLKKVKIFFE IEEELILKYA EAEEIPYTTV ECKYAERAIT LKHRAYLNEL EKERPGIKYQ FLSGYMKNRH LFKVEEEDFQ FRECEVCGMT SAGKICSFCR VWKLYKKKKE NRN // ID Y1479_METJA Reviewed; 432 AA. AC Q58874; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized aminotransferase MJ1479; DE EC=2.6.1.-; GN OrderedLocusNames=MJ1479; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the class-II pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99491.1; -; Genomic_DNA. DR PIR; F64484; F64484. DR ProteinModelPortal; Q58874; -. DR STRING; 243232.MJ_1479; -. DR EnsemblBacteria; AAB99491; AAB99491; MJ_1479. DR KEGG; mja:MJ_1479; -. DR eggNOG; arCOG01135; Archaea. DR eggNOG; COG0436; LUCA. DR InParanoid; Q58874; -. DR OMA; YDLFIIC; -. DR PhylomeDB; Q58874; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR004839; Aminotransferase_I/II. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR Pfam; PF00155; Aminotran_1_2; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Cytoplasm; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 432 Uncharacterized aminotransferase MJ1479. FT /FTId=PRO_0000163832. FT MOD_RES 243 243 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 432 AA; 49430 MW; 14D1602E32DB31FE CRC64; MRNPIIDVGA KELSYEIREI VDVAKKIEEF GINITWENIG DPVAKGEKIP DWIKDIIAEI VKNDCSYAYC PTKGLLETRE FLAEQVNKRG GVQITAEDII FFNGLGDAIA KIYGLLKRQV RVINPSPSYS THSSAEASHA GSPPVTYFLD PYNYWYPDID DLEKRIKYNP AVSGILVINP DNPTGAVYPK KILNEIVDLA NEYDLFIICD EIYCNLVYNG KKQHLLCEVI DDVCGLSLKG ISKELPWPGA RCGWIEIYNA DKDEEFKKYV ESIYKAKLIE VCSTTLPQMA IPRIMGHRNY KKYLEERNRF FEKRSNTAYK KLKDLDGVIA NKANGAFYMS VVFEDNYLNG NNSIKIENEK LKEFIEHQIK DASIDKKFVY YLLASTGICV VPLTSFCSQL NGFRVTLLER DDEKFEWIFD TLAEKIDEFL KT // ID Y1495_METJA Reviewed; 292 AA. AC Q58890; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1495; GN OrderedLocusNames=MJ1495; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0137. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99506.1; -; Genomic_DNA. DR PIR; F64486; F64486. DR ProteinModelPortal; Q58890; -. DR STRING; 243232.MJ_1495; -. DR EnsemblBacteria; AAB99506; AAB99506; MJ_1495. DR KEGG; mja:MJ_1495; -. DR eggNOG; arCOG01911; Archaea. DR eggNOG; COG0616; LUCA. DR InParanoid; Q58890; -. DR OMA; EIIMDKN; -. DR PhylomeDB; Q58890; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 3. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR002825; Pept_S49_ser-pept_pro. DR Pfam; PF01972; SDH_sah; 1. DR SUPFAM; SSF52096; SSF52096; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 292 Uncharacterized protein MJ1495. FT /FTId=PRO_0000107378. FT TRANSMEM 17 37 Helical. {ECO:0000255}. SQ SEQUENCE 292 AA; 33509 MW; B8A34C29B3A51246 CRC64; MILIIYLTKI MGDEMTSMDM FFFLFIFLLF IYPEMMMRYR IMKRLRCIRE IERQRGTRVI AMIHRQEALT FLGIPIYKFI TIEDSEEILR AIRLTPEDMP IDLIIHTPGG LALASEQIAL ALKEHKAKTT VIIPHYAMSG GSLIALAADE IIMDKNAVMG PVDPQIGQYP AASILEAYYR KGEKVSDETL ILVDISKKAI KQMEEFVYEL LKDKYGDEKA KEIAKKLTSG TWTHDYPLTV SKLKELGIEV NTNVPRKVYE LLELYPQPMG AKPSVYYIPV PYSKKESEKN AK // ID Y1505_METJA Reviewed; 778 AA. AC Q58900; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 109. DE RecName: Full=Putative ATP-dependent RNA helicase MJ1505; DE EC=3.6.4.13; GN OrderedLocusNames=MJ1505; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the DEAD box helicase family. DEAH CC subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99518.1; -; Genomic_DNA. DR ProteinModelPortal; Q58900; -. DR SMR; Q58900; 711-776. DR STRING; 243232.MJ_1505; -. DR PRIDE; Q58900; -. DR EnsemblBacteria; AAB99518; AAB99518; MJ_1505. DR KEGG; mja:MJ_1505; -. DR eggNOG; arCOG00872; Archaea. DR eggNOG; COG1111; LUCA. DR eggNOG; COG1948; LUCA. DR InParanoid; Q58900; -. DR KO; K10896; -. DR OMA; FYEPVPT; -. DR PhylomeDB; Q58900; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.40.50.10130; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR020819; DNA_repair_nuc_XPF/helicase. DR InterPro; IPR006166; ERCC4_domain. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR003583; Hlx-hairpin-Hlx_DNA-bd_motif. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR010994; RuvA_2-like. DR Pfam; PF02732; ERCC4; 1. DR Pfam; PF00271; Helicase_C; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00891; ERCC4; 1. DR SMART; SM00490; HELICc; 1. DR SMART; SM00278; HhH1; 2. DR SUPFAM; SSF47781; SSF47781; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR SUPFAM; SSF52980; SSF52980; 1. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome; RNA-binding. FT CHAIN 1 778 Putative ATP-dependent RNA helicase FT MJ1505. FT /FTId=PRO_0000055117. FT DOMAIN 22 186 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 338 516 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 35 42 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 137 140 DEAH box. FT COMPBIAS 532 535 Poly-Glu. SQ SEQUENCE 778 AA; 88883 MW; DCB1F220801338D8 CRC64; MFIEHPLIKP KTLEARLYQQ IIAANALKKK TLCVLSTGLG KTAIAILVIA GILTKKDGKV LILAPSRPLV EQHYNRLKQV LNIDEDKIIA LTGKIQPKKR AELYKKGKIF IATPQVIEND IIAGRINVDE FILLIADEAH HTTGDHAYAF VAKKFKDKCH ILGLTASPGS DIDKVMEICE NLGIEHVEVR TEDDEDVKPY IAKVKLIPIR IDLPNEFKRA LKLINEALKE RLKILKDAGV INSIADVTKT ELIELNNKLF SYDEEVKYEL IKVCSEALKL MHAKELLESQ GKSVFLNYIN KLSMQRTKSA KSIVNDEKVR EAVNLLMKSD VEHPKLGKVV DMVKNILEKN KDERIIIFAQ YRDTVEKIVN LLTQNGIKAI RFIGQANKEG KGMSQKEQIE AIERFKKEGS VLVSTSVSEE GIDIPSVNYI IFYEPVPSEI RFIQRRGRAM RGEGGKVYVL IAKGTADEAY YRSALYKERE MKRLLKNMCY LLNKRLQKKF EEKSKEEIKE ETEEIKEKEI ESKTAVKEET KEEEEKTKKP VTILDFIKQI EVKERSKSEE DKIKQEIKIP KKPIKIIVDV REKNMAKLLH NYANIELKTL EVGDYVLSDR VVVERKTAED FVNSIIDKRL FSQLKNLKKV EKPLLIVEGE NFSRLHENAL KGAILSIILD FGIPIIFTKN AEETADLLIK IAEKEQIKEK RTVMVRYGKT AMSLKEQQKF IVESLPDVGG ALAERLLKHF KTVENVFTAK EEELMKVEGV GKERAKKIRE VLTAEYEG // ID Y1507_METJA Reviewed; 399 AA. AC Q58902; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized ABC transporter permease MJ1507; GN OrderedLocusNames=MJ1507; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99519.1; -; Genomic_DNA. DR PIR; B64488; B64488. DR STRING; 243232.MJ_1507; -. DR EnsemblBacteria; AAB99519; AAB99519; MJ_1507. DR KEGG; mja:MJ_1507; -. DR eggNOG; arCOG02312; Archaea. DR eggNOG; COG0577; LUCA. DR InParanoid; Q58902; -. DR KO; K02004; -. DR OMA; LVTYNDQ; -. DR PhylomeDB; Q58902; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 399 Uncharacterized ABC transporter permease FT MJ1507. FT /FTId=PRO_0000107382. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. FT TRANSMEM 301 321 Helical. {ECO:0000255}. FT TRANSMEM 324 344 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. SQ SEQUENCE 399 AA; 44008 MW; 18A17826BBB25297 CRC64; MGKSMKVDDI ITFAFKNIKQ KRTQSLLTII GIVIGVLAMV SLISLGYGVQ NYIHEEMMKM GSNKITILPM KQFGVPPSHL FTKKEIKAIK NVKGVDTVMY GWYGGCEIEY NGEKKFVSYY YAIPSKLREV YKDSGYDIEE GRWLEDNDKY ACVIGYGTAH NLFDREIKVG DVIKIKDKKF RVVGILKQIG NQQDDNSIIL NIDVGEKLFG NEGKYNFISV TVKEGEDIEK VSEEIKKALK KSFGDEDFSV LTAEQLAKTV SSVLGVITIF VVGVAAISLL VGAVGISNTM HMSILERRKD IGILKALGAE TTDILAIFVV ESGFLGLFGG IVGLVLGILL AEVIEALAHK MGYLMVNAWI SWELIVGVLI FSFLVGVISG YFPARSGAKL NPIETLRGE // ID Y1509_METJA Reviewed; 153 AA. AC Q58904; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1509; GN OrderedLocusNames=MJ1509; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99534.1; -; Genomic_DNA. DR PIR; D64488; D64488. DR ProteinModelPortal; Q58904; -. DR STRING; 243232.MJ_1509; -. DR EnsemblBacteria; AAB99534; AAB99534; MJ_1509. DR KEGG; mja:MJ_1509; -. DR eggNOG; arCOG05087; Archaea. DR eggNOG; ENOG4111PDI; LUCA. DR InParanoid; Q58904; -. DR OMA; IKMRHIP; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.20.10; -; 1. DR InterPro; IPR015207; DUF1931. DR InterPro; IPR009072; Histone-fold. DR Pfam; PF09123; DUF1931; 1. DR SUPFAM; SSF47113; SSF47113; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 153 Uncharacterized protein MJ1509. FT /FTId=PRO_0000107383. SQ SEQUENCE 153 AA; 17718 MW; 0B1AABEDC831685B CRC64; MAEMIIPYPQ LKKIMKTTCE IDLYKTEAED IMDVVEKKLA DLFEVAHRNA KEENAKIIKM RHIPLTKGFL NSMELFRSVI EEENIVAETI KKYVMKKIPG DLPLDDIVVD NLPLITGTIF IVVGRVIKAL HEDIERIRKE HIEEAKKVLD YTL // ID Y150_METJA Reviewed; 173 AA. AC Q57614; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0150; GN OrderedLocusNames=MJ0150; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98141.1; -; Genomic_DNA. DR PIR; G64318; G64318. DR ProteinModelPortal; Q57614; -. DR STRING; 243232.MJ_0150; -. DR EnsemblBacteria; AAB98141; AAB98141; MJ_0150. DR KEGG; mja:MJ_0150; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q57614; -. DR KO; K07013; -. DR OMA; DECITCA; -. DR PhylomeDB; Q57614; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019642; DUF2507. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF10702; DUF2507; 1. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 173 Uncharacterized protein MJ0150. FT /FTId=PRO_0000106720. SQ SEQUENCE 173 AA; 19524 MW; A273F382C91D0315 CRC64; MGDVKMDKEL LHKKIKKDIE DLINNHPPER TLGNLIPLSI FQAVRIGVLT AGCGIEAIIY NIGKDIGREV ISRYVDRDNL LESFAEILKK AKIGILEVKK VEENEMILIL KDCISCHNVP NVGTTLCHFE AGLIAGTLEK KLRRKVNAVE TKCCGKGDEY CEFLVKIEDK LYW // ID Y1511_METJA Reviewed; 107 AA. AC Q58906; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1511; GN OrderedLocusNames=MJ1511; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99530.1; -; Genomic_DNA. DR PIR; F64488; F64488. DR ProteinModelPortal; Q58906; -. DR STRING; 243232.MJ_1511; -. DR EnsemblBacteria; AAB99530; AAB99530; MJ_1511. DR KEGG; mja:MJ_1511; -. DR eggNOG; arCOG02148; Archaea. DR eggNOG; COG0599; LUCA. DR OMA; FYEAVAN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 107 Uncharacterized protein MJ1511. FT /FTId=PRO_0000107384. SQ SEQUENCE 107 AA; 11891 MW; E93B27785FFF7C82 CRC64; MAEFVPAETI EVVKKNCPEF YEAVANLQKE VFSGKKLDEK MQRLVLLAVV ATLGDEKAVK RQTKKLMEMG ATIEEIQDVM KVVYIGAGMP RFIKAVEAIL EVAGDQC // ID Y1513_METJA Reviewed; 335 AA. AC Q58908; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1513; GN OrderedLocusNames=MJ1513; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99535.1; -; Genomic_DNA. DR PIR; H64488; H64488. DR ProteinModelPortal; Q58908; -. DR STRING; 243232.MJ_1513; -. DR EnsemblBacteria; AAB99535; AAB99535; MJ_1513. DR KEGG; mja:MJ_1513; -. DR eggNOG; ENOG4102TYW; Archaea. DR eggNOG; ENOG41122ZG; LUCA. DR OMA; CAMILNK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 335 Uncharacterized protein MJ1513. FT /FTId=PRO_0000107385. SQ SEQUENCE 335 AA; 38469 MW; 40BFB2D49842FF4C CRC64; MSKMTNDLEK IRGGVHIAVQ GYEVDRITEV PIMRRAEKVY LICKPGNNDS KRGKAFKNVI IKKFEEKRVN YEIVEADLFD LDDIVKKMKL IIAHERKEFG DVKFYINVSS GSTIGCIAGI TCAMILNKEN SRIIPYYVMP EKSLDGLSEK EKEELKKEYE SKYNCPYLPR SFGVRGVKLI YPFEVTLPRE ELLIFLKFIG RAGNRGLTIK ELSILTKEEF LNVDLNDNES IKELIKAVER KESVSNSSVK KMKNLVRELK EVVGSDVDDL KKIITWRKKC RSSVSSTGQS DLVWVNKNVV EKLLELELIE KPEKIGKSKY IRISEKGKML LNYVG // ID Y1525_METJA Reviewed; 933 AA. AC Q58920; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Uncharacterized membrane protein MJ1525; GN OrderedLocusNames=MJ1525; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the STT3 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99543.1; -; Genomic_DNA. DR PIR; D64490; D64490. DR ProteinModelPortal; Q58920; -. DR STRING; 243232.MJ_1525; -. DR EnsemblBacteria; AAB99543; AAB99543; MJ_1525. DR KEGG; mja:MJ_1525; -. DR eggNOG; arCOG02044; Archaea. DR eggNOG; COG1287; LUCA. DR InParanoid; Q58920; -. DR KO; K07151; -. DR OMA; DNGHIYT; -. DR BRENDA; 2.4.99.18; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004576; F:oligosaccharyl transferase activity; IEA:InterPro. DR GO; GO:0006486; P:protein glycosylation; IEA:InterPro. DR InterPro; IPR003674; Oligo_trans_STT3. DR Pfam; PF02516; STT3; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 933 Uncharacterized membrane protein MJ1525. FT /FTId=PRO_0000107392. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 147 167 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 237 257 Helical. {ECO:0000255}. FT TRANSMEM 264 284 Helical. {ECO:0000255}. FT TRANSMEM 319 339 Helical. {ECO:0000255}. FT TRANSMEM 362 382 Helical. {ECO:0000255}. FT TRANSMEM 428 448 Helical. {ECO:0000255}. FT TRANSMEM 455 475 Helical. {ECO:0000255}. FT TRANSMEM 480 500 Helical. {ECO:0000255}. FT TRANSMEM 507 527 Helical. {ECO:0000255}. FT TRANSMEM 536 556 Helical. {ECO:0000255}. FT TRANSMEM 582 602 Helical. {ECO:0000255}. SQ SEQUENCE 933 AA; 103964 MW; F3B555913A77379C CRC64; MYIKVKLMSN ALEKINNFFK EKSWIKVFLI ILMLMFVSFQ LRAQTADMKF AQDNEFLKDM FSDEHGRMYL LALDPYYYLR LSENLYNNGH CGDTIKVVDG KETPYDLYQY APPGHPLPWE PPVICLATLA IYYIWHSIDL TVTIMNAAFW VPAVLGMLLG IPIYFVVRRV TNSNIGGIAG AIALISAPGL LYKTCAGFAD TPIFEVLPIL FIVWFILESI HSQEKTALFK KDLKNPISLF VIAALIIELI IGAYLNIASG ESVVIASILF YTVSLAFILA GLIIAGIKKL KGNELEFELF ALLAVILTAV SPKMWGAWWY GFDVITAFLV IYIIALALLK SQVKIKEFIN IGNLKNIVYL SIFYIFGSFV LLVAIYGMGI AISPITSPLG YNQILSTYTQ TTGWPNVYTT VAELAKPSSW SEIFTNAIGS DTIAIVGILG ILLSFLSLRY EKVKLDIKYS ILLAIWLAVT LYAATKGIRF AALATPPLAI GLGIFVGQLE RFLKMKSDIA IFGIGIPAGI FGLLILSKYS AKISQILLPT TYVPIIAYGF LIVLALLAIY KISDIISTLN DKKETIIKVS TLLLCIGVVI PPLSAVVPFS VAPTFNNGWK EGLDWIKANT PNNSVITCWW DNGHIYTYEA RRMVTFDGGS QNSPRAYWVG RAFATSNENL SIGIIRMLAT SGDEAFKKGS VLMNFTHNNV SKTVKILNEI LPVDRSKAYD ILTKKYGLSD KKAKLVLNAT HPEHPNPDYL ITYNRMTDIA PVWSMFGFWN FSLPPNTPND KREKGAFFKG TAYYLGNGTI LANVNVYTYS YVTLINSTNI STAIVQKING QAKIIGTFKI HKLYIKTPLG VKELVLNKDG QLSEFIRIEA DGRGYAWLAT RNLEDSIYAK LHFLDGYGLK HIKLVKATID PTDFGIQPGF KIYKVDYGTD YLK // ID Y1527_METJA Reviewed; 140 AA. AC Q58922; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=UPF0132 membrane protein MJ1527; GN OrderedLocusNames=MJ1527; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0132 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99545.1; -; Genomic_DNA. DR PIR; F64490; F64490. DR ProteinModelPortal; Q58922; -. DR STRING; 243232.MJ_1527; -. DR EnsemblBacteria; AAB99545; AAB99545; MJ_1527. DR KEGG; mja:MJ_1527; -. DR eggNOG; arCOG04344; Archaea. DR eggNOG; COG4818; LUCA. DR InParanoid; Q58922; -. DR OMA; FIRFHAM; -. DR PhylomeDB; Q58922; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019109; DUF4870. DR Pfam; PF09685; DUF4870; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 140 UPF0132 membrane protein MJ1527. FT /FTId=PRO_0000158603. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. SQ SEQUENCE 140 AA; 16481 MW; 1FD660864492BC72 CRC64; MNIYLISKVF IKYHLFQNIL KSYLLNFLVR LMALGLDRNM EGVLCYLLFW ISGLIFLLLE REDDFIRFHA MQSFITFLSL NLIAIIVSAI PIIGWVASTL INIAIIILWI VGMIKAYNGE RYKFPVFGDI AERYYREFLK // ID Y1531_METJA Reviewed; 425 AA. AC Q58926; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1531; GN OrderedLocusNames=MJ1531; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0130 and MJ1218. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99552.1; -; Genomic_DNA. DR PIR; B64491; B64491. DR ProteinModelPortal; Q58926; -. DR STRING; 243232.MJ_1531; -. DR REBASE; 3899; S.MjaORF1531P. DR EnsemblBacteria; AAB99552; AAB99552; MJ_1531. DR KEGG; mja:MJ_1531; -. DR eggNOG; arCOG02626; Archaea. DR eggNOG; COG0732; LUCA. DR InParanoid; Q58926; -. DR KO; K01154; -. DR OMA; KIATHEF; -. DR PhylomeDB; Q58926; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006304; P:DNA modification; IEA:InterPro. DR InterPro; IPR000055; Restrct_endonuc_typeI_HsdS. DR Pfam; PF01420; Methylase_S; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 425 Uncharacterized protein MJ1531. FT /FTId=PRO_0000107393. SQ SEQUENCE 425 AA; 48889 MW; DB879AC2D8911AE9 CRC64; MVILLQFYKE ENFKKTEIGE IPEDWEVREL KDILEVIRNG LTAKQNKDKI GYPITRIETI SDSKIDITKL GYVEDIKQED IAKYRLIIGD ILFSHINSEE HIGKVAIYEG KPEFLLHGMN LLLLRPNKNK IEPYYLLYLL RHFKQKNIFK YIAKRAVNQS SINQTQLKHL KIPLPPLEEQ KQIAKILSDF DNLIGTINKQ IEVLNKAKKG MMKKLFTKGV FEHKSFKKSE IGEIPEDWEV VELGNEKYFK IIMGQSPPSS SYNKEGEGVP FLQGKAEFGN IYPNPVLYTN KPLKVVDDED ILISVRAPVG DVNIAPFKLC IGRGLAGIKS NKEKVDNFFV FYYLSYIKPK IEYLGGGAVF KAITKKDLES IKIPLPPLEE QKAIAKRLKA IDDLIEIKRK EKEQIEKAKK KIMNLLLTGK IRVKT // ID Y1533_METJA Reviewed; 642 AA. AC Q58928; DT 29-MAR-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 101. DE RecName: Full=Uncharacterized KH and PIN-domain containing protein MJ1533; GN OrderedLocusNames=MJ1533; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.64 ANGSTROMS) OF 27-165. RG Midwest center for structural genomics (MCSG); RT "A domain of a functionally unknown protein from Methanocaldococcus RT jannaschii DSM 2661."; RL Submitted (JUL-2009) to the PDB data bank. CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000305}; CC -!- SIMILARITY: In the N-terminal section; belongs to the PINc/VapC CC protein family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 KH domain. {ECO:0000255|PROSITE- CC ProRule:PRU00117}. CC -!- SIMILARITY: Contains 1 PINc domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99554.1; -; Genomic_DNA. DR PIR; D64491; D64491. DR PDB; 3I8O; X-ray; 2.64 A; A=27-165. DR PDBsum; 3I8O; -. DR ProteinModelPortal; Q58928; -. DR STRING; 243232.MJ_1533; -. DR DNASU; 1452441; -. DR EnsemblBacteria; AAB99554; AAB99554; MJ_1533. DR KEGG; mja:MJ_1533; -. DR eggNOG; arCOG04116; Archaea. DR eggNOG; COG1855; LUCA. DR InParanoid; Q58928; -. DR KO; K06865; -. DR OMA; SLIIQHK; -. DR PhylomeDB; Q58928; -. DR EvolutionaryTrace; Q58928; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.30.1370.10; -; 1. DR Gene3D; 3.40.50.1010; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR009019; KH_prok-type. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00013; KH_1; 1. DR Pfam; PF01850; PIN; 1. DR Pfam; PF00437; T2SSE; 1. DR SMART; SM00322; KH; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF54814; SSF54814; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR PROSITE; PS50084; KH_TYPE_1; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Magnesium; Metal-binding; KW Reference proteome; RNA-binding. FT CHAIN 1 642 Uncharacterized KH and PIN-domain FT containing protein MJ1533. FT /FTId=PRO_0000050166. FT DOMAIN 29 149 PINc. FT DOMAIN 510 578 KH. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT METAL 15 15 Magnesium. {ECO:0000255}. FT METAL 118 118 Magnesium. {ECO:0000255}. FT STRAND 28 31 {ECO:0000244|PDB:3I8O}. FT HELIX 33 37 {ECO:0000244|PDB:3I8O}. FT HELIX 40 46 {ECO:0000244|PDB:3I8O}. FT TURN 47 52 {ECO:0000244|PDB:3I8O}. FT STRAND 54 58 {ECO:0000244|PDB:3I8O}. FT HELIX 59 69 {ECO:0000244|PDB:3I8O}. FT TURN 70 72 {ECO:0000244|PDB:3I8O}. FT HELIX 74 92 {ECO:0000244|PDB:3I8O}. FT STRAND 97 101 {ECO:0000244|PDB:3I8O}. FT HELIX 106 110 {ECO:0000244|PDB:3I8O}. FT STRAND 114 116 {ECO:0000244|PDB:3I8O}. FT HELIX 117 127 {ECO:0000244|PDB:3I8O}. FT STRAND 131 135 {ECO:0000244|PDB:3I8O}. FT HELIX 137 145 {ECO:0000244|PDB:3I8O}. FT STRAND 150 152 {ECO:0000244|PDB:3I8O}. SQ SEQUENCE 642 AA; 72907 MW; 9CA730BFA10ABE69 CRC64; MKVTFMNLEE RKKLETKSID ELDLIGKKVC VDTCVVIDGR ITELIERGKL KDATIIIPEA VVSELEYQAN MGREIGYKGI EELRKLIEKA SEHNIKVEYY GERPTREEIF LAKSGEIDAM IRKVAKETNS ILLTSDWIQY NLAKAQGIEA YFLEAAEEEV ELVLDKYFDE ETMSVHLKEG CLPYAKKGKP GEVKLVPIGD KELTKEEMED IIDNIIKYAE QNNGFFEIQR KGATVIQLGN IRISIARPPF SEALEVTAVR PVVKASLEDY ELSDKLMERL KERAEGIFVS GPPGSGKSTF VAALAEFYRS QGKIVKTMES PRDLQVSKEI TQYAPLEGDM EKTCDILLLV RPDYTIYDEV RKTRDFEIFA DMRMAGVGMV GVVHASKPID AIQRLIGRVE LGVIPQVVDT VIFIKDGKIQ KVYEIDFTVK VPYGMVEEDL ARPVIEVKDF ETGRVEYEIY TYGEQVVVMP IKEEGGKKAP IYGYAEEKLE EILKKLLPRK AKPMVKVTGD NSIDLIVPEK YIGAIIGKGG KEISKLEDML GLKISVKEKE KEEEKDMERI YRKYEYVNEL ESTRIYETDK YVVVDVGEDF AGENIRIYID GKLLTTVTVR NDGTVRINKK TKVGKEILEA IDEGRDIYVD LQ // ID Y1546_METJA Reviewed; 345 AA. AC Q58941; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 3. DT 11-MAY-2016, entry version 90. DE RecName: Full=UPF0219 protein MJ1546 {ECO:0000255|HAMAP-Rule:MF_01409}; GN OrderedLocusNames=MJ1546; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0219 family. {ECO:0000255|HAMAP- CC Rule:MF_01409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99564.1; -; Genomic_DNA. DR PIR; A64493; A64493. DR ProteinModelPortal; Q58941; -. DR STRING; 243232.MJ_1546; -. DR EnsemblBacteria; AAB99564; AAB99564; MJ_1546. DR KEGG; mja:MJ_1546; -. DR eggNOG; arCOG01767; Archaea. DR eggNOG; COG3425; LUCA. DR InParanoid; Q58941; -. DR KO; K01641; -. DR OMA; VWFGTES; -. DR PhylomeDB; Q58941; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004421; F:hydroxymethylglutaryl-CoA synthase activity; IEA:InterPro. DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.47.10; -; 2. DR HAMAP; MF_01409; UPF0219; 1. DR InterPro; IPR013747; ACP_syn_III_C. DR InterPro; IPR004656; FabH-rel. DR InterPro; IPR013528; HMG_CoA_synth_N. DR InterPro; IPR016039; Thiolase-like. DR Pfam; PF08541; ACP_syn_III_C; 1. DR Pfam; PF01154; HMG_CoA_synt_N; 1. DR SUPFAM; SSF53901; SSF53901; 2. DR TIGRFAMs; TIGR00748; HMG_CoA_syn_Arc; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 345 UPF0219 protein MJ1546. FT /FTId=PRO_0000057614. SQ SEQUENCE 345 AA; 37549 MW; 8FDA1A9379064F0C CRC64; MAGIVGYGAY IPKYRIKVEE IARVWNKDPE SIKKGLLVYE KAVPSLDEDT ATIAVEAARN ALKRAEIDPK DIGAVYVGSE SHPYAVKPTA TIVAEAIDAT PDLTAADLEF ACKAGTAGIQ MCMGLVESGL IKYGLAIGAD TAQGAPGDAL EYTAAAGGAA YIIGKSNVIA EFNGTYSYTT DTPDFWRREG KPYPRHGGRF TGEPAYFRHV INAAKGLMEK MGTKPEDYDY CVFHQPNGKF YIRVAKILGF KEEQYKIGLL TPYIGNTYSG AVPLGLSNVL DNCEGGERIL AVSYGSGAGS DAFDITVTDR INKVKDKAPK TAYYLERKEY IDYAIYAKFR KKIKM // ID Y1547_METJA Reviewed; 122 AA. AC Q58942; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1547; GN OrderedLocusNames=MJ1547; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99565.1; -; Genomic_DNA. DR PIR; B64493; B64493. DR ProteinModelPortal; Q58942; -. DR STRING; 243232.MJ_1547; -. DR EnsemblBacteria; AAB99565; AAB99565; MJ_1547. DR KEGG; mja:MJ_1547; -. DR eggNOG; arCOG02107; Archaea. DR eggNOG; COG1708; LUCA. DR InParanoid; Q58942; -. DR KO; K07076; -. DR OMA; SYAKNEY; -. DR PhylomeDB; Q58942; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 122 Uncharacterized protein MJ1547. FT /FTId=PRO_0000107401. SQ SEQUENCE 122 AA; 14759 MW; 0992EFA439E40EF9 CRC64; MSKVFGILLY GSYAKNEYTK RSDIDICLVG VDRNTYLEIL GKLGNKYDIK IFEELPLYIK MEIIKNHKVI FGDELELSEH FYKFRKIWRD MEKRIRENQF NSVREKVMLR RRFNAKKEEI LG // ID Y1562_METJA Reviewed; 388 AA. AC Q58957; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Putative membrane protein MJ1562; GN OrderedLocusNames=MJ1562; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the resistance-nodulation-cell division CC (RND) (TC 2.A.6) family. MmpL subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99583.1; -; Genomic_DNA. DR PIR; A64495; A64495. DR ProteinModelPortal; Q58957; -. DR STRING; 243232.MJ_1562; -. DR TCDB; 2.A.6.7.2; the resistance-nodulation-cell division (rnd) superfamily. DR PRIDE; Q58957; -. DR EnsemblBacteria; AAB99583; AAB99583; MJ_1562. DR KEGG; mja:MJ_1562; -. DR eggNOG; arCOG02174; Archaea. DR eggNOG; COG1033; LUCA. DR InParanoid; Q58957; -. DR KO; K07003; -. DR OMA; MDESQAV; -. DR PhylomeDB; Q58957; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR004869; MMPL_dom. DR InterPro; IPR000731; SSD. DR Pfam; PF03176; MMPL; 1. DR PROSITE; PS50156; SSD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 388 Putative membrane protein MJ1562. FT /FTId=PRO_0000103587. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TRANSMEM 246 266 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. FT TRANSMEM 320 340 Helical. {ECO:0000255}. FT TRANSMEM 351 371 Helical. {ECO:0000255}. SQ SEQUENCE 388 AA; 42770 MW; 40B048F80AE24D54 CRC64; MVVLMLREIL KKVAHFSEQK PFLMLLIILI ITVFAGISAT NVKSQTAFEK MLPQDNPIIK TLYEVRDEFG GTDVITICIK LKPSDSSDKV VDIRDPRVLK AIKELEDNLR YVDGITSVSS PVDIIIQKNN GIVPNDIDTV KDILNKLPED KRKRIFNSDY SMTVVNAYTD AGGDQKKLMR VMDDVNERIE ETPFPPGVEV IATGTPPMRK LMDELMKESQ SFTTTVGLIG ILIILIIYFR KPLSSIMPLL PVLIAVIWTG GAMGLLDIPL DMATAGIGSL ILGLGIDYGI HLMHRYDEER RKGMPIDKAI ETAVVETGTA VMATTATTVV GFLALVLAPL PMMANLGKVC ALGISFCMVV VLTLLPALIV IEERHIMPLI KRLKGDTQ // ID Y1589_METJA Reviewed; 241 AA. AC Q58984; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1589; GN OrderedLocusNames=MJ1589; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0871, MJ0880 and MJ1556. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99617.1; -; Genomic_DNA. DR PIR; D64498; D64498. DR ProteinModelPortal; Q58984; -. DR STRING; 243232.MJ_1589; -. DR EnsemblBacteria; AAB99617; AAB99617; MJ_1589. DR KEGG; mja:MJ_1589; -. DR eggNOG; arCOG00360; Archaea. DR eggNOG; COG3366; LUCA. DR OMA; FGIHIIL; -. DR PhylomeDB; Q58984; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 241 Uncharacterized protein MJ1589. FT /FTId=PRO_0000107430. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255}. FT TRANSMEM 200 220 Helical. {ECO:0000255}. SQ SEQUENCE 241 AA; 27083 MW; 45C5AFD0496723EF CRC64; MMMALQIFIK ILPIMFFGIL LANLMCHLNI LYKLQKYIKN KYFPIIAVFF VSSTSGSFLL KNLLKKGEIS EENLLPIYFL GMFVFGIHII LFYAIPMATS LGWYVGGIYV LIKFLVTCNY LIISVLMLKK RKYNIDIEFK SKSEGLYGAI RDTFKQYFRV LTSFVPSVLI ITYLIEHGLL DIVEDFAGSL LNALNLSPTI LVIVLTGLAT ISGAIGIASG LLDENILSPN EVLFSLFLAG F // ID Y1609_METJA Reviewed; 374 AA. AC Q59004; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized ATP-binding protein MJ1609; GN OrderedLocusNames=MJ1609; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99636.1; -; Genomic_DNA. DR PIR; H64500; H64500. DR ProteinModelPortal; Q59004; -. DR SMR; Q59004; 275-374. DR STRING; 243232.MJ_1609; -. DR EnsemblBacteria; AAB99636; AAB99636; MJ_1609. DR KEGG; mja:MJ_1609; -. DR eggNOG; ENOG4102U6V; Archaea. DR eggNOG; ENOG410YC3J; LUCA. DR InParanoid; Q59004; -. DR KO; K06921; -. DR OMA; GMPIKIP; -. DR PhylomeDB; Q59004; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 374 Uncharacterized ATP-binding protein FT MJ1609. FT /FTId=PRO_0000184676. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 374 AA; 43985 MW; 211D5BEB98269E9C CRC64; MKFFNREKEI NKILSIIEGE PNNIYFIYGS LNSGKSTLMR EIVVNRLDIS KYIPFFIDFR TRNILNVDNF IECLFEVDEK SEIDDFREYA KSLADLLVKG SEEISKYYLG MPIKIPKPFF DKIFNKKDKS ADVYQYIEYL FAKLNEKGKK PILIFDELQM IKEITLNGNR KLLWSLFQFL VALTKVQHLC HVFCLSSDSL FIEYVYKTGE LEGRADYILV DDFDKQTALK FIDFLAKEIL NKKLPKDEKE LIYSYVGGKP VLIIKVIDKL RYENLNDILD FMLKDATQKL KYFLNDLDYI KPKVEVGDEV IELKKEDIVK ALKLFKDSYE ISDSEVAKPI YVYLVKKNIL FLNPIEGILK PQSFLIWNAI KRLL // ID Y1615_METJA Reviewed; 255 AA. AC Q59010; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ1615; GN OrderedLocusNames=MJ1615; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99637.1; -; Genomic_DNA. DR PIR; F64501; F64501. DR ProteinModelPortal; Q59010; -. DR STRING; 243232.MJ_1615; -. DR EnsemblBacteria; AAB99637; AAB99637; MJ_1615. DR KEGG; mja:MJ_1615; -. DR eggNOG; arCOG02394; Archaea. DR eggNOG; COG2469; LUCA. DR InParanoid; Q59010; -. DR KO; K09156; -. DR OMA; APIDNFL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007381; CheF. DR Pfam; PF04283; CheF-arch; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 255 Uncharacterized protein MJ1615. FT /FTId=PRO_0000107438. SQ SEQUENCE 255 AA; 29634 MW; A40BF51E0F469B3E CRC64; MIDKSSEIAR FSGKGILITP KTLEKPLLKW EKLEIILYKD KIVFEFVDKT IEVGVEDIED VGAELPKKVI DIAKSTLEDI TYHSSIIIKS KEFGNVMVGF APETSIYGKA PIDNFLRKLF YILLNKKEVK ILYNAGENSE NTKWENGFLT FIKKRIKDGL VTKIEYRLVV EILDNEDSKI YDIFSNIKDV EIEEKDVDGE IEPVLKILQV KDGKDIISYL YTKDKKVRLF ILRYMVILLD YKYIGILRYL QETVE // ID Y1631_METJA Reviewed; 519 AA. AC Q59025; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1631; GN OrderedLocusNames=MJ1631; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the glycogen phosphorylase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99652.1; -; Genomic_DNA. DR PIR; E64503; E64503. DR ProteinModelPortal; Q59025; -. DR STRING; 243232.MJ_1631; -. DR CAZy; GT35; Glycosyltransferase Family 35. DR EnsemblBacteria; AAB99652; AAB99652; MJ_1631. DR KEGG; mja:MJ_1631; -. DR eggNOG; arCOG01421; Archaea. DR eggNOG; COG0058; LUCA. DR InParanoid; Q59025; -. DR KO; K00688; -. DR OMA; KPTAYFC; -. DR PhylomeDB; Q59025; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008184; F:glycogen phosphorylase activity; IEA:InterPro. DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR011834; Agluc_phsphrylas. DR InterPro; IPR000811; Glyco_trans_35. DR PANTHER; PTHR11468; PTHR11468; 1. DR Pfam; PF00343; Phosphorylase; 1. DR TIGRFAMs; TIGR02094; more_P_ylases; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 519 Uncharacterized protein MJ1631. FT /FTId=PRO_0000188563. SQ SEQUENCE 519 AA; 60470 MW; D2C9D64C7C0D2093 CRC64; MKPTAYFCME FAIHQPLKTY AGGLGFLAGS HFRAAKRLNQ PLVGVSILWS YGYYDQLRDR EGKMKVEYIR KYYDFLEDIK LKVPVTINNN TVWVKAYKLE EDVFGTCPIY FLTTDIPEND DFSRTITHNL YDANNILHIA QQIVLGIGGY KVIKECENVK LFHMNEPHPL PLVFKLIEEY GLEYTREHTV FTTHTPLPEG NETQDINLLK SMGFFGNVDV KLAEKLGGNP FNYTVCALRV CKRANAVSKK HKEVCDRMWS WVKDRCEIVA ITNAQDKYYW QDPVIREAAK KYDIDMLRER KMELKEILFE EVADQTGKIF KKDRLTVVWA RRFTAYKRPH ILLHDEMRLL ELLKKKRIQV IWAGKPHPND HNMIATFNWI VSKTRDMKGA TILTGYELKL SKMLKQGSDI WLNTPKLNHE ASGTSGMTAS MNASIHMSTL DGWHVEWAKM YPDDSFTIGD GVRDDDAYVA NCIYNLLEEV ADMYDTERWW MKACNCVNHI VEYFDAERMA KEYAEKLYK // ID Y1632_METJA Reviewed; 255 AA. AC Q59026; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Putative glycyl-radical enzyme activating enzyme MJ1632 {ECO:0000305}; DE Short=GRE activating enzyme MJ1632 {ECO:0000305}; DE EC=1.97.1.- {ECO:0000305}; GN OrderedLocusNames=MJ1632; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:P0A9N4}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:P0A9N4}; CC -!- SIMILARITY: Belongs to the organic radical-activating enzymes CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99653.1; -; Genomic_DNA. DR PIR; F64503; F64503. DR ProteinModelPortal; Q59026; -. DR STRING; 243232.MJ_1632; -. DR EnsemblBacteria; AAB99653; AAB99653; MJ_1632. DR KEGG; mja:MJ_1632; -. DR eggNOG; arCOG00954; Archaea. DR eggNOG; COG2896; LUCA. DR InParanoid; Q59026; -. DR OMA; INCLALE; -. DR PhylomeDB; Q59026; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR001989; Radical_activat_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PROSITE; PS01087; RADICAL_ACTIVATING; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 255 Putative glycyl-radical enzyme activating FT enzyme MJ1632. FT /FTId=PRO_0000200546. FT REGION 51 53 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT REGION 134 136 S-adenosyl-L-methionine binding. FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 45 45 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 49 49 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT METAL 52 52 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:P0A9N4}. FT BINDING 88 88 S-adenosyl-L-methionine; via carbonyl FT oxygen. {ECO:0000250|UniProtKB:P0A9N4}. SQ SEQUENCE 255 AA; 29795 MW; D1F2EC1BA31D39A7 CRC64; MLNTLMLREW LRSMLRSCIS KIFGDLMLIS HISLSDKITL LTYGCNFKCK YCFFKPLSCK KYSVDEILNK ILEVNENYKL DKILIAGGEP TLQNDLSELT KLLKDEGFYL MLSTNGYYLK DMLDKLEVDE IHIDLKAYDE NKHIYLTSCS NKKVLDCISY IGKYRDEFNF KVEIDTVLIP NIVDLDEIEK IAKFLSNWDL PYRITGYVKY NNNLNAEKPD EDKILKAKEI ALKYLSNVSC SLDFKRHKKS KKVII // ID Y1638_METJA Reviewed; 260 AA. AC Q59032; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ1638; GN OrderedLocusNames=MJ1638; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99659.1; -; Genomic_DNA. DR PIR; D64504; D64504. DR ProteinModelPortal; Q59032; -. DR STRING; 243232.MJ_1638; -. DR EnsemblBacteria; AAB99659; AAB99659; MJ_1638. DR KEGG; mja:MJ_1638; -. DR eggNOG; arCOG00045; Archaea. DR eggNOG; COG1365; LUCA. DR InParanoid; Q59032; -. DR KO; K07134; -. DR OMA; YHPCGRC; -. DR PhylomeDB; Q59032; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012096; ATPase_PP-loop_MJ1638. DR InterPro; IPR022310; NAD/GMP_synthase. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF02540; NAD_synthase; 1. DR PIRSF; PIRSF006601; ATPase_UCP006601; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 260 Uncharacterized protein MJ1638. FT /FTId=PRO_0000107452. SQ SEQUENCE 260 AA; 30016 MW; 8F74C0A746676051 CRC64; MNFEKIIEEK VNQKLKELRL KNSLEILEKL DINTELKEAL KSTLLKRLNG EKEFYKISID KKPKAVVAFS GGVDSSTSAI IAKQIFDVKA VSCYSKYIMT DEMRENAKNI AKKIGISLEF VSIDLEEVYK GVVNGKFHPC GRCHKVIENA VIDYAKKIDA EFVIFGDLLA FGYLALYRED EIFRFNLPSF FALTKDEERE ILKNNGIELK MSYGCPLLKI YHKHNKGYKF TIQRILREVR GRVVNEEEGF KNIVEILNQQ // ID Y1642_METJA Reviewed; 161 AA. AC Q59036; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ1642; GN OrderedLocusNames=MJ1642; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99662.1; -; Genomic_DNA. DR PIR; H64504; H64504. DR ProteinModelPortal; Q59036; -. DR STRING; 243232.MJ_1642; -. DR EnsemblBacteria; AAB99662; AAB99662; MJ_1642. DR KEGG; mja:MJ_1642; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q59036; -. DR KO; K07013; -. DR OMA; KETHCAG; -. DR PhylomeDB; Q59036; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019642; DUF2507. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF10702; DUF2507; 1. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 161 Uncharacterized protein MJ1642. FT /FTId=PRO_0000107455. SQ SEQUENCE 161 AA; 18847 MW; CA58BE280E7B2D17 CRC64; MEELGRNVDV SIFRILRFMN LRKYIGIDNE MLMYYFGKEL SKNLNFKNFK ELSNFYKEYK LGRIEMVSEN PIKIRIYDCI SCSGLPDVGK PLCHFEAGFL AGYIENVFNK KCYIIETHCW GLGNKFCQFE VRLVDNKKSE NCFASSGDCN GYFGKNRTKK L // ID Y164_METJA Reviewed; 395 AA. AC Q57628; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0164; GN OrderedLocusNames=MJ0164; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98152.1; -; Genomic_DNA. DR PIR; E64320; E64320. DR ProteinModelPortal; Q57628; -. DR STRING; 243232.MJ_0164; -. DR EnsemblBacteria; AAB98152; AAB98152; MJ_0164. DR KEGG; mja:MJ_0164; -. DR eggNOG; arCOG06658; Archaea. DR eggNOG; COG1667; LUCA. DR KO; K09718; -. DR OMA; IDVYEYN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019249; DUF2226. DR Pfam; PF09987; DUF2226; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 395 Uncharacterized protein MJ0164. FT /FTId=PRO_0000106726. SQ SEQUENCE 395 AA; 46274 MW; 5EA400ABDCC9A412 CRC64; MRENMIKVVD GEYVKTLYEG NLEEIINEID TGYILILVKE GNKLHEGYIF VEDGKIVGCY YTDSESTEVF GNKEKVIELL NYENKVIDIY KYNKDKINLM KWLYPEIFAC KDTNKVSEKN EDMSEKRDIV EKYLNIKLDI PLDNLIEANT KDFEKYLEDN KYIIINAYRK KDGKFENGYI IYKGQTPIAA AYECDLGVLL GKDAYEKLEE MLKDENTVID VYEYNEKKTH VILELYPQMK ILDENENKSS EKADSLESEG SITTAEEIEE ESTVSREELL KKLGIKEPDE NWIETILEDV FRPSDEELEE LKEKIESEIV NKVKRMEGVS DVLVNLKIKW ENGRYYIFGD VNVKRKRILG IIKKDIDPSI VKFEIDNTIK KYVSKYTSRI NINIE // ID Y1680_METJA Reviewed; 155 AA. AC Q59074; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1680; GN OrderedLocusNames=MJ1680; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99701.1; -; Genomic_DNA. DR PIR; F64509; F64509. DR ProteinModelPortal; Q59074; -. DR STRING; 243232.MJ_1680; -. DR EnsemblBacteria; AAB99701; AAB99701; MJ_1680. DR KEGG; mja:MJ_1680; -. DR eggNOG; arCOG02120; Archaea. DR eggNOG; COG1569; LUCA. DR InParanoid; Q59074; -. DR KO; K07063; -. DR OMA; ILTWDDD; -. DR PhylomeDB; Q59074; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR002716; PIN_dom. DR InterPro; IPR029060; PIN_domain-like. DR InterPro; IPR002850; PIN_toxin-like. DR Pfam; PF13470; PIN_3; 1. DR SMART; SM00670; PINc; 1. DR SUPFAM; SSF88723; SSF88723; 1. DR TIGRFAMs; TIGR00305; TIGR00305; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein MJ1680. FT /FTId=PRO_0000107480. SQ SEQUENCE 155 AA; 17778 MW; 57D1306D3F7948C7 CRC64; MEKMEKIKIK VVIDTNVFIS ALINPNGIPG KILDLIFEEK IVNYTSPSIL KEIGFKCLSP KLRKYLGNEN RILKILTAFS SVSVIINPNT NFNVCRDEDD NKFINVAYES KAIIITGDKD LISLRDENKY LKINNIHLKV PTPKEFIEEF EKFIS // ID Y173_METJA Reviewed; 137 AA. AC Q57637; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 28-FEB-2003, sequence version 2. DT 17-FEB-2016, entry version 98. DE RecName: Full=Putative transcriptional regulatory protein MJ0173 {ECO:0000255|HAMAP-Rule:MF_00620}; GN OrderedLocusNames=MJ0173; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative transcriptional regulator. {ECO:0000255|HAMAP- CC Rule:MF_00620}. CC -!- SIMILARITY: Belongs to the Tfx family. {ECO:0000255|HAMAP- CC Rule:MF_00620}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98158.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98158.1; ALT_INIT; Genomic_DNA. DR PIR; F64321; F64321. DR ProteinModelPortal; Q57637; -. DR STRING; 243232.MJ_0173; -. DR EnsemblBacteria; AAB98158; AAB98158; MJ_0173. DR KEGG; mja:MJ_0173; -. DR eggNOG; arCOG04554; Archaea. DR eggNOG; COG1356; LUCA. DR InParanoid; Q57637; -. DR KO; K09714; -. DR OMA; LEFLYTL; -. DR PhylomeDB; Q57637; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0003677; F:DNA binding; IBA:GO_Central. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0016987; F:sigma factor activity; IBA:GO_Central. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:UniProtKB-HAMAP. DR GO; GO:0006352; P:DNA-templated transcription, initiation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IBA:GO_Central. DR Gene3D; 3.30.1190.10; -; 1. DR HAMAP; MF_00620; HTH_type_Tfx; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR007630; RNA_pol_sigma70_r4. DR InterPro; IPR029291; Tfx_C. DR InterPro; IPR004645; Tfx_DNA-bd_arc. DR InterPro; IPR018384; Tfx_DNA-bd_euryarc. DR Pfam; PF04545; Sigma70_r4; 1. DR Pfam; PF14601; TFX_C; 1. DR PIRSF; PIRSF004932; DNA_bind_Tfx; 1. DR SUPFAM; SSF89915; SSF89915; 1. DR TIGRFAMs; TIGR00721; tfx; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 137 Putative transcriptional regulatory FT protein MJ0173. FT /FTId=PRO_0000144170. SQ SEQUENCE 137 AA; 15695 MW; CDAF26114D7FAB79 CRC64; MVEDSFLTDT QIKVLKLRKK GLTQEEIAKM LGTSRANISM IEKRAKENIK KAYNTIKIYN RIMAPLSIEI EEGTDVLEIP DIVFKKADEE GIKVKYNTLE LIELIKENAS EFIEKRTVKK KFKIYILENG DLDVGGS // ID Y175_METJA Reviewed; 222 AA. AC Q57639; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0175; GN OrderedLocusNames=MJ0175; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98160.1; -; Genomic_DNA. DR PIR; H64321; H64321. DR ProteinModelPortal; Q57639; -. DR STRING; 243232.MJ_0175; -. DR EnsemblBacteria; AAB98160; AAB98160; MJ_0175. DR KEGG; mja:MJ_0175; -. DR eggNOG; arCOG04318; Archaea. DR eggNOG; COG2178; LUCA. DR InParanoid; Q57639; -. DR KO; K07477; -. DR OMA; TTDMVRG; -. DR PhylomeDB; Q57639; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR Gene3D; 1.20.58.190; -; 1. DR Gene3D; 1.20.58.200; -; 1. DR InterPro; IPR002848; Translin. DR InterPro; IPR016069; Translin_C. DR InterPro; IPR016068; Translin_N. DR PANTHER; PTHR10741; PTHR10741; 1. DR Pfam; PF01997; Translin; 1. DR SUPFAM; SSF74784; SSF74784; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 222 Uncharacterized protein MJ0175. FT /FTId=PRO_0000106729. SQ SEQUENCE 222 AA; 26426 MW; 9FBBB385C9FFD3D3 CRC64; MYKQILTIGY IKFLVVAMDE LNYLINYLAN KDSVREEILK LSREITRDCA MLIRKIHKSD DKDEFKDKLN EISEKIKKLN SLATFPEFVG YLSTPQQEFV EALSLYMIKF DNKIPSFKEL DFIKEENYIL GLADVIGELR REVLEAMKND NLAEVERYFK FMEDLYEFLM NFDYYHVVDN LRRKQDISRG ILEKTHGDIV TFIQNLKLRE HLKRVQIGLS QE // ID Y185_METJA Reviewed; 49 AA. AC Q57644; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0185; GN OrderedLocusNames=MJ0185; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98182.1; -; Genomic_DNA. DR PIR; B64323; B64323. DR STRING; 243232.MJ_0185; -. DR EnsemblBacteria; AAB98182; AAB98182; MJ_0185. DR KEGG; mja:MJ_0185; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 49 Uncharacterized protein MJ0185. FT /FTId=PRO_0000106734. FT TRANSMEM 22 42 Helical. {ECO:0000255}. SQ SEQUENCE 49 AA; 5332 MW; D1594F2AAD47CEF4 CRC64; MCYGIIVMIL FSLYKGLAPN SAIVGISIMI IIAIGIYLII EYAIKKIIG // ID Y213_METJA Reviewed; 149 AA. AC Q57666; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0213; GN OrderedLocusNames=MJ0213; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98204.1; -; Genomic_DNA. DR PIR; F64326; F64326. DR ProteinModelPortal; Q57666; -. DR STRING; 243232.MJ_0213; -. DR EnsemblBacteria; AAB98204; AAB98204; MJ_0213. DR KEGG; mja:MJ_0213; -. DR eggNOG; arCOG01042; Archaea. DR eggNOG; COG1325; LUCA. DR InParanoid; Q57666; -. DR KO; K07581; -. DR OMA; FIHATED; -. DR PhylomeDB; Q57666; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.1440.10; -; 1. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR002739; UPF0201. DR Pfam; PF01877; RNA_binding; 1. DR SUPFAM; SSF55282; SSF55282; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 149 Uncharacterized protein MJ0213. FT /FTId=PRO_0000106744. SQ SEQUENCE 149 AA; 17269 MW; 21286C2F1E190CCD CRC64; MLNSIKLSAI VHATEDEDKV LEAIEFFIPE NVDEEKIDLD VVETQGYFGN PIKIINVNVE GKEAKKIFKH IIDLIKSDDK NINKLKKDLH LRVEDNKFYV RFDKQKAYLG ECRVVDGDDI IRAVFNFKIF TPKNKEEKVK EIVANELGF // ID Y22B_METJA Reviewed; 122 AA. AC P81305; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0226.2; GN OrderedLocusNames=MJ0226.2; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98218.1; -; Genomic_DNA. DR STRING; 243232.MJ_0226.2; -. DR EnsemblBacteria; AAB98218; AAB98218; MJ_0226.2. DR KEGG; mja:MJ_0226.2; -. DR eggNOG; arCOG09659; Archaea. DR eggNOG; ENOG4111177; LUCA. DR OMA; IFALFIC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 122 Uncharacterized protein MJ0226.2. FT /FTId=PRO_0000106749. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. SQ SEQUENCE 122 AA; 14629 MW; 87ED41E0ABD17C46 CRC64; MGTMNVVGLA IYLYAGFLSF IFGFISLYAF IKYSKLERKN KEIIYVYVDN LKNFSPYMFY SILLTFTIVF VIFALFICFV FNFDLYLGLT MLFSYFLIIY LFCFKKYRVE IYKDGFYGVF QN // ID Y258_METJA Reviewed; 404 AA. AC Q57706; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0258; GN OrderedLocusNames=MJ0258; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98245.1; -; Genomic_DNA. DR PIR; C64332; C64332. DR ProteinModelPortal; Q57706; -. DR STRING; 243232.MJ_0258; -. DR EnsemblBacteria; AAB98245; AAB98245; MJ_0258. DR KEGG; mja:MJ_0258; -. DR eggNOG; arCOG02822; Archaea. DR eggNOG; COG0770; LUCA. DR InParanoid; Q57706; -. DR OMA; NINPGLD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro. DR Gene3D; 3.40.1190.10; -; 1. DR InterPro; IPR013221; Mur_ligase_cen. DR Pfam; PF08245; Mur_ligase_M; 1. DR SUPFAM; SSF53623; SSF53623; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 404 Uncharacterized protein MJ0258. FT /FTId=PRO_0000106760. FT NP_BIND 112 117 ATP. {ECO:0000255}. SQ SEQUENCE 404 AA; 46913 MW; C9FDE688807D0746 CRC64; MVFFMLIIDV NHGALTLAEE YLNLGYEVDV WDIYQKIKKS EDFKVKYQKL KEKFGNKLNL FFEQPNFEKY DRVIAPIHCP IDVDFIPFTD AVSKILKEKF GNIHKKIINV TGVKGKTTTT SLINHILKDK YSTYLHNSNF GSIAPPTILK VLNSLDIDKY DFFIFETSLG LIKCKYGAIT NVLENYKIAG GRKDALTAKF SSLKNAELSF INKRDINRYD LNINHKCLNV VDVDRAKILD KYPLKFKYFD EIFEFSKNIF GLHFVENSLF AIEICKNLVD MEEIRYRLKT FTIKNRMEIK EINKKILVKN INPGLDVKAI SYAIKDFLEV FGGDIYIGGD FGIVCEEIDV KKLSEVLKRF NCRYIFVGEI GKELLNYLNG GYIKSYDENK IKRDSLVILR EKIK // ID Y275_METJA Reviewed; 204 AA. AC Q57723; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0275; GN OrderedLocusNames=MJ0275; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98262.1; -; Genomic_DNA. DR PIR; D64334; D64334. DR ProteinModelPortal; Q57723; -. DR STRING; 243232.MJ_0275; -. DR EnsemblBacteria; AAB98262; AAB98262; MJ_0275. DR KEGG; mja:MJ_0275; -. DR eggNOG; arCOG08265; Archaea. DR eggNOG; ENOG410YYIE; LUCA. DR OMA; ISYCYYR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 204 Uncharacterized protein MJ0275. FT /FTId=PRO_0000106768. FT TRANSMEM 6 26 Helical. {ECO:0000255}. SQ SEQUENCE 204 AA; 24482 MW; 63E81963985BFA1C CRC64; MSMKKVSIIV LFILSLILTI SICGCFENEK EEVNKPNMTV IEKENIKVQN NKPIENLKEE SCKLNITNDE NRTNNITKTT KKYDFSKPVD MDKMFLNLPY NEETDFDDKI IKKYKNITFV VSRKPIDLSY AYIYNEVKEY PERDIFGNYI YYEFIPKNAN LSISYCYYRK VGNYYIIMQT YEKSRKANDL WMNWTKYVFS LFEE // ID Y296_METJA Reviewed; 203 AA. AC Q57744; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 77. DE RecName: Full=Probable metallo-hydrolase MJ0296; DE EC=3.-.-.-; GN OrderedLocusNames=MJ0296; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98284.1; -; Genomic_DNA. DR PIR; A64337; A64337. DR ProteinModelPortal; Q57744; -. DR STRING; 243232.MJ_0296; -. DR EnsemblBacteria; AAB98284; AAB98284; MJ_0296. DR KEGG; mja:MJ_0296; -. DR eggNOG; arCOG00504; Archaea. DR eggNOG; COG0491; LUCA. DR InParanoid; Q57744; -. DR OMA; KMIPPKL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 203 Probable metallo-hydrolase MJ0296. FT /FTId=PRO_0000106779. FT METAL 86 86 Zinc 1. {ECO:0000250}. FT METAL 88 88 Zinc 1. {ECO:0000250}. FT METAL 90 90 Zinc 2. {ECO:0000250}. FT METAL 91 91 Zinc 2. {ECO:0000250}. FT METAL 135 135 Zinc 1. {ECO:0000250}. FT METAL 152 152 Zinc 1. {ECO:0000250}. FT METAL 152 152 Zinc 2. {ECO:0000250}. FT METAL 193 193 Zinc 2. {ECO:0000250}. SQ SEQUENCE 203 AA; 23236 MW; 9039A9CB6DF9E75D CRC64; MIYISMFKFL FKILIGEIMI KLLYEGILIR ENGIIKKASS SSTLIITDNN NIIVDTSTKD MENIIIKGLS ELNLSPNDID VVINTHLHYD HIENNPIFKN ATFYASPKEF GFNDNFEDFK KFKDKEIEII ETPGHTYGSI SVIYKDYVVV GDASPLKNNI LKMIPPKLNV DEKLALESLK KIRKLRKNVI TGHEGIVYKE KLL // ID Y297_METJA Reviewed; 251 AA. AC Q57745; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0297; GN OrderedLocusNames=MJ0297; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98285.1; -; Genomic_DNA. DR PIR; B64337; B64337. DR ProteinModelPortal; Q57745; -. DR EnsemblBacteria; AAB98285; AAB98285; MJ_0297. DR KEGG; mja:MJ_0297; -. DR eggNOG; arCOG09664; Archaea. DR eggNOG; ENOG41110VV; LUCA. DR OMA; RIVNYME; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 251 Uncharacterized protein MJ0297. FT /FTId=PRO_0000106780. SQ SEQUENCE 251 AA; 29568 MW; 931564A2C27ADDDC CRC64; MMKYRQKDDK MNFENENALF KKALEEKEKG NYDDAIYYLD WASLIAFAKG NLQKIKEIEK ILSELVEKTD YLSLYASFFI KITNSILKKE KLPNNIIDEF FEAIEGIEEK DKEFKFVVMA LKRIVNYMEP MNQKVPEWIY EWIEDKEEMI KEVEKFNPEK DKVLIQSKDF KKGFVTGTFI GGELDKSKMK IVERAKMMFG IIEVDGAVIE IPLMAMNFTG GIFRAKGVKN EEHLNKIIKT IEDLMIDSYF Y // ID Y299_METJA Reviewed; 389 AA. AC Q57747; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0299; GN OrderedLocusNames=MJ0299; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98286.1; -; Genomic_DNA. DR PIR; D64337; D64337. DR ProteinModelPortal; Q57747; -. DR SMR; Q57747; 8-366. DR STRING; 243232.MJ_0299; -. DR EnsemblBacteria; AAB98286; AAB98286; MJ_0299. DR KEGG; mja:MJ_0299; -. DR eggNOG; arCOG04180; Archaea. DR eggNOG; COG1980; LUCA. DR InParanoid; Q57747; -. DR KO; K01622; -. DR OMA; HLVAGWM; -. DR PhylomeDB; Q57747; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002803; FBPase_V. DR Pfam; PF01950; FBPase_3; 1. DR PIRSF; PIRSF015647; FBPtase_archl; 1. DR ProDom; PD014260; FBPase_V; 1. DR SUPFAM; SSF111249; SSF111249; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 389 Uncharacterized protein MJ0299. FT /FTId=PRO_0000106782. SQ SEQUENCE 389 AA; 43246 MW; 1BB8D890F931CE73 CRC64; MSRMENNKVT ISVIKADVGG LCGHTLAPDE LLEACEAVLE EAVDEIILDY YVTRCGDDID LIMSHKLGCD NEKVHGLAWR AFEEATKVAK ELKLYGAGQD LLADSFSGNV RGMGPGCAEM EFVERKSEPI VVFCCDKTDP TAFNYPLFKM FADPFNTAGL VFDPSMISGF KFEVHDVVGH KKVFLDTPEE MYMLLALIGD YEKYAIKRVY RRRDNEIAAV VSTEKLNYIA GEYVGKDDPV AIVRAQSGFP AVGEVLEPFA NPHFVPGWMR GSHWGPLMPV GEEDATPTRF DGPARIIALG FQVCDGMLIG PNDLFADKGF DKAREKALEM ADIIRRMGPF QPHRLPATMM EYTTVPKVLE ALEDRFIPLE GLELIEEGGI TRKDRGDVE // ID Y323_METJA Reviewed; 89 AA. AC P81301; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0323; GN OrderedLocusNames=MJ0323; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98307.1; -; Genomic_DNA. DR EnsemblBacteria; AAB98307; AAB98307; MJ_0323. DR KEGG; mja:MJ_0323; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 89 Uncharacterized protein MJ0323. FT /FTId=PRO_0000106793. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 28 48 Helical. {ECO:0000255}. SQ SEQUENCE 89 AA; 9228 MW; F22EF5FDC5C2CE6C CRC64; MFLALTSIAI PAAIVIPISL IANLPNCGIS LTFSMTIGFV GLILTIAASP VFKNCGFSSM TCPVLGSNFF NNSMNVHATC AVCAWKTGV // ID Y332_METJA Reviewed; 110 AA. AC Q57778; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0332; GN OrderedLocusNames=MJ0332; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98320.1; -; Genomic_DNA. DR PIR; D64341; D64341. DR STRING; 243232.MJ_0332; -. DR EnsemblBacteria; AAB98320; AAB98320; MJ_0332. DR KEGG; mja:MJ_0332; -. DR eggNOG; arCOG09638; Archaea. DR eggNOG; ENOG4111178; LUCA. DR OMA; HGLENGT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 110 Uncharacterized protein MJ0332. FT /FTId=PRO_0000106801. SQ SEQUENCE 110 AA; 12180 MW; 88EA0EBA982A3301 CRC64; MGVSMSLWKK LDEKENQRTH NLSNSDANDR ILRVINSAFG VPDDIKEEVI AAIDKAIKHG LENGTLNYLK VIELACEGYT KEDIAEAYGH QILGAYVAVL ILTGKPLKLK // ID Y3408_METJA Reviewed; 1064 AA. AC Q60307; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJECS08; GN OrderedLocusNames=MJECS08; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37066.1; -; Genomic_DNA. DR PIR; H64516; H64516. DR ProteinModelPortal; Q60307; -. DR EnsemblBacteria; AAC37066; AAC37066; MJ_ECS08. DR KEGG; mja:MJECS08; -. DR Proteomes; UP000000805; Plasmid small ECE. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 1064 Uncharacterized protein MJECS08. FT /FTId=PRO_0000107489. SQ SEQUENCE 1064 AA; 125624 MW; 3F57ECCF0ACEA482 CRC64; MDKYVNGSIN NIQNNNVLEY TINEINQYPE DVLEVAIKLL NIRYDPNTIK ELDEHNKNNT EILGNIWLFS LNKLPLKERQ LLLKYGLWEL GAELPTDKLY RLEDAITSIL GWSFWEIHDP KEVVLKLVKA GEMLHQQNRD IKIGEIVGEE FTALHQQNND FTMLHQCGEE FTALHQQNND FTMLHQLLHN IQDNSMIEDL CNKIGERANT LKKSYKNDDC KKTAKIFTIL TFEGMRFDEF MNKAIEQLKI GEGTLKQHLK IYKQLEWIDI RKNPEDYDRK YIYLTYKFYE DIKDILDEYL PKKAFQEAEA KSEFMEDLKK SLKKFIEERL TPEGFEFDIN EVDRLKGKER IVGAYFRSLL LNEPYEAIEM IYKVYYEKYF QFKPLEINII GLETLRSRTI MTKAKDWGEF RNKLCVFRGD IAGIIHHRKS RPILRRYVCI DLDKNGNNKG CNCEVIRLYE PVENSQDYKI KCPECGRDIK YSESLFKDED GEPIKLERDL TIAIIQLKET DEVYRVYLPY TPEINNLRDV EIVGILKTNH KGEYYIEGLS INPQKTINFN YDAFVRKVKN AGYSNALDYI KDRVFYEVKA ILDKEGKNPT IDTLITLEIL ASSHIYWDKN RDGHLKPETI DCLFIGSYGQ GKSLTIEPLA KLHNTTEDMI RVDMPNIENL IGLVISRDNI KFYKKGIIPM NHNRPIFIEE MMDFILRVGN DLDLLKSGKT SGIWKREREG YNIPMIGVSP WIGVGNIKDI DLMELWEIYH LKGFEEFKEA MINYFAKKLL KQHDYDRNEA EDRAKKIVNN ILGANPQLNA SEWLLSKILD FTLKNLRGMT DRIPLIYLLK PYTNEDWKEI KLHTYKVKRL REDNNFIKQK NLEAYECALF ISYIKNKDIE FKEDALKTLW EVEEKLRDLL RDYGLFKGYS DRLFNQIEYM AKAYAKLKFK EYVDLEDVRD ALKIWFKTIL GVLLRIKAPD KVKEIFKLVG EEIKETQQKD EELEEINKLI EESRKLSQLK REILNYMLQN PKIYTTVEIA ENFNISEDTA RGILKELWKN GDVDNPESDQ WRPL // ID Y3412_METJA Reviewed; 70 AA. AC Q60311; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Uncharacterized protein MJECS12; GN OrderedLocusNames=MJECS12; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37070.1; -; Genomic_DNA. DR PIR; D64517; D64517. DR EnsemblBacteria; AAC37070; AAC37070; MJ_ECS12. DR KEGG; mja:MJ_ECS12; -. DR Proteomes; UP000000805; Plasmid small ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 70 Uncharacterized protein MJECS12. FT /FTId=PRO_0000107492. SQ SEQUENCE 70 AA; 8339 MW; 969A84B1E1CC3845 CRC64; MKSKKPNFEF ELKNYAIWYD INDAIIKESL CRYIKNILRK EFCGNCSKIK DIELKQKGKD IVVHLQFKLG // ID Y341_METJA Reviewed; 120 AA. AC Q57787; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0341; GN OrderedLocusNames=MJ0341; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98329.1; -; Genomic_DNA. DR PIR; E64342; E64342. DR STRING; 243232.MJ_0341; -. DR EnsemblBacteria; AAB98329; AAB98329; MJ_0341. DR KEGG; mja:MJ_0341; -. DR eggNOG; arCOG09646; Archaea. DR eggNOG; ENOG41111B8; LUCA. DR OMA; ALKYIPI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 120 Uncharacterized protein MJ0341. FT /FTId=PRO_0000106811. SQ SEQUENCE 120 AA; 14055 MW; 495706AA47ED311F CRC64; MDKNEFLKKL DEKFKESEQK NLEALEKIRS NLPQLEIEIF GEKLTAIIPP LSVEKEMIED AKNLEPLDFA LKYIPILYGI PKEKVEELPS IVIAELIKKY FEAYKQLNKD KSFRNRVGTK // ID Y347_METJA Reviewed; 151 AA. AC Q57793; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0347; GN OrderedLocusNames=MJ0347; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98331.1; -; Genomic_DNA. DR PIR; C64343; C64343. DR ProteinModelPortal; Q57793; -. DR STRING; 243232.MJ_0347; -. DR EnsemblBacteria; AAB98331; AAB98331; MJ_0347. DR KEGG; mja:MJ_0347; -. DR eggNOG; ENOG410Y1SB; LUCA. DR InParanoid; Q57793; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 151 Uncharacterized protein MJ0347. FT /FTId=PRO_0000106817. SQ SEQUENCE 151 AA; 16627 MW; B620EC8566457E37 CRC64; MGFDPVTFAK IKKISIDSNA DGYIDYANQA GNADKLDGKD ASDFLSIDSF KDLKEDNGYI KFPTGLIMQW GKVYVNNTTS YQEIPVNFTI EFPNKCLNVF ASIYEGSGVD NDYIKCITRI ANITTKGCVV CITDISGASG DVGFFWFAIG Y // ID Y3504_METJA Reviewed; 439 AA. AC Q60260; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Uncharacterized protein MJECL04; GN OrderedLocusNames=MJECL04; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37078.1; -; Genomic_DNA. DR PIR; D64510; D64510. DR ProteinModelPortal; Q60260; -. DR EnsemblBacteria; AAC37078; AAC37078; MJ_ECL04. DR KEGG; mja:MJECL04; -. DR HOGENOM; HOG000101642; -. DR InParanoid; Q60260; -. DR KO; K06921; -. DR OMA; EPALYNS; -. DR PhylomeDB; Q60260; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR004256; DUF234_ATPase_C. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR Pfam; PF03008; DUF234; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; Plasmid; KW Reference proteome. FT CHAIN 1 439 Uncharacterized protein MJECL04. FT /FTId=PRO_0000107496. FT NP_BIND 28 35 ATP. {ECO:0000255}. SQ SEQUENCE 439 AA; 52422 MW; AA50918A58EFC354 CRC64; MFVDREEELK ALNEKLDSNN FEFIVIYGRR RIGKTKLALK SVENREHIYY LAVEGDNLKH FKRYASKVEP TIEYAKEDWE AYFNFLKDKI IIIDEFPNLI KENPNVLSLF QRIVDIHLKN TKTKLIILGS SISMMGEKVL SYKSPLYGRK TGVLKIKPLK FKHLKEFFPK AIWEELVEIY GFADGIPYYL EKVKLPFWDY LDKEIKRVDS FLRYEVDFLM KYEFEEPTTY KKILEAIAFG NHTLGEIKNY LGFKHSDLTP YLKNLIEVEF IERQTPITES VKSKKGRYYI KDNFIAFYFR YIFPNLSAIE EGIFDIEEIK ADYNQYLGFV FEKVAKEFLI ELNKMNKLPF KFLKIGRWWH RGEEIDLIAL NDNDKKALFV EVKWKDLKDR DVKKIYRDLY RKSKLVGLDD YEKYYAIVGK KIESKENGDC LLFDLEDFS // ID Y3508_METJA Reviewed; 520 AA. AC Q60270; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 74. DE RecName: Full=Probable helicase MJECL08 {ECO:0000305}; DE EC=3.6.4.12 {ECO:0000250|UniProtKB:F2Z5Z6}; GN OrderedLocusNames=MJECL08 {ECO:0000312|EMBL:AAC37081.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000250|UniProtKB:F2Z5Z6}. CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37081.1; -; Genomic_DNA. DR PIR; H64510; H64510. DR ProteinModelPortal; Q60270; -. DR EnsemblBacteria; AAC37081; AAC37081; MJ_ECL08. DR KEGG; mja:MJECL08; -. DR HOGENOM; HOG000223323; -. DR InParanoid; Q60270; -. DR KO; K06915; -. DR OMA; WINRIAK; -. DR PhylomeDB; Q60270; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR008571; HerA. DR InterPro; IPR018538; HerA_barrel_dom. DR InterPro; IPR033186; HerA_C. DR InterPro; IPR002789; HerA_central. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR30121:SF2; PTHR30121:SF2; 1. DR Pfam; PF05872; DUF853; 1. DR Pfam; PF01935; DUF87; 1. DR Pfam; PF09378; HAS-barrel; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Plasmid; Reference proteome. FT CHAIN 1 520 Probable helicase MJECL08. FT /FTId=PRO_0000107500. FT NP_BIND 171 176 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT NP_BIND 501 502 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT BINDING 162 162 ATP. {ECO:0000250|UniProtKB:Q97WG8}. SQ SEQUENCE 520 AA; 58182 MW; D1888AFDFE1D9079 CRC64; MMVINSVVVG TVVASKNVNE FEFVIENQVI DKIKKGEFVI TKNTHGDYLL SKITKIVSVN ALIGDKSEDA SELAKIRGVI YSEEMLNNSS KFLASAKILG VINNESGSIE SNVYPINVPQ NVYLTKDDLL AKIFSNGSIE VGYLKVRSST KVKLNAKELC SRHFAVLAMT GAGKSNTIAV LVQELFEKDK GKMNIVIVDP HGEYVKMRNT HILPAKLNPI LVPEEHLAKL LGIGENSSVQ KSFLVYAALT VKYECKENKK QISGLEYLKK IEEKLVECAD KIANSEDKKR IYIEYYDGTR CRXKTVKKDD EMSINRVIEK LRWFINKNKN ILGENEGMFD IKSDKINVLP LQKIEDEEAI TIVGEFLKRV LKERIKSVHD EIVEIKALEK PTLVIIEEAH LFAAKNLKDR SGYWINRIAK EGRKFGVGLG LVSQRPKELN PTVLSQMNTK IILRIVEPTD QKYILESSEN VGEDLLQDLP QLSTGEAIVV GSSLPLPALV KIKKYDGVLG GEDGLKNLKI // ID Y3512_METJA Reviewed; 241 AA. AC Q60274; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJECL12; GN OrderedLocusNames=MJECL12; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37085.1; -; Genomic_DNA. DR PIR; D64511; D64511. DR ProteinModelPortal; Q60274; -. DR EnsemblBacteria; AAC37085; AAC37085; MJ_ECL12. DR KEGG; mja:MJECL12; -. DR HOGENOM; HOG000114780; -. DR InParanoid; Q60274; -. DR OMA; CLSGLYE; -. DR Proteomes; UP000000805; Plasmid large ECE. DR InterPro; IPR024508; DUF3226. DR Pfam; PF11536; DUF3226; 1. DR ProDom; PD038575; PD038575; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 241 Uncharacterized protein MJECL12. FT /FTId=PRO_0000107504. SQ SEQUENCE 241 AA; 27268 MW; C5D3C7742A35A097 CRC64; MRILLLEGIT DVAFFIPILK KLYGFSEISC DGIIRAEKMG DISKPICLEN EDVKLIVFHS GGKSKQKHAL TAMLTAIKMG YLSNIKILGI ARDIDQEHDV KNWTKSIIKN AGFEVKEGDK FLIIEDLNLK IAVLGIANYD EDDFNIPSFE LKRELEAVIT DMAKEISIIE KFKNSLESLS NDAERRLKPK DITHVLAIAK NFDGDSMSGL YRKFIEEQIN NKNKVNFLLT LICILPCLTI F // ID Y3516_METJA Reviewed; 70 AA. AC Q60263; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJECL16; GN OrderedLocusNames=MJECL16; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37072.1; -; Genomic_DNA. DR PIR; H64511; H64511. DR EnsemblBacteria; AAC37072; AAC37072; MJ_ECL16. DR KEGG; mja:MJECL16; -. DR PhylomeDB; Q60263; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 3: Inferred from homology; KW Complete proteome; Membrane; Plasmid; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 70 Uncharacterized protein MJECL16. FT /FTId=PRO_0000107505. FT TRANSMEM 50 70 Helical. {ECO:0000255}. SQ SEQUENCE 70 AA; 8592 MW; 47267115DB4D4E16 CRC64; MSILISNKQF NHGLKDEFAT KKDLELLEER ILRYVDNKFN QLDKKIDRTF YLLVFFIILW VSREAFFYLI // ID Y3522_METJA Reviewed; 79 AA. AC Q60259; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJECL22; GN OrderedLocusNames=MJECL22; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37093.1; -; Genomic_DNA. DR PIR; E64512; E64512. DR ProteinModelPortal; Q60259; -. DR EnsemblBacteria; AAC37093; AAC37093; MJ_ECL22. DR KEGG; mja:MJECL22; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 2.140.10.10; -; 1. DR InterPro; IPR002372; PQQ_repeat. DR InterPro; IPR027295; Quinoprotein_ADH-like_fam. DR InterPro; IPR011047; Quinoprotein_ADH-like_supfam. DR Pfam; PF01011; PQQ; 1. DR SUPFAM; SSF50998; SSF50998; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 79 Uncharacterized protein MJECL22. FT /FTId=PRO_0000107510. SQ SEQUENCE 79 AA; 9201 MW; 3C7D0F6F65B7AE2D CRC64; MLELRSLSIR GGIAVLECGR RCISAINLKT GDKIWEFKTE WDIESISIKD NRVMLKCNGR RHIYIDLKTG RKIRELIIL // ID Y366_METJA Reviewed; 92 AA. AC Q57812; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0366; GN OrderedLocusNames=MJ0366; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98357.1; -; Genomic_DNA. DR PIR; F64345; F64345. DR PDB; 2EFV; X-ray; 1.90 A; A=1-92. DR PDBsum; 2EFV; -. DR ProteinModelPortal; Q57812; -. DR SMR; Q57812; 6-87. DR STRING; 243232.MJ_0366; -. DR EnsemblBacteria; AAB98357; AAB98357; MJ_0366. DR KEGG; mja:MJ_0366; -. DR eggNOG; arCOG05030; Archaea. DR eggNOG; ENOG410ZAP0; LUCA. DR OMA; NCELVKL; -. DR EvolutionaryTrace; Q57812; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR InterPro; IPR024254; DUF2540. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR Pfam; PF10802; DUF2540; 1. DR ProDom; PD015174; PD015174; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 92 Uncharacterized protein MJ0366. FT /FTId=PRO_0000106835. FT STRAND 12 19 {ECO:0000244|PDB:2EFV}. FT HELIX 23 32 {ECO:0000244|PDB:2EFV}. FT HELIX 33 35 {ECO:0000244|PDB:2EFV}. FT HELIX 41 49 {ECO:0000244|PDB:2EFV}. FT STRAND 54 59 {ECO:0000244|PDB:2EFV}. FT HELIX 62 71 {ECO:0000244|PDB:2EFV}. FT HELIX 72 74 {ECO:0000244|PDB:2EFV}. FT HELIX 75 86 {ECO:0000244|PDB:2EFV}. SQ SEQUENCE 92 AA; 10854 MW; CCB9B3E16BAF403A CRC64; MPLVGFMKEK KRATFYLYKN IDGRKLRYLL HKLENVENVD IDTLRRAIEA EKKYKRSITL TEEEEVIIQR LGKSANLLLN CELVKLDEGE RA // ID Y388_METJA Reviewed; 207 AA. AC Q57833; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0388; GN OrderedLocusNames=MJ0388; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98374.1; -; Genomic_DNA. DR PIR; D64348; D64348. DR ProteinModelPortal; Q57833; -. DR STRING; 243232.MJ_0388; -. DR EnsemblBacteria; AAB98374; AAB98374; MJ_0388. DR KEGG; mja:MJ_0388; -. DR eggNOG; arCOG00908; Archaea. DR eggNOG; COG3286; LUCA. DR InParanoid; Q57833; -. DR KO; K09742; -. DR OMA; ISSKVSC; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019202; DUF2067. DR Pfam; PF09840; DUF2067; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 207 Uncharacterized protein MJ0388. FT /FTId=PRO_0000106850. SQ SEQUENCE 207 AA; 24118 MW; F33B51B95271F6D7 CRC64; MRKIISSKVS CDEELLELCE RLSRMDIDCT IESKGNRVRV YVFGYDKDSL KXNYRTIREV MEKVKRKYQK DDEGLYKYPL FELKYPVNKN LIIDALKTLG YKVIYLEDEN AIKTNVDINK FNEILGELHE LSQELRFSNL GSKPVKNLVV LVSYITKKPV DDVIEEALEK GFFREEEGRI VLNKDINLAK KALLEGEDGD KDIGEER // ID Y419_METJA Reviewed; 354 AA. AC Q57862; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Uncharacterized protein MJ0419; GN OrderedLocusNames=MJ0419; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98417.1; -; Genomic_DNA. DR PIR; C64352; C64352. DR ProteinModelPortal; Q57862; -. DR STRING; 243232.MJ_0419; -. DR EnsemblBacteria; AAB98417; AAB98417; MJ_0419. DR KEGG; mja:MJ_0419; -. DR eggNOG; arCOG03206; Archaea. DR eggNOG; COG1822; LUCA. DR InParanoid; Q57862; -. DR OMA; LLGYRTQ; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002760; O_anti_polymase. DR Pfam; PF01901; O_anti_polymase; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 354 Uncharacterized protein MJ0419. FT /FTId=PRO_0000106865. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 278 298 Helical. {ECO:0000255}. FT TRANSMEM 306 326 Helical. {ECO:0000255}. FT TRANSMEM 327 347 Helical. {ECO:0000255}. SQ SEQUENCE 354 AA; 40036 MW; D6C7180C6418A641 CRC64; MLLLHWDNMG KIELHHVFVM LSCIYLIFSD ISINSAVVFL FSSIFFYISF TAGKRLYYLI GIDKENLKIN LKKHYNFGIF LMIVGLIAVT SDLIWVKDVP LFNPLSRKFL NVYFTTLSHL FLVGWAIVVA SSNIDKKKIL LYTIIFSILI MLLGYRTNVL VLLISVGAIL YYKNKISNRE ILKYGILVFV ILLGLSILRL YALGVEGNPI TSRISLTMSI YDIIFNNFNG VFNGYIHYSA VFSYLGLCNG ARTVIAKTLG IYNVSITPTI VGAVIGDYGT LAIIPYFGIL GIFLGFFYKL AKDVKGIYLG IYGILFAYTL IGIESGILDI DVILYYFFGL ILCIYAILLR KLKR // ID Y425_METJA Reviewed; 140 AA. AC Q57868; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0425; GN OrderedLocusNames=MJ0425; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98412.1; -; Genomic_DNA. DR PIR; A64353; A64353. DR STRING; 243232.MJ_0425; -. DR EnsemblBacteria; AAB98412; AAB98412; MJ_0425. DR KEGG; mja:MJ_0425; -. DR eggNOG; arCOG03171; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004518; F:nuclease activity; IEA:InterPro. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR Gene3D; 3.40.1350.10; -; 1. DR InterPro; IPR004256; DUF234_ATPase_C. DR InterPro; IPR011335; Restrct_endonuc-II-like. DR InterPro; IPR011856; tRNA_endonuc-like_dom. DR Pfam; PF03008; DUF234; 1. DR SUPFAM; SSF52980; SSF52980; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MJ0425. FT /FTId=PRO_0000106870. SQ SEQUENCE 140 AA; 16447 MW; 280D4027E1D06ED7 CRC64; MVQVVYPNMA DLEIGNVKEV YNKILASLNE YYGKMFENLV FEMLKLKIID FGQKSVAKWW HKGEEIDVLA YNNNKMIAFE VKWKDLSFKE AKGILRDLER KLDKVDFDGE KECYIIAKSI EGKEKLKALD LMDLEKLIIF // ID Y433_METJA Reviewed; 175 AA. AC Q57875; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0433; GN OrderedLocusNames=MJ0433; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98433.1; -; Genomic_DNA. DR PIR; A64354; A64354. DR ProteinModelPortal; Q57875; -. DR STRING; 243232.MJ_0433; -. DR EnsemblBacteria; AAB98433; AAB98433; MJ_0433. DR KEGG; mja:MJ_0433; -. DR eggNOG; arCOG09667; Archaea. DR eggNOG; ENOG410YKVX; LUCA. DR OMA; CYFDKIF; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 175 Uncharacterized protein MJ0433. FT /FTId=PRO_0000106874. SQ SEQUENCE 175 AA; 20494 MW; 54DFCBA805D0EDAE CRC64; MDAKEILELV EESYKSEDGD YKNKVYFISY FLSSLIFVLI HISIKYWNFN ILFIVSLLLI IGSILIVRQQ KLYKKTRCYF DKIFEKIVKY GMIAVVLSSV ITLYTYPRIS GVAIAGIFGF LLVIDGILFK SKKRKFLGLL MMFSSIPMFI FHEYQFLIFA FVQFLVALCF LICKE // ID Y450_METJA Reviewed; 186 AA. AC Q57892; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0450; GN OrderedLocusNames=MJ0450; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98439.1; -; Genomic_DNA. DR PIR; B64356; B64356. DR ProteinModelPortal; Q57892; -. DR STRING; 243232.MJ_0450; -. DR EnsemblBacteria; AAB98439; AAB98439; MJ_0450. DR KEGG; mja:MJ_0450; -. DR eggNOG; arCOG00606; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q57892; -. DR OMA; PVLLIMK; -. DR PhylomeDB; Q57892; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 186 Uncharacterized protein MJ0450. FT /FTId=PRO_0000106881. FT DOMAIN 10 69 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 77 133 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 186 AA; 20791 MW; 472E1C56DDB607AB CRC64; MVGEIPVLLI MKKPIVVSGD VSVYDVAKLM VEQDVPCVLV VCERPNHESI EVATDKDIIK KVLIRKLPPD KVKVEDISSG KLVTIPPNTT IDEALEIMNK YKTNELFIVD DGKIVGVITE EDLIKIAPEI ISTLKELVNY LLQIIDEVTS GDISDKSKEI QNINQGKDNK KDSESDIRKK KIMLIK // ID Y456_METJA Reviewed; 352 AA. AC Q57898; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Uncharacterized transporter MJ0456; GN OrderedLocusNames=MJ0456; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98444.1; -; Genomic_DNA. DR PIR; H64356; H64356. DR ProteinModelPortal; Q57898; -. DR STRING; 243232.MJ_0456; -. DR EnsemblBacteria; AAB98444; AAB98444; MJ_0456. DR KEGG; mja:MJ_0456; -. DR eggNOG; arCOG00237; Archaea. DR eggNOG; COG0471; LUCA. DR InParanoid; Q57898; -. DR OMA; LTFICFF; -. DR PhylomeDB; Q57898; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR InterPro; IPR004680; Cit_transptr-like_dom. DR Pfam; PF03600; CitMHS; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 352 Uncharacterized transporter MJ0456. FT /FTId=PRO_0000106885. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 226 246 Helical. {ECO:0000255}. FT TRANSMEM 291 311 Helical. {ECO:0000255}. FT TRANSMEM 330 350 Helical. {ECO:0000255}. SQ SEQUENCE 352 AA; 40636 MW; A18197DC93B24412 CRC64; MKIDTFIFLM FISIGILLLL LNIINPMEVF HIVEWKTIFS LFYLMVIINI MRDTKFLDYI SLKILKKSKR IFIALIFLTL FLSSLITNDV SLFVIIPLTL IIHRYTNMPF KDLEKLIIFE GVSANIGSGL TPIGNPQNLF LFHFYNIGTL EFIINMIPFE IFGILAILPF LEFKKYDTKI NIDIKFKKEW IFYILSFILV LLCVFGYLNF IYILPLILAI LMYKRVKVDY LFLLTFIFLF VDIEGLKRIG IINIFSIKCG NVMLMIYASL LSQIISNVPA TVLLSHLYKN WLPIAYGVNI GGNGTLIASF ANLITLRLSN GNVRVGRFLL IGGIIYIMHL IVLVAYAKIF WV // ID Y482_METJA Reviewed; 240 AA. AC Q57905; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Uncharacterized protein MJ0482; GN OrderedLocusNames=MJ0482; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98473.1; -; Genomic_DNA. DR PIR; A64360; A64360. DR ProteinModelPortal; Q57905; -. DR STRING; 243232.MJ_0482; -. DR DNASU; 1451343; -. DR EnsemblBacteria; AAB98473; AAB98473; MJ_0482. DR KEGG; mja:MJ_0482; -. DR eggNOG; arCOG02408; Archaea. DR eggNOG; COG1432; LUCA. DR InParanoid; Q57905; -. DR OMA; GEIMWKK; -. DR PhylomeDB; Q57905; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.1010; -; 1. DR InterPro; IPR002790; CHP00288. DR InterPro; IPR021139; NYN_limkain-b1. DR InterPro; IPR029060; PIN_domain-like. DR Pfam; PF01936; NYN; 1. DR TIGRFAMs; TIGR00288; TIGR00288; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 240 Uncharacterized protein MJ0482. FT /FTId=PRO_0000106890. SQ SEQUENCE 240 AA; 27868 MW; 3192B56BDBE60D48 CRC64; MKSPHKVIYC YLIILYKLSS CHIYYKYIPF RLTVLVNYFL LLNVGEIMWK KLESLTSKIY EKARKRKGEH RIALLIDGPN MLRKEFNIDL DKIREVLSEF GDIVIGRVYL NQYASDKLIE AVINQGFEPK ISAGDVDVEM AVDATELVFN PNIDTIAYVT RDADFLPAIR KAKERGKKVI VIGAEPGFST ALQNIADYVI KIGEEFQLDR EKLEKKKKNK FLKVEEKQKD KEETENREEP // ID Y505_METJA Reviewed; 250 AA. AC Q57928; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0505; GN OrderedLocusNames=MJ0505; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98501.1; -; Genomic_DNA. DR PIR; A64363; A64363. DR ProteinModelPortal; Q57928; -. DR STRING; 243232.MJ_0505; -. DR EnsemblBacteria; AAB98501; AAB98501; MJ_0505. DR KEGG; mja:MJ_0505; -. DR eggNOG; arCOG05033; Archaea. DR eggNOG; COG3233; LUCA. DR InParanoid; Q57928; -. DR KO; K06986; -. DR OMA; HDVSPVY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016810; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds; IEA:InterPro. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.370; -; 2. DR InterPro; IPR018763; DUF2334. DR InterPro; IPR011330; Glyco_hydro/deAcase_b/a-brl. DR InterPro; IPR002509; NODB_dom. DR Pfam; PF10096; DUF2334; 1. DR SUPFAM; SSF88713; SSF88713; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 250 Uncharacterized protein MJ0505. FT /FTId=PRO_0000106904. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 250 AA; 29848 MW; 5A645296E7E2E153 CRC64; MNKFKYLLFL VVFAVFFLTF AFFDNSSKSH QDDDEQKPII LIHDVSPVYF KELKEIVKII DKYHYQNRSY LFLIVNHANK YNLKNYPEFV DYLHKLEKEG YHIEFHAYNH IDDEFNCNKT VAEEKLNKSF KILEECGFNP KKIKYFIPPR YKLSEDAEKL FLGRNITIIL ENKMITEKDG KIVEISITNR EYTWYLPKPL VKVAEKIATT DYKLSIKENR KFFLSIHPKA VNYGSGLEFL DYFLNETSKN // ID Y514_METJA Reviewed; 250 AA. AC Q57934; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ0514; GN OrderedLocusNames=MJ0514; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 6 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98503.1; -; Genomic_DNA. DR PIR; B64364; B64364. DR ProteinModelPortal; Q57934; -. DR STRING; 243232.MJ_0514; -. DR EnsemblBacteria; AAB98503; AAB98503; MJ_0514. DR KEGG; mja:MJ_0514; -. DR eggNOG; arCOG00958; Archaea. DR eggNOG; COG1145; LUCA. DR InParanoid; Q57934; -. DR OMA; CEICAQT; -. DR PhylomeDB; Q57934; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF00037; Fer4; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 6. DR PROSITE; PS51379; 4FE4S_FER_2; 6. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 250 Uncharacterized polyferredoxin-like FT protein MJ0514. FT /FTId=PRO_0000159148. FT DOMAIN 38 67 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 69 98 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 124 153 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 154 183 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 191 220 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 220 249 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 47 47 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 50 50 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 53 53 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 57 57 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 78 78 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 81 81 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 84 84 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 88 88 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 133 133 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 136 136 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 139 139 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 143 143 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 163 163 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 166 166 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 169 169 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 173 173 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 200 200 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 203 203 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 206 206 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 210 210 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 229 229 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 232 232 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 235 235 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 239 239 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 250 AA; 28246 MW; 5C4D611D53ED2960 CRC64; MITLIEIKKS LDEILSKIDG DKKYINEVAK KITPITYKLL YINETKCIRC NLCYKECPVD AIEKAKVKKS AKIIEDKCVK CEICAQTCPV GAIYVIEGRA EIEDSEVHYT IKEKSIPHRK IRLKKYELDE NTCIKCGICA RFCPTNAIKA VRRKSIEVNL DLCMGCGACA EVCPKKCIKV ERELGEVIKT RDIEVDKNLC VGCLVCIEEC PINAIDQDGD KVKINKDKCI LCGRCVDVCP TNAIKMWEKK // ID Y518_METJA Reviewed; 94 AA. AC Q57938; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0518; GN OrderedLocusNames=MJ0518; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98507.1; -; Genomic_DNA. DR PIR; F64364; F64364. DR STRING; 243232.MJ_0518; -. DR EnsemblBacteria; AAB98507; AAB98507; MJ_0518. DR KEGG; mja:MJ_0518; -. DR eggNOG; arCOG04834; Archaea. DR eggNOG; COG4035; LUCA. DR KO; K14103; -. DR OMA; MNEVPFM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019211; DUF2104_membrane. DR InterPro; IPR011305; Prd_NiFe_hyd_3_EhaL. DR Pfam; PF09877; DUF2104; 1. DR PIRSF; PIRSF004953; EhaL; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 94 Uncharacterized protein MJ0518. FT /FTId=PRO_0000106908. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. SQ SEQUENCE 94 AA; 10552 MW; BD9002A28C1B2D73 CRC64; MGLFELNLAI ILFIIGNFIG LEYSYRKYSS PYVEKGIDKF ALAISVFGGI LINSPLYMLG CLLIGFPLGM RPGYGRVEFV VGLAVALFLY FLRW // ID Y520_METJA Reviewed; 295 AA. AC Q57940; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Putative NADH-ubiquinone oxidoreductase MJ0520; DE EC=1.6.5.3; GN OrderedLocusNames=MJ0520; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: NADH + ubiquinone + 5 H(+)(In) = NAD(+) + CC ubiquinol + 4 H(+)(Out). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the complex I subunit 1 family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98508.1; -; Genomic_DNA. DR PIR; H64364; H64364. DR ProteinModelPortal; Q57940; -. DR STRING; 243232.MJ_0520; -. DR EnsemblBacteria; AAB98508; AAB98508; MJ_0520. DR KEGG; mja:MJ_0520; -. DR eggNOG; arCOG01545; Archaea. DR eggNOG; COG0650; LUCA. DR InParanoid; Q57940; -. DR KO; K14101; -. DR OMA; TEHYGLL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:UniProtKB-EC. DR InterPro; IPR001694; NADH_UbQ_OxRdtase_su1/FPO. DR PANTHER; PTHR11432; PTHR11432; 1. DR Pfam; PF00146; NADHdh; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; NAD; Oxidoreductase; KW Reference proteome; Transmembrane; Transmembrane helix; Ubiquinone. FT CHAIN 1 295 Putative NADH-ubiquinone oxidoreductase FT MJ0520. FT /FTId=PRO_0000117536. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 129 149 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. SQ SEQUENCE 295 AA; 31909 MW; F9903DBC914DFAD6 CRC64; MMLMDTSLIG AINLTIHAFL VGSLLLGLHR KIMARIQGRP GPPIIQYLLH TLKFYVKEIT FPITAGNPLY IFVALLDIAI WLAALIIAID FKSSLLIIIG IYVLQKIVEH GCGLSSGSPY GKIGGVRSVF SAAAEVPLFA VVAAIYLTTH SVLISDILSY QEIHGSLLFK MPICAFAFFI LLVSKAPNSP FGIVKGKDIV SGYMTEHYGL LGAIIYIAEA IAYFVLLWLF IAVFIGPLVI NSPVLTLAVM VVMTVILAFV NGLTPLLAPH HSVMLQMTIA GLVLCDVLYR LIVGG // ID Y1245_METJA Reviewed; 112 AA. AC Q58642; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ1245; GN OrderedLocusNames=MJ1245; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1244 and M.thermoautotrophicum CC MTH1110. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99257.1; -; Genomic_DNA. DR PIR; D64455; D64455. DR STRING; 243232.MJ_1245; -. DR EnsemblBacteria; AAB99257; AAB99257; MJ_1245. DR KEGG; mja:MJ_1245; -. DR eggNOG; arCOG03424; Archaea. DR eggNOG; COG4075; LUCA. DR OMA; NERWTVM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR024184; UCP005637. DR InterPro; IPR019296; Unchr_N-regulatory-PII-rel. DR Pfam; PF10126; Nit_Regul_Hom; 1. DR PIRSF; PIRSF005637; UCP005637; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 112 Uncharacterized protein MJ1245. FT /FTId=PRO_0000107236. SQ SEQUENCE 112 AA; 13105 MW; F605E8244C6C5B71 CRC64; MTKRVLFELF VEEKNVGKAI NIMTLAGITG FFLHKYRGLS PDKFKNLSKE ELEDIEKVYE IIRDESDKAV VIGTVVKEEK AKKIEELLKE KMNNERWTVM KIPILKVKVH RV // ID Y124_METJA Reviewed; 1075 AA. AC Q57588; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein MJ0124; GN OrderedLocusNames=MJ0124; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1214. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98104.1; -; Genomic_DNA. DR ProteinModelPortal; Q57588; -. DR STRING; 243232.MJ_0124m; -. DR REBASE; 3900; MjaORF132P. DR PRIDE; Q57588; -. DR EnsemblBacteria; AAB98104; AAB98104; MJ_0124. DR eggNOG; arCOG00878; Archaea. DR eggNOG; COG0610; LUCA. DR InParanoid; Q57588; -. DR OMA; LFRFVQF; -. DR PhylomeDB; Q57588; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0009035; F:Type I site-specific deoxyribonuclease activity; IEA:InterPro. DR GO; GO:0009307; P:DNA restriction-modification system; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 3. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007409; Restrct_endonuc_type1_HsdR_N. DR InterPro; IPR004473; Restrct_endonuc_typeI_HsdR. DR Pfam; PF04313; HSDR_N; 1. DR Pfam; PF04851; ResIII; 2. DR SMART; SM00487; DEXDc; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR TIGRFAMs; TIGR00348; hsdR; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 1075 Uncharacterized protein MJ0124. FT /FTId=PRO_0000106704. SQ SEQUENCE 1075 AA; 127797 MW; 4F765E19E0B52889 CRC64; MDYLKYGIEV VVKKSEKRKF KLIDYKNIDK NTFFYLCEAE FKGNPKNSRP DITLFINGIP VVIIEAKATL KIDSHLEGIS QIRRYEKFSP DLFRFVQFAI SYGEEQLYTP TMPNWYKENI HLPAYYWRIR QKINGKKVVK DDIFYILNPS ILLEIIRYFI FYRKDEYSKT KTLSKIIARY NQYFATKKAM KRIDEYLSGD SKNKGLIWHW QGSGKTYTMF FIANYFLDKY FSENPVIFFV VDRVDLERQS KEFYEAIQEK KFKTILKRID SINKLYEVIK SIKMSELSNK VIVRGIYTTT IQKFQYERSK KEKDNNKEKD KDDEDLDLSK PIEEIIKKIE DKLKKEEKEG KIKGLKDLLI ILAFIYLKHL KEKNPEEYKK HIENLKKLKD KDKKEEYLIN LGNIKRKHIL ILIDEAHRTQ YGILGGMRKI TFPNAITFGF TGTPVFKNEK NTFTEFSYPE KGEFYLDVYF IGDSIKDKFT LPLTYQIVKE GDIKSEGIQI TLDEEDIKEF IDEWIKRGED INLFDRKKLP KYINKSKTIL LNPKRIDKVA KYIVDRIEED TENFKFKAMV VAVNRLGCVR FKKALDKYLK EKFGDEAEKW AEVVMTYHHN EEEKEIIEYM KKLKKERNSN DFNEINQIIR EEFLNSENPK ILIVTDMLLT GFDAPRLKVM YLDKPLYGHR LLQAIARTNR PYPDKEFGLI VDSVGLFKVL TETMALYNML AEEEIREDFK NNLISSIDEI FQEFKLKLEM VKESLKNLKI NDEDLSIDVN TLKTLTKNKD FNNNELKEKL DLIAFYAEDG KNARILKLID DLKAVIKLYK ALGSYPQKIF YIEDIELLSF IYAYLIKKLK PKKKSNRKFW EELISFIHNK MLVDDLTVIE EINLNPDDLD KILKENIGKR EIKRAVANYY FILKNSILDK QHDPIYKEIL ERLERLRRDW IMKRIDDKIY LNAIKNLMEL KNNYDKKIKG KSSIERIKES ISTYIGENIL KDQDIKLNLE NTEKLITKMQ NLNKLSKLQR KKFKKELSCA LLEDLLKELK GKIKDEDAKK VAELSDNLVS EFILKEIWGE NYENQ // ID Y1266_METJA Reviewed; 417 AA. AC Q58662; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ1266; DE Flags: Precursor; GN OrderedLocusNames=MJ1266; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99272.1; -; Genomic_DNA. DR PIR; A64458; A64458. DR ProteinModelPortal; Q58662; -. DR STRING; 243232.MJ_1266; -. DR EnsemblBacteria; AAB99272; AAB99272; MJ_1266. DR KEGG; mja:MJ_1266; -. DR eggNOG; arCOG01021; Archaea. DR eggNOG; COG0683; LUCA. DR InParanoid; Q58662; -. DR KO; K01999; -. DR OMA; YAYNAYD; -. DR PhylomeDB; Q58662; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR028081; Leu-bd. DR InterPro; IPR028082; Peripla_BP_I. DR Pfam; PF13458; Peripla_BP_6; 1. DR SUPFAM; SSF53822; SSF53822; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 21 {ECO:0000255}. FT CHAIN 22 417 Uncharacterized protein MJ1266. FT /FTId=PRO_0000014010. SQ SEQUENCE 417 AA; 46249 MW; DD8E13FDB556EF40 CRC64; MPYYWGAILI GGVFLAGCTQ NQETTTTQSG SKENVIKVGL LVDLSGGLAT YGNNEKHICE IAEEKINKYF EEKGMPYKVK LYVEDTRADP NICLQKVQAL HAQGITFFLG PMASGEVKNI KGFINSNKIV IISPSSTAPP QMLGFRTPEE KKYVFRFVPT DNFQGNAIGD VAKQLGLKNV IVIYRKDAWG DGLERATVEK LKANGINIID EIPYDPNIGD WSPIIQTTTN KIAGKGNDTG VIFIGYEEVA TLLSQIDDNS PLLKHVWIGC DGTANSKKVL EEAKNKAVKV KLYSTMFQSE TDEAEKIKEE FKKRGYGEPD QYALNVYDAF WVGAISYAEM LNKTGGKYDA DLLSKLIKEN TVKYSEGQFG VKSVTGYIKL NEWNDRASGN YGIFAVTEDG WKLVGVWDST TGKINWK // ID Y1280_METJA Reviewed; 157 AA. AC Q58676; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1280; GN OrderedLocusNames=MJ1280; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99286.1; -; Genomic_DNA. DR PIR; G64459; G64459. DR STRING; 243232.MJ_1280; -. DR EnsemblBacteria; AAB99286; AAB99286; MJ_1280. DR KEGG; mja:MJ_1280; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 157 Uncharacterized protein MJ1280. FT /FTId=PRO_0000107248. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. SQ SEQUENCE 157 AA; 17732 MW; 1340F75DAEE5B530 CRC64; MNLILTLLII FAIIGLLILI FGIWLIKKLL FPKKKPKPYQ VRHGSSSSKR GYGSHDVYHH HYVTKDVYVH DYGDDDIYDE RGKKEGDKDD SLIDKAIAFG AGAVTGYGVA EYGEEIKEEV EDIVKEGEDI IDDIVEEAED FVEDVVDDFD NGGDDDY // ID Y1308_METJA Reviewed; 108 AA. AC Q58704; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ1308; GN OrderedLocusNames=MJ1308; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99328.1; -; Genomic_DNA. DR PIR; C64463; C64463. DR ProteinModelPortal; Q58704; -. DR STRING; 243232.MJ_1308; -. DR EnsemblBacteria; AAB99328; AAB99328; MJ_1308. DR KEGG; mja:MJ_1308; -. DR eggNOG; arCOG05076; Archaea. DR eggNOG; ENOG410YU0U; LUCA. DR KO; K14116; -. DR OMA; YQLFWLS; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 108 Uncharacterized protein MJ1308. FT /FTId=PRO_0000107266. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. SQ SEQUENCE 108 AA; 12336 MW; 6EAD33F5583B8A09 CRC64; MVDFMDYNDF QKKLDKEEHG DGITVGAVYT GEFTLYLLFI FGALIIGRVY GKTLMTLFGL AALAFSLSVS PLIFKFKEEN SNAINYQLFW LSIFLGAIAF CIYMTTRW // ID Y1316_METJA Reviewed; 80 AA. AC Q58712; DT 20-JUN-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=UPF0248 protein MJ1316 {ECO:0000255|HAMAP-Rule:MF_01245}; GN OrderedLocusNames=MJ1316; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0248 family. {ECO:0000255|HAMAP- CC Rule:MF_01245}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99323.1; -; Genomic_DNA. DR PIR; C64464; C64464. DR STRING; 243232.MJ_1316; -. DR EnsemblBacteria; AAB99323; AAB99323; MJ_1316. DR KEGG; mja:MJ_1316; -. DR eggNOG; arCOG01302; Archaea. DR eggNOG; COG1531; LUCA. DR InParanoid; Q58712; -. DR KO; K09715; -. DR OMA; NKIFWHP; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01245; UPF0248; 1. DR InterPro; IPR007547; UPF0248. DR Pfam; PF04457; DUF504; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 80 UPF0248 protein MJ1316. FT /FTId=PRO_0000053413. SQ SEQUENCE 80 AA; 9683 MW; D39072CF898CC1CE CRC64; MGIFMLKEIL NKIFWHPDYK REDFEVVILH RGAEENKKAI SLDDVELKGN YLIYFDTYIP LHRILEIRNK KTGEILYKKK // ID Y1330_METJA Reviewed; 127 AA. AC Q58726; DT 26-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1330; GN OrderedLocusNames=MJ1330; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99339.1; -; Genomic_DNA. DR PIR; A64466; A64466. DR ProteinModelPortal; Q58726; -. DR STRING; 243232.MJ_1330; -. DR EnsemblBacteria; AAB99339; AAB99339; MJ_1330. DR KEGG; mja:MJ_1330; -. DR eggNOG; arCOG01869; Archaea. DR eggNOG; COG1267; LUCA. DR InParanoid; Q58726; -. DR OMA; GCMSKVF; -. DR PhylomeDB; Q58726; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008962; F:phosphatidylglycerophosphatase activity; IEA:InterPro. DR GO; GO:0006629; P:lipid metabolic process; IEA:InterPro. DR Gene3D; 1.10.3760.10; -; 1. DR InterPro; IPR027416; YutG-like. DR InterPro; IPR007686; YutG/PgpA. DR Pfam; PF04608; PgpA; 1. DR SUPFAM; SSF101307; SSF101307; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 127 Uncharacterized protein MJ1330. FT /FTId=PRO_0000107277. SQ SEQUENCE 127 AA; 14151 MW; F33BC568A9CDF378 CRC64; MDAGMDLYIG SNEERDRVKE KLKEILLKQL SNPNVSTLLI AAILLDNEGR ANNLPFNYNE DPNYVYVDEV IGLAIANEIA GTKAIFNFRF YDAKKPGIIG ELDRKGFMFL DDAIAGLLAG CMSKVFE // ID Y133_METJA Reviewed; 273 AA. AC Q57597; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ0133; GN OrderedLocusNames=MJ0133; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98114.1; -; Genomic_DNA. DR PIR; E64316; E64316. DR ProteinModelPortal; Q57597; -. DR STRING; 243232.MJ_0133; -. DR DNASU; 1450974; -. DR EnsemblBacteria; AAB98114; AAB98114; MJ_0133. DR KEGG; mja:MJ_0133; -. DR eggNOG; arCOG01894; Archaea. DR eggNOG; COG0648; LUCA. DR InParanoid; Q57597; -. DR KO; K01151; -. DR OMA; HIHISGI; -. DR PhylomeDB; Q57597; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) lyase activity; IBA:GO_Central. DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central. DR Gene3D; 3.20.20.150; -; 1. DR InterPro; IPR001719; AP_endonuc_2. DR InterPro; IPR013022; Xyl_isomerase-like_TIM-brl. DR PANTHER; PTHR21445; PTHR21445; 1. DR Pfam; PF01261; AP_endonuc_2; 1. DR SMART; SM00518; AP2Ec; 1. DR SUPFAM; SSF51658; SSF51658; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 273 Uncharacterized protein MJ0133. FT /FTId=PRO_0000106711. SQ SEQUENCE 273 AA; 31386 MW; 87069E801903BC49 CRC64; MNREIMLIFG TAGVPISAED EFKAVDVLRK LNLGAMELEF VKGVYMKEDY AKKLKEYGED IIFSAHAPHY INLNANEEEK VENSIRRIIK TAKVLNNCGK NLVFHPGYYL KRSKEVTYNR IKSNIQRILD KLEALNLNVM LRPETTGKTT QFGDIDETLK LCFELNILPC IDFSHIYARS RGVINDYNSF YKILEKVENV LGKEAIKDMH IHLSGIEYGK GGERRHLPLN ESNFNYRDVL KALKDFDASG TVICESPMLE YDAVLLMKCY NEL // ID Y1348_METJA Reviewed; 336 AA. AC Q58743; DT 13-DEC-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1348; GN OrderedLocusNames=MJ1348; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP DISCUSSION OF SEQUENCE. RX PubMed=9697413; DOI=10.1016/S0968-0004(98)01228-6; RA Kyrpides N.C., Woese C.R.; RT "Tetratrico-peptide-repeat proteins in the archaeon Methanococcus RT jannaschii."; RL Trends Biochem. Sci. 23:245-247(1998). CC -!- CAUTION: PubMed:9697413 reported that this sequence contains TPR CC repeats. These are not detected using our methodology. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99360.1; -; Genomic_DNA. DR PIR; C64468; C64468. DR ProteinModelPortal; Q58743; -. DR STRING; 243232.MJ_1348; -. DR EnsemblBacteria; AAB99360; AAB99360; MJ_1348. DR KEGG; mja:MJ_1348; -. DR eggNOG; arCOG09679; Archaea. DR eggNOG; ENOG41111N2; LUCA. DR OMA; KGCEFYN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR011716; TPR-3. DR Pfam; PF07720; TPR_3; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 336 Uncharacterized protein MJ1348. FT /FTId=PRO_0000107289. SQ SEQUENCE 336 AA; 40443 MW; 41BF2F28CDB036FE CRC64; MRCLELNWEI MNKDSSNFLY KYWLKGCEFY NKKDYDKAIE YFSLSNKIFK ENVPKCDYYG LREEAYKEIL NNNIEEGIKK FDWFVEGILA DGDYYNLSGE LSTIASIFAK IGKLDITKNF LNSGGEWIYN DVIKDANSED ILKSVLTFDF SYEERKEILN REPHLRKLFE DNIYNFNSDF FDFMMMFFIG AGNWKRFLEV YEEFKNKIKS CQISNEIVNE IIKRFDKSMS DLLAIAHLLK ENYEKCLYYV MLFKEYFDLD EFNEIEKNKI NLIVDIAYNL KNGNVKKEEW LNRLNEIYKE IIKRPLPNTY KDAHNDDLLN EILDYYVLKE FIEKKL // ID Y1350_METJA Reviewed; 261 AA. AC Q58745; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1350; GN OrderedLocusNames=MJ1350; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FwdC/FmdC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99361.1; -; Genomic_DNA. DR PIR; E64468; E64468. DR ProteinModelPortal; Q58745; -. DR STRING; 243232.MJ_1350; -. DR EnsemblBacteria; AAB99361; AAB99361; MJ_1350. DR KEGG; mja:MJ_1350; -. DR eggNOG; arCOG00096; Archaea. DR eggNOG; COG0070; LUCA. DR InParanoid; Q58745; -. DR OMA; APGNTMD; -. DR PhylomeDB; Q58745; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.160.20.60; -; 1. DR InterPro; IPR002489; Glu_synth_asu_C. DR InterPro; IPR012061; Glu_synth_lsu_3. DR Pfam; PF01493; GXGXG; 1. DR PIRSF; PIRSF006519; GOGAT_dom3; 1. DR SUPFAM; SSF69336; SSF69336; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein MJ1350. FT /FTId=PRO_0000144200. SQ SEQUENCE 261 AA; 28957 MW; CB4023B5B88B0B58 CRC64; MKGMEEVVID AKDMHYRELN EKIHEILREN PDIKKIVLKN VLGQRFIADG IQKKDLTIEI YGIPGGDLGM FMSGPTIIVH GNAEFAPGNT MDDGTIVIYG SSGDVTAHSM RGGKVFVRGD VGYRSGIHMK AYKDKVPVLV IGGRAKDFLG EYMAGGIIIV LNIDEKGNDL GKVKGRMIGT GIHGGAIYIR GEIDKDQLGV AADIKEFTEE DLEKIKPYIE EFCKWFNLPE DVKNKLLNSK WTKIAPISKR PFGKLYTPDL M // ID Y1356_METJA Reviewed; 189 AA. AC Q58751; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1356; GN OrderedLocusNames=MJ1356; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1461. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99367.1; -; Genomic_DNA. DR PIR; C64469; C64469. DR STRING; 243232.MJ_1356; -. DR EnsemblBacteria; AAB99367; AAB99367; MJ_1356. DR KEGG; mja:MJ_1356; -. DR eggNOG; arCOG09681; Archaea. DR eggNOG; ENOG4111W0I; LUCA. DR OMA; YIGINQN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0019825; F:oxygen binding; IEA:InterPro. DR Gene3D; 1.10.490.10; -; 1. DR InterPro; IPR012292; Globin/Proto. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 189 Uncharacterized protein MJ1356. FT /FTId=PRO_0000107295. SQ SEQUENCE 189 AA; 22350 MW; A3812C6308D6390E CRC64; MNVTFDGIYN EIIENMHHFA SEEKDFSKLT QYKDLISKTI DEVVEEVFND IFSYEKTKTL FDESKRKELE EDFKNWIKGL FEISNDSDLN EFYKEIVKRG IKYVEKDFLP EYLTAIIIKI EDRLKNKLKE ELKEDAQEIV DILDDLLKRV ILLNVAAYMN FESKVLDYIG INQNLKKNAV KLGIKKMGL // ID Y1359_METJA Reviewed; 242 AA. AC Q58754; DT 15-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 92. DE RecName: Full=UPF0273 protein MJ1359 {ECO:0000255|HAMAP-Rule:MF_01076}; GN OrderedLocusNames=MJ1359; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0273 family. {ECO:0000255|HAMAP- CC Rule:MF_01076}. CC -!- SIMILARITY: Contains 1 kaiC domain. {ECO:0000255|HAMAP- CC Rule:MF_01076}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99368.1; -; Genomic_DNA. DR PIR; F64469; F64469. DR ProteinModelPortal; Q58754; -. DR SMR; Q58754; 2-240. DR STRING; 243232.MJ_1359; -. DR EnsemblBacteria; AAB99368; AAB99368; MJ_1359. DR KEGG; mja:MJ_1359; -. DR eggNOG; arCOG01171; Archaea. DR eggNOG; COG0467; LUCA. DR InParanoid; Q58754; -. DR OMA; EEHPVQI; -. DR PhylomeDB; Q58754; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP. DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro. DR GO; GO:0008094; F:DNA-dependent ATPase activity; IBA:GO_Central. DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000400; F:four-way junction DNA binding; IBA:GO_Central. DR GO; GO:0000150; F:recombinase activity; IBA:GO_Central. DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central. DR GO; GO:0000730; P:DNA recombinase assembly; IBA:GO_Central. DR GO; GO:0006312; P:mitotic recombination; IBA:GO_Central. DR GO; GO:0010212; P:response to ionizing radiation; IBA:GO_Central. DR GO; GO:0042148; P:strand invasion; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR HAMAP; MF_01076; UPF0273; 1. DR InterPro; IPR004504; DNA_repair_RadA. DR InterPro; IPR014774; KaiC-like_dom. DR InterPro; IPR010624; KaiC_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR022475; UPF0273_KaiC-like. DR Pfam; PF06745; ATPase; 1. DR PRINTS; PR01874; DNAREPAIRADA. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR03877; thermo_KaiC_1; 1. DR PROSITE; PS51146; KAIC; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 242 UPF0273 protein MJ1359. FT /FTId=PRO_0000184585. FT DOMAIN 2 242 KaiC. {ECO:0000255|HAMAP-Rule:MF_01076}. FT NP_BIND 29 36 ATP. {ECO:0000255|HAMAP-Rule:MF_01076}. SQ SEQUENCE 242 AA; 26988 MW; 28F86D37CB25811B CRC64; MKRVKTGIPG MDEILHGGIP ERNVVLLSGG PGTGKSIFCQ QFLYKGVVDY NEPSILVALE EHPVQIRENM RQFGWDIRKL EEEGKFAIID AFTYGIGSAA KREKYVVNDP NDERELIDVL KTAINDIGAK RIGIDSVTTL YINKPMLARR TVFLLKRVIS GLGCTAIFTS QISVGERGFG GPGVEHAVDG IIRLDLDEID GELKRSLIVW KMRGTSHSLK RHPFDITNEG IIVYPDKVLK LR // ID Y1360_METJA Reviewed; 99 AA. AC Q58755; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ1360; GN OrderedLocusNames=MJ1360; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99378.1; -; Genomic_DNA. DR PIR; G64469; G64469. DR STRING; 243232.MJ_1360; -. DR EnsemblBacteria; AAB99378; AAB99378; MJ_1360. DR KEGG; mja:MJ_1360; -. DR eggNOG; arCOG05080; Archaea. DR eggNOG; ENOG410ZHFC; LUCA. DR OMA; MFLDDIP; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 99 Uncharacterized protein MJ1360. FT /FTId=PRO_0000107297. SQ SEQUENCE 99 AA; 11595 MW; 1BF321FD8A283B3E CRC64; MWGSMPRRKI DKLYVKIYFE GNAIEGEYDF DAVTHLKNGI LKYLWTGKKD PIIIWNMDNK SFTIIDPSKI CAVEVQGSLM FLDDIPEKKL EMKSFSERD // ID Y1361_METJA Reviewed; 292 AA. AC Q58756; DT 04-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ1361; GN OrderedLocusNames=MJ1361; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99369.1; -; Genomic_DNA. DR PIR; H64469; H64469. DR ProteinModelPortal; Q58756; -. DR STRING; 243232.MJ_1361; -. DR EnsemblBacteria; AAB99369; AAB99369; MJ_1361. DR KEGG; mja:MJ_1361; -. DR eggNOG; arCOG02715; Archaea. DR eggNOG; COG4071; LUCA. DR OMA; PKFWAYF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR002847; F420-0_gamma-glut_ligase-dom. DR InterPro; IPR012030; UCP006563. DR Pfam; PF01996; F420_ligase; 1. DR PIRSF; PIRSF006563; UCP006563; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 292 Uncharacterized protein MJ1361. FT /FTId=PRO_0000107298. FT TRANSMEM 175 197 Helical. {ECO:0000255}. SQ SEQUENCE 292 AA; 33193 MW; 4F4DC241760F1A36 CRC64; MRAYPIKTRY IKRGENFIPI VVEAIKNSGI KLEDGDFVVL SEKMVSTAEG NFIDESKFKP GVLAYLCYYW SKYLWGYVLG KLLKVKEDKI KNLRRMPKEE TLKHKQTIIE IVGLRYALKP YAEGGVDLTN VPGTYACPLP KNPKKWAEEL YKEIKKELGV DVVVMVADTD ATYRVLNFYF TALPYAIDGI ISGIGVFGFI LGRLADVLKI GGFAGCTPLA IAGNEVYKKY SIGELTRIAF ICDRVHKTIK NINEVLEKYN TYVITEEILE KLEHTPVVVV KIKEEYKPES QR // ID Y1400_METJA Reviewed; 67 AA. AC Q58795; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=UPF0333 protein MJ1400; GN OrderedLocusNames=MJ1400; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0333 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99411.1; -; Genomic_DNA. DR PIR; G64474; G64474. DR STRING; 243232.MJ_1400; -. DR EnsemblBacteria; AAB99411; AAB99411; MJ_1400. DR KEGG; mja:MJ_1400; -. DR eggNOG; arCOG05082; Archaea. DR eggNOG; ENOG410Z9R8; LUCA. DR OMA; NTHNTAM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR Pfam; PF04021; Class_IIIsignal; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 67 UPF0333 protein MJ1400. FT /FTId=PRO_0000218268. FT TRANSMEM 18 38 Helical. {ECO:0000255}. SQ SEQUENCE 67 AA; 7485 MW; 30B893EF421AAC34 CRC64; MKFIMKFIKS NKGQISLEFS LLVMVVVLSA IIVSYYLIKT AIETRNANMD VINQSSNVAE KSLSNVT // ID Y1403_METJA Reviewed; 374 AA. AC Q58798; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1403; GN OrderedLocusNames=MJ1403; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99413.1; -; Genomic_DNA. DR PIR; B64475; B64475. DR ProteinModelPortal; Q58798; -. DR EnsemblBacteria; AAB99413; AAB99413; MJ_1403. DR KEGG; mja:MJ_1403; -. DR eggNOG; arCOG05987; Archaea. DR eggNOG; ENOG410YSPP; LUCA. DR OMA; YDERFIV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR013373; Flagellin/pilin_N. DR TIGRFAMs; TIGR02537; arch_flag_Nterm; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 374 Uncharacterized protein MJ1403. FT /FTId=PRO_0000107312. FT TRANSMEM 27 49 Helical. {ECO:0000255}. SQ SEQUENCE 374 AA; 41002 MW; BC56B019D75D7E59 CRC64; MTVSHGGILE GSSRGGKMMD WLKNKKAISP ILALLIVLGV TIVVGAVFYA WGSNLFGNSQ EKTQAAVEGT ATNMFYDAGA IRVAATCIDK IRYQDADDSD SWLGYPNGNG KIAKPSTSNG CYNSTYGTVF YDERFIVEIP VTIDTQDYKL TGVKVVGGIP KIVDMGGTYT NAFEDISAKF YAFWLHLNDN YQLLKKDGTL FVGYVNKSGM FEVSNGYVIA WNQTRDTYGK LASSVGATSD SSWDAVNTTT GVAPLVETSW PYYGTYCSNV KLYTATGEEL KPGFGSGTLV AQWFCSSATY LDKLFNNPEY VVGTLPKNSE KTVKTYLFFN TLYLPNYKGS TNDGYVTFEV PLKVVSNEGV TKEVKVKFTV YDDE // ID Y1405_METJA Reviewed; 75 AA. AC Q58800; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=Acylphosphatase-like protein MJ1405; GN OrderedLocusNames=MJ1405; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99422.1; -; Genomic_DNA. DR PIR; D64475; D64475. DR ProteinModelPortal; Q58800; -. DR STRING; 243232.MJ_1405; -. DR EnsemblBacteria; AAB99422; AAB99422; MJ_1405. DR KEGG; mja:MJ_1405; -. DR eggNOG; arCOG01674; Archaea. DR eggNOG; COG1254; LUCA. DR PhylomeDB; Q58800; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR Pfam; PF00708; Acylphosphatase; 1. DR SUPFAM; SSF54975; SSF54975; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 75 Acylphosphatase-like protein MJ1405. FT /FTId=PRO_0000158565. FT DOMAIN 8 75 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. SQ SEQUENCE 75 AA; 8950 MW; 10A601F869514B90 CRC64; MVKFMPTTYE IIIYGRIQHV GFRERIENLG HALGIDGIVY NYEDGTVRIL ANFPSERKKK LFKDKTNFWR VRKCK // ID Y1423_METJA Reviewed; 352 AA. AC Q58818; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ1423; GN OrderedLocusNames=MJ1423; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH1522. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99434.1; -; Genomic_DNA. DR PIR; F64477; F64477. DR ProteinModelPortal; Q58818; -. DR STRING; 243232.MJ_1423; -. DR EnsemblBacteria; AAB99434; AAB99434; MJ_1423. DR KEGG; mja:MJ_1423; -. DR eggNOG; arCOG04888; Archaea. DR eggNOG; COG2710; LUCA. DR InParanoid; Q58818; -. DR OMA; AKKETAY; -. DR PhylomeDB; Q58818; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR InterPro; IPR017675; Methan_mark_13_metalloprotein. DR InterPro; IPR000510; Nase/OxRdtase_comp1. DR Pfam; PF00148; Oxidored_nitro; 1. DR TIGRFAMs; TIGR03282; methan_mark_13; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 352 Uncharacterized protein MJ1423. FT /FTId=PRO_0000107317. SQ SEQUENCE 352 AA; 39470 MW; F95B6F9C6095B0EB CRC64; MIFHPRPSPI AAAMYQLRDL GVDAIILHGP SGCCFRTARL LELDGVRVFT SNIDENAIVF GASENLKKAL DYAIEYLKKE LKKERPMIGI VGTCASMIIG EDLWEFVDDD RAIIIPVEVH SGSGDNTIGA IKAMESALKL GIIDEKEFER QKFLLKKATE VEKKRGMAKK EYIKPTYDDD LNEAIKVLKD LKEKDGKIAC VLNAKKETAY LFAHPLIVLN KYFNCVNIAN LDINKGLPKI RRDAQNILRR FKADYITGGL DEYPITGERA VEILKDLDVD AIVVSGVPHA LPIEEIDKDI IKIGISDGPR TYHPIKEIYD YAIVELDAHA KVLGKRDIVK SRFGEILDYA LE // ID Y1458_METJA Reviewed; 218 AA. AC Q58853; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1458; GN OrderedLocusNames=MJ1458; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99466.1; -; Genomic_DNA. DR PIR; A64482; A64482. DR ProteinModelPortal; Q58853; -. DR SMR; Q58853; 4-216. DR STRING; 243232.MJ_1458; -. DR EnsemblBacteria; AAB99466; AAB99466; MJ_1458. DR KEGG; mja:MJ_1458; -. DR eggNOG; arCOG00813; Archaea. DR eggNOG; COG1707; LUCA. DR KO; K06862; -. DR OMA; YTQQFIK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR011006; CheY-like_superfamily. DR InterPro; IPR015832; UCP006363_ACT. DR Pfam; PF01842; ACT; 1. DR PIRSF; PIRSF006363; UCP006363_ACT; 1. DR SUPFAM; SSF52172; SSF52172; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 218 Uncharacterized protein MJ1458. FT /FTId=PRO_0000107346. FT DOMAIN 4 83 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 218 AA; 23472 MW; DD96DA57FFCB8A78 CRC64; MEIGISIEAE NKVGVLHKLT GILSELGGNI TYTQQFIKDD GKIGFIYMEV EGIKDIEELK RRMESCECVK SFEIHSSLKK IYGKRVIIIG GGAQVAEVAR GAISEADRHN IRGERISVDT LPIVGEENLY EAVKAVATLP RVGILVLAGS LMGGKITEAV KELKEKTGIP VISLKMFGSV PKVADLVVGD PLQAGVLAVM AIAETAKFDI NKVKGRVL // ID Y1460_METJA Reviewed; 162 AA. AC Q58855; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ1460; GN OrderedLocusNames=MJ1460; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99471.1; -; Genomic_DNA. DR PIR; C64482; C64482. DR PDB; 2OSD; X-ray; 2.30 A; A=1-162. DR PDB; 2OSO; X-ray; 1.90 A; A=1-162. DR PDBsum; 2OSD; -. DR PDBsum; 2OSO; -. DR ProteinModelPortal; Q58855; -. DR SMR; Q58855; 1-158. DR STRING; 243232.MJ_1460; -. DR DNASU; 1452364; -. DR EnsemblBacteria; AAB99471; AAB99471; MJ_1460. DR KEGG; mja:MJ_1460; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q58855; -. DR KO; K07013; -. DR OMA; KIFKLMN; -. DR PhylomeDB; Q58855; -. DR EvolutionaryTrace; Q58855; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 162 Uncharacterized protein MJ1460. FT /FTId=PRO_0000107349. FT HELIX 8 14 {ECO:0000244|PDB:2OSO}. FT HELIX 18 23 {ECO:0000244|PDB:2OSO}. FT HELIX 29 43 {ECO:0000244|PDB:2OSO}. FT HELIX 52 63 {ECO:0000244|PDB:2OSO}. FT HELIX 68 77 {ECO:0000244|PDB:2OSO}. FT STRAND 82 84 {ECO:0000244|PDB:2OSO}. FT HELIX 87 92 {ECO:0000244|PDB:2OSO}. FT STRAND 97 103 {ECO:0000244|PDB:2OSO}. FT HELIX 117 131 {ECO:0000244|PDB:2OSO}. FT STRAND 133 141 {ECO:0000244|PDB:2OSO}. FT HELIX 143 145 {ECO:0000244|PDB:2OSO}. FT STRAND 148 157 {ECO:0000244|PDB:2OSO}. SQ SEQUENCE 162 AA; 18783 MW; 1A50EDE6483E424D CRC64; MAFMEKIFPD ILEAIRNEEI IKESKKIPMP YFGLFALVIF DKVKELGSET SLYEIGEEFG KMLSPKNIEE LKKIFKLMNF GDLEIDENKI LLKNPPYKIK LSNPPYQWVS KEEPIHDFIA GILAGCLEEI FKKKFVVNEV ECVSQGKDKC VFEVKEVDEL NK // ID Y1470_METJA Reviewed; 624 AA. AC Q58865; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ1470; GN OrderedLocusNames=MJ1470; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99485.1; -; Genomic_DNA. DR PIR; E64483; E64483. DR ProteinModelPortal; Q58865; -. DR STRING; 243232.MJ_1470; -. DR EnsemblBacteria; AAB99485; AAB99485; MJ_1470. DR KEGG; mja:MJ_1470; -. DR eggNOG; arCOG03508; Archaea. DR eggNOG; arCOG06599; Archaea. DR eggNOG; COG5306; LUCA. DR OMA; IDWVFVR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR013320; ConA-like_dom. DR InterPro; IPR018765; DUF2341. DR Pfam; PF10102; DUF2341; 1. DR SUPFAM; SSF49899; SSF49899; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 624 Uncharacterized protein MJ1470. FT /FTId=PRO_0000107356. FT TRANSMEM 10 30 Helical. {ECO:0000255}. SQ SEQUENCE 624 AA; 72858 MW; CEBF3B4A86A0EF80 CRC64; MFRKIVSKRG YIFTYEAIVI AFIFLSVFYI GYMVYSHNML TALEEKKDTE KFHKALLLKD YFLRNNKFPG KFYNKTYLDN FTNELDIKEK TFDLFNNFSE YKGLIRFIIY PNIYDEELDN ISDEICANDG LQAITYNFSS NTFKIYSNVN TTFNNANLSI SGMDLIYFKE NVYIPKITGM KYGDSINLYG CNGDHIYFKV NSEIISASAR VVTNNGNPFI TWQNWRYATP ILIINNLNQN LNDYDVKIVF DSQSYINSGE MRTDCGDVRF VDEDGNPLSY WIEPNTIDTP HTVAWVKVNL APNEHKLIYM LYGNPTATTT ANGDNTFPLF FDDFSKGNLD NTKWTYNFNN PLFVNDTYPN GINFTYLSLD YTYYNNHNYI IYDINNTHIS SISTYYPNTS VRFHANFHKK YEEWGGFYIN INGNDYNREV ITNYHWGGEW LRAESSVLNQ DYDSYIILQD PDLYDNWHTY EIQRDGGSSV NFIIDDAIYK TIYSNIYTGD LPISFYARKY DYSTKYGYYP VPQDEQNGNI SIDWVFVRKY VEPEPTVTLL SSDVIFTVNG YIYKKPLKSV FDNIDITPNL NVGINEIRIL SSPLPVEFLI KTNENTDFYY LTLSPNNVTI VVKP // ID Y1480_METJA Reviewed; 423 AA. AC Q58875; DT 07-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ1480; GN OrderedLocusNames=MJ1480; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99492.1; -; Genomic_DNA. DR PIR; G64484; G64484. DR PDB; 3MGJ; X-ray; 2.70 A; A/B=1-110. DR PDBsum; 3MGJ; -. DR ProteinModelPortal; Q58875; -. DR SMR; Q58875; 78-400. DR STRING; 243232.MJ_1480; -. DR EnsemblBacteria; AAB99492; AAB99492; MJ_1480. DR KEGG; mja:MJ_1480; -. DR eggNOG; arCOG04422; Archaea. DR eggNOG; COG1915; LUCA. DR InParanoid; Q58875; -. DR OMA; HKHHIYA; -. DR PhylomeDB; Q58875; -. DR EvolutionaryTrace; Q58875; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR005239; CHP00300. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR007545; LOR/SDH_bifunc_enz_cons_dom. DR Pfam; PF04455; Saccharop_dh_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR TIGRFAMs; TIGR00300; TIGR00300; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 423 Uncharacterized protein MJ1480. FT /FTId=PRO_0000107363. FT STRAND 2 10 {ECO:0000244|PDB:3MGJ}. FT HELIX 17 27 {ECO:0000244|PDB:3MGJ}. FT STRAND 31 38 {ECO:0000244|PDB:3MGJ}. FT STRAND 47 57 {ECO:0000244|PDB:3MGJ}. FT HELIX 58 74 {ECO:0000244|PDB:3MGJ}. FT STRAND 78 83 {ECO:0000244|PDB:3MGJ}. FT STRAND 86 88 {ECO:0000244|PDB:3MGJ}. SQ SEQUENCE 423 AA; 47181 MW; E2EFD16142F2816E CRC64; MFMREIELRG HIIDSLILPK VFDKILDMGG DYKVLEFEIG KRKTDPSYAK ILVIGRDERH VDEILNELRD LGAEIPEIEE VELQPAEKDM VLPEGFYSTT NHKTFIRFKG KWIEVENQKM DGAIVVYPDE MRAEVKTIRN IKKGDLVVVG HKGVRVIPPE KPREGGGLFE FMKSDASSEK PKETIIRRIA KEMYEIREKY RKTGKGGIVV VGGPAIIHTG AGWALAKLIR MGYVQALFAG NALATHDIES VLYGTSLGVD LKTGKSVPGG HSHHLRAINT IMRAGSIKDA VEQGILKEGV MYECIKNNIP YVLAGSIRDD GPLPDVITDV VKAQEKMREL LKGKDMVLML STMLHSIATG NLLPSWVKTI CVDINPAVVT KLMDRGTSQA LGIVTDVGVF LPMLVEELEK LEKEKEKSEK REE // ID Y1483_METJA Reviewed; 152 AA. AC Q58878; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ1483; GN OrderedLocusNames=MJ1483; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99498.1; -; Genomic_DNA. DR PIR; B64485; B64485. DR STRING; 243232.MJ_1483; -. DR EnsemblBacteria; AAB99498; AAB99498; MJ_1483. DR KEGG; mja:MJ_1483; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 152 Uncharacterized protein MJ1483. FT /FTId=PRO_0000107369. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 152 AA; 17659 MW; 90227132448E8802 CRC64; MINMDKTLSV IVFLISLIII FGIYFSSSNF SFKKVEINKS TINDFGDENI LTFVPEVCDR FYYEKDGFDW ERNINNIETV IIGSDAVVIE KGDFNETEIL KELIENGYSV ESCRGVYYYK NEKALSDRYI IVGNNLIIKA NDISGIRWRY LQ // ID Y1484_METJA Reviewed; 150 AA. AC Q58879; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ1484; GN OrderedLocusNames=MJ1484; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99499.1; -; Genomic_DNA. DR PIR; C64485; C64485. DR STRING; 243232.MJ_1484; -. DR EnsemblBacteria; AAB99499; AAB99499; MJ_1484. DR KEGG; mja:MJ_1484; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 150 Uncharacterized protein MJ1484. FT /FTId=PRO_0000107370. SQ SEQUENCE 150 AA; 17896 MW; 45BF3EED4000DB52 CRC64; MEIFTIKYNA SLFSNKTLRD KVYKILKENT KSYYESNSNG FFRIGGISRV DYINNNSIYF KGECKKYFGK NEVIITNFWI FKNESLADKF YNKMLKEYGN KSYIDKNPKL KYYNMSEIIN YSVEMYDKDV VLIKEHTKDI KLFEVNVSMG // ID Y149_METJA Reviewed; 58 AA. AC Q57613; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 73. DE RecName: Full=Uncharacterized protein MJ0149; GN OrderedLocusNames=MJ0149; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98140.1; -; Genomic_DNA. DR PIR; F64318; F64318. DR STRING; 243232.MJ_0149; -. DR EnsemblBacteria; AAB98140; AAB98140; MJ_0149. DR KEGG; mja:MJ_0149; -. DR eggNOG; arCOG08276; Archaea. DR eggNOG; ENOG41111SU; LUCA. DR OMA; IFCAFGR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR032820; ATPase_put. DR Pfam; PF09527; ATPase_gene1; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 58 Uncharacterized protein MJ0149. FT /FTId=PRO_0000106719. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. SQ SEQUENCE 58 AA; 6917 MW; CD7CB74F2F2CCC3E CRC64; MLRDIAFEFF IMIALGIFIG YIIAEYTDNN LWIVVFLLLG IFCAFGRLFK MIKDYEKR // ID Y1535_METJA Reviewed; 299 AA. AC Q58930; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ1535; GN OrderedLocusNames=MJ1535; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99558.1; -; Genomic_DNA. DR PIR; F64491; F64491. DR ProteinModelPortal; Q58930; -. DR EnsemblBacteria; AAB99558; AAB99558; MJ_1535. DR KEGG; mja:MJ_1535; -. DR eggNOG; arCOG05088; Archaea. DR eggNOG; ENOG410YRNN; LUCA. DR OMA; KYWKIGG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 299 Uncharacterized protein MJ1535. FT /FTId=PRO_0000107394. FT TRANSMEM 4 20 Helical. {ECO:0000255}. SQ SEQUENCE 299 AA; 34958 MW; C201F18230F66769 CRC64; MKRLFFIFVM LIVLLCGCTS NKTTNVNNEI NINKIETNKT LENESLIQKT EKNQLAKIKE IKYMYIVKEG NKTKIQFALA YENGSLARVS NGKVVLKIFD DSGLLFNKTY YINELPLKAG YYYEIELPKI KGFYKNAKFV LTFKNDNVNL SKTTYGTIER YSEEEMKEIF EKEYHENSIK TNIEEFRDVV GIKFTVKEYG YYKIYNNQTD RIEKVFRVDF VAKNLNPDTY EFAPIGVCLI SGDKKYWKIG GLDEIEIGIN QEIAGYWIFN KPDSIENLRL DFKMGNIVYD IPLTQNNLK // ID Y1548_METJA Reviewed; 122 AA. AC Q58943; DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=UPF0331 protein MJ1548; GN OrderedLocusNames=MJ1548; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0331 family. MJ1548 subfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99566.1; -; Genomic_DNA. DR PIR; C64493; C64493. DR ProteinModelPortal; Q58943; -. DR STRING; 243232.MJ_1548; -. DR EnsemblBacteria; AAB99566; AAB99566; MJ_1548. DR KEGG; mja:MJ_1548; -. DR eggNOG; arCOG02109; Archaea. DR eggNOG; COG2445; LUCA. DR OMA; AIVHKYD; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 122 UPF0331 protein MJ1548. FT /FTId=PRO_0000158265. SQ SEQUENCE 122 AA; 14470 MW; 85BEBFD3BFD2D37D CRC64; MRLQKGLYYI SLQVCVDITM DVVAMLVKDI GLNVEDDYTN IKKLLKHDVI TKDEATLLKQ YNRLRNAIVH KYDKLNLEVV KEGLKRIDEL YEIAYESMRV MKCEAFHLII IKLIEFYEKV EE // ID Y1564_METJA Reviewed; 170 AA. AC Q58959; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=UPF0201 protein MJ1564; GN OrderedLocusNames=MJ1564; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0201 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99591.1; -; Genomic_DNA. DR PIR; C64495; C64495. DR PDB; 2PZZ; X-ray; 2.20 A; A/B/C/D=2-139. DR PDBsum; 2PZZ; -. DR ProteinModelPortal; Q58959; -. DR SMR; Q58959; 1-133. DR STRING; 243232.MJ_1564; -. DR PRIDE; Q58959; -. DR EnsemblBacteria; AAB99591; AAB99591; MJ_1564. DR KEGG; mja:MJ_1564; -. DR eggNOG; arCOG01043; Archaea. DR eggNOG; COG1931; LUCA. DR InParanoid; Q58959; -. DR KO; K09736; -. DR OMA; FDIDTHG; -. DR PhylomeDB; Q58959; -. DR EvolutionaryTrace; Q58959; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.1440.10; -; 1. DR HAMAP; MF_01112; UPF0201; 1. DR InterPro; IPR022803; Ribosomal_L5_domain. DR InterPro; IPR002739; UPF0201. DR Pfam; PF01877; RNA_binding; 1. DR SUPFAM; SSF55282; SSF55282; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 170 UPF0201 protein MJ1564. FT /FTId=PRO_0000094510. FT COMPBIAS 134 156 Glu-rich. FT STRAND 2 9 {ECO:0000244|PDB:2PZZ}. FT HELIX 15 25 {ECO:0000244|PDB:2PZZ}. FT STRAND 30 35 {ECO:0000244|PDB:2PZZ}. FT STRAND 41 48 {ECO:0000244|PDB:2PZZ}. FT HELIX 51 59 {ECO:0000244|PDB:2PZZ}. FT HELIX 63 72 {ECO:0000244|PDB:2PZZ}. FT STRAND 76 83 {ECO:0000244|PDB:2PZZ}. FT HELIX 85 89 {ECO:0000244|PDB:2PZZ}. FT STRAND 103 108 {ECO:0000244|PDB:2PZZ}. FT HELIX 115 122 {ECO:0000244|PDB:2PZZ}. FT STRAND 126 129 {ECO:0000244|PDB:2PZZ}. SQ SEQUENCE 170 AA; 19330 MW; F857091593FE494F CRC64; MEVIIKAKVK PTEDKYKVKK AILNIFPKAK LTFIEKDNEF GEWEGKTKSV EKLKELLRSQ SILDAARMVL EKGMTENATK FYLNKQAAYV GAVNFDIDTH GGIFVKILAD ENEDIMKIIK DIAPRTKGGV IINEDELEEE EEKEDSEEIK EGHKEENNLK IKVIDNSSGD // ID Y1565_METJA Reviewed; 513 AA. AC Q58960; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Probable helicase MJ1565 {ECO:0000305}; DE EC=3.6.4.12 {ECO:0000250|UniProtKB:F2Z5Z6}; GN OrderedLocusNames=MJ1565 {ECO:0000312|EMBL:AAB99585.1}; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC {ECO:0000250|UniProtKB:F2Z5Z6}. CC -!- SIMILARITY: Belongs to the HerA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99585.1; -; Genomic_DNA. DR PIR; D64495; D64495. DR ProteinModelPortal; Q58960; -. DR STRING; 243232.MJ_1565; -. DR EnsemblBacteria; AAB99585; AAB99585; MJ_1565. DR KEGG; mja:MJ_1565; -. DR eggNOG; arCOG00280; Archaea. DR eggNOG; COG0433; LUCA. DR InParanoid; Q58960; -. DR KO; K06915; -. DR OMA; MIFEEAH; -. DR PhylomeDB; Q58960; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR008571; HerA. DR InterPro; IPR018538; HerA_barrel_dom. DR InterPro; IPR033186; HerA_C. DR InterPro; IPR002789; HerA_central. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR30121:SF2; PTHR30121:SF2; 1. DR Pfam; PF05872; DUF853; 1. DR Pfam; PF01935; DUF87; 1. DR Pfam; PF09378; HAS-barrel; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 513 Probable helicase MJ1565. FT /FTId=PRO_0000107413. FT NP_BIND 160 165 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT NP_BIND 467 468 ATP. {ECO:0000250|UniProtKB:Q97WG8}. FT BINDING 151 151 ATP. {ECO:0000250|UniProtKB:Q97WG8}. SQ SEQUENCE 513 AA; 58672 MW; A45C1EAD7D932526 CRC64; MDNNEIIGYT IGETRIDELT FLAKEAPKVG DYVKINYDDS ELLGMVESTI QGNMALEDIL NIEHLEKIRE FEDNSSYYIL GKIKVLGDIR DLNKDGALKL PRVPPKPGIP IYRADDELLK KVFGNGHLKI GHLVTREDVE VKLDANKLCS RHLAILAMTG MGKSNTVAVL LRELNKLKAT VLVFDMHGEY KDIYCESEKL RVHIIEPKIN IYRINDDDLC DLAGVDAQAT KQRPYIRKAI KEIKEERKEH DFSTVDDYIN AIIGKLEEYK SNDNYKKDES SIQTAIFRLE DMLQFRKNII TLHYNPINDI REHYINIIPM EELDENAVDI VVSYIAKAVL DDRKRIIIDK GRDFAKPIFM IFEEAHLIAP QHRKTRAKHY LSRIAREGRK FGVGLCLVSQ RPKTLDAETL SQCSNLIISK LIEPTDQKHV QMASENLSED LVKQLTSLNI GEAIILGPCI KVPAIVKVDK FDGRYGGEDL NLVELWEKDF INTERLKTDD IEENAFGDDD LFS // ID Y1567_METJA Reviewed; 175 AA. AC Q58962; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ1567; GN OrderedLocusNames=MJ1567; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99593.1; -; Genomic_DNA. DR PIR; F64495; F64495. DR ProteinModelPortal; Q58962; -. DR STRING; 243232.MJ_1567; -. DR EnsemblBacteria; AAB99593; AAB99593; MJ_1567. DR KEGG; mja:MJ_1567; -. DR eggNOG; arCOG08282; Archaea. DR eggNOG; ENOG410YUS7; LUCA. DR InParanoid; Q58962; -. DR OMA; KFINISY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 175 Uncharacterized protein MJ1567. FT /FTId=PRO_0000107415. SQ SEQUENCE 175 AA; 20726 MW; 20524D646C38EFD6 CRC64; MVAMNENQQK LHYIINLLTN GNKKRWVKQT VLFALIYYFI KLDVFKGYDY APTPFMWEDE IKFINISYEA INDLNYLLDN NYLNEILLSV RGLNEFIVGY SIGKKIDYNF NQKDKETIDK TLLENGRLKE IQITKNGIII KSKNEKLEIE ITKIDKISYK SKSYIMKVSL WDSNI // ID Y1588_METJA Reviewed; 112 AA. AC Q58983; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1588; GN OrderedLocusNames=MJ1588; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99609.1; -; Genomic_DNA. DR PIR; C64498; C64498. DR STRING; 243232.MJ_1588; -. DR EnsemblBacteria; AAB99609; AAB99609; MJ_1588. DR KEGG; mja:MJ_1588; -. DR eggNOG; arCOG00306; Archaea. DR eggNOG; COG0613; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 112 Uncharacterized protein MJ1588. FT /FTId=PRO_0000107429. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT COMPBIAS 102 110 Lys-rich. SQ SEQUENCE 112 AA; 12800 MW; 0CEC073B0907E14E CRC64; MVGNAYTLFE GNSADDLYKA IVKKRTTYEG KPTPLYQAIL WSYKVVYTSE KKLIKSLIFR IGDNTIDSIK LYKKILGVFG GFIYILTPLP IVSGFLGNYY LKKKAKEKMK EV // ID Y1623_METJA Reviewed; 512 AA. AC Q59017; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Uncharacterized protein MJ1623; GN OrderedLocusNames=MJ1623; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99648.1; -; Genomic_DNA. DR PIR; E64502; E64502. DR ProteinModelPortal; Q59017; -. DR STRING; 243232.MJ_1623; -. DR EnsemblBacteria; AAB99648; AAB99648; MJ_1623. DR KEGG; mja:MJ_1623; -. DR eggNOG; arCOG02037; Archaea. DR eggNOG; arCOG02838; Archaea. DR eggNOG; COG1378; LUCA. DR eggNOG; COG3287; LUCA. DR InParanoid; Q59017; -. DR OMA; LDGKPAY; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR019494; FIST_C. DR InterPro; IPR013702; FIST_domain_N. DR InterPro; IPR002831; Tscrpt_reg_TrmB_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF08495; FIST; 1. DR Pfam; PF10442; FIST_C; 1. DR Pfam; PF01978; TrmB; 1. DR SMART; SM00897; FIST; 1. DR SMART; SM01204; FIST_C; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 512 Uncharacterized protein MJ1623. FT /FTId=PRO_0000107444. SQ SEQUENCE 512 AA; 59701 MW; 78172A3E6C9396E4 CRC64; MIYIHKKIKN PIKDGIEIGE EIKRNVGRAS LIIFITSILE RDKLKQVFDG MKQHIPLDNL IGCSTGGTFS GKDYIKEDGV LILAFDEYYK SAISCEKVDR EAEYVGKKIA DKIKTCIRDK YPKLDIDDNF LGFVFFDWNV DSEQEILDVL GRELTIPIIG GTAADDGSFD KFFQIYKGEV VKDCCVFGVV GGKLKFDLIY GHGYEPTDIY ARVTKAEGKV VYELDGKPAY QRYLEMLSEY TKLPMDIIKK YFYRDLRRLD FYLVHPLGFM DINGNYITAF LERVEENTLV FRRDILEGSF LVLMKTDIEK QVKSIVDELK KAEDFENPLI FINECYGREV LKNSMFREFE EDILKYFLNF YKAGKKVEEY VIEDNCIGWL SYGETIAKDL IRFHNNLSFT GVIFELSQSS NINWREELKN FNFEDDEIEV IVNLINKQLT AKELLQLTNL SQTKLYHILN KLEKEGIIKS VSGKPKLYYI DNIKEILQKT HEKIEHENMV KKIKRKKLLR LL // ID Y1654_METJA Reviewed; 225 AA. AC Q59048; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1654; GN OrderedLocusNames=MJ1654; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 PCI domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99683.1; -; Genomic_DNA. DR PIR; D64506; D64506. DR ProteinModelPortal; Q59048; -. DR STRING; 243232.MJ_1654; -. DR EnsemblBacteria; AAB99683; AAB99683; MJ_1654. DR KEGG; mja:MJ_1654; -. DR eggNOG; arCOG02261; Archaea. DR eggNOG; ENOG410YKGY; LUCA. DR OMA; RYVAYKI; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF50249; SSF50249; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MJ1654. FT /FTId=PRO_0000107460. FT DOMAIN 166 214 PCI. SQ SEQUENCE 225 AA; 26418 MW; 82D66A10FA1B43D2 CRC64; MGYPTPIKLG LSAPINVPLI YKTGEKMRYV AYKIYPEEFL NNEVVDNALI IEGRKVRRVR ILGKVENINV GNIISFYVDG VNVRYFEEKP VYIEEGDIVD VIGRPRTYDG EKYIMAEIIR KRDERWIKLR DLEIKKTRKY LLERAELYEE ENEEMSLEEE VYTEILNSDV IKDKILAIIE NVGEITYEEL AEKINIPEED LEKYLSELKE SGDIFEPRPG VYKVL // ID Y1671_METJA Reviewed; 45 AA. AC Q59065; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ1671; GN OrderedLocusNames=MJ1671; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99694.1; -; Genomic_DNA. DR PIR; E64508; E64508. DR STRING; 243232.MJ_1671; -. DR EnsemblBacteria; AAB99694; AAB99694; MJ_1671. DR KEGG; mja:MJ_1671; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 45 Uncharacterized protein MJ1671. FT /FTId=PRO_0000107469. SQ SEQUENCE 45 AA; 5353 MW; 0AFB6B337C51D337 CRC64; MEYVKFLEDY VREKVKKMFS SNVKLSFNDL KVSAKIVELK KRGVK // ID Y227_METJA Reviewed; 308 AA. AC Q57680; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0227; GN OrderedLocusNames=MJ0227; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98212.1; -; Genomic_DNA. DR PIR; D64328; D64328. DR STRING; 243232.MJ_0227; -. DR DNASU; 1451080; -. DR EnsemblBacteria; AAB98212; AAB98212; MJ_0227. DR KEGG; mja:MJ_0227; -. DR eggNOG; arCOG04238; Archaea. DR eggNOG; COG1767; LUCA. DR InParanoid; Q57680; -. DR KO; K05966; -. DR OMA; GNTHFGA; -. DR PhylomeDB; Q57680; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0046917; F:triphosphoribosyl-dephospho-CoA synthase activity; IEA:InterPro. DR GO; GO:0016310; P:phosphorylation; IEA:InterPro. DR InterPro; IPR002736; CitG. DR Pfam; PF01874; CitG; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 308 Uncharacterized protein MJ0227. FT /FTId=PRO_0000106750. SQ SEQUENCE 308 AA; 35190 MW; E191FB42772BCE58 CRC64; MHLPNSQIYK NFGESMNPFD IMKASQIACC LEVSSFKPGN VHRNRDYRDI KYHHFINAGI AFGNVVYEAA QKDRDVGLYI KKAVIESKKW SPTNANLGII MLHIPIAMAA GKLENFDENK LKENLKKIAE NTTVEDALNV YDAINIAMAY VNKPKKGPDV TSEDAKKELI EKGLTLLDVY KISAEWDNIS KEWVDNFKIS FEGYNLLKKY YDELNNINLA VTKTFLNLLA KYPDTLIARK RGFETALKVS KMAEDVLNNF KEEKVKEFDK YLSKEGNKLN PGTTADLIAS SLMIFILDRI DKRETILW // ID Y229_METJA Reviewed; 95 AA. AC Q57682; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 96. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0229; GN OrderedLocusNames=MJ0229; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98214.1; -; Genomic_DNA. DR PIR; F64328; F64328. DR ProteinModelPortal; Q57682; -. DR STRING; 243232.MJ_0229; -. DR EnsemblBacteria; AAB98214; AAB98214; MJ_0229. DR KEGG; mja:MJ_0229; -. DR eggNOG; arCOG01679; Archaea. DR eggNOG; COG0640; LUCA. DR InParanoid; Q57682; -. DR OMA; AKRIYKA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 95 Uncharacterized HTH-type transcriptional FT regulator MJ0229. FT /FTId=PRO_0000160631. SQ SEQUENCE 95 AA; 11180 MW; FF6B8F2CD9D7488D CRC64; MKLIDVVKMG EALSNPIRVK ILYILNKQPK NIYELAKELE LSRPVVYAHL RKLEDADLVE SDLVLEGSRA KRIYKAKEFK FYIDNEIIKK LFENE // ID Y241_METJA Reviewed; 145 AA. AC Q57693; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0241; GN OrderedLocusNames=MJ0241; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 ACT domain. {ECO:0000255|PROSITE- CC ProRule:PRU01007}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98229.1; -; Genomic_DNA. DR PIR; B64330; B64330. DR ProteinModelPortal; Q57693; -. DR STRING; 243232.MJ_0241; -. DR EnsemblBacteria; AAB98229; AAB98229; MJ_0241. DR KEGG; mja:MJ_0241; -. DR eggNOG; arCOG00814; Archaea. DR eggNOG; ENOG410YIQJ; LUCA. DR OMA; TKKIMEH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016597; F:amino acid binding; IEA:InterPro. DR GO; GO:0008152; P:metabolic process; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002912; ACT_dom. DR InterPro; IPR030489; TR_Rrf2-type_CS. DR InterPro; IPR000944; Tscrpt_reg_Rrf2-type. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02082; Rrf2; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS51671; ACT; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 145 Uncharacterized protein MJ0241. FT /FTId=PRO_0000106758. FT DOMAIN 78 145 ACT. {ECO:0000255|PROSITE- FT ProRule:PRU01007}. SQ SEQUENCE 145 AA; 16280 MW; D55F5A96CCF28534 CRC64; MKVVGLTKKI MEHLKEPITI KELAKKLNMH PKNLDVKIRV LRDLGLVETK KGRNGGVRLT KEGLYLLEKG EITLGSLKLQ IVAKDRIGLL ADITSRISKI GGNITSTVLE REGDEVIIYL VVENVDKDEI KNTLEDVVEK ISILW // ID Y260_METJA Reviewed; 203 AA. AC Q57708; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ0260; GN OrderedLocusNames=MJ0260; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98246.1; -; Genomic_DNA. DR PIR; E64332; E64332. DR ProteinModelPortal; Q57708; -. DR STRING; 243232.MJ_0260; -. DR MEROPS; S26.017; -. DR EnsemblBacteria; AAB98246; AAB98246; MJ_0260. DR KEGG; mja:MJ_0260; -. DR eggNOG; arCOG01739; Archaea. DR eggNOG; COG0681; LUCA. DR InParanoid; Q57708; -. DR KO; K13280; -. DR OMA; SAHWTNA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0008233; F:peptidase activity; IEA:InterPro. DR GO; GO:0006465; P:signal peptide processing; IEA:InterPro. DR Gene3D; 2.10.109.10; -; 2. DR InterPro; IPR028360; Peptidase_S24/S26_b-rbn. DR InterPro; IPR019759; Peptidase_S24_S26. DR InterPro; IPR015927; Peptidase_S24_S26A/B/C. DR InterPro; IPR001733; Peptidase_S26B. DR PANTHER; PTHR10806; PTHR10806; 2. DR Pfam; PF00717; Peptidase_S24; 1. DR SUPFAM; SSF51306; SSF51306; 2. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 203 Uncharacterized protein MJ0260. FT /FTId=PRO_0000106762. FT TRANSMEM 171 191 Helical. {ECO:0000255}. SQ SEQUENCE 203 AA; 23724 MW; 9A6DC1DE1D8DF8C8 CRC64; MVVLFLIWSH VNVVVSDSMY PIMKRGDLVI VENAGFEFNP NDVDVGDIVV YKAHWPYYQY LLSEIDYKLN LNPYTTLYIF KEGDFKDMSV KVLGEIKTDK SSYKILEADI PKSPTKPVIH RVIDKVEFNN KTYFIIKGDN NPIHDPELVS INQIKQRVIV VDGHPLVIPY VGYLSIWLKE YWYLVVLFVL IYYAYNYLKG GRK // ID Y270_METJA Reviewed; 78 AA. AC Q57718; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0270; GN OrderedLocusNames=MJ0270; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98259.1; -; Genomic_DNA. DR PIR; G64333; G64333. DR STRING; 243232.MJ_0270; -. DR EnsemblBacteria; AAB98259; AAB98259; MJ_0270. DR KEGG; mja:MJ_0270; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 78 Uncharacterized protein MJ0270. FT /FTId=PRO_0000106763. FT TRANSMEM 13 33 Helical. {ECO:0000255}. SQ SEQUENCE 78 AA; 8962 MW; 85CB456F9F271F08 CRC64; MKNKREKMRP KSSTILILLM SVLILLLSID ILANHIIIKV DGYYYDGLGQ KLAMKDVIPI NASFNKIKSQ LEKSMKFH // ID Y274_METJA Reviewed; 543 AA. AC Q57722; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 81. DE RecName: Full=Uncharacterized protein MJ0274; GN OrderedLocusNames=MJ0274; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98258.1; -; Genomic_DNA. DR PIR; C64334; C64334. DR ProteinModelPortal; Q57722; -. DR STRING; 243232.MJ_0274; -. DR EnsemblBacteria; AAB98258; AAB98258; MJ_0274. DR KEGG; mja:MJ_0274; -. DR eggNOG; arCOG01359; Archaea. DR eggNOG; COG1031; LUCA. DR InParanoid; Q57722; -. DR OMA; HTPGKYL; -. DR PhylomeDB; Q57722; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR002792; TRAM_dom. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 543 Uncharacterized protein MJ0274. FT /FTId=PRO_0000106766. FT DOMAIN 470 534 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. SQ SEQUENCE 543 AA; 62048 MW; 8D2D2966EC84D4DA CRC64; MLIRFITDSA KPIVIIGDFL VIIMMIGRAL ILDGYTDEPA GLGVPPYIGI YPRYAYGALD KYNVKVDYIT IDKFREIRGD FNLNKYDAII CICGFHTPGK YLNANPATLK EFVSILYKYD GLKILGGPAA TKYGSSMIGG KIEDESKYKA FFDVVAEGDL EAVLNDLLRE GSIEKIDFNR YRTYEELREY AIRGAKVVKK HPNYPYIIAE IETYRGCPRA LTGGCSFCTE PRRFGLPKFR DEKDIIDEIK VLYNEGIKYF RIGRQPCMFS YKSIDSEKEE VPKPNVEAIE KLFKGIRNVS NPKVLHIDNA NPAVIARHED ESREVAKILV KYCTSGNVAA FGVESFDEKV IKANNLLTTP EDVLKAVEIL NEVGGKRGET GLPYLLPGIN LLFGLKGERK ETFTINFEYL KEIYDRGFMI RRINIRQVVP FFGTDITLKD IKKAEKRKKL FLWFKEKVRE EIDNKMLKRV VPKGTILRDV FVEVKEREDL YFGRQFGSYP LLVGILDKNL KIGEFVDVEV VDYGRRSITG KVVRDIRKIH IVG // ID Y27B_METJA Reviewed; 148 AA. AC P81234; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0275.1; GN OrderedLocusNames=MJ0275.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0696. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98263.1; -; Genomic_DNA. DR STRING; 243232.MJ_0275.1; -. DR EnsemblBacteria; AAB98263; AAB98263; MJ_0275.1. DR KEGG; mja:MJ_0275.1; -. DR eggNOG; arCOG09660; Archaea. DR eggNOG; ENOG4110ZMV; LUCA. DR OMA; NSIQINL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 148 Uncharacterized protein MJ0275.1. FT /FTId=PRO_0000106769. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. SQ SEQUENCE 148 AA; 17356 MW; 305E22EC236661CD CRC64; MCGIMRVYRV YNAYKIVGAV IFSMSIIVIL YISIILHSLK LSFSIILAVD ILIIALFAYI FLKPKKLVVL DNGIKVDNEF YSWDEVIEFF VSLNSIQINL KGKREETFNW ETPGLFKYRP QIEYVVKKDA ELLKILREKI ENKERKRG // ID Y282_METJA Reviewed; 149 AA. AC Q57730; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0282; GN OrderedLocusNames=MJ0282; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98270.1; -; Genomic_DNA. DR PIR; C64335; C64335. DR ProteinModelPortal; Q57730; -. DR STRING; 243232.MJ_0282; -. DR EnsemblBacteria; AAB98270; AAB98270; MJ_0282. DR KEGG; mja:MJ_0282; -. DR eggNOG; arCOG00518; Archaea. DR eggNOG; COG3576; LUCA. DR InParanoid; Q57730; -. DR KO; K07006; -. DR OMA; GYQIKGT; -. DR PhylomeDB; Q57730; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0004733; F:pyridoxamine-phosphate oxidase activity; IEA:InterPro. DR Gene3D; 2.30.110.10; -; 1. DR InterPro; IPR011576; Pyridox_Oxase_FMN-bd. DR InterPro; IPR012349; Split_barrel_FMN-bd. DR Pfam; PF01243; Pyridox_oxidase; 1. DR SUPFAM; SSF50475; SSF50475; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 149 Uncharacterized protein MJ0282. FT /FTId=PRO_0000106771. SQ SEQUENCE 149 AA; 16574 MW; CD913E94F5813601 CRC64; MKMFHKIYFG DSVVKLTEEM VKSLENEIVF IATASKDGVP NVAAMRAIKV LDAEKGIVLI ADNFMNKTLK NILENPKVAL TTANCKDMPY QYKGTAEYYK EGEYLKIAEE VDKALKPDLK PKGAVVIKIT EIYNLKSGPD AGKLIAKDE // ID Y284_METJA Reviewed; 219 AA. AC Q57732; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0284; GN OrderedLocusNames=MJ0284; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98272.1; -; Genomic_DNA. DR PIR; E64335; E64335. DR ProteinModelPortal; Q57732; -. DR STRING; 243232.MJ_0284; -. DR EnsemblBacteria; AAB98272; AAB98272; MJ_0284. DR KEGG; mja:MJ_0284; -. DR eggNOG; arCOG00910; Archaea. DR eggNOG; COG2263; LUCA. DR InParanoid; Q57732; -. DR KO; K07579; -. DR OMA; QNPPFGI; -. DR PhylomeDB; Q57732; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR SUPFAM; SSF53335; SSF53335; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 219 Uncharacterized protein MJ0284. FT /FTId=PRO_0000106772. SQ SEQUENCE 219 AA; 25139 MW; 04DD0C9ACBF4E51B CRC64; MIKKKHLEMM LDSLKRHPNP KADLEQYTID GKLAADILFF AVNDFYNNVV IDLGCGTGRL AIGSKILGAK RAIGIDIDRE SIEAAKENAK KLNVDVDFYC MDIRDVDDEF LNNVLGEDRD LKRVVIQNPP FGAQKKHADR VFLDKALEIG DIIYTIHNYP TKDFVIKYVE DKGGKITHIY EAFFRIPAIY EFHKKKVVEI PVVIFRIEKL GFETVFNFL // ID Y286_METJA Reviewed; 117 AA. AC Q57734; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0286; GN OrderedLocusNames=MJ0286; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98275.1; -; Genomic_DNA. DR PIR; G64335; G64335. DR STRING; 243232.MJ_0286; -. DR EnsemblBacteria; AAB98275; AAB98275; MJ_0286. DR KEGG; mja:MJ_0286; -. DR eggNOG; arCOG09661; Archaea. DR eggNOG; ENOG4111176; LUCA. DR OMA; EIKWISM; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 117 Uncharacterized protein MJ0286. FT /FTId=PRO_0000106773. SQ SEQUENCE 117 AA; 14099 MW; 09DCBDDD263919C5 CRC64; MKKFGTVLLS DIVKECLSGD EFAREMMEDL FNFLIKLRLW RWKYLLSQNQ KNEIQMSDLL ALIKEEKEGI NRLFSFLYQT DIPVENRIEI LMLLKEFVKE EIKWISMDVS EINFVKK // ID Y288_METJA Reviewed; 178 AA. AC Q57736; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0288; GN OrderedLocusNames=MJ0288; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98281.1; -; Genomic_DNA. DR PIR; A64336; A64336. DR ProteinModelPortal; Q57736; -. DR STRING; 243232.MJ_0288; -. DR DNASU; 1451143; -. DR EnsemblBacteria; AAB98281; AAB98281; MJ_0288. DR KEGG; mja:MJ_0288; -. DR eggNOG; arCOG09662; Archaea. DR eggNOG; ENOG411113H; LUCA. DR OMA; KVAIMVV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 178 Uncharacterized protein MJ0288. FT /FTId=PRO_0000106775. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. SQ SEQUENCE 178 AA; 19266 MW; 7F0DE50289012476 CRC64; MKKFSAIFGL LSVIFVIMAI SQVSGLSGAI TPPKIDIMVN ASNGLPQDIN SIIYVKNPNS FPVKVEMVTT GDLNNSKKVE VKIMKNNFTL KPGETVGVNI TFTVKEKDNY EGDILTKISP VDYGDDKKGV NLKASVVLPT KVAIMVVGNE IHTKELVITA VLIISILGLG AMLIRRHL // ID Y289_METJA Reviewed; 338 AA. AC Q57737; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0289; GN OrderedLocusNames=MJ0289; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98282.1; -; Genomic_DNA. DR PIR; B64336; B64336. DR STRING; 243232.MJ_0289; -. DR EnsemblBacteria; AAB98282; AAB98282; MJ_0289. DR KEGG; mja:MJ_0289; -. DR eggNOG; arCOG09663; Archaea. DR eggNOG; ENOG4110ZR5; LUCA. DR OMA; LEVNFTL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 338 Uncharacterized protein MJ0289. FT /FTId=PRO_0000106776. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TRANSMEM 318 338 Helical. {ECO:0000255}. SQ SEQUENCE 338 AA; 36045 MW; 74A5CE21F5273AEC CRC64; MFEMKNSTRY ILSLLLSIIM GVAVMGSTFA ISTTYGTGHT TATVDNLKPV VNCSSYEMVI RTVQGIKVYE YKNTTGVTPG LLRSDALEAY AYTGEGVTFY VNVSDPNGEQ DLQTNGAGVD FLLVPQGQSP SNPTYVIHAG FDTSTSGDAD LTTLTFYAQW TVPAGAYGCF DVYVKATDKH GACTGYIKKG KIFLNPMIGI NVTKDNDAYP APFTGLSFGN VNPGDTNVPA TENVVTIHNI DPDGVGTKIA VFVSATSMTQ AGGTGIIPAE NIKAHVIKAN NMTQSYNTHL QNNVKVLLWQ PLKPCHTNAL EVNFTLDVPT PLPSGCYGGS ITFYGLGL // ID Y309_METJA Reviewed; 284 AA. AC Q57757; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein MJ0309; GN OrderedLocusNames=MJ0309; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00742}; CC -!- SIMILARITY: Belongs to the arginase family. {ECO:0000255|PROSITE- CC ProRule:PRU00742}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98295.1; -; Genomic_DNA. DR PIR; F64338; F64338. DR ProteinModelPortal; Q57757; -. DR STRING; 243232.MJ_0309; -. DR EnsemblBacteria; AAB98295; AAB98295; MJ_0309. DR KEGG; mja:MJ_0309; -. DR eggNOG; arCOG01700; Archaea. DR eggNOG; COG0010; LUCA. DR InParanoid; Q57757; -. DR KO; K01480; -. DR OMA; KRNKFVT; -. DR PhylomeDB; Q57757; -. DR BRENDA; 3.5.3.11; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.800.10; -; 1. DR InterPro; IPR005925; Agmatinase-rel. DR InterPro; IPR006035; Ureohydrolase. DR InterPro; IPR023696; Ureohydrolase_domain. DR InterPro; IPR020855; Ureohydrolase_Mn_BS. DR PANTHER; PTHR11358; PTHR11358; 1. DR Pfam; PF00491; Arginase; 1. DR PIRSF; PIRSF036979; Arginase; 1. DR PRINTS; PR00116; ARGINASE. DR TIGRFAMs; TIGR01230; agmatinase; 1. DR PROSITE; PS01053; ARGINASE_1; 1. DR PROSITE; PS51409; ARGINASE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 284 Uncharacterized protein MJ0309. FT /FTId=PRO_0000173784. FT METAL 110 110 Manganese 1. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 133 133 Manganese 1. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 133 133 Manganese 2. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 135 135 Manganese 2. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 137 137 Manganese 1. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 211 211 Manganese 1. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 211 211 Manganese 2. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. FT METAL 213 213 Manganese 2. {ECO:0000255|PROSITE- FT ProRule:PRU00742}. SQ SEQUENCE 284 AA; 32477 MW; 0F76B94B1562236E CRC64; MEEHFIDLSK FMMANCPYEE AEGVIFSIPY DETTSFKPGA REGGNAIRTA SWGLETYSPI LDRDLAELKY CDLKDLDLYG SQEEIFGTIH SVSREILKEN KKIIVFGGEH SITYPIIKAV KDIYDDFIVI QFDAHCDLRD EYLGNKLSHA CVMRRVYELT KNIFQFGIRS GDKEEWDLAR KNNLYLKMDL MNKDDLEYIK SLDKPIYVTI DIDVLDPAYA PGTGTPEPCG FSTRELFNSL YLLEEVKDKI IGFDIVEVSP IYDIANITAI TAAKIARELM LMIL // ID Y328_METJA Reviewed; 146 AA. AC Q57774; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0328; GN OrderedLocusNames=MJ0328; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98316.1; -; Genomic_DNA. DR PIR; H64340; H64340. DR STRING; 243232.MJ_0328; -. DR EnsemblBacteria; AAB98316; AAB98316; MJ_0328. DR KEGG; mja:MJ_0328; -. DR eggNOG; arCOG09635; Archaea. DR eggNOG; ENOG4111TKP; LUCA. DR OMA; EKYNEDI; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 146 Uncharacterized protein MJ0328. FT /FTId=PRO_0000106797. SQ SEQUENCE 146 AA; 16795 MW; 418FFB0F00662027 CRC64; MPNNTNNKLC KVCNSPHRAE IEALYFQGWG AKKISKYLKE KYNEDISYSA ILRHMQNHVK PQLLEAIEEE TTEIYSKMYK EIANNFGLAL EGLFTMIKTA KKDLENPKAT AREKEVAGRN LVMAIREMKE LLQLTEDKEG ADDIDL // ID Y33A_METJA Reviewed; 132 AA. AC P81306; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0332.1; GN OrderedLocusNames=MJ0332.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98330.1; -; Genomic_DNA. DR STRING; 243232.MJ_0332.1; -. DR EnsemblBacteria; AAB98330; AAB98330; MJ_0332.1. DR KEGG; mja:MJ_0332.1; -. DR eggNOG; arCOG09639; Archaea. DR eggNOG; ENOG41110N7; LUCA. DR OMA; LYQSMAL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 132 Uncharacterized protein MJ0332.1. FT /FTId=PRO_0000106802. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. SQ SEQUENCE 132 AA; 14972 MW; 6E11E1A58AB1641D CRC64; MMNGENMDKQ TVIGFVVLFC VLELVFYLKK LYQSMALTLA VFGIFSLLFF LLYIPVLSKK AVPYVINYFK PPHQRVREIK VGSDETTDNS IIRLKEKAKT LHPDEGNRIS GRSSNSFKDS ASCIITIVDD SN // ID Y3409_METJA Reviewed; 237 AA. AC Q60308; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 48. DE RecName: Full=Uncharacterized protein MJECS09; GN OrderedLocusNames=MJECS09; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37067.1; -; Genomic_DNA. DR PIR; A64517; A64517. DR EnsemblBacteria; AAC37067; AAC37067; MJ_ECS09. DR KEGG; mja:MJECS09; -. DR Proteomes; UP000000805; Plasmid small ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJECS09. FT /FTId=PRO_0000107490. SQ SEQUENCE 237 AA; 28011 MW; 06A87D28E3683F85 CRC64; MPLPEYGTDN SDNFVRFIYF EIKKNSVKPP SFPKLGKYLE NHCKGGDYMC VINNYIYFLI IIDLEYLVKW IKCYSDNVLK GTIKLLTNYY SKLYYIKLSL SHWLFSLCNL PLEDEMLFLS CGSLVKYQDA STHKLYKLEY LTKLILGYNR INVDNCICSI KVFAISTFER FLYHEFENNA FKLIMLHKRT SFNVYKVKTS KIALLNILEK IGRTYKRYLH TLKTPKNLTT TEVVRHG // ID Y3410_METJA Reviewed; 286 AA. AC Q60309; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJECS10; GN OrderedLocusNames=MJECS10; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37068.1; -; Genomic_DNA. DR PIR; B64517; B64517. DR ProteinModelPortal; Q60309; -. DR EnsemblBacteria; AAC37068; AAC37068; MJ_ECS10. DR KEGG; mja:MJECS10; -. DR Proteomes; UP000000805; Plasmid small ECE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Plasmid; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 286 Uncharacterized protein MJECS10. FT /FTId=PRO_0000107491. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TRANSMEM 231 251 Helical. {ECO:0000255}. SQ SEQUENCE 286 AA; 33271 MW; E4A26112108033A9 CRC64; MNFKKVSNMP DEIICNFYVN ISYLEISATY DSKNKRYSLS SKTGNFNVGV KGFEKLLSIF EKIGHVMKIN EKTYKIIIQN KILNLKHLYS KKNKTHTLEI LDEYNNLMKL SGKKLIDVAL QLFKTFKINE NIENSLNVKK TENDIQIINN NQNLKIEENI NDSKTKENDN KCYREIIDRV LKSRSEQLFI ENLENIPPKS VIYSITGAFS FIFGLGVLCE TLESGKIRWK AIILGFIILI LILAIVNYLM MKEKNVDEHE YNIPTKLMED VYTTDCENFP CGYFPK // ID Y346_METJA Reviewed; 101 AA. AC Q57792; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0346; GN OrderedLocusNames=MJ0346; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98336.1; -; Genomic_DNA. DR PIR; B64343; B64343. DR STRING; 243232.MJ_0346; -. DR EnsemblBacteria; AAB98336; AAB98336; MJ_0346. DR KEGG; mja:MJ_0346; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 101 Uncharacterized protein MJ0346. FT /FTId=PRO_0000106816. SQ SEQUENCE 101 AA; 11750 MW; A467A4DB2728BF87 CRC64; MEDMITLTDE RKTVKFENLP EIYVRVHDEA KGLVLTVKNP YDTDVYAKVY YAPDGENYDT VTSEVVKYDY QAQKTELIPI KHPYMKISFD SAVSGWVSYI K // ID Y350_METJA Reviewed; 88 AA. AC Q57796; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0350; GN OrderedLocusNames=MJ0350; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98339.1; -; Genomic_DNA. DR PIR; F64343; F64343. DR STRING; 243232.MJ_0350; -. DR EnsemblBacteria; AAB98339; AAB98339; MJ_0350. DR KEGG; mja:MJ_0350; -. DR eggNOG; arCOG09653; Archaea. DR eggNOG; ENOG4110ZMW; LUCA. DR OMA; CRTERIE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 88 Uncharacterized protein MJ0350. FT /FTId=PRO_0000106821. SQ SEQUENCE 88 AA; 10593 MW; 58E111FC57ECA619 CRC64; MAKVRHGCRT ERIELIIKIN HLKRENLKLR NKIADYKRTL YLIRGKGCKL TEELLKIEIE NCIKMIKFNE ETIRDLKEKV EMIPNEQL // ID Y3511_METJA Reviewed; 114 AA. AC Q60273; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJECL11; GN OrderedLocusNames=MJECL11; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37084.1; -; Genomic_DNA. DR PIR; C64511; C64511. DR ProteinModelPortal; Q60273; -. DR EnsemblBacteria; AAC37084; AAC37084; MJ_ECL11. DR KEGG; mja:MJECL11; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003959; ATPase_AAA_core. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13304; AAA_21; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJECL11. FT /FTId=PRO_0000107503. SQ SEQUENCE 114 AA; 12826 MW; 99A168C6C180676B CRC64; MGEGFKSALI IALLTSILKN GYLLIDSAEA FHHPSSLEIT SQMLTKSVKN NNVQVFLTTH SLELIDFLLE HASKEGIEGR LIYMRRDGEN LISSMESFEN VREMRETLGI DLRG // ID Y3513_METJA Reviewed; 602 AA. AC Q60275; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized MCM-type protein MJECL13; GN OrderedLocusNames=MJECL13; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MCM domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37086.1; -; Genomic_DNA. DR PIR; E64511; E64511. DR ProteinModelPortal; Q60275; -. DR PRIDE; Q60275; -. DR EnsemblBacteria; AAC37086; AAC37086; MJ_ECL13. DR KEGG; mja:MJECL13; -. DR HOGENOM; HOG000224127; -. DR InParanoid; Q60275; -. DR OMA; IECILEC; -. DR PhylomeDB; Q60275; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031327; MCM. DR InterPro; IPR018525; MCM_CS. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Complete proteome; DNA replication; KW DNA-binding; Nucleotide-binding; Plasmid; Reference proteome; KW Transcription; Transcription regulation. FT CHAIN 1 602 Uncharacterized MCM-type protein MJECL13. FT /FTId=PRO_0000194132. FT DOMAIN 271 472 MCM. FT NP_BIND 315 322 ATP. {ECO:0000255}. SQ SEQUENCE 602 AA; 69323 MW; 07C1EABB3D305AD3 CRC64; MINMCYNFEN VKKAYEDQLK NYIKNSLIPN LSSHANNEVV KISMKKLANL GFGYLVDSTL SSITGYYKVR DWIEELLKEE LQKSGENKCC NIVLCDYPEE FEISMREIPY YVNKVVKFNG VIISASYPCV LSKKHLYICP KCGRIKEVYF SELFWDDKVF CEFCGGKMEF ANVMDYENFQ ELVVQDLSDE SEYYGIEKNP IVWYCGAKPY YFGHVKITGI VREVPRSSKS RIYELIVQAI NVEKLGVEKS LINLTEEDVK NIKKVAKRGD IIDILADILI PPLLCDDAIV RKAILIQQIA PYLEDIGKIN ILLVTEVGID KTAILKRIGN IPGNNFINIA ALKEEELATP YDKRSNILGK FYTVCGGVIP RTLGVLCIDD FNENNKLSTK LSEAFERNVL TTNKGSFYCV PAECSFLCAC YPKTKFRKFD QKKSIIKQIG ISSILLKNFD LIFPIRDIPD KDRDEEVAKY IFLKYINSDN EEIEGYDYVF VDVGGEKIKI DFEFLKKYVV YSRQITPKIT DEVIEKISNW YDEMRKNHYI TAKQLNTVIK LSIAVARAKL KECVDEDDVK EAIDIIMHYL KQVVYNPKKG IIDVILLYKN KT // ID Y3515_METJA Reviewed; 365 AA. AC Q60277; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Uncharacterized ATP-binding protein MJECL15; GN OrderedLocusNames=MJECL15; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37088.1; -; Genomic_DNA. DR PIR; G64511; G64511. DR PDB; 3H92; X-ray; 2.20 A; A=274-365. DR PDBsum; 3H92; -. DR ProteinModelPortal; Q60277; -. DR SMR; Q60277; 312-365. DR EnsemblBacteria; AAC37088; AAC37088; MJ_ECL15. DR KEGG; mja:MJECL15; -. DR HOGENOM; HOG000154927; -. DR InParanoid; Q60277; -. DR KO; K06921; -. DR OMA; GMPIKVP; -. DR PhylomeDB; Q60277; -. DR EvolutionaryTrace; Q60277; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Plasmid; Reference proteome. FT CHAIN 1 365 Uncharacterized ATP-binding protein FT MJECL15. FT /FTId=PRO_0000184679. FT NP_BIND 29 36 ATP. {ECO:0000255}. FT HELIX 281 299 {ECO:0000244|PDB:3H92}. FT HELIX 306 318 {ECO:0000244|PDB:3H92}. FT STRAND 320 323 {ECO:0000244|PDB:3H92}. FT HELIX 324 326 {ECO:0000244|PDB:3H92}. FT HELIX 329 337 {ECO:0000244|PDB:3H92}. FT STRAND 340 344 {ECO:0000244|PDB:3H92}. FT TURN 345 348 {ECO:0000244|PDB:3H92}. FT STRAND 349 354 {ECO:0000244|PDB:3H92}. FT HELIX 355 364 {ECO:0000244|PDB:3H92}. SQ SEQUENCE 365 AA; 43299 MW; C3D54F7DCD1A8789 CRC64; MKFFNREKEI NEILLILEEE PNNIYFIYGP LNSGKSTLIR EVITNRLDKS KYIPFFIDFR TRNILNVDNF IECLFEVDEK SKIDDFREYA KSLADLLVKG SEEISKYYLG MPIKVPKPFF DRIFSKRDKS ADVYQYIEYL FAKLNEKGKK PILIFDELQM IREITLNGNR LLLWSLFQFL VALTKVQHLC HVFCLSSDSL FIEYIYGKAE LKGGVDYILV DDFDKKTALK FMDFLAKQKN INLTNEDKEL IYSYVGGKAK YIYDVIVKLK AVKDLKYILE TKLEEERNHL EELLEKVEED YEGINYDEVL EALKLFKDNY ELPKSKIKRK IRIFLIKENI LFLNPQKGTL KPQSYLVWNA IKRML // ID Y352_METJA Reviewed; 239 AA. AC Q57798; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0352; GN OrderedLocusNames=MJ0352; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98341.1; -; Genomic_DNA. DR PIR; H64343; H64343. DR ProteinModelPortal; Q57798; -. DR STRING; 243232.MJ_0352; -. DR EnsemblBacteria; AAB98341; AAB98341; MJ_0352. DR KEGG; mja:MJ_0352; -. DR eggNOG; arCOG09665; Archaea. DR eggNOG; ENOG410Z7YE; LUCA. DR OMA; EANEHLP; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 239 Uncharacterized protein MJ0352. FT /FTId=PRO_0000106823. SQ SEQUENCE 239 AA; 27547 MW; 98C05CE3E6595316 CRC64; MCKYELAAKA HKNVYGVEIE VEEIKKQVEE IRKEHNNWID ESAAFVKWLE TLELKDEFKK LREEERMNKN GNSIEVKASN NAMVVLEKTA EKVDSLDDVI EKMDSLDEDL MLLDEANEHL PLAYTYPDKK TGKEKIILSW AGIVKAMRMQ GNIEVEPPTF QEVNGKIIAT CRVRDLKRNI VMVGTAERVS PGRMGEEFKY TVLASKAIRN ALKHIIEPKY LQMVIAEAKK RKSYVIITY // ID Y3539_METJA Reviewed; 351 AA. AC Q60294; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=UPF0252 protein MJECL39; GN OrderedLocusNames=MJECL39; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0252 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37108.1; -; Genomic_DNA. DR PIR; F64514; F64514. DR ProteinModelPortal; Q60294; -. DR EnsemblBacteria; AAC37108; AAC37108; MJ_ECL39. DR KEGG; mja:MJECL39; -. DR OMA; VINIWIN; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007562; Transglutaminase-like_domain. DR Pfam; PF04473; DUF553; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Plasmid; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 351 UPF0252 protein MJECL39. FT /FTId=PRO_0000159556. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. SQ SEQUENCE 351 AA; 41438 MW; AACBF7C32BC213B0 CRC64; MPILLEHIQL NDEDLKDTKH LAEILKYKNN SIKTIINVLE WEDSNIRYCY EKSNVYYFIT FFIIVGLVWA IFPEVWLWCE QVFCISPTIH IIICCLYFII TIILFLFLCG VVGTFLHLWA TFFTLSKCDS KILKLKEGLF TTLSLIWIST SLKTILKTKY AICRDYAKLT SAILHNLNIK HYFLVYPTHV AVAVKIDDYY YVIDQKLPIY KIDVWLKKLG KEKVKIYTPV DIYNSKLKFV EKYYKNENNL KSEISDDILR KIEEDVKKEL QIKNAEQYNK KVEPIPVKLS IPIENYDEIT HYSIVRVISK EIYNKFLTNI KNVSNIEIKK DEGKFAVNVY YEIPNSIPNS K // ID Y360_METJA Reviewed; 135 AA. AC Q57806; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0360; GN OrderedLocusNames=MJ0360; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98352.1; -; Genomic_DNA. DR PIR; H64344; H64344. DR STRING; 243232.MJ_0360; -. DR EnsemblBacteria; AAB98352; AAB98352; MJ_0360. DR KEGG; mja:MJ_0360; -. DR eggNOG; arCOG10172; Archaea. DR eggNOG; ENOG410ZUVW; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 135 Uncharacterized protein MJ0360. FT /FTId=PRO_0000106831. FT TRANSMEM 4 24 Helical. {ECO:0000255}. SQ SEQUENCE 135 AA; 14803 MW; E1938F1628AA213F CRC64; MKRLGVFLIL ASIVCGVVAI CGCTGGGGTD YSSSTASAET ETCPVQILEH HLVRKDYGTV YVEGVAQNVG NKRLKFVEIK ARFYDADGVL IDEFMDVHRD VDPGQKFRFK IIGPIGEEGK KVAKYDIAVG TWWTE // ID Y361_METJA Reviewed; 107 AA. AC Q57807; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 88. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0361; GN OrderedLocusNames=MJ0361; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98353.1; -; Genomic_DNA. DR PIR; A64345; A64345. DR ProteinModelPortal; Q57807; -. DR STRING; 243232.MJ_0361; -. DR EnsemblBacteria; AAB98353; AAB98353; MJ_0361. DR KEGG; mja:MJ_0361; -. DR eggNOG; arCOG01057; Archaea. DR eggNOG; COG1733; LUCA. DR InParanoid; Q57807; -. DR OMA; GRIPKNY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 107 Uncharacterized HTH-type transcriptional FT regulator MJ0361. FT /FTId=PRO_0000160632. SQ SEQUENCE 107 AA; 12343 MW; A1BF198CE20561EE CRC64; MILKILAKKH VKDVLKLLNS KDMYFSELQK TLNLHPKILD SILSDLVNEG FVEKREGESP YKFGKVYYSI TPRGKRALEI LDLIETFDTL REGQDIVINY KIVNSTA // ID Y395_METJA Reviewed; 158 AA. AC Q57838; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0218 protein MJ0395 {ECO:0000255|HAMAP-Rule:MF_00590}; GN OrderedLocusNames=MJ0395; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0218 family. {ECO:0000255|HAMAP- CC Rule:MF_00590}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98385.1; -; Genomic_DNA. DR PIR; C64349; C64349. DR ProteinModelPortal; Q57838; -. DR STRING; 243232.MJ_0395; -. DR EnsemblBacteria; AAB98385; AAB98385; MJ_0395. DR KEGG; mja:MJ_0395; -. DR eggNOG; arCOG04076; Archaea. DR eggNOG; COG1909; LUCA. DR InParanoid; Q57838; -. DR KO; K09735; -. DR OMA; LAIYDHK; -. DR PhylomeDB; Q57838; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00590; UPF0218; 1. DR InterPro; IPR007164; DUF359. DR Pfam; PF04019; DUF359; 1. DR PIRSF; PIRSF006533; UCP006533; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 158 UPF0218 protein MJ0395. FT /FTId=PRO_0000137608. SQ SEQUENCE 158 AA; 17968 MW; 56C5423CB778FC8B CRC64; MLVLPEELRE KLKKPFGKVY KTLPDIDGDI VTVGDIVTKT AIENNIIPKL SIFDLKTRRN IPVKINHVFK KVIKVKNPPG CISDEAIESI KYLSTINDRN IALLVDGEED LLALIVIKYF PIGTYVLYGQ PDEGIVVLKI NKKLKQEIEE ILKQFKKI // ID Y398_METJA Reviewed; 271 AA. AC Q57841; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0398; GN OrderedLocusNames=MJ0398; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98393.1; -; Genomic_DNA. DR PIR; F64349; F64349. DR ProteinModelPortal; Q57841; -. DR EnsemblBacteria; AAB98393; AAB98393; MJ_0398. DR KEGG; mja:MJ_0398; -. DR eggNOG; arCOG03156; Archaea. DR eggNOG; COG3780; LUCA. DR InParanoid; Q57841; -. DR KO; K07500; -. DR OMA; YIIGVYF; -. DR PhylomeDB; Q57841; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR Gene3D; 3.10.28.10; -; 2. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR004860; LAGLIDADG_2. DR Pfam; PF14528; LAGLIDADG_3; 1. DR SUPFAM; SSF55608; SSF55608; 2. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 271 Uncharacterized protein MJ0398. FT /FTId=PRO_0000106852. FT DOMAIN 77 205 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 271 AA; 32120 MW; 63C4432642CB3644 CRC64; MVNLKELSQN EVLELINYVK SLRKQNFSYS QISKKIEIER NIKISKSTII RWCKNSNNPF NKTKFIDLSP SPELSYIIGV YFGDANIYYR KKTGSYYFRI KVVDKDFVDV VKNSLIKIGL NPTISYVEEK TRSNRWHVEA SSKSLYKFLS QNKEELFKVA EKYPEDFLRG FFDSEGYVTS NKIALENYDL ELLEFSKELL KKLDVHSTIH IAKKKGTESN IRGEIYHYKD DFYRLSIHRK ESVRNFAIKV SFSIKRKRER LQKLLESMDK H // ID Y409_METJA Reviewed; 703 AA. AC O53113; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0409; GN OrderedLocusNames=MJ0409; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98405.1; -; Genomic_DNA. DR PIR; A64351; A64351. DR ProteinModelPortal; O53113; -. DR STRING; 243232.MJ_0409; -. DR EnsemblBacteria; AAB98405; AAB98405; MJ_0409. DR KEGG; mja:MJ_0409; -. DR eggNOG; arCOG06686; Archaea. DR eggNOG; ENOG410YC0C; LUCA. DR OMA; FAYINKV; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 703 Uncharacterized protein MJ0409. FT /FTId=PRO_0000106858. FT COMPBIAS 86 203 Tyr-rich. SQ SEQUENCE 703 AA; 81654 MW; A74D0DF5037D0545 CRC64; MKKLIFVVLL LAVISYTYPS NLDYKYTSSI PIEFVKLSEI KNVDELNRLL NSNALVIFCL DSNNINKDIL YHLGIKRYNP SEIPDYGNYS YVSINGVIVV YPKYSVYEEN GALIYNPPKE ENYSKYEFVR PYKIKVPNVS KIPDYGGYVL IENSTFILYP KKYIIRGDEG GIYYIPPKNS SDNYYYKYSY NLPEKCIPDY YDYVFIDNNG IFIIYPKKYV VRSNDGVLVF SPPVDAKEAP IYKIDYKKID EGVYEIKKNK LLFLYPTTLN NKSTLDIIGE YIAKNGGVFA YINKVPPYYK HMLATGVAID KVIPDESGSY AIDVAGRKIK VDVLDDEIIN NKLKCIKALK ALGINVSYIV TGSEGIDIVE KSNVDTDELE DLYNYYWFKK WWQNYTHLYF NPSQLKNIEF NGFEDILALS YYPLIYVDKA PETFRNDPIG GYYPKVISYK GTKNYGYWEE GAKSENVYYH LDEGEPYWDG KANEPSKWYY EGQPVSMEND SEMWNRYEYF NHWFVKNYAY ALANGCDGLF LESSDKNLID AIFGNDNENL SWKLDIKNKV DYVVIPGNKG FEVINGIPVI RIPSPLKEVY GANVINTLYI PPKDEDFGIY ISDIRNYNTN LVVELKENGT DIVSFKDLAD WLNKYYRNNI FYNGTAIKIW DNRGIKITIF KKNFGMGNYT FEEFDKEHCK YVIVNPPKII PLK // ID Y414_METJA Reviewed; 395 AA. AC Q57857; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0414; GN OrderedLocusNames=MJ0414; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98403.1; -; Genomic_DNA. DR PIR; F64351; F64351. DR ProteinModelPortal; Q57857; -. DR STRING; 243232.MJ_0414; -. DR EnsemblBacteria; AAB98403; AAB98403; MJ_0414. DR KEGG; mja:MJ_0414; -. DR eggNOG; arCOG04218; Archaea. DR eggNOG; COG1423; LUCA. DR InParanoid; Q57857; -. DR KO; K07468; -. DR OMA; ICPFTTK; -. DR PhylomeDB; Q57857; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR021122; RNA_ligase_dom_REL/Rnl2. DR InterPro; IPR001072; Uncharacterised_MJ0414. DR Pfam; PF09414; RNA_ligase; 1. DR PRINTS; PR01048; Y414FAMILY. DR TIGRFAMs; TIGR01209; TIGR01209; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 395 Uncharacterized protein MJ0414. FT /FTId=PRO_0000106860. SQ SEQUENCE 395 AA; 46417 MW; 47AD62037D44D33B CRC64; MRLIMMKVSA YDLNKIAEKL NLSIKDLNKA FSRKILREDE YKEIKTLLFK KEFKGIEKGT VIFLNDNLDV VRGYPKTYRA ITLYPTIKKH FIDKVVIEEK LNGYNIRIVK IDGEVYALTR SGYICPFTTK KVKKFLNLEI LDDYSEYMLC GEMIGINNPY TPYYYKEVDR GFENLGFYIF DIKERETNKS LPIKERINLC EKYNLPYVKP LAVVDKDEAH IHVREIIEKL NKEGREGVVL KDPDMAVSPI KYTTHYTQCE DLKSAFTFFF DLGMDFLFSR VVREGFMSYE FKETLEERKN RAKDLGEAIL LPMVETINKV ASGERVSEDF ELIFDSEEDF DEFLDFMRKM KMVITIKNIE KIDTEEGVKI KAVIGKIYNK TNDKIISYLN GTLWE // ID Y416_METJA Reviewed; 190 AA. AC Q57859; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Double zinc ribbon protein MJ0416; GN OrderedLocusNames=MJ0416; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 DZANK-type zinc finger. {ECO:0000255}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98407.1; -; Genomic_DNA. DR PIR; H64351; H64351. DR ProteinModelPortal; Q57859; -. DR STRING; 243232.MJ_0416; -. DR EnsemblBacteria; AAB98407; AAB98407; MJ_0416. DR KEGG; mja:MJ_0416; -. DR eggNOG; arCOG01917; Archaea. DR eggNOG; ENOG410XV0G; LUCA. DR OMA; PYCGYRL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR025874; DZR. DR Pfam; PF12773; DZR; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 190 Double zinc ribbon protein MJ0416. FT /FTId=PRO_0000106862. FT ZN_FING 134 183 DZANK-type. {ECO:0000255}. SQ SEQUENCE 190 AA; 21889 MW; D7E2AB55B759606F CRC64; MVRVVPLTDE EKMSIVSGLR SSVPATKLVT LRKLQEIAEV RPEAILYLDT YDKVTLNEII TLLNQIIEYD PDEILRREAM ITLEKVKKAL GTKFSTFVPL CNSCKSPIDL GWTYCTNCGA EIKNMTFEEE VERCPNCNNY ISDSWKYCAH CGAKLKEEEE EVLRCPNCKR PVQPEWIVCP YCGYRLKRKP // ID Y420_METJA Reviewed; 380 AA. AC Q57863; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=Uncharacterized protein MJ0420; GN OrderedLocusNames=MJ0420; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98408.1; -; Genomic_DNA. DR PIR; D64352; D64352. DR ProteinModelPortal; Q57863; -. DR STRING; 243232.MJ_0420; -. DR EnsemblBacteria; AAB98408; AAB98408; MJ_0420. DR KEGG; mja:MJ_0420; -. DR eggNOG; arCOG03207; Archaea. DR eggNOG; COG1822; LUCA. DR OMA; CEIGINY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002760; O_anti_polymase. DR Pfam; PF01901; O_anti_polymase; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 380 Uncharacterized protein MJ0420. FT /FTId=PRO_0000106866. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TRANSMEM 217 237 Helical. {ECO:0000255}. FT TRANSMEM 303 323 Helical. {ECO:0000255}. FT TRANSMEM 341 361 Helical. {ECO:0000255}. SQ SEQUENCE 380 AA; 43660 MW; 77E6B309C63B41B1 CRC64; MHICNIIEKI KKIDLFHPVS IVIIGHLMIF ILAFPYLDDI GLYSLFKILG VLSIFIVGFF LPFIFPMQIK FNRHILYLSF LLLSFLSIFG AFKITHSLFL SIAYLLFILI IAELFVKFYK KKIFVDILFS IGIIAFLLIV LIYGAIPLFN YEVRMTINSE PLRLISMGAL IYAGIENKVY FIIAFMILVL LGYKAGVLML FIAYIIYRYR NILFKYMVLL AFALLIFLGI MGKIILLSSN QNWDLNPIEL LCYRAYFDLY VLSKIVESNI LTLGKITLTP NGEHFIGELL FKYPHNITTT LFGTIYLDFG IFGGLFAMLL GVISKYIYEG DKKLYAIYAS LLLAYCEIGI NYGFLVVLSL LLYINAKLVF AKLLKLINEL // ID Y432_METJA Reviewed; 92 AA. AC Q57874; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0432; GN OrderedLocusNames=MJ0432; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98421.1; -; Genomic_DNA. DR PIR; H64353; H64353. DR ProteinModelPortal; Q57874; -. DR STRING; 243232.MJ_0432; -. DR EnsemblBacteria; AAB98421; AAB98421; MJ_0432. DR KEGG; mja:MJ_0432; -. DR eggNOG; arCOG00732; Archaea. DR eggNOG; COG1846; LUCA. DR InParanoid; Q57874; -. DR OMA; GLEYCEF; -. DR PhylomeDB; Q57874; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR027395; WH_DNA-bd_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF13601; HTH_34; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 92 Uncharacterized protein MJ0432. FT /FTId=PRO_0000106873. SQ SEQUENCE 92 AA; 10768 MW; FA5EDD9849A0DFB2 CRC64; MKIFNSVVRV KILALLYGLE YCEFNYLKEK LNLTDGNLEH HLKKLEECGF VETKKSVIKG RVKTIIKITN KGRVAFKNYI YEILQLSKNI EC // ID Y437_METJA Reviewed; 79 AA. AC Q57879; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0437; GN OrderedLocusNames=MJ0437; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98425.1; -; Genomic_DNA. DR PIR; E64354; E64354. DR STRING; 243232.MJ_0437; -. DR EnsemblBacteria; AAB98425; AAB98425; MJ_0437. DR KEGG; mja:MJ_0437; -. DR eggNOG; arCOG03076; Archaea. DR eggNOG; COG1563; LUCA. DR InParanoid; Q57879; -. DR KO; K14113; -. DR OMA; AYLYYAL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR025383; DUF4040. DR Pfam; PF13244; DUF4040; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 79 Uncharacterized protein MJ0437. FT /FTId=PRO_0000106876. FT TRANSMEM 28 48 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. SQ SEQUENCE 79 AA; 8717 MW; 5ECADEC8B82977C6 CRC64; MEIIHYIVII MTLLSSLASL LQRDLIKCII LSGFAGLCMA YLYYALLAPD VALTEAILGG AILPALFAFT VRRTQRIDE // ID Y457_METJA Reviewed; 410 AA. AC Q57899; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized metallohydrolase MJ0457; DE EC=3.-.-.-; GN OrderedLocusNames=MJ0457; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98445.1; -; Genomic_DNA. DR PIR; A64357; A64357. DR ProteinModelPortal; Q57899; -. DR STRING; 243232.MJ_0457; -. DR EnsemblBacteria; AAB98445; AAB98445; MJ_0457. DR KEGG; mja:MJ_0457; -. DR eggNOG; arCOG01107; Archaea. DR eggNOG; COG0624; LUCA. DR InParanoid; Q57899; -. DR KO; K01439; -. DR OMA; FKASQQD; -. DR PhylomeDB; Q57899; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR010182; ArgE/DapE. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. DR TIGRFAMs; TIGR01910; DapE-ArgE; 1. PE 3: Inferred from homology; KW Cobalt; Complete proteome; Hydrolase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 410 Uncharacterized metallohydrolase MJ0457. FT /FTId=PRO_0000185352. FT ACT_SITE 89 89 {ECO:0000250}. FT ACT_SITE 154 154 Proton acceptor. {ECO:0000250}. FT METAL 87 87 Cobalt or zinc 1. {ECO:0000250}. FT METAL 120 120 Cobalt or zinc 1. {ECO:0000250}. FT METAL 120 120 Cobalt or zinc 2. {ECO:0000250}. FT METAL 155 155 Cobalt or zinc 2. {ECO:0000250}. FT METAL 184 184 Cobalt or zinc 1. {ECO:0000250}. FT METAL 387 387 Cobalt or zinc 2. {ECO:0000250}. SQ SEQUENCE 410 AA; 47170 MW; 90E7ADB625339D86 CRC64; MDLIEEAIKL ESDLIRINSV NPSFGGKGEK EKAEYVKKKL MEYVESYNIE NYTLKEYNII DKYGIERPNI VFKIDFGRDK TLHIISHLDT VPEGDISLWG TNPYEPVIKD GKIYGRGSED NHKGIVSSLL LLKMIFENNI EPKYNLSLIF VSDEEDGSEY GLKYLLNNFE DEIFKKDDLI IVPDFGTPTG EFVEIGEKGI LWIKFNIKGK QCHGSTPENG LNADIVAFNF ANELYNGLYE KFDEINSIFL PEYSTFEPTI LKNKVENPNT IPGYVEVVFD CRILPTYKIE EVLEFINKFI KNFEFKKYIK HYDNSIKAEI TYEILKSENP NYTDENAEII KELKKAIKNV LNRDAKLCGM GGGTVAAFLR YKGYNVAVWG IGEETAHQPN EHIKIEDLVK MAEVFYEILK // ID Y501_METJA Reviewed; 202 AA. AC Q57924; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0501; GN OrderedLocusNames=MJ0501; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98492.1; -; Genomic_DNA. DR PIR; E64362; E64362. DR ProteinModelPortal; Q57924; -. DR STRING; 243232.MJ_0501; -. DR EnsemblBacteria; AAB98492; AAB98492; MJ_0501. DR KEGG; mja:MJ_0501; -. DR eggNOG; arCOG04894; Archaea. DR eggNOG; COG4073; LUCA. DR InParanoid; Q57924; -. DR OMA; PEFYFEI; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019218; DUF2119. DR Pfam; PF09892; DUF2119; 1. DR PIRSF; PIRSF005919; UCP005919; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 202 Uncharacterized protein MJ0501. FT /FTId=PRO_0000106902. SQ SEQUENCE 202 AA; 23743 MW; 8F407212641089A5 CRC64; MKIMEIFEFK GNGVKKLFIG GLHGNEGKFT EIILKDFVNS LKECNYIGDI VVIPKLVENS KYISTLSEKY YESDEGKTLI NIIKKYKPKV YFELHAYKKE NYKKLTSNNR KKVPPLIDIG NNVLIASISP ILRKRFSKED FCMTIEIPSW KVYEVKDEIL KILKIGAESL RREEIIEKLK KIYPEHIEKA EYFSKKYNLM LF // ID Y522_METJA Reviewed; 218 AA. AC Q57942; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0522; GN OrderedLocusNames=MJ0522; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98514.1; -; Genomic_DNA. DR PIR; B64365; B64365. DR STRING; 243232.MJ_0522; -. DR EnsemblBacteria; AAB98514; AAB98514; MJ_0522. DR KEGG; mja:MJ_0522; -. DR eggNOG; arCOG04833; Archaea. DR eggNOG; COG4078; LUCA. DR KO; K14099; -. DR OMA; ETGIAPF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR017059; NiFe-hyd_3_EhaH_prd. DR Pfam; PF10125; NADHdeh_related; 1. DR PIRSF; PIRSF036536; EhaH; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 218 Uncharacterized protein MJ0522. FT /FTId=PRO_0000106911. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 161 181 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. SQ SEQUENCE 218 AA; 23897 MW; 2E2EC3ACE9714CA5 CRC64; MIESITGYLF GIVPFGDIVF GFSEFSIIGF ITAVIFTIIV YLTKPEKQLE AQKFKIEDKL EVVTLNELKI RRMMAIVCGI ATAGAMLTYD LFDYALFLTL VGIANIGIVS AVKREWVLNA SYQYGLIAMI ATLPLFGSAG MILAKTGTLS IFELPKIQTS LLFEKIIFAA GMAGETGIAP FYAAKAEMFR APGSPYILMI HLSSLLLIVR TVEILLTI // ID Y540_METJA Reviewed; 85 AA. AC Q57960; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0540; GN OrderedLocusNames=MJ0540; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98537.1; -; Genomic_DNA. DR PIR; D64367; D64367. DR STRING; 243232.MJ_0540; -. DR EnsemblBacteria; AAB98537; AAB98537; MJ_0540. DR KEGG; mja:MJ_0540; -. DR eggNOG; arCOG05038; Archaea. DR eggNOG; COG4013; LUCA. DR OMA; HVEGRLM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019208; DUF2097. DR Pfam; PF09870; DUF2097; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 85 Uncharacterized protein MJ0540. FT /FTId=PRO_0000106921. SQ SEQUENCE 85 AA; 10174 MW; 9978D3AF344582DE CRC64; MEEIIDVKNP KEVIEYLNNI DVDEYVEIYF GRVHVEGRLM HYNDGLIRLV HEKYGIIEVE IEKILDDLLE LVHSNGEKRV VLRFY // ID Y544_METJA Reviewed; 229 AA. AC Q57964; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 73. DE RecName: Full=Uncharacterized protein MJ0544; GN OrderedLocusNames=MJ0544; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98538.1; -; Genomic_DNA. DR PIR; H64367; H64367. DR ProteinModelPortal; Q57964; -. DR STRING; 243232.MJ_0544; -. DR CAZy; GT2; Glycosyltransferase Family 2. DR EnsemblBacteria; AAB98538; AAB98538; MJ_0544. DR KEGG; mja:MJ_0544; -. DR eggNOG; arCOG00895; Archaea. DR eggNOG; COG0463; LUCA. DR InParanoid; Q57964; -. DR OMA; VQCGFRI; -. DR PhylomeDB; Q57964; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004582; F:dolichyl-phosphate beta-D-mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0004169; F:dolichyl-phosphate-mannose-protein mannosyltransferase activity; IBA:GO_Central. DR GO; GO:0019348; P:dolichol metabolic process; IBA:GO_Central. DR GO; GO:0006506; P:GPI anchor biosynthetic process; IBA:GO_Central. DR GO; GO:0006487; P:protein N-linked glycosylation; IBA:GO_Central. DR GO; GO:0035269; P:protein O-linked mannosylation; IBA:GO_Central. DR Gene3D; 3.90.550.10; -; 1. DR InterPro; IPR001173; Glyco_trans_2-like. DR InterPro; IPR029044; Nucleotide-diphossugar_trans. DR Pfam; PF00535; Glycos_transf_2; 1. DR SUPFAM; SSF53448; SSF53448; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 229 Uncharacterized protein MJ0544. FT /FTId=PRO_0000106922. SQ SEQUENCE 229 AA; 26470 MW; D2760B2D92FCB26F CRC64; MIAIIPAFNE EKNILKVLKD LEKLRVDAVV VDDGSKDNTS KIVEEFAKKA KINVYLIRNE KNEGKAKAIE KGTKFALSLN KYKYIIYIDG DYQHKPMDIP KLLKKLEDTN ADAVFGIRKY KHIPLHRQIS NFFASILTSL AVLIYSKRFY FFRDVQCGFR IIKAEFLKDM KFGDGYAVEH FIALQLAKKG AKIVEEYVSV EYHDEAVSYI TTKKILEVAK QVIKFIFLE // ID Y545_METJA Reviewed; 251 AA. AC Q57965; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0545; GN OrderedLocusNames=MJ0545; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98547.1; -; Genomic_DNA. DR PIR; A64368; A64368. DR ProteinModelPortal; Q57965; -. DR STRING; 243232.MJ_0545; -. DR EnsemblBacteria; AAB98547; AAB98547; MJ_0545. DR KEGG; mja:MJ_0545; -. DR eggNOG; arCOG05039; Archaea. DR eggNOG; ENOG410ZGUM; LUCA. DR OMA; ATEIGNY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 251 Uncharacterized protein MJ0545. FT /FTId=PRO_0000106923. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. SQ SEQUENCE 251 AA; 28349 MW; ED36603E1C61DC67 CRC64; MVGKMKKVII PLLISLFIFL IPNYALNPEI IVTPEKCLVN NSVYVIFQWR APYNVEDFNV TVLSDAVVFK NSTLYYAGVA EDAKVFHIFE GEAVTPGNHT INVQMSYIID GTLIKKKFLL NISILTLPEN IYVSYNNTYN RDEENTSLLE NITKIFENTT NVTTPNSTNA IINETNITQN KTNISKNIDI GNITKANTTS QEKITQKFNN TSTQTIENVQ KDKGNNWLMY GILGLIIGIV FGFVVMYIIK I // ID Y546_METJA Reviewed; 56 AA. AC Q57966; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0546; GN OrderedLocusNames=MJ0546; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98548.1; -; Genomic_DNA. DR PIR; B64368; B64368. DR STRING; 243232.MJ_0546; -. DR EnsemblBacteria; AAB98548; AAB98548; MJ_0546. DR KEGG; mja:MJ_0546; -. DR eggNOG; arCOG05040; Archaea. DR eggNOG; ENOG410Z9YA; LUCA. DR OMA; FLFMKLV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 56 Uncharacterized protein MJ0546. FT /FTId=PRO_0000106924. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT COMPBIAS 27 47 Glu-rich. SQ SEQUENCE 56 AA; 6460 MW; 66CBFC395548BA5D CRC64; MILYIIVAIS ILLNIILGIK VIMLQKELEE VKKATRLTKE EVEKLNERIR KLKLGG // ID Y562_METJA Reviewed; 74 AA. AC Q57982; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0562; GN OrderedLocusNames=MJ0562; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98560.1; -; Genomic_DNA. DR PIR; B64370; B64370. DR EnsemblBacteria; AAB98560; AAB98560; MJ_0562. DR KEGG; mja:MJ_0562; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 74 Uncharacterized protein MJ0562. FT /FTId=PRO_0000106932. SQ SEQUENCE 74 AA; 8770 MW; 8A99FF0EF7017898 CRC64; MIGMNFKDPI EELLDNYFNA KKEYEKNPIE KNLNRLKKAE AKLMINYPNT NATYIYKNKK YKIIIKDSVS VIPI // ID Y565_METJA Reviewed; 147 AA. AC Q57985; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0565; GN OrderedLocusNames=MJ0565; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98561.1; -; Genomic_DNA. DR PIR; E64370; E64370. DR ProteinModelPortal; Q57985; -. DR STRING; 243232.MJ_0565; -. DR EnsemblBacteria; AAB98561; AAB98561; MJ_0565. DR KEGG; mja:MJ_0565; -. DR eggNOG; arCOG04938; Archaea. DR eggNOG; ENOG411292W; LUCA. DR InParanoid; Q57985; -. DR OMA; FEDWADW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 147 Uncharacterized protein MJ0565. FT /FTId=PRO_0000106933. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. SQ SEQUENCE 147 AA; 15900 MW; A19D2A29BDFB36AB CRC64; MDIKNMRNVI VSLSLVFGLL FTVSGIIEII IGLYSILGFK IELPLFVGDV FGGLALLAVG IAYFLGVKKA VDRDIKAVSY LFTASIIGLG IGVIAFLILI SDAIGFLLGF EDWADWGFFN DLTVYLVLGM LAIIPYRIAK IISSSTT // ID Y579_METJA Reviewed; 269 AA. AC Q57999; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0579; GN OrderedLocusNames=MJ0579; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0578. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98570.1; -; Genomic_DNA. DR PIR; C64372; C64372. DR ProteinModelPortal; Q57999; -. DR STRING; 243232.MJ_0579; -. DR EnsemblBacteria; AAB98570; AAB98570; MJ_0579. DR KEGG; mja:MJ_0579; -. DR eggNOG; arCOG04073; Archaea. DR eggNOG; COG1149; LUCA. DR InParanoid; Q57999; -. DR OMA; PNGHLFF; -. DR PhylomeDB; Q57999; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 269 Uncharacterized protein MJ0579. FT /FTId=PRO_0000106940. FT NP_BIND 12 19 ATP. {ECO:0000255}. FT NP_BIND 130 137 ATP. {ECO:0000255}. SQ SEQUENCE 269 AA; 30192 MW; B5BE21D15BFF7079 CRC64; MSEMMIVAVT GGKGGTGKST LSANLFFYFI ENYKTALIDC DVETPNLPYL TGCEDLFLAR EVFIEVPNIE EGKTYNYNNV CKEGALLKVG DKLIFIEDLC SGCKACGINS NITFKKKSIG KIYEKKFDNG YLIVGKSNLG ERKTAKIVTE TKKYGLSKNC EINIVDTAAG THCNVVRALI NADKVLIVTE PTPFGVSDAK RIIKVVEKLN IPYKIVLNRY GISDLKIGYN FKIPYDKRIV ECYCKGESFL KYNDLRNYIE EIANWIIWG // ID Y587_METJA Reviewed; 153 AA. AC Q58007; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0587; GN OrderedLocusNames=MJ0587; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0129 and MJ0554. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98584.1; -; Genomic_DNA. DR PIR; C64373; C64373. DR ProteinModelPortal; Q58007; -. DR STRING; 243232.MJ_0587; -. DR DNASU; 1451452; -. DR EnsemblBacteria; AAB98584; AAB98584; MJ_0587. DR KEGG; mja:MJ_0587; -. DR PhylomeDB; Q58007; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 153 Uncharacterized protein MJ0587. FT /FTId=PRO_0000106946. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 118 138 Helical. {ECO:0000255}. SQ SEQUENCE 153 AA; 17733 MW; 282C1DABE1827DDC CRC64; MVNEYKAHSS FILKVVITLI GYWIASILAI IIYSMFFKIE TNTFLLCLLL PTPIIWFNIL IGMGLTYRCM ENLTIYDKHK LWCVFVRDLT LTILATILAT LTTMELYQIE HPLKPIEFVF IVGLVLIVGF TIITTLIIKY LKIIKNLKKI SKN // ID Y597_METJA Reviewed; 357 AA. AC Q58014; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0597; GN OrderedLocusNames=MJ0597; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98589.1; -; Genomic_DNA. DR PIR; E64374; E64374. DR ProteinModelPortal; Q58014; -. DR STRING; 243232.MJ_0597; -. DR EnsemblBacteria; AAB98589; AAB98589; MJ_0597. DR KEGG; mja:MJ_0597; -. DR eggNOG; arCOG00659; Archaea. DR eggNOG; COG0502; LUCA. DR OMA; YSLNPQK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 357 Uncharacterized protein MJ0597. FT /FTId=PRO_0000106950. SQ SEQUENCE 357 AA; 40900 MW; BC16E3B3FFA774F4 CRC64; MTIGREKMKV EEILENARKA FKLTTKHFGN TVTFERALFL GWYCNLKQPC KFCYMATQKN KIKDPRKARR RLESVLAEAI LMKRIGWKLE FISGGYGYTP KEINDIAEMV AYVQKCRQYL NVGVIDLDNI NLDVIEGVVG AVETVSKDRD WICPGKPLDK IKDNLLKAKE LGLKTGITII LGLGEKEEDI EKLLNLIEEL DLNRITFYSL NPQKGTIYEN KPSVTTIEYM NWVSSVRLNF PKIKIITGVW VDKIPMISPL IMSGSNVITK FPLFSVFGTK EAHWIEKEIL ATGRELLGTF TDIDILAGKK VLEKTPYIEE EINISSENIK RVEELRENIN ERIESYVSKV LRKIKAS // ID Y606_METJA Reviewed; 91 AA. AC Q58023; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0606; GN OrderedLocusNames=MJ0606; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98600.1; -; Genomic_DNA. DR PIR; F64375; F64375. DR STRING; 243232.MJ_0606; -. DR EnsemblBacteria; AAB98600; AAB98600; MJ_0606. DR KEGG; mja:MJ_0606; -. DR eggNOG; arCOG05042; Archaea. DR eggNOG; ENOG41126WM; LUCA. DR OMA; LTNYVYT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 91 Uncharacterized protein MJ0606. FT /FTId=PRO_0000106954. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. SQ SEQUENCE 91 AA; 9831 MW; FA2B983CA10406F6 CRC64; MDLEGKCCLI HAIGGIIFGY LANYVYTAGL GIFSGIATLI FLFIGAVIFG HISAKTFGEE SLTQKQWLGC GVLPFFLVAI VVWVLKFNGL I // ID Y607_METJA Reviewed; 79 AA. AC Q58024; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0607; GN OrderedLocusNames=MJ0607; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98607.1; -; Genomic_DNA. DR PIR; G64375; G64375. DR STRING; 243232.MJ_0607; -. DR EnsemblBacteria; AAB98607; AAB98607; MJ_0607. DR KEGG; mja:MJ_0607; -. DR eggNOG; arCOG05043; Archaea. DR eggNOG; ENOG410YX6R; LUCA. DR OMA; MHYSIIK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 79 Uncharacterized protein MJ0607. FT /FTId=PRO_0000106955. SQ SEQUENCE 79 AA; 9398 MW; D89880B83C5B782E CRC64; MHYSIIKPKC KKEIIEIDKG SLKTKRKFAF LLEIGDKILN NKEFYANDDV EVVVDYSFTD SKRPKEKIEL YIIEDIKRD // ID Y618_METJA Reviewed; 98 AA. AC Q58035; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 78. DE RecName: Full=UPF0235 protein MJ0618 {ECO:0000255|HAMAP-Rule:MF_00634}; GN OrderedLocusNames=MJ0618; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0235 family. {ECO:0000255|HAMAP- CC Rule:MF_00634}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98613.1; -; Genomic_DNA. DR PIR; B64377; B64377. DR ProteinModelPortal; Q58035; -. DR STRING; 243232.MJ_0618; -. DR EnsemblBacteria; AAB98613; AAB98613; MJ_0618. DR KEGG; mja:MJ_0618; -. DR eggNOG; arCOG04058; Archaea. DR eggNOG; COG1872; LUCA. DR InParanoid; Q58035; -. DR KO; K09131; -. DR OMA; TNAKKNE; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.1200.10; -; 1. DR HAMAP; MF_00634; UPF0235; 1. DR InterPro; IPR005228; CHP00251. DR InterPro; IPR003746; DUF167. DR Pfam; PF02594; DUF167; 1. DR SMART; SM01152; DUF167; 1. DR SUPFAM; SSF69786; SSF69786; 1. DR TIGRFAMs; TIGR00251; TIGR00251; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 98 UPF0235 protein MJ0618. FT /FTId=PRO_0000139468. SQ SEQUENCE 98 AA; 11289 MW; E01AAF935D15500A CRC64; MIEKIIKESR EGVLIDIDVQ ANAKKNEIVG INEWRKRLSI KIKAPATEGK ANKEIIKFFK EIFKKDVEIV SGKLNPQKTV LIGDIKKDEV IEILKRYL // ID Y666_METJA Reviewed; 398 AA. AC Q58080; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 96. DE RecName: Full=Putative molybdopterin biosynthesis protein MJ0666; GN OrderedLocusNames=MJ0666; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98661.1; -; Genomic_DNA. DR PIR; B64383; B64383. DR ProteinModelPortal; Q58080; -. DR STRING; 243232.MJ_0666; -. DR EnsemblBacteria; AAB98661; AAB98661; MJ_0666. DR KEGG; mja:MJ_0666; -. DR eggNOG; arCOG00216; Archaea. DR eggNOG; COG0303; LUCA. DR InParanoid; Q58080; -. DR KO; K03750; -. DR OMA; PGNRREY; -. DR PhylomeDB; Q58080; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 2.40.340.10; -; 1. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR InterPro; IPR005111; MoeA_C_domain_IV. DR InterPro; IPR005110; MoeA_linker/N. DR Pfam; PF00994; MoCF_biosynth; 1. DR Pfam; PF03454; MoeA_C; 1. DR Pfam; PF03453; MoeA_N; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR SUPFAM; SSF63867; SSF63867; 1. DR SUPFAM; SSF63882; SSF63882; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 398 Putative molybdopterin biosynthesis FT protein MJ0666. FT /FTId=PRO_0000171004. SQ SEQUENCE 398 AA; 44418 MW; 81747A9908607ACB CRC64; MKLIKNLMPL KSAEKIVFEK LSEYLDENKK VKEVDIVEAL NRISAEDIKA PIDLPYFNKA AMDGYAVIAE DTFGASETNP IILNLADGDE ITYGEAKKIF TGDKLPKNAN AVVMKEFCNE VDDFVEVYKT VHPNENVSRI GEDVKKGDVV LKKGEIINPY HLNMLASLGI KKIKVYDLSF GIISTGDELI NLDEIRDIEE DISKLDGKII NSNSYMLYGL VKNLGFNAKI YDIVKDDKEK LKKAIKTALS ENDALLITGG TSVSERDITV ETVRELGDVI VHGVNIRPGK PFGFGIINDK PVFMLSGYPV ASAVQFELFI QRFFIERKKV TLPLKRNMAS ELGRVDFVRV KVDIEVEPIR ITGSGVISSL IKSDGYILIP ENVEGYEKGE LVDVYLLK // ID Y668_METJA Reviewed; 85 AA. AC Q58082; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0668; GN OrderedLocusNames=MJ0668; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98670.1; -; Genomic_DNA. DR PIR; D64383; D64383. DR STRING; 243232.MJ_0668; -. DR EnsemblBacteria; AAB98670; AAB98670; MJ_0668. DR KEGG; mja:MJ_0668; -. DR eggNOG; arCOG09634; Archaea. DR eggNOG; ENOG41110N8; LUCA. DR KO; K03054; -. DR OMA; ILMIRHI; -. DR PhylomeDB; Q58082; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 85 Uncharacterized protein MJ0668. FT /FTId=PRO_0000106982. SQ SEQUENCE 85 AA; 10091 MW; 242BB65671A2C305 CRC64; MLFYMLFFLV VIMENDEKII EDLKIINSKA KFVGIKILMI RHIIESHMKD KKSIYKILES TKNTELYKLI LIACPKLEEI NEESN // ID Y688_METJA Reviewed; 137 AA. AC Q58101; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 27-APR-2001, sequence version 3. DT 11-NOV-2015, entry version 78. DE RecName: Full=UPF0146 protein MJ0688; GN OrderedLocusNames=MJ0688; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0146 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98683.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98683.1; ALT_INIT; Genomic_DNA. DR ProteinModelPortal; Q58101; -. DR STRING; 243232.MJ_0688; -. DR EnsemblBacteria; AAB98683; AAB98683; MJ_0688. DR KEGG; mja:MJ_0688; -. DR eggNOG; arCOG04385; Archaea. DR eggNOG; COG1255; LUCA. DR InParanoid; Q58101; -. DR KO; K09713; -. DR OMA; FRRIPIY; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR HAMAP; MF_00341; UPF0146; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR005353; UPF0146. DR Pfam; PF03686; UPF0146; 1. DR PIRSF; PIRSF016725; UCP016725; 1. DR ProDom; PD021130; UPF0146; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 137 UPF0146 protein MJ0688. FT /FTId=PRO_0000145094. SQ SEQUENCE 137 AA; 16008 MW; 27D3948A98FACB66 CRC64; MNVKIIVEFI KKFAEENNCK KIAEIGIGFK FDVARELSKY FDLIAIDINE KAIEKAKLLG LNAYKDDLFN PNISLYKNID LIYSIRPPRD LQPYILDLSK KVNANLIIRP LLNEMPIKEL KLKNYKGEVF YIKEKQI // ID Y693_METJA Reviewed; 241 AA. AC Q58104; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0693; GN OrderedLocusNames=MJ0693; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98688.1; -; Genomic_DNA. DR PIR; E64386; E64386. DR ProteinModelPortal; Q58104; -. DR STRING; 243232.MJ_0693; -. DR EnsemblBacteria; AAB98688; AAB98688; MJ_0693. DR KEGG; mja:MJ_0693; -. DR eggNOG; arCOG01677; Archaea. DR eggNOG; COG4015; LUCA. DR OMA; EVHRGGF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008641; F:small protein activating enzyme activity; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR000594; ThiF_NAD_FAD-bd. DR InterPro; IPR012028; UCP006529_dinclt. DR Pfam; PF00899; ThiF; 1. DR PIRSF; PIRSF006529; UCP006529_dinclt; 1. DR SUPFAM; SSF69572; SSF69572; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 241 Uncharacterized protein MJ0693. FT /FTId=PRO_0000106992. SQ SEQUENCE 241 AA; 27485 MW; D183FD4DECBBFB8F CRC64; MNAFFEGVQC SLINFNNFAK NYYTFLLKKF CLDGIFMNVE EMERKLKPKG EVSIIGCGRL GVRVAFDLLE VHRGGVEKVY VFDNAKIEEN DIVHRRLGGK VGEYKVDFIK RFFGNRVEAF RENITKDNLH LIKGDVAVIC IAGGDTIPTT KAIINYCKER GIKTIGTNGV FGIEEKIKVC DAKYAKGPAK FLNLDEEGHI VVGTEKFIRD FEPITPYTLD EIAKRMVIEC LRILWSKYYK S // ID Y711_METJA Reviewed; 322 AA. AC Q58121; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0711; GN OrderedLocusNames=MJ0711; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98714.1; -; Genomic_DNA. DR PIR; G64388; G64388. DR ProteinModelPortal; Q58121; -. DR STRING; 243232.MJ_0711; -. DR EnsemblBacteria; AAB98714; AAB98714; MJ_0711. DR KEGG; mja:MJ_0711; -. DR eggNOG; arCOG07502; Archaea. DR eggNOG; ENOG410ZZGQ; LUCA. DR InParanoid; Q58121; -. DR OMA; DIIELAC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 322 Uncharacterized protein MJ0711. FT /FTId=PRO_0000106999. FT TRANSMEM 299 319 Helical. {ECO:0000255}. SQ SEQUENCE 322 AA; 38631 MW; D756464175044F27 CRC64; MDSVLSGKIV QILVGYLKEN IYSEQMIKLR MKRICSYEEF LPTYSLIERI TEESKEIAIK VYEKNIIVEI VKDFKNKDLI ELFELKEELF DEALSYLKKY NADKFLESYT LYCFSEYSDP DSFIKENKSI LTKLLRNQYE EVPEEYINEL LKSKIKYSTK DLIILDWDNG IILDKNEDFW EEVDIIELAC IRVLNLRVFD SMLSEAIQYF TRLQWEKLGY FKLKKLSKDL YLQRISYISY FDSIENVLML YGDRYYAELY ERLCKIFYVS EWIKRVEKKM EMISDIYTMT RQHLTEFYGL LLEGTIVALI LLEIILALAK IV // ID Y727_METJA Reviewed; 298 AA. AC Q58137; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0727; GN OrderedLocusNames=MJ0727; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98723.1; -; Genomic_DNA. DR PIR; G64390; G64390. DR ProteinModelPortal; Q58137; -. DR STRING; 243232.MJ_0727; -. DR EnsemblBacteria; AAB98723; AAB98723; MJ_0727. DR KEGG; mja:MJ_0727; -. DR eggNOG; arCOG01549; Archaea. DR eggNOG; COG3259; LUCA. DR KO; K00440; -. DR OMA; CERCYYL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 2. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00374; NiFeSe_Hases; 1. DR SUPFAM; SSF56762; SSF56762; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 298 Uncharacterized protein MJ0727. FT /FTId=PRO_0000107004. SQ SEQUENCE 298 AA; 33519 MW; 4DAAD534096A680D CRC64; MKIRGFESSM MGKDIDFIPP AMTRLCCLNE ISHALAGVMA VEKAYNITVP NEGQYLREIA RLGEIVEVDA IKLREFKNTD DLADIGNKIK SVLGKKAKYL AVGGVLENIS DKRKEKLINL AKEGLNLVDK DFVKLVDERK AKIPLPDVEL IDAYNFDANK VETNGLPKTA LYDGKVVYSG SLARMYKEGL INSKNLWDVL SSRMIEIEFC LNKIIELLNK LKLTHPYMEP IIKDGKAIGE AVIEGGEGIV YHKVELLGRE ILDYTILTSE NFNKAVLDSV DNDEAKRIIQ LCERCYYL // ID Y733_METJA Reviewed; 121 AA. AC Q58143; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0733; GN OrderedLocusNames=MJ0733; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98743.1; -; Genomic_DNA. DR PIR; E64391; E64391. DR ProteinModelPortal; Q58143; -. DR STRING; 243232.MJ_0733; -. DR EnsemblBacteria; AAB98743; AAB98743; MJ_0733. DR KEGG; mja:MJ_0733; -. DR eggNOG; arCOG01670; Archaea. DR eggNOG; ENOG4111Y7W; LUCA. DR OMA; ENDLFGH; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR Pfam; PF02635; DrsE; 1. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Uncharacterized protein MJ0733. FT /FTId=PRO_0000107008. SQ SEQUENCE 121 AA; 14094 MW; D1A69F7091B27BC7 CRC64; MRWGFMKVAF LIFSYFHKNQ PNMPVMMHTL LFANELKEKG DEVKIILEGE AVLWAKDLLS ENHPLKSHFE KVKDDFVVCE ACASMFNVKE EIKGKLKLEN DLFGHVSLKK YLDGGYRIIE L // ID Y1485_METJA Reviewed; 474 AA. AC Q58880; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized cation transporter MJ1485; GN OrderedLocusNames=MJ1485; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TrkH potassium transport family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99495.1; -; Genomic_DNA. DR PIR; D64485; D64485. DR ProteinModelPortal; Q58880; -. DR STRING; 243232.MJ_1485; -. DR EnsemblBacteria; AAB99495; AAB99495; MJ_1485. DR KEGG; mja:MJ_1485; -. DR eggNOG; arCOG04145; Archaea. DR eggNOG; COG0168; LUCA. DR InParanoid; Q58880; -. DR KO; K03498; -. DR OMA; FHMESSD; -. DR PhylomeDB; Q58880; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR003445; Cat_transpt. DR Pfam; PF02386; TrkH; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Ion transport; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 474 Uncharacterized cation transporter FT MJ1485. FT /FTId=PRO_0000070483. FT TRANSMEM 17 39 Helical. {ECO:0000255}. FT TRANSMEM 44 61 Helical. {ECO:0000255}. FT TRANSMEM 81 103 Helical. {ECO:0000255}. FT TRANSMEM 144 166 Helical. {ECO:0000255}. FT TRANSMEM 186 208 Helical. {ECO:0000255}. FT TRANSMEM 239 256 Helical. {ECO:0000255}. FT TRANSMEM 268 286 Helical. {ECO:0000255}. FT TRANSMEM 319 341 Helical. {ECO:0000255}. FT TRANSMEM 385 407 Helical. {ECO:0000255}. FT TRANSMEM 444 466 Helical. {ECO:0000255}. SQ SEQUENCE 474 AA; 52537 MW; C78608E4645BE7A2 CRC64; MGICRLTKKD IEGILHILGG IIQIIGIFTL VPCIVSVYYN ENTFLNFLIP GLFFSIFGFV LKRATKPKNL KLHHTMVASA LAWLIASFIG AIPLYLSIDY FSYVDAVYES MSAWTTTGMT LIPNVEVLPK SILFWRSFQQ WIGGVGILVL SALVLARSGT VAYLLYTSEA RQERIMPSAI GTIKTIIWIY ILYTILGVLL LYLSGLSFWD ALNLTMTGIS TGGMSISNYS FPYNDFAKIV MIGIMMVGGV MSFSIHHKLL TGKYFNDIQT KYALIVTAFI SIIISIKDKV PIIDSLFTVV SAMTSTGFTT INVGNLSSLS LFLIIFLMLI GGGAGTTTGG VKIIRFLVIL KALLYEIKEI IYPKSAVIHE HLDDMDLNYR IIREAFVVFF LYCLSSFLTA LIFIALGYNP YDSIFDAVSF TSNIGISLGV VTLKTPVIGK IAGIIAMWIG RLEIIPVLVL FATLYFKTLR LLKK // ID Y1489_METJA Reviewed; 682 AA. AC Q58884; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Uncharacterized MCM-type protein MJ1489; GN OrderedLocusNames=MJ1489; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MCM domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99502.1; -; Genomic_DNA. DR PIR; H64485; H64485. DR ProteinModelPortal; Q58884; -. DR STRING; 243232.MJ_1489; -. DR EnsemblBacteria; AAB99502; AAB99502; MJ_1489. DR KEGG; mja:MJ_1489; -. DR eggNOG; arCOG00439; Archaea. DR eggNOG; COG1241; LUCA. DR InParanoid; Q58884; -. DR KO; K10726; -. DR OMA; QYIDWQK; -. DR PhylomeDB; Q58884; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0042555; C:MCM complex; IEA:InterPro. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003678; F:DNA helicase activity; IEA:InterPro. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006270; P:DNA replication initiation; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 2. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031327; MCM. DR InterPro; IPR008047; MCM_4. DR InterPro; IPR018525; MCM_CS. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR PRINTS; PR01660; MCMPROTEIN4. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Complete proteome; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 682 Uncharacterized MCM-type protein MJ1489. FT /FTId=PRO_0000194131. FT DOMAIN 284 487 MCM. FT NP_BIND 329 336 ATP. {ECO:0000255}. SQ SEQUENCE 682 AA; 77706 MW; 9D332196B6C54049 CRC64; MISSYGDVDM ELRDEDLILE EVRDYLTAYL RNIHQEDIIL DNERVVVDLN QLYNYGLMEF VEFLINNPQK GIDFIKECYN DAYYTLRNEY PTNVIIAVKN LPKIFKTTRK GKIFTIEDIR SKTLGKLVEF EGIIVMASKI RPMLKKAYYI CPKCGREVVR EIDILNTDSE KAVCECGAEL NLIEHKSIYT DFQEIKVQQP LDLMENPEEP PKYITVFLEN SPGIYAGRVK ITGIPIKVKK SKKLPIYDIH VKALHCEVLD GEVKIKLTNS DIENIKKIAK RKDVVNILAD RLIPEIKGHS AIKKAVLLQQ IKGVKKPGKR ADIHILLITD PGIGKTVILR KIAEIPGNLY GSVTTATGVG LTAAVVREKT EIGEDTWVIK PGLLVKAHKG TACIDELTVN KELQSYVLEA MESQTIHISK GGINAKLPAE CAILAACNPR WGRFNPEVSV AEQINIPAPL LSRFDLIFPI RDVSDKDKDK DIAEYIVDLH RAYLDEKINR EMGLDYLEVD GVKIDKEFII KYIYYARQKK PIISEKAKEL FVNYYVEMRK KHQITARQLE AAIRIAEAHA KAKLKDVVDE EDAKEAINII TECLKEIAYD PETGIFDVDK ILGVSKKERD KLTTVYEIIK ELSEKSELVE HEDIAEEAKK KGIKEDELEN IIKKLIKYGD IDEPKPGRYR LL // ID Y1491_METJA Reviewed; 127 AA. AC Q58886; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1491; GN OrderedLocusNames=MJ1491; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99510.1; -; Genomic_DNA. DR PIR; B64486; B64486. DR ProteinModelPortal; Q58886; -. DR STRING; 243232.MJ_1491; -. DR EnsemblBacteria; AAB99510; AAB99510; MJ_1491. DR KEGG; mja:MJ_1491; -. DR eggNOG; arCOG04907; Archaea. DR eggNOG; ENOG4112D66; LUCA. DR OMA; DYENCGL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 127 Uncharacterized protein MJ1491. FT /FTId=PRO_0000107374. FT TRANSMEM 16 36 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. SQ SEQUENCE 127 AA; 13006 MW; 6D3FB594A7961C96 CRC64; MKYMVSFDQE RMLKPAVIGG IINGILGAIC CLCYVIGGAV AAHLYVNAGG ICDYENCGLV GAISGVIGGV IASILSFLFM SAYLSALGLK AAMFTGASFI IGFITAIIFG AILGAVGGVI YVVIKNR // ID Y1497_METJA Reviewed; 346 AA. AC Q58892; DT 03-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized metallohydrolase MJ1497; DE EC=3.-.-.-; GN OrderedLocusNames=MJ1497; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Name=Co(2+); Xref=ChEBI:CHEBI:48828; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) or Co(2+) ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M20A family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99508.1; -; Genomic_DNA. DR PIR; H64486; H64486. DR ProteinModelPortal; Q58892; -. DR STRING; 243232.MJ_1497; -. DR MEROPS; M20.016; -. DR EnsemblBacteria; AAB99508; AAB99508; MJ_1497. DR KEGG; mja:MJ_1497; -. DR eggNOG; arCOG01107; Archaea. DR eggNOG; COG0624; LUCA. DR InParanoid; Q58892; -. DR KO; K01438; -. DR OMA; FFNATCE; -. DR PhylomeDB; Q58892; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.70.360; -; 1. DR InterPro; IPR002933; Peptidase_M20. DR InterPro; IPR011650; Peptidase_M20_dimer. DR Pfam; PF07687; M20_dimer; 1. DR Pfam; PF01546; Peptidase_M20; 1. DR SUPFAM; SSF55031; SSF55031; 1. PE 3: Inferred from homology; KW Cobalt; Complete proteome; Hydrolase; Metal-binding; KW Reference proteome; Zinc. FT CHAIN 1 346 Uncharacterized metallohydrolase MJ1497. FT /FTId=PRO_0000185353. FT ACT_SITE 67 67 {ECO:0000250}. FT ACT_SITE 115 115 Proton acceptor. {ECO:0000250}. FT METAL 65 65 Cobalt or zinc 1. {ECO:0000250}. FT METAL 89 89 Cobalt or zinc 1. {ECO:0000250}. FT METAL 89 89 Cobalt or zinc 2. {ECO:0000250}. FT METAL 116 116 Cobalt or zinc 2. {ECO:0000250}. FT METAL 145 145 Cobalt or zinc 1. {ECO:0000250}. FT METAL 319 319 Cobalt or zinc 2. {ECO:0000250}. SQ SEQUENCE 346 AA; 39800 MW; 97E0E7B0DE358CFA CRC64; MIIMDYLKIL EDLVKIRTDN RIGVKKAFKY LSNLFNNLGI KNTIIEGCFV AYKEKENFDL ILNSHIDTVK IQSNFKKDDN NFYGTGVIDA KGNVVLMIHA FLNSNNSLLV ISPDEETESN GIYNFCQYLR NKNKIQRGIK CIVGEPTDLN VCIGHKGRFE YIVESFGEAR HASSQGLNPI EILSRVILDL KNLPLEKIKV DKIYSSSITP TIIKGGIQSN IIPDYAYVLF DVRSVEKDII KKIDDFLSQK NYSKHIKSSL NPERHYANFY MLENKELINK LSKHFKISFF NATCEAYYFN KFLKADTIIY GVGKLELAHS KEEYLNLNDF DRGIKEVEKL AELMIE // ID Y1503_METJA Reviewed; 132 AA. AC Q58898; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1503; GN OrderedLocusNames=MJ1503; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99516.1; -; Genomic_DNA. DR PIR; F64487; F64487. DR ProteinModelPortal; Q58898; -. DR STRING; 243232.MJ_1503; -. DR EnsemblBacteria; AAB99516; AAB99516; MJ_1503. DR KEGG; mja:MJ_1503; -. DR eggNOG; arCOG02242; Archaea. DR eggNOG; COG3355; LUCA. DR InParanoid; Q58898; -. DR OMA; FTLETIM; -. DR PhylomeDB; Q58898; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002831; Tscrpt_reg_TrmB_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01978; TrmB; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 132 Uncharacterized protein MJ1503. FT /FTId=PRO_0000107380. SQ SEQUENCE 132 AA; 15528 MW; 44046F77C6F1D0CD CRC64; MSKLLLKTPC TTWTFDSLMA CVFGIKVSDV KVYFDILKNG PSKINDIAER INRDRSTVQR AVQNLMNAGL VKRKQVNIKD GGYYYVYEAI PFEETKKIIK KTMEEWCNNM KKWVEELEFE DVVKEYLENI EE // ID Y1514_METJA Reviewed; 120 AA. AC Q58909; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Putative gamma-glutamylcyclotransferase MJ1514; DE EC=2.3.2.-; GN OrderedLocusNames=MJ1514; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative gamma-glutamylcyclotransferase. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the gamma-glutamylcyclotransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99532.1; -; Genomic_DNA. DR PIR; A64489; A64489. DR ProteinModelPortal; Q58909; -. DR STRING; 243232.MJ_1514; -. DR EnsemblBacteria; AAB99532; AAB99532; MJ_1514. DR KEGG; mja:MJ_1514; -. DR eggNOG; arCOG03271; Archaea. DR eggNOG; COG2105; LUCA. DR InParanoid; Q58909; -. DR OMA; SWYPAIV; -. DR PhylomeDB; Q58909; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016746; F:transferase activity, transferring acyl groups; IEA:UniProtKB-KW. DR Gene3D; 3.10.490.10; -; 1. DR InterPro; IPR009288; AIG2-like. DR InterPro; IPR013024; Butirosin_synth_BtrG-like. DR Pfam; PF06094; GGACT; 1. DR SUPFAM; SSF110857; SSF110857; 1. PE 3: Inferred from homology; KW Acyltransferase; Complete proteome; Reference proteome; Transferase. FT CHAIN 1 120 Putative gamma-glutamylcyclotransferase FT MJ1514. FT /FTId=PRO_0000184794. FT REGION 7 10 Substrate binding. {ECO:0000250}. FT ACT_SITE 74 74 Proton acceptor. {ECO:0000250}. SQ SEQUENCE 120 AA; 14209 MW; 8AD873043D6ABEF3 CRC64; MEYVFVYGSL RKGFWNHEPY LKNSKFIGKG KTKEKYAMYV NIIPYVVENE KISHIVGEVY EVDEKTLKRI DCLEGHPDYY RRKKVSIILD SGKEIEAWLY FYPESCGILV ESGDYKDYRG // ID Y1519_METJA Reviewed; 1175 AA. AC Q58914; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized protein MJ1519; GN OrderedLocusNames=MJ1519; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99538.1; -; Genomic_DNA. DR PIR; F64489; F64489. DR ProteinModelPortal; Q58914; -. DR STRING; 243232.MJ_1519; -. DR EnsemblBacteria; AAB99538; AAB99538; MJ_1519. DR KEGG; mja:MJ_1519; -. DR eggNOG; COG0507; LUCA. DR InParanoid; Q58914; -. DR KO; K03581; -. DR OMA; VSKEMLY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central. DR GO; GO:0005634; C:nucleus; IBA:GO_Central. DR GO; GO:0005657; C:replication fork; IBA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0043141; F:ATP-dependent 5'-3' DNA helicase activity; IBA:GO_Central. DR GO; GO:0010521; F:telomerase inhibitor activity; IBA:GO_Central. DR GO; GO:0032508; P:DNA duplex unwinding; IBA:GO_Central. DR GO; GO:0006260; P:DNA replication; IBA:GO_Central. DR GO; GO:0044806; P:G-quadruplex DNA unwinding; IBA:GO_Central. DR GO; GO:0000002; P:mitochondrial genome maintenance; IBA:GO_Central. DR GO; GO:0051974; P:negative regulation of telomerase activity; IBA:GO_Central. DR GO; GO:0032211; P:negative regulation of telomere maintenance via telomerase; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR003840; DNA_helicase. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR029493; RecD-like_HHH. DR InterPro; IPR027785; UvrD-like_helicase_C. DR PANTHER; PTHR23274; PTHR23274; 2. DR Pfam; PF14490; HHH_4; 1. DR Pfam; PF13538; UvrD_C_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 1175 Uncharacterized protein MJ1519. FT /FTId=PRO_0000107391. FT NP_BIND 586 593 ATP. {ECO:0000255}. SQ SEQUENCE 1175 AA; 138619 MW; 99082EA5A4D11140 CRC64; MRNLISLIAW HDSGWNGRVC RNPKENKYCE SFGYVIRKRK YEFCVNNPDA NLGNSRERAC SEAIVFCKGK VQEHNIRFPA IFYVDRKNRN EHEIKMIKKE IEEQLRMING KYAILYVREN PLSENRVIVG CVKIKEIIDG SKDYIRKKQS PNRVGRGIVF DVENDVIFAL PYQELLEYCK NKNKEIEEIL KEFNLIFEVG DFERYFKGMS NFISDEVAVQ ILKKGLEIVE EFNKFREENQ DFDKYLTDEN IAFRPHVMKK FDEFAENIKK VIAELEGSKY KYPGLPGVLY FLGMEDAYSR YIELWKNEGE KGEEKLYNAL IESLENRKEN LEFGITKKVI DKFIAQKEEF REFLKNYAVY YELSAFKLEK IKEQYEKEFI NLDNIIKNPY ILVEDLKEND SFERIIFEEL DSWERRRLGD KFNPYSPYRV RALLVEILKR HLSSGNTTIS TKDLKDFFEK MDKDIVKITF DEFLRIIEEY KDIISEKVEI VKKEVKNNEN KEIIELFTLK EIREYEEIIE NTINYLLKSK APNIDLNPLE IREKLRIKNE NKKPAGVDNE EYEKALDMQT EAVVNLLKNR VGILTGPAGT GKTTVIKTIM ELMKEVLGLN KIYILTPTGK SAMVVNEKLN NLATAKTIHR YIAEEFKDYF EGDNYFILRL DKITGNDKKE IDALIIDESS MVDIETMGRL LGTIKLDNLK YLIFVGDINQ LPPVGAGKPF YDIYNYLEKV NPQSICKLEI VLRADSKKIV ELSKLFLDID KEERIKILNE MFKNKETLGD NEIYRIKENI GGIEKEIITI EVVKDGNIKK SLENAIETIL KENNTEDFFD FAVFNDKLQI LVPTKTKGEF GSYMINLFIK QESKFIPDKY KNKMLENWFF GDGKVADKVI QIRNNYKKWV YDTERRKWVK EHGVFNGMMG FAYTFKKWNK YQKKYENKTI IRFYYPKIEA YTDEKEMEHA YAITIHKSQG SGFENVILII PKGLNKFVSK EMLYTAITRA KKRLYVIVEE ELKNFLETNI SDLARRKTNL LENFNISYLV PYIENRQIIT INGEKVRSWQ ECVLANLFHE VGIEYIYELL SEYLKIGVLP DFKLNIKNRT ILWEHYGMLE NEKYRKRQKE EKEPIYKQNG FEIIKLSEIN ENTKLGDKVL IISTSEDLKN NSQVLEKLKT LQQIS // ID Y1524_METJA Reviewed; 108 AA. AC Q58919; DT 20-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=UPF0166 protein MJ1524; GN OrderedLocusNames=MJ1524; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0166 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99550.1; -; Genomic_DNA. DR PIR; C64490; C64490. DR ProteinModelPortal; Q58919; -. DR STRING; 243232.MJ_1524; -. DR EnsemblBacteria; AAB99550; AAB99550; MJ_1524. DR KEGG; mja:MJ_1524; -. DR eggNOG; arCOG04967; Archaea. DR eggNOG; COG1993; LUCA. DR InParanoid; Q58919; -. DR KO; K09137; -. DR OMA; IECIDYE; -. DR PhylomeDB; Q58919; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.70.120; -; 1. DR InterPro; IPR003793; DUF190. DR InterPro; IPR011322; N-reg_PII-like_a/b. DR InterPro; IPR015867; N-reg_PII/ATP_PRibTrfase_C. DR Pfam; PF02641; DUF190; 1. DR SUPFAM; SSF54913; SSF54913; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 108 UPF0166 protein MJ1524. FT /FTId=PRO_0000185233. SQ SEQUENCE 108 AA; 12398 MW; D3E286AFB9D4AF8B CRC64; MIKAKILKIY LREGDKFEGE LMYKHIMKIL KREGISGATV YKGICGYGVR GVAEFDIFRL SVNLPVIIEC VDIEENINRV LPKLYEVIKN NGLIIITDCH VYKGETYE // ID Y1539_METJA Reviewed; 109 AA. AC Q58934; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ1539; GN OrderedLocusNames=MJ1539; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To A.fulgidus AF1885. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99568.1; -; Genomic_DNA. DR PIR; B64492; B64492. DR ProteinModelPortal; Q58934; -. DR STRING; 243232.MJ_1539; -. DR EnsemblBacteria; AAB99568; AAB99568; MJ_1539. DR KEGG; mja:MJ_1539; -. DR eggNOG; arCOG08297; Archaea. DR eggNOG; ENOG411104K; LUCA. DR OMA; VKIVFNK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein MJ1539. FT /FTId=PRO_0000107397. SQ SEQUENCE 109 AA; 12451 MW; C0E04280C5960831 CRC64; MGIDMSEEKE VKEIKVEIPK EIADKIEKIT SFLNSLKDKK EMVSKEKIEE MLKLIDEVKD KLPKLNVDIE KLAKILEGSG SEVKIVFNKL TIDGEVGLKI IPLKKEKKE // ID Y1542_METJA Reviewed; 808 AA. AC Q58937; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ1542; GN OrderedLocusNames=MJ1542; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99570.1; -; Genomic_DNA. DR PIR; E64492; E64492. DR ProteinModelPortal; Q58937; -. DR STRING; 243232.MJ_1542; -. DR EnsemblBacteria; AAB99570; AAB99570; MJ_1542. DR KEGG; mja:MJ_1542; -. DR eggNOG; arCOG03240; Archaea. DR eggNOG; ENOG410ZCSB; LUCA. DR InParanoid; Q58937; -. DR OMA; VGKTNLF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 4. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 2. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 808 Uncharacterized protein MJ1542. FT /FTId=PRO_0000107399. FT NP_BIND 35 42 ATP. {ECO:0000255}. SQ SEQUENCE 808 AA; 95564 MW; CD716B4B9AB7B04C CRC64; MVKFMKIKSI AAKNLLSFDD FKITFEDGDV VTIFGPNNVG KTNLFRVLKL LRNIINEKIS AVDLEIYLHN KNLKAAKIEV DVIFDKSDKE VIAKFLKIFF KINAPDLIRL CNNLKLNIIN SIIDYFSAGS YIWECSELRC YRPYFMLRLR SLEEDIEKIK IYLKERELSE ITPDLIDHSK VIHELDRNVE IIEVTNDLKN IITSSVNALI TIYEKNEKLF FSTLIDGKEN ITTRIGDGNI ENIVEISMKD FTKDIEKYED CFKRLTMDKN ILRAFVVLLA LDKLLANKMS IYVKKVLEYS KENPWDKEII EDLKYIVRFC GFDYRDIYEI SDISLNDILL KIYENSLIFY EDYLPNEGKV MIPDYMIVEL LAGLKNNSLE KNVKSKILEL FKTSTTKDDL YLGILSMPSE KWIPSYLFYL KNNANLKLRK RYMKIKEMFE YIFNSGSLSF DVILANNKPD IVVYSEDIEI PLNMVGLGVK KILEILTLVF GYESKVILLD TPFNQLYPKY QKRFSKILKD TENIDSQVFI ILHSPYFINN ENIFNTFRFY KPKKSTKYIC IGSIIKDLEK TFGTVILDRT TRKILLSDAV ILLSSALRDI PLFDLAEYED IPIDEYNIEV IRPQNTLSFG KYYALLQYTS IPYILMLRSW ILYNLYEEIK DGEGKVRYKL LEKGKYHKIV EERLNFFKNR HPFWISKEEF DKVINIYIKT LEAHREKLIE LGYIYLSSKE EVVKYCIEPL RKQLEDILRK KLFIFTVPTD FIIEPQDLKN IQIEKDKYIV HNYIGYRKDV LKEFKEFFDY FVKFHNLQ // ID Y1577_METJA Reviewed; 598 AA. AC Q58972; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1577; GN OrderedLocusNames=MJ1577; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99606.1; -; Genomic_DNA. DR PIR; H64496; H64496. DR ProteinModelPortal; Q58972; -. DR STRING; 243232.MJ_1577; -. DR EnsemblBacteria; AAB99606; AAB99606; MJ_1577. DR KEGG; mja:MJ_1577; -. DR eggNOG; arCOG03432; Archaea. DR eggNOG; COG4907; LUCA. DR InParanoid; Q58972; -. DR OMA; EWLVYGT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR018702; DUF2207_membrane. DR Pfam; PF09972; DUF2207; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 598 Uncharacterized protein MJ1577. FT /FTId=PRO_0000107423. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. FT TRANSMEM 435 455 Helical. {ECO:0000255}. FT TRANSMEM 467 487 Helical. {ECO:0000255}. FT COMPBIAS 579 596 Poly-Gly. SQ SEQUENCE 598 AA; 68959 MW; 8B2AF84D60FEA45E CRC64; MREEKEIIIV CLLIFIVGVV GIFLTTSFNG MKYTSIYIKD YEANLYIGKN LTLEEIYSYE VLEGRKYRML YRDWKAPLVY NGSLNTPYVK VLNLSTSSKD MVGYVVDYKG DIFVFSDEDW IKRNIEEIVD KYYIRNEVGF YNPLYIRNPG IYTTSYKFVI YPPIETDNVF YHINLKLADE HLPYKNVKIN VIDENNSILD LFVYPSTFKV YKTYFGYTIE GSSPKNDPIE VEMLLKPNSV NGFTRYVYNV EGKTISAYKK YTFVSNIVMT LKYLLMAIIL LFPLIAYIIY LKFGKEKFYV VPEYLSYVPN KNRKPWIVNL IFAGDAGFFD KEGFYATLLD LHNRGYIKIM NGGKIEILKT DLENLDVYES DVMKFLMKYS KNNVFDPEYI KSLAQKYKSS KDKLKKLKDE LDKIMEYPRY SSKVVNAFLE TRGKKIIIAL LVISILLAVF LYFIPKYSQT FNEVFYLSIV FVVQNIILAL TPTSLFGRWK ANYYKEKLEW DAFKNFLSNL AMIKKYSPED ISIWKDWLIY GTALGVGDKV VEAMKSLNLS ELVADYVIIH SNYDSMKTSV DSVYSSTTGS GGGFGAGGGF GGGGGGAR // ID Y1587_METJA Reviewed; 171 AA. AC Q58982; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ1587; GN OrderedLocusNames=MJ1587; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0417. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99616.1; -; Genomic_DNA. DR PIR; B64498; B64498. DR ProteinModelPortal; Q58982; -. DR STRING; 243232.MJ_1587; -. DR EnsemblBacteria; AAB99616; AAB99616; MJ_1587. DR KEGG; mja:MJ_1587; -. DR eggNOG; arCOG00306; Archaea. DR eggNOG; COG0613; LUCA. DR InParanoid; Q58982; -. DR KO; K07053; -. DR OMA; VNERNIR; -. DR PhylomeDB; Q58982; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR004013; PHP_dom. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR Pfam; PF02811; PHP; 1. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 171 Uncharacterized protein MJ1587. FT /FTId=PRO_0000107428. SQ SEQUENCE 171 AA; 19198 MW; 7D4F7B936C5C7472 CRC64; MKADLHIHTK YSGIGKFWKL KFPDSVEEPR NILKVAKKKG IEVVAITDHN TIRGGVETKK LEKEFGVEVV IGSEIMTTEG EIIGLFLNED IPKGLSPEET IEKIKEQGGL AIAPHPYSPI CKALGDRIFD LDLDGVEVFN AYHRDGIVNN IALNKVIKEL PQKAFCIYWR E // ID Y158_METJA Reviewed; 374 AA. AC Q57622; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 89. DE RecName: Full=UPF0425 pyridoxal phosphate-dependent protein MJ0158; GN OrderedLocusNames=MJ0158; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS) OF APOPROTEIN AND COMPLEX WITH RP COFACTOR, SUBUNIT, MASS SPECTROMETRY, AND PYRIDOXAL PHOSPHATE AT RP LYS-208. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=16201757; DOI=10.1021/bi051110r; RA Kaiser J.T., Gromadski K., Rother M., Engelhardt H., Rodnina M.V., RA Wahl M.C.; RT "Structural and functional investigation of a putative archaeal RT selenocysteine synthase."; RL Biochemistry 44:13315-13327(2005). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16201757}. CC -!- MASS SPECTROMETRY: Mass=41886; Method=Unknown; Range=1-374; CC Evidence={ECO:0000269|PubMed:16201757}; CC -!- MASS SPECTROMETRY: Mass=42114; Method=Unknown; Range=1-374; CC Note=The measured mass is that of the PLP-bound protein.; CC Evidence={ECO:0000269|PubMed:16201757}; CC -!- SIMILARITY: Belongs to the UPF0425 family. {ECO:0000305}. CC -!- CAUTION: Despite a certain similarity to SelA, PubMed:16201757 CC reported that this protein does not harbor SelA activity, i.e. it CC fails to bind to Ser-tRNA(Sec) and is not able to convert this CC substrate to selenocysteinyl-tRNA(Sec). It also does not convert CC O-phosphoseryl-tRNA(Sec) to selenocysteinyl-tRNA(Sec). CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98142.1; -; Genomic_DNA. DR PIR; G64319; G64319. DR PDB; 2AEU; X-ray; 1.70 A; A=1-374. DR PDB; 2AEV; X-ray; 2.00 A; A=1-374. DR PDBsum; 2AEU; -. DR PDBsum; 2AEV; -. DR ProteinModelPortal; Q57622; -. DR SMR; Q57622; 9-374. DR STRING; 243232.MJ_0158; -. DR EnsemblBacteria; AAB98142; AAB98142; MJ_0158. DR KEGG; mja:MJ_0158; -. DR eggNOG; arCOG00114; Archaea. DR eggNOG; COG1921; LUCA. DR InParanoid; Q57622; -. DR KO; K01042; -. DR OMA; YVGPAIF; -. DR EvolutionaryTrace; Q57622; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004125; F:L-seryl-tRNASec selenium transferase activity; IBA:GO_Central. DR GO; GO:0097056; P:selenocysteinyl-tRNA(Sec) biosynthetic process; IBA:GO_Central. DR Gene3D; 3.40.640.10; -; 1. DR InterPro; IPR020033; PyrdxlP-dep_transferase_arc. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR018319; SelA-like. DR Pfam; PF03841; SelA; 1. DR SUPFAM; SSF53383; SSF53383; 1. DR TIGRFAMs; TIGR03576; pyridox_MJ0158; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Pyridoxal phosphate; KW Reference proteome. FT CHAIN 1 374 UPF0425 pyridoxal phosphate-dependent FT protein MJ0158. FT /FTId=PRO_0000106722. FT MOD_RES 208 208 N6-(pyridoxal phosphate)lysine. FT HELIX 13 24 {ECO:0000244|PDB:2AEU}. FT HELIX 27 29 {ECO:0000244|PDB:2AEU}. FT HELIX 44 50 {ECO:0000244|PDB:2AEU}. FT HELIX 55 71 {ECO:0000244|PDB:2AEU}. FT STRAND 77 84 {ECO:0000244|PDB:2AEU}. FT HELIX 85 96 {ECO:0000244|PDB:2AEU}. FT STRAND 99 104 {ECO:0000244|PDB:2AEU}. FT STRAND 106 109 {ECO:0000244|PDB:2AEU}. FT HELIX 113 120 {ECO:0000244|PDB:2AEU}. FT STRAND 124 129 {ECO:0000244|PDB:2AEU}. FT HELIX 131 135 {ECO:0000244|PDB:2AEU}. FT STRAND 142 147 {ECO:0000244|PDB:2AEU}. FT HELIX 158 171 {ECO:0000244|PDB:2AEU}. FT STRAND 175 178 {ECO:0000244|PDB:2AEU}. FT HELIX 182 188 {ECO:0000244|PDB:2AEU}. FT HELIX 194 197 {ECO:0000244|PDB:2AEU}. FT STRAND 200 205 {ECO:0000244|PDB:2AEU}. FT STRAND 208 212 {ECO:0000244|PDB:2AEU}. FT STRAND 216 221 {ECO:0000244|PDB:2AEU}. FT HELIX 222 233 {ECO:0000244|PDB:2AEU}. FT TURN 234 236 {ECO:0000244|PDB:2AEU}. FT HELIX 241 253 {ECO:0000244|PDB:2AEU}. FT HELIX 256 268 {ECO:0000244|PDB:2AEU}. FT HELIX 272 281 {ECO:0000244|PDB:2AEU}. FT TURN 282 284 {ECO:0000244|PDB:2AEU}. FT STRAND 288 294 {ECO:0000244|PDB:2AEU}. FT STRAND 296 307 {ECO:0000244|PDB:2AEU}. FT HELIX 308 326 {ECO:0000244|PDB:2AEU}. FT HELIX 331 333 {ECO:0000244|PDB:2AEV}. FT STRAND 334 336 {ECO:0000244|PDB:2AEU}. FT STRAND 342 346 {ECO:0000244|PDB:2AEU}. FT HELIX 350 354 {ECO:0000244|PDB:2AEU}. FT HELIX 357 371 {ECO:0000244|PDB:2AEU}. SQ SEQUENCE 374 AA; 41880 MW; 3ED87DC642AA0AB8 CRC64; MLSDYEEFLR LEKARKIILE ILNEKGRDAL YDLSGLSGGF LIDEKDKALL NTYIGSSYFA EKVNEYGLKH LGGDENDKCV GFNRTSSAIL ATILALKPKK VIHYLPELPG HPSIERSCKI VNAKYFESDK VGEILNKIDK DTLVIITGST MDLKVIELEN FKKVINTAKN KEAIVFVDDA SGARVRLLFN QPPALKLGAD LVVTSTDKLM EGPRGGLLAG KKELVDKIYI EGTKFGLEAQ PPLLAGIYRA LKNFNLERIR KAFERAKNFD LSKIEKLNKE LKAIDDNINI VYERTPTGFV IKRVYKDDTI NIKKLIEIGF NLLKNYGIIT ITVAGMPGAS KSLRIDLTSR DAERIDDNYI IKAIVESIKM AFKS // ID Y1590_METJA Reviewed; 105 AA. AC Q58985; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1590; GN OrderedLocusNames=MJ1590; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99618.1; -; Genomic_DNA. DR PIR; E64498; E64498. DR STRING; 243232.MJ_1590; -. DR EnsemblBacteria; AAB99618; AAB99618; MJ_1590. DR KEGG; mja:MJ_1590; -. DR eggNOG; arCOG05117; Archaea. DR eggNOG; ENOG410XPA5; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 105 Uncharacterized protein MJ1590. FT /FTId=PRO_0000107431. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 41 61 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 105 AA; 11685 MW; 37A60722D7DCC2B3 CRC64; MRISPLIAGL IGGFTAAILQ ALFKVFPPPA YGICIACHTR DLVNWIINHL FGTTLGMALV SKAFPVLTVV GIFIGALITT FIYKETELKQ THSPVYWFHI RNFSY // ID Y1613_METJA Reviewed; 255 AA. AC Q59008; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ1613; GN OrderedLocusNames=MJ1613; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99633.1; -; Genomic_DNA. DR PIR; D64501; D64501. DR STRING; 243232.MJ_1613; -. DR EnsemblBacteria; AAB99633; AAB99633; MJ_1613. DR KEGG; mja:MJ_1613; -. DR eggNOG; arCOG01870; Archaea. DR eggNOG; COG1865; LUCA. DR InParanoid; Q59008; -. DR OMA; FLTICHI; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002808; AdoCbi_amidolase. DR Pfam; PF01955; CbiZ; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 255 Uncharacterized protein MJ1613. FT /FTId=PRO_0000107436. SQ SEQUENCE 255 AA; 28552 MW; 495F5F0DE97FCB25 CRC64; MIEKVLEMDD WKAYKIPHTV EIDGMVEETK TLIIEFKNKR KVLSTREGFK EVKYVGNHSI PVPFWDKVHN YKDYENQVLN KIGIKKEDIA LLSTGANMDN LAVAKEEFDE FYVVAFTTAG AKHNAIRLGD EEADYIEKDF KTYKIVDGKI VPKEEIGTVN IILITNANLT DGAMARAIIT ITEAKTNAFQ ELNIRSTKHP ELQATGTGTD NIVVVKGFGS GVDYTGGHTK MGEMIAKAVK RSVIEALIKQ DKIKI // ID Y1626_METJA Reviewed; 765 AA. AC Q59019; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1626; GN OrderedLocusNames=MJ1626; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99649.1; -; Genomic_DNA. DR PIR; G64502; G64502. DR ProteinModelPortal; Q59019; -. DR STRING; 243232.MJ_1626; -. DR EnsemblBacteria; AAB99649; AAB99649; MJ_1626. DR KEGG; mja:MJ_1626; -. DR eggNOG; arCOG08290; Archaea. DR eggNOG; ENOG41110SV; LUCA. DR OMA; YYSKLAF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR016024; ARM-type_fold. DR SUPFAM; SSF48371; SSF48371; 3. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 765 Uncharacterized protein MJ1626. FT /FTId=PRO_0000107446. SQ SEQUENCE 765 AA; 89607 MW; 056EEAA4FEF9B098 CRC64; MLITSSLLPP SGTWIFNINS LFCSLSIKNA LSNLPLMRFC NSSTTQHTST LVISLFIISP ENIIFFFRIF YYCDNMEREE FLKYLRQGKY DKLAKLINSY SDILSFLDEL FTSNKKDDVR RALLVLKRLD NEVIERYLYY ILLNLNEKRI IAKEAEEILK KITNKESVEE AILEIAKKPL DEKIVYLFLQ NMKEGNIFFR AILEHTKSKN MEESIKILLK NYNSEMILKI LANKLYSSEK DERELTINIL LNIVDSLTDE QKNILRGHLS VSLLGDEDKK LYRKFKQLFE KLDIPAELSD EQIKSLLKSH GKTTLNIILR ENIKLPANFY NREFLKDFLY TGDEEKQFVG VKLISLKKDS KKKVDLLFRF LNYGYGKAKT AAIRELKKIA QNNNELKKYI ENKTLMYAKK MNLGLKISSL RILKEFAKKE HLEFLINEHK RLKELVYKLE EEKFMGGFRH LLMMEEEIRK CNVAMRLIEE IVAEICLKND IHYNDLKISE KLGYEFYRTM ELIGVKNLNL IDIHEFLEDV KRDGELITYL SGIVINNNKI DDNLAKKILE VTEKAEMEDK DVLNANKIMI YASLNRVDKI GEIINMAEGY YSKLAFINGV KKFIDEKLLD EEKINLLIPK IAEMIYSTKK LRLMALEFFK NYPNELVLPI LINEIGNYRG EDKLMIDVIS NVIFKYPNNI HSIRELLNTD KRNSALKILL KVSEKRPELL EDFIYLLAGM YSSANEEDKK LIKKILKNIT TEEQKLILKP IIGDL // ID Y1633_METJA Reviewed; 478 AA. AC Q59027; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 93. DE RecName: Full=Uncharacterized protein MJ1633; GN OrderedLocusNames=MJ1633; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 RCK N-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00543}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99654.1; -; Genomic_DNA. DR PIR; G64503; G64503. DR ProteinModelPortal; Q59027; -. DR STRING; 243232.MJ_1633; -. DR PRIDE; Q59027; -. DR EnsemblBacteria; AAB99654; AAB99654; MJ_1633. DR KEGG; mja:MJ_1633; -. DR eggNOG; arCOG01566; Archaea. DR eggNOG; COG0618; LUCA. DR eggNOG; COG1226; LUCA. DR InParanoid; Q59027; -. DR OMA; AWAYQLI; -. DR PhylomeDB; Q59027; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006813; P:potassium ion transport; IEA:InterPro. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR003148; RCK_N. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. DR Pfam; PF02254; TrkA_N; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR PROSITE; PS51201; RCK_N; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 478 Uncharacterized protein MJ1633. FT /FTId=PRO_0000107448. FT DOMAIN 4 128 RCK N-terminal. {ECO:0000255|PROSITE- FT ProRule:PRU00543}. SQ SEQUENCE 478 AA; 52989 MW; 555CDADF98BD109D CRC64; MMNMITVIGF GSFGRKVVNF IKNKEPITII DKNIDDADDL VKEGVTVIVG DATQDEVLKK AKIENADIVL ILTNEPEVNR RIAERVCELS PNSYKIARAI PRYPELYMGL NIDKIINILE SGAKDIAKEV EDAKLKRKLM QLKSVLIEGK KRCMKLEKTE EEKKAPLLIL THINPDPDAI ASAMALKTLA ERWGVDSDIA YGGNIGYDEN KAMINLLGIK LLNVEDIDLD NYCVIAVIDT STSKQLPIEL PNIDIIIDHH NNTDLTAKYM DVRPEVGATA SILTQYLMEL DIEPSRNLAT ALFYGIQSDT DYFKRETSKL DFEAAAYLQS YIDASILNMI ENPEISTEVM EVLAKAVMNR RVVKGNIALA YVGEISNRDA LPKAADFLLK MEGISTTFVF GIVGDEIHIS ARTKDLRLNL GEILNKAFGG GGHQTAAAAK IPLGIFKAVS DKEALRKLVE EAIRAKILEV IGIKEEEK // ID Y163_METJA Reviewed; 187 AA. AC Q57627; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0163; GN OrderedLocusNames=MJ0163; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98151.1; -; Genomic_DNA. DR PIR; D64320; D64320. DR ProteinModelPortal; Q57627; -. DR STRING; 243232.MJ_0163; -. DR EnsemblBacteria; AAB98151; AAB98151; MJ_0163. DR KEGG; mja:MJ_0163; -. DR eggNOG; arCOG03412; Archaea. DR eggNOG; ENOG410Y1WW; LUCA. DR OMA; YIYISTI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 187 Uncharacterized protein MJ0163. FT /FTId=PRO_0000106725. FT TRANSMEM 3 23 Helical. {ECO:0000255}. SQ SEQUENCE 187 AA; 21510 MW; DC1FAA5F5CBA3861 CRC64; MDAIIIFLIL FIVGVLIGVG VYYYKEKERK KTYKIIEMEI IENLKELKPY VAPDEGREYT KEFDLVEIAL SYDIEDIIVV NDEGLVIATT LKDADEVGAT ASSIFEYIKK LCGNIKKVVI FKEDSYLYIY PLKLYGENLY VIIESKIALD VIEEKEILKR ITGVLKKYFS TITTIEQEIP EEALLSI // ID Y1641_METJA Reviewed; 287 AA. AC Q59035; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ1641; GN OrderedLocusNames=MJ1641; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99661.1; -; Genomic_DNA. DR PIR; G64504; G64504. DR ProteinModelPortal; Q59035; -. DR STRING; 243232.MJ_1641; -. DR EnsemblBacteria; AAB99661; AAB99661; MJ_1641. DR KEGG; mja:MJ_1641; -. DR eggNOG; arCOG00318; Archaea. DR eggNOG; COG0704; LUCA. DR KO; K02039; -. DR OMA; DRCVNIV; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR026022; PhoU_dom. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01895; PhoU; 2. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 287 Uncharacterized protein MJ1641. FT /FTId=PRO_0000107454. SQ SEQUENCE 287 AA; 33433 MW; 2DAE68A6F06B7642 CRC64; MNLWDNMLRG KEATLAGIIR VIIEEEPETQ DEIAEKLGIS RRYVAKLLKP LIDEKIVRHP YIVDMSKLHK INLEFDEYIL MKEIKTTLEK MEKTLLNNLD LVYTALKNSD KKLAEDIIIK DYALNKMEEE VRILLSMNAL KYLPGAYANA LATIASNLER LGDYIANIAE EVVHGLKLDK DIENEVNMIF TLLKEMLTEA IDVVKSKKKE TKIHELEEKL HKNLELLLNK VLENKREDLN FYVQFGMFLK DIERFGDRCV NIVDIALELY HNIPRNPIPE RLKRGML // ID Y1649_METJA Reviewed; 387 AA. AC Q59043; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Putative ribosomal RNA large subunit methyltransferase MJ1649; DE EC=2.1.1.-; GN OrderedLocusNames=MJ1649; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + rRNA = S-adenosyl-L- CC homocysteine + rRNA containing C(5)-methylcytosine. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. RlmI CC family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 PUA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00161}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99670.1; -; Genomic_DNA. DR PIR; G64505; G64505. DR ProteinModelPortal; Q59043; -. DR STRING; 243232.MJ_1649; -. DR EnsemblBacteria; AAB99670; AAB99670; MJ_1649. DR KEGG; mja:MJ_1649; -. DR eggNOG; arCOG00032; Archaea. DR eggNOG; COG1092; LUCA. DR InParanoid; Q59043; -. DR KO; K06969; -. DR OMA; YRWIYAE; -. DR PhylomeDB; Q59043; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR GO; GO:0006364; P:rRNA processing; IEA:UniProtKB-KW. DR Gene3D; 2.30.130.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002478; PUA. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR019614; SAM-dep_methyl-trfase. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF10672; Methyltrans_SAM; 1. DR Pfam; PF01472; PUA; 1. DR SMART; SM00359; PUA; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR SUPFAM; SSF88697; SSF88697; 1. DR PROSITE; PS50890; PUA; 1. PE 3: Inferred from homology; KW Complete proteome; Cytoplasm; Methyltransferase; Reference proteome; KW RNA-binding; rRNA processing; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 387 Putative ribosomal RNA large subunit FT methyltransferase MJ1649. FT /FTId=PRO_0000213172. FT DOMAIN 5 81 PUA. {ECO:0000255|PROSITE- FT ProRule:PRU00161}. SQ SEQUENCE 387 AA; 45222 MW; 7A03FF3C1B6730B6 CRC64; MVMILIKLEI DRRAYNSIKN FSRLVYTKAI KNRGDLPKKE EIVTLTYNGK FVAKALYNPK SVILKILTTE DEEIDYDFFY KRIFNAKIYR ENILNYKNTY RWIYAEGDEL PTIIFDKYNE LGAMQLMSKL IEKEYLKDIV DILFELSDLE TIYVKRGKKG ERIRDKIFGD KNKFETVIKE GDAKFKVNVR GHKTGFFLDQ RENRLYLEKF IKEGDRVLDI CCYTGGFSVH AAIRGAEVVG VDLSKKALKL AEENIELNNI PKDRYEFIEG NAFEVMKEMI EDKEKFDVVI LDPPAFTQTE DDIKNALRAY ASLNYLGIKL AKRIFVTCSC SHHVDKEMFK RTVISSAFRA KKELIMIDYK GQAPDHPISI GNKNLEYLKC IFFYVKN // ID Y1650_METJA Reviewed; 384 AA. AC Q59044; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1650; GN OrderedLocusNames=MJ1650; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99671.1; -; Genomic_DNA. DR PIR; H64505; H64505. DR ProteinModelPortal; Q59044; -. DR STRING; 243232.MJ_1650; -. DR EnsemblBacteria; AAB99671; AAB99671; MJ_1650. DR KEGG; mja:MJ_1650; -. DR eggNOG; arCOG04149; Archaea. DR eggNOG; COG1499; LUCA. DR InParanoid; Q59044; -. DR KO; K07562; -. DR OMA; YRCGISE; -. DR PhylomeDB; Q59044; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007064; NMD3. DR Pfam; PF04981; NMD3; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 384 Uncharacterized protein MJ1650. FT /FTId=PRO_0000107458. SQ SEQUENCE 384 AA; 44427 MW; 75400E0724358C3F CRC64; MIMVNLRIIN FIGDIMKIRG ICYRCGAEDE LIDGLCPICY AQEHPLIEVP DRVEIEVCHM CGSYKRKIWQ TPKSEEAFEI LNEIAYYATK DAIKKKSVMV EVEIYPEVTQ LPGGKRSKLI IPVHIVARGR LPGEKEDRTY EKDIEVHLRM VQCPRCSRFM SNYYEATLQV RAMNRYLTEE EREELDNFVR EELAKRLKKD RMAFIAKFIP QKEGLDYQLG SVGAARNVAQ RIKEKYGGKI TETATLVGVD RDSGKELYRV TVSVRVPEYK VGDVVEYKDK YYLVTAITED KVYMKSIDYK REKIGLAWHI AEKETKMAKK KDELDTATVI ATTPTIMVMD DKSYEVYEFD NIGDVKIKEG DKVKIFKKEG VSYLVNKIEG KDKQ // ID Y1657_METJA Reviewed; 332 AA. AC Q59051; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protease MJ1657; DE EC=3.4.-.-; GN OrderedLocusNames=MJ1657; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase U32 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99684.1; -; Genomic_DNA. DR PIR; G64506; G64506. DR ProteinModelPortal; Q59051; -. DR STRING; 243232.MJ_1657; -. DR DNASU; 1452566; -. DR EnsemblBacteria; AAB99684; AAB99684; MJ_1657. DR KEGG; mja:MJ_1657; -. DR eggNOG; arCOG03202; Archaea. DR eggNOG; COG0826; LUCA. DR InParanoid; Q59051; -. DR OMA; LVNEACL; -. DR PhylomeDB; Q59051; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR001539; Peptidase_U32. DR Pfam; PF01136; Peptidase_U32; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome. FT CHAIN 1 332 Uncharacterized protease MJ1657. FT /FTId=PRO_0000079187. SQ SEQUENCE 332 AA; 38535 MW; F1DC6C3FC0B62B5A CRC64; MFSISHPGDF ESLKIIVNEI NKLRKINKKL KKESFEVYVG FPEFVGTGRA TLYKPNFEDL AKQVNYAKKH NVRFEVVINA SCIGGMHLTP KGISYINWIF SQLKNIGVDS VALSDPYLVD LAKNNGLEVN VSCIALVDSL DKALFWDEKE VYAITLDSSI NRHFDIIQEI RENVSCKLKI LVNEACLYKC PMRIQHFNFF SHANAQNIPA LDDYYYNKCI NLRIKKKELI IKSPFIRPED LKYYKGLVDI FKISGRSHPI GWIKRVINAY LNERWDGNLM ELLDCPRELE HFYYLDNRAL DGAIEYWKSC NKLCSKCNFC KELAEKALKV KY // ID Y231_METJA Reviewed; 416 AA. AC Q57684; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0231; GN OrderedLocusNames=MJ0231; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98219.1; -; Genomic_DNA. DR PIR; H64328; H64328. DR ProteinModelPortal; Q57684; -. DR STRING; 243232.MJ_0231; -. DR EnsemblBacteria; AAB98219; AAB98219; MJ_0231. DR KEGG; mja:MJ_0231; -. DR eggNOG; arCOG00322; Archaea. DR eggNOG; COG0312; LUCA. DR InParanoid; Q57684; -. DR KO; K03592; -. DR OMA; YVTEVMG; -. DR PhylomeDB; Q57684; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:InterPro. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 416 Uncharacterized protein MJ0231. FT /FTId=PRO_0000106752. SQ SEQUENCE 416 AA; 46661 MW; 48C4CC8AA0DAEEBA CRC64; MDLEKLIKIG EKEGFETEVL FVKSYEVSVD LDGKSVDSFQ TGISYGIGVR VIKDGKVGFA YANKFDENIV YKAMKNLVED KYTEFAHPQK YKEPKGMFYK EILDLDEEKL LEDLITMRDI ALDNNAIVLS GGVSKEVGYA RLINSNGVDV EEQDTYFSAA ISIMYDGETS YECRTRHNIF DVEEISYRAL DLAKKSANGK AISYKGNIVL SPRALYDLLS YTLMPAFSAE NVQRDRSVLK GKIGEQIFGE NITIIDDGTL DYALYSSKCD GEGTATQKTV LVENGVLKNY LYDIKRANRE GKTSTGNASR GYRSLPYVSP TNFIIKETKN SLDDFDEYVY INGVIGSHTS NPITGDFAVE IQNSYYYKNG KIIPIKRGMF GGNIFEMFKE AIPLNDVEQR GKLISPSVVF KGEIIN // ID Y240_METJA Reviewed; 175 AA. AC Q57692; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Putative adenylate cyclase MJ0240; DE EC=4.6.1.1; DE AltName: Full=ATP pyrophosphate-lyase; DE AltName: Full=Adenylyl cyclase; GN OrderedLocusNames=MJ0240; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Could catalyze the biosynthesis of cyclic AMP (cAMP) CC from ATP. {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: ATP = 3',5'-cyclic AMP + diphosphate. CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. CC -!- SIMILARITY: Belongs to the adenylyl cyclase CyaB family. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 CYTH domain. {ECO:0000255|PROSITE- CC ProRule:PRU01044}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98225.1; -; Genomic_DNA. DR PIR; A64330; A64330. DR ProteinModelPortal; Q57692; -. DR STRING; 243232.MJ_0240; -. DR EnsemblBacteria; AAB98225; AAB98225; MJ_0240. DR KEGG; mja:MJ_0240; -. DR eggNOG; arCOG01723; Archaea. DR eggNOG; COG1437; LUCA. DR InParanoid; Q57692; -. DR KO; K05873; -. DR OMA; KGPKIDK; -. DR PhylomeDB; Q57692; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0004016; F:adenylate cyclase activity; ISS:UniProtKB. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 2.40.320.10; -; 1. DR InterPro; IPR008173; Adenylyl_cyclase_CyaB. DR InterPro; IPR033469; CYTH-like_dom. DR InterPro; IPR023577; CYTH_domain. DR Pfam; PF01928; CYTH; 1. DR SMART; SM01118; CYTH; 1. DR SUPFAM; SSF55154; SSF55154; 1. DR TIGRFAMs; TIGR00318; cyaB; 1. DR PROSITE; PS51707; CYTH; 1. PE 3: Inferred from homology; KW ATP-binding; cAMP biosynthesis; Complete proteome; Cytoplasm; Lyase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 175 Putative adenylate cyclase MJ0240. FT /FTId=PRO_0000106757. FT DOMAIN 1 175 CYTH. {ECO:0000255|PROSITE- FT ProRule:PRU01044}. FT ACT_SITE 37 37 Proton acceptor. {ECO:0000250}. SQ SEQUENCE 175 AA; 20821 MW; 7A85A90FD46F97F9 CRC64; MIEVEIKVKI DDKNKVVEQL KKLGFKFIKK KFQEDIYFNG IDRDFRETDE ALRIRDEDGN FFVTYKGPKI DKISKTREEI EVKIEDKEKM RQIFKKLGFK EVPPIRKIRE IYKKEDIEAS IDDVEGLGLF LELEKSISDI NEKDKVLEEM MEILKALNIS KDNIIRKSYL ELRGL // ID Y272_METJA Reviewed; 66 AA. AC Q57720; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0272; GN OrderedLocusNames=MJ0272; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98257.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98257.1; ALT_INIT; Genomic_DNA. DR PIR; A64334; A64334. DR ProteinModelPortal; Q57720; -. DR STRING; 243232.MJ_0272; -. DR EnsemblBacteria; AAB98257; AAB98257; MJ_0272. DR KEGG; mja:MJ_0272; -. DR eggNOG; arCOG01864; Archaea. DR eggNOG; COG1476; LUCA. DR InParanoid; Q57720; -. DR KO; K07729; -. DR OMA; WRAKKDI; -. DR PhylomeDB; Q57720; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 66 Uncharacterized HTH-type transcriptional FT regulator MJ0272. FT /FTId=PRO_0000149789. FT DOMAIN 5 59 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 16 35 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 66 AA; 7738 MW; 32667152D3AD810E CRC64; MKNKLKYYRA LHNLTQEDLA KKLGVSRQTI IAIEKGKYDP SLKLAFKIAK FFGVKIEDIF IYEDDE // ID Y292_METJA Reviewed; 93 AA. AC Q57740; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein MJ0292; GN OrderedLocusNames=MJ0292; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98277.1; -; Genomic_DNA. DR PIR; E64336; E64336. DR STRING; 243232.MJ_0292; -. DR EnsemblBacteria; AAB98277; AAB98277; MJ_0292. DR KEGG; mja:MJ_0292; -. DR eggNOG; arCOG04877; Archaea. DR eggNOG; COG1320; LUCA. DR KO; K14112; -. DR OMA; GVIDCAC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein MJ0292. FT /FTId=PRO_0000106778. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT COMPBIAS 75 86 Ala-rich. SQ SEQUENCE 93 AA; 10483 MW; B2A8CC8115AC160C CRC64; MVMLMEQFIG IVKDILVLIA SFGILLASYR LWIEKDRKNI IYARIHILGV IDCACFLIFI ALGETLLAFV YLILAPFLAH AIAHAAYNDN LSE // ID Y310_METJA Reviewed; 114 AA. AC Q57758; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0310; GN OrderedLocusNames=MJ0310; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98296.1; -; Genomic_DNA. DR PIR; G64338; G64338. DR ProteinModelPortal; Q57758; -. DR STRING; 243232.MJ_0310; -. DR EnsemblBacteria; AAB98296; AAB98296; MJ_0310. DR KEGG; mja:MJ_0310; -. DR eggNOG; arCOG02603; Archaea. DR eggNOG; COG2018; LUCA. DR InParanoid; Q57758; -. DR KO; K07131; -. DR OMA; MFENVIA; -. DR PhylomeDB; Q57758; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJ0310. FT /FTId=PRO_0000106786. SQ SEQUENCE 114 AA; 11872 MW; 55030A1155D57A5E CRC64; MIDRVLLELN KTEGIKGSMV VGKDGLVIAS QLPGSVDAEL VGAMASAAFG AAERTAAEIG MGTLEQTMIE GEHGKTLMVD AGEGILVVLT DAKVNLGLIR ITMKRAADKI KAMF // ID Y314_METJA Reviewed; 263 AA. AC Q57762; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Uncharacterized protein MJ0314; GN OrderedLocusNames=MJ0314; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98310.1; -; Genomic_DNA. DR PIR; C64339; C64339. DR ProteinModelPortal; Q57762; -. DR STRING; 243232.MJ_0314; -. DR EnsemblBacteria; AAB98310; AAB98310; MJ_0314. DR KEGG; mja:MJ_0314; -. DR eggNOG; arCOG03156; Archaea. DR eggNOG; COG3780; LUCA. DR PhylomeDB; Q57762; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0000150; F:recombinase activity; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 2. DR Gene3D; 3.10.28.10; -; 2. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR025246; IS30-like_HTH. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR006120; Resolvase_HTH_dom. DR Pfam; PF13936; HTH_38; 1. DR Pfam; PF02796; HTH_7; 1. DR Pfam; PF14528; LAGLIDADG_3; 2. DR SUPFAM; SSF46689; SSF46689; 1. DR SUPFAM; SSF55608; SSF55608; 2. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 263 Uncharacterized protein MJ0314. FT /FTId=PRO_0000106789. FT DOMAIN 107 246 DOD-type homing endonuclease. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 263 AA; 30805 MW; A7520A3BBE0CC5CD CRC64; MELYKKGYSA RTIAKILGCS KSTVCYRLYK LGITPRRGLD LNPQEIIKLY QNGYTTTEIA KIMKCSHETI RRILRNNNID IRKSSESLII KNTKKINLNP SESLAYILGV LNGDGSVNKQ ESNYVIELKV TDKDFIEEFK RNLENIGFKY INEYVRKFEN KKDQYVVRVR SKGFYYWYKS LNVDYYMNVI GNNEKLMISW LKGFYDSEGS VVINKKGNYV YKYVSIANTN RNLIDVCCSF LEKLGIEYSV YCEKNNRYKS GYL // ID Y331_METJA Reviewed; 135 AA. AC Q57777; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0331; GN OrderedLocusNames=MJ0331; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98319.1; -; Genomic_DNA. DR PIR; C64341; C64341. DR STRING; 243232.MJ_0331; -. DR EnsemblBacteria; AAB98319; AAB98319; MJ_0331. DR KEGG; mja:MJ_0331; -. DR eggNOG; arCOG08300; Archaea. DR eggNOG; ENOG410YKZZ; LUCA. DR OMA; VINNMEY; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR006522; Phage_virion_morphogenesis. DR Pfam; PF05069; Phage_tail_S; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 135 Uncharacterized protein MJ0331. FT /FTId=PRO_0000106800. SQ SEQUENCE 135 AA; 15878 MW; 5ED8E259ECA9D98F CRC64; MDYKQWVREF KKELAHEIEK ELVAEVDDNI QRGFQKKELK WKPLSKDYQK RKEKEGRNTK GLIYHGALLK ATDSKVKITS KGLQVKVFNN MVYAGVHEFG SKKKNIPARP FIQPALKKVQ KDLPKIVEKV IKRMR // ID Y343_METJA Reviewed; 849 AA. AC Q57789; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0343; GN OrderedLocusNames=MJ0343; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98333.1; -; Genomic_DNA. DR PIR; G64342; G64342. DR ProteinModelPortal; Q57789; -. DR STRING; 243232.MJ_0343; -. DR EnsemblBacteria; AAB98333; AAB98333; MJ_0343. DR KEGG; mja:MJ_0343; -. DR eggNOG; arCOG07425; Archaea. DR eggNOG; ENOG4111U0W; LUCA. DR OMA; FMENIIG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 849 Uncharacterized protein MJ0343. FT /FTId=PRO_0000106813. FT TRANSMEM 587 607 Helical. {ECO:0000255}. FT TRANSMEM 620 640 Helical. {ECO:0000255}. SQ SEQUENCE 849 AA; 94457 MW; D7103CAD1CAB5C5C CRC64; MDCMKKLKVE GTLELNLDDK DVRKNLKSLE KIKSKLEIES NINAVIKQLD ELKNVKSEVE FKSNINMIIR ELEEIEADAS KMNINFDYDL SKLKSELEQL KNTKIDIKTN TDQILKQINK IKSELSEKQT IRAKVEVDRT EWDKLKKEWS EKYHINAIAD VASVGTAYMG ISDAEKYNEL MTILRERGLT KDQAERLIQI GLYNGYSLDE IRDGIVYSNE AVLKLAASND KYAAQILAAM AMAERGGEPG ADDIARMISA LTAMGKSNEE IMKMVNAEVL EMKQGHTEVA EAIREFSITM GDTLDPEKFA SILIQAQAAG AQDVGQLAEA INDLALNSRQ MGFDVEKALR EIQKTKDDKT LAELAKKYGL TYEQIVKIHD YLQRVDLDKG LPDNTNELDR LISINKDQKG ILETIKQDIE GWLAGHGYLQ YGAELGVGLG GLGKILEIAI GAAIGSALKD AFGEIKSTLF GKISLDNLKL PELSKIKLPV DLEIPKIPKI SMPKIKLPVD LKLPKIPKIN IPKINLPNVS GLSNAFKGLG EAVRFAGRAF GFLSVVVEPV KQLLEGDIQG AIEHLKVGLI ELAAWPVALG EALAAVTLAV GDFLGLFDLD GDSPLSAARA GILTLLAAFE SIYSFITGDW SVVQNTLQEA FEELGMKEDE ARQAAENLAQ QWQQLPQQIL DAFNGFVDNI KQTFDEWWNG LNEWWSQKIE EAKNWGSDLI QNIIDGIKEK FSELENAVSQ AAGIISSYLH HTTPDVGPLK DDDKWGIHFM ENIIGGIRKE IPNLKKTIDY TAKLMSSANP KNWKIQQVGI THSTSYSYGD IHINVVGNSF NEHQLAQKIA LILKKQRFR // ID Y3502_METJA Reviewed; 129 AA. AC Q60267; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 47. DE RecName: Full=Uncharacterized protein MJECL02; GN OrderedLocusNames=MJECL02; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37076.1; -; Genomic_DNA. DR PIR; B64510; B64510. DR EnsemblBacteria; AAC37076; AAC37076; MJ_ECL02. DR KEGG; mja:MJECL02; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MJECL02. FT /FTId=PRO_0000107494. SQ SEQUENCE 129 AA; 15215 MW; F6C24D21B1495B77 CRC64; MLMMSIILSM CIQMIRIKSG LSSVICVYSQ MNNFRIFWWD IMTAFEELLE LPTIEAIYKL KKLILKMESS KNSEVYYYQG VIKRIIQRLS LLDQEKSLKE NLKFCVDNYI LSQRTIEDLK TAIEIASKL // ID Y3503_METJA Reviewed; 108 AA. AC Q60268; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 47. DE RecName: Full=Uncharacterized protein MJECL03; GN OrderedLocusNames=MJECL03; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37077.1; -; Genomic_DNA. DR PIR; C64510; C64510. DR EnsemblBacteria; AAC37077; AAC37077; MJ_ECL03. DR KEGG; mja:MJECL03; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 108 Uncharacterized protein MJECL03. FT /FTId=PRO_0000107495. SQ SEQUENCE 108 AA; 12603 MW; 36E6408CDEFA49EB CRC64; MRDCKVQVGG FGEWIIKCDL ELTFDEVMRG EIEELVEFIK SLESLLKSSS EDSFRKNVLN ALISTLKTLP WTSRLEYADD EHNIIDVYPD DKNKKWIIKC NLCLFPDE // ID Y3519_METJA Reviewed; 174 AA. AC Q60279; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 09-DEC-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJECL19; GN OrderedLocusNames=MJECL19; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37090.1; -; Genomic_DNA. DR PIR; B64512; B64512. DR ProteinModelPortal; Q60279; -. DR EnsemblBacteria; AAC37090; AAC37090; MJ_ECL19. DR KEGG; mja:MJECL19; -. DR InParanoid; Q60279; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 174 Uncharacterized protein MJECL19. FT /FTId=PRO_0000107507. SQ SEQUENCE 174 AA; 20273 MW; D1082FF3171527E4 CRC64; MESKEFDDDK IKIISMTPKS EKSDKIVMQI VEEFINSFPD DRYKFRVLLK VAELICKNGL CNEAFLILDK IPDSYYKSSA LYKMADILYR NKEHDRLIQI AEKIPDDYKK SEVLLKVVEL LCESGKYDEA INIAEKIPDN YYKSEALFKI AETLSNKGYY DKAVEIAEKI PDNF // ID Y3527_METJA Reviewed; 162 AA. AC Q60286; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 71. DE RecName: Full=Uncharacterized protein MJECL27; GN OrderedLocusNames=MJECL27; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 C2H2-type zinc finger. {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJECS06. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37098.1; -; Genomic_DNA. DR PIR; B64513; B64513. DR ProteinModelPortal; Q60286; -. DR EnsemblBacteria; AAC37098; AAC37098; MJ_ECL27. DR KEGG; mja:MJECL27; -. DR HOGENOM; HOG000155253; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Metal-binding; Plasmid; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 162 Uncharacterized protein MJECL27. FT /FTId=PRO_0000107513. FT ZN_FING 29 50 C2H2-type. SQ SEQUENCE 162 AA; 18670 MW; C2FBD6BAC47555D7 CRC64; MDILGEIVNV DEYVEKLELQ KNDIGFYKCP FCDYTNADAK VVRKHVKSKH LEEIEKELKK LESQKSKNNG KKQTGQKKQG KGKKQPKRVR ETCVSTQERK DYVLFFCHNH KVRLHLANGE VLEGKCCCKD PYTVLVDVGK GDVVIVNKAY IVKYVPLDLE KL // ID Y3531_METJA Reviewed; 65 AA. AC Q60265; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 20-JUN-2001, sequence version 2. DT 09-DEC-2015, entry version 66. DE RecName: Full=Putative antitoxin MJECL31; GN OrderedLocusNames=MJECL31; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Possibly the antitoxin component of a toxin-antitoxin CC (TA) module. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0165 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37074.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37074.1; ALT_INIT; Genomic_DNA. DR PIR; F64513; F64513. DR ProteinModelPortal; Q60265; -. DR EnsemblBacteria; AAC37074; AAC37074; MJ_ECL31. DR KEGG; mja:MJECL31; -. DR HOGENOM; HOG000232276; -. DR InParanoid; Q60265; -. DR OMA; CKDIDYK; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 4.10.1150.10; -; 1. DR InterPro; IPR024069; AF2212-like_dom. DR InterPro; IPR008203; UPF0165. DR Pfam; PF01954; DUF104; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 65 Putative antitoxin MJECL31. FT /FTId=PRO_0000156859. SQ SEQUENCE 65 AA; 7737 MW; DFE63A96F3FCF801 CRC64; MSEIIEVIYE DGVLKPLKPL KIKGKKRLKI KIVNDDVEEF LKSMIIKKCK DIDYKKLKEA YYESF // ID Y356_METJA Reviewed; 97 AA. AC Q57802; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0356; GN OrderedLocusNames=MJ0356; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98348.1; -; Genomic_DNA. DR PIR; D64344; D64344. DR STRING; 243232.MJ_0356; -. DR EnsemblBacteria; AAB98348; AAB98348; MJ_0356. DR KEGG; mja:MJ_0356; -. DR eggNOG; arCOG09654; Archaea. DR eggNOG; ENOG41110VX; LUCA. DR OMA; MKFLVVK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ0356. FT /FTId=PRO_0000106827. SQ SEQUENCE 97 AA; 10738 MW; 2020A0628CBE1BE0 CRC64; MALKEFGGLI MKFLVVKKGS ETKRINVEEI KEISNVGSFV IIRYSGGEVK IKAKGDAEEA ADWITKMITD FPNKIIDLRA GFESGDKAKT NLRVEAC // ID Y364_METJA Reviewed; 114 AA. AC Q57810; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0364; GN OrderedLocusNames=MJ0364; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98355.1; -; Genomic_DNA. DR PIR; D64345; D64345. DR STRING; 243232.MJ_0364; -. DR EnsemblBacteria; AAB98355; AAB98355; MJ_0364. DR KEGG; mja:MJ_0364; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJ0364. FT /FTId=PRO_0000106833. SQ SEQUENCE 114 AA; 13315 MW; 87C1148084DF542F CRC64; MGSMIEINFS HDYFKLREQR FTTIRSKHYL KNKGLRVGDV VKIKHPSGEF PAKIVGVEVK RICDIPLEIL KKDAEFEGFN IKTHQDFVDL LNSFIPYKSN KLTTEKAIIY LERV // ID Y367_METJA Reviewed; 330 AA. AC Q57813; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 89. DE RecName: Full=Probable integrase/recombinase protein MJ0367; GN OrderedLocusNames=MJ0367; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the 'phage' integrase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98346.1; -; Genomic_DNA. DR PIR; G64345; G64345. DR ProteinModelPortal; Q57813; -. DR STRING; 243232.MJ_0367; -. DR DNASU; 1451224; -. DR EnsemblBacteria; AAB98346; AAB98346; MJ_0367. DR KEGG; mja:MJ_0367; -. DR eggNOG; arCOG01241; Archaea. DR eggNOG; COG0582; LUCA. DR InParanoid; Q57813; -. DR KO; K04763; -. DR OMA; FYAKEAF; -. DR PhylomeDB; Q57813; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0075713; P:establishment of integrated proviral latency; IEA:UniProtKB-KW. DR GO; GO:0046718; P:viral entry into host cell; IEA:UniProtKB-KW. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR InterPro; IPR004107; Integrase_SAM-like_N. DR Pfam; PF13495; Phage_int_SAM_4; 1. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 3: Inferred from homology; KW Complete proteome; DNA integration; DNA recombination; KW Reference proteome; Viral genome integration; KW Virus entry into host cell. FT CHAIN 1 330 Probable integrase/recombinase protein FT MJ0367. FT /FTId=PRO_0000197583. FT ACT_SITE 310 310 O-(3'-phospho-DNA)-tyrosine intermediate. FT {ECO:0000250}. SQ SEQUENCE 330 AA; 39424 MW; F397DBF4B9A54531 CRC64; MREKELKHIE NLLLLKVKKE KIEETDKIKE YLKRFEDERR FDGIKESTIK SDLDRLRVFL DYCINYLGKN PEELKTSDFV KFFNYLDTVR KVSKSSQRKY FLLLKVFYRV LRMYNVIQEF VEESKDRKRF ARIEIQHYDA VDAEMLNMIL KKIIESGSRT RIRDALIIRL LWDTGCRVSE VLNLKYKDCD LDNGIFKIRN TKTHEERTVV CSSDTLELLR NYVQFNVRQG SDDYLFQNSQ GGRVRKEWIS EVFRKAVNEL KEEGKIPKNR RIVIHSIRHG RAVDLLNKGV PIDIVKEYLG HKSMNTTLIY AHSKERAESL EFIKKLLRIQ // ID Y415_METJA Reviewed; 162 AA. AC Q57858; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0415; GN OrderedLocusNames=MJ0415; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98406.1; -; Genomic_DNA. DR PIR; G64351; G64351. DR STRING; 243232.MJ_0415; -. DR EnsemblBacteria; AAB98406; AAB98406; MJ_0415. DR KEGG; mja:MJ_0415; -. DR eggNOG; arCOG06574; Archaea. DR eggNOG; ENOG410Z58P; LUCA. DR OMA; QIICYYA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 162 Uncharacterized protein MJ0415. FT /FTId=PRO_0000106861. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 162 AA; 18253 MW; 79D77FE542F10BFF CRC64; MKRLKLLGGV MLFAIVSLMV CGCMVVFPKK YPDVLYKEYD VIKIENRTIN GVKTAIVYQV KTEIGARSSP YSLDADSKKD IGAITYYVFK NTDVDEVQII CYYAGGGGLQ PYYKFKIKRR DAELSGLLNV SEKELPSATL YYIDKLISLG DLWINDRLPV NG // ID Y424_METJA Reviewed; 103 AA. AC Q57867; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 69. DE RecName: Full=Uncharacterized protein MJ0424; GN OrderedLocusNames=MJ0424; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98418.1; -; Genomic_DNA. DR PIR; H64352; H64352. DR ProteinModelPortal; Q57867; -. DR STRING; 243232.MJ_0424; -. DR EnsemblBacteria; AAB98418; AAB98418; MJ_0424. DR KEGG; mja:MJ_0424; -. DR eggNOG; arCOG03166; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 103 Uncharacterized protein MJ0424. FT /FTId=PRO_0000106869. SQ SEQUENCE 103 AA; 12056 MW; 4C7B826FE537D176 CRC64; MLTNDSMNEN LNELKRVFSS LTGKEYFKNL DVGLVDLFRY LRDEIKDEKV VIALDEFQYL MQLNRGVLSI FQKIWDGILA DTKVFLIICG SSCVSKHGRF RDW // ID Y426_METJA Reviewed; 180 AA. AC Q57869; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0426; GN OrderedLocusNames=MJ0426; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98419.1; -; Genomic_DNA. DR PIR; B64353; B64353. DR STRING; 243232.MJ_0426; -. DR EnsemblBacteria; AAB98419; AAB98419; MJ_0426. DR KEGG; mja:MJ_0426; -. DR eggNOG; arCOG08292; Archaea. DR eggNOG; ENOG41111ST; LUCA. DR OMA; GENYALY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 180 Uncharacterized protein MJ0426. FT /FTId=PRO_0000106871. FT COMPBIAS 45 51 Poly-Glu. SQ SEQUENCE 180 AA; 21609 MW; E9BE603DEBAE4053 CRC64; MIMKELIKIL KQFGIYSEYL KILDVELDGD RYITILIPTT LNWIEEEEIE EILEEMLKNV RVKISRLPLN KFIKIYLEKN VKNKAYGENI ENVKIEGENY ALYIDWKNKK IVIHKFNGKN PIKESCKLSS NWETMWGIWV LGFESKEKAK EFAENLADEI YKYYEIDFDI EEHKRCLEDN // ID Y435_METJA Reviewed; 93 AA. AC Q57877; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0435; GN OrderedLocusNames=MJ0435; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98423.1; -; Genomic_DNA. DR ProteinModelPortal; Q57877; -. DR STRING; 243232.MJ_0435; -. DR PRIDE; Q57877; -. DR EnsemblBacteria; AAB98423; AAB98423; MJ_0435. DR KEGG; mja:MJ_0435; -. DR eggNOG; arCOG01206; Archaea. DR eggNOG; COG1669; LUCA. DR InParanoid; Q57877; -. DR KO; K07075; -. DR OMA; YNSIHPL; -. DR PhylomeDB; Q57877; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 93 Uncharacterized protein MJ0435. FT /FTId=PRO_0000106875. SQ SEQUENCE 93 AA; 10661 MW; AA6FD2014B942A68 CRC64; MNINEIKRKI IPILLKHGVK RASIFGSYAR NEQKETSDID ILVEFGEGKS LLDLVRLKYE LEEVLGKEVD VLTYNSIHPL LKDRILNEAV DVL // ID Y440_METJA Reviewed; 299 AA. AC Q57882; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0440; GN OrderedLocusNames=MJ0440; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98427.1; -; Genomic_DNA. DR PIR; H64354; H64354. DR ProteinModelPortal; Q57882; -. DR STRING; 243232.MJ_0440; -. DR DNASU; 1451300; -. DR EnsemblBacteria; AAB98427; AAB98427; MJ_0440. DR KEGG; mja:MJ_0440; -. DR eggNOG; arCOG02177; Archaea. DR eggNOG; COG1967; LUCA. DR InParanoid; Q57882; -. DR OMA; YDATTTF; -. DR PhylomeDB; Q57882; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002749; DUF63. DR Pfam; PF01889; DUF63; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 299 Uncharacterized protein MJ0440. FT /FTId=PRO_0000106877. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. FT TRANSMEM 122 142 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. SQ SEQUENCE 299 AA; 34301 MW; BE64A14E71FFC5B6 CRC64; MYYKLVLSHY SKTSTLINIT LIKHLINILR ERMIQEIKNF IYKYYIEPAE KGTGYNIVQE ITYGIILALA LYLFYKALRK LNINIDEKFA IPGIVFTVLI ALMRALVDCG YIERSFLTIT PGIVFLIGGF FILTILTTGL VFKEKYYKAS AVIGLILLLY FLFVFLQHIT HLEAILYVGI LVGIFYYLVK FLDKTLKLNI IQSKIDDYVV IGQLIDASAT TIGIGVYGYW EQHPIPRFLM ETFGVYAFIP FKLLIILLAL YILNKEVEDE NIKNIIKLCI MALGLAPGLR DLFRTVMGV // ID Y443_METJA Reviewed; 227 AA. AC Q57885; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=KH domain-containing protein MJ0443; GN OrderedLocusNames=MJ0443; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 KH domains. {ECO:0000255|PROSITE- CC ProRule:PRU00117}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98430.1; -; Genomic_DNA. DR PIR; C64355; C64355. DR ProteinModelPortal; Q57885; -. DR STRING; 243232.MJ_0443; -. DR EnsemblBacteria; AAB98430; AAB98430; MJ_0443. DR KEGG; mja:MJ_0443; -. DR eggNOG; arCOG04150; Archaea. DR eggNOG; COG1094; LUCA. DR InParanoid; Q57885; -. DR KO; K06961; -. DR OMA; HVKIPQD; -. DR PhylomeDB; Q57885; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.1370.10; -; 2. DR InterPro; IPR004087; KH_dom. DR InterPro; IPR004088; KH_dom_type_1. DR InterPro; IPR019964; KH_domain_protein_archaea. DR Pfam; PF00013; KH_1; 2. DR SMART; SM00322; KH; 2. DR SUPFAM; SSF54791; SSF54791; 2. DR TIGRFAMs; TIGR03665; arCOG04150; 1. DR PROSITE; PS50084; KH_TYPE_1; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; RNA-binding. FT CHAIN 1 227 KH domain-containing protein MJ0443. FT /FTId=PRO_0000050165. FT DOMAIN 14 77 KH 1. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. FT DOMAIN 106 163 KH 2. {ECO:0000255|PROSITE- FT ProRule:PRU00117}. SQ SEQUENCE 227 AA; 25840 MW; 9E59A5FE3CDE8E9C CRC64; MVIIMVFGNI GQDKSIEILK IPKDRVGVLI GKKGNVKKTI EKELGVKLEI DADGTVTIYG TDKQKDPLAV WKARDIVRAI GRGFNPEIAL KLVSDEYVLE VIDIEDYASS DNSIRRLKGR VIGKEGKSRR YIESLTGANV SVYGNTVAIV GEHEPVQIAK EAVEMLLRGA SHAKTYKFLE RERQKIKRAR FELWKKKSDV DELYEKMNPN YEEIEIEEDE DEIEDEE // ID Y485_METJA Reviewed; 337 AA. AC Q57909; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=CTU1/ATPBD3 family protein MJ0485; GN OrderedLocusNames=MJ0485; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TtcA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98476.1; -; Genomic_DNA. DR PIR; E64360; E64360. DR ProteinModelPortal; Q57909; -. DR STRING; 243232.MJ_0485; -. DR EnsemblBacteria; AAB98476; AAB98476; MJ_0485. DR KEGG; mja:MJ_0485; -. DR eggNOG; arCOG00042; Archaea. DR eggNOG; COG0037; LUCA. DR InParanoid; Q57909; -. DR OMA; DNCEYLN; -. DR PhylomeDB; Q57909; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR012089; 2-thiocytidine_tRNA_synth_TtcA. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR011063; TilS/TtcA_N. DR Pfam; PF01171; ATP_bind_3; 1. DR PIRSF; PIRSF004976; ATPase_YdaO; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 337 CTU1/ATPBD3 family protein MJ0485. FT /FTId=PRO_0000106892. SQ SEQUENCE 337 AA; 39323 MW; 6FB9C66BB619F065 CRC64; MVEINLRELK KYANPFFLTI RKDKILVNNK RMARLSRTKM DKIEEEFGIP VIYSKTYEYV STKVGRFINK HKIIAPRDIV IVGLSGGKDS LLLLHLLEVY RRKYGIKLIA VTVDVNIGGI RPWKEDTEGV KLIKHHCEML NVPHIILKND LDVVELSEIL TKHSKGMEFS PCFSCSVIKR HLLGKLAKEI AENENIPYEK VKLAYGHNLD DNSDTILANI FKGERLKFMR PLTRFKYNEV DYQSFKIPLE ECIIIRPMLP ILERDIIKAL EECGIEYYKD KDMCPYSRDR GDSVRRRCHE ILEKLEEEIP NIREMVVSSA LKTVEYYSKN PYGEDNL // ID Y491_METJA Reviewed; 167 AA. AC Q57914; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0491; GN OrderedLocusNames=MJ0491; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98482.1; -; Genomic_DNA. DR PIR; C64361; C64361. DR STRING; 243232.MJ_0491; -. DR EnsemblBacteria; AAB98482; AAB98482; MJ_0491. DR KEGG; mja:MJ_0491; -. DR eggNOG; arCOG04873; Archaea. DR eggNOG; COG4077; LUCA. DR OMA; PDTFGFE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014515; UCP921964. DR Pfam; PF09893; DUF2120; 1. DR PIRSF; PIRSF021964; UCP921964; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 167 Uncharacterized protein MJ0491. FT /FTId=PRO_0000106896. SQ SEQUENCE 167 AA; 19481 MW; D77A570BA3AB583C CRC64; MHLENLLKSL KNTVKKLKTY NFGVSMWKVN IGRLMHALNA FKGSKPLFET DEMLMVKGVC RDEEVEKYGS IKDYLVKKLE KEGFEIVEDI KEIDKFVSRI NEILKENPLY PDTFGFERMK ESFEMIGCEC DYVIAKKRNI MVGVCMYFDK KMKNPKFVEV VGVLLPS // ID Y500_METJA Reviewed; 259 AA. AC Q57923; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0500; GN OrderedLocusNames=MJ0500; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98491.1; -; Genomic_DNA. DR PIR; D64362; D64362. DR ProteinModelPortal; Q57923; -. DR STRING; 243232.MJ_0500; -. DR EnsemblBacteria; AAB98491; AAB98491; MJ_0500. DR KEGG; mja:MJ_0500; -. DR eggNOG; arCOG03216; Archaea. DR eggNOG; COG2014; LUCA. DR InParanoid; Q57923; -. DR KO; K09138; -. DR OMA; THLASMK; -. DR PhylomeDB; Q57923; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007161; DUF364. DR InterPro; IPR025251; DUF4213. DR Pfam; PF04016; DUF364; 1. DR Pfam; PF13938; DUF4213; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 259 Uncharacterized protein MJ0500. FT /FTId=PRO_0000106901. SQ SEQUENCE 259 AA; 29193 MW; 5C528A176B1C2D36 CRC64; MSFMIIEEIK ERALNLLSEK EEDFKVIDFS FALPYSYVLI ESNGKKALGV AMTLLEEYRG HGNRKDLNIN KNLEEFINMA DSFDIVERTL GVAAINAVSQ YYFNFEANGK DAAELVLNRD DIKKIAFVGN MIPVVNMLKK SEKFDIYVFE RSPSLLMDGV LSDAFEYRLL PEMDAVFISG TTLLNDTLDF VLDRAKNAKL KILVGPTAQS LPELFKGFGI THIASTKIID VDKALLYLKF ASSSMLFKGA SKKYTMEVE // ID Y513_METJA Reviewed; 241 AA. AC Q57933; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0513; GN OrderedLocusNames=MJ0513; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98512.1; -; Genomic_DNA. DR PIR; A64364; A64364. DR ProteinModelPortal; Q57933; -. DR STRING; 243232.MJ_0513; -. DR EnsemblBacteria; AAB98512; AAB98512; MJ_0513. DR KEGG; mja:MJ_0513; -. DR eggNOG; arCOG08281; Archaea. DR eggNOG; ENOG411110K; LUCA. DR OMA; KDYTIFR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 241 Uncharacterized protein MJ0513. FT /FTId=PRO_0000106906. FT COMPBIAS 230 233 Poly-Glu. SQ SEQUENCE 241 AA; 27890 MW; 88C7D3ACE842AC57 CRC64; MMIMVKYGIK IEDDRVEIVR YSTVYTDEGV EELEEIYLQI KADDYESILG IYEPYPKKDV RFVGNLDDLK VVKGQEMRTA VPIPLSLCRA KYLKRIDEDD ERITYLDING VPIQRGIIVG IVVGVQHKRT STGKDYTIFR IFDGYGWGRL RLFGIKANPE IFTGMFIRGF VRFGAVEFRT EEGELRKAIS LTLNDIPVIV QPKEYIVHKK FIDEVVLPRV APELIEEDKE EEETDEETIN S // ID Y51B_METJA Reviewed; 408 AA. AC P81293; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-MAY-2016, entry version 85. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ0514.2; GN OrderedLocusNames=MJ0514.2; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 8 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98509.1; -; Genomic_DNA. DR ProteinModelPortal; P81293; -. DR STRING; 243232.MJ_0514.2; -. DR EnsemblBacteria; AAB98509; AAB98509; MJ_0514.2. DR KEGG; mja:MJ_0514.2; -. DR eggNOG; arCOG02183; Archaea. DR eggNOG; COG1145; LUCA. DR InParanoid; P81293; -. DR KO; K14107; -. DR OMA; IGCRICY; -. DR PhylomeDB; P81293; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF12838; Fer4_7; 2. DR Pfam; PF13187; Fer4_9; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 5. DR PROSITE; PS51379; 4FE4S_FER_2; 8. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 408 Uncharacterized polyferredoxin-like FT protein MJ0514.2. FT /FTId=PRO_0000159150. FT DOMAIN 42 72 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 78 107 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 122 151 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 151 181 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 212 241 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 233 265 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 273 302 4Fe-4S ferredoxin-type 7. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 304 333 4Fe-4S ferredoxin-type 8. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 52 52 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 55 55 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 58 58 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 62 62 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 87 87 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 90 90 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 93 93 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 97 97 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 131 131 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 134 134 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 137 137 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 141 141 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 160 160 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 163 163 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 166 166 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 170 170 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 282 282 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 285 285 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 288 288 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 292 292 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 408 AA; 46462 MW; 2D3C2C10D5ECCD1D CRC64; MIVMASSLWY LYEFARKKWI KRFIDAKSDK SSYIPPERYR KIPPIVKFPE KCISCEGCKE SCPAFAIEMI YNEEYNKKLP VIDEGSCVAC ANCIEVCPTG VLEMDKHRVE TEGLFFDKPK YSNLIIDEEV CVRCGNCERA CPINVIERKE GKYVINMALC ISCKECIKVC PIENAIVVVD EKTLKEKIDK AFEIKNKKIT GKLEIKENVI EKIPHIVSGL CVSCGICKDV CVGEIDLNEK KVVECVKCGL CIEVCSTTAI RIYKPIIPKR KDICYVIDED LCIGCRICQK VCGSGAIKIS KETKLPYIVP ELCVRGGACA RECPVGAIKV VKPEEAEEAV KVRIIEDKII ESIEKDLVLY TEKYGKVKEE IEKLSLKKLK EELKRRVYEE NKRIMEKKRE LYDKGNNS // ID Y538_METJA Reviewed; 260 AA. AC Q57958; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0538; GN OrderedLocusNames=MJ0538; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98536.1; -; Genomic_DNA. DR PIR; B64367; B64367. DR ProteinModelPortal; Q57958; -. DR STRING; 243232.MJ_0538; -. DR EnsemblBacteria; AAB98536; AAB98536; MJ_0538. DR KEGG; mja:MJ_0538; -. DR eggNOG; arCOG05037; Archaea. DR eggNOG; ENOG410Z4DI; LUCA. DR OMA; KISGNEM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020292; Uncharacterised_MJ0538. DR ProDom; PD039347; Uncharacterised_MJ0538; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 260 Uncharacterized protein MJ0538. FT /FTId=PRO_0000106920. SQ SEQUENCE 260 AA; 30184 MW; AD68C8FC3846EB3D CRC64; MIKIHALEEV KGNSKEIVEK EFENLANELK EKYNAKLKYV DEDIEEDENL KFYTKIGEFE INFDNFKDYI NFCLKYGADI EVIKPEKLKL TANEINEVLA LVISAFKSFM DTYKIGFDVY VKEKKDIDVE GYKKGKYDED EIADFEEEGF IRVKAVFEAI GKNENEVVKN LLISLDRDEI IINKIITKNF NENNENFNGL MAVDLLCNPF EMFEIAYKYL PVAISIQRDE IELSLADIQD IGNELSGAMF ELSHAVIMRK // ID Y548_METJA Reviewed; 293 AA. AC Q57968; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0548; GN OrderedLocusNames=MJ0548; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98540.1; -; Genomic_DNA. DR PIR; D64368; D64368. DR ProteinModelPortal; Q57968; -. DR STRING; 243232.MJ_0548; -. DR EnsemblBacteria; AAB98540; AAB98540; MJ_0548. DR KEGG; mja:MJ_0548; -. DR eggNOG; arCOG03213; Archaea. DR eggNOG; COG4079; LUCA. DR OMA; KRRRMYL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR016754; UCP019262. DR Pfam; PF09894; DUF2121; 1. DR PIRSF; PIRSF019262; UCP019262; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 293 Uncharacterized protein MJ0548. FT /FTId=PRO_0000106926. SQ SEQUENCE 293 AA; 33877 MW; 57D83285180D8F9A CRC64; MSLIICYYGK NGAVIGGDRR QIFFRGSEEN RKILEEKLYS GEIKSEEELY KLAEKLNIKI IIEDDREKVR KISDSVVCGE VRSLGIDAKR RRVYATKGKC AIVDILNDTV TNQTIKEGFG IVVLGNRFLK KKAEEELKRT AKLFPMMPIQ QIEDAIKEIF EKLKWHPTVS KEYDIYSVNK YEKNFEEVIK KDIESLFKYR EQLRKQLIDF GKVMSIVNKI VKNGEIGVIK DGKLHLYDDY IAIDKIDPNP KVFKVVDVEG NFKDGDIVVI ENGDMKIKGT NEKVTTKYII IHK // ID Y568_METJA Reviewed; 125 AA. AC Q57988; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 94. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0568; GN OrderedLocusNames=MJ0568; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH dtxR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00296}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98562.1; -; Genomic_DNA. DR PIR; H64370; H64370. DR ProteinModelPortal; Q57988; -. DR STRING; 243232.MJ_0568; -. DR EnsemblBacteria; AAB98562; AAB98562; MJ_0568. DR KEGG; mja:MJ_0568; -. DR eggNOG; arCOG02100; Archaea. DR eggNOG; COG1321; LUCA. DR InParanoid; Q57988; -. DR KO; K03709; -. DR OMA; EACKIEH; -. DR PhylomeDB; Q57988; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 1.10.60.10; -; 1. DR InterPro; IPR001367; Fe_dep_repressor. DR InterPro; IPR022687; HTH_DTXR. DR InterPro; IPR022689; Iron_dep_repressor. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF02742; Fe_dep_repr_C; 1. DR Pfam; PF01325; Fe_dep_repress; 1. DR SMART; SM00529; HTH_DTXR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS50944; HTH_DTXR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 125 Uncharacterized HTH-type transcriptional FT regulator MJ0568. FT /FTId=PRO_0000201124. FT DOMAIN 1 63 HTH dtxR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00296}. SQ SEQUENCE 125 AA; 14588 MW; AC4703013A3F7577 CRC64; MSQSIEDYLE RIYLFIKENN RPIKTTELAK LLNIKPSAVT NMAKKLHRLG YVNYEPYIGI TLTEKGIEEA KKILDKHKTI KIFLVEFLGL DEKTASEEAC KLEHALSDEI LERLKIFMEK FKDKV // ID Y575_METJA Reviewed; 229 AA. AC Q57995; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0575; GN OrderedLocusNames=MJ0575; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0838. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98566.1; -; Genomic_DNA. DR PIR; G64371; G64371. DR ProteinModelPortal; Q57995; -. DR STRING; 243232.MJ_0575; -. DR DNASU; 1451440; -. DR EnsemblBacteria; AAB98566; AAB98566; MJ_0575. DR KEGG; mja:MJ_0575; -. DR eggNOG; arCOG02469; Archaea. DR eggNOG; COG1810; LUCA. DR InParanoid; Q57995; -. DR OMA; EMCLLDE; -. DR PhylomeDB; Q57995; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR003745; DUF166. DR Pfam; PF02593; DUF166; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 229 Uncharacterized protein MJ0575. FT /FTId=PRO_0000106938. SQ SEQUENCE 229 AA; 26218 MW; 32A33DF47C2E5BD3 CRC64; MAKILVVTDG AYGYRIKGTI NSFGKKNKFI GIYKINKPDD LIVDDIEFPD ELLEKIKEAD ILLLYTQHPD NTYYLCYEAR RLNKDIAIIV ATWSGEGEKK ELKKFDAICP EEMCLLDENE VGSLIDKYPK LKEFLEEFGT PKVKVYVKDN KVIDVEVLRT SICGSTLFMA KLMKGMEVND IEEFAKKSAM LIQRYPCVAG KIKIFRGDCR KQKALNIHKE AVLEGIIFI // ID Y576_METJA Reviewed; 347 AA. AC Q57996; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized transporter MJ0576; GN OrderedLocusNames=MJ0576; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate CC transporter (TDT) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98567.1; -; Genomic_DNA. DR PIR; H64371; H64371. DR ProteinModelPortal; Q57996; -. DR STRING; 243232.MJ_0576; -. DR EnsemblBacteria; AAB98567; AAB98567; MJ_0576. DR KEGG; mja:MJ_0576; -. DR eggNOG; arCOG04355; Archaea. DR eggNOG; COG1275; LUCA. DR InParanoid; Q57996; -. DR OMA; DFINIGH; -. DR PhylomeDB; Q57996; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011552; TehA/Mae1. DR InterPro; IPR004695; Voltage-dep_anion_channel. DR Pfam; PF03595; SLAC1; 1. DR TIGRFAMs; TIGR00816; tdt; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 347 Uncharacterized transporter MJ0576. FT /FTId=PRO_0000106939. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 111 131 Helical. {ECO:0000255}. FT TRANSMEM 149 169 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TRANSMEM 214 234 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TRANSMEM 283 303 Helical. {ECO:0000255}. FT TRANSMEM 312 332 Helical. {ECO:0000255}. SQ SEQUENCE 347 AA; 39557 MW; 632F7671A31DE183 CRC64; MLEACESKLD IIKNFVPSWF AAVMGTGILA VDSLLYSSYL PILKDVAVGL FYFNVLLFFI FLVPWVLRWI MFKDNALADL KHPVLSAFYP TIAVSCLVLG ADFINIGHNM FWGGVFWTLG AIGMFLFSLI VPFYMFKSES IKLDHVNPGW YIPPVGLIVI PIAGSLIMPH LTGVWHELTV LINYFGWGAG FFLYLALLAV VIYRFILHHP LPSAMAPTVW INLGPIGAGI VALINMVNNS PFITIKEPFY IFSFIFWGFG LWWSLMAIIM TLYYVKKLKL PYAMSWWAFI FPLGAYVASS HLVYKIFKFS IIDYIGFGLY WLLFFFWAIT LIKTTNKVYT GEVFKGH // ID Y578_METJA Reviewed; 276 AA. AC Q57998; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Uncharacterized protein MJ0578; GN OrderedLocusNames=MJ0578; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98569.1; -; Genomic_DNA. DR PIR; B64372; B64372. DR ProteinModelPortal; Q57998; -. DR STRING; 243232.MJ_0578; -. DR EnsemblBacteria; AAB98569; AAB98569; MJ_0578. DR KEGG; mja:MJ_0578; -. DR eggNOG; arCOG04073; Archaea. DR eggNOG; COG1149; LUCA. DR InParanoid; Q57998; -. DR OMA; CEGCAVC; -. DR PhylomeDB; Q57998; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR Pfam; PF00037; Fer4; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; ATP-binding; Complete proteome; Iron; Iron-sulfur; KW Metal-binding; Nucleotide-binding; Reference proteome; Repeat. FT CHAIN 1 276 Uncharacterized protein MJ0578. FT /FTId=PRO_0000159310. FT DOMAIN 68 96 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 92 121 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT NP_BIND 15 22 ATP. {ECO:0000255}. FT METAL 76 76 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 79 79 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 82 82 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 86 86 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 101 101 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 104 104 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 107 107 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 111 111 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 276 AA; 30794 MW; 0F900CE7F2E88669 CRC64; MDYLGIIMKI AIISGKGGVG KSSISTSLAK LFSKEFNIVA LDCDVDAPNF NLMFDVKDKK LLEVIYREIY EINDDCIRCG KCLDVCQFDA IGDFKINPIL CEGCGACELI CEFDAIEPIK RESGYIYEGF VGFPLIWGEL EVGESGSGKI IEHIKNHAKK YKAELGIIDG PPGVGCPLIS TVKDVDLALC IVEPTKSSVN DCLRLIETLN FFNVEYLIVE NKKGMNNINY PFKIFHSIPF DFDVPKLIAN KILLCDSNSK VSESIKELYE KLKEFI // ID Y589_METJA Reviewed; 102 AA. AC Q58009; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0589; GN OrderedLocusNames=MJ0589; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98585.1; -; Genomic_DNA. DR PIR; E64373; E64373. DR STRING; 243232.MJ_0589; -. DR EnsemblBacteria; AAB98585; AAB98585; MJ_0589. DR KEGG; mja:MJ_0589; -. DR eggNOG; arCOG08294; Archaea. DR eggNOG; ENOG41111JE; LUCA. DR OMA; RFVENWD; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 102 Uncharacterized protein MJ0589. FT /FTId=PRO_0000106947. SQ SEQUENCE 102 AA; 12265 MW; A613FC1184D66358 CRC64; MRPKEVWREL LEIAKNYYDE DKIFYSKTKR GAYRIKSFTK DKIVIEKLRG KLDEVLGKKR FVENWDKLVH GVEWNIPPAI KSFLKLHPKI VENEDGNLIY KE // ID Y604_METJA Reviewed; 100 AA. AC Q58021; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0604; GN OrderedLocusNames=MJ0604; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0126/MJ0128/MJ0141/MJ0435/MJ0604/MJ1215/MJ1217/MJ1305/MJ1379 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98594.1; -; Genomic_DNA. DR PIR; D64375; D64375. DR ProteinModelPortal; Q58021; -. DR STRING; 243232.MJ_0604; -. DR EnsemblBacteria; AAB98594; AAB98594; MJ_0604. DR KEGG; mja:MJ_0604; -. DR eggNOG; arCOG01201; Archaea. DR eggNOG; COG1708; LUCA. DR InParanoid; Q58021; -. DR KO; K07076; -. DR OMA; YTEESDI; -. DR PhylomeDB; Q58021; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016779; F:nucleotidyltransferase activity; IEA:InterPro. DR InterPro; IPR002934; Polymerase_NTP_transf_dom. DR Pfam; PF01909; NTP_transf_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 100 Uncharacterized protein MJ0604. FT /FTId=PRO_0000106953. SQ SEQUENCE 100 AA; 11667 MW; A259493170FF0BC2 CRC64; MNEEKAIKEF VNALKSKYRG RIKKIILFGS YARGDYTEES DIDILIVGDV DFDYVIDLCT KLLLKYGVVI NAIVESEELF NKKINWSFHR NVLEEGRVLY // ID Y625_METJA Reviewed; 336 AA. AC Q58042; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Uncharacterized ATP-binding protein MJ0625; GN OrderedLocusNames=MJ0625; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98625.1; -; Genomic_DNA. DR PIR; A64378; A64378. DR ProteinModelPortal; Q58042; -. DR STRING; 243232.MJ_0625; -. DR EnsemblBacteria; AAB98625; AAB98625; MJ_0625. DR KEGG; mja:MJ_0625; -. DR eggNOG; ENOG4102U6X; Archaea. DR eggNOG; ENOG410Z1ZF; LUCA. DR InParanoid; Q58042; -. DR KO; K06921; -. DR OMA; WYAIREI; -. DR PhylomeDB; Q58042; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 336 Uncharacterized ATP-binding protein FT MJ0625. FT /FTId=PRO_0000184669. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 336 AA; 40111 MW; 7B17DB2D17C412B6 CRC64; MKFYNREKEL NYLKTYCQLD PNSILFVYGP KSSGKSTVMR RVIKELEDSN IVFFYYNLRK YATYSKEEFL RVFFEKSEKK YLLNKLELNL GVFKFGVEEN FDFNNLKLND VFAKINESIN AVVEDGKKPV LIIDELQKLK NIYFNGGKSL LNELFNLFVS LTKMEHLCHV ICLTSDTLFI EEIYQSSTLE NTSKYYLIDW LRKGTIRNIL KEEGFSEEEI NYCLDYLSLP YEIVDLIENK KLGLSVEETI RQWINIEKDK IKYLIDTTDL DEEELYKVLS KFKDKIKISY EKEVKKEEMK YFKFLIKNEI LFYDVINGII KPTSVKKWYA IREILK // ID Y630_METJA Reviewed; 297 AA. AC Q58047; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Putative phosphate permease MJ0630; GN OrderedLocusNames=MJ0630; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Potential transporter for phosphate. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the inorganic phosphate transporter (PiT) CC (TC 2.A.20) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98622.1; -; Genomic_DNA. DR PIR; F64378; F64378. DR ProteinModelPortal; Q58047; -. DR STRING; 243232.MJ_0630; -. DR TCDB; 2.A.20.3.1; the inorganic phosphate transporter (pit) family. DR EnsemblBacteria; AAB98622; AAB98622; MJ_0630. DR KEGG; mja:MJ_0630; -. DR eggNOG; arCOG02267; Archaea. DR eggNOG; COG0306; LUCA. DR InParanoid; Q58047; -. DR KO; K03306; -. DR OMA; FRNKAPY; -. DR PhylomeDB; Q58047; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0005315; F:inorganic phosphate transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0035435; P:phosphate ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR001204; Phos_transporter. DR PANTHER; PTHR11101; PTHR11101; 1. DR Pfam; PF01384; PHO4; 2. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Phosphate transport; KW Reference proteome; Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 297 Putative phosphate permease MJ0630. FT /FTId=PRO_0000080804. FT TRANSMEM 2 22 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 121 141 Helical. {ECO:0000255}. FT TRANSMEM 154 174 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. FT TRANSMEM 274 294 Helical. {ECO:0000255}. SQ SEQUENCE 297 AA; 32036 MW; 4A51E12ADE68026C CRC64; MITIEISINL ELIISFYLLF ILGANNVANA IGTAYASRAT TYRNLLILFS ISVIIGSLFA KNVGSTVNSL SSDALTALII SALVMTLSTY KKVPISLHTV IICSLIGLNF NSSNLYVFGE ILLSWILSPI IAVVIAYILY SAYEKIDISI LKKITMIRYF LLISAAVVAF NLGSNDLPTV LGTFTTSQII YIIGAIFLCL GAYLYGNRVS ETLSMITNLS VSSAFIAQLS GGLAVTIFTA LGMPVSTTQA IVGGILGVGL TKGIKTVRWK VLKNIIFWWV VAPIIALIIG FIINRMI // ID Y634_METJA Reviewed; 620 AA. AC Q58051; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 94. DE RecName: Full=Uncharacterized KamA family protein MJ0634; GN OrderedLocusNames=MJ0634; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the radical SAM superfamily. KamA family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98629.1; -; Genomic_DNA. DR PIR; B64379; B64379. DR ProteinModelPortal; Q58051; -. DR STRING; 243232.MJ_0634; -. DR EnsemblBacteria; AAB98629; AAB98629; MJ_0634. DR KEGG; mja:MJ_0634; -. DR eggNOG; arCOG03246; Archaea. DR eggNOG; COG1509; LUCA. DR InParanoid; Q58051; -. DR KO; K01843; -. DR OMA; TFYPKGK; -. DR PhylomeDB; Q58051; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR003739; Lys_aminomutase/Glu_NH3_mut. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR TIGRFAMs; TIGR00238; TIGR00238; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Pyridoxal phosphate; Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 620 Uncharacterized KamA family protein FT MJ0634. FT /FTId=PRO_0000172295. FT METAL 338 338 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 342 342 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 345 345 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT MOD_RES 552 552 N6-(pyridoxal phosphate)lysine. FT {ECO:0000250}. SQ SEQUENCE 620 AA; 73372 MW; 4A5E12147E5F159C CRC64; MTIKSMTEYE TISYKTFLDI FSPLPEIGEI LEESESVEEA REKLFEFCKE LEWEIRMGRI KFDNEVDRWL ALKAIEVFLN IISKDNERLA GFSTLEYLWK AYKGDEEALK EIREGFIEEF RHLFLAMSGK ADYSLGFLGK RLLEEGVKFI DFSKIKGREA GIARSNFLDK VYEIMREYIS RYPSGLDKRI ILKRKKNREI LEEFFGITDE EWFNYKWQFK NVLRGLKGVK ILRELREVTN FKISDEDLEI IEKAVKNGIP FGLTPYYLHL FDFENPYVED LAVRRQVIPP EWYVEKMIEH KEDRNIAFDF MGEHDTSPID LVTRRYVTIA IIKPYESCPQ ICVYCQRNWM VQDFDAKAFP GWEKVEKALD WFAEHDSMIE ILITGGDPFS LSDKAIEKML NRIAEMNHVV GVRFGTRTIV TAPMRITDEL AELLGSFEKS LMISTHVESC YEITPEVAEA VKKLRTNNIY IYNQHVFHRY VSRRFENVAL RIALKKVGII PYYTFYPKGK MEHKDYLVPI ARLAQEVKEE ARLLPGSFRT DEPIFNVPRM GKNHLRAWQD RELIAIKPNG SRVYLMHPWE KGIYPTKLYT YEDVPIKEYL DSLKEIGENI EEYKTIWYYY // ID Y636_METJA Reviewed; 397 AA. AC Q58053; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Uncharacterized protein MJ0636; GN OrderedLocusNames=MJ0636; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98630.1; -; Genomic_DNA. DR PIR; D64379; D64379. DR ProteinModelPortal; Q58053; -. DR STRING; 243232.MJ_0636; -. DR EnsemblBacteria; AAB98630; AAB98630; MJ_0636. DR KEGG; mja:MJ_0636; -. DR eggNOG; arCOG01068; Archaea. DR eggNOG; COG1249; LUCA. DR InParanoid; Q58053; -. DR KO; K00382; -. DR OMA; MNRIYYE; -. DR PhylomeDB; Q58053; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 3. DR InterPro; IPR023753; FAD/NAD-binding_dom. DR Pfam; PF07992; Pyr_redox_2; 1. DR SUPFAM; SSF51905; SSF51905; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 397 Uncharacterized protein MJ0636. FT /FTId=PRO_0000106964. SQ SEQUENCE 397 AA; 45232 MW; F97631613501CA3A CRC64; MLFGESMTLK IAVVGAGPAG RTSAMFLAKN GFDVDLFEKD RVGGTCLNYG CTYITGLREM ADIINNLSIL KGEKVHLEEI ISFKELQEKI NKIQDRIRNK LEKETKELGV NIKYKEFKNK HKNDYDYIIY ATGRNYPSNY NGYEVLTHKD IPNLRELPEN ILIIGGGVVA TEYASIFSDF GCNVVLYTRS KILKEIKDEE IRDYLMKKVI NFKIINDKEE LENLLKDESY TKILAIGGNG RFKTDDYLRV LNEEKVYACG DCLINGGGNT PISRMEGRVV AQNIYNEINN KPLIKPNYEL IPKTIRLSLT ISYVGKQTNN YKTIRSCVGK GNFFKVLSGV GINKIYYEDG KIVGAITMMP CAEILPYFTQ LIRGIDVYNN FMEVHPSTDI FYKEFRS // ID Y651_METJA Reviewed; 311 AA. AC Q58067; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 90. DE RecName: Full=Putative protease MJ0651; DE EC=3.4.21.-; GN OrderedLocusNames=MJ0651; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase S49 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98642.1; -; Genomic_DNA. DR ProteinModelPortal; Q58067; -. DR STRING; 243232.MJ_0651; -. DR EnsemblBacteria; AAB98642; AAB98642; MJ_0651. DR KEGG; mja:MJ_0651; -. DR eggNOG; arCOG01311; Archaea. DR eggNOG; COG0616; LUCA. DR InParanoid; Q58067; -. DR KO; K04773; -. DR OMA; MYLAVKR; -. DR PhylomeDB; Q58067; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW. DR Gene3D; 3.90.226.10; -; 2. DR InterPro; IPR029045; ClpP/crotonase-like_dom. DR InterPro; IPR004635; Pept_S49_SppA. DR InterPro; IPR002142; Peptidase_S49. DR Pfam; PF01343; Peptidase_S49; 1. DR SUPFAM; SSF52096; SSF52096; 2. DR TIGRFAMs; TIGR00706; SppA_dom; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Protease; Reference proteome; KW Serine protease. FT CHAIN 1 311 Putative protease MJ0651. FT /FTId=PRO_0000171456. FT ACT_SITE 128 128 Nucleophile. {ECO:0000250}. FT ACT_SITE 180 180 Proton donor/acceptor. {ECO:0000250}. SQ SEQUENCE 311 AA; 34665 MW; C46AAC8451216D64 CRC64; MKKIYIILLI LFVILISLIG ASILLVMSLS GENVDLFGGE KIAKVYLCNE IYFDYNQGDG IFPQQKKDAR YYINLLDDLE KDDSVKGVLL VVNSPGGEVI ASEKLARKVE ELAKKKPVVV YVEGLDASGA YMVSAPADYI VAEKHSIVGS IGVRMDLMHY YGLMKKLGIN VTTIKAGKYK DIGSPFRPMT KEEKEYLQKM INETYMDFVK WVAEHRHLSI NYTLKIADGK IYSGEDAKKV GLVDEVGTEE DALKKLEQLA NVSNPEIVEY GLEENKGLFG LTYYLGYGIG KGIGEVLYGM EKINGRVELL S // ID Y658_METJA Reviewed; 318 AA. AC P82736; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAR-2001, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0658; GN OrderedLocusNames=MJ0658; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH238. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98657.1; -; Genomic_DNA. DR ProteinModelPortal; P82736; -. DR STRING; 243232.MJ_0658; -. DR EnsemblBacteria; AAB98657; AAB98657; MJ_0658. DR KEGG; mja:MJ_0658; -. DR eggNOG; arCOG00098; Archaea. DR eggNOG; COG2218; LUCA. DR KO; K00202; -. DR OMA; FTYNFIW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 2.160.20.60; -; 2. DR InterPro; IPR002489; Glu_synth_asu_C. DR Pfam; PF01493; GXGXG; 2. DR SUPFAM; SSF69336; SSF69336; 2. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 318 Uncharacterized protein MJ0658. FT /FTId=PRO_0000106974. SQ SEQUENCE 318 AA; 35714 MW; 92948BAE49469523 CRC64; MLFNIFKKSN KKKLDEFLNE NKDKVLTLKL DKPVDCLCDF TYNFIWQSKF NPETEIKENI TFKTLVEHLK NGGVVYIKGN VGKRFCSSMG VDLKYFSGSG ERIKVGTVIV DGDVDTRFGI SMLSGTVYIN EKNKIKEPMG NVIEVESDIK GYRKFISITE FVEERYKEEK LLKPNKFDKN KGILEINDKI KRDTVGARLN EDKTIVVNGD VDLSTGILMR KGKVIVNGNA GKNTGAVLNG GTVIINGNTN DFTGFEMRDG IIVVDGNAGK YLGAKKKEGV IYARDGKEVP PTKKYELNND DIAFLKSLGY TGKFYKFI // ID Y70A_METJA Reviewed; 102 AA. AC P81311; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0703.1; GN OrderedLocusNames=MJ0703.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98706.1; -; Genomic_DNA. DR STRING; 243232.MJ_0703.1; -. DR EnsemblBacteria; AAB98706; AAB98706; MJ_0703.1. DR KEGG; mja:MJ_0703.1; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 102 Uncharacterized protein MJ0703.1. FT /FTId=PRO_0000106996. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 35 55 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. SQ SEQUENCE 102 AA; 11685 MW; 1A1A282B05A7CBA0 CRC64; MVGNMNIRDK IKSIKNWINF IKPIITIVGI VISAVAFTIS ILWGMLFLIL FLILITFSKT IRKILSKKER SYQGLILSII GSIIIISIIV YSHCYIEFKL LI // ID Y716_METJA Reviewed; 95 AA. AC Q58126; DT 01-NOV-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0716; GN OrderedLocusNames=MJ0716; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98715.1; -; Genomic_DNA. DR PIR; D64389; D64389. DR ProteinModelPortal; Q58126; -. DR EnsemblBacteria; AAB98715; AAB98715; MJ_0716. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR SUPFAM; SSF111126; SSF111126; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 95 Uncharacterized protein MJ0716. FT /FTId=PRO_0000107001. SQ SEQUENCE 95 AA; 11014 MW; 2CD4174BE8DA3A5C CRC64; MEFYNIGDIM ALKFTIEELS NQKRDTLGRN IDVTVFRLIR FMDLERYLGR GAHGVIYECG RELGLALNPK TVEDVVKFCE EYKIGKVEIV NKEPL // ID Y726_METJA Reviewed; 216 AA. AC Q58136; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Uncharacterized protein MJ0726; GN OrderedLocusNames=MJ0726; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FrhG family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98722.1; -; Genomic_DNA. DR PIR; F64390; F64390. DR ProteinModelPortal; Q58136; -. DR STRING; 243232.MJ_0726; -. DR EnsemblBacteria; AAB98722; AAB98722; MJ_0726. DR KEGG; mja:MJ_0726; -. DR eggNOG; arCOG02473; Archaea. DR eggNOG; COG1941; LUCA. DR KO; K00443; -. DR OMA; TSNKELC; -. DR PhylomeDB; Q58136; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF01058; Oxidored_q6; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Oxidoreductase; Reference proteome; Repeat; Transport. FT CHAIN 1 216 Uncharacterized protein MJ0726. FT /FTId=PRO_0000159235. FT DOMAIN 160 189 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 188 216 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 169 169 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 172 172 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 175 175 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. FT METAL 179 179 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 197 197 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 200 200 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 203 203 Iron-sulfur 2 (4Fe-4S). {ECO:0000255}. FT METAL 207 207 Iron-sulfur 1 (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 216 AA; 23789 MW; 2FD9F067698982FE CRC64; MTGCGSCGKI IKNIEKKYYN QLKEKDIVLV GGAVNLDDEE EVKKIMEIRK NSKVLIAVGS CAVSGGFQRM LIGLENGFPQ RFVRIGDVVK VDYAIIGCPP DEEEVERIVK AVIEKDKEIV DSYLILKPYE VIAGKPIIDA YMKVNDVLLT SNKELCLGCD DKPINDEFCT GCGTCVAKCP ANALTIDEKP KVNISKCIKC GTCFFNCIRV KEALLP // ID Y730_METJA Reviewed; 186 AA. AC Q58140; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0730; GN OrderedLocusNames=MJ0730; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0208. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98726.1; -; Genomic_DNA. DR PIR; B64391; B64391. DR ProteinModelPortal; Q58140; -. DR STRING; 243232.MJ_0730; -. DR EnsemblBacteria; AAB98726; AAB98726; MJ_0730. DR KEGG; mja:MJ_0730; -. DR eggNOG; arCOG01705; Archaea. DR eggNOG; COG1036; LUCA. DR InParanoid; Q58140; -. DR OMA; IYPPDNK; -. DR PhylomeDB; Q58140; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.40.50.1950; -; 1. DR InterPro; IPR014072; Archaeoflavo_AfpA. DR InterPro; IPR003382; Flavoprotein. DR Pfam; PF02441; Flavoprotein; 1. DR SUPFAM; SSF52507; SSF52507; 1. DR TIGRFAMs; TIGR02699; archaeo_AfpA; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein MJ0730. FT /FTId=PRO_0000107006. SQ SEQUENCE 186 AA; 21182 MW; DE9526F02DB1B25A CRC64; MLKIAWGITG CGDKLPEVVE IMKKLKNKYN LDVDIYLSKN AKIVVKWYKL WQVLEDEFYD LRVEVNANAP FLVGKLQTGK YDLFLVAPAT ANTTAKIAYG IADTLITNSV AQAMKAKVPV YIFPPDNKKG TVETILPGNK KLTLYMRDVD VENVERLRRM EGIEVLDKPE DIEKVILKHI EVKKQQ // ID Y732_METJA Reviewed; 393 AA. AC Q58142; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 93. DE RecName: Full=Uncharacterized protein MJ0732; GN OrderedLocusNames=MJ0732; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98728.1; -; Genomic_DNA. DR PIR; D64391; D64391. DR ProteinModelPortal; Q58142; -. DR STRING; 243232.MJ_0732; -. DR EnsemblBacteria; AAB98728; AAB98728; MJ_0732. DR KEGG; mja:MJ_0732; -. DR eggNOG; arCOG00509; Archaea. DR eggNOG; COG0426; LUCA. DR InParanoid; Q58142; -. DR OMA; KFIRTPM; -. DR PhylomeDB; Q58142; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR016440; Rubredoxin-O_OxRdtase. DR Pfam; PF00258; Flavodoxin_1; 1. DR Pfam; PF00753; Lactamase_B; 1. DR PIRSF; PIRSF005243; ROO; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 393 Uncharacterized protein MJ0732. FT /FTId=PRO_0000107007. FT DOMAIN 250 389 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. SQ SEQUENCE 393 AA; 45555 MW; CF01B59793BBA20F CRC64; MILMVLEIKN GIYWVGVIDW EIRDFHGYGT PYGSTYNSYL IKDKKNVLID TAKDYMFNEL IYGISKFIDP KDLDYIIVNH VEKDHSGCVD KLVEISNATI ITNEKGKEHL SLYYDTKDWD FIIVDTGDEI NIGDRTLKFI RTPMLHWPDN MLTYCKEEKI LFSNDAFGQH IASSERFDYE IGEGIFEHAK DYFANILMPY KMLIPDAIKA VKNLDIELIC PSHGVIWKEY INEIIEKYNE WAMNKTKNKA VIVYDTMYNS TKKMAHAIAE GLMEKGVEVK IYRVCETSLS RIMTEILDAK YVLVGSPTVN RNLYPEVGKF LAYMDCIRPL DKIGVAFGSY GWMECATEKI KEIFKNLGFK IVDDECLTVR FAPKEEHLKK CYEFGKRLAD IGF // ID Y749_METJA Reviewed; 246 AA. AC Q58159; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 104. DE RecName: Full=Uncharacterized protein MJ0749; GN OrderedLocusNames=MJ0749; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98742.1; -; Genomic_DNA. DR PIR; E64393; E64393. DR ProteinModelPortal; Q58159; -. DR STRING; 243232.MJ_0749; -. DR EnsemblBacteria; AAB98742; AAB98742; MJ_0749. DR KEGG; mja:MJ_0749; -. DR eggNOG; arCOG02772; Archaea. DR eggNOG; COG0348; LUCA. DR InParanoid; Q58159; -. DR OMA; TIFFIRA; -. DR PhylomeDB; Q58159; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12801; Fer4_5; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 246 Uncharacterized protein MJ0749. FT /FTId=PRO_0000159311. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 121 141 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. FT DOMAIN 185 213 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 210 239 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 194 194 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 197 197 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 200 200 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 204 204 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 219 219 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 222 222 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 225 225 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 229 229 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 246 AA; 28500 MW; 40B6D4918D395F0C CRC64; MDSRVYIIKF DNWGFMVNLM NKIQILRKIS QTLFFVRALI VTGFYLSIVG FIKRFIIGDR ILATIITKII AIVLAFIAGR VFCGWMCPFG FLFNLVYELR VKLFKLKKLP TVDEKIHNKL IYFKYVVLIL VVLAYLSGVK ISGYTLAYLL LALFLVLGFI YPMFFCRYVC PVGSLLSIFA RFSIFKLKLD ENKCVGCRLC ERKCPMQIKI TEKIDQMECI RCFECMSVCK KGALSFSAFT KNTKKE // ID Y763_METJA Reviewed; 121 AA. AC Q58173; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0763; GN OrderedLocusNames=MJ0763; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98759.1; -; Genomic_DNA. DR PIR; C64395; C64395. DR STRING; 243232.MJ_0763; -. DR EnsemblBacteria; AAB98759; AAB98759; MJ_0763. DR KEGG; mja:MJ_0763; -. DR eggNOG; arCOG08263; Archaea. DR eggNOG; ENOG410YX4X; LUCA. DR OMA; IRQATIH; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 121 Uncharacterized protein MJ0763. FT /FTId=PRO_0000107021. SQ SEQUENCE 121 AA; 14411 MW; FE74E2735AA0E393 CRC64; MDEIKEYLAK ILENKIKISM IAKFKSVEEY EGRIFKDLFD VEMKNLEILY EKYLIYFNEK PNIKAEVDTN ADVIEILKET IELEKFLAKK LGVNFGVRQA VIHALSDDER FLYFLTKKPY F // ID Y769_METJA Reviewed; 169 AA. AC Q58179; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0769; GN OrderedLocusNames=MJ0769; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98774.1; -; Genomic_DNA. DR PIR; A64396; A64396. DR ProteinModelPortal; Q58179; -. DR STRING; 243232.MJ_0769; -. DR EnsemblBacteria; AAB98774; AAB98774; MJ_0769. DR KEGG; mja:MJ_0769; -. DR eggNOG; arCOG03352; Archaea. DR eggNOG; ENOG410YQU3; LUCA. DR OMA; KSVYEYM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0000150; F:recombinase activity; IEA:InterPro. DR Gene3D; 1.10.10.60; -; 1. DR InterPro; IPR009057; Homeodomain-like. DR InterPro; IPR006120; Resolvase_HTH_dom. DR Pfam; PF02796; HTH_7; 1. DR SUPFAM; SSF46689; SSF46689; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein MJ0769. FT /FTId=PRO_0000107024. SQ SEQUENCE 169 AA; 20167 MW; C1DEDFB1EF123898 CRC64; MIEIKISKIP RWDEINKIVK LREKDLVLLK LPKSVYEHPK MAYKLEYLKK KGIFIEVENA KRGRKRKVDD ETVKKIHELI IEGYSVREIG NILGIGKSTV WDYAKDCIKE LKLERFKKLV WEYREYLINK GKYSPSLQVL FLELEATVDY DLEKAKKILE DIIKHVKEF // ID Y780_METJA Reviewed; 335 AA. AC Q58190; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0780; GN OrderedLocusNames=MJ0780; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98779.1; -; Genomic_DNA. DR PIR; D64397; D64397. DR STRING; 243232.MJ_0780; -. DR EnsemblBacteria; AAB98779; AAB98779; MJ_0780. DR KEGG; mja:MJ_0780; -. DR eggNOG; arCOG01812; Archaea. DR eggNOG; COG2064; LUCA. DR InParanoid; Q58190; -. DR KO; K07333; -. DR OMA; DYQYAGI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR018076; T2SS_F. DR Pfam; PF00482; T2SSF; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 335 Uncharacterized protein MJ0780. FT /FTId=PRO_0000107031. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 128 148 Helical. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. FT TRANSMEM 310 330 Helical. {ECO:0000255}. SQ SEQUENCE 335 AA; 38139 MW; C6028EDBA1455C08 CRC64; MKGIFEKLKR RIDILLYKLG IRPLSIETLK ELKESRKERE VLEFYDVYME PEEFVDIEKY EFILYEGDIV GKTAESLSKI FKGNLFPSRN ELRYMGVKDE VAYFKKVVIY MIITFLALLF MGLLDNNLLQ GFVNGLIGAG IILVLSLFYP KIRLILFKGE IKLQILFTLI YMISILRAGA SLPEVLESIS KSREYGVVAF EAKSIIRDVN IGGYNLVEAL ERAKMRTRIP ILKKLYDQMI VGYNKGNLPL LLGKLYEDIV RESMVKLDSS KFMIQNLGNL AFGVGLILPF TGMILSTMIG NQGFSGILST INLLLLKIGP LLTLIFGIFV KLKIE // ID Y78A_METJA Reviewed; 81 AA. AC P81312; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 09-DEC-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0782.1; GN OrderedLocusNames=MJ0782.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH886. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98772.1; -; Genomic_DNA. DR ProteinModelPortal; P81312; -. DR STRING; 243232.MJ_0782.1; -. DR PRIDE; P81312; -. DR EnsemblBacteria; AAB98772; AAB98772; MJ_0782.1. DR KEGG; mja:MJ_0782.1; -. DR eggNOG; arCOG02466; Archaea. DR eggNOG; COG3277; LUCA. DR KO; K07569; -. DR OMA; RIIITHK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0001522; P:pseudouridine synthesis; IEA:InterPro. DR GO; GO:0042254; P:ribosome biogenesis; IEA:InterPro. DR InterPro; IPR020321; H/ACA_rnp_Gar1_arc. DR InterPro; IPR009000; Transl_B-barrel. DR ProDom; PD064583; UPF_MJ0782.1/MTH886; 1. DR SUPFAM; SSF50447; SSF50447; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 81 Uncharacterized protein MJ0782.1. FT /FTId=PRO_0000107032. SQ SEQUENCE 81 AA; 9169 MW; 3B1B0ED0220433AC CRC64; MKVEILHKTP KGFLIARGKR EIKIGSVVIF KNKKIGKVVD IFGPVAKPYI KILPINKDIE VSGTAYIKND KSKYKNTEKK N // ID Y800_METJA Reviewed; 415 AA. AC Q58210; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0800; GN OrderedLocusNames=MJ0800; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000305}; CC -!- SUBUNIT: Homodimer. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98795.1; -; Genomic_DNA. DR PIR; H64399; H64399. DR ProteinModelPortal; Q58210; -. DR STRING; 243232.MJ_0800; -. DR PRIDE; Q58210; -. DR EnsemblBacteria; AAB98795; AAB98795; MJ_0800. DR KEGG; mja:MJ_0800; -. DR eggNOG; arCOG02679; Archaea. DR eggNOG; COG1924; LUCA. DR InParanoid; Q58210; -. DR OMA; CIVFGTQ; -. DR PhylomeDB; Q58210; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002731; ATPase_BadF. DR InterPro; IPR008275; CoA_E_activase. DR InterPro; IPR017676; Methan_mark_15. DR Pfam; PF01869; BcrAD_BadFG; 1. DR TIGRFAMs; TIGR00241; CoA_E_activ; 1. DR TIGRFAMs; TIGR03286; methan_mark_15; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 415 Uncharacterized protein MJ0800. FT /FTId=PRO_0000107051. FT METAL 276 276 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000255}. FT METAL 316 316 Iron-sulfur (4Fe-4S); shared with dimeric FT partner. {ECO:0000255}. SQ SEQUENCE 415 AA; 44842 MW; 36365D04F28D28F3 CRC64; MKLMVKIALL TCGAEWSGVY HEIEKAAQKV GGELIFPEVD LSYIDEVEDR LGFKVGSANL KLMFARAMSI IEGNTDAEAV FIATCFRCAE GALVRNEVRK LIQQNTNLPV VMYSFTERTK ASELLTRMEA LTTIVERKSL LARKKQEGIS LGIDSGSTTT KAVVMIDDEV AGTGWIYTKD VIESAKEAVN NALKEAGISL DQVETIGTTG YGRYTVGEYF KADLIQEELT VNSKGAAYLA DKQEGEATVI DIGGMDNKAI SLYDAIPDGF TMGGICAGAS GRFFEITARR LGVSLQELGE LAAKGDWRKI KMNSYCIVFG IQDLVTALAE GAKAEDVAAA AAHSVAEQVF EQQLQEVDVR DPVILVGGSS LLKGLVIAME EVLGRKIIVP RYSQLIGAVG AALLSSGYRY KKMKA // ID Y801_METJA Reviewed; 379 AA. AC Q58211; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Uncharacterized ATP-binding protein MJ0801; GN OrderedLocusNames=MJ0801; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98799.1; -; Genomic_DNA. DR PIR; A64400; A64400. DR ProteinModelPortal; Q58211; -. DR SMR; Q58211; 279-379. DR STRING; 243232.MJ_0801; -. DR EnsemblBacteria; AAB98799; AAB98799; MJ_0801. DR KEGG; mja:MJ_0801; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q58211; -. DR KO; K06921; -. DR OMA; FERIDYE; -. DR PhylomeDB; Q58211; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 379 Uncharacterized ATP-binding protein FT MJ0801. FT /FTId=PRO_0000184671. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 379 AA; 44716 MW; 1BAF2567E0C5D0B4 CRC64; MKFFDREREI NEILHILNRE PDDIYFIYGP LNSGKTALIK HIIENKLSDD YKVFYINFRT YLISEKREFI EAIFTTKKDD FFEKIKDKDE VLNLITKGVR ILTGIPIPEV EFDKLFEEKI NDAFQYLNSL LLEVKKSGKK PILIFDELQM IKDVVLNTEN QRFSAFPSLR FGNGQKYLLK ELFQFLVSLT KEQHLCHVFC LSSDSLFIEY VYSTGELEGR AKYLLVDDFD KETALKFMDF LAVENNINLT NEDKELIYSY VGGKPKDIKY VVEESKFKDL REILEFMLKD AVQKLDMFLD MLNYSKPKVD VGDEVIEIKK DNVIEALKLF KDEYEVSKKH IPVPVYTYLI KRNILFLNPI EGILKPQSYL VWNAIKRLL // ID Y823_METJA Reviewed; 257 AA. AC Q58233; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized ATP-binding protein MJ0823; GN OrderedLocusNames=MJ0823; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0084 and MJ0685. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98822.1; -; Genomic_DNA. DR PIR; G64402; G64402. DR ProteinModelPortal; Q58233; -. DR STRING; 243232.MJ_0823; -. DR EnsemblBacteria; AAB98822; AAB98822; MJ_0823. DR KEGG; mja:MJ_0823; -. DR eggNOG; arCOG00587; Archaea. DR eggNOG; COG3640; LUCA. DR InParanoid; Q58233; -. DR KO; K07321; -. DR OMA; ADMKREP; -. DR PhylomeDB; Q58233; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR014433; CooC. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF005647; CooC; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 257 Uncharacterized ATP-binding protein FT MJ0823. FT /FTId=PRO_0000107063. FT NP_BIND 7 14 ATP. {ECO:0000255}. SQ SEQUENCE 257 AA; 28541 MW; 73D265E67852C685 CRC64; MKIAITGKGG VGKTFIASTL MRLFEKNGFK VIGVDCDPNP TLALAFGVEE EIVPLSKRHD IIEERTGAKP GTYGNIFKIN PKVDDLIDKV GYKIGNITLL VMGTIEEGGE GCVCPASVLL RRLLRHLILK RDEVVILDME AGIEHFGRKT IDTVDLMLIV IEPTKKSLIT AKRMKKLAND LGIKNLGVIV NKVRNEDKEL LKDIIKEELG LEVLGFVPYD EEVIKSEFLG KPINLDSKAA KEIEKIFNYI IKLKNTT // ID Y832_METJA Reviewed; 1750 AA. AC Q58242; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 16-MAR-2016, entry version 107. DE RecName: Full=Uncharacterized protein MJ0832; DE Contains: DE RecName: Full=Mja rnr-1 intein; DE Contains: DE RecName: Full=Mja rnr-2 intein; GN OrderedLocusNames=MJ0832; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-cone domain. {ECO:0000255|PROSITE- CC ProRule:PRU00492}. CC -!- SIMILARITY: Contains 2 DOD-type homing endonuclease domains. CC {ECO:0000255|PROSITE-ProRule:PRU00273}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98834.1; -; Genomic_DNA. DR PIR; H64403; H64403. DR ProteinModelPortal; Q58242; -. DR STRING; 243232.MJ_0832; -. DR MEROPS; N10.007; -. DR EnsemblBacteria; AAB98834; AAB98834; MJ_0832. DR KEGG; mja:MJ_0832; -. DR eggNOG; arCOG03145; Archaea. DR eggNOG; arCOG03154; Archaea. DR eggNOG; arCOG03714; Archaea. DR eggNOG; arCOG04889; Archaea. DR eggNOG; COG1328; LUCA. DR eggNOG; COG1372; LUCA. DR eggNOG; ENOG4111WGK; LUCA. DR InParanoid; Q58242; -. DR KO; K00527; -. DR OMA; RQNDIPE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro. DR GO; GO:0008998; F:ribonucleoside-triphosphate reductase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 3. DR Gene3D; 3.10.28.10; -; 3. DR InterPro; IPR005144; ATP-cone_dom. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR027434; Homing_endonucl. DR InterPro; IPR006142; INTEIN. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR004042; Intein_endonuc. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR004860; LAGLIDADG_2. DR InterPro; IPR012833; NrdD. DR Pfam; PF03477; ATP-cone; 2. DR Pfam; PF14528; LAGLIDADG_3; 2. DR Pfam; PF13597; NRDD; 3. DR PRINTS; PR00379; INTEIN. DR SMART; SM00305; HintC; 2. DR SMART; SM00306; HintN; 2. DR SUPFAM; SSF51294; SSF51294; 4. DR SUPFAM; SSF55608; SSF55608; 3. DR TIGRFAMs; TIGR01443; intein_Cterm; 2. DR TIGRFAMs; TIGR01445; intein_Nterm; 2. DR PROSITE; PS51161; ATP_CONE; 1. DR PROSITE; PS50818; INTEIN_C_TER; 2. DR PROSITE; PS50819; INTEIN_ENDONUCLEASE; 2. DR PROSITE; PS50817; INTEIN_N_TER; 2. PE 3: Inferred from homology; KW ATP-binding; Autocatalytic cleavage; Complete proteome; KW Nucleotide-binding; Protein splicing; Reference proteome; Repeat. FT CHAIN 1 337 Uncharacterized protein MJ0832, 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000013999. FT CHAIN 338 790 Mja rnr-1 intein. {ECO:0000255}. FT /FTId=PRO_0000014000. FT CHAIN 791 1058 Uncharacterized protein MJ0832, 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000014001. FT CHAIN 1059 1591 Mja rnr-2 intein. {ECO:0000255}. FT /FTId=PRO_0000014002. FT CHAIN 1592 1750 Uncharacterized protein MJ0832, 3rd part. FT {ECO:0000255}. FT /FTId=PRO_0000014003. FT DOMAIN 14 101 ATP-cone. {ECO:0000255|PROSITE- FT ProRule:PRU00492}. FT DOMAIN 507 634 DOD-type homing endonuclease 1. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. FT DOMAIN 1286 1426 DOD-type homing endonuclease 2. FT {ECO:0000255|PROSITE-ProRule:PRU00273}. SQ SEQUENCE 1750 AA; 203281 MW; 6D6893B770A25359 CRC64; MISAKDFAEK VMEFYVIKRD KRKEKFNVNK LAKSLINSGV NYGDLDTIIS EVCAKVYNGI TTDELKDIVY NVLKKIDKDV AENYRNGIIL KVRTSEKEFE SFDKEKIAKA LIRETGADEE TARKIADEVE RELKKLKVKY LTAPMIREIV NYKLIEYGFE ELRHKHTRLG MPVYDITKLI KSGSRENANL MYNPESIHKW VADETMKQYA LLAIFPKHIA DAHIKGDIHL HDLEYAATRP VCLQHDLRPF FKYGLKVDGT GLHTSVSKPA KHPEVAIQHA AKVMMAAQTN MSGGQSIDEF NVWLAPYVRG LSYEKIKQLM QMFIYELNQM YVARGGQSLG RDELIFIKEG DKLKVCKIGE AIDEFMEKYK DKIIVDGDTE ILYLDGIAEV YTISVNVKTG KAEFKRVYAI SRHKPRGKVY KVIGKDGTSI IVTEDHSLFN YDENGNLVCV KPRQMKHIIR NFNNPYDVEY RIGDYIETNY QRTDSKYNSR QNDIPEKLKI TKELCQFLGL FVAEGSYITN GISITTKDDD IAKFIERFVK EQINENIAVK RYEDSVRFVN KGFYRFLKEH INGKAINKNS PEFILKGDKE MKLAFLGGLI SGDGYVSKDG RVQIYTTSEQ LLGQLHLLLS DLGMIYSITK IKEEGEKIEI KRNEIVRNYK LYVIEIAKNC TEDLKPYVIP KYKKERIKPA NYDQLPYDYR IIKEHLRKIT DKKPYNDYAW KSNNRKLKLN TLEKIEQLNP HLREEINKFK LNIPFEIKEI KEIDYNGYVY DLSVEDNENF ITATGILCHN TIFSSINLEL EIPEFLKDKP AVIAGTTRGT YGDYEEEAKL ILEALVDVMM EGDAMGKPFL FPNFIIKLRE NAFKDENKEL MYKIHQLSAK FGIPYFINML PDWQVTNTNA MGCRTRLSGN WTGDAEIDTL RTGNMQWYSL NLPRIAYEAN GDDTKLFEIL HERLEILKEA LLIKHEVTKE RLYVDNLMPF LTQEFDGESY YRYENTTKTF GFVGLNEMLK YHLGEELHES KDAVKFGEKV IEYIREYADK LKEETGLRWT VTQTPAESSL PYDEKILIFE NNEYKLVKIG EFVEKYLNRY KDRAITYGDN NIEVYIKDEN IYAPSFDKDG KIVLKPITHA IRHRGKEIYE IELESGKKVR VTGDHSVFTI NDNLDVVEVK ASDLKVGDFI ITPKIIPSIS KDKIYLSEIV KNKDKYYVKI KDHIKFIEEH EEILKESYKE YKTKWKDLKP VLKKKNAFRL DLIEDLVDKE KIEKISYGHA NYINNKIKLD EKFGYLIGAF LSEGHWNDKC VEISSTNKEF IENLVEIIEE ILGKDAYYIT VKGDKRRYKD LYVIGLNKTV AMIFESLGLN KLSSNKEIPS ILLSNETFLK GLIKGYIDGD GSIYVDESKR DYSIRLYTTS ETLRDTLCLA LKILGINYRL SIDKKSKVNE NWRDCYVIKI TGKENIEKLL DVEIKNNGGK DVIPKIAEKF KEIINQYSQR EWKERFGIDV NNLHIWEDLK KGYMSRYRAK KVLNIMKNVK EIEEKYGRLL DKIGQLIDND LLFERIKSIR VLDEIPEYVY DISVEGTENF IGGEGFICLH NTAGRFARLD YKYYKEETIS VVRGDLNDVD SLYYTNSSHV RVDAPITLGE KVRIEEKFHP LCNGGHIMHI WNIESAADPE VLMDITKKIT KTHIGFWTYT KNLSVCNRCG ISMGGLRDRC INCGSEDVAK FSRITGYLQN ISNWNRAKQK ELEDRKLPRI // ID Y83B_METJA Reviewed; 130 AA. AC P81323; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=UPF0333 protein MJ0835.1; GN OrderedLocusNames=MJ0835.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0333 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98841.1; -; Genomic_DNA. DR ProteinModelPortal; P81323; -. DR STRING; 243232.MJ_0835.1; -. DR EnsemblBacteria; AAB98841; AAB98841; MJ_0835.1. DR KEGG; mja:MJ_0835.1; -. DR eggNOG; arCOG05055; Archaea. DR eggNOG; COG1991; LUCA. DR OMA; FEFSIIV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR Pfam; PF04021; Class_IIIsignal; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 130 UPF0333 protein MJ0835.1. FT /FTId=PRO_0000218267. FT TRANSMEM 20 40 Helical. {ECO:0000255}. SQ SEQUENCE 130 AA; 14578 MW; 212874E92CA64C33 CRC64; MNTMENKIIK SKKAQVSLEF SFLFLAILLA SIITISHFLS QNFTKDDKVI SDVENAAKTA VILANSGYNG INPNVTLIYG GISWSGNKKN IYIYISPKSY ITPEIKNFIV SYIYNVTKIN QSEYNITVNP // ID Y865_METJA Reviewed; 449 AA. AC Q58275; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Putative methylthiotransferase MJ0865; DE EC=2.-.-.-; GN OrderedLocusNames=MJ0865; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250}; CC -!- SIMILARITY: Belongs to the methylthiotransferase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98870.1; -; Genomic_DNA. DR PIR; A64408; A64408. DR ProteinModelPortal; Q58275; -. DR STRING; 243232.MJ_0865; -. DR EnsemblBacteria; AAB98870; AAB98870; MJ_0865. DR KEGG; mja:MJ_0865; -. DR eggNOG; arCOG01356; Archaea. DR eggNOG; COG1032; LUCA. DR InParanoid; Q58275; -. DR OMA; THRGCLG; -. DR PhylomeDB; Q58275; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0031419; F:cobalamin binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR023979; CHP04014_B12-bd/rSAM. DR InterPro; IPR006158; Cobalamin-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR020612; Methylthiotransferase_CS. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF02310; B12-binding; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR04014; B12_SAM_MJ_0865; 1. DR PROSITE; PS01278; MTTASE_RADICAL; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 449 Putative methylthiotransferase MJ0865. FT /FTId=PRO_0000141759. FT METAL 177 177 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 181 181 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. FT METAL 184 184 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255|PROSITE-ProRule:PRU00780}. SQ SEQUENCE 449 AA; 50957 MW; 6A97907DAF81DBB6 CRC64; MNKIKEGANV RITIYSPEVY TYGAMLIGGI LKHKGYNVHL VRKIDKTLFL KSDVIIFSLY STLHILDKNI REAIDFIKKV RKNKTKVYVA GCVSTYPEII LNELNVDGVI VGEGEITTPK IIEGDKEGLA YKEGDEIVIN YPKEKPDLNH PLPLIPKDIE QQSIRGANVY IETHRGCLGN CTFCQVPKFF GKTIRSRDVE DVVEEVKAFK RAGAKRIAIS GGTGSLYAFK KSINRDKFFE LLEKVSEVIG KNNLSVPDMR VDYVDEEILE AIKNYTIGWV FYGIESGSDK ILKDMKKGTN REKNLDAIKL AKDCGVKVAG SFIVAYPTET EMDYLLTKDF IVDAELDDVF VSIAEPIPTT ELCDLVLSMP KEENLLYKMH EGEYRKLGLS EAEARCFDLL IHAEMWKSMP KPLTPQLYNL YLNEARIQGK DIRAITDLLF KYRDLLLKK // ID Y873_METJA Reviewed; 290 AA. AC Q58283; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 4. DT 11-NOV-2015, entry version 89. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0873; GN OrderedLocusNames=MJ0873; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98878.1; -; Genomic_DNA. DR PIR; A64409; A64409. DR ProteinModelPortal; Q58283; -. DR STRING; 243232.MJ_0873; -. DR EnsemblBacteria; AAB98878; AAB98878; MJ_0873. DR KEGG; mja:MJ_0873; -. DR eggNOG; arCOG00198; Archaea. DR eggNOG; COG1120; LUCA. DR InParanoid; Q58283; -. DR KO; K02013; -. DR OMA; HKIELTL; -. DR PhylomeDB; Q58283; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 290 Uncharacterized ABC transporter ATP- FT binding protein MJ0873. FT /FTId=PRO_0000093222. FT DOMAIN 2 238 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 34 41 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 290 AA; 32550 MW; 01388AC7D21D153D CRC64; MLKTENLSVG YGNYVVVEGI NLEINRGEIL CIIGPNGAGK STLLKTIATY LKPKKGVVYL NGKKIHDLKP KDLAKEMAVV LTERVNPGNM TGFDVVAIGR HPYTDLFGRL TERDKKIIIE SARAVNAEYL LEKNFFEMSD GERQKIMIAR ALAQEPKVLI LDEPTSFLDA KHKIELTLLL RKLADEKNLA IVVTLHDIEL ALRIADKMAL IKNHKVIAYG YPENVMKREI VNELYDLKNA NYSEVIGYFE LKNNPIKNKK IFVICGGGTG ANVLRYLVKN RYDVVVGHLA // ID Y874_METJA Reviewed; 93 AA. AC Q58284; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0874; GN OrderedLocusNames=MJ0874; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To B.subtilis YdcN C-terminal region. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98881.1; -; Genomic_DNA. DR PIR; B64409; B64409. DR STRING; 243232.MJ_0874; -. DR DNASU; 1451763; -. DR EnsemblBacteria; AAB98881; AAB98881; MJ_0874. DR KEGG; mja:MJ_0874; -. DR eggNOG; arCOG00199; Archaea. DR eggNOG; COG1120; LUCA. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020322; Uncharacterised_MJ0874. DR ProDom; PD064925; Uncharacterised_MJ0874; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 93 Uncharacterized protein MJ0874. FT /FTId=PRO_0000107087. SQ SEQUENCE 93 AA; 10860 MW; 07603737C0CC494D CRC64; MMLLLAILHK NDADYFIAEA MGVKIIEEEA YKKISKETFE EALKELKNSD VVVYTDFPIG EMNELNLKLI EEAKNLKKRM IFYEDDISVL KEI // ID Y875_METJA Reviewed; 748 AA. AC Q58285; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0875; GN OrderedLocusNames=MJ0875; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98882.1; -; Genomic_DNA. DR PIR; C64409; C64409. DR ProteinModelPortal; Q58285; -. DR STRING; 243232.MJ_0875; -. DR EnsemblBacteria; AAB98882; AAB98882; MJ_0875. DR KEGG; mja:MJ_0875; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 748 Uncharacterized protein MJ0875. FT /FTId=PRO_0000107088. SQ SEQUENCE 748 AA; 90732 MW; 5515ED3B541562EA CRC64; MDSNILNIRE LRKQAVNLEK EAKKEKQNGN YKKSAELFLK ASEIYNKIRD EKNKKWTLAN YYSIMAKEYS FSNEFDKARE FYKKAEELFL ELGIKKSAMY CFYYYLKTYI YEEKEKVEKK DNDKYLELLN KYIIEAEQFL EKYKEFSDIW MYFDIKIYYY KKLSIKHRKF EGNLDKAIEL TEKCYKLAEE SYNKFNDKNY KKAEIFNKHF YYNLMAQKFE SERKFKEAAE YYKKSGDTIK EIDEKIAYDE YANSYKWLAI ENKYNKEKFE EYINKAIEFS EKRGDKLQEY YYLGLKYDHL VRFANDLEEK IDYIKKSKEY YYRSKSFEFA KYMEYLEYYY QFKYELLNGN YEKALNFLQK AKKSLKNVKI SNIIFSKYTL ECDELICRFY LSISQGEFKK SVELLDEYLE ISLKILSDWK NTRKYKFYEY LKPCVEILSK ESFTKDDLFL LEDVILEVRN EKISLNLYKI CSLTYAYVSL WKNKIRDKEI LEKIKLKIIK QITTEDVSKD LENRIKIQMA IERNDWLLRL PPALVENFDN CIYFLEEVLD EFKHAAYREF YRLLENYLKI IVEFNAMALW GDTWKQILEE KISNRKKPFE IFTFGDFAQS LRLLKNEGCE YCKNIDDEIF DLLDKHVKIR NNLSHDFNAK APEDIDIKGD TLKIIYSTLN AFPICVKVTH DKKKPWYGVE VIWNQLPKKM SLYSNTELKK GCLYYIEPYS NILDKNKMHP KIIIPIEVSK DIVYPNKN // ID Y910_METJA Reviewed; 174 AA. AC Q58320; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0910; GN OrderedLocusNames=MJ0910; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98912.1; -; Genomic_DNA. DR PIR; F64413; F64413. DR ProteinModelPortal; Q58320; -. DR STRING; 243232.MJ_0910; -. DR EnsemblBacteria; AAB98912; AAB98912; MJ_0910. DR KEGG; mja:MJ_0910; -. DR eggNOG; arCOG06472; Archaea. DR eggNOG; COG1240; LUCA. DR KO; K03404; -. DR OMA; NISTHIM; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR002035; VWF_A. DR Pfam; PF13519; VWA_2; 1. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF53300; SSF53300; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 174 Uncharacterized protein MJ0910. FT /FTId=PRO_0000107100. SQ SEQUENCE 174 AA; 19707 MW; A28670E3FF18042A CRC64; MGAMRRMEAA KGAIISLLLD AYQKRNKIGM IAFRKDKAEL ILPFTSSVEL GEKLLKDLPT GGKTPLADAF IKSYEVFDRE IRKNPNIIPI MIVISDFKPN VAVKEDYVKE VFDACEKIAE KGINVILIDT EPQSFIKIGI GKEIANRFGF KYYKIEELSK DKILDICKSL EINF // ID Y916_METJA Reviewed; 89 AA. AC Q58326; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0916; GN OrderedLocusNames=MJ0916; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98921.1; -; Genomic_DNA. DR PIR; D64414; D64414. DR ProteinModelPortal; Q58326; -. DR STRING; 243232.MJ_0916; -. DR EnsemblBacteria; AAB98921; AAB98921; MJ_0916. DR KEGG; mja:MJ_0916; -. DR eggNOG; arCOG02155; Archaea. DR eggNOG; COG1873; LUCA. DR InParanoid; Q58326; -. DR OMA; PFNLITA; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR027275; PRC-brl_dom. DR InterPro; IPR011033; PRC_barrel-like. DR Pfam; PF05239; PRC; 1. DR SUPFAM; SSF50346; SSF50346; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 89 Uncharacterized protein MJ0916. FT /FTId=PRO_0000107103. SQ SEQUENCE 89 AA; 9673 MW; ADA40C45D1D858F9 CRC64; MAIRVSDILD KPIYTTTAIY VGKVYDVMLD LNKGVISGLI VSDIQNGCLK DYVTDPSKKV VLPFNLITAI GNIILVKPPA DSGYGFLKK // ID Y925_METJA Reviewed; 106 AA. AC Q58335; DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 80. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0925; GN OrderedLocusNames=MJ0925; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH hxlR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00435}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98937.1; -; Genomic_DNA. DR PIR; E64415; E64415. DR ProteinModelPortal; Q58335; -. DR STRING; 243232.MJ_0925; -. DR EnsemblBacteria; AAB98937; AAB98937; MJ_0925. DR KEGG; mja:MJ_0925; -. DR eggNOG; arCOG01057; Archaea. DR eggNOG; COG1733; LUCA. DR InParanoid; Q58335; -. DR OMA; AKIPKII; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR002577; HTH_HxlR. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01638; HxlR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR PROSITE; PS51118; HTH_HXLR; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 106 Uncharacterized HTH-type transcriptional FT regulator MJ0925. FT /FTId=PRO_0000148893. FT DOMAIN 1 93 HTH hxlR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00435}. SQ SEQUENCE 106 AA; 12115 MW; 09ADFAF2CA628223 CRC64; MSIFYVLGKK GTIEILYKIK EGVNSFTSIK NALDMEGCGV STRTLAERLN ELEDENLIQK DGSKYYLTKK GQEALEIIEN VMKWEAKWKE AKIPKIIIGM LGDKER // ID Y939_METJA Reviewed; 276 AA. AC Q58349; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0939; GN OrderedLocusNames=MJ0939; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98946.1; -; Genomic_DNA. DR PIR; C64417; C64417. DR ProteinModelPortal; Q58349; -. DR STRING; 243232.MJ_0939; -. DR EnsemblBacteria; AAB98946; AAB98946; MJ_0939. DR KEGG; mja:MJ_0939; -. DR eggNOG; arCOG05059; Archaea. DR eggNOG; COG0727; LUCA. DR KO; K06940; -. DR OMA; FMVKWNG; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR005358; Puta_zinc/iron-chelating_dom. DR Pfam; PF03692; CxxCxxCC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 276 Uncharacterized protein MJ0939. FT /FTId=PRO_0000107113. SQ SEQUENCE 276 AA; 33454 MW; 97BD69D392BC8FDF CRC64; MMPMDWEITF KGITYECINC AYCCSCKGWR IYLNYFDRLK LKDYEYAIEP CEGEFKYRLK VNEKGCVLLN NNLCRIHLEK GYEFKPLMCM IFPFSCMIKW DGTPLLIIKH YCSGIKKGKI SKKVVNEAIE LIKELYFDMF EEIIENGMEH SSKTEIFENF RVDWEEREDF GRYIFSSKTF DEMFERCREI FGNKINKLNL EEIDEIKNNL QRYNTKENEE EILRYLLELN RREHFRKLPF YREVNKLINI GNYLTKYKNV FKGEGEVDKK LFLNLK // ID Y954_METJA Reviewed; 440 AA. AC Q58364; DT 11-JUL-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0954; DE Flags: Precursor; GN OrderedLocusNames=MJ0954; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the Mj S-layer protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98959.1; -; Genomic_DNA. DR PIR; B64419; B64419. DR ProteinModelPortal; Q58364; -. DR STRING; 243232.MJ_0954; -. DR EnsemblBacteria; AAB98959; AAB98959; MJ_0954. DR KEGG; mja:MJ_0954; -. DR eggNOG; arCOG03420; Archaea. DR eggNOG; ENOG410YANH; LUCA. DR OMA; TKACVLA; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR022651; S_layer_C. DR Pfam; PF05124; S_layer_C; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 29 {ECO:0000255}. FT CHAIN 30 440 Uncharacterized protein MJ0954. FT /FTId=PRO_0000032622. SQ SEQUENCE 440 AA; 50745 MW; 22988D6DD2534A84 CRC64; MLRLQMMEGL IVKRTLLLIL LLVISVSYAL PIEPIIYVNK STVDYQNAKI LMDNFYSSRE ININGDNVTI VINDIMYIPS IDELEIKNGD KNLIIKFDRD GNKVKYKDIE CIEYLNLKKG EEISLFNKSY IVEDITSNYV ILKEKDGKEV LTNESFEYDG YKVVVKLVSS DLNTIIVDIY KNEKVLDSPK LTKGKIYYMK GGTLGLMYEN CTRIGKGYRF TFRVYSTIKI EEGEDYPLDK EFKVKEISTD KIKLEYKNID SLGNEIYLFN YTIIPEKCYK DYVLFKVIKR KEKTVDVKDV AYIGDGIYAV KVNNTVHVFY KGKELKNHEK IYLGSVDVYS SNPLNVNKDI ILIGGPKVNK IVKELEDKGL LKVNISTNYP GNNRGIILKI KNPYNDNNIY ILAGSDRWGT KAAILVFLTK YNDEDTLMVE WDKGEIKIIK // ID Y966_METJA Reviewed; 444 AA. AC Q58376; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 86. DE RecName: Full=Uncharacterized protein MJ0966; GN OrderedLocusNames=MJ0966; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98968.1; -; Genomic_DNA. DR PIR; F64420; F64420. DR ProteinModelPortal; Q58376; -. DR STRING; 243232.MJ_0966; -. DR EnsemblBacteria; AAB98968; AAB98968; MJ_0966. DR KEGG; mja:MJ_0966; -. DR eggNOG; arCOG01355; Archaea. DR eggNOG; COG1032; LUCA. DR InParanoid; Q58376; -. DR OMA; CGRESAD; -. DR PhylomeDB; Q58376; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0035596; F:methylthiotransferase activity; IBA:GO_Central. DR GO; GO:0035600; P:tRNA methylthiolation; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR023970; MeThioTfrase/rSAM. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR PANTHER; PTHR11918; PTHR11918; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 444 Uncharacterized protein MJ0966. FT /FTId=PRO_0000107122. FT METAL 178 178 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 182 182 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 185 185 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 444 AA; 51348 MW; 25ABAB5890A20C70 CRC64; MIKMIKNVAI IYPNKFKAGI SCLAVHVLAN HLSKYRDLNV GVYFLENYDR IKNFDAIFIT LQYENDYFNA IKIIKDLRKN NPNAIFVAGG PCVMENFFPI AEFFDVFIVG EIEGSDVMLK VINREFDVEG VYSKYLEKDK VKRIYPKKLT IDDYPIYQPT SEEGAYGKSF LLEIGRGCPR RCRFCLARAI YYPPRFRKLD DLMYLAEEGV KVNKVNKVAL IAPSVGDYKY IVELCNFLDD MGVHISPSSL RADTLNDDLM RILKPKTLTI APEAGSERLR EFIKKDIRER DIANAIDLAK KFGVEKVKLY FMVGIPTETD EDIEELINLT KKVKKEIRKV EISVNPMIPK PHTDFEVEEF DLSSKKKIKY IEKALKKEGI RVEYENFNSM ICQCILARGD ENLSKYLDYS KNPTSLISAL KKDRLLDKYL GRFEDKGVWK NIIL // ID Y972_METJA Reviewed; 228 AA. AC Q58382; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=UPF0056 membrane protein MJ0972; GN OrderedLocusNames=MJ0972; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0056 (MarC) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98977.1; -; Genomic_DNA. DR PIR; D64421; D64421. DR ProteinModelPortal; Q58382; -. DR STRING; 243232.MJ_0972; -. DR EnsemblBacteria; AAB98977; AAB98977; MJ_0972. DR KEGG; mja:MJ_0972; -. DR eggNOG; arCOG01997; Archaea. DR eggNOG; COG2095; LUCA. DR InParanoid; Q58382; -. DR KO; K05595; -. DR OMA; FFIVIGQ; -. DR PhylomeDB; Q58382; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002771; Multi_antbiot-R_MarC. DR Pfam; PF01914; MarC; 1. DR TIGRFAMs; TIGR00427; TIGR00427; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 228 UPF0056 membrane protein MJ0972. FT /FTId=PRO_0000156917. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. SQ SEQUENCE 228 AA; 25360 MW; D259B7E8C5F38D6E CRC64; MVGYSGEHFI FNVVKYMDIL NFYIYGFVSL FITIDPIGLI PIVHSLTYPY PKEQRIRIIK KAIISSTVVL LLFALFGNYI FGYFGITIDA FRVAGGILLF KIAWDMLHAE IPKTKHKPDE RLDLEDIDSI VYVPLAIPLI SGPGAITTTM ILISKTQSIL EKGVVVLSIL SAMLVSGIIL SLTDFIIRRV NIYGINAFVR IMGLLLVAIS VQIIFTGIVG LYNSISVQ // ID Y973_METJA Reviewed; 411 AA. AC Q58383; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0973; GN OrderedLocusNames=MJ0973; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: In the C-terminal section; belongs to the PAPS CC reductase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98978.1; -; Genomic_DNA. DR PIR; E64421; E64421. DR ProteinModelPortal; Q58383; -. DR STRING; 243232.MJ_0973; -. DR PRIDE; Q58383; -. DR EnsemblBacteria; AAB98978; AAB98978; MJ_0973. DR KEGG; mja:MJ_0973; -. DR eggNOG; arCOG00074; Archaea. DR eggNOG; COG0175; LUCA. DR InParanoid; Q58383; -. DR OMA; ECIGILE; -. DR PhylomeDB; Q58383; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR002500; PAPS_reduct. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR Pfam; PF01507; PAPS_reduct; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 411 Uncharacterized protein MJ0973. FT /FTId=PRO_0000100694. SQ SEQUENCE 411 AA; 48904 MW; E823355794A38F94 CRC64; MDDKFASKFE IDVLNKLLNK NFSYDLAIIL KKIGGLDYRK KVFINGECIG ILEFDLIDLD WKFHPYASYY LIEEPKIKIK PTKRKLKGKK VPVDLIENAE ELKDINENDY VGVEVGNYVG VAVKKGDTIK IKDLTLKKEL RFEKIEDYLR KNKDRIEKLE KKSLSIIKKY YEMCKNKNYA INTSFSGGKD SSVSTLLANK VIDDLEVIFI DTGLEFKDTI DFVKKFAKKY DLNLVVLKGK NFWEYLEKEG IPTKDYRWCN SVCKLEPLKE YLKKYKRVYT IDGSRRYESF TREKLTYERK SGFIENQINI FPILDWRGTD VWSWIYLNDV IYNELYDKGF ERIGCYMCPA ALNAEFLRVK ELYPELFNKW VDVLKRFGYD EDEILRGFWR WKELPPKMKE LKKILENKEK K // ID Y988_METJA Reviewed; 329 AA. AC Q58395; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=Uncharacterized protein MJ0988; GN OrderedLocusNames=MJ0988; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98990.1; -; Genomic_DNA. DR PIR; D64423; D64423. DR ProteinModelPortal; Q58395; -. DR STRING; 243232.MJ_0988; -. DR EnsemblBacteria; AAB98990; AAB98990; MJ_0988. DR KEGG; mja:MJ_0988; -. DR eggNOG; arCOG01565; Archaea. DR eggNOG; COG0618; LUCA. DR InParanoid; Q58395; -. DR OMA; SSHEASC; -. DR PhylomeDB; Q58395; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0004309; F:exopolyphosphatase activity; IBA:GO_Central. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0006798; P:polyphosphate catabolic process; IBA:GO_Central. DR InterPro; IPR001667; DDH_dom. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF01368; DHH; 1. DR Pfam; PF02272; DHHA1; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 329 Uncharacterized protein MJ0988. FT /FTId=PRO_0000107131. SQ SEQUENCE 329 AA; 37316 MW; 7AE87D2F92E535E4 CRC64; MELLEYLKRD EVLFLCHHNA DPDAVGSCVA LKYLASQLNP NGKFRISADS VSKLSRNILN EIGERVDIEI YPKLPETVFI VDTASINQLK VNFDELKERE VILIDHHKKT DLADICKYYI IKEDYPSTSE IIAEIFKELN IFPPKNVRIA LLCGIVYDTK HLKLANSKTF ELISYLIKDI SFQKILYLLS QESDVSKRTA HLKACSRMEI REFDKLRIAL SHVSSHEASC AKTIVSIGAD VAFVVAVRKK EKEIRVSARC RKHVSKYVHL GNLMEKIGKE LGGSGGGHSE AGGLNAPYDK SKSKEKVIKE VLNLCYKRFV EEYKKAKQN // ID Y181_METJA Reviewed; 246 AA. AC Q57640; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0181; GN OrderedLocusNames=MJ0181; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98178.1; -; Genomic_DNA. DR PIR; F64322; F64322. DR ProteinModelPortal; Q57640; -. DR STRING; 243232.MJ_0181; -. DR PRIDE; Q57640; -. DR EnsemblBacteria; AAB98178; AAB98178; MJ_0181. DR KEGG; mja:MJ_0181; -. DR eggNOG; ENOG410Z4CS; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 246 Uncharacterized protein MJ0181. FT /FTId=PRO_0000106730. SQ SEQUENCE 246 AA; 30120 MW; 3EA28EBF3FCE8790 CRC64; MEKIFNISFS MPKSYELKDF IKQYDFFNDD KIAEKLERFF KAINFTNPRH LKKVLNKYAI LIEFKNSKID NERLIPEIIR IENGERKRKG YLFDTVFVLY FIILYEFYYG KYLEVKRYKC RLQTNTGLQS YFERYSLLSQ IMKVIKNRNA NDMDRVITNL MLLYSQLGYR YNYEIKGRKF YKLVINREIR DKDYNIANEL SIELKEAGIT VDFWEYIKNN YEDLIEENYP NPYPFTNLFK MVETYL // ID Y182_METJA Reviewed; 194 AA. AC Q57641; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0182; GN OrderedLocusNames=MJ0182; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98179.1; -; Genomic_DNA. DR PIR; G64322; G64322. DR ProteinModelPortal; Q57641; -. DR STRING; 243232.MJ_0182; -. DR EnsemblBacteria; AAB98179; AAB98179; MJ_0182. DR KEGG; mja:MJ_0182; -. DR eggNOG; arCOG010127; Archaea. DR eggNOG; COG4928; LUCA. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR011646; KAP_P-loop. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07693; KAP_NTPase; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 194 Uncharacterized protein MJ0182. FT /FTId=PRO_0000106731. SQ SEQUENCE 194 AA; 22208 MW; 846E28002862EAF9 CRC64; MSKLDKNEFI CLKFDAWLYE KDDNLPYSLL EFIWDELEAK LNKDETITKE IKDKIKKLGK KSVNLWKNMV LGAINATNIK AGTSPITELS GIKINASFDG SKFVGYVVNA SKEDENEEES YHKKVKELQN CFKELSKTLA DNGKKLIIFI DELDRCEAEN ILNLLASIKL FFSLGGEDED ENKNDDEIKI LFIL // ID Y201_METJA Reviewed; 160 AA. AC Q57654; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 20-JAN-2016, entry version 69. DE RecName: Full=Uncharacterized protein MJ0201; GN OrderedLocusNames=MJ0201; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98185.1; -; Genomic_DNA. DR PIR; B64325; B64325. DR STRING; 243232.MJ_0201; -. DR DNASU; 1451050; -. DR EnsemblBacteria; AAB98185; AAB98185; MJ_0201. DR KEGG; mja:MJ_0201; -. DR eggNOG; arCOG03118; Archaea. DR eggNOG; COG1238; LUCA. DR InParanoid; Q57654; -. DR OMA; SEPIFQP; -. DR PhylomeDB; Q57654; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR032818; DedA. DR InterPro; IPR032816; SNARE_assoc. DR PANTHER; PTHR30353; PTHR30353; 1. DR Pfam; PF09335; SNARE_assoc; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 160 Uncharacterized protein MJ0201. FT /FTId=PRO_0000106738. SQ SEQUENCE 160 AA; 18626 MW; EDEACBF3DA3B24E2 CRC64; MINLELFKEF LLNLIKDYGY FGIFLVGFSE PIFQPFPTEI FIIAGILLGL DWKLVWLIST IACNFGAVVT YYLAKKYGEK LMLKLFDEEK IKKGSHYLKK WGILGVIIAS FTPIPFEVIC WVCGSFEMPF ERYMIAVFLS RLIRHGMVIL PFVLKDHIHF // ID Y223_METJA Reviewed; 104 AA. AC Q57676; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0223; GN OrderedLocusNames=MJ0223; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98215.1; -; Genomic_DNA. DR PIR; H64327; H64327. DR PDB; 2K6I; NMR; -; A=3-46. DR PDBsum; 2K6I; -. DR ProteinModelPortal; Q57676; -. DR STRING; 243232.MJ_0223; -. DR EnsemblBacteria; AAB98215; AAB98215; MJ_0223. DR KEGG; mja:MJ_0223; -. DR KO; K02107; -. DR OMA; DCIVANE; -. DR EvolutionaryTrace; Q57676; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014275; ATPase_A1A0-cplx_hsu. DR TIGRFAMs; TIGR02926; AhaH; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MJ0223. FT /FTId=PRO_0000106746. FT TURN 6 8 {ECO:0000244|PDB:2K6I}. FT HELIX 14 43 {ECO:0000244|PDB:2K6I}. SQ SEQUENCE 104 AA; 11805 MW; 9BB4DED252DF0732 CRC64; MSVSVMEAIK EVKLAEEQAV KEIEEAKNRA EQIKAEAIEE AKKLIAEAEE EAKKLVEEMI KKAEEEAKKE AEKILEETEK EIKEIISIAK VKILSLKLSE ILEI // ID Y224_METJA Reviewed; 169 AA. AC Q57677; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0224; GN OrderedLocusNames=MJ0224; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98209.1; -; Genomic_DNA. DR PIR; A64328; A64328. DR STRING; 243232.MJ_0224; -. DR EnsemblBacteria; AAB98209; AAB98209; MJ_0224. DR KEGG; mja:MJ_0224; -. DR eggNOG; arCOG04364; Archaea. DR eggNOG; COG1772; LUCA. DR InParanoid; Q57677; -. DR KO; K09725; -. DR OMA; ETCTAIG; -. DR PhylomeDB; Q57677; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007501; DUF531. DR Pfam; PF04407; DUF531; 1. DR PIRSF; PIRSF006006; UCP006006; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein MJ0224. FT /FTId=PRO_0000106747. SQ SEQUENCE 169 AA; 19283 MW; F24320F7DCA02BBF CRC64; MKKLKRLTLI LYNSYDKTRW HEAHKRAIAR AAPICYAFDC NLAIMDFPCK MEDILNIKTT IGNSGEYLEK LIEKNRFFIV DKFLPQFGIP IASTSKPDEK KAITPLDTAY LLKKKPIGVY VGLGRHGLPK DIMESCVYHL DVTEKRVSLE TCTAIGSIPA VIYCYTKYI // ID Y230_METJA Reviewed; 87 AA. AC Q57683; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0230; GN OrderedLocusNames=MJ0230; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98216.1; -; Genomic_DNA. DR PIR; G64328; G64328. DR STRING; 243232.MJ_0230; -. DR EnsemblBacteria; AAB98216; AAB98216; MJ_0230. DR KEGG; mja:MJ_0230; -. DR eggNOG; arCOG05236; Archaea. DR eggNOG; ENOG410Z4AH; LUCA. DR OMA; MIIWIVI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 87 Uncharacterized protein MJ0230. FT /FTId=PRO_0000106751. FT TRANSMEM 29 49 Helical. {ECO:0000255}. SQ SEQUENCE 87 AA; 10070 MW; C4185109EA09D52F CRC64; MFVGEIMPMG FGVHYVGSEG VAINPFYDIL WMIIFVVIIA VIIYILISPL KKQSSSIDNE KLIKIEKDVE EIKEIVKELK KKWEEIE // ID Y253_METJA Reviewed; 154 AA. AC Q57701; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 97. DE RecName: Full=Putative hydrogenase maturation protease MJ0253; DE EC=3.4.23.-; GN OrderedLocusNames=MJ0253; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98240.1; -; Genomic_DNA. DR PIR; F64331; F64331. DR ProteinModelPortal; Q57701; -. DR STRING; 243232.MJ_0253; -. DR EnsemblBacteria; AAB98240; AAB98240; MJ_0253. DR KEGG; mja:MJ_0253; -. DR eggNOG; arCOG04429; Archaea. DR eggNOG; COG0680; LUCA. DR InParanoid; Q57701; -. DR KO; K00442; -. DR OMA; GCGNLIF; -. DR PhylomeDB; Q57701; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 3.40.50.1450; -; 1. DR InterPro; IPR004411; Pept_A31_F420-red_hyd_d. DR InterPro; IPR023430; Pept_HybD-like_dom. DR InterPro; IPR000671; Peptidase_A31. DR Pfam; PF01750; HycI; 1. DR PRINTS; PR00446; HYDRGNUPTAKE. DR SUPFAM; SSF53163; SSF53163; 1. DR TIGRFAMs; TIGR00130; frhD; 1. DR TIGRFAMs; TIGR00072; hydrog_prot; 1. PE 3: Inferred from homology; KW Aspartyl protease; Complete proteome; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 154 Putative hydrogenase maturation protease FT MJ0253. FT /FTId=PRO_0000201948. SQ SEQUENCE 154 AA; 16846 MW; DE03F82A1C91B365 CRC64; MKKKDILIVG CGNLLFGDDG FGCEVVSKLE KMNLPDNVEV IDAGASGAYY LMTLVDEDIK KIIVVDAIDF DLEPGTIKKI DVDELPNIKK YSFDAHNVPL APFLKDLHNK GIEVVVIGCQ GKEFTMPDIK PGLSEEVAKA VDKAIEIILG EIKK // ID Y273_METJA Reviewed; 103 AA. AC Q57721; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0273; GN OrderedLocusNames=MJ0273; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98261.1; -; Genomic_DNA. DR PIR; B64334; B64334. DR ProteinModelPortal; Q57721; -. DR STRING; 243232.MJ_0273; -. DR EnsemblBacteria; AAB98261; AAB98261; MJ_0273. DR KEGG; mja:MJ_0273; -. DR eggNOG; arCOG01224; Archaea. DR eggNOG; COG1849; LUCA. DR InParanoid; Q57721; -. DR KO; K09728; -. DR OMA; ECYFNDA; -. DR PhylomeDB; Q57721; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.1270.90; -; 1. DR InterPro; IPR023140; DUF357. DR Pfam; PF04010; DUF357; 1. DR SUPFAM; SSF158372; SSF158372; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 103 Uncharacterized protein MJ0273. FT /FTId=PRO_0000106765. SQ SEQUENCE 103 AA; 11972 MW; BDE81755780AF7EB CRC64; MMVRNVIKEI TEEKLENYFK RTEEAIKIIK KGMPPKRSLL YDVAKDFLLM IESYFEDAKA FKERGDYVTA FASLNYAYGW IDAGVRLGIF DVGDDDVRFT LAK // ID Y287_METJA Reviewed; 97 AA. AC Q57735; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0287; GN OrderedLocusNames=MJ0287; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98274.1; -; Genomic_DNA. DR PIR; H64335; H64335. DR ProteinModelPortal; Q57735; -. DR STRING; 243232.MJ_0287; -. DR EnsemblBacteria; AAB98274; AAB98274; MJ_0287. DR KEGG; mja:MJ_0287; -. DR eggNOG; arCOG01055; Archaea. DR eggNOG; COG3432; LUCA. DR InParanoid; Q57735; -. DR OMA; RIMYAAN; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ0287. FT /FTId=PRO_0000106774. SQ SEQUENCE 97 AA; 11764 MW; 87120EAF43973F6B CRC64; MRIPPPLSNN KNRNRRYKRS QFEVIFEILH IIKEGEQIKT RIMYAANLDW RNFSKYIDFL ISNGFIKKNK EKFELTELGK KLYSSLYELF EIMNSKP // ID Y290_METJA Reviewed; 211 AA. AC Q57738; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0290; GN OrderedLocusNames=MJ0290; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98283.1; -; Genomic_DNA. DR PIR; C64336; C64336. DR ProteinModelPortal; Q57738; -. DR STRING; 243232.MJ_0290; -. DR EnsemblBacteria; AAB98283; AAB98283; MJ_0290. DR KEGG; mja:MJ_0290; -. DR eggNOG; arCOG01055; Archaea. DR eggNOG; arCOG06652; Archaea. DR eggNOG; COG3432; LUCA. DR OMA; VFRLIYP; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR016024; ARM-type_fold. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF48371; SSF48371; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 211 Uncharacterized protein MJ0290. FT /FTId=PRO_0000106777. SQ SEQUENCE 211 AA; 24620 MW; FB64861E06896025 CRC64; MKCISKQGEI KELIKNGKIN DVLQLIEEDT LLLEEIYGFL KSDDIQLKIT CLAILGNLYL KGKVQITQLI KHLEEVLLEN DKDAILNALL ILKEIPEVYQ EDLLKRIILK YIGKDIKDCE DDKDKSTLPS VKRDKIMIIF EILKAVKNKE LKKTKIMYAA NLDWKTFRNY IGYLLDNEFI RKTDGVYTLT PKGELLLEKI EEVFRLIYPD K // ID Y305_METJA Reviewed; 395 AA. AC Q57753; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 96. DE RecName: Full=Uncharacterized protein MJ0305; GN OrderedLocusNames=MJ0305; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the chloride channel (TC 2.A.49) family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98292.1; -; Genomic_DNA. DR PIR; B64338; B64338. DR ProteinModelPortal; Q57753; -. DR STRING; 243232.MJ_0305; -. DR TCDB; 2.A.49.4.1; the chloride carrier/channel (clc) family. DR EnsemblBacteria; AAB98292; AAB98292; MJ_0305. DR KEGG; mja:MJ_0305; -. DR eggNOG; arCOG02569; Archaea. DR eggNOG; COG0038; LUCA. DR InParanoid; Q57753; -. DR KO; K03281; -. DR OMA; KEGPCVQ; -. DR PhylomeDB; Q57753; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0034707; C:chloride channel complex; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005247; F:voltage-gated chloride channel activity; IEA:InterPro. DR Gene3D; 1.10.3080.10; -; 1. DR InterPro; IPR014743; Cl-channel_core. DR InterPro; IPR001807; Cl-channel_volt-gated. DR Pfam; PF00654; Voltage_CLC; 1. DR PRINTS; PR00762; CLCHANNEL. DR SUPFAM; SSF81340; SSF81340; 1. PE 3: Inferred from homology; KW Cell membrane; Chloride; Chloride channel; Complete proteome; KW Ion channel; Ion transport; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 395 Uncharacterized protein MJ0305. FT /FTId=PRO_0000094500. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 172 192 Helical. {ECO:0000255}. FT TRANSMEM 206 226 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. FT TRANSMEM 279 299 Helical. {ECO:0000255}. FT TRANSMEM 311 331 Helical. {ECO:0000255}. FT TRANSMEM 359 379 Helical. {ECO:0000255}. SQ SEQUENCE 395 AA; 42618 MW; 9CDC65D6201CF7C0 CRC64; MPMNIVNMFG KYIKIIKWIG IASLIGIVGG LSSVIIAIII EYFPEKHNVL LIPIVFFIAG LFVDYIYELK GSGIDRVLKA LNTNEKLTWI RGLLKVLLAG AVIAVGGSAG KEGPCVQSSA SFADELYRLL KLKNRELVII TGIAGGLGGA FSAPLGTAIL ACEIIEHENF NYINLIPPII ASVVGYLIFY LITGRKHLFN ITLSYTINIH DFLLFILGAF FCSLIAHCYI KTYRKISSTF DNLKIPYCIK TLIGGILVAV ISYFIPEVMG MGLTLTKELF IMEFSLVFLV LLLIGKILAT SFTVGSGTPG GLVFPSMCIG AISGIIFGSL IGDCSAPYIV LGIATTLSAT TNAPLGGAVL CTEIFGFDFA VPASIGAVIG YQMTKLETIF KYIRF // ID Y306_METJA Reviewed; 78 AA. AC Q57754; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0306; GN OrderedLocusNames=MJ0306; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98298.1; -; Genomic_DNA. DR PIR; C64338; C64338. DR STRING; 243232.MJ_0306; -. DR EnsemblBacteria; AAB98298; AAB98298; MJ_0306. DR KEGG; mja:MJ_0306; -. DR eggNOG; arCOG08293; Archaea. DR eggNOG; ENOG41110WU; LUCA. DR OMA; ELCIKCE; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 78 Uncharacterized protein MJ0306. FT /FTId=PRO_0000106784. SQ SEQUENCE 78 AA; 9301 MW; AC895EC26103A839 CRC64; MRQSKKDYKL KIFNLVKVMK LRVVCKDENL TDDELCIKCE LCIGKDLMTI IEMMNEEYKI DEIIIPNCET LKRILNMD // ID Y308_METJA Reviewed; 233 AA. AC Q57756; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0308; GN OrderedLocusNames=MJ0308; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98294.1; -; Genomic_DNA. DR PIR; E64338; E64338. DR STRING; 243232.MJ_0308; -. DR EnsemblBacteria; AAB98294; AAB98294; MJ_0308. DR KEGG; mja:MJ_0308; -. DR eggNOG; arCOG02289; Archaea. DR eggNOG; COG2043; LUCA. DR InParanoid; Q57756; -. DR OMA; KGGAYAI; -. DR PhylomeDB; Q57756; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR003748; DUF169. DR Pfam; PF02596; DUF169; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 233 Uncharacterized protein MJ0308. FT /FTId=PRO_0000106785. SQ SEQUENCE 233 AA; 26244 MW; D575639D0E34C079 CRC64; MDVNEIRENA KKLMELMMLD KPFVAVKLAK SKEEIPEGYE TLDEEKRHCE MIQMARLERK KLYATVDKHL CKGGAYAMGV FRNPPEPLAT GKLYVKLGNF KDEEAAKKTV DAIPKVEEEI YATVYAPLDE TDFIPDSIVF IGEPLYALRL VQAILYHKGG RFQADFSGIQ SLCADAVAAV YTRKAPNMTL GCNGSRKYAG IKPEEVVVAF PPEKLKDIVE AIEHFRQVWT CGH // ID Y321_METJA Reviewed; 122 AA. AC Q57769; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0321; GN OrderedLocusNames=MJ0321; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98312.1; -; Genomic_DNA. DR PIR; B64340; B64340. DR STRING; 243232.MJ_0321; -. DR EnsemblBacteria; AAB98312; AAB98312; MJ_0321. DR KEGG; mja:MJ_0321; -. DR eggNOG; arCOG10171; Archaea. DR eggNOG; ENOG410Y5S6; LUCA. DR OMA; YFGYRSG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 122 Uncharacterized protein MJ0321. FT /FTId=PRO_0000106792. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. SQ SEQUENCE 122 AA; 13504 MW; 952EE0C8D020250B CRC64; MTNNDKIVAI VTSIAVICIS LTVIFCDTLV LAVGVPTLVL LWLVFLGWIN NKKLDKGEMR RAITGSIVIA FFIILIAISK NPDIYSNNKE IFSLFFGMVT TIIGYYFGYR SGKESKNSSG NE // ID Y334_METJA Reviewed; 102 AA. AC Q57780; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0334; GN OrderedLocusNames=MJ0334; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98322.1; -; Genomic_DNA. DR PIR; F64341; F64341. DR STRING; 243232.MJ_0334; -. DR EnsemblBacteria; AAB98322; AAB98322; MJ_0334. DR KEGG; mja:MJ_0334; -. DR eggNOG; arCOG08301; Archaea. DR eggNOG; ENOG410Z7RB; LUCA. DR OMA; EMEQFYH; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 102 Uncharacterized protein MJ0334. FT /FTId=PRO_0000106804. FT COMPBIAS 60 89 Glu/Lys-rich. SQ SEQUENCE 102 AA; 11555 MW; 1C9A45826A0B2AE3 CRC64; MSKMGLFKKE KDNGVIDDLV PKKSDYVEKI AQEAIRKDKV DALVRKHEME QFYHEVSQNE KIAELKAELA KKEKEIEELK EEIRGLKGKA GGLGIGGSQV TR // ID Y339_METJA Reviewed; 107 AA. AC Q57785; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0339; GN OrderedLocusNames=MJ0339; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98327.1; -; Genomic_DNA. DR PIR; C64342; C64342. DR STRING; 243232.MJ_0339; -. DR EnsemblBacteria; AAB98327; AAB98327; MJ_0339. DR KEGG; mja:MJ_0339; -. DR eggNOG; arCOG09644; Archaea. DR eggNOG; ENOG41110S4; LUCA. DR OMA; DFHCEAD; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 107 Uncharacterized protein MJ0339. FT /FTId=PRO_0000106809. SQ SEQUENCE 107 AA; 12450 MW; 9CC983A8F7F7596F CRC64; MKKRGRCSLT NYANAKALVE KILEDLKNNG IKVKSPLSKI QDFHCEADFS VEIENRVAYV DATFTFDKLP NEDLVEKIEA VMTTYNSYLE RIDFESDYTK LEFRSVR // ID Y3404_METJA Reviewed; 135 AA. AC Q60303; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 45. DE RecName: Full=Uncharacterized protein MJECS04; GN OrderedLocusNames=MJECS04; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37062.1; -; Genomic_DNA. DR PIR; D64516; D64516. DR EnsemblBacteria; AAC37062; AAC37062; MJ_ECS04. DR KEGG; mja:MJECS04; -. DR Proteomes; UP000000805; Plasmid small ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 135 Uncharacterized protein MJECS04. FT /FTId=PRO_0000107485. SQ SEQUENCE 135 AA; 15786 MW; 3C4A9DFB71D51AC0 CRC64; MLKKAIIKLL GIDNYIEKIE ELEGERKEIF ENFEKLNKKL DNFENELNFI KKEIERIQLE FNNVINSNNN DYVSKKELND IVNQLNTLST LVNGLIINIS HGNNLKESSN TVDDVKNRLL ELLQSEKDYC ITEIN // ID Y340_METJA Reviewed; 234 AA. AC Q57786; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0340; GN OrderedLocusNames=MJ0340; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98328.1; -; Genomic_DNA. DR PIR; D64342; D64342. DR ProteinModelPortal; Q57786; -. DR STRING; 243232.MJ_0340; -. DR EnsemblBacteria; AAB98328; AAB98328; MJ_0340. DR KEGG; mja:MJ_0340; -. DR eggNOG; arCOG09645; Archaea. DR eggNOG; ENOG410YPRD; LUCA. DR OMA; YKNGASK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 234 Uncharacterized protein MJ0340. FT /FTId=PRO_0000106810. SQ SEQUENCE 234 AA; 25463 MW; 4A9F5966C1F03056 CRC64; MVLSLTPPSQ ENILASGKLA YFGAKSQVDT FTGDEQNDTF ELTKDDAVLG SEIVKVNGVL QFEGQDYTAI HENGILKKIK FTQPPANGAS ITVEYLYLDL PLGGASELSV KEDKDKEELT VDCSYGKIQI EKGSSITLSF KDIITVGDIK LTAYFSGEIL EGNTYSKYKN GASKSANIVV LAFSKEATMA YGVEPPKRIV IIRGAMPNNL EFDWSGGSKS FDLTAQSYEI IDVK // ID Y34A_METJA Reviewed; 183 AA. AC P81307; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0347.1; GN OrderedLocusNames=MJ0347.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98344.1; -; Genomic_DNA. DR STRING; 243232.MJ_0347.1; -. DR EnsemblBacteria; AAB98344; AAB98344; MJ_0347.1. DR KEGG; mja:MJ_0347.1; -. DR eggNOG; arCOG09650; Archaea. DR eggNOG; ENOG410YM5Q; LUCA. DR OMA; NYNTRFY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 183 Uncharacterized protein MJ0347.1. FT /FTId=PRO_0000106818. SQ SEQUENCE 183 AA; 21756 MW; 769FCF680E86C895 CRC64; MKTIVIDKSM SVDIEYSINA IDQCNITSLK DLQIQPFDQC IILWNDKIIF RGYCIDARLS QSFGQQQYEY TINSPLWILS QQKTTAKTTF LQIFLKECCN LCNLELDYQL DSNPLIYIEE SSYFDALKKC ILYTKNYNTR FYVDYEYNSL IFTDKISGQH PKEEKVVGYE FEWDTEIINQ VRW // ID Y3510_METJA Reviewed; 219 AA. AC Q60272; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 55. DE RecName: Full=Uncharacterized protein MJECL10; GN OrderedLocusNames=MJECL10; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37083.1; -; Genomic_DNA. DR PIR; B64511; B64511. DR ProteinModelPortal; Q60272; -. DR EnsemblBacteria; AAC37083; AAC37083; MJ_ECL10. DR KEGG; mja:MJECL10; -. DR InParanoid; Q60272; -. DR OMA; MIETIHI; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR004604; DNA_recomb/repair_RecN. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR11059; PTHR11059; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 219 Uncharacterized protein MJECL10. FT /FTId=PRO_0000107502. SQ SEQUENCE 219 AA; 25362 MW; 1F147DF46DAC9017 CRC64; MHIHLFRCQC MIETIHIKNF RGIRELKLEN LGQINIIAGK NNASKSSILE ALALFLSAKE GFSLFIKILR EILLWRGWYG EKSIYDLFYK NSKELEVSVK FLNQDFANLT LKNSNQSFAN KNIAVELKSD KNSWSGRFDS HLIHPDYISS ILTSAEATQS NFEFITSLTL IKFGYIESIY SQAYETQVLQ DAIRLLREAY PEVKSLSPLQ KYNKWIIHV // ID Y3525_METJA Reviewed; 110 AA. AC Q60284; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Uncharacterized protein MJECL25; GN OrderedLocusNames=MJECL25; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37096.1; -; Genomic_DNA. DR PIR; H64512; H64512. DR EnsemblBacteria; AAC37096; AAC37096; MJ_ECL25. DR KEGG; mja:MJECL25; -. DR InParanoid; Q60284; -. DR OMA; PSMSSEV; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 110 Uncharacterized protein MJECL25. FT /FTId=PRO_0000107512. SQ SEQUENCE 110 AA; 12650 MW; 828470CFA71E24C9 CRC64; MSNDDLNALK KLKEISSGTV KQITSLPKKE PQEEKMSKTL RIKNTTHEKI IEMYGKKVGS QGEVVDKGVA VLYALWKILP EEQFKRVVKL AEEDRFEEFA DRLGIEIKEE // ID Y3533_METJA Reviewed; 408 AA. AC Q60290; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 53. DE RecName: Full=Uncharacterized protein MJECL33; GN OrderedLocusNames=MJECL33; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37102.1; -; Genomic_DNA. DR PIR; H64513; H64513. DR ProteinModelPortal; Q60290; -. DR EnsemblBacteria; AAC37102; AAC37102; MJ_ECL33. DR KEGG; mja:MJECL33; -. DR HOGENOM; HOG000138096; -. DR InParanoid; Q60290; -. DR OMA; LEVTPWW; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 408 Uncharacterized protein MJECL33. FT /FTId=PRO_0000107517. SQ SEQUENCE 408 AA; 48364 MW; 8E05C11F03D844A9 CRC64; MIIMDTIFVG SAIPDITNRP QLYEWLERNM ERSYKDILDD TKLEPEQNVV KTYILESNIH PKKLSRIIKT GKIKPLDEYE FYMLRIGDEG YFFIDAKNPR FWKLYTLQKS EESDKYFNKL ISPIKSRLDN LWMPTGDLEK FLKKADYVRG LSTKHDETPF YLDNDVEERA NKLSISSNGE SVYELIKIIQ SLSSDEIQEF EKLIKDFQLL NDTKIKKIFN TIKKLHEFKH LMRITKSKIK IVSEDDKDKF VLEDIYYWGK FTVKGTSIEK HNEIVDKTIE NYEQKIEIIE DSLIDYTSSD WGDRIPLIYE FEKEIEDLKN FVEGLISVKE PFKIWGLAKQ VEEDMYYISG VDLHNGDRFS LEVTPWWMRL YLPKGSCGNT ALRLLSNIQQ TYDSETILEV EKYGERIR // ID Y3536_METJA Reviewed; 144 AA. AC Q60257; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 11-NOV-2015, entry version 73. DE RecName: Full=UPF0310 protein MJECL36; GN OrderedLocusNames=MJECL36; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0310 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAC37105.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37105.1; ALT_INIT; Genomic_DNA. DR PIR; C64514; C64514. DR PDB; 2P5D; X-ray; 1.70 A; A=1-144. DR PDBsum; 2P5D; -. DR ProteinModelPortal; Q60257; -. DR SMR; Q60257; 1-144. DR STRING; 243232.MJ_1382; -. DR EnsemblBacteria; AAC37105; AAC37105; MJ_ECL36. DR KEGG; mja:MJECL36; -. DR eggNOG; arCOG02727; Archaea. DR eggNOG; COG1673; LUCA. DR HOGENOM; HOG000244906; -. DR InParanoid; Q60257; -. DR OMA; EKNVWGV; -. DR PhylomeDB; Q60257; -. DR EvolutionaryTrace; Q60257; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 3.10.590.10; -; 1. DR HAMAP; MF_00771; UPF0310; 1. DR InterPro; IPR002740; EVE_domain. DR InterPro; IPR015947; PUA-like_domain. DR InterPro; IPR022996; UPF0310. DR Pfam; PF01878; EVE; 1. DR SUPFAM; SSF88697; SSF88697; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 144 UPF0310 protein MJECL36. FT /FTId=PRO_0000059636. FT STRAND 3 8 {ECO:0000244|PDB:2P5D}. FT HELIX 10 19 {ECO:0000244|PDB:2P5D}. FT STRAND 21 24 {ECO:0000244|PDB:2P5D}. FT HELIX 26 28 {ECO:0000244|PDB:2P5D}. FT HELIX 29 32 {ECO:0000244|PDB:2P5D}. FT STRAND 40 45 {ECO:0000244|PDB:2P5D}. FT STRAND 57 64 {ECO:0000244|PDB:2P5D}. FT STRAND 89 104 {ECO:0000244|PDB:2P5D}. FT HELIX 105 108 {ECO:0000244|PDB:2P5D}. FT HELIX 109 111 {ECO:0000244|PDB:2P5D}. FT STRAND 118 120 {ECO:0000244|PDB:2P5D}. FT STRAND 129 133 {ECO:0000244|PDB:2P5D}. FT HELIX 135 142 {ECO:0000244|PDB:2P5D}. SQ SEQUENCE 144 AA; 17183 MW; 11B4604B5D323070 CRC64; MAYWLCITNE DNWKVIKEKK IWGVAERYKN TINKVKVGDK LIIYEIQRSG KDYKPPYIRG VYEVVSEVYK DSSKIFKPTP RNPNEKFPYR VKLKEIKVFE PPINFKELIP KLKFITNKKR WSGHLMGKAM REIPEEDYKL IVGN // ID Y3543_METJA Reviewed; 384 AA. AC Q60298; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 17-FEB-2016, entry version 52. DE RecName: Full=Uncharacterized protein MJECL43; GN OrderedLocusNames=MJECL43; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37112.1; -; Genomic_DNA. DR PIR; B64515; B64515. DR ProteinModelPortal; Q60298; -. DR PRIDE; Q60298; -. DR EnsemblBacteria; AAC37112; AAC37112; MJ_ECL43. DR KEGG; mja:MJECL43; -. DR OMA; ISEREMS; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 384 Uncharacterized protein MJECL43. FT /FTId=PRO_0000107522. SQ SEQUENCE 384 AA; 45886 MW; DA032E83C2433D2E CRC64; MNIDIEDFEK KPLYIQRIIL RNSCIEFSKM LKKYWDKNIM IGIQISEREM SFEIEERDNK NEPIKITLPE YRSKGFKWYL AYLITLEYLR ILKNGGNNDI VLLLDDPAVY LHPNVQKSFL EKLEELSKEY QILYNTHLMS LFNEEELDRV LLVYLDKENR TKIKRPWSNE QKDIIYPIRR ALGVDKILFK ENLSKILFVE GISDKFILEG LGKLETLKNL KNWYIHPLSG GDKLEDNEIV KKVRLYSCLS NFEEIKYYFL LDGDKKEKFE RDKISNKIIF LGDENQEIED LIDKNFYLDC VLETYKRIFT HDLEKFKKVK EIVEKLRKSK SKIIEELNNE FRLNNLGDFS KVDVAITIKR KLYENPELAN KFEKIIDCLN GKII // ID Y355_METJA Reviewed; 109 AA. AC Q57801; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0355; GN OrderedLocusNames=MJ0355; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98347.1; -; Genomic_DNA. DR PIR; C64344; C64344. DR STRING; 243232.MJ_0355; -. DR EnsemblBacteria; AAB98347; AAB98347; MJ_0355. DR KEGG; mja:MJ_0355; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein MJ0355. FT /FTId=PRO_0000106826. SQ SEQUENCE 109 AA; 12942 MW; 8EFACB812E200839 CRC64; MLRFKKTPDE VKEMIKLAIK KGYRQIKISS VNPNEFLLRF DGRMWIMGFE FLSDKEIKYS CFENYSFKCI LETDAKKVRE FLEEIYSKSK IVNGRVKEIP TDVFQVVVA // ID Y380_METJA Reviewed; 118 AA. AC Q57825; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0380; GN OrderedLocusNames=MJ0380; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98377.1; -; Genomic_DNA. DR PIR; D64347; D64347. DR STRING; 243232.MJ_0380; -. DR EnsemblBacteria; AAB98377; AAB98377; MJ_0380. DR KEGG; mja:MJ_0380; -. DR eggNOG; arCOG06572; Archaea. DR eggNOG; ENOG410Y6RI; LUCA. DR KO; K19087; -. DR OMA; WIRNIGR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 118 Uncharacterized protein MJ0380. FT /FTId=PRO_0000106843. SQ SEQUENCE 118 AA; 13758 MW; 322C1759E495B1DD CRC64; MSIDEVIKLE NWMKNIGRYL SYLISDKFEE YAYDIIDGVA KARNANELLE ALYKGLRLSP KLKKKGNIEV PSPEDVKKLE ETLREIGDNE KEVRKIGLSM ALWAFADWEK DHRKRGDQ // ID Y392_METJA Reviewed; 339 AA. AC Q57837; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 116. DE RecName: Full=Zinc metalloprotease MJ0392; DE EC=3.4.24.-; DE AltName: Full=MjS2P; DE AltName: Full=S2P endopeptidase; DE AltName: Full=Site-2-type intramembrane protease; GN OrderedLocusNames=MJ0392; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-224, FUNCTION AS A RP PROTEASE, ENZYME REGULATION, COFACTOR, SUBUNIT, ACTIVE SITE, AND RP ZINC-BINDING SITES. RX PubMed=18063795; DOI=10.1126/science.1150755; RA Feng L., Yan H., Wu Z., Yan N., Wang Z., Jeffrey P.D., Shi Y.; RT "Structure of a site-2 protease family intramembrane RT metalloprotease."; RL Science 318:1608-1612(2007). CC -!- FUNCTION: A site-2 regulated intramembrane protease (S2P), its CC endogenous substrate is unknown. Regulated intramembrane CC proteolysis (RIP) occurs when an extracytoplasmic signal triggers CC a concerted proteolytic cascade to transmit information and elicit CC cellular responses. A membrane-spanning regulatory substrate CC protein is first cut extracytoplasmically (site-1 protease, S1P), CC then within the membrane itself (site-2 protease, S2P, this CC enzyme), while cytoplasmic proteases finish degrading the CC regulatory protein, liberating the effector protein. Possible CC signals, S1P and substrates are unknown in this organism. CC {ECO:0000269|PubMed:18063795}. CC -!- CATALYTIC ACTIVITY: Cleaves type-2 transmembrane proteins within CC their membrane-spanning domains. CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; CC Evidence={ECO:0000269|PubMed:18063795}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000269|PubMed:18063795}; CC -!- ENZYME REGULATION: Inhibited by 1,10-phenanthroline. CC {ECO:0000269|PubMed:18063795}. CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:18063795}. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}. CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98382.1; -; Genomic_DNA. DR PIR; H64348; H64348. DR PDB; 3B4R; X-ray; 3.30 A; A/B=1-224. DR PDBsum; 3B4R; -. DR ProteinModelPortal; Q57837; -. DR SMR; Q57837; 3-220. DR STRING; 243232.MJ_0392; -. DR MEROPS; M50.006; -. DR EnsemblBacteria; AAB98382; AAB98382; MJ_0392. DR KEGG; mja:MJ_0392; -. DR eggNOG; arCOG00607; Archaea. DR eggNOG; COG0517; LUCA. DR eggNOG; COG1994; LUCA. DR InParanoid; Q57837; -. DR OMA; KKHMGYP; -. DR PhylomeDB; Q57837; -. DR BRENDA; 3.4.24.85; 3260. DR EvolutionaryTrace; Q57837; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. DR InterPro; IPR000644; CBS_dom. DR InterPro; IPR008915; Peptidase_M50. DR InterPro; IPR016483; UCP006404_Pept_M50_CBS. DR Pfam; PF00571; CBS; 2. DR Pfam; PF02163; Peptidase_M50; 2. DR PIRSF; PIRSF006404; UCP006404_Pept_M50_CBS; 1. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. DR PROSITE; PS00142; ZINC_PROTEASE; 1. PE 1: Evidence at protein level; KW 3D-structure; CBS domain; Cell membrane; Complete proteome; Hydrolase; KW Membrane; Metal-binding; Metalloprotease; Protease; KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Zinc. FT CHAIN 1 339 Zinc metalloprotease MJ0392. FT /FTId=PRO_0000088480. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 251 271 Helical. {ECO:0000255}. FT DOMAIN 226 281 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 281 335 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT ACT_SITE 55 55 {ECO:0000255|PROSITE-ProRule:PRU10095, FT ECO:0000269|PubMed:18063795}. FT METAL 54 54 Zinc; catalytic. FT METAL 58 58 Zinc; catalytic. FT METAL 148 148 Zinc; catalytic. FT STRAND 4 10 {ECO:0000244|PDB:3B4R}. FT STRAND 13 18 {ECO:0000244|PDB:3B4R}. FT HELIX 19 31 {ECO:0000244|PDB:3B4R}. FT HELIX 38 63 {ECO:0000244|PDB:3B4R}. FT STRAND 72 74 {ECO:0000244|PDB:3B4R}. FT STRAND 76 78 {ECO:0000244|PDB:3B4R}. FT STRAND 88 90 {ECO:0000244|PDB:3B4R}. FT HELIX 91 112 {ECO:0000244|PDB:3B4R}. FT HELIX 125 139 {ECO:0000244|PDB:3B4R}. FT STRAND 142 147 {ECO:0000244|PDB:3B4R}. FT HELIX 148 161 {ECO:0000244|PDB:3B4R}. FT HELIX 163 187 {ECO:0000244|PDB:3B4R}. FT HELIX 191 218 {ECO:0000244|PDB:3B4R}. SQ SEQUENCE 339 AA; 37965 MW; A56EB35F186A6457 CRC64; MNYSIRLFKI MGIPIELHIT FILFLVVIIG LSIMNNSIFW AVLFILLFVS VVLHELGHSY VAKKYGVKIE KILLLPIGGV AMMDKIPKEG ELRIGIAGPL VSFIIGIVLL IVSQFFDINI NGYPLLYTLS LLNLMLGGFN LIPAFPMDGG RILRAILSKK YGYLKSTKIA ANIGKSLALI MLLFGLLSMN IILILVSLFV YFGAEQESRV VEVETIFKNI KAKDIMTPNP VYVTPDMSIE EFLDFMLKHK YFGYPVVENG KLVGCIGIGN IHKKEGTVRD YMEKPVVVSE DTDIKEILRK MANTDRVFVV EGGKLKGIIS KTDILRAMSI LELKEELKD // ID Y417_METJA Reviewed; 237 AA. AC Q57860; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0417; GN OrderedLocusNames=MJ0417; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98404.1; -; Genomic_DNA. DR PIR; A64352; A64352. DR ProteinModelPortal; Q57860; -. DR STRING; 243232.MJ_0417; -. DR EnsemblBacteria; AAB98404; AAB98404; MJ_0417. DR KEGG; mja:MJ_0417; -. DR eggNOG; arCOG00302; Archaea. DR eggNOG; COG0613; LUCA. DR InParanoid; Q57860; -. DR KO; K07053; -. DR OMA; WEVGNAY; -. DR PhylomeDB; Q57860; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro. DR GO; GO:0006260; P:DNA replication; IEA:InterPro. DR InterPro; IPR003141; Pol/His_phosphatase_N. DR InterPro; IPR016195; Pol/histidinol_Pase-like. DR SMART; SM00481; POLIIIAc; 1. DR SUPFAM; SSF89550; SSF89550; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJ0417. FT /FTId=PRO_0000106863. SQ SEQUENCE 237 AA; 27454 MW; 7C97038BBA2E52AD CRC64; MKVDLHVHSI VSKCSLNPKG LLEKFCIKKN IVPAICDHNK LTKLNFAIPG EEIATNSGEF IGLFLTEEIP ANLDLYEALD RVREQGALIY LPHPFDLNRR RSLAKFNVLE EREFLKYVHV VEVFNSRCRS IEPNLKALEY AEKYDFAMAF GSDAHFIWEV GNAYIKFSEL NIEKPDDLSP KEFLNLLKIK TDELLKAKSN LLKNPWKTRW HYGKLGSKYN IALYSKVVKN VRRKLNI // ID Y448_METJA Reviewed; 256 AA. AC Q57890; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0448; GN OrderedLocusNames=MJ0448; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98437.1; -; Genomic_DNA. DR PIR; H64355; H64355. DR ProteinModelPortal; Q57890; -. DR STRING; 243232.MJ_0448; -. DR PRIDE; Q57890; -. DR EnsemblBacteria; AAB98437; AAB98437; MJ_0448. DR KEGG; mja:MJ_0448; -. DR eggNOG; arCOG00503; Archaea. DR eggNOG; COG1237; LUCA. DR InParanoid; Q57890; -. DR KO; K06897; -. DR OMA; KSSWAND; -. DR PhylomeDB; Q57890; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.15.10; -; 2. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 256 Uncharacterized protein MJ0448. FT /FTId=PRO_0000106880. SQ SEQUENCE 256 AA; 29409 MW; 0A4773E57FDECCEE CRC64; MIKILVDNTA YKKFFAQHGF SALIEINNKR ILFDAGQNSI TLRENLRLFN EKEGFDYIVL SHGHYDHCDG LKYVIENDLI NGKVIAHKDA FLDKYAGNRY IGIDEEIKEY LLKKADLEII EEPYKIDKDI IVSGYVPREY EYEMEEFQCI KDGKRVKDEV NDDMFLIAKG ILITGCSHSG IINVVEYGKK LSEIKGVLGG FHLVGVSDNY LNRIVDYFKS QDFWIMPMHC TGFKALTKLS QLNNFVYGHV GKIIGI // ID Y449_METJA Reviewed; 283 AA. AC Q57891; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 95. DE RecName: Full=Uncharacterized transporter MJ0449; GN OrderedLocusNames=MJ0449; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the cation diffusion facilitator (CDF) CC transporter (TC 2.A.4) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98438.1; -; Genomic_DNA. DR PIR; A64356; A64356. DR ProteinModelPortal; Q57891; -. DR STRING; 243232.MJ_0449; -. DR EnsemblBacteria; AAB98438; AAB98438; MJ_0449. DR KEGG; mja:MJ_0449; -. DR eggNOG; arCOG01474; Archaea. DR eggNOG; COG0053; LUCA. DR InParanoid; Q57891; -. DR OMA; SHPFGHS; -. DR PhylomeDB; Q57891; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005385; F:zinc ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0061088; P:regulation of sequestering of zinc ion; IBA:GO_Central. DR GO; GO:0010043; P:response to zinc ion; IBA:GO_Central. DR GO; GO:0071577; P:zinc II ion transmembrane transport; IBA:GOC. DR Gene3D; 1.20.1510.10; -; 1. DR Gene3D; 3.30.70.1350; -; 1. DR InterPro; IPR002524; Cation_efflux. DR InterPro; IPR027470; Cation_efflux_CTD. DR InterPro; IPR027469; Cation_efflux_TMD. DR PANTHER; PTHR11562; PTHR11562; 1. DR Pfam; PF01545; Cation_efflux; 1. DR Pfam; PF16916; ZT_dimer; 1. DR TIGRFAMs; TIGR01297; CDF; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 283 Uncharacterized transporter MJ0449. FT /FTId=PRO_0000206139. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 38 58 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. SQ SEQUENCE 283 AA; 31286 MW; 4F9128C4222365FE CRC64; MREVEKPLIL SIVGNILLGL IKIIIGYVYS SISLISDGIH SLSDVITSII GIIGVKIASK PPDESHPYGH SRFECLFSFF IGLALFFTAY EIGKFAVERI IYGEVIEVNA IMVGVAILSI VVKELMTRYS LFVGKKLNSQ VLIADAYHHR SDALSSVVVL VGLLLQKFGI YYGDAIAGII VALMIAKVAF DICLTNIDYL TGRAPPKKFF ELIEKEALNV DKVIGVHDIK AHYVGPRIHV ELHVEVPSNI SAKEMHDIEV AVKNRLESLE NVERAYVHVD IVD // ID Y512_METJA Reviewed; 237 AA. AC Q57932; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0512; GN OrderedLocusNames=MJ0512; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98511.1; -; Genomic_DNA. DR PIR; H64363; H64363. DR ProteinModelPortal; Q57932; -. DR STRING; 243232.MJ_0512; -. DR EnsemblBacteria; AAB98511; AAB98511; MJ_0512. DR KEGG; mja:MJ_0512; -. DR eggNOG; arCOG08280; Archaea. DR eggNOG; ENOG41110JI; LUCA. DR OMA; SKRCYIP; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJ0512. FT /FTId=PRO_0000106905. SQ SEQUENCE 237 AA; 27072 MW; FF08A53188543448 CRC64; MIFMVLGKIK SLLPNSQILT KVKIVDIRRK ESEEGSIFYI GTMVDKDGVA NFITTIPLER GKCYEIFGRI TEEKSVRIVE KVIKGVKYPR EIPEIPKEQL YNRGEVLDVK VPAILEVSQS TIFVNYYCKI CRGIVDTKIK PRGLVYICRN CGEIDPEDVD VKIKVFGKIH FGTSSKRCYI PPATLEQFMP GILDMLEEYG IDDTIREICL KLNGKTFLVR GFEGKEGNYI ITEMEDI // ID Y521_METJA Reviewed; 69 AA. AC Q57941; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0521; GN OrderedLocusNames=MJ0521; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98528.1; -; Genomic_DNA. DR PIR; A64365; A64365. DR STRING; 243232.MJ_0521; -. DR DNASU; 1451385; -. DR EnsemblBacteria; AAB98528; AAB98528; MJ_0521. DR KEGG; mja:MJ_0521; -. DR eggNOG; arCOG05034; Archaea. DR eggNOG; ENOG410ZAQD; LUCA. DR KO; K14100; -. DR OMA; KLPFRGY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 69 Uncharacterized protein MJ0521. FT /FTId=PRO_0000106910. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 36 56 Helical. {ECO:0000255}. SQ SEQUENCE 69 AA; 7769 MW; F9D0AAF9875D6451 CRC64; MKNMDEERKY GLYSLIIGLL CVIGIVMLNG LICYVLYIIA VPSLLYGIGA FIIPKTRRKD AGKLPFRGY // ID Y530_METJA Reviewed; 198 AA. AC Q57950; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Uncharacterized ZPR1-like protein MJ0530; GN OrderedLocusNames=MJ0530; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ZPR1 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98521.1; -; Genomic_DNA. DR PIR; B64366; B64366. DR ProteinModelPortal; Q57950; -. DR STRING; 243232.MJ_0530; -. DR EnsemblBacteria; AAB98521; AAB98521; MJ_0530. DR KEGG; mja:MJ_0530; -. DR eggNOG; arCOG04265; Archaea. DR eggNOG; COG1779; LUCA. DR InParanoid; Q57950; -. DR KO; K06874; -. DR OMA; HSAIIGD; -. DR PhylomeDB; Q57950; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR004457; Znf_ZPR1. DR InterPro; IPR004470; Znf_ZPR1-type_subgr. DR Pfam; PF03367; zf-ZPR1; 1. DR SMART; SM00709; Zpr1; 1. DR TIGRFAMs; TIGR00340; zpr1_rel; 1. DR TIGRFAMs; TIGR00310; ZPR1_znf; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome; Zinc; KW Zinc-finger. FT CHAIN 1 198 Uncharacterized ZPR1-like protein MJ0530. FT /FTId=PRO_0000119041. FT ZN_FING 9 43 C4-type. SQ SEQUENCE 198 AA; 22591 MW; 230B073CCA8C3C1A CRC64; MENVQRLDCP VCGGKGTFVI TSHQIDIPYF GPVLETTMIC EKCNFRRSDV FPLEVREPKK YILKIESERD LNKRVVRSSS AYIQIPELGV EIKPGPLAEG FVSNVEGVLN RVDNILQTLI RWAETEEQKK KAEELRERIK KLKEGKEEAT LILIDPLGHS AIIGEGVEEE ILSEEEVEKL KEGIVIMDLD KDKEKEKE // ID Y547_METJA Reviewed; 264 AA. AC Q57967; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized ATP-binding protein MJ0547; GN OrderedLocusNames=MJ0547; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98539.1; -; Genomic_DNA. DR PIR; C64368; C64368. DR ProteinModelPortal; Q57967; -. DR STRING; 243232.MJ_0547; -. DR EnsemblBacteria; AAB98539; AAB98539; MJ_0547. DR KEGG; mja:MJ_0547; -. DR eggNOG; arCOG00589; Archaea. DR eggNOG; COG0455; LUCA. DR InParanoid; Q57967; -. DR KO; K03609; -. DR OMA; MEDIPIT; -. DR PhylomeDB; Q57967; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR025501; MinD. DR InterPro; IPR010224; MinD_archaea. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF003092; MinD; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01969; minD_arch; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 264 Uncharacterized ATP-binding protein FT MJ0547. FT /FTId=PRO_0000106925. FT NP_BIND 14 21 ATP. {ECO:0000255}. SQ SEQUENCE 264 AA; 27737 MW; B9AF5108CDD0CEC3 CRC64; MVTLMAIAIA IASGKGGTGK TTISANLAVA LAKFGKKVAV LDADIAMANL ELIMGLEGKP VTLNDVLAGK ADIKDAIYEG PEGVLVIPAG VSLEKFRRAK PEKLEEVLKA IHDLVEILII DCPAGIGKET LIAISSADGL IVVVNPEISS ISDALKIIAI TKRLGTDIIG AIVNRVSNES TELGVKAIET ILEVPVIGVV PEDPHVRKAA AFGTPLVIMY PDSPAAQAIM EIAAKLIGAK YEAQLKKKKE SFISKFIKGL FGRR // ID Y551_METJA Reviewed; 275 AA. AC Q57971; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein MJ0551; GN OrderedLocusNames=MJ0551; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98543.1; -; Genomic_DNA. DR PIR; G64368; G64368. DR ProteinModelPortal; Q57971; -. DR STRING; 243232.MJ_0551; -. DR DNASU; 1451416; -. DR EnsemblBacteria; AAB98543; AAB98543; MJ_0551. DR KEGG; mja:MJ_0551; -. DR eggNOG; arCOG02059; Archaea. DR eggNOG; COG2221; LUCA. DR InParanoid; Q57971; -. DR OMA; NCGKCKD; -. DR PhylomeDB; Q57971; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 1. DR SUPFAM; SSF55124; SSF55124; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 1. DR PROSITE; PS00365; NIR_SIR; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Heme; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1 275 Uncharacterized protein MJ0551. FT /FTId=PRO_0000199969. FT METAL 97 97 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 102 102 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 136 136 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 140 140 Iron (siroheme axial ligand). FT {ECO:0000250}. FT METAL 140 140 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 275 AA; 31188 MW; D4916B68EEA5882E CRC64; MVKRMHCNIN LKYGVIMKKD CYTLRISLKP GFINAEQLKA IAYVIENFGD NKAHITTRQG IEFKISPEHL EEVEKILNNV GLNLGSTGNR VRQVVSCIGL ECYNAIGDSV SLARRIHEEF EGVWVPRKVK INVSGCPNSC TFHRFCDIGI CYRYKITINK EICTNCGKCK DFCDLNAIDW ERKIIKDNCT GEGKCTGLCN AFKAERVISI FVGGKGGRIY KEGKHLIDLK NEDDVLFVID ELISLYAKFG KGRMADFVEN YGIENLRNNI KELIK // ID Y553_METJA Reviewed; 153 AA. AC Q57973; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 83. DE RecName: Full=Acylphosphatase-like protein MJ0553; GN OrderedLocusNames=MJ0553; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98549.1; -; Genomic_DNA. DR PIR; A64369; A64369. DR ProteinModelPortal; Q57973; -. DR STRING; 243232.MJ_0553; -. DR EnsemblBacteria; AAB98549; AAB98549; MJ_0553. DR KEGG; mja:MJ_0553; -. DR eggNOG; arCOG01674; Archaea. DR eggNOG; COG1254; LUCA. DR InParanoid; Q57973; -. DR OMA; GQDTIIK; -. DR PhylomeDB; Q57973; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR InterPro; IPR017968; Acylphosphatase_CS. DR Pfam; PF00708; Acylphosphatase; 1. DR SUPFAM; SSF54975; SSF54975; 1. DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 153 Acylphosphatase-like protein MJ0553. FT /FTId=PRO_0000158562. FT DOMAIN 4 102 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. SQ SEQUENCE 153 AA; 17880 MW; 3AC47E49C620686B CRC64; MITTYELIIY GRVQHVGFRD RIEHIGRGLG ISGVVYNHKD GTVRILANFD DEEIKELFKK SIKALEKKDK LIKIEKIEEK ELNAYIEFPE GISRLSSDDI LELNKKLDEG VKYIKLIFSE LEEHKKILLD IKDTQIKTIK VLNEIKELLE KKL // ID Y582_METJA Reviewed; 128 AA. AC Q58002; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0582; GN OrderedLocusNames=MJ0582; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0766. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98576.1; -; Genomic_DNA. DR PIR; F64372; F64372. DR ProteinModelPortal; Q58002; -. DR STRING; 243232.MJ_0582; -. DR DNASU; 1451447; -. DR EnsemblBacteria; AAB98576; AAB98576; MJ_0582. DR KEGG; mja:MJ_0582; -. DR eggNOG; arCOG02639; Archaea. DR eggNOG; COG5561; LUCA. DR InParanoid; Q58002; -. DR OMA; VGYPPCP; -. DR PhylomeDB; Q58002; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014925; Uncharacterised_CGGC-dom. DR Pfam; PF08821; CGGC; 1. DR SMART; SM01078; CGGC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein MJ0582. FT /FTId=PRO_0000106942. SQ SEQUENCE 128 AA; 14086 MW; B39A14381AA19EA0 CRC64; MKVAIIACQK MVEMGCPGKE ACVSCFKAIN EKSGAFERYK DVELVAFTTC GGCPGRRFPM RVKLLKTAAG AEAIHIANCT FLQPECPYIN FDEICKKLME ELEIPIVFGT HTLVKKGEVV CTCGDNKE // ID Y583_METJA Reviewed; 57 AA. AC Q58003; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0583; GN OrderedLocusNames=MJ0583; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98582.1; -; Genomic_DNA. DR PIR; G64372; G64372. DR STRING; 243232.MJ_0583; -. DR EnsemblBacteria; AAB98582; AAB98582; MJ_0583. DR KEGG; mja:MJ_0583; -. DR eggNOG; arCOG05041; Archaea. DR eggNOG; ENOG410Z92P; LUCA. DR OMA; EVDVCPC; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR029037; YfgJ-like. DR SUPFAM; SSF161187; SSF161187; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Uncharacterized protein MJ0583. FT /FTId=PRO_0000106943. FT COMPBIAS 51 56 Poly-Arg. SQ SEQUENCE 57 AA; 6626 MW; E643AD862336DDA8 CRC64; MIVWNLICPK CGKRLRYKVD VCPCMASEVE LPNCPDCGEK MVHDYTSLKG RRRIRRG // ID Y602_METJA Reviewed; 261 AA. AC Q58019; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0602; GN OrderedLocusNames=MJ0602; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98598.1; -; Genomic_DNA. DR PIR; B64375; B64375. DR ProteinModelPortal; Q58019; -. DR STRING; 243232.MJ_0602; -. DR EnsemblBacteria; AAB98598; AAB98598; MJ_0602. DR KEGG; mja:MJ_0602; -. DR eggNOG; arCOG08295; Archaea. DR eggNOG; ENOG41111NZ; LUCA. DR OMA; YIEKKPY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein MJ0602. FT /FTId=PRO_0000106952. SQ SEQUENCE 261 AA; 30835 MW; 81E4A011C761E8F4 CRC64; MLLEKSKIEI IEQFIHILEI LEMYAKEGSD EKAIIRLMLD YLEKGYVLDD DILPIASKIS EIAKKVGSFD MKREISLLLF GERKRLTKSQ KNKIKKIIEI LEYLKSYIEK KPYKSYEDKL ILNLIGLKIL RLDNGIVLDY NSEVRSLTNM ALRVGSYELK NEIELLLTGR RRRKLTEEFI QKRLSIIKIL EMVKDFIDKK EFKSSFDYEA LFLINLKIYR IEEGILKNFD EEIESILNIA RKVGNHKLRE QIVLLKESIK N // ID Y605_METJA Reviewed; 134 AA. AC Q58022; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=UPF0332 protein MJ0605; GN OrderedLocusNames=MJ0605; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0332 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98599.1; -; Genomic_DNA. DR PIR; E64375; E64375. DR ProteinModelPortal; Q58022; -. DR STRING; 243232.MJ_0605; -. DR EnsemblBacteria; AAB98599; AAB98599; MJ_0605. DR KEGG; mja:MJ_0605; -. DR eggNOG; arCOG02123; Archaea. DR eggNOG; COG1895; LUCA. DR InParanoid; Q58022; -. DR KO; K09132; -. DR OMA; YYAMFYA; -. DR PhylomeDB; Q58022; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007842; HEPN_dom. DR Pfam; PF05168; HEPN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 134 UPF0332 protein MJ0605. FT /FTId=PRO_0000159640. SQ SEQUENCE 134 AA; 15596 MW; 4C1D5D5288D3452C CRC64; MKALLNKDIR EEIQALIEIA EENLSAAKIL FENKLYRDAV ARAYYAIFHS AKALLLTKNL NPKKHAGVIK MFGLYFVNEG YIEEIYGRII TKSYNLRWKA DYTTDKPTEE EAESIIYEAE MFVDRIKKAL KEIL // ID Y611_METJA Reviewed; 191 AA. AC Q58028; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 90. DE RecName: Full=Putative zinc metalloprotease MJ0611; DE EC=3.4.24.-; GN OrderedLocusNames=MJ0611; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the peptidase M50B family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98604.1; -; Genomic_DNA. DR PIR; C64376; C64376. DR ProteinModelPortal; Q58028; -. DR STRING; 243232.MJ_0611; -. DR MEROPS; M50.A07; -. DR EnsemblBacteria; AAB98604; AAB98604; MJ_0611. DR KEGG; mja:MJ_0611; -. DR eggNOG; arCOG00614; Archaea. DR eggNOG; COG1994; LUCA. DR InParanoid; Q58028; -. DR OMA; FIFHELA; -. DR PhylomeDB; Q58028; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0004222; F:metalloendopeptidase activity; IEA:InterPro. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Hydrolase; Membrane; Metal-binding; KW Metalloprotease; Protease; Reference proteome; Transmembrane; KW Transmembrane helix; Zinc. FT CHAIN 1 191 Putative zinc metalloprotease MJ0611. FT /FTId=PRO_0000106957. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 73 93 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT ACT_SITE 50 50 {ECO:0000250}. FT METAL 49 49 Zinc; catalytic. {ECO:0000250}. FT METAL 53 53 Zinc; catalytic. {ECO:0000250}. SQ SEQUENCE 191 AA; 21834 MW; 0F613A043DEF7DA9 CRC64; MSIFRFSQRE IIDLTISVLA IAFIFSYPNF SILVFIISLI AVGSGFIFHE LMHRTVARKY GAWSEFRAWY EGLILGFILK LVFGATFIAP GAVYIYKDYL TPEENGKIAL AGPLTNVALA FVFFILMLIF KPGSLLYWIG IFGFHINLFL AGFNMLPIPP FDGEKVLKWN PFIWAIVGLP LIGYMLYMMF W // ID Y623_METJA Reviewed; 192 AA. AC Q58040; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative metallophosphoesterase MJ0623; DE EC=3.1.4.-; GN OrderedLocusNames=MJ0623; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the metallophosphoesterase superfamily. CC YfcE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98618.1; -; Genomic_DNA. DR PIR; G64377; G64377. DR ProteinModelPortal; Q58040; -. DR STRING; 243232.MJ_0623; -. DR EnsemblBacteria; AAB98618; AAB98618; MJ_0623. DR KEGG; mja:MJ_0623; -. DR eggNOG; arCOG01141; Archaea. DR eggNOG; COG0622; LUCA. DR InParanoid; Q58040; -. DR KO; K07095; -. DR OMA; IIHCGDI; -. DR PhylomeDB; Q58040; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR020935; PdiEstase_YfcE_CS. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 1. DR Pfam; PF12850; Metallophos_2; 1. DR SUPFAM; SSF56300; SSF56300; 1. DR TIGRFAMs; TIGR00040; yfcE; 1. DR PROSITE; PS01269; UPF0025; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 192 Putative metallophosphoesterase MJ0623. FT /FTId=PRO_0000155611. SQ SEQUENCE 192 AA; 21361 MW; D56A8AC4287CE6D4 CRC64; MRDGEGIWGR GRTGGHAHPK EAMHTTFFIL GGTMLIGVIS DTHLYDRAFE LPKAVFDEFS NVDLIIHCGD VTDKEILDSL KDLAKVVAVK GNMDYLNLPR KEILEINDIK IGVIHGDVVY PRGDRLKLRL LGKEMGVDVL ISGHTHTPFI DDCRDILLLN PGSPTVPRCP LKSIMKLSVE DKLEAKLIPI EE // ID Y652_METJA Reviewed; 134 AA. AC Q58068; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Probable RNA-binding protein MJ0652; GN OrderedLocusNames=MJ0652; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 CRM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00626}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98643.1; -; Genomic_DNA. DR PIR; D64381; D64381. DR ProteinModelPortal; Q58068; -. DR STRING; 243232.MJ_0652; -. DR EnsemblBacteria; AAB98643; AAB98643; MJ_0652. DR KEGG; mja:MJ_0652; -. DR eggNOG; arCOG01346; Archaea. DR eggNOG; COG1534; LUCA. DR InParanoid; Q58068; -. DR KO; K07574; -. DR OMA; VRGKRFI; -. DR PhylomeDB; Q58068; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW. DR Gene3D; 3.30.110.60; -; 1. DR InterPro; IPR001890; RNA-binding_CRM. DR InterPro; IPR017924; RNA-binding_YhbY. DR Pfam; PF01985; CRS1_YhbY; 1. DR ProDom; PD010559; RNA-binding_CRM; 1. DR SMART; SM01103; CRS1_YhbY; 1. DR SUPFAM; SSF75471; SSF75471; 1. DR TIGRFAMs; TIGR00253; RNA_bind_YhbY; 1. DR PROSITE; PS51295; CRM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; RNA-binding. FT CHAIN 1 134 Probable RNA-binding protein MJ0652. FT /FTId=PRO_0000202169. FT DOMAIN 11 108 CRM. {ECO:0000255|PROSITE- FT ProRule:PRU00626}. FT COMPBIAS 85 89 Val-rich. FT COMPBIAS 103 133 Lys-rich. SQ SEQUENCE 134 AA; 15731 MW; 8183CEEB75B07A12 CRC64; MVIFMTEEQK RKLTGKMKRM LRAKAHHLEP VVWVGKEGSE KVIKEVDRQL KERGLIKVKV RKAALLYEDK YEIAEKLAKA CDAEVVSVVG HVITLFRPRE GWKKYLAKKP KKKVKKDEKI IELFEKFKKK AVKE // ID Y660_METJA Reviewed; 77 AA. AC Q58074; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0660; GN OrderedLocusNames=MJ0660; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 TRAM domain. {ECO:0000255|PROSITE- CC ProRule:PRU00208}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98653.1; -; Genomic_DNA. DR PIR; D64382; D64382. DR ProteinModelPortal; Q58074; -. DR SMR; Q58074; 17-77. DR STRING; 243232.MJ_0660; -. DR EnsemblBacteria; AAB98653; AAB98653; MJ_0660. DR KEGG; mja:MJ_0660; -. DR eggNOG; arCOG01641; Archaea. DR eggNOG; COG3269; LUCA. DR InParanoid; Q58074; -. DR OMA; FREESRP; -. DR PhylomeDB; Q58074; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002792; TRAM_dom. DR Pfam; PF01938; TRAM; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR PROSITE; PS50926; TRAM; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 77 Uncharacterized protein MJ0660. FT /FTId=PRO_0000106977. FT DOMAIN 20 77 TRAM. {ECO:0000255|PROSITE- FT ProRule:PRU00208}. SQ SEQUENCE 77 AA; 8631 MW; A8A2ED23F22F68C0 CRC64; MFNNKGRRNV RNNEVRRNVP VKEGETYTVT IEDMGRGGDG IARVEGFVVF VPETQKGETV NVKITAVKSK FAFAEKI // ID Y663_METJA Reviewed; 494 AA. AC Q58077; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized protein MJ0663; GN OrderedLocusNames=MJ0663; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the TPP enzyme family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98655.1; -; Genomic_DNA. DR PIR; G64382; G64382. DR ProteinModelPortal; Q58077; -. DR STRING; 243232.MJ_0663; -. DR EnsemblBacteria; AAB98655; AAB98655; MJ_0663. DR KEGG; mja:MJ_0663; -. DR eggNOG; arCOG02000; Archaea. DR eggNOG; COG0028; LUCA. DR InParanoid; Q58077; -. DR KO; K01652; -. DR OMA; IGVKFGC; -. DR PhylomeDB; Q58077; -. DR BioCyc; MetaCyc:MONOMER-14614; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0030976; F:thiamine pyrophosphate binding; IEA:InterPro. DR Gene3D; 3.40.50.1220; -; 1. DR Gene3D; 3.40.50.970; -; 2. DR InterPro; IPR029035; DHS-like_NAD/FAD-binding_dom. DR InterPro; IPR029061; THDP-binding. DR InterPro; IPR012000; Thiamin_PyroP_enz_cen_dom. DR InterPro; IPR012001; Thiamin_PyroP_enz_TPP-bd_dom. DR InterPro; IPR011766; TPP_enzyme-bd_C. DR Pfam; PF02775; TPP_enzyme_C; 1. DR Pfam; PF00205; TPP_enzyme_M; 1. DR Pfam; PF02776; TPP_enzyme_N; 1. DR SUPFAM; SSF52467; SSF52467; 1. DR SUPFAM; SSF52518; SSF52518; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Thiamine pyrophosphate. FT CHAIN 1 494 Uncharacterized protein MJ0663. FT /FTId=PRO_0000090834. SQ SEQUENCE 494 AA; 55355 MW; 1C62956C33D09D82 CRC64; MGGNIKFLEA MVDFLERNVK TIFSYPGEQI LPLYNEIEGS SIKNIMVRDE RGAGFMADGY ARITNYIGVC LATAGPGATN LTTPIATAYK DNSSVLAITG RCQRKYIGKN YFQEVNMDFL NFYKGYFVDK AEVSYIAKAF ADCLFNKKPV QLNIPVDLYK EEAKDINITT YTDIYKDDET PSNNIKEIDV KKPLFLIGQG IFGTLSYKEI VKISKILEKI NCPIATTFPA RGVINEKLEN CIGLVGRRGD LKSLLEADKI INIGSSLSYN TYVESVREKL LSKTENIQLK PKSIKELKEF FENLDVKNSS WIYKNSNKFQ PSGDYSNKIY EIIKNIPEDA IIVTDAGKHT VFTCLLKTCV IPRNIISSHS FGTMGFGLPA SIGVKFGTID FNIDREVVLI SGDGGFLMNV EELQVVAENN LKILMVVMKN NSLAEFCKIK NPNFNKIADA FEIDNCYIEN VDEIGSEIKG YLKKNKPLLV VVETENEPLP KPNI // ID Y670_METJA Reviewed; 356 AA. AC Q58084; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0670; GN OrderedLocusNames=MJ0670; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98664.1; -; Genomic_DNA. DR PIR; F64383; F64383. DR ProteinModelPortal; Q58084; -. DR STRING; 243232.MJ_0670; -. DR EnsemblBacteria; AAB98664; AAB98664; MJ_0670. DR KEGG; mja:MJ_0670; -. DR eggNOG; arCOG00120; Archaea. DR eggNOG; COG4121; LUCA. DR InParanoid; Q58084; -. DR OMA; CSGMGYN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016645; F:oxidoreductase activity, acting on the CH-NH group of donors; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR008471; MnmC-like_methylTransf. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF05430; Methyltransf_30; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 356 Uncharacterized protein MJ0670. FT /FTId=PRO_0000106983. SQ SEQUENCE 356 AA; 41684 MW; D7B8BA2E16A92E11 CRC64; MRVMLPNKKA LEIIRKYMKI YNGKNEKDIK ERLIKELKEE HVLVETEDGT YTLKAEDEEE MMHSKVGALK EAIYKFAKPS KITDLSNPRV LDLCSGMGYN AIAALHYNKN AEIDMVEICE EVLFLTLFLD IPYKEHEIIK DKVREYFLNK IGIEYKSDYD NINLYVGDAR KFIIKSDKKY NVVFHDAFSP KRDPTLYTYD FLKEIYKRME DNGVLISYSS AIPFRSALVD CGFVISEKES VGRKRGITLA YKNPNFKPNR INEVDERVIA LSVIALPYRD ETLSLTKDKI IEDREERREK LKEKLIKIGK YLSTKQIKKG NIPEEILKIQ KEDLNSSEII KKMRLKFFKD ANIFIL // ID Y690_METJA Reviewed; 200 AA. AC Q58102; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0690; GN OrderedLocusNames=MJ0690; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98685.1; -; Genomic_DNA. DR PIR; B64386; B64386. DR PDB; 3K32; X-ray; 2.50 A; A/B/C/D/E/F=1-200. DR PDBsum; 3K32; -. DR ProteinModelPortal; Q58102; -. DR STRING; 243232.MJ_0690; -. DR DNASU; 1451556; -. DR EnsemblBacteria; AAB98685; AAB98685; MJ_0690. DR KEGG; mja:MJ_0690; -. DR eggNOG; arCOG00037; Archaea. DR eggNOG; COG2117; LUCA. DR InParanoid; Q58102; -. DR KO; K07585; -. DR OMA; FYDVTLV; -. DR PhylomeDB; Q58102; -. DR EvolutionaryTrace; Q58102; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 200 Uncharacterized protein MJ0690. FT /FTId=PRO_0000106991. FT STRAND 4 9 {ECO:0000244|PDB:3K32}. FT HELIX 14 25 {ECO:0000244|PDB:3K32}. FT STRAND 28 36 {ECO:0000244|PDB:3K32}. FT STRAND 38 40 {ECO:0000244|PDB:3K32}. FT HELIX 44 53 {ECO:0000244|PDB:3K32}. FT STRAND 56 61 {ECO:0000244|PDB:3K32}. FT HELIX 65 77 {ECO:0000244|PDB:3K32}. FT STRAND 78 80 {ECO:0000244|PDB:3K32}. FT HELIX 81 95 {ECO:0000244|PDB:3K32}. FT TURN 96 98 {ECO:0000244|PDB:3K32}. FT STRAND 100 103 {ECO:0000244|PDB:3K32}. FT HELIX 117 127 {ECO:0000244|PDB:3K32}. FT STRAND 130 132 {ECO:0000244|PDB:3K32}. FT HELIX 134 137 {ECO:0000244|PDB:3K32}. FT HELIX 140 150 {ECO:0000244|PDB:3K32}. FT STRAND 151 156 {ECO:0000244|PDB:3K32}. FT STRAND 158 161 {ECO:0000244|PDB:3K32}. FT HELIX 167 177 {ECO:0000244|PDB:3K32}. FT HELIX 181 183 {ECO:0000244|PDB:3K32}. FT STRAND 190 198 {ECO:0000244|PDB:3K32}. SQ SEQUENCE 200 AA; 22905 MW; 14257CFBF3F59080 CRC64; MKLMDVHVLF SGGKDSSLSA VILKKLGYNP HLITINFGVI PSYKLAEETA KILGFKHKVI TLDRKIVEKA ADMIIEHKYP GPAIQYVHKT VLEILADEYS ILADGTRRDD RVPKLSYSEI QSLEMRKNIQ YITPLMGFGY KTLRHLASEF FILEEIKSGT KLSSDYEAEI RHILKERGES PEKYFPEHKQ TRVVGLKKEI // ID Y704_METJA Reviewed; 377 AA. AC Q58115; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0704; GN OrderedLocusNames=MJ0704; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98705.1; -; Genomic_DNA. DR PIR; H64387; H64387. DR STRING; 243232.MJ_0704; -. DR EnsemblBacteria; AAB98705; AAB98705; MJ_0704. DR KEGG; mja:MJ_0704; -. DR eggNOG; arCOG05096; Archaea. DR eggNOG; ENOG4112CFK; LUCA. DR OMA; YAVIKCL; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 377 Uncharacterized protein MJ0704. FT /FTId=PRO_0000106997. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. SQ SEQUENCE 377 AA; 44630 MW; 2746A0A96425C285 CRC64; MFAFEGFKWE IVEIFDWKGL KKLQTTFQNY LLILSMIVSI AVVVAIKNYD SLWSLITNSS DSSNFLTVGS ILATISALLV SISWVIIQTS SDRLSNILMW IWVRDVRFLT FVVISFTTVF LFILISLTHV QLHVIDYGII YYVIMLNFLM YALYIKAFAN VINPKYAVDL ILRDKDIGDK SGGYGDLTDA ESRLFAVYEI IEKRIKVGDV YAVIKCLNMI NKNFNKYWMF IKDEKREKYL RDFLRILSKL RVEYRKNCLN RKNKPYSKKG LEAFKKTEFI VSFYKTIEEK IKTRDINSIN KFLSETYNNI SNYEMFNDKT YLEIFVHHLK ELLEKYEKEK NENKLDEEIF NELKDELEKL INKCNNKLRE LESQNNN // ID Y709_METJA Reviewed; 450 AA. AC Q58119; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Uncharacterized transporter MJ0709; GN OrderedLocusNames=MJ0709; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the multi antimicrobial extrusion (MATE) CC (TC 2.A.66.1) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98703.1; -; Genomic_DNA. DR PIR; E64388; E64388. DR ProteinModelPortal; Q58119; -. DR STRING; 243232.MJ_0709; -. DR TCDB; 2.A.66.1.26; the multidrug/oligosaccharidyl-lipid/polysaccharide (mop) flippase superfamily. DR EnsemblBacteria; AAB98703; AAB98703; MJ_0709. DR KEGG; mja:MJ_0709; -. DR eggNOG; arCOG01731; Archaea. DR eggNOG; COG0534; LUCA. DR InParanoid; Q58119; -. DR OMA; NTIGYYV; -. DR PhylomeDB; Q58119; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015297; F:antiporter activity; IEA:InterPro. DR GO; GO:0015238; F:drug transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0006855; P:drug transmembrane transport; IBA:GO_Central. DR InterPro; IPR002528; MATE_fam. DR Pfam; PF01554; MatE; 2. DR PIRSF; PIRSF006603; DinF; 1. DR TIGRFAMs; TIGR00797; matE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 450 Uncharacterized transporter MJ0709. FT /FTId=PRO_0000164254. FT TRANSMEM 22 42 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 188 208 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 283 303 Helical. {ECO:0000255}. FT TRANSMEM 321 341 Helical. {ECO:0000255}. FT TRANSMEM 363 383 Helical. {ECO:0000255}. FT TRANSMEM 400 420 Helical. {ECO:0000255}. FT TRANSMEM 423 443 Helical. {ECO:0000255}. SQ SEQUENCE 450 AA; 48495 MW; 52EFE11132C4B79A CRC64; MKNVEILLDD PKKAVIEVSK PIIVATFIES IYSLVDSIWV SGLGADALAA VGASFPILIS IYAVSWGLSI GISSGIARRV GAKNKEEADK VANHAIILAL IAGILYIIAV YPNLDTLFSL MGTYGDCKSL AIKYSSILVL GTVIFTICDA LYGIFRGEGN TKIVMIASVI GTLTNIILDP IFIYMLNLGI SGASYATLIA IIISLLILAY ELFIKKSCYV TVKLSKFKPD LKIIADLIRV GIPSALIEIT VAVSFFIMTS IIMMVGDSRG LAVYTGALRI TEFGFIPMLG LASGATSVIG ATYGARSFEK LKTAYFYTIK IGVLMEIIIV ALIMLLSPIL AYLFTYTKTS MGIHEELVKA LRIVPLYLLF TPFILTTSAM FQGIGKGEKS LIISIFRSLI CHISYAYLFA VILGLGMFGI YSGLVVGEFT AGIFAFLFGV LAIKALIKSK // ID Y717_METJA Reviewed; 119 AA. AC Q58127; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0717; GN OrderedLocusNames=MJ0717; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To Synechocystis PCC 6803 slr0903. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98711.1; -; Genomic_DNA. DR PIR; E64389; E64389. DR ProteinModelPortal; Q58127; -. DR STRING; 243232.MJ_0717; -. DR EnsemblBacteria; AAB98711; AAB98711; MJ_0717. DR KEGG; mja:MJ_0717; -. DR eggNOG; arCOG00534; Archaea. DR eggNOG; COG0314; LUCA. DR InParanoid; Q58127; -. DR KO; K03635; -. DR OMA; FVREYDL; -. DR PhylomeDB; Q58127; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005829; C:cytosol; IBA:GO_Central. DR GO; GO:0030366; F:molybdopterin synthase activity; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:InterPro. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 3.90.1170.40; -; 1. DR InterPro; IPR003448; Mopterin_biosynth_MoaE. DR Pfam; PF02391; MoaE; 1. DR SUPFAM; SSF54690; SSF54690; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein MJ0717. FT /FTId=PRO_0000107002. SQ SEQUENCE 119 AA; 14062 MW; D9943113FBFC5B45 CRC64; MIFNEYEEFC KKMDECIEKY KGKFGCIVTF NGFVREYDLK DGEKVPSKGM KIDEDILEKL KLVIEEAKNK FDVIDILFYH NTGFLSIGER IASIAVFARH RKEGFEALEY IINEMKKYH // ID Y745_METJA Reviewed; 181 AA. AC Q58155; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0745; GN OrderedLocusNames=MJ0745; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98745.1; -; Genomic_DNA. DR PIR; A64393; A64393. DR ProteinModelPortal; Q58155; -. DR STRING; 243232.MJ_0745; -. DR EnsemblBacteria; AAB98745; AAB98745; MJ_0745. DR KEGG; mja:MJ_0745; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q58155; -. DR KO; K07013; -. DR OMA; ICYFDAG; -. DR PhylomeDB; Q58155; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 181 Uncharacterized protein MJ0745. FT /FTId=PRO_0000107012. SQ SEQUENCE 181 AA; 21150 MW; 9C25AA8EECF08DCE CRC64; MKNMRVELKT KDMKEFYKIF SESEFIITDD SKLINETVNY LKKKYKNSTT KKKLIPLDLF KAIVLIMMKK IKELDSEITL YDIGYEFGKH LNPKRYSDLK KFFKENNLGT LKVDSRKPLV LKVENCSFCE DLSFEEPICY FDAGLIAGAY ECILKKPVVV DEIKCMARGD DACYFKVEVV K // ID Y746_METJA Reviewed; 141 AA. AC Q58156; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 86. DE RecName: Full=Uncharacterized protein MJ0746; GN OrderedLocusNames=MJ0746; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 ferritin-like diiron domain. CC {ECO:0000255|PROSITE-ProRule:PRU00085}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98739.1; -; Genomic_DNA. DR PIR; B64393; B64393. DR ProteinModelPortal; Q58156; -. DR STRING; 243232.MJ_0746; -. DR EnsemblBacteria; AAB98739; AAB98739; MJ_0746. DR KEGG; mja:MJ_0746; -. DR eggNOG; arCOG01097; Archaea. DR eggNOG; COG1592; LUCA. DR InParanoid; Q58156; -. DR KO; K19824; -. DR OMA; FEGECKE; -. DR PhylomeDB; Q58156; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR009040; Ferritin-like_diiron. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR InterPro; IPR003251; Rubrerythrin. DR Pfam; PF02915; Rubrerythrin; 1. DR SUPFAM; SSF47240; SSF47240; 1. DR PROSITE; PS50905; FERRITIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Metal-binding; Reference proteome. FT CHAIN 1 141 Uncharacterized protein MJ0746. FT /FTId=PRO_0000135071. FT DOMAIN 13 141 Ferritin-like diiron. FT {ECO:0000255|PROSITE-ProRule:PRU00085}. FT METAL 63 63 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 66 66 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 125 125 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. FT METAL 128 128 Iron. {ECO:0000255|PROSITE- FT ProRule:PRU00085}. SQ SEQUENCE 141 AA; 15905 MW; 043E256886F34C07 CRC64; MELDLINEHK IGVTKGTELE KEVQANFEGE CKEVGLYLAM ARQAQREGLP EVAEVLIRIA MEEAQHAAHF AEMNGLISEN LKENIEMMLK GECMANKEKK AAATKAKELG IDPAHDFFDE SSRDEARHAK MLKGILDRYF K // ID Y751_METJA Reviewed; 278 AA. AC Q58161; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Putative transposase MJ0751; GN OrderedLocusNames=MJ0751; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: In the N-terminal section; belongs to the transposase CC 2 family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the transposase CC 35 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98747.1; -; Genomic_DNA. DR PIR; G64393; G64393. DR STRING; 243232.MJ_0751; -. DR EnsemblBacteria; AAB98747; AAB98747; MJ_0751. DR KEGG; mja:MJ_0751; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR InParanoid; Q58161; -. DR KO; K07496; -. DR OMA; IMTIDIN; -. DR PhylomeDB; Q58161; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. DR TIGRFAMs; TIGR01766; tspaseT_teng_C; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Metal-binding; KW Reference proteome; Transposable element; Transposition; Zinc. FT CHAIN 1 278 Putative transposase MJ0751. FT /FTId=PRO_0000107013. FT METAL 222 222 Zinc. {ECO:0000255}. FT METAL 225 225 Zinc. {ECO:0000255}. FT METAL 239 239 Zinc. {ECO:0000255}. FT METAL 242 242 Zinc. {ECO:0000255}. SQ SEQUENCE 278 AA; 32990 MW; B4EFAFF1893A58B3 CRC64; MLFKFEGDKI KIITAPRKFI TINLVVSDYQ KKFIEEWKNG NFKIGEVIIK KDSIIIPFKK VVNPKNFEHI MTIDINEKNI TYSIFDKDGN VIKTTRLDVY KLKRIHENFS KKREKIQKKL SNKPMKLKTL MEKYSGREKR KVEDYLHKIS KFLISEALKY NVKILMEDLT NIREAVNKKS KNFRRRLNRW NFSKLQFFIE YKAKWDGLDV EYVNPSRTSK LCPICGCKLD PNGQRLLKCN NCNLVFDRDV VATFNLFKKS QDVGSFRSPE RSLMKSSY // ID Y759_METJA Reviewed; 118 AA. AC Q58169; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0759; GN OrderedLocusNames=MJ0759; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98750.1; -; Genomic_DNA. DR PIR; G64394; G64394. DR ProteinModelPortal; Q58169; -. DR STRING; 243232.MJ_0759; -. DR EnsemblBacteria; AAB98750; AAB98750; MJ_0759. DR KEGG; mja:MJ_0759; -. DR eggNOG; arCOG04884; Archaea. DR eggNOG; ENOG4112AS4; LUCA. DR OMA; GMRLMPH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 118 Uncharacterized protein MJ0759. FT /FTId=PRO_0000107018. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. SQ SEQUENCE 118 AA; 12908 MW; DDC37AA7855ACACE CRC64; MVIKKGEIMN EIISLVSLSV IFGAMLSGFA TFRLTGMRLM PHFASLMIAF ILTLASLFIS NNIIGYLAIA FQVITPLTVC PTICNILKTQ FQNTGIYSAH LALMGMMFIL ALGNVILF // ID Y806_METJA Reviewed; 347 AA. AC Q58216; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 99. DE RecName: Full=Uncharacterized peptidase MJ0806; DE EC=3.4.-.-; GN OrderedLocusNames=MJ0806; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000305}; CC Note=Binds 2 manganese ions per subunit. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the peptidase M24B family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98806.1; -; Genomic_DNA. DR PIR; F64400; F64400. DR ProteinModelPortal; Q58216; -. DR STRING; 243232.MJ_0806; -. DR EnsemblBacteria; AAB98806; AAB98806; MJ_0806. DR KEGG; mja:MJ_0806; -. DR eggNOG; arCOG01000; Archaea. DR eggNOG; COG0006; LUCA. DR InParanoid; Q58216; -. DR KO; K01271; -. DR OMA; GEPNKEA; -. DR PhylomeDB; Q58216; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.350.10; -; 1. DR Gene3D; 3.90.230.10; -; 1. DR InterPro; IPR029149; Creatin/AminoP/Spt16_NTD. DR InterPro; IPR028980; Creatinase/Aminopeptidase_P_N. DR InterPro; IPR000587; Creatinase_N. DR InterPro; IPR001714; Pept_M24_MAP. DR InterPro; IPR000994; Pept_M24_structural-domain. DR InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS. DR Pfam; PF01321; Creatinase_N; 1. DR Pfam; PF00557; Peptidase_M24; 1. DR PRINTS; PR00599; MAPEPTIDASE. DR SUPFAM; SSF53092; SSF53092; 1. DR SUPFAM; SSF55920; SSF55920; 1. DR PROSITE; PS00491; PROLINE_PEPTIDASE; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Manganese; Metal-binding; KW Reference proteome. FT CHAIN 1 347 Uncharacterized peptidase MJ0806. FT /FTId=PRO_0000185104. FT METAL 207 207 Manganese 2. {ECO:0000255}. FT METAL 218 218 Manganese 1. {ECO:0000255}. FT METAL 218 218 Manganese 2. {ECO:0000255}. FT METAL 279 279 Manganese 1. {ECO:0000255}. FT METAL 312 312 Manganese 1. {ECO:0000255}. FT METAL 326 326 Manganese 1. {ECO:0000255}. FT METAL 326 326 Manganese 2. {ECO:0000255}. SQ SEQUENCE 347 AA; 40549 MW; 60A4AA7224217C4D CRC64; MQKTIGDIMN NRIERFLKYM ESEGIKKAVI LKKENINYFL GKYFMSFSVL VFEEQPYLYV GKLDKDYAEE HFNFLEIREF KSWEEIFKGC DGVEKELSIG YLKYIDKEYK IISDKIKEMR MIKDKEEIKL IKKAAEISDK AINWVLNNLD EVKNLTEYEL VAEIEYIMKK HGSIKPAFDS IVVSGKKTSF PHALPTKDKI ADILLVDIGA VYEGYCSDIT RTFLLKDDEE MKKIYNLVYE AKKVAEEHLK EGISAKQIDN IVREFFNDYK ELFIHSLGHG VGLEVHEEPR LSNKLKDDED IILKEGMVVT IEPGLYLKDK FGVRIEDLYL VKKNGFEKLS KAEISEY // ID Y810_METJA Reviewed; 201 AA. AC Q58220; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2003, sequence version 2. DT 11-NOV-2015, entry version 85. DE RecName: Full=Protein MJ0810 {ECO:0000255|HAMAP-Rule:MF_00645}; GN OrderedLocusNames=MJ0810; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 AMMECR1 domain. {ECO:0000255|HAMAP- CC Rule:MF_00645}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98809.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98809.1; ALT_INIT; Genomic_DNA. DR PIR; B64401; B64401. DR ProteinModelPortal; Q58220; -. DR SMR; Q58220; 7-200. DR STRING; 243232.MJ_0810; -. DR EnsemblBacteria; AAB98809; AAB98809; MJ_0810. DR KEGG; mja:MJ_0810; -. DR eggNOG; arCOG01336; Archaea. DR eggNOG; COG2078; LUCA. DR InParanoid; Q58220; -. DR KO; K09141; -. DR OMA; TCWKAGL; -. DR PhylomeDB; Q58220; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.700.20; -; 1. DR HAMAP; MF_00645; AMMECR1; 1. DR InterPro; IPR023473; AMMECR1. DR InterPro; IPR002733; AMMECR1_domain. DR InterPro; IPR027485; AMMECR1_N. DR InterPro; IPR027623; AmmeMemoSam_A. DR InterPro; IPR023472; Uncharacterised_MJ0810. DR PANTHER; PTHR13016; PTHR13016; 1. DR Pfam; PF01871; AMMECR1; 1. DR SUPFAM; SSF143447; SSF143447; 1. DR TIGRFAMs; TIGR04335; AmmeMemoSam_A; 1. DR TIGRFAMs; TIGR00296; TIGR00296; 1. DR PROSITE; PS51112; AMMECR1; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 201 Protein MJ0810. FT /FTId=PRO_0000142377. FT DOMAIN 7 197 AMMECR1. {ECO:0000255|HAMAP- FT Rule:MF_00645}. SQ SEQUENCE 201 AA; 22936 MW; E5C68B8FE4609B76 CRC64; MRLLTLEEGT FAVRYARAVI ENYLAGKKIV IESYPEVFNE KRGCFCTLHT YPDKELRGCI GIPEPIMPLI EALEEAAISA ATKDPRFPPV TLEEMDSIVV EVSILTPPEL IKVNHPKEYL EKIKIGRDGL IIEYGFYRGL LLPQVPVEYG WDVEEYLAHL CLKAGLPPDM WLAEGVKIYR FEAQIFEEVE PRGEVIEKKL L // ID Y811_METJA Reviewed; 439 AA. AC Q58221; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0811; GN OrderedLocusNames=MJ0811; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 VWFA domain. {ECO:0000255|PROSITE- CC ProRule:PRU00219}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98810.1; -; Genomic_DNA. DR PIR; C64401; C64401. DR ProteinModelPortal; Q58221; -. DR STRING; 243232.MJ_0811; -. DR EnsemblBacteria; AAB98810; AAB98810; MJ_0811. DR KEGG; mja:MJ_0811; -. DR eggNOG; arCOG00442; Archaea. DR eggNOG; COG2425; LUCA. DR InParanoid; Q58221; -. DR OMA; CEKFFEN; -. DR PhylomeDB; Q58221; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.410; -; 1. DR InterPro; IPR002035; VWF_A. DR SMART; SM00327; VWA; 1. DR SUPFAM; SSF53300; SSF53300; 1. DR PROSITE; PS50234; VWFA; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 439 Uncharacterized protein MJ0811. FT /FTId=PRO_0000107059. FT DOMAIN 273 439 VWFA. {ECO:0000255|PROSITE- FT ProRule:PRU00219}. SQ SEQUENCE 439 AA; 51119 MW; 2F85F2B942C1CDFD CRC64; MKNIIKHDAY DKKAYERFLK NSKYLQKLIS YYSQYHPIHE KLAEDTFYAF FKYVVEFNEY VEEKFKINKA ILEGAIKNIE YEKSKLLTEL DEVNAGTATI MFCEKFFENL KLAKLNKELK KFASEGKGEG LEDKLKEIAK NTMKDIAEEV SEVIQGFNAV ENFGKGEGDK KLLSPEDRIK LADKILQNKK IREIVKKLGK LRLLAINEYK SKIKHYSGEI YSTKIGRDLK HLLPKEIVNL SDEILYYDFL RRFVDKKLLI YDIQNKLEKQ KGPIIILLDH SGSMYGDREI WGKAVALSII EIAKRENRDI YYIAFDDGVR FEKKINPKTI TFDEIIEIAS LYFGGGTNFI MPLNRAMSII KEHETFKNAD ILLITDGYAE VNDVFLKEFD KFKNEYNAKL ISVFVETFPT ETLKAISDEV IKVYDLADEE ARKIYKSIS // ID Y816_METJA Reviewed; 297 AA. AC Q58226; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0816; GN OrderedLocusNames=MJ0816; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98818.1; -; Genomic_DNA. DR PIR; H64401; H64401. DR ProteinModelPortal; Q58226; -. DR STRING; 243232.MJ_0816; -. DR EnsemblBacteria; AAB98818; AAB98818; MJ_0816. DR KEGG; mja:MJ_0816; -. DR eggNOG; arCOG04823; Archaea. DR eggNOG; ENOG410YGYX; LUCA. DR OMA; LCIQSCK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 297 Uncharacterized protein MJ0816. FT /FTId=PRO_0000107061. SQ SEQUENCE 297 AA; 34913 MW; 724C69341CB90230 CRC64; MQDKQLLQLK EQIINDIKKR VLKIREDLGL KKVEFDIVDI EIEGKVLIIY TKNRTDKSTI IGPGGWVVGK LREEMKNRFE IIRVEDYTDK VLFEEIVKAI KSLFDDEVIQ DICNYFLYRK IPKEKKNIIC LIHCQYDLYA LDILSNIFNV KAITYDFPAL IPNKTKKKIA NFLNNKDIGH KFLKLDITKD KIKNLIDSFP YGFLKDKIIE DLEGYVFTSC LDTAVFKYNK GTIINFFELF PIKIKKDENY LNYCPLCIQS CKIDKNKEKF IKKVVKEVYK GFKEPTDASE EILSMIK // ID Y819_METJA Reviewed; 109 AA. AC Q58229; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 69. DE RecName: Full=Putative uncharacterized protein MJ0819; GN OrderedLocusNames=MJ0819; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. MJ0821, MJ0820 and CC MJ0819 respectively represent the N-terminal, central and C- CC terminal sections of other members of this family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98831.1; -; Genomic_DNA. DR PIR; C64402; C64402. DR ProteinModelPortal; Q58229; -. DR SMR; Q58229; 18-109. DR STRING; 243232.MJ_0819; -. DR EnsemblBacteria; AAB98831; AAB98831; MJ_0819. DR KEGG; mja:MJ_0819; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Putative uncharacterized protein MJ0819. FT /FTId=PRO_0000184681. SQ SEQUENCE 109 AA; 13065 MW; C72C396D1BF6EC9A CRC64; MLVGSQLIEI VIDSLRYENL KEILDEMFRD EVQKLKYFLE DVKEEDEELY NKIVDALKLF KENYEIEDIK IPKKIRVFLV KNNILFLNPQ KGSLKPQSYL VWNAIKMLL // ID Y835_METJA Reviewed; 377 AA. AC Q58245; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0835; GN OrderedLocusNames=MJ0835; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98838.1; -; Genomic_DNA. DR PIR; C64404; C64404. DR ProteinModelPortal; Q58245; -. DR STRING; 243232.MJ_0835; -. DR EnsemblBacteria; AAB98838; AAB98838; MJ_0835. DR KEGG; mja:MJ_0835; -. DR eggNOG; arCOG03421; Archaea. DR eggNOG; COG1627; LUCA. DR OMA; NTQIFDE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007509; DUF515. DR Pfam; PF04415; DUF515; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 377 Uncharacterized protein MJ0835. FT /FTId=PRO_0000107070. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 251 271 Helical. {ECO:0000255}. SQ SEQUENCE 377 AA; 42951 MW; FC2920714DE90FA9 CRC64; MVDTSKIKAL KEKSRRTVKS GSLKFILIIL VVVIVGLLAF IAYNEISNLQ FQEKITLENQ KKAAIESINQ MFAKYPNDPQ KLIYINKIQM ANNIEEINEV LEEAKKYISF KNYKIEAINQ IKSMYGEYYS LSLSAQELVH KISLAQSTEE IENLLKSVDI EKDIRSIIEK QIDYVLASGD KYYYVEINGK SMFMTRDEIL KYKKFWTLSE LKSLKITPVS QLNKVAIEIS AKQCGKLPHK GDIISIYSKD GSFITYGIID SSYVILSSIS YSESKSTSSN INELGESYSS SSSSSISYSL NNLPGILHAT VIDRLDYDKI KKMFGEYGKK LNEIEDDTQI FDENVNYFLI ISIPDDKIPD IIQIDPKDIV IVIKSKE // ID Y836_METJA Reviewed; 119 AA. AC Q58246; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0836; GN OrderedLocusNames=MJ0836; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98839.1; -; Genomic_DNA. DR PIR; D64404; D64404. DR STRING; 243232.MJ_0836; -. DR EnsemblBacteria; AAB98839; AAB98839; MJ_0836. DR KEGG; mja:MJ_0836; -. DR eggNOG; arCOG05056; Archaea. DR eggNOG; COG2158; LUCA. DR KO; K07162; -. DR OMA; LWCYCPF; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007212; Zf-like. DR Pfam; PF04071; zf-like; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 119 Uncharacterized protein MJ0836. FT /FTId=PRO_0000107073. SQ SEQUENCE 119 AA; 14176 MW; 196AB7DB9B52BC83 CRC64; MIELAKNHLK KVLEVCGANR NCEYYPCHFD GQVCLWCYCP FYPCEDEELG EYVEKKDGTK IWSCMKCFWV HREDVATEIL REILNLTKDK DIDEALKLLD NHELMLKIKD RVKAKYPNR // ID Y83A_METJA Reviewed; 142 AA. AC P81322; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=UPF0333 protein MJ0832.1; GN OrderedLocusNames=MJ0832.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0333 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98840.1; -; Genomic_DNA. DR STRING; 243232.MJ_0832.1; -. DR EnsemblBacteria; AAB98840; AAB98840; MJ_0832.1. DR KEGG; mja:MJ_0832.1; -. DR eggNOG; arCOG05053; Archaea. DR eggNOG; COG1991; LUCA. DR OMA; QVSVEFI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR Pfam; PF04021; Class_IIIsignal; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 142 UPF0333 protein MJ0832.1. FT /FTId=PRO_0000218266. FT TRANSMEM 17 37 Helical. {ECO:0000255}. SQ SEQUENCE 142 AA; 15689 MW; A76E07F498D74FC0 CRC64; MLKFRKRGQI SLEFSLLFLG VLLAIVIAVG YPGMFGFNKT VSISSMSLAH AAVSKMKQNI ELVSSADEGT MKIVYIKCPP GTWGANNNIL YFYRDGNIKF NITAKCDINI ILNGNKTVST PKIIIANITK IDETHVIVTL YQ // ID Y841_METJA Reviewed; 415 AA. AC Q58251; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized protein MJ0841; GN OrderedLocusNames=MJ0841; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98846.1; -; Genomic_DNA. DR PIR; A64405; A64405. DR ProteinModelPortal; Q58251; -. DR STRING; 243232.MJ_0841; -. DR DNASU; 1451729; -. DR EnsemblBacteria; AAB98846; AAB98846; MJ_0841. DR KEGG; mja:MJ_0841; -. DR eggNOG; arCOG00950; Archaea. DR eggNOG; COG1625; LUCA. DR InParanoid; Q58251; -. DR OMA; KGCDYCT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR017672; Methan_mark_10. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR TIGRFAMs; TIGR03278; methan_mark_10; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 415 Uncharacterized protein MJ0841. FT /FTId=PRO_0000107078. FT METAL 18 18 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 22 22 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 25 25 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 415 AA; 46721 MW; 0F67E63793A587F1 CRC64; MKEANLLIDL RGEPGINCNG FCKFCYFRKV NKNNPQPFGC RYCQFTVGCD YCMYSVREIN GDFIPLPFAL MELQSSLLFK RYSKVNLTAG GDVSCYPQLE ELCKAINNIG LKIHLGYTSG KGFDNVEIAK NLVDYGVDEV TFSVFSTNPK LRKEWMNDKN AETALKCLRY FCENCEVHCA IIVIPGVNDG EELKKTVSDL VDWGANAVIL MRFANSEEQG LILGNAPLIE GIKPHSVEEF KNIVDEIHNE FGDYIRVTGT PLHDPVAGTP FALAKEENSH ILERLKDKIN GEATIITGNV AYPFLKKIFD ETSVNVVKVN KDIADLITAK DLEKLDLKDV KETVFIPPKA FVHDRVAEEI LRRDGVDRIV VRGVEQLTLD GEVSGIYTRE EALKFEIEAF EELIGMINFF GMKKQ // ID Y855_METJA Reviewed; 228 AA. AC Q58265; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0855; GN OrderedLocusNames=MJ0855; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98862.1; -; Genomic_DNA. DR PIR; G64406; G64406. DR ProteinModelPortal; Q58265; -. DR PRIDE; Q58265; -. DR EnsemblBacteria; AAB98862; AAB98862; MJ_0855. DR KEGG; mja:MJ_0855; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q58265; -. DR KO; K07013; -. DR OMA; CYLTAGF; -. DR PhylomeDB; Q58265; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019642; DUF2507. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF10702; DUF2507; 1. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 228 Uncharacterized protein MJ0855. FT /FTId=PRO_0000107079. SQ SEQUENCE 228 AA; 26405 MW; 0064010139B99F9A CRC64; MTNAMKIIEM LRIIDNRAKF MGIKLTMMKN LLEKYKDNKE LLKEVLKLTE GTRLHELILE AYPPLEELKK EIREEEHKIK ITSESGGEEK KEFCTFEGPV SLIAYIKEYL RKYYLGNNVK RIFYDIGKDY AIKLGINTYD DMITFMKKDF GEVVIEKSEP LTVVVKDNKE CKNCKASEPI CYLTAGFIAG CLENMTNKTY IVEVTEEKCQ AVGDPYCTFV AKKSIRLD // ID Y859_METJA Reviewed; 164 AA. AC Q58269; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0859; GN OrderedLocusNames=MJ0859; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98874.1; -; Genomic_DNA. DR PIR; C64407; C64407. DR ProteinModelPortal; Q58269; -. DR SMR; Q58269; 2-156. DR STRING; 243232.MJ_0859; -. DR EnsemblBacteria; AAB98874; AAB98874; MJ_0859. DR KEGG; mja:MJ_0859; -. DR eggNOG; arCOG01724; Archaea. DR eggNOG; COG4072; LUCA. DR InParanoid; Q58269; -. DR OMA; LYVENAE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019217; DUF2118. DR Pfam; PF09891; DUF2118; 1. DR PIRSF; PIRSF019115; UCP019115; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 164 Uncharacterized protein MJ0859. FT /FTId=PRO_0000107084. SQ SEQUENCE 164 AA; 18986 MW; D1C3930A857C2366 CRC64; MNIMRIPRLY VENAEKHEGR KVVIENGGKV IKFLDKDEEY EGDGKVLYQV IYDDFDNYVL MGTVTKDMII EYEVGGVRQI TYIKKGTKLL EIPAEGYKVY PIVDFGCRIL GGHRIAALQS RKGDIRFVNT PVNGIVLFLK EVPAKRENYV FYILPEEEIK FEEE // ID Y868_METJA Reviewed; 127 AA. AC Q58278; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0868; GN OrderedLocusNames=MJ0868; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98873.1; -; Genomic_DNA. DR PIR; D64408; D64408. DR ProteinModelPortal; Q58278; -. DR STRING; 243232.MJ_0868; -. DR EnsemblBacteria; AAB98873; AAB98873; MJ_0868. DR KEGG; mja:MJ_0868; -. DR eggNOG; ENOG4102TZI; Archaea. DR eggNOG; ENOG410XUIV; LUCA. DR InParanoid; Q58278; -. DR OMA; TMAKYDI; -. DR PhylomeDB; Q58278; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 127 Uncharacterized protein MJ0868. FT /FTId=PRO_0000107085. FT DOMAIN 11 68 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 71 127 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 127 AA; 14173 MW; 12B55235ADFE14D3 CRC64; MISKYLVRDV MKKGVVEVTL DTKLSDVIKT MAKYDISSVV VSDGETFWGI ITDTDVLKHY NDLDKTAEEI MTTNPITVSP EAPLEKAVEI MAEKGIHHLY VKSPCEDKIV GVLSSKDIIK LFSDLIE // ID Y877_METJA Reviewed; 123 AA. AC Q58287; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Putative ABC transporter permease protein MJ0877; GN OrderedLocusNames=MJ0877; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR PIR; E64409; E64409. DR ProteinModelPortal; Q58287; -. DR InParanoid; Q58287; -. DR PhylomeDB; Q58287; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 123 Putative ABC transporter permease protein FT MJ0877. FT /FTId=PRO_0000060307. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. SQ SEQUENCE 123 AA; 13107 MW; BE821011FE767D86 CRC64; MDANLLGEKY AISVGVDIKS LRMWLIILSC VLTATVVAFT GPIAFVGITC PILARMICGT SKHIYVIPVT MLLGAVFLVV ADILTRPGVL ISSTNVLPLL CPLSIIGAPI AIIIYLKIRK MGI // ID Y903_METJA Reviewed; 643 AA. AC Q58313; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0903; GN OrderedLocusNames=MJ0903; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98908.1; -; Genomic_DNA. DR PIR; G64412; G64412. DR ProteinModelPortal; Q58313; -. DR STRING; 243232.MJ_0903; -. DR EnsemblBacteria; AAB98908; AAB98908; MJ_0903. DR KEGG; mja:MJ_0903; -. DR eggNOG; arCOG05057; Archaea. DR eggNOG; ENOG410YACR; LUCA. DR OMA; YEVKTWI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 643 Uncharacterized protein MJ0903. FT /FTId=PRO_0000107095. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT COMPBIAS 2 5 Poly-Gly. FT COMPBIAS 11 18 Poly-Leu. SQ SEQUENCE 643 AA; 72968 MW; 8FBD01772DBD88DD CRC64; MGGGGMKKIV LALLLLLLPV VCGDVSVYKV WSPYDPPNSP ILHVDISEQV LYLGVVNKDE YEHDVIVKVE CNGKTWGSGL IPLPPNSHIE KIVEVRVPIS DDKEHDAKIS LIENGKTIAS TTVKVRPYFP VDVKNVTCED SYKIGNTEVC YSNWFDITLK SNPTAKSDYI AKVWINVKDG DNIIYNGKND FKTVYIPLGE EVTVSFKVPK IVLDKEKFTV ETNVEIMNVT HTIDGVEETI QRRDDSGIYY DYKSVTKYYY FPVVIKNVEL YRKIDENTSE FVKNFYDSAN ILDDEIRDIL SDKYLQKDDV LPRYYVIDDP TLAILKITVE NKYDRDVKAK LTVKYDNVIF TKIINIDKKE KKDVFIPIYT KKGSKNIVVT INPIDADTLI FNRSYSINID PKPIPPVIIE KIILPKDEEI GEETNISGYV IIGKRYNMTI FIKNIYNKTL SGKITIDDNF KDGIANYSKE IPFTIEPHQI KEINVPIIFY KEVNGDLKIT VSVKGGAKDY TSLAHFYAIS PIGIVRIYYN NTLLLGKINV IKENSGIYSA KPIAGFNNTC VVILRNNLNS KVDCDVWIEV IDKDGKVRAK SGIKTVKLDN YSEAKVAFPI FFEEGFEGYT VAHIIPKSVE NVDIIYTEVM EST // ID Y922_METJA Reviewed; 138 AA. AC Q58332; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0922; GN OrderedLocusNames=MJ0922; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98926.1; -; Genomic_DNA. DR PIR; B64415; B64415. DR PDB; 2P9M; X-ray; 2.59 A; A/B/C/D=1-138. DR PDBsum; 2P9M; -. DR ProteinModelPortal; Q58332; -. DR SMR; Q58332; 4-137. DR STRING; 243232.MJ_0922; -. DR EnsemblBacteria; AAB98926; AAB98926; MJ_0922. DR KEGG; mja:MJ_0922; -. DR eggNOG; arCOG00606; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q58332; -. DR OMA; DIMSSDV; -. DR PhylomeDB; Q58332; -. DR EvolutionaryTrace; Q58332; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 1: Evidence at protein level; KW 3D-structure; CBS domain; Complete proteome; Reference proteome; KW Repeat. FT CHAIN 1 138 Uncharacterized protein MJ0922. FT /FTId=PRO_0000107107. FT DOMAIN 14 70 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 79 138 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT HELIX 10 12 {ECO:0000244|PDB:2P9M}. FT HELIX 27 37 {ECO:0000244|PDB:2P9M}. FT STRAND 41 45 {ECO:0000244|PDB:2P9M}. FT STRAND 50 56 {ECO:0000244|PDB:2P9M}. FT HELIX 57 64 {ECO:0000244|PDB:2P9M}. FT TURN 65 67 {ECO:0000244|PDB:2P9M}. FT HELIX 75 78 {ECO:0000244|PDB:2P9M}. FT HELIX 92 99 {ECO:0000244|PDB:2P9M}. FT STRAND 111 115 {ECO:0000244|PDB:2P9M}. FT STRAND 119 126 {ECO:0000244|PDB:2P9M}. FT HELIX 127 136 {ECO:0000244|PDB:2P9M}. SQ SEQUENCE 138 AA; 15469 MW; CCBFFA3534EB48D0 CRC64; MIDTLKNIKV KDVMTKNVIT AKRHEGVVEA FEKMLKYKIS SLPVIDDENK VIGIVTTTDI GYNLIRDKYT LETTIGDVMT KDVITIHEDA SILEAIKKMD ISGKKEEIIN QLPVVDKNNK LVGIISDGDI IRTISKII // ID Y949_METJA Reviewed; 123 AA. AC Q58359; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0949; GN OrderedLocusNames=MJ0949; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98950.1; -; Genomic_DNA. DR PIR; E64418; E64418. DR STRING; 243232.MJ_0949; -. DR EnsemblBacteria; AAB98950; AAB98950; MJ_0949. DR KEGG; mja:MJ_0949; -. DR eggNOG; arCOG04842; Archaea. DR eggNOG; COG1844; LUCA. DR InParanoid; Q58359; -. DR KO; K09727; -. DR OMA; HPPAHII; -. DR PhylomeDB; Q58359; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd. DR InterPro; IPR007154; DUF356. DR Pfam; PF04009; DUF356; 1. DR PIRSF; PIRSF006606; UCP006606; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 123 Uncharacterized protein MJ0949. FT /FTId=PRO_0000107118. FT COMPBIAS 113 123 Poly-Lys. SQ SEQUENCE 123 AA; 13959 MW; DA8F66F87739E34B CRC64; MTILLIRGDS YEKLKNALAD VDRHAELTII GKPKIIVPEA ADEILSHILG EVKKPCKTAC LAKIAEKAPK AIDRIRKIHP PAHIVVISER YGDIYYKLLD DFPKLPVLKG YYKSKKKDKK KKK // ID Y981_METJA Reviewed; 204 AA. AC Q58390; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0981; GN OrderedLocusNames=MJ0981; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98984.1; -; Genomic_DNA. DR PIR; E64422; E64422. DR ProteinModelPortal; Q58390; -. DR STRING; 243232.MJ_0981; -. DR EnsemblBacteria; AAB98984; AAB98984; MJ_0981. DR KEGG; mja:MJ_0981; -. DR eggNOG; arCOG02680; Archaea. DR eggNOG; COG1326; LUCA. DR InParanoid; Q58390; -. DR OMA; KHERSFR; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR InterPro; IPR012041; UCP015877_Znf. DR InterPro; IPR007853; Znf_DNL-typ. DR Pfam; PF05180; zf-DNL; 1. DR PIRSF; PIRSF015877; UCP015877; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 204 Uncharacterized protein MJ0981. FT /FTId=PRO_0000107129. FT COMPBIAS 23 29 Lys-rich. FT COMPBIAS 163 181 Lys-rich. SQ SEQUENCE 204 AA; 23595 MW; 6AB7CA2A26421FB6 CRC64; MEMTEKIYLK CENCGFEEQE VLKKKIYNKS AYYLVRCPNC GSVREIVDKV KLSQAKLIIS RYDISESKVI NIPEDETYKV GDTIEIDGEK IEITKIETPE SVKSALGEDI KVIWGKSLSI PKKLGISIND RSKTYGIYIY VPNDFEFEVE KVYRINDGFF RLKKIKTEKG TAKKAKAKDI KRLYGDVTRP VRNYVDLSEF YKGE // ID YB5B_METJA Reviewed; 73 AA. AC P81317; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ1155.2; GN OrderedLocusNames=MJ1155.2; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99160.1; -; Genomic_DNA. DR STRING; 243232.MJ_1155.2; -. DR EnsemblBacteria; AAB99160; AAB99160; MJ_1155.2. DR KEGG; mja:MJ_1155.2; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 73 Uncharacterized protein MJ1155.2. FT /FTId=PRO_0000107195. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 47 67 Helical. {ECO:0000255}. SQ SEQUENCE 73 AA; 7963 MW; FB33C20926CA058A CRC64; MILDKTLFSS LTFSLTVLFL LLLIPNLKGF GKLSAIIGGF IALIFQYFGY PSLGILFAGI LSPIIILKIK SVK // ID Y233_METJA Reviewed; 277 AA. AC Q57685; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0233; GN OrderedLocusNames=MJ0233; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1189. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98226.1; -; Genomic_DNA. DR PIR; B64329; B64329. DR ProteinModelPortal; Q57685; -. DR STRING; 243232.MJ_0233; -. DR EnsemblBacteria; AAB98226; AAB98226; MJ_0233. DR KEGG; mja:MJ_0233; -. DR eggNOG; arCOG02880; Archaea. DR eggNOG; ENOG410Z0NF; LUCA. DR OMA; WFYSKLA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR025098; DUF4013. DR Pfam; PF13197; DUF4013; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 277 Uncharacterized protein MJ0233. FT /FTId=PRO_0000106753. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 61 81 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. FT TRANSMEM 144 164 Helical. {ECO:0000255}. FT TRANSMEM 197 217 Helical. {ECO:0000255}. FT TRANSMEM 221 241 Helical. {ECO:0000255}. FT TRANSMEM 243 263 Helical. {ECO:0000255}. SQ SEQUENCE 277 AA; 31307 MW; 31F66D38BD552B39 CRC64; MGTIESYLTN SYNYIIFNFK KLCIGGLMSA IVGAMSGVTT AFIDLFMERA NYDIMHIIMS FLIYFGIIFI IGLIVSAIIG GYNVRIMKTT VEGLNVAPDW NNITDLLYRG ILYIVGLVLL NIIFYFIPAI LFVFGIFSLY ISKIIGAFLI IISILIFIIS VISLWLYSKL AEVNYSVKGF YGFFEFKEIF KMIGIRYIIL VIIIAIINFI ISLIVVLPLN IIDIFISYSA LANSILTIIY ISIKGISYAL STFVDFYLGV FSIRAVALYY KDRKGIT // ID Y239_METJA Reviewed; 164 AA. AC Q57691; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0239; GN OrderedLocusNames=MJ0239; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98228.1; -; Genomic_DNA. DR PIR; H64329; H64329. DR STRING; 243232.MJ_0239; -. DR EnsemblBacteria; AAB98228; AAB98228; MJ_0239. DR KEGG; mja:MJ_0239; -. DR eggNOG; arCOG05026; Archaea. DR eggNOG; ENOG410YHWP; LUCA. DR OMA; ITARINC; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 164 Uncharacterized protein MJ0239. FT /FTId=PRO_0000106756. FT COMPBIAS 19 83 Asp/Leu/Lys-rich. SQ SEQUENCE 164 AA; 19548 MW; 4E62BF73D6E64389 CRC64; MKNMDVYEIL YQFCLEYEVL LDDEKIPLWK LKKEDLDKVD LDLPWTSIRD LAIYLYELKK KQQNSKELIK CDIVEILVGI ALLKPEEGSN YMGLVTEDMC LTYLSELITA RINCIARYYY MMKKPQNTNI FDEIILKFPQ KKDIRASNIN DLRELVGKIR NYFK // ID Y248_METJA Reviewed; 194 AA. AC Q57698; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0248; GN OrderedLocusNames=MJ0248; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98243.1; -; Genomic_DNA. DR PIR; A64331; A64331. DR ProteinModelPortal; Q57698; -. DR STRING; 243232.MJ_0248; -. DR EnsemblBacteria; AAB98243; AAB98243; MJ_0248. DR KEGG; mja:MJ_0248; -. DR eggNOG; arCOG00551; Archaea. DR eggNOG; COG1711; LUCA. DR OMA; HEDEKKD; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 194 Uncharacterized protein MJ0248. FT /FTId=PRO_0000106759. SQ SEQUENCE 194 AA; 23542 MW; 05E03103175CC003 CRC64; MRVFIIIIYF RCFSKDHKPY FVITMYESLK NYFFEEIKND KLLKLPDDFY DDIREYIKNI KDDIELERVK YYFKELRKLR IYKALYLDNE RENLLPEELN IIHAIENIVV ELKIEETPEF KKPTEIDTPK PIYTINDIDV VKVDKNFPPF TDGTFIYDLN KNDVLSLDRK ISHILEKHRI ISRIGESYEN PEES // ID Y263_METJA Reviewed; 320 AA. AC O06917; DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=TPR repeat-containing protein MJ0263; GN OrderedLocusNames=MJ0263; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP DOMAINS TPR REPEATS. RX PubMed=9697413; DOI=10.1016/S0968-0004(98)01228-6; RA Kyrpides N.C., Woese C.R.; RT "Tetratrico-peptide-repeat proteins in the archaeon Methanococcus RT jannaschii."; RL Trends Biochem. Sci. 23:245-247(1998). CC -!- SIMILARITY: Contains 9 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98249.1; -; Genomic_DNA. DR PIR; H64332; H64332. DR ProteinModelPortal; O06917; -. DR STRING; 243232.MJ_0263; -. DR EnsemblBacteria; AAB98249; AAB98249; MJ_0263. DR KEGG; mja:MJ_0263; -. DR eggNOG; arCOG03038; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; O06917; -. DR OMA; CYLSPFH; -. DR PhylomeDB; O06917; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 4. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13174; TPR_6; 1. DR Pfam; PF13181; TPR_8; 3. DR SMART; SM00028; TPR; 8. DR SUPFAM; SSF48452; SSF48452; 2. DR PROSITE; PS50005; TPR; 7. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 320 TPR repeat-containing protein MJ0263. FT /FTId=PRO_0000106456. FT REPEAT 12 45 TPR 1. FT REPEAT 46 79 TPR 2. FT REPEAT 80 113 TPR 3. FT REPEAT 114 147 TPR 4. FT REPEAT 148 181 TPR 5. FT REPEAT 182 215 TPR 6. FT REPEAT 216 249 TPR 7. FT REPEAT 250 283 TPR 8. FT REPEAT 289 320 TPR 9. SQ SEQUENCE 320 AA; 36862 MW; 8D818C197D8B0352 CRC64; MDYDNMVKTL EILKDVVNAL ECADKGNFDK ALEYLEKAQK VDKDNPLVLY VKGIVLKLKG DMEKAEKYFE CLENIEGTSL LSLGNLICLT FVKGEYERTL KYIEKLSRLS KPCYLSPFHK ALIYIEFGEF EKALEALDEF LKIYPNLTSI LRQKASILEI LGKLDEALDC VNKILSIKKD DAHAWYLKGR ILKKLGNIKE ALDALKMAIN LNENLVHVYK DIAYLELANN NYEEALNYIT KYLEKFPNDV EAKFYLALIY ENLNKVDDAL KIYDKIISNK NVKDKLLIKS SILNKARILE KLGKIEEAVE TYNKAFDNNI // ID Y311_METJA Reviewed; 110 AA. AC Q57759; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0311; GN OrderedLocusNames=MJ0311; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98299.1; -; Genomic_DNA. DR PIR; H64338; H64338. DR ProteinModelPortal; Q57759; -. DR STRING; 243232.MJ_0311; -. DR EnsemblBacteria; AAB98299; AAB98299; MJ_0311. DR KEGG; mja:MJ_0311; -. DR eggNOG; arCOG02603; Archaea. DR eggNOG; COG2018; LUCA. DR KO; K07131; -. DR OMA; YNENTEC; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 110 Uncharacterized protein MJ0311. FT /FTId=PRO_0000106787. SQ SEQUENCE 110 AA; 12552 MW; F086C6258FBF8B7B CRC64; MIQKEILEEL KDLDYIHGVL LIKNDGLVEY SSLSEDSNME SLGARLSIIL NSISEVIKDI YNEKTECVFI KVKDDGIILI PKDNEILTIL FKANNDILHK IIPIIQEIIK // ID Y312_METJA Reviewed; 206 AA. AC Q57760; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0312; GN OrderedLocusNames=MJ0312; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98309.1; -; Genomic_DNA. DR PIR; A64339; A64339. DR ProteinModelPortal; Q57760; -. DR STRING; 243232.MJ_0312; -. DR EnsemblBacteria; AAB98309; AAB98309; MJ_0312. DR KEGG; mja:MJ_0312; -. DR eggNOG; arCOG08213; Archaea. DR eggNOG; ENOG410YU8J; LUCA. DR OMA; MSQAHEL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 206 Uncharacterized protein MJ0312. FT /FTId=PRO_0000106788. SQ SEQUENCE 206 AA; 22367 MW; 1168AB576BFE033A CRC64; MSKGINPPKG GGTMEGRYMS QAHELLTNTG VENMANRTAE RMIPLMNSLV TGYSIALAKT LGSGAGAMTQ ILLSEIGEVL SAMVDEILGS GQASYELENV EELLKNAFLE LGIAKDVKIE KNIKDNMVIY KLYIKGSLFA PVHKILIDRG LKEFPLSPEG LLAASIVRRV LRERKDGNTK ARINVNTKLP VNGETLIVEI KEVGSL // ID Y329_METJA Reviewed; 616 AA. AC Q57775; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0329; GN OrderedLocusNames=MJ0329; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98317.1; -; Genomic_DNA. DR PIR; A64341; A64341. DR ProteinModelPortal; Q57775; -. DR STRING; 243232.MJ_0329; -. DR EnsemblBacteria; AAB98317; AAB98317; MJ_0329. DR KEGG; mja:MJ_0329; -. DR eggNOG; arCOG09636; Archaea. DR eggNOG; COG2369; LUCA. DR OMA; ERIFPSN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR006528; Phage_head_morphogenesis. DR Pfam; PF04233; Phage_Mu_F; 1. DR TIGRFAMs; TIGR01641; phageSPP1_gp7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 616 Uncharacterized protein MJ0329. FT /FTId=PRO_0000106798. SQ SEQUENCE 616 AA; 72037 MW; 2991EC36D4D64B82 CRC64; MEDDKIQMET VSIDLAKDTA VNMALRILFT QIFTPYSIVS IDGKQLSKDV IDEISGLIDR HIRDLQLAFS DFLLKGKCYL YKLHYINPNS MNFKERKHWN PQKGRYEYCI TYTIKRNNAE RWWEVDTEED VRVVIAPMEL RQHFPADVEF YDEKYLGVYY NPIPIHETIQ EIADQKNTLA LKVLPLMVQK TLIPTIIGIT QNTKAGEIIK KALSNHQNRT RVYIPATPDE VKFETISIGK DIPTDLIETM LYYYDSAIFM GLGTSISIVK ASGQELTTSR TVDRNILRIV QGYQQEIERW IADQLEKMGY KGIWVKFANP DPDWEINMLQ KAKMVAELKA QEQVAKYDFS ALIERIFPSN EFGEILAAYP DLTEKEVEKL LKMAKEGKGG LEYADEEKQK LLEKKRKSLE KIISKLEKVG DKFGKKSMEN FVNWILETYE RLGYNELMQD WDELLREFTR EEVDMFFLDY VAPTLNSLKI YDDLDQQTID ILKQHWEQAF YNIYSSYSQQ FLDVLTEGIQ KGLGEEEIAK NLKKVAKDVK GSRLQMRARE EMNKTYNLTR ARRFWNDKVI YVTMKDERVR PSHRKLHGLI FVPAERPELV PPLGYGCRCT ITPVRD // ID Y338_METJA Reviewed; 104 AA. AC Q57784; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0338; GN OrderedLocusNames=MJ0338; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98326.1; -; Genomic_DNA. DR PIR; B64342; B64342. DR STRING; 243232.MJ_0338; -. DR EnsemblBacteria; AAB98326; AAB98326; MJ_0338. DR KEGG; mja:MJ_0338; -. DR eggNOG; arCOG09643; Archaea. DR eggNOG; ENOG41110VY; LUCA. DR OMA; IAILACY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MJ0338. FT /FTId=PRO_0000106808. SQ SEQUENCE 104 AA; 11842 MW; 12C9316CFCC498E0 CRC64; MIFMVDVSEI LAKMKPLLGM SADEEFANPE QAEASANLAI KTSQVEDVDI IAILACYYYT ESRDMKTDEN VSVMANHFYR MYQIAIEEAK QKELNEEEGA VFFD // ID Y3401_METJA Reviewed; 276 AA. AC Q60300; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 49. DE RecName: Full=Uncharacterized protein MJECS01; GN OrderedLocusNames=MJECS01; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37059.1; -; Genomic_DNA. DR PIR; A64516; A64516. DR ProteinModelPortal; Q60300; -. DR EnsemblBacteria; AAC37059; AAC37059; MJ_ECS01. DR KEGG; mja:MJECS01; -. DR OMA; KCHREYL; -. DR Proteomes; UP000000805; Plasmid small ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 276 Uncharacterized protein MJECS01. FT /FTId=PRO_0000107483. SQ SEQUENCE 276 AA; 32558 MW; 2CA3E1D51756BAFE CRC64; MKFIFEKYYR HPINKYNGSK ITPISQKNIF VVIKVELDDN ELNNIHDEAK KLAEDVCEKN PSGDIRTEER KLLSSFCGLI AEKVVKQLIT EKLMLIKDYI EIKGANVSNE NFNYESHNDI EIHLSNDEII TIEIRSSIAT KYDLNDILNK DFDILGSYTT SYKSKEHNKD YYFRIIFHNP GDYGYNPHLK KWEYNKRLEN AFKQEKNKAL DYFKNNVKVY FVGGCTFDDL ENYGEHDDLK QKNAEYWIIR PITKGRDVLE ILEILEKDIL NKLGFL // ID Y345_METJA Reviewed; 317 AA. AC Q57791; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0345; GN OrderedLocusNames=MJ0345; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98335.1; -; Genomic_DNA. DR PIR; A64343; A64343. DR ProteinModelPortal; Q57791; -. DR STRING; 243232.MJ_0345; -. DR EnsemblBacteria; AAB98335; AAB98335; MJ_0345. DR KEGG; mja:MJ_0345; -. DR eggNOG; arCOG09649; Archaea. DR eggNOG; ENOG410YRKN; LUCA. DR OMA; NVICEIT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 317 Uncharacterized protein MJ0345. FT /FTId=PRO_0000106815. SQ SEQUENCE 317 AA; 35379 MW; 9234BE19C4BA5533 CRC64; MDCVTNATTR CRKGSIVVIV MPPLISNNTF FLMNTTNDGN GGSVSYDYPL LSNQNSLITN TTNNLTSDST NTDISNETPI LSNNTPILMN TPTNPNSDSD TTTPTVVSHT VELITEEKKV ISKIVYSDGT EDVKELDLTD FYNSAYNEGY SAGVNSVDFS KTGYIIENGI IKVTTTLTNG KSQEYNITLD ENLVVSLYNQ IMANKSSCFQ IRQNETEYSF LVESRQYQPQ PNLAYQPAVD GTPVYEVLGQ EQKTWSFTLY VDSIPKMQFL QQLASNPLIE VYFDEIGDWK QALIQSISLS RITTGHYYAD IELIILE // ID Y349_METJA Reviewed; 105 AA. AC Q57795; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0349; GN OrderedLocusNames=MJ0349; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0023/MJ0349/MJ1072/MJ1074/MJ1107/MJECL16 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98338.1; -; Genomic_DNA. DR PIR; E64343; E64343. DR STRING; 243232.MJ_0349; -. DR EnsemblBacteria; AAB98338; AAB98338; MJ_0349. DR KEGG; mja:MJ_0349; -. DR eggNOG; arCOG09652; Archaea. DR eggNOG; ENOG4110ZR7; LUCA. DR OMA; EYKLIIH; -. DR PhylomeDB; Q57795; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 105 Uncharacterized protein MJ0349. FT /FTId=PRO_0000106820. SQ SEQUENCE 105 AA; 12195 MW; 8A75B451662B963C CRC64; MAVAYAKLYE LILKKVKDEK EAEELYNAII EIVKEEKLAV KTELKDELRG ELATKEDIKY LDGKIEMVKK ELEYKLIIHT LIILFAIIIT NPNAIELIKL LFGFK // ID Y3505_METJA Reviewed; 62 AA. AC Q60262; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 52. DE RecName: Full=Uncharacterized protein MJECL05; GN OrderedLocusNames=MJECL05; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37071.1; -; Genomic_DNA. DR PIR; E64510; E64510. DR EnsemblBacteria; AAC37071; AAC37071; MJ_ECL05. DR KEGG; mja:MJECL05; -. DR OMA; EEGICII; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 62 Uncharacterized protein MJECL05. FT /FTId=PRO_0000107497. FT COMPBIAS 3 15 Ile-rich. SQ SEQUENCE 62 AA; 7327 MW; 1624EC72E75EBAD7 CRC64; MEIIALLIEE GIIIIKDKKV AERFLKDLES SQGMDWKEIR ERAERAKKQL EEGIEWAKKT KL // ID Y3507_METJA Reviewed; 415 AA. AC Q60269; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJECL07; GN OrderedLocusNames=MJECL07; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37080.1; -; Genomic_DNA. DR PIR; G64510; G64510. DR ProteinModelPortal; Q60269; -. DR EnsemblBacteria; AAC37080; AAC37080; MJ_ECL07. DR KEGG; mja:MJECL07; -. DR InParanoid; Q60269; -. DR OMA; TRPPVYP; -. DR PhylomeDB; Q60269; -. DR Proteomes; UP000000805; Plasmid large ECE. DR InterPro; IPR018977; NurA_domain. DR Pfam; PF09376; NurA; 1. DR SMART; SM00933; NurA; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 415 Uncharacterized protein MJECL07. FT /FTId=PRO_0000107499. SQ SEQUENCE 415 AA; 48153 MW; 335548C397EE9B79 CRC64; MIKMFIISKN HLDIIYNFVD WEFKNISSIG NIINDEVVWN ELPKGVEGVL CGVDGSRGKV EFCSGIVYGL SSYAIGKNIE KGMFELGVLP FFKEEDRVRR LMMTLEYRLA TLVSKNVDLI LLDGTLSGAL IMPPLLSGDT NPLTVYPDLA EDLGWKFIKS LDNFWDEVLE NLDGNIYDNT LLAIKIFQKF DSTYSEYVED IREELFAANI LNSRLEIACW GVYFEYIELL HSLNRLLEYD CTFIAKNFEN SIITEKLKEN NINVDILLDA TLLNQIFRGR GYTTLKLEDC YNKKRSRRHI NKICDVFGDY FKFLEVIREN PFEMIPKTYV RFAESSPILA LEVPRTNKKS IEEVISLLIP YSKLGYPRYL KDAHNKAKIS KKEFKKQILF MIKYISEKNR DFSLFFQSGR EVLGE // ID Y3509_METJA Reviewed; 108 AA. AC Q60271; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 48. DE RecName: Full=Uncharacterized protein MJECL09; GN OrderedLocusNames=MJECL09; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37082.1; -; Genomic_DNA. DR PIR; A64511; A64511. DR EnsemblBacteria; AAC37082; AAC37082; MJ_ECL09. DR KEGG; mja:MJECL09; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 108 Uncharacterized protein MJECL09. FT /FTId=PRO_0000107501. SQ SEQUENCE 108 AA; 13308 MW; 482EE7DFA65A277D CRC64; MNYMKFMWNS EDGFIVEEQH KEEIPFEDWI VNTVEQLKNL QYTRYTFEEL TPKTKNLEAY NKLLEILKKH TNMDIENNVK RIYHCIAENN NYKYEIAFYI VISKNWNE // ID Y3514_METJA Reviewed; 314 AA. AC Q60276; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Uncharacterized protein MJECL14; GN OrderedLocusNames=MJECL14; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC -!- CAUTION: Lacks the ATP-binding site. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37087.1; -; Genomic_DNA. DR PIR; F64511; F64511. DR ProteinModelPortal; Q60276; -. DR EnsemblBacteria; AAC37087; AAC37087; MJ_ECL14. DR KEGG; mja:MJECL14; -. DR HOGENOM; HOG000154927; -. DR InParanoid; Q60276; -. DR KO; K06921; -. DR OMA; LTKERHI; -. DR PhylomeDB; Q60276; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 314 Uncharacterized protein MJECL14. FT /FTId=PRO_0000184678. SQ SEQUENCE 314 AA; 36754 MW; 59E9992DDB441580 CRC64; MLSFMLISES MIFTSMDNFV EALFEIDENS KEKKIKSYIE SFTKGVNDII NLYYGIKIPE PILDKFFGEK EKGGLVFKFI RDLFMSLNKK GVQPVFILDE LQMIKDIVMN GGKPLLKSLF QFLVSLTKER HIAHVFCLSS DSLFIEYVYN AGELEGRAKY LLVDDFDKET SLKFMDFLAV EGNINLTNED KELIYSYVGG KAKDIKYVIE ESKFKDLREV LDFMLKDEVS KLRKLLVKIK TKKIAEVEYE NVVKALKLFK DNYEINEYLM DENTKEFLIK RNILFLNPVE EILKPQSYLV WNAIKRVLQN INDF // ID Y3521_METJA Reviewed; 432 AA. AC Q60281; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 47. DE RecName: Full=Uncharacterized protein MJECL21; GN OrderedLocusNames=MJECL21; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37092.1; -; Genomic_DNA. DR PIR; D64512; D64512. DR EnsemblBacteria; AAC37092; AAC37092; MJ_ECL21. DR KEGG; mja:MJECL21; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 432 Uncharacterized protein MJECL21. FT /FTId=PRO_0000107509. SQ SEQUENCE 432 AA; 51082 MW; DBADF2C5C43A4F90 CRC64; MWRGVGMVVQ QFINRIRNCP LARDIIKKFF IPVIKERKNI EKEVEDILKV LRKNYCSGEY ANKDCICAWF KFFEDVGRLH EALELKAFWE IIFPNHLNDL SESLQLFISN YAYMRPFGSS YSSIRVRIHG FIGAVCIDRN FNLHNNTWIS NICNCYENNL RMLGLGFYTS DTLDPRYNIN PSCNINSTTT NKCGLLYIIS NTQITASLVS YLLNLLRNGN IYDAYNFLIR IRGVGDKIAC LFLRDISIIH NLMLYGDCRD LLYKPIDRVV KKVIEELVKC KCKLNYNFDI NEVLEKFDYT ECRCIQKLRK NAKIDSNDFK TLYPYKIFLY EYSKKCKLDQ RYVEMGMWFF NSKVAKYYNR RLCKYTIQEA CKDLIKRLRK AINNTNIRYI GNNQFEININ GKIIIVSEDE LIDLILKGEI EIYDELLDII FF // ID Y3526_METJA Reviewed; 343 AA. AC Q60285; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Uncharacterized ATP-binding protein MJECL26; GN OrderedLocusNames=MJECL26; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37097.1; -; Genomic_DNA. DR PIR; A64513; A64513. DR ProteinModelPortal; Q60285; -. DR DNASU; 1450810; -. DR EnsemblBacteria; AAC37097; AAC37097; MJ_ECL26. DR KEGG; mja:MJECL26; -. DR HOGENOM; HOG000154927; -. DR InParanoid; Q60285; -. DR KO; K06921; -. DR OMA; EWHAIRE; -. DR PhylomeDB; Q60285; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; Plasmid; KW Reference proteome. FT CHAIN 1 343 Uncharacterized ATP-binding protein FT MJECL26. FT /FTId=PRO_0000184680. FT NP_BIND 33 40 ATP. {ECO:0000255}. SQ SEQUENCE 343 AA; 40442 MW; EC7181030B46D227 CRC64; MGEIMKFYDR EKELNYLKTY CQLEPNSILF VYGPKSSGKS TVMRRVIKEL ENSNIVFFYY NLRKYATPTR DEFLRVFFEK SDKKYLLNKL ELNLGVCKFG IEENFDFNNL CLNDVFAKIN ESINAVVEEG KKPVLIIDEL QKLKNIYFNG GKSLLNELFN LFVSLTKMEH LCHVICLTSD TLFIDEIYRN STLKNASEYY LIDWLRKGTI RNILKEEGFS EEEINYALDY LSLPYEISQL INNKKLGLSV EQTIKQWINV EKDGLKYLID TTDLDEEGLY NVLSKFKDKI KISYDKEVKK EEMKYLKFLI ENEILFYDVI NGIIKPTSII EWHAIKEIIN AMQ // ID Y3537_METJA Reviewed; 237 AA. AC Q60292; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MJECL37; GN OrderedLocusNames=MJECL37; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37106.1; -; Genomic_DNA. DR PIR; D64514; D64514. DR ProteinModelPortal; Q60292; -. DR EnsemblBacteria; AAC37106; AAC37106; MJ_ECL37. DR KEGG; mja:MJECL37; -. DR HOGENOM; HOG000254137; -. DR OMA; FAMSITH; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJECL37. FT /FTId=PRO_0000107520. SQ SEQUENCE 237 AA; 27184 MW; B0DF621202CDDA11 CRC64; MNNFSKNLEE CFQKYGYENF TLLLAGYIAK YPKYEEISNN TKFLNEYHNE VSNITTCLHV YKNLAEGVKR DFNLDLLYLN DYEIKKVKSM VEPNVISDAI TVVTLVNDYN NLIDAARNVK KGDKESYTKF YIALGIVVFD VILIKENVAY KVSYKLVGIL ISKTGFYKVI YKYGGSTALK PIESCTHWIS RGEINSMPSK LYNNSDKLTN ISIKINTSKL YNKSINTIRS KIMEVSS // ID Y357_METJA Reviewed; 155 AA. AC Q57803; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0357; GN OrderedLocusNames=MJ0357; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98349.1; -; Genomic_DNA. DR PIR; E64344; E64344. DR ProteinModelPortal; Q57803; -. DR STRING; 243232.MJ_0357; -. DR EnsemblBacteria; AAB98349; AAB98349; MJ_0357. DR KEGG; mja:MJ_0357; -. DR eggNOG; COG1952; LUCA. DR OMA; MMANIEE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051262; P:protein tetramerization; IEA:InterPro. DR GO; GO:0015031; P:protein transport; IEA:InterPro. DR Gene3D; 3.10.420.10; -; 1. DR InterPro; IPR003708; SecB. DR Pfam; PF02556; SecB; 1. DR SUPFAM; SSF54611; SSF54611; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein MJ0357. FT /FTId=PRO_0000106828. SQ SEQUENCE 155 AA; 17715 MW; FBE28D58597DEEF7 CRC64; MEAPPKCALK FSNYIVKHIE FILNEVPEKD EKIRLNVNID TEIRYNKNEP NKFITIIKIT AGEKKDFAKS PVYLSVEVWG FFEVIEEAID KVRQFAEINS VAILFPYVRA LISTITANAN IPPVILPPIN VAGMMANIEE VKEENTEKQE TEAYE // ID Y359_METJA Reviewed; 214 AA. AC Q57805; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0359; GN OrderedLocusNames=MJ0359; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98351.1; -; Genomic_DNA. DR PIR; G64344; G64344. DR STRING; 243232.MJ_0359; -. DR DNASU; 1451216; -. DR EnsemblBacteria; AAB98351; AAB98351; MJ_0359. DR KEGG; mja:MJ_0359; -. DR eggNOG; ENOG4110147; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 214 Uncharacterized protein MJ0359. FT /FTId=PRO_0000106830. SQ SEQUENCE 214 AA; 25993 MW; 9A88675453535E8B CRC64; MMSYVRMTLY HGTDRKSAEK IMESKEILPS QGDNHWLGDG IYFYEEEFHA FKWIWYKEKN RNRLLKNFAI IKAEVICEES RIFDLTKIEH KLLFDMMYKL INTTKLRLDK LRGDMCAEGV VINYMFKNKE LGYNKRFDIV RALFPIPVKK YQKIENREKN KKYKERTHRL TFMPEIQVCV KNPSVIKKLE WYDLEKTIDK FLIYTEIYKE DLGI // ID Y363_METJA Reviewed; 759 AA. AC Q57809; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Uncharacterized MCM-type protein MJ0363; GN OrderedLocusNames=MJ0363; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MCM domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98345.1; -; Genomic_DNA. DR PIR; C64345; C64345. DR ProteinModelPortal; Q57809; -. DR STRING; 243232.MJ_0363; -. DR PRIDE; Q57809; -. DR EnsemblBacteria; AAB98345; AAB98345; MJ_0363. DR KEGG; mja:MJ_0363; -. DR eggNOG; arCOG00439; Archaea. DR eggNOG; COG1241; LUCA. DR InParanoid; Q57809; -. DR KO; K10726; -. DR OMA; QADWDND; -. DR PhylomeDB; Q57809; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR031327; MCM. DR InterPro; IPR018525; MCM_CS. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00382; AAA; 1. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Complete proteome; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 759 Uncharacterized MCM-type protein MJ0363. FT /FTId=PRO_0000194129. FT DOMAIN 352 556 MCM. FT NP_BIND 397 404 ATP. {ECO:0000255}. SQ SEQUENCE 759 AA; 86167 MW; 12240104136FAA05 CRC64; MVYDNIKREI IGMLKRMPNK QADWDNDLLP TLKAMFNPKS VSNAKSQLIS EGVISQEIVD GKKIITLIKD PYELQAPNVF DEEMFLAYYT DKLKEYFKHK LSTEGPEWDI FDVKEFIMHF PESGDLNDKL IEHPYEVRKS ITNVYIEAYE ELFNETPNVE FIHIRNPIDC RISLSELSSA HKGKLVEFRA MILQATKLKL RYAKGFYYCP KCGATKTLDL GFWDKPKEVG KSLTCPADGC DCKGLIFDED LSGKVDFQEI KVQTPLQESI YANKHSTTVF YEFNKPKKAV YSGYVKIVGV PIVKENKNGS VGELYIHAFY IEKDDEDIEE IAKNLNEKDL ELINRIAKDK NVIQKLSDYA FREVTGYDMI KRAVLLQLVS SGTNIDMRTS IHILMISDPG VGKSTLMESL IQKFPFVKKV YAVTSSGPGL VGSVVREKAE FGDSWVLKAG VLTEADGGVV CIDEFSRNKE VYDYLLGVME QQKIEINKAG VIDAVLPARV AILAACNPRF GRFNPDLTVW EQINLPKELL DRFDLIFVIK DKIDKKKDED IADFSIDNYN SKVRERKGKS SGKKFVINGV ELNDELLLKY VLYARQIEPE ISDEARKIIK EYYVSVRKMS EAKGTFGISA RQLGSIIRLA VAHAKLRLSE VVKAVDAEEA IRLVDTCLKQ IAYDPESGSI DIDKIAGTPK SKRDKVEKVL NIIKEISNSR DDGLAPEEEI YERAERAGLS EKEVEDAINY LKRVGDIYSP KSGYWQLMS // ID Y368_METJA Reviewed; 106 AA. AC Q57814; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0368; GN OrderedLocusNames=MJ0368; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98368.1; -; Genomic_DNA. DR PIR; H64345; H64345. DR STRING; 243232.MJ_0368; -. DR EnsemblBacteria; AAB98368; AAB98368; MJ_0368. DR KEGG; mja:MJ_0368; -. DR OMA; LLMDVIL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 106 Uncharacterized protein MJ0368. FT /FTId=PRO_0000106836. SQ SEQUENCE 106 AA; 12705 MW; 4EA3F47CB582668A CRC64; MGGDMTFDEF ESLKNYPPKE SIKEEKRVFN PKNIEVGNNF IKIEDIKIIF SKDIEKGEEE YLLMDVILSS LEGIYNLIED EVYKKEIKKI WEKINEIRNY YNPEFL // ID Y405_METJA Reviewed; 131 AA. AC Q57848; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJ0405; GN OrderedLocusNames=MJ0405; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98392.1; -; Genomic_DNA. DR PIR; E64350; E64350. DR ProteinModelPortal; Q57848; -. DR STRING; 243232.MJ_0405; -. DR EnsemblBacteria; AAB98392; AAB98392; MJ_0405. DR KEGG; mja:MJ_0405; -. DR eggNOG; arCOG04902; Archaea. DR eggNOG; COG4048; LUCA. DR InParanoid; Q57848; -. DR OMA; DNYEGYV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR012029; UCP006557. DR Pfam; PF09884; DUF2111; 1. DR PIRSF; PIRSF006557; UCP006557_sign; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 131 Uncharacterized protein MJ0405. FT /FTId=PRO_0000106856. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. SQ SEQUENCE 131 AA; 14224 MW; 2849EAA7A9851B82 CRC64; MKIMITISEN SEAKELMPIA QAVHILVNKL PVAMRSKNKP GVRLEKGEVV DTNYEGYVLK VAIEKGEVVR ATPIIGPYAG LPVIVAPIKD GDNVLGAIGV VDITAGIFED IVAISRRPEL YKFLPEDAFP K // ID Y413_METJA Reviewed; 267 AA. AC Q57856; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 92. DE RecName: Full=Putative ABC transporter permease protein MJ0413; GN OrderedLocusNames=MJ0413; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00441}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. CysTW subfamily. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transmembrane type-1 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00441}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98402.1; -; Genomic_DNA. DR PIR; E64351; E64351. DR ProteinModelPortal; Q57856; -. DR STRING; 243232.MJ_0413; -. DR EnsemblBacteria; AAB98402; AAB98402; MJ_0413. DR KEGG; mja:MJ_0413; -. DR eggNOG; arCOG00169; Archaea. DR eggNOG; COG0600; LUCA. DR InParanoid; Q57856; -. DR KO; K02050; -. DR OMA; PFAIVWF; -. DR PhylomeDB; Q57856; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0042959; F:alkanesulfonate transporter activity; IBA:GO_Central. DR GO; GO:0042918; P:alkanesulfonate transport; IBA:GO_Central. DR Gene3D; 1.10.3720.10; -; 1. DR InterPro; IPR000515; MetI-like. DR Pfam; PF00528; BPD_transp_1; 1. DR SUPFAM; SSF161098; SSF161098; 1. DR PROSITE; PS50928; ABC_TM1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 267 Putative ABC transporter permease protein FT MJ0413. FT /FTId=PRO_0000060305. FT TRANSMEM 18 38 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 48 68 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 78 98 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 115 135 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 136 156 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 188 208 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT TRANSMEM 228 248 Helical. {ECO:0000255|PROSITE- FT ProRule:PRU00441}. FT DOMAIN 71 252 ABC transmembrane type-1. FT {ECO:0000255|PROSITE-ProRule:PRU00441}. SQ SEQUENCE 267 AA; 29043 MW; 2A6B9AAEC07A4111 CRC64; MMNHKKGISV KINTKELVLK ISLPALAVVI WELLAIYINN PVILPRVEAV INVLIHPFQG ILGTGSLIDN TIISIKRVIS GFLLASAVAI PLGILMGYYR TVNSLCDTLI ELLRPIPPLA WVPLSLAWFG LGEMSMIFII FIGAFFPILI NTISGVKGVP TPLIEAALTL GAKGRDILIK VVIPASSPSI LTGLRVGAGI AWMCVVAAEM LPSSNAGLGY LIMYAYSLSR MDVVIACMII IGLIGLVLDR GLRYIEDKYF VWRKMMK // ID Y431_METJA Reviewed; 75 AA. AC Q57873; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=UPF0333 protein MJ0431; GN OrderedLocusNames=MJ0431; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0333 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98432.1; -; Genomic_DNA. DR PIR; G64353; G64353. DR STRING; 243232.MJ_0431; -. DR EnsemblBacteria; AAB98432; AAB98432; MJ_0431. DR KEGG; mja:MJ_0431; -. DR eggNOG; arCOG11030; Archaea. DR eggNOG; COG1991; LUCA. DR OMA; VKYSDTH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR007166; Class3_signal_pept_motif. DR Pfam; PF04021; Class_IIIsignal; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 75 UPF0333 protein MJ0431. FT /FTId=PRO_0000218265. FT TRANSMEM 20 40 Helical. {ECO:0000255}. SQ SEQUENCE 75 AA; 7890 MW; A48FB475CFD9F629 CRC64; MGKMKILKKL LSKKGQLSME VGVLVAAAVL VAIIAAYFYV KNAKSAVASA GNKSAAFINV TANKSQEYIS NLSNI // ID Y452_METJA Reviewed; 148 AA. AC Q57894; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0452; GN OrderedLocusNames=MJ0452; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98441.1; -; Genomic_DNA. DR PIR; D64356; D64356. DR ProteinModelPortal; Q57894; -. DR STRING; 243232.MJ_0452; -. DR EnsemblBacteria; AAB98441; AAB98441; MJ_0452. DR KEGG; mja:MJ_0452; -. DR eggNOG; arCOG04845; Archaea. DR eggNOG; COG4081; LUCA. DR InParanoid; Q57894; -. DR OMA; HNDAAVN; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.10160; -; 1. DR InterPro; IPR012033; UCP006600. DR Pfam; PF09001; DUF1890; 1. DR PIRSF; PIRSF006600; UCP006600; 1. DR SUPFAM; SSF75181; SSF75181; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 148 Uncharacterized protein MJ0452. FT /FTId=PRO_0000106882. SQ SEQUENCE 148 AA; 16226 MW; D468F9C1D0C1E949 CRC64; MMSVLVIVGC PEPPALIPSV LYLTNQLKKK GFNVIIAANP AALKLLEVAD DDKYYLKGVG AVDIDGGLRG IEGINKIISF VHNDGGVSYT VTYKAKYNKP TYAIVFGRQI NKDYVETLKN SNIGVYTARA FHNPMPIVNR IKEILANL // ID Y455_METJA Reviewed; 193 AA. AC Q57897; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0455; GN OrderedLocusNames=MJ0455; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98448.1; -; Genomic_DNA. DR PIR; G64356; G64356. DR ProteinModelPortal; Q57897; -. DR STRING; 243232.MJ_0455; -. DR EnsemblBacteria; AAB98448; AAB98448; MJ_0455. DR KEGG; mja:MJ_0455; -. DR eggNOG; arCOG05003; Archaea. DR eggNOG; COG4887; LUCA. DR InParanoid; Q57897; -. DR OMA; VESEGYC; -. DR PhylomeDB; Q57897; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014997; DUF1847. DR Pfam; PF08901; DUF1847; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 193 Uncharacterized protein MJ0455. FT /FTId=PRO_0000106884. SQ SEQUENCE 193 AA; 22113 MW; 655279BEE3396404 CRC64; MKCSQCNKKL CYTGKDCKKD ITQKIIEEYK KEENLKIAEV SAYIEATYYM KKTRLEEIIE FCKLMEYKKI GIAFCIGLEN EAKILAKILS KHFEVYSVCC KVCGIDKDVF KFKKINKGEK EAMCNPIGQA EILNEIGTDL NIIVGLCIGH DILFQKYSKA PTTTFIVKDR VLSHNTAGAI YTKYYLKKLL EGK // ID Y45A_METJA Reviewed; 57 AA. AC P81308; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0458.1; GN OrderedLocusNames=MJ0458.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98468.1; -; Genomic_DNA. DR ProteinModelPortal; P81308; -. DR STRING; 243232.MJ_0458.1; -. DR EnsemblBacteria; AAB98468; AAB98468; MJ_0458.1. DR KEGG; mja:MJ_0458.1; -. DR eggNOG; arCOG01989; Archaea. DR eggNOG; COG2888; LUCA. DR InParanoid; P81308; -. DR KO; K07580; -. DR OMA; VEIVRCE; -. DR PhylomeDB; P81308; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR011668; DUF1610. DR Pfam; PF07754; DUF1610; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 57 Uncharacterized protein MJ0458.1. FT /FTId=PRO_0000106887. SQ SEQUENCE 57 AA; 6459 MW; 0FB4D7019B6BC426 CRC64; MGEMKYVCIS CNAEIAPREK STKFPCPNCG EVEIVRCERC RKLNNPYKCP KCGFEGP // ID Y519_METJA Reviewed; 84 AA. AC Q57939; DT 01-JUN-2001, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0519; GN OrderedLocusNames=MJ0519; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98513.1; -; Genomic_DNA. DR PIR; G64364; G64364. DR STRING; 243232.MJ_0519; -. DR EnsemblBacteria; AAB98513; AAB98513; MJ_0519. DR KEGG; mja:MJ_0519; -. DR eggNOG; arCOG08277; Archaea. DR eggNOG; ENOG41111C2; LUCA. DR KO; K14102; -. DR OMA; TIACIIA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011319; Prd_NiFe_hyd_3_EhaK. DR PIRSF; PIRSF036538; EhaK; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 84 Uncharacterized protein MJ0519. FT /FTId=PRO_0000106909. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 84 AA; 9680 MW; 51E95DA171C2F48A CRC64; MDKMKSYIYF FTIACIIAVI YCVLVNLLQI NVIPVVLAFS LILILTISTI NKKIAHKMED IEVLFMLLVL AFFAYAIYKL YIPV // ID Y51A_METJA Reviewed; 163 AA. AC P81292; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ0514.1; GN OrderedLocusNames=MJ0514.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 4 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98510.1; -; Genomic_DNA. DR ProteinModelPortal; P81292; -. DR STRING; 243232.MJ_0514.1; -. DR EnsemblBacteria; AAB98510; AAB98510; MJ_0514.1. DR KEGG; mja:MJ_0514.1; -. DR eggNOG; arCOG02185; Archaea. DR eggNOG; COG1145; LUCA. DR InParanoid; P81292; -. DR OMA; KCVLCGH; -. DR PhylomeDB; P81292; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12838; Fer4_7; 1. DR Pfam; PF13187; Fer4_9; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 4. DR PROSITE; PS51379; 4FE4S_FER_2; 4. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 163 Uncharacterized polyferredoxin-like FT protein MJ0514.1. FT /FTId=PRO_0000159149. FT DOMAIN 30 59 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 61 90 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 105 136 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 136 163 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 39 39 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 42 42 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 45 45 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 49 49 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 70 70 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 73 73 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 76 76 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 80 80 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 116 116 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 119 119 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 122 122 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 126 126 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 145 145 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 148 148 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 151 151 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 155 155 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 163 AA; 18645 MW; 5A9022DA3AB4633A CRC64; MIKEIIAKHF NLADKNIQLL PKFNIILNKR EIIVKEDKCI SCGKCIEICP VNAITYSSDG LYITINKEKC VFCGKCKKVC PTNAIVIIRL RCEINEDARI IEVDKYEFID YISERCASCL VCLRNCPFNA IEEYGSKIRI DINKCELCGK CEEICPLNAI ILR // ID Y524_METJA Reviewed; 158 AA. AC Q57944; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0524; GN OrderedLocusNames=MJ0524; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98516.1; -; Genomic_DNA. DR PIR; D64365; D64365. DR STRING; 243232.MJ_0524; -. DR EnsemblBacteria; AAB98516; AAB98516; MJ_0524. DR KEGG; mja:MJ_0524; -. DR eggNOG; arCOG04831; Archaea. DR eggNOG; COG4037; LUCA. DR KO; K14097; -. DR OMA; YTRGMDT; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011313; Prd_NiFe_hyd_3_EhaF. DR Pfam; PF09879; DUF2106; 1. DR PIRSF; PIRSF019373; EhaF; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 158 Uncharacterized protein MJ0524. FT /FTId=PRO_0000106913. FT TRANSMEM 25 45 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. SQ SEQUENCE 158 AA; 18293 MW; 4381CA8F0625E931 CRC64; MRWVIMKKLG KIWNYLSKPE IVPRIFSVFL ALVFIFGLLM PHYLNPNQLY PKPIPHSQTL KTPLAPYDRG GIPLKEPAEL KAQYPQYEPN LGKITAYLTP IAEWIKDKTY YFGTTIVSTP GGILDEILYY TRGMDTVLES SILLISFIIF SWLFFNKD // ID Y525_METJA Reviewed; 53 AA. AC Q57945; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0525; GN OrderedLocusNames=MJ0525; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98517.1; -; Genomic_DNA. DR PIR; E64365; E64365. DR STRING; 243232.MJ_0525; -. DR EnsemblBacteria; AAB98517; AAB98517; MJ_0525. DR KEGG; mja:MJ_0525; -. DR eggNOG; arCOG04830; Archaea. DR eggNOG; COG4038; LUCA. DR KO; K14096; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR011317; Prd_NiFe_hyd_3_EhaE. DR Pfam; PF09880; DUF2107; 1. DR PIRSF; PIRSF036535; EhaE; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 53 Uncharacterized protein MJ0525. FT /FTId=PRO_0000106914. FT TRANSMEM 24 44 Helical. {ECO:0000255}. SQ SEQUENCE 53 AA; 5837 MW; 5394D0250D5A9D98 CRC64; MLNVEVPTIG VSLIFLAYDE ALALMTFIAV NAVLSLILIR AVILDAEYKE NNQ // ID Y534_METJA Reviewed; 391 AA. AC Q57954; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 17-FEB-2016, entry version 90. DE RecName: Full=Uncharacterized protein MJ0534; GN OrderedLocusNames=MJ0534; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 flavodoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00088}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98525.1; -; Genomic_DNA. DR PIR; F64366; F64366. DR ProteinModelPortal; Q57954; -. DR STRING; 243232.MJ_0534; -. DR EnsemblBacteria; AAB98525; AAB98525; MJ_0534. DR KEGG; mja:MJ_0534; -. DR eggNOG; arCOG00509; Archaea. DR eggNOG; COG0426; LUCA. DR InParanoid; Q57954; -. DR OMA; CMSFIEW; -. DR PhylomeDB; Q57954; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0010181; F:FMN binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR Gene3D; 3.40.50.360; -; 1. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR008254; Flavodoxin/NO_synth. DR InterPro; IPR029039; Flavoprotein-like_dom. DR InterPro; IPR001279; Metallo-B-lactamas. DR InterPro; IPR016440; Rubredoxin-O_OxRdtase. DR Pfam; PF00258; Flavodoxin_1; 1. DR PIRSF; PIRSF005243; ROO; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF52218; SSF52218; 1. DR SUPFAM; SSF56281; SSF56281; 1. DR PROSITE; PS50902; FLAVODOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 391 Uncharacterized protein MJ0534. FT /FTId=PRO_0000106919. FT DOMAIN 247 387 Flavodoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00088}. SQ SEQUENCE 391 AA; 45532 MW; C08636FC7C18D516 CRC64; MVKYMVLKIK DNIYCMSFIE WKIKEYRGLD IEKGTTYNSY LILDKNNVII DTTRIKYFDE LLSYLKDVAN LKLDYIISNH ISPDHNECIE KLIELTEAKI VTTKIRKYYL DAQFNTKDWE FVIVKNGDEL NIGNRTLKFI TDDKCEYMLT YCVEDKILFS NDLFSQHVVY KEKIDSDIGH KIMLDAKEYF ANILLPYRKS ILKILNILKD LDLEYICPSH GVIWHIMIDE ILTKYRMWCS DSYKNTAVIV YATIYSSTEK IAKALGEGLS EEGVDVIYHR LDTSPLNIIM RDILDAKYVL VGSPTINMNV HPKVGMLLTY IEGLKPSNKK IGVAFGSYGW KECATKKIIE AFKRLGFKIV DDKILTFRFA PKENDIKKIK EFGRKLAKIN V // ID Y570_METJA Reviewed; 223 AA. AC Q57990; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MJ0570; GN OrderedLocusNames=MJ0570; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98564.1; -; Genomic_DNA. DR PIR; B64371; B64371. DR ProteinModelPortal; Q57990; -. DR SMR; Q57990; 2-223. DR STRING; 243232.MJ_0570; -. DR EnsemblBacteria; AAB98564; AAB98564; MJ_0570. DR KEGG; mja:MJ_0570; -. DR eggNOG; arCOG00035; Archaea. DR eggNOG; COG2102; LUCA. DR InParanoid; Q57990; -. DR OMA; YGLGKEW; -. DR PhylomeDB; Q57990; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR002761; Diphthami_syn_dom. DR InterPro; IPR030662; DPH6/MJ0570. DR InterPro; IPR005237; MJ0570. DR InterPro; IPR022427; MJ0570_ATP-bd. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PANTHER; PTHR12196; PTHR12196; 1. DR Pfam; PF01902; Diphthami_syn_2; 1. DR PIRSF; PIRSF039123; Diphthamide_synthase; 1. DR TIGRFAMs; TIGR03679; arCOG00187; 1. DR TIGRFAMs; TIGR00290; MJ0570_dom; 1. DR TIGRFAMs; TIGR00289; TIGR00289; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 223 Uncharacterized protein MJ0570. FT /FTId=PRO_0000106935. SQ SEQUENCE 223 AA; 25618 MW; 5D1EF288E77B2AF8 CRC64; MKVAVLYSGG KDSNYALYWA LKEGFDVKYL VNVESENKES YMFHIPNVHL TELSAEAVGI PLIKLYTKGE KEKEVEDLKK GLEKLDVEGI VTGAVASIYQ KSRIDRVCEE LGLKSFAPLW HKDPEWILRT VSELFNVRIV GVYAYGLGKE WLGKRITKEN IDKLLNICEK YGIHKAFEGG EAETFVFDAP MFKKRIEVVE AEIEWHETWG IYHIKKAKLV DKE // ID Y572_METJA Reviewed; 86 AA. AC Q57992; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ0572; GN OrderedLocusNames=MJ0572; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98572.1; -; Genomic_DNA. DR PIR; D64371; D64371. DR ProteinModelPortal; Q57992; -. DR STRING; 243232.MJ_0572; -. DR EnsemblBacteria; AAB98572; AAB98572; MJ_0572. DR KEGG; mja:MJ_0572; -. DR eggNOG; arCOG05273; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q57992; -. DR OMA; EARECFF; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SMART; SM00028; TPR; 2. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 2. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 86 Uncharacterized protein MJ0572. FT /FTId=PRO_0000106936. FT REPEAT 8 41 TPR 1. FT REPEAT 42 75 TPR 2. SQ SEQUENCE 86 AA; 10258 MW; 4B1EF4C549045020 CRC64; MDENIKKAEY YYKKGVEVGN KGDVEKALEY FNKAIELNPF YRDAWFNKAL ALRILGRYEE ARECFFRGLA VEKHLTHKKY NSDDEK // ID Y577_METJA Reviewed; 162 AA. AC Q57997; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Universal stress protein MJ0577; DE Short=USP MJ0577; GN OrderedLocusNames=MJ0577; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.7 ANGSTROMS). RX PubMed=9860944; DOI=10.1073/pnas.95.26.15189; RA Zarembinski T.I., Hung L.-W., Mueller-Dieckmann H.-J., Kim K.-K., RA Yokota H., Kim R., Kim S.-H.; RT "Structure-based assignment of the biochemical function of a RT hypothetical protein: a test case of structural genomics."; RL Proc. Natl. Acad. Sci. U.S.A. 95:15189-15193(1998). CC -!- COFACTOR: CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; CC Note=Binds 1 Mn(2+) ion per subunit.; CC -!- SUBUNIT: Homodimer. CC -!- SUBCELLULAR LOCATION: Cytoplasm. CC -!- SIMILARITY: Belongs to the universal stress protein A family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98568.1; -; Genomic_DNA. DR PIR; A64372; A64372. DR PDB; 1MJH; X-ray; 1.70 A; A/B=1-162. DR PDBsum; 1MJH; -. DR ProteinModelPortal; Q57997; -. DR SMR; Q57997; 3-162. DR STRING; 243232.MJ_0577; -. DR EnsemblBacteria; AAB98568; AAB98568; MJ_0577. DR KEGG; mja:MJ_0577; -. DR eggNOG; arCOG02053; Archaea. DR eggNOG; COG0589; LUCA. DR InParanoid; Q57997; -. DR OMA; IPHEEIV; -. DR PhylomeDB; Q57997; -. DR EvolutionaryTrace; Q57997; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR006015; Universal_stress_UspA. DR InterPro; IPR006016; UspA. DR Pfam; PF00582; Usp; 1. DR PRINTS; PR01438; UNVRSLSTRESS. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Cytoplasm; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 162 Universal stress protein MJ0577. FT /FTId=PRO_0000147446. FT STRAND 7 11 {ECO:0000244|PDB:1MJH}. FT HELIX 16 27 {ECO:0000244|PDB:1MJH}. FT STRAND 35 43 {ECO:0000244|PDB:1MJH}. FT HELIX 44 46 {ECO:0000244|PDB:1MJH}. FT HELIX 67 94 {ECO:0000244|PDB:1MJH}. FT STRAND 98 106 {ECO:0000244|PDB:1MJH}. FT HELIX 108 118 {ECO:0000244|PDB:1MJH}. FT STRAND 122 128 {ECO:0000244|PDB:1MJH}. FT HELIX 141 149 {ECO:0000244|PDB:1MJH}. FT STRAND 154 157 {ECO:0000244|PDB:1MJH}. SQ SEQUENCE 162 AA; 18339 MW; 0A1060E6A2E6E1F4 CRC64; MSVMYKKILY PTDFSETAEI ALKHVKAFKT LKAEEVILLH VIDEREIKKR DIFSLLLGVA GLNKSVEEFE NELKNKLTEE AKNKMENIKK ELEDVGFKVK DIIVVGIPHE EIVKIAEDEG VDIIIMGSHG KTNLKEILLG SVTENVIKKS NKPVLVVKRK NS // ID Y584_METJA Reviewed; 365 AA. AC Q58004; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-NOV-2015, entry version 81. DE RecName: Full=UPF0718 protein MJ0584; GN OrderedLocusNames=MJ0584; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0718 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98577.1; -; Genomic_DNA. DR PIR; H64372; H64372. DR ProteinModelPortal; Q58004; -. DR STRING; 243232.MJ_0584; -. DR EnsemblBacteria; AAB98577; AAB98577; MJ_0584. DR KEGG; mja:MJ_0584; -. DR eggNOG; arCOG02712; Archaea. DR eggNOG; COG0701; LUCA. DR InParanoid; Q58004; -. DR KO; K07089; -. DR OMA; VLAVCSC; -. DR PhylomeDB; Q58004; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR005524; DUF318. DR Pfam; PF03773; ArsP_1; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 365 UPF0718 protein MJ0584. FT /FTId=PRO_0000106944. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 174 194 Helical. {ECO:0000255}. FT TRANSMEM 201 221 Helical. {ECO:0000255}. FT TRANSMEM 245 265 Helical. {ECO:0000255}. FT TRANSMEM 282 302 Helical. {ECO:0000255}. FT TRANSMEM 308 328 Helical. {ECO:0000255}. FT TRANSMEM 344 364 Helical. {ECO:0000255}. SQ SEQUENCE 365 AA; 39663 MW; FB7C58364885C699 CRC64; MKMDVMSFIM NIINVMINTI IDYLNVNRVL ALLMAFLMAG GIASMINKNF IIKYFGSNTP KYISYTVAAV SGSLLAVCSC TILPLFASIY KRGAGIGPAT TFLFSGPAIN VLAIFYSAAL LGWDIGFLRA VFAVVVSILI GLSMEIIFKS HEKKRALRVP KADKISDRPL YQTITFFALQ FIMLLVITAS PKLFPTLSMP LYDGFLLKHL LFIILGIILA VTTKIWFKDE EIKNWLRESF TLLKIVFPLL IIGVAIAGAI KAIIPPSYIA TYVGGNSITA NFIASFIGAL MYFATLTEVP IIKALMELGM GVGPAMALLL AGPSLSIPTV LTISKVLGKT KALTYLGLVV IFSTICGYIA GIILR // ID Y631_METJA Reviewed; 169 AA. AC Q58048; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Putative hydrogenase maturation protease MJ0631; DE EC=3.4.23.-; GN OrderedLocusNames=MJ0631; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase A31 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98623.1; -; Genomic_DNA. DR PIR; G64378; G64378. DR ProteinModelPortal; Q58048; -. DR STRING; 243232.MJ_0631; -. DR MEROPS; A31.003; -. DR EnsemblBacteria; AAB98623; AAB98623; MJ_0631. DR KEGG; mja:MJ_0631; -. DR eggNOG; arCOG04429; Archaea. DR eggNOG; COG0680; LUCA. DR InParanoid; Q58048; -. DR KO; K08315; -. DR OMA; VAFYFPI; -. DR PhylomeDB; Q58048; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0004175; F:endopeptidase activity; IBA:GO_Central. DR GO; GO:0008047; F:enzyme activator activity; IEA:InterPro. DR GO; GO:0006464; P:cellular protein modification process; IBA:GO_Central. DR GO; GO:0016485; P:protein processing; IBA:GO_Central. DR Gene3D; 3.40.50.1450; -; 1. DR InterPro; IPR004420; Pept_A31_hyd_mat_HycI. DR InterPro; IPR023430; Pept_HybD-like_dom. DR InterPro; IPR000671; Peptidase_A31. DR Pfam; PF01750; HycI; 1. DR PRINTS; PR00446; HYDRGNUPTAKE. DR SUPFAM; SSF53163; SSF53163; 1. DR TIGRFAMs; TIGR00142; hycI; 1. DR TIGRFAMs; TIGR00072; hydrog_prot; 1. PE 3: Inferred from homology; KW Aspartyl protease; Complete proteome; Hydrolase; Protease; KW Reference proteome. FT CHAIN 1 169 Putative hydrogenase maturation protease FT MJ0631. FT /FTId=PRO_0000201949. SQ SEQUENCE 169 AA; 19271 MW; 398028DD88236EE7 CRC64; MKEMLLDKLK NCKKLVIMGI GNELKGDDAV GIYVVKKLMR YFGEEKEFIN IKNLYLINAG TVPDFFTDIL KEIKPTHILI IDCALMDKDV GEVKIIKEDE IINYSFSTHT LPLSIIVKYL KKFINAEIII LGIQPKIIDF CPISEEVKLS GDKLVNTLIE IIEELKLAK // ID Y632_METJA Reviewed; 363 AA. AC Q58049; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 83. DE RecName: Full=Uncharacterized ATP-binding protein MJ0632; GN OrderedLocusNames=MJ0632; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98624.1; -; Genomic_DNA. DR PIR; H64378; H64378. DR ProteinModelPortal; Q58049; -. DR SMR; Q58049; 273-363. DR STRING; 243232.MJ_0632; -. DR DNASU; 1451498; -. DR EnsemblBacteria; AAB98624; AAB98624; MJ_0632. DR KEGG; mja:MJ_0632; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q58049; -. DR KO; K06921; -. DR OMA; VINEMKY; -. DR PhylomeDB; Q58049; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 363 Uncharacterized ATP-binding protein FT MJ0632. FT /FTId=PRO_0000184670. FT NP_BIND 29 36 ATP. {ECO:0000255}. SQ SEQUENCE 363 AA; 43204 MW; FEB47501ABE63810 CRC64; MKFFNREKEI EEILHIIESE PQRINFIFGS INSGKTALIN EIINNRLNKD KYVVFYFDLR EIFISKYDDF IEVLFEEYEE PFIDKVKRLF LSLIKDYPDV IKSYALLNIT GVVDSIPIPK NTLNELLKKR NVKNVFRYIT SVLIKIKREG KQPIIIIDEL QKIGDLKLNG FLIYELFNYF VSLTKHKHLC HVFCLSSDSL FIERVYNEAM LEGRCKYILV DDFDRETALK FMDFLAKENN INLTNEDKEL IYNYVGGKPI DIIYVINEMK YKKLEDILTS MLKEETQKLK YFLENVKEED EELYKKVVDA LKIFKDSYEI EDIKIPKKLR EFLVKKNILF LNPIEGTLKP QSFLVWNAIK RIL // ID Y635_METJA Reviewed; 283 AA. AC Q58052; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0635; GN OrderedLocusNames=MJ0635; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98633.1; -; Genomic_DNA. DR PIR; C64379; C64379. DR ProteinModelPortal; Q58052; -. DR STRING; 243232.MJ_0635; -. DR EnsemblBacteria; AAB98633; AAB98633; MJ_0635. DR KEGG; mja:MJ_0635; -. DR eggNOG; arCOG08205; Archaea. DR eggNOG; ENOG41110WX; LUCA. DR OMA; IIAGTKQ; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 283 Uncharacterized protein MJ0635. FT /FTId=PRO_0000106963. SQ SEQUENCE 283 AA; 32502 MW; 1CE52FC8457C5E20 CRC64; MKFMRIVRIL AILLALIIGT SLCGCLNDSK SEADELIKML PVDYNGFVYV NFKNIEDSKY SSEYRSKILN ALRLGNANGE KTGIYINKTK RMIFSGSGYD RFVIIIEGDY DFDKFKNHLK EIGVNPVEEY GGFKIYTKPN DDKIALTFYK DMIIAGTKQG VYDCINVING EMDSLLKNRE VMEIYDRLPS DACVYEVSGT YSPWYKTVAE GMSISFENND RVKVVRVEKY KDEETAKEKY EELLKKKDRD KEEMEKKGIT ADIKLDGQYL IVTVEGPEDE LKI // ID Y647_METJA Reviewed; 71 AA. AC Q58063; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0647; GN OrderedLocusNames=MJ0647; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98645.1; -; Genomic_DNA. DR PIR; G64380; G64380. DR STRING; 243232.MJ_0647; -. DR EnsemblBacteria; AAB98645; AAB98645; MJ_0647. DR KEGG; mja:MJ_0647; -. DR eggNOG; arCOG09669; Archaea. DR eggNOG; ENOG41110VU; LUCA. DR OMA; IEMSGIW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016272; C:prefoldin complex; IEA:InterPro. DR GO; GO:0006457; P:protein folding; IEA:InterPro. DR Gene3D; 1.10.287.370; -; 1. DR InterPro; IPR002777; PFD_beta-like. DR InterPro; IPR009053; Prefoldin. DR Pfam; PF01920; Prefoldin_2; 1. DR SUPFAM; SSF46579; SSF46579; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 71 Uncharacterized protein MJ0647. FT /FTId=PRO_0000106971. FT COMPBIAS 3 21 Lys-rich. SQ SEQUENCE 71 AA; 8606 MW; 273B54B8197DC95D CRC64; MQKLNKHLKK KKQKRKKMKK KLNNEFQEVI DFLKSLPEGR RVYIEMSGIW IEVTKEEAIN YLKSKINEKE A // ID Y665_METJA Reviewed; 341 AA. AC Q58079; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0665; GN OrderedLocusNames=MJ0665; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98656.1; -; Genomic_DNA. DR PIR; A64383; A64383. DR ProteinModelPortal; Q58079; -. DR STRING; 243232.MJ_0665; -. DR EnsemblBacteria; AAB98656; AAB98656; MJ_0665. DR KEGG; mja:MJ_0665; -. DR eggNOG; arCOG01395; Archaea. DR eggNOG; COG1817; LUCA. DR InParanoid; Q58079; -. DR KO; K09726; -. DR OMA; MKVWIDI; -. DR PhylomeDB; Q58079; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007152; DUF354. DR Pfam; PF04007; DUF354; 1. DR PIRSF; PIRSF005357; UCP005357; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 341 Uncharacterized protein MJ0665. FT /FTId=PRO_0000106981. SQ SEQUENCE 341 AA; 38789 MW; DC678410BC847458 CRC64; MINLDVWIDL TNAPHVHYFC QLIKKFEKEG IEYLLTFRDS GNLAKLVEIY NFVGKCIGKH GNTLKDKLIF YAERVIGLTE LISNVKPKVA IAKHSVELPR VAFGLNIPVI FVVDNEHAEA QNKLTLPLAD EIIKPIATDE NKLKEFGGRN FISFEGTCEV ANVNSRLKGY YPIDNEILKK LGICDDNPTI VMRPCPNSSY CNGHKDILPK IIEKLQKRID CNIVVFPRDE HQKEIYREVN AIVPKETIDA LSLLYNSDFM IGAGGTMNRE SAILGIPTVS CYPQELLGVD KYLIEKDRMI HTNDIKEIIN YVEDNLGKRM GVIELEDPTD LMFERVCNYL K // ID Y687_METJA Reviewed; 335 AA. AC Q58100; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-MAY-2016, entry version 72. DE RecName: Full=Uncharacterized protein MJ0687; GN OrderedLocusNames=MJ0687; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98682.1; -; Genomic_DNA. DR PIR; G64385; G64385. DR ProteinModelPortal; Q58100; -. DR STRING; 243232.MJ_0687; -. DR EnsemblBacteria; AAB98682; AAB98682; MJ_0687. DR KEGG; mja:MJ_0687; -. DR eggNOG; arCOG02470; Archaea. DR eggNOG; COG2834; LUCA. DR InParanoid; Q58100; -. DR OMA; NAMATKQ; -. DR PhylomeDB; Q58100; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019207; DUF2092. DR InterPro; IPR025377; DUF4367. DR InterPro; IPR029046; LolA/LolB/LppX. DR Pfam; PF09865; DUF2092; 1. DR Pfam; PF14285; DUF4367; 1. DR SUPFAM; SSF89392; SSF89392; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 335 Uncharacterized protein MJ0687. FT /FTId=PRO_0000106990. SQ SEQUENCE 335 AA; 38437 MW; B42CF3FA368841C3 CRC64; MNYKYLILSL FLIVGVFFAG CTQQMNADEI AKKMQEKYEA MKSMEADVLI TTNIMGQTET MQYKYAFEKP NKFYMENDDV LIVCDGKTYY MYDKKKNQYT KMEIKGELNN MFNPDYGKFI KSMLEKFNVS YLGEKTYDGR KCYVLELISK ENPEEKMKMY VDEEYWQPLK IEMDGVTIEY KNVKFNVDVP DDRFKFVPPE GAKLMSSGAM TTSKNIDEVQ KDVSFKILVP KYTAGLELQN AMATKQNANN EESETVILTY GENGELAIIE SKDNKPLTIP ENGSNLITLK NGVKALISDS GDVKMLMFEY NGIKVIIAGK LDKNELIKIA NSMIE // ID Y694_METJA Reviewed; 414 AA. AC Q58105; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 79. DE RecName: Full=Uncharacterized NOP5 family protein MJ0694; GN OrderedLocusNames=MJ0694; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- INTERACTION: CC P54066:rpl7ae; NbExp=4; IntAct=EBI-2944259, EBI-2944269; CC -!- SIMILARITY: Belongs to the NOP5/NOP56 family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 Nop domain. {ECO:0000255|PROSITE- CC ProRule:PRU00690}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98689.1; -; Genomic_DNA. DR PIR; F64386; F64386. DR PDB; 3T7Z; X-ray; 1.70 A; A=1-119. DR PDBsum; 3T7Z; -. DR ProteinModelPortal; Q58105; -. DR IntAct; Q58105; 2. DR STRING; 243232.MJ_0694; -. DR EnsemblBacteria; AAB98689; AAB98689; MJ_0694. DR KEGG; mja:MJ_0694; -. DR eggNOG; arCOG01923; Archaea. DR eggNOG; COG1498; LUCA. DR InParanoid; Q58105; -. DR KO; K14564; -. DR OMA; ACKLAIA; -. DR PhylomeDB; Q58105; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030515; F:snoRNA binding; IBA:GO_Central. DR GO; GO:0000154; P:rRNA modification; IBA:GO_Central. DR InterPro; IPR002687; Nop_dom. DR InterPro; IPR012976; NOSIC. DR Pfam; PF01798; Nop; 1. DR SMART; SM00931; NOSIC; 1. DR SUPFAM; SSF89124; SSF89124; 1. DR PROSITE; PS51358; NOP; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 414 Uncharacterized NOP5 family protein FT MJ0694. FT /FTId=PRO_0000219034. FT DOMAIN 246 360 Nop. {ECO:0000255|PROSITE- FT ProRule:PRU00690}. FT COMPBIAS 349 414 Asp/Glu/Lys-rich. FT STRAND 2 7 {ECO:0000244|PDB:3T7Z}. FT STRAND 10 15 {ECO:0000244|PDB:3T7Z}. FT HELIX 23 25 {ECO:0000244|PDB:3T7Z}. FT STRAND 28 31 {ECO:0000244|PDB:3T7Z}. FT HELIX 34 36 {ECO:0000244|PDB:3T7Z}. FT HELIX 37 46 {ECO:0000244|PDB:3T7Z}. FT HELIX 48 59 {ECO:0000244|PDB:3T7Z}. FT STRAND 63 65 {ECO:0000244|PDB:3T7Z}. FT HELIX 66 68 {ECO:0000244|PDB:3T7Z}. FT HELIX 74 81 {ECO:0000244|PDB:3T7Z}. FT HELIX 83 89 {ECO:0000244|PDB:3T7Z}. FT HELIX 96 117 {ECO:0000244|PDB:3T7Z}. SQ SEQUENCE 414 AA; 47799 MW; A9092EFC3C82C407 CRC64; MIYVTFTPYG AFGVKDNKEV SGLEDIEYKK LFNEEEIPDI MFKLKTQPNK IADELKEEWG DEIKLETLST EPFNIGEFLR NNLFKVGKEL GYFNNYDEFR KKMHYWSTEL TKKVIKSYAQ QKDKIIIQVA EAISDLDKTL NLLSERLREW YSLYFPELDH LVNKHEVYAN LITKLGKRKN FTKSQLKKIL PSKLAGKIAE AAKNSMGGEL EDYDLDVIVK FAEEINHLYE KRKELYNYLE KLMNEEAPNI TKLAGVSLGA RLIGLAGGLE KLAKMPASTI QVLGAEKALF AHLRMGVEPP KHGIIYNHPL IQGSPHWQRG KIARALACKL AIAARADYVG DYIADELLEK LNKRVEEIRR KYPKPPKKKK KEKPKAKKKE KKGKKEKSKK KKDKKKDKKG KKERKVIGKT KSRK // ID Y739_METJA Reviewed; 151 AA. AC Q58149; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0739; GN OrderedLocusNames=MJ0739; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the M.jannaschii CC MJ0150/MJ0739/MJ0745/MJ1460/MJ1642 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98744.1; -; Genomic_DNA. DR PIR; C64392; C64392. DR ProteinModelPortal; Q58149; -. DR STRING; 243232.MJ_0739; -. DR EnsemblBacteria; AAB98744; AAB98744; MJ_0739. DR KEGG; mja:MJ_0739; -. DR eggNOG; arCOG01688; Archaea. DR eggNOG; COG1719; LUCA. DR InParanoid; Q58149; -. DR KO; K07013; -. DR OMA; FEANNIG; -. DR PhylomeDB; Q58149; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019642; DUF2507. DR InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd. DR InterPro; IPR004096; V4R. DR Pfam; PF10702; DUF2507; 1. DR Pfam; PF02830; V4R; 1. DR SMART; SM00989; V4R; 1. DR SUPFAM; SSF111126; SSF111126; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 151 Uncharacterized protein MJ0739. FT /FTId=PRO_0000107010. SQ SEQUENCE 151 AA; 17461 MW; 465891BCFEE7044D CRC64; MISVKDVVNY NPEEYKFKSR EIPSDLLAII IYAYMQKVKD LGSDTTLYEI GYEVGRLVSP KSYEDIKKFF EANNIGYIEI KEKDNGEVEI KVKDCIFCRT QKSEEPMCDF EAGLIAGFLE SIKNKKYFVK EMYCQAQGYD ACVFIAKPLH N // ID Y764_METJA Reviewed; 116 AA. AC Q58174; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0764; GN OrderedLocusNames=MJ0764; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98760.1; -; Genomic_DNA. DR PIR; D64395; D64395. DR PDB; 2B8M; X-ray; 1.70 A; A=1-116. DR PDBsum; 2B8M; -. DR ProteinModelPortal; Q58174; -. DR SMR; Q58174; 1-108. DR STRING; 243232.MJ_0764; -. DR EnsemblBacteria; AAB98760; AAB98760; MJ_0764. DR KEGG; mja:MJ_0764; -. DR eggNOG; ENOG4102TPQ; Archaea. DR eggNOG; COG1917; LUCA. DR OMA; FFVIKAP; -. DR EvolutionaryTrace; Q58174; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0045735; F:nutrient reservoir activity; IEA:InterPro. DR Gene3D; 2.60.120.10; -; 1. DR InterPro; IPR006045; Cupin_1. DR InterPro; IPR014710; RmlC-like_jellyroll. DR InterPro; IPR011051; RmlC_Cupin. DR Pfam; PF00190; Cupin_1; 1. DR SUPFAM; SSF51182; SSF51182; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 116 Uncharacterized protein MJ0764. FT /FTId=PRO_0000107022. FT STRAND 16 22 {ECO:0000244|PDB:2B8M}. FT STRAND 27 34 {ECO:0000244|PDB:2B8M}. FT STRAND 48 61 {ECO:0000244|PDB:2B8M}. FT STRAND 67 70 {ECO:0000244|PDB:2B8M}. FT STRAND 74 77 {ECO:0000244|PDB:2B8M}. FT STRAND 82 86 {ECO:0000244|PDB:2B8M}. FT STRAND 89 99 {ECO:0000244|PDB:2B8M}. FT HELIX 103 106 {ECO:0000244|PDB:2B8M}. SQ SEQUENCE 116 AA; 13568 MW; 4DCED95DE14DFADD CRC64; MIEKVYEFKR DAKTKVVEKL VNTEHVQINH IVLPRGEQMP KHYSNSYVHL IIIKGEMTLT LEDQEPHNYK EGNIVYVPFN VKMLIQNINS DILEFFVVKA PHPKKLNAPE DPIKCE // ID Y766_METJA Reviewed; 66 AA. AC Q58176; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 60. DE RecName: Full=Uncharacterized protein MJ0766; GN OrderedLocusNames=MJ0766; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0582. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98773.1; -; Genomic_DNA. DR PIR; F64395; F64395. DR STRING; 243232.MJ_0766; -. DR EnsemblBacteria; AAB98773; AAB98773; MJ_0766. DR KEGG; mja:MJ_0766; -. DR eggNOG; arCOG02639; Archaea. DR eggNOG; COG5561; LUCA. DR OMA; SEPACRY; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR014925; Uncharacterised_CGGC-dom. DR Pfam; PF08821; CGGC; 1. DR SMART; SM01078; CGGC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 66 Uncharacterized protein MJ0766. FT /FTId=PRO_0000107023. SQ SEQUENCE 66 AA; 7235 MW; A206FD6CB000CCCB CRC64; MSVITCGGCP GRLGLNQIKQ LIGKNGAEVV HFATCMTAFK PKCRYAEKMK EEIEKMGAKV VMSSHF // ID Y776_METJA Reviewed; 383 AA. AC Q58186; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ0776; GN OrderedLocusNames=MJ0776; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ATP-grasp domain. {ECO:0000255|PROSITE- CC ProRule:PRU00409}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98766.1; -; Genomic_DNA. DR PIR; H64396; H64396. DR ProteinModelPortal; Q58186; -. DR STRING; 243232.MJ_0776; -. DR EnsemblBacteria; AAB98766; AAB98766; MJ_0776. DR KEGG; mja:MJ_0776; -. DR eggNOG; arCOG01595; Archaea. DR eggNOG; COG2232; LUCA. DR InParanoid; Q58186; -. DR KO; K06913; -. DR OMA; NTRPVVN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. DR Gene3D; 3.30.1490.20; -; 1. DR Gene3D; 3.30.470.20; -; 1. DR InterPro; IPR011761; ATP-grasp. DR InterPro; IPR003806; ATP-grasp_DUF201-type. DR InterPro; IPR013815; ATP_grasp_subdomain_1. DR InterPro; IPR013816; ATP_grasp_subdomain_2. DR InterPro; IPR016677; UCP016817_carboligase. DR Pfam; PF02655; ATP-grasp_3; 1. DR PIRSF; PIRSF016817; UCP016817_carboligase; 1. DR PROSITE; PS50975; ATP_GRASP; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 383 Uncharacterized protein MJ0776. FT /FTId=PRO_0000107027. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT DOMAIN 131 303 ATP-grasp. {ECO:0000255|PROSITE- FT ProRule:PRU00409}. SQ SEQUENCE 383 AA; 43948 MW; FD11A7D7E8C241AC CRC64; MNNFTLFLFS CLYFIGGNLK ALVLGINTRP VVNSLKKLGF YVYSVSYYAP EDLNADEKYY LINPLVHGRL KENYDENKLI EIANKLADEV DCIFITSGVF EFENSKIPGW DNVIGNGPKK INEISNKYKT YKKLKNLGFN IPETKKINNK TQLYKFLEEF KTCILKPIYG SGGSILKIEL NNFDDEIINE IKFPIIAQEY IRGKSFSANF IGNTFITFNK QIIIKGMYAG NLTPYINLPN KFVEIFGEVI ESFELKGMSG IDFLIKDNGP YIVDINPRIL GTYETIEMSA SQNLAMVLLN NKYAKEIKPR KVYIKRILFA KEKIIANISK RDFIHDIPKK NAVIEKGEPI ATVIAKENIK SIINSVYEEC AEYEKRKEDR ENI // ID Y783_METJA Reviewed; 186 AA. AC Q58193; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0783; GN OrderedLocusNames=MJ0783; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98780.1; -; Genomic_DNA. DR PIR; G64397; G64397. DR PDB; 2B0A; X-ray; 1.45 A; A=2-186. DR PDBsum; 2B0A; -. DR ProteinModelPortal; Q58193; -. DR SMR; Q58193; 2-186. DR STRING; 243232.MJ_0783; -. DR EnsemblBacteria; AAB98780; AAB98780; MJ_0783. DR KEGG; mja:MJ_0783; -. DR eggNOG; arCOG02462; Archaea. DR eggNOG; COG1878; LUCA. DR InParanoid; Q58193; -. DR OMA; HLCTHID; -. DR PhylomeDB; Q58193; -. DR EvolutionaryTrace; Q58193; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004061; F:arylformamidase activity; IBA:GO_Central. DR GO; GO:0019441; P:tryptophan catabolic process to kynurenine; IBA:GO_Central. DR InterPro; IPR007325; KFase. DR Pfam; PF04199; Cyclase; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein MJ0783. FT /FTId=PRO_0000107034. FT STRAND 3 5 {ECO:0000244|PDB:2B0A}. FT STRAND 22 28 {ECO:0000244|PDB:2B0A}. FT STRAND 31 37 {ECO:0000244|PDB:2B0A}. FT STRAND 42 47 {ECO:0000244|PDB:2B0A}. FT HELIX 49 52 {ECO:0000244|PDB:2B0A}. FT HELIX 61 63 {ECO:0000244|PDB:2B0A}. FT STRAND 65 73 {ECO:0000244|PDB:2B0A}. FT TURN 74 76 {ECO:0000244|PDB:2B0A}. FT STRAND 86 91 {ECO:0000244|PDB:2B0A}. FT HELIX 94 97 {ECO:0000244|PDB:2B0A}. FT HELIX 101 105 {ECO:0000244|PDB:2B0A}. FT HELIX 113 118 {ECO:0000244|PDB:2B0A}. FT STRAND 123 129 {ECO:0000244|PDB:2B0A}. FT STRAND 131 133 {ECO:0000244|PDB:2B0A}. FT HELIX 134 142 {ECO:0000244|PDB:2B0A}. FT STRAND 146 149 {ECO:0000244|PDB:2B0A}. FT HELIX 153 158 {ECO:0000244|PDB:2B0A}. FT STRAND 162 169 {ECO:0000244|PDB:2B0A}. FT STRAND 176 185 {ECO:0000244|PDB:2B0A}. SQ SEQUENCE 186 AA; 21238 MW; E4A68C828AE48310 CRC64; MEILDLTQTL INFPYPGDPE LRIIEKKIDG FIVSEIIMGS HLCTHIDYPK HVGLENRIPF KDGIIKGKGY CISLDDFERN KLPACDILLI YTGFSKYWGR DEYFEKIPEI PFLDDIIKSN IKCVGIDACT IGGFEEHKRL LSNNILIIEN LNENLKNLVG KSFYFLGLPL KIFDIDASPI RCIAIL // ID Y795_METJA Reviewed; 504 AA. AC Q58205; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0795; GN OrderedLocusNames=MJ0795; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1506 and MJ1561. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98798.1; -; Genomic_DNA. DR PIR; C64399; C64399. DR ProteinModelPortal; Q58205; -. DR STRING; 243232.MJ_0795; -. DR EnsemblBacteria; AAB98798; AAB98798; MJ_0795. DR KEGG; mja:MJ_0795; -. DR eggNOG; arCOG04400; Archaea. DR eggNOG; COG1361; LUCA. DR InParanoid; Q58205; -. DR OMA; ELHCQIN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 504 Uncharacterized protein MJ0795. FT /FTId=PRO_0000107046. FT TRANSMEM 6 26 Helical. {ECO:0000255}. SQ SEQUENCE 504 AA; 57147 MW; A1A659DB7EAEC74B CRC64; MKRLKNLFII FIFLFLLSQV SAYITFKNID YNAQYLEPSK TYDLYITIES DKEINNTVVY IEPTNQISKE NIEIIRGKQW IGHLFPYEYG VAHLIIKINP NAPNYDYKIT GYCNYTKGNQ QYSENRIFTL PVRGKANLVI ETTNNILKVG NNQILLLLTN KGTGTAENIK IEFQNSNNLM VLGDNTFTIS ALGSKTSTYI PLTIFAKKEG VYSINYKISY KNPYNLLELT QKSETIEGDS KTETLTYQNK NIVEETGILT FNVFPNELIS INIKNPTITV GKIENLTISI KNNYKDSLFV VQISKYFIGN NQKSIFIKKG ETKNLTFQIK VDKEGVTSIP IVIYFDNNQI EKNLTINVVG KADLVLSGID IESSFNEIKI TGDIDNIGTG KAKSVLISIE KTKNIIPKKP YENYFVGTLN PDDYGSFELH CQINGNVNEI PLKISYRDED NNLITIYKTV KISKEVVSLK TNNNGGINYL VVGIAILFCV GVVYLIYRGF VKKK // ID Y797_METJA Reviewed; 367 AA. AC Q58207; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized ABC transporter permease MJ0797; GN OrderedLocusNames=MJ0797; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the ABC-4 integral membrane protein family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98792.1; -; Genomic_DNA. DR PIR; E64399; E64399. DR STRING; 243232.MJ_0797; -. DR TCDB; 3.A.1.122.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAB98792; AAB98792; MJ_0797. DR KEGG; mja:MJ_0797; -. DR eggNOG; arCOG02312; Archaea. DR eggNOG; COG0577; LUCA. DR InParanoid; Q58207; -. DR KO; K02004; -. DR OMA; FTSNFQT; -. DR PhylomeDB; Q58207; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR003838; ABC_permease_dom. DR InterPro; IPR025857; MacB_PCD. DR Pfam; PF02687; FtsX; 1. DR Pfam; PF12704; MacB_PCD; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 367 Uncharacterized ABC transporter permease FT MJ0797. FT /FTId=PRO_0000107049. FT TRANSMEM 18 38 Helical. {ECO:0000255}. FT TRANSMEM 239 259 Helical. {ECO:0000255}. FT TRANSMEM 296 316 Helical. {ECO:0000255}. FT TRANSMEM 329 349 Helical. {ECO:0000255}. SQ SEQUENCE 367 AA; 41039 MW; 3CC882FF21ED3746 CRC64; MYFELAKRNL KRNLLRSILA LLGIIIGVAA ISSLGILGGG LKQGIMENLG SISNYIIVFP NYQNGYTSFD KRDIEKLRVL NCKVIPVYAT SDFVYIKGKN RKAYANIFGI DKNDIKYLNL KVKVSDTSVA VDTFFSNVND VNVGNQLEIK NISLRICGIY NSTFLFPDNS LILTAKTYRR FYGENNYNYS RIILYVKNIN DIDKIKNETD KILNRKEKKC IIISLNSILE AINGVITKVS YFLMGIGAIS LLVAGIGIGN VMLMSVVERT TEIGVMRSIG ASKKDIIILF LYEALILGVI GSLIGAFLSL FFGYLIVHYL LKTSLSYYAI FYMIIGIIFG ILTSLISALY PAYKASKLDP IKSLRNE // ID Y79C_METJA Reviewed; 137 AA. AC P81314; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0796.1; GN OrderedLocusNames=MJ0796.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98802.1; -; Genomic_DNA. DR STRING; 243232.MJ_0796.1; -. DR EnsemblBacteria; AAB98802; AAB98802; MJ_0796.1. DR KEGG; mja:MJ_0796.1; -. DR eggNOG; arCOG09675; Archaea. DR eggNOG; ENOG410YP56; LUCA. DR OMA; NISNFDK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 137 Uncharacterized protein MJ0796.1. FT /FTId=PRO_0000107048. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. SQ SEQUENCE 137 AA; 15905 MW; 9FE225FF3A3C698E CRC64; MMIDNISNFD KVRAVVVAIL LYIFIILVVD GSISSLIGKY ITYPSDEYHI IEFYDFIHII GFLLSLSIST YFSSKDIIKD FAKFFTIFFG ITFILGITLF LGLTFFENHI PSMRGYTTLM LFFFLLNLFK KLDKITN // ID Y802_METJA Reviewed; 188 AA. AC Q58212; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0802; GN OrderedLocusNames=MJ0802; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98803.1; -; Genomic_DNA. DR PIR; B64400; B64400. DR ProteinModelPortal; Q58212; -. DR STRING; 243232.MJ_0802; -. DR EnsemblBacteria; AAB98803; AAB98803; MJ_0802. DR KEGG; mja:MJ_0802; -. DR eggNOG; arCOG04904; Archaea. DR eggNOG; COG4051; LUCA. DR InParanoid; Q58212; -. DR OMA; IYTKVIQ; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR016762; UCP019464_methan. DR Pfam; PF09886; DUF2113; 1. DR PIRSF; PIRSF019464; UCP019464; 1. DR TIGRFAMs; TIGR03291; methan_mark_17; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 188 Uncharacterized protein MJ0802. FT /FTId=PRO_0000107052. SQ SEQUENCE 188 AA; 21768 MW; D651D0C61F9D1028 CRC64; MAEIVVHCED KAGKEIYTKV IQTALEDLLL GKSIIRVEFI AKEKEPYFIL GVLPKHTRRA IKLRDFAEIV EQKKEGGKII YKLKITDETY LPHLLKKIHV IDQPSRFEVV TDSDIDLDME VYDAGKDFID KVMDFMGRVF PEGMRIKNTY IDKAIVCIAS ERPLKDEEIE EALKLKDKLE KMNTAGYY // ID Y821_METJA Reviewed; 56 AA. AC Q58231; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 72. DE RecName: Full=Putative uncharacterized protein MJ0821; GN OrderedLocusNames=MJ0821; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. MJ0821, MJ0820 and CC MJ0819 respectively represent the N-terminal, central and C- CC terminal sections of other members of this family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98833.1; -; Genomic_DNA. DR PIR; E64402; E64402. DR STRING; 243232.MJ_0821; -. DR EnsemblBacteria; AAB98833; AAB98833; MJ_0821. DR KEGG; mja:MJ_0821; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01637; ATPase_2; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 56 Putative uncharacterized protein MJ0821. FT /FTId=PRO_0000184683. SQ SEQUENCE 56 AA; 6512 MW; 7E19C78530493060 CRC64; MKFFNREKEI NKILSIIEGE PNLIYFIYGS LNSGKFNLTE ETQFIYSIVV TDGLFS // ID Y83C_METJA Reviewed; 339 AA. AC P81324; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0835.2; GN OrderedLocusNames=MJ0835.2; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.thermoautotrophicum MTH421. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98835.1; -; Genomic_DNA. DR ProteinModelPortal; P81324; -. DR STRING; 243232.MJ_0835.2; -. DR MEROPS; A24.018; -. DR EnsemblBacteria; AAB98835; AAB98835; MJ_0835.2. DR KEGG; mja:MJ_0835.2; -. DR eggNOG; arCOG02300; Archaea. DR eggNOG; COG1989; LUCA. DR InParanoid; P81324; -. DR KO; K07991; -. DR OMA; RKAMPFA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR009639; Pept_A24A_C_arc. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF06819; Arc_PepC; 1. DR Pfam; PF01478; Peptidase_A24; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 339 Uncharacterized protein MJ0835.2. FT /FTId=PRO_0000107071. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 27 47 Helical. {ECO:0000255}. FT TRANSMEM 48 68 Helical. {ECO:0000255}. FT TRANSMEM 75 95 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. FT TRANSMEM 146 166 Helical. {ECO:0000255}. FT TRANSMEM 180 200 Helical. {ECO:0000255}. FT TRANSMEM 204 224 Helical. {ECO:0000255}. FT TRANSMEM 319 339 Helical. {ECO:0000255}. SQ SEQUENCE 339 AA; 39339 MW; 7A8C60062CEF5BFA CRC64; MDLLNVVYII NFILLLLAAI TDIKERIIPH KYTIAMIIIN LVVGYYYFGF NAIIAFFSTL ILCLILSIGM GGGDVKLFTA LAPIFAYPNS FVFYIPKYIL YLIAISMFIA AVFPMYKILM RYWKDIIPSA CYLTMMLGIL YYFINIYEIP YASIIIWAYI VLSIFVSRKV PKYKEYTKKL GYLFPAYLLF LYIIDTTYFI KYNVLLTSII YLCEIILISI VIYALTGVET SDKKHIEELK EGDILRDVII IDKDGVEVKN LNIMKRIKFL LEHEIKENEK EIILTDGEGL SNEDIRKIKK LYMEGKIPDK LNVIKTYPFV PFVVIGYVIV LMLMKLAII // ID Y856_METJA Reviewed; 181 AA. AC Q58266; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0856; GN OrderedLocusNames=MJ0856; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98860.1; -; Genomic_DNA. DR PIR; H64406; H64406. DR ProteinModelPortal; Q58266; -. DR STRING; 243232.MJ_0856; -. DR EnsemblBacteria; AAB98860; AAB98860; MJ_0856. DR KEGG; mja:MJ_0856; -. DR eggNOG; arCOG04906; Archaea. DR eggNOG; COG4010; LUCA. DR OMA; HGVIFEY; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR017098; UCP037052. DR Pfam; PF09869; DUF2096; 1. DR PIRSF; PIRSF037052; UCP037052; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 181 Uncharacterized protein MJ0856. FT /FTId=PRO_0000107080. SQ SEQUENCE 181 AA; 21124 MW; DBB6B58BCD8F9F56 CRC64; MEMGNGMKDA RNLDKQWVVL SELSAELVNR GIKVPEIVFE KLRLANALLS YYILDPHASI NILANVEREL NYVQSQLFSL CDTELTEKYL DRMIKAIRGE INAKFPVSKS NYNREVKKRG KVEAIRVKLQ KEMQIERLSD LGEWHGVIFE YSDEKDKVII EGNIDRVKRA LKDFAFMWKE D // ID Y85A_METJA Reviewed; 109 AA. AC P81315; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Putative transposase MJ0856.1; GN OrderedLocusNames=MJ0856.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the transposase 35 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98861.1; -; Genomic_DNA. DR ProteinModelPortal; P81315; -. DR STRING; 243232.MJ_0856.1; -. DR EnsemblBacteria; AAB98861; AAB98861; MJ_0856.1. DR KEGG; mja:MJ_0856.1; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR InParanoid; P81315; -. DR KO; K07496; -. DR PhylomeDB; P81315; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW. DR GO; GO:0032196; P:transposition; IEA:UniProtKB-KW. DR InterPro; IPR010095; Transposase_IS605_OrfB_C. DR Pfam; PF07282; OrfB_Zn_ribbon; 1. PE 3: Inferred from homology; KW Complete proteome; DNA recombination; DNA-binding; Metal-binding; KW Reference proteome; Transposable element; Transposition; Zinc. FT CHAIN 1 109 Putative transposase MJ0856.1. FT /FTId=PRO_0000107081. FT METAL 36 36 Zinc. {ECO:0000255}. FT METAL 39 39 Zinc. {ECO:0000255}. FT METAL 62 62 Zinc. {ECO:0000255}. FT METAL 65 65 Zinc. {ECO:0000255}. SQ SEQUENCE 109 AA; 12230 MW; 23D38A215FA87354 CRC64; MHNISAKKFL GYLKNKCLEF GVKVIEGNPA YTSIKCPNCG SRLSQLYKLA DERALPSRLM YCFDCGFYAD RDTVAVFNLI KRFTGLYPFS PKSNEPIAEG TVFPDEAMG // ID Y878_METJA Reviewed; 414 AA. AC Q58288; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=Uncharacterized lipoprotein MJ0878; DE Flags: Precursor; GN OrderedLocusNames=MJ0878; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98893.1; -; Genomic_DNA. DR PIR; F64409; F64409. DR ProteinModelPortal; Q58288; -. DR STRING; 243232.MJ_0878; -. DR EnsemblBacteria; AAB98893; AAB98893; MJ_0878. DR KEGG; mja:MJ_0878; -. DR eggNOG; arCOG03417; Archaea. DR eggNOG; COG0614; LUCA. DR InParanoid; Q58288; -. DR KO; K02016; -. DR OMA; YLENDPL; -. DR PhylomeDB; Q58288; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 414 Uncharacterized lipoprotein MJ0878. FT /FTId=PRO_0000014005. FT DOMAIN 119 389 Fe/B12 periplasmic-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00344}. FT LIPID 21 21 S-archaeol cysteine. {ECO:0000255}. SQ SEQUENCE 414 AA; 47112 MW; BF7F9F2D294E62BF CRC64; MKKLLAIGIL CIMVTAVMSG CVSEKEININ NSNKITTNMP VSEKNITKIL KYAKNMNLIY YDENGNIVNP YNGDKWKYKV FIDATGQKFL LKNKDDPVPS WAKEKLGDNF KVINVPLTRV IVMSSTEIAL MEAINDDGSV IGSVKGIMWG KSYKWYFKDI NKSLAEGKII DVGSSSNPNW DKIIEINPQV IFVYPGYDGD KIIAKCKELG ITYVADAEYL ENDPLGRCEW VKMFAAFYNK EPEAKRYFEK VEDNCLKVIN KTKNCPKVTV AWGYNSQWGC YVPENNSYVA KEIMFYCNGD YIFKDLNGTG SAKINYETFA ERAKDADVWV VPSSTAWLST FKEDNPGYET FKAVKNGRVF CESDDYWQLG LLKTDEVIMD LATILHPEAF KGRKTHFFLK YNIENNTATP FIAK // ID Y904_METJA Reviewed; 195 AA. AC Q58314; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0904; GN OrderedLocusNames=MJ0904; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98914.1; -; Genomic_DNA. DR PIR; H64412; H64412. DR ProteinModelPortal; Q58314; -. DR STRING; 243232.MJ_0904; -. DR EnsemblBacteria; AAB98914; AAB98914; MJ_0904. DR KEGG; mja:MJ_0904; -. DR eggNOG; arCOG05057; Archaea. DR eggNOG; ENOG410YACR; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 195 Uncharacterized protein MJ0904. FT /FTId=PRO_0000107096. FT TRANSMEM 175 195 Helical. {ECO:0000255}. SQ SEQUENCE 195 AA; 21909 MW; ED92E6C6B7E30392 CRC64; MNIENLAYNS SSDVLKAKIK NDKFPVNLTV QYWVDVSRGS NIYYKSSIFQ TEIYPKSEKE LIVPLTLGDL ESGIYNITLY VRVNNFALFN YQKVPVILKK SISIEINGSK GVMQQKSNKE SDEIINETSE THKNMTIDIK NLSNNKDNKS NIEESTAKNV KSNIETKKSA DNNSILGKIS GFFGSIVSTI FSLFG // ID Y919_METJA Reviewed; 149 AA. AC Q58329; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0919; GN OrderedLocusNames=MJ0919; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98927.1; -; Genomic_DNA. DR PIR; G64414; G64414. DR ProteinModelPortal; Q58329; -. DR STRING; 243232.MJ_0919; -. DR EnsemblBacteria; AAB98927; AAB98927; MJ_0919. DR KEGG; mja:MJ_0919; -. DR eggNOG; arCOG02263; Archaea. DR eggNOG; COG2450; LUCA. DR KO; K09152; -. DR OMA; GYIVIAK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0000917; P:barrier septum assembly; IEA:InterPro. DR InterPro; IPR007561; Cell_div_SepF/SepF-rel. DR Pfam; PF04472; DUF552; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 149 Uncharacterized protein MJ0919. FT /FTId=PRO_0000107104. SQ SEQUENCE 149 AA; 16953 MW; 07B1A6483F957AE4 CRC64; MLEKLKKLLS KKGDNFSTPA PVSVDDYLEE IEEIPLTPVE EEKVIIKVCS IEDEKDAVNA IVMAEAGYIV IAKTPNLEKE IDDEFIEIIR KMRNEVAKFG GMLLALGDEH LLITPRNVVI EKLIKEKKEE SNVTKENIEI KEEKEENSE // ID Y921_METJA Reviewed; 300 AA. AC Q58331; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0921; GN OrderedLocusNames=MJ0921; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98925.1; -; Genomic_DNA. DR PIR; A64415; A64415. DR ProteinModelPortal; Q58331; -. DR STRING; 243232.MJ_0921; -. DR EnsemblBacteria; AAB98925; AAB98925; MJ_0921. DR KEGG; mja:MJ_0921; -. DR eggNOG; arCOG01116; Archaea. DR eggNOG; COG1571; LUCA. DR InParanoid; Q58331; -. DR OMA; QNCVSIA; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR013696; DUF1743. DR InterPro; IPR017674; Methan_mark_11. DR Pfam; PF08489; DUF1743; 1. DR TIGRFAMs; TIGR03280; methan_mark_11; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 300 Uncharacterized protein MJ0921. FT /FTId=PRO_0000107106. SQ SEQUENCE 300 AA; 33031 MW; 601DB0F8F1BF822C CRC64; MSVNYKSVIA MVDDALNLVE IVEEHPCPNG SEWVIYQYQR TSPLILSAWR EGNKHHFVTK IGKEKLNLVP SLSAAGIEEV YIENNRVHIV YAGLAGGGVG AELRKGAKNV LEVNILEKGG GSRLGKAEVI TPKMEKVIIG IDDTDTKEEG ATWVLAHEIG LEVEKEGLGY YLDHTIVQLY PGNPNKTQNC VSIALSFAVY PEYKYKLDKF IKKLLKERSL SDETAMAVYY GLFPSKSMKL FALKAKKEMV KIEEAKSIAL RNNIKIIPIN GEGGIIGAVA ALGLAEHHSL APKLCEDIKL // ID Y926_METJA Reviewed; 87 AA. AC Q58336; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0926; GN OrderedLocusNames=MJ0926; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98938.1; -; Genomic_DNA. DR PIR; F64415; F64415. DR EnsemblBacteria; AAB98938; AAB98938; MJ_0926. DR KEGG; mja:MJ_0926; -. DR eggNOG; arCOG06658; Archaea. DR eggNOG; COG1667; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 87 Uncharacterized protein MJ0926. FT /FTId=PRO_0000107110. SQ SEQUENCE 87 AA; 10458 MW; 2FD59227A291A76D CRC64; MELSIENELD KNILSILKDQ DLIEDYALKV KIERCNNKYI CTCDVIIIQK KLFIKKPVKI EPIKKRLMEI LEAKPYNVEY RIDIRLY // ID Y976_METJA Reviewed; 366 AA. AC Q58386; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0976; GN OrderedLocusNames=MJ0976; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98982.1; -; Genomic_DNA. DR PIR; H64421; H64421. DR STRING; 243232.MJ_0976; -. DR EnsemblBacteria; AAB98982; AAB98982; MJ_0976. DR KEGG; mja:MJ_0976; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 366 Uncharacterized protein MJ0976. FT /FTId=PRO_0000107126. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 66 86 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 198 218 Helical. {ECO:0000255}. FT TRANSMEM 225 245 Helical. {ECO:0000255}. SQ SEQUENCE 366 AA; 42587 MW; 59302DEF70EEE594 CRC64; MSEDSNPKND LKLKMYETFR SHIERAENSF WTYMLFYLQF LVGINGAVGI LCRYLSNNLQ NFPTEIIIAF LALVNILLSL IGIIVIIERG KWFFRNMILT VNLERYILKE EHIKIIPKRY SKFDNFNKVI DTTGRIFISI FIGIYMISVI ALGYLANSCK TIILFGTGFF IIVVIIYFLD LLDWIYRRID SNEYRKVIGV VLFISFIPPL MNYFIYDIIN LICSYIPESF IVAMIVILIF VIIDVYYNAK KHIENTIIML SLERTVNDID DIIKILKNIR LDDTKKEELK KKLRKIKKLI ENVIKLLGGT SENGTQNNNL EEAKSKITEA CRKISGNNIF EAINELNEAK YIINNKINEL TQSDSS // ID Y991_METJA Reviewed; 144 AA. AC Q58398; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0991; GN OrderedLocusNames=MJ0991; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98996.1; -; Genomic_DNA. DR PIR; G64423; G64423. DR STRING; 243232.MJ_0991; -. DR EnsemblBacteria; AAB98996; AAB98996; MJ_0991. DR KEGG; mja:MJ_0991; -. DR eggNOG; arCOG09630; Archaea. DR eggNOG; ENOG41111RZ; LUCA. DR OMA; DYDGIDD; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 144 Uncharacterized protein MJ0991. FT /FTId=PRO_0000107134. SQ SEQUENCE 144 AA; 17271 MW; 00F1CFCD0007A09E CRC64; MVIIMPTKTI TLKVPSNISK KKIEEAIKKL ELEEKYKKTE NFKLFVKDED LKMKIYKIAE FVEDYLKKKY SDEEFEIVLD YDGIDDKVVV EIVFKKKLDK RELKDIKVII RKLKEIIFDA WRKVDEKYPD MRGFLIVTSD LEVL // ID Y996_METJA Reviewed; 451 AA. AC Q58403; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 30-MAY-2000, sequence version 2. DT 11-NOV-2015, entry version 75. DE RecName: Full=Metalloprotease MJ0996; DE EC=3.4.-.-; GN OrderedLocusNames=MJ0996; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probable metalloprotease. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the peptidase U62 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99001.1; -; Genomic_DNA. DR PIR; D64424; D64424. DR ProteinModelPortal; Q58403; -. DR STRING; 243232.MJ_0996; -. DR MEROPS; U62.002; -. DR EnsemblBacteria; AAB99001; AAB99001; MJ_0996. DR KEGG; mja:MJ_0996; -. DR eggNOG; arCOG00321; Archaea. DR eggNOG; COG0312; LUCA. DR InParanoid; Q58403; -. DR KO; K03568; -. DR OMA; ENGNLQY; -. DR PhylomeDB; Q58403; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR InterPro; IPR025502; TldD. DR InterPro; IPR002510; TldD/PmbA. DR Pfam; PF01523; PmbA_TldD; 1. DR PIRSF; PIRSF004919; TldD; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metalloprotease; Protease; KW Reference proteome. FT CHAIN 1 451 Metalloprotease MJ0996. FT /FTId=PRO_0000142364. SQ SEQUENCE 451 AA; 49814 MW; D5245F2E9551FB79 CRC64; MLNLEKIEKL LEVGDYADIR INFGESNTIT LKDGKIEEIS SGFGNGVAVR VLYKNGWGFV TSNIVSEEEI EKLINKAYKM AKISNEYSEK EIILKDYKAI IDNYKMIGKI NPTDVDIEEK KEIIIDTYKN MTDEKIKSIS VSYSDVFGKR IFMISEGSRI EGEITRCIMY MNCVAKENGN LQYGAERTGG FGFEKIKDNY LNLALEAKNR ALRLLKAKPC PKGKFKVILD PELAGVFIHE AVGHASEADL VLQNDSVFKD KLGERVGSEY VTVIDDATIE GAFGSYKYDD EGVEGKKTVI IENGILKTYL HSRETAGRMD AELTGNGRAE GLNKPIVRMS NTFIKPGDWS FEELLEDTKE GIFLKGSRGG QVDTGKGLFQ FSAVEAYLIE NGELTQVLKD AGLSGEILDI LFKVDAVTKD FELSVGYCGK DGQSVPVGDG GGCVRTIATV S // ID Y998_METJA Reviewed; 241 AA. AC Q58404; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0998; GN OrderedLocusNames=MJ0998; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99006.1; -; Genomic_DNA. DR PIR; E64424; E64424. DR EnsemblBacteria; AAB99006; AAB99006; MJ_0998. DR KEGG; mja:MJ_0998; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 241 Uncharacterized protein MJ0998. FT /FTId=PRO_0000107137. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 37 57 Helical. {ECO:0000255}. FT TRANSMEM 72 92 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 138 158 Helical. {ECO:0000255}. FT COMPBIAS 48 59 Leu-rich. SQ SEQUENCE 241 AA; 27835 MW; CC8495C38B098D02 CRC64; MKSLYALIFL LFVIVVSYIF NGLWSVFNIK HVFWVNLFLL IAFHPQHLDG LIILLLIPLK IFSNFKLKLQ CIIALVGILL TIIKGVIKSG FGWILRILFF FVRMMTVSFI NLVVFSILLT SVYVLGYVAF LKPDDIQFGT LYTAFGGLAL LGAGIKIIQH FIKQSEEIAQ EEFKKWYETE VKNFMYSLFI TAKNAFPKFL DDLLAKGVVS QEEYQNLIKL YSHILARILK NDEEKMKIPT F // ID Y319_METJA Reviewed; 97 AA. AC Q57767; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0319; GN OrderedLocusNames=MJ0319; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98304.1; -; Genomic_DNA. DR PIR; H64339; H64339. DR ProteinModelPortal; Q57767; -. DR SMR; Q57767; 3-93. DR STRING; 243232.MJ_0319; -. DR EnsemblBacteria; AAB98304; AAB98304; MJ_0319. DR KEGG; mja:MJ_0319; -. DR eggNOG; arCOG04140; Archaea. DR eggNOG; COG1888; LUCA. DR InParanoid; Q57767; -. DR KO; K09732; -. DR OMA; VHSIDMV; -. DR PhylomeDB; Q57767; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.70.1340; -; 1. DR InterPro; IPR003831; DUF211. DR InterPro; IPR023129; MTH889-like_domain. DR Pfam; PF02680; DUF211; 1. DR ProDom; PD012512; DUF211; 1. DR SUPFAM; SSF160363; SSF160363; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 97 Uncharacterized protein MJ0319. FT /FTId=PRO_0000106791. SQ SEQUENCE 97 AA; 10920 MW; 85BB11AC11236FC5 CRC64; MNGIRRIVLD ILKPHEPKIT DMALKLTSLS NIDGVNITVY EIDKETENVK VTIEGNNLDF DEIQEIIESL GGTIHSIDEV VAGKKIIEEV RTPQDRH // ID Y327_METJA Reviewed; 104 AA. AC Q57773; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0327; GN OrderedLocusNames=MJ0327; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98315.1; -; Genomic_DNA. DR PIR; G64340; G64340. DR PDB; 2KLA; NMR; -; A=1-104. DR PDB; 2QTD; X-ray; 1.70 A; A=1-104. DR PDBsum; 2KLA; -. DR PDBsum; 2QTD; -. DR ProteinModelPortal; Q57773; -. DR SMR; Q57773; 1-104. DR STRING; 243232.MJ_0327; -. DR EnsemblBacteria; AAB98315; AAB98315; MJ_0327. DR KEGG; mja:MJ_0327; -. DR eggNOG; arCOG02734; Archaea. DR eggNOG; COG1433; LUCA. DR InParanoid; Q57773; -. DR OMA; CILEFIE; -. DR EvolutionaryTrace; Q57773; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.420.130; -; 1. DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth. DR Pfam; PF02579; Nitro_FeMo-Co; 1. DR SUPFAM; SSF53146; SSF53146; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MJ0327. FT /FTId=PRO_0000106796. FT STRAND 4 10 {ECO:0000244|PDB:2QTD}. FT STRAND 12 15 {ECO:0000244|PDB:2QTD}. FT TURN 19 21 {ECO:0000244|PDB:2QTD}. FT STRAND 23 31 {ECO:0000244|PDB:2QTD}. FT STRAND 34 44 {ECO:0000244|PDB:2QTD}. FT HELIX 45 53 {ECO:0000244|PDB:2QTD}. FT STRAND 57 62 {ECO:0000244|PDB:2QTD}. FT HELIX 66 73 {ECO:0000244|PDB:2QTD}. FT STRAND 77 80 {ECO:0000244|PDB:2QTD}. FT HELIX 86 94 {ECO:0000244|PDB:2QTD}. SQ SEQUENCE 104 AA; 11898 MW; 519531CD7ACC8741 CRC64; MINMKVAISM DVDKISNSFE DCKYFLIVRI DDNEVKSTKV IFNDESGKKS IVKENVNAII CKNISEENYK KFSKKIEIYH AEGDDVDKNI SLFIEGELSK ISNP // ID Y330_METJA Reviewed; 549 AA. AC Q57776; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0330; GN OrderedLocusNames=MJ0330; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98318.1; -; Genomic_DNA. DR PIR; B64341; B64341. DR STRING; 243232.MJ_0330; -. DR EnsemblBacteria; AAB98318; AAB98318; MJ_0330. DR KEGG; mja:MJ_0330; -. DR eggNOG; arCOG09637; Archaea. DR eggNOG; ENOG410ZK2R; LUCA. DR OMA; WTRFPTP; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 549 Uncharacterized protein MJ0330. FT /FTId=PRO_0000106799. SQ SEQUENCE 549 AA; 64471 MW; CB4A8859FFC6AF99 CRC64; MMYIVELVRE SLKKKTFNKK IFLELCKKLD IPIPQKLNKH NFPPLFYELI DKLKSLNIIE FCEITMDLHT ITEKQKEILL NMVEHPINIL IIGKGGGKDF MVSLLFNYMM FRACVEDYYE KFTRIDFVNV APNDHLAKNV FFKEFKAWFL KCKVWQMIGI DKKKRQKAPI CVLETKAEIG DKITMHSGHS RATSFEGMNA LCVVADEISD PDFKNAEQLF EQGLSSAKSR FKDKARVVAI TWTRFPTPNP RDDVGYRLYL DYKAVDEAYT FKGKTWEVNT RVSKEDFKAQ YQKNPILARC MYECEPPELN AYFISLEALE ARHKVEMGLF TWRAIYENNL IRLEFKQLQS TDKTIYCHTD LAINRDKGVI AISYFDKGKV IISDIIVLTP TLGHKIDYLS LEKFYNHLQN HFSVKFTFDR FQSEYFIQKF KGERLSKHVK LWTTFQELVE GTKEYYDATG VKRKKAKIEI RCNEDIWQKL RTQILQHQID GDKVIYFGEG SPDLADAVVS SAYNCITHNV NAIDEEDYSY RQVFDDEEEF EEFEFGSFF // ID Y337_METJA Reviewed; 262 AA. AC Q57783; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0337; GN OrderedLocusNames=MJ0337; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98325.1; -; Genomic_DNA. DR PIR; A64342; A64342. DR ProteinModelPortal; Q57783; -. DR STRING; 243232.MJ_0337; -. DR EnsemblBacteria; AAB98325; AAB98325; MJ_0337. DR KEGG; mja:MJ_0337; -. DR eggNOG; arCOG09642; Archaea. DR eggNOG; ENOG410YIEK; LUCA. DR OMA; IMEYSSA; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 262 Uncharacterized protein MJ0337. FT /FTId=PRO_0000106807. SQ SEQUENCE 262 AA; 29045 MW; 7D2C22E3EBE580E3 CRC64; MMALNEYDAQ IVEQAMKPIL DSNLFSRKIF QKKKIPEDVE VYNLVQVVFD ENAFKKGSME LTEVPIKTTT SPFTVFDINL KVTKARRFVE GPNADYNKAQ IFEGLAKVVA RAENQYSIDA LSKNNTAVGA SASWNGADTT PDKIANDIID AKTKIEQYSN AKCALVAPVD AIACFRKIGT QGFSAYDETK DFIKEIIPTN LITDKSAYLV PIDIAILQMG VAVEADQFIE KKATQVEFIF TEAISPMVKE KNGIIKIQKV LG // ID Y3407_METJA Reviewed; 441 AA. AC Q60306; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJECS07; GN OrderedLocusNames=MJECS07; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid small ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77119; AAC37065.1; -; Genomic_DNA. DR PIR; G64516; G64516. DR ProteinModelPortal; Q60306; -. DR EnsemblBacteria; AAC37065; AAC37065; MJ_ECS07. DR KEGG; mja:MJECS07; -. DR Proteomes; UP000000805; Plasmid small ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 441 Uncharacterized protein MJECS07. FT /FTId=PRO_0000107488. SQ SEQUENCE 441 AA; 53092 MW; 5A494246188B0104 CRC64; METTIMVVAM DRLTYYKLTS RYLYYFCLDR LLSCHRLDLD RDRKINWRHP KYWNYNNIPK GEKPYLRHID LWDYRGNFKD WIIENLRSIY CSPYYFESPR YELEYPAIDY NYWDWVIDID FKGNFKKSKE IAKEVREIFK DYGVKDIHIK FSGSKGFHIW INARYLPNEI LNKGYVEGST ILTNFLNFKL RKLLDFVGKE GDTGIDLSIY KENMTVTAPF SLYYADIEGK TPISIPFPIN KVEKFKPIYL QNVKPYFIRK LTKYYENFGE IRGDLTDFVD DALRYYQATK KVNNDIKIDL EINTNKKAKP KVEHSKREYI KTTIGDKEVV LNKVKLESYL NELINSNWED GKMRGCYYLT SLCKLLGYGR DKTIKLLNRW ASKYGNKYIK HIDYEVRYLY DRNGKVCSIK WLKENIPEAK TQIEIYKKYY ELDKNNYLVK K // ID Y342_METJA Reviewed; 123 AA. AC Q57788; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0342; GN OrderedLocusNames=MJ0342; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98332.1; -; Genomic_DNA. DR PIR; F64342; F64342. DR STRING; 243232.MJ_0342; -. DR EnsemblBacteria; AAB98332; AAB98332; MJ_0342. DR KEGG; mja:MJ_0342; -. DR eggNOG; arCOG09647; Archaea. DR eggNOG; ENOG41111IH; LUCA. DR OMA; LIMEVIH; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 123 Uncharacterized protein MJ0342. FT /FTId=PRO_0000106812. SQ SEQUENCE 123 AA; 14008 MW; E2463D19323D5919 CRC64; MRWLTPFGML FISGTYYGLI FFGLIMEVIH NALISLVLAF FVVFAWDLVL SLIYGLRFVK EGDYIALDWD GQFPDCYGLF ASTCLSAVIW TYTDSLLLGL IVPVIIVFLG KQLMRGLYEK IKS // ID Y3506_METJA Reviewed; 116 AA. AC Q60261; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 46. DE RecName: Full=Uncharacterized protein MJECL06; GN OrderedLocusNames=MJECL06; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37079.1; -; Genomic_DNA. DR PIR; F64510; F64510. DR EnsemblBacteria; AAC37079; AAC37079; MJ_ECL06. DR KEGG; mja:MJECL06; -. DR OMA; MEMCNIA; -. DR Proteomes; UP000000805; Plasmid large ECE. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 116 Uncharacterized protein MJECL06. FT /FTId=PRO_0000107498. SQ SEQUENCE 116 AA; 13827 MW; A71627F7FFA2ED0F CRC64; MSVELRTLFR LIAVLEHSEE FKKVLFACER HFESGYCKCG PMEMCNIALA EAMKEDPTLV LRKWRRVFTY LEEVGIIKTR KLEAPANRPR RYIKLSENWM EALRTAIDKE YEKLIR // ID Y3518_METJA Reviewed; 211 AA. AC Q60278; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Uncharacterized protein MJECL18; GN OrderedLocusNames=MJECL18; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37089.1; -; Genomic_DNA. DR PIR; A64512; A64512. DR ProteinModelPortal; Q60278; -. DR EnsemblBacteria; AAC37089; AAC37089; MJ_ECL18. DR KEGG; mja:MJECL18; -. DR InParanoid; Q60278; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR SMART; SM00028; TPR; 3. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 211 Uncharacterized protein MJECL18. FT /FTId=PRO_0000107506. SQ SEQUENCE 211 AA; 24214 MW; 6D4175EE98133EF5 CRC64; MIFMFHSGAM ELLKIAEKLY DKDSEKAVEV YDKAIKKAER IYDDYAKAVI LSNIAKSLYS RGLTNKVIEV YNKAIKIAEE SSKRDVILSK IIENLCSNRL IDKALEVVNK ISDDSSKAIA LSEIAKAQYN IGMHDEALKN YDKAIFITEG VFDDEIKSSI LFEISRDFYN YGLVDKAFEV IGKIPYSKYR FRLLDKMAED LHKNIKYIHG E // ID Y3544_METJA Reviewed; 331 AA. AC Q60299; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJECL44; GN OrderedLocusNames=MJECL44; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37113.1; -; Genomic_DNA. DR PIR; C64515; C64515. DR ProteinModelPortal; Q60299; -. DR EnsemblBacteria; AAC37113; AAC37113; MJ_ECL44. DR KEGG; mja:MJECL44; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; Plasmid; KW Reference proteome. FT CHAIN 1 331 Uncharacterized protein MJECL44. FT /FTId=PRO_0000107523. FT NP_BIND 43 50 ATP. {ECO:0000255}. SQ SEQUENCE 331 AA; 38593 MW; E88952E0D5FEFC3F CRC64; MFIKWGDRLM TKTLHLTKVT IRNFRSIKVA HINNIGDIAV FVGANESGKS NILKALNWFG TDKPLGGDDI PVEFLGKENK EYSKKPIIEA YFEIVNKDKF KEKIISNIKE ILEVIKVDIN EDILINFEDM LNKIQFLKFE KYADGLFKTY IYDDQLEDIT KEFYDCFKNV ISKKTPLDLF NLIYEEVLKE EVKKQNIPEN QISNAVANIR GNPNFNNHYR KILDEIRTLN TFEEFYEICK RIENIVKSIP NTSVSISIPG RNIQLNPYNI FTEILTKFNS IVTIAFINLK PKFVYLDEEM ELKGAVIKNT SWSNTLKEEN KTTLLMPDFL E // ID Y358_METJA Reviewed; 128 AA. AC Q57804; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0358; GN OrderedLocusNames=MJ0358; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98350.1; -; Genomic_DNA. DR PIR; F64344; F64344. DR STRING; 243232.MJ_0358; -. DR EnsemblBacteria; AAB98350; AAB98350; MJ_0358. DR KEGG; mja:MJ_0358; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein MJ0358. FT /FTId=PRO_0000106829. SQ SEQUENCE 128 AA; 15084 MW; CEE12E04BBC2FA59 CRC64; MTFDLLKELK RIYKHFENID LEQFERDLIE CGFGKIKPGP LATDEVLTEE DIAKYREIIM KSQTCNVNTH NQIVIKINLK EINADNKMYC KFRKGYKFKE DIKVGEESSY IITLQQDSLH ICNNYEVA // ID Y362_METJA Reviewed; 63 AA. AC Q57808; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0362; GN OrderedLocusNames=MJ0362; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98354.1; -; Genomic_DNA. DR PIR; B64345; B64345. DR ProteinModelPortal; Q57808; -. DR STRING; 243232.MJ_0362; -. DR EnsemblBacteria; AAB98354; AAB98354; MJ_0362. DR KEGG; mja:MJ_0362; -. DR eggNOG; arCOG03884; Archaea. DR eggNOG; COG3466; LUCA. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019205; DUF2080_transposon-encoded. DR Pfam; PF09853; DUF2080; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 63 Uncharacterized protein MJ0362. FT /FTId=PRO_0000106832. SQ SEQUENCE 63 AA; 7107 MW; 490E45E7CCAF260B CRC64; MKIRKKTWRL PKDATISFKG VVKPIGNSGM ILIPKDYVGC KVLVTILDEL GNEEFEIVET EKS // ID Y402_METJA Reviewed; 106 AA. AC Q57845; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0402; GN OrderedLocusNames=MJ0402; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98395.1; -; Genomic_DNA. DR PIR; B64350; B64350. DR STRING; 243232.MJ_0402; -. DR EnsemblBacteria; AAB98395; AAB98395; MJ_0402. DR KEGG; mja:MJ_0402; -. DR eggNOG; arCOG08261; Archaea. DR eggNOG; ENOG410Z40K; LUCA. DR OMA; HAWDLYR; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 106 Uncharacterized protein MJ0402. FT /FTId=PRO_0000106854. SQ SEQUENCE 106 AA; 12600 MW; 6398888ABD46CFF3 CRC64; MFGWGRGWFG RGRGFWRYFP VSTVGGRYRY VGPCRCGLGP HAFYVDEKTG ALVHAWDLYR GYVPGYAEVD ERRYLEETIK ELEEEKRMLE EELARIKKRL DELKKD // ID Y404_METJA Reviewed; 150 AA. AC Q57847; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0404; GN OrderedLocusNames=MJ0404; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98391.1; -; Genomic_DNA. DR PIR; D64350; D64350. DR STRING; 243232.MJ_0404; -. DR EnsemblBacteria; AAB98391; AAB98391; MJ_0404. DR KEGG; mja:MJ_0404; -. DR eggNOG; arCOG04903; Archaea. DR eggNOG; COG4050; LUCA. DR InParanoid; Q57847; -. DR OMA; CMGCART; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR012356; UCP018781_methan. DR Pfam; PF09885; DUF2112; 1. DR PIRSF; PIRSF018781; UCP018781; 1. DR TIGRFAMs; TIGR03271; methan_mark_5; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 150 Uncharacterized protein MJ0404. FT /FTId=PRO_0000106855. FT COMPBIAS 127 149 Glu-rich. SQ SEQUENCE 150 AA; 16867 MW; 3D3803E0DAC73296 CRC64; MKKIFIYPPN SLILTDLVER FGHKPLNLNI VIGKLVRNPE IDSPPMNITD EEPKKGLKYA AVEVPSGVRG RMALIGPLIE EAEAAIIMDD APIAFGCIGC QRTNELTLYL VRRKNIPILR VKYPTNEEEA EILVNKIANF LKSLEENQEN // ID Y406_METJA Reviewed; 302 AA. AC Q57849; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Uncharacterized sugar kinase MJ0406; DE EC=2.7.1.-; GN OrderedLocusNames=MJ0406; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the carbohydrate kinase PfkB family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98396.1; -; Genomic_DNA. DR PIR; F64350; F64350. DR PDB; 2C49; X-ray; 1.92 A; A/B=1-302. DR PDB; 2C4E; X-ray; 1.70 A; A=1-302. DR PDBsum; 2C49; -. DR PDBsum; 2C4E; -. DR ProteinModelPortal; Q57849; -. DR SMR; Q57849; 3-301. DR STRING; 243232.MJ_0406; -. DR EnsemblBacteria; AAB98396; AAB98396; MJ_0406. DR KEGG; mja:MJ_0406; -. DR eggNOG; arCOG00014; Archaea. DR eggNOG; COG0524; LUCA. DR InParanoid; Q57849; -. DR OMA; FTAQAMI; -. DR PhylomeDB; Q57849; -. DR BRENDA; 2.7.1.B20; 3260. DR EvolutionaryTrace; Q57849; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004747; F:ribokinase activity; IEA:InterPro. DR GO; GO:0006014; P:D-ribose metabolic process; IEA:InterPro. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR002173; Carboh/pur_kinase_PfkB_CS. DR InterPro; IPR011611; PfkB_dom. DR InterPro; IPR002139; Ribokinase. DR InterPro; IPR029056; Ribokinase-like. DR Pfam; PF00294; PfkB; 1. DR PRINTS; PR00990; RIBOKINASE. DR SUPFAM; SSF53613; SSF53613; 1. DR PROSITE; PS00583; PFKB_KINASES_1; 1. DR PROSITE; PS00584; PFKB_KINASES_2; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Kinase; Reference proteome; KW Transferase. FT CHAIN 1 302 Uncharacterized sugar kinase MJ0406. FT /FTId=PRO_0000080152. FT STRAND 5 12 {ECO:0000244|PDB:2C4E}. FT STRAND 15 21 {ECO:0000244|PDB:2C4E}. FT STRAND 28 35 {ECO:0000244|PDB:2C49}. FT STRAND 37 42 {ECO:0000244|PDB:2C4E}. FT HELIX 44 54 {ECO:0000244|PDB:2C4E}. FT STRAND 58 62 {ECO:0000244|PDB:2C4E}. FT TURN 67 71 {ECO:0000244|PDB:2C4E}. FT HELIX 73 80 {ECO:0000244|PDB:2C4E}. FT STRAND 92 94 {ECO:0000244|PDB:2C4E}. FT STRAND 98 103 {ECO:0000244|PDB:2C4E}. FT STRAND 109 114 {ECO:0000244|PDB:2C49}. FT HELIX 116 123 {ECO:0000244|PDB:2C4E}. FT STRAND 131 136 {ECO:0000244|PDB:2C4E}. FT HELIX 141 151 {ECO:0000244|PDB:2C4E}. FT STRAND 155 159 {ECO:0000244|PDB:2C4E}. FT HELIX 162 167 {ECO:0000244|PDB:2C4E}. FT HELIX 170 178 {ECO:0000244|PDB:2C4E}. FT STRAND 181 186 {ECO:0000244|PDB:2C4E}. FT HELIX 187 197 {ECO:0000244|PDB:2C4E}. FT HELIX 201 205 {ECO:0000244|PDB:2C4E}. FT STRAND 209 214 {ECO:0000244|PDB:2C4E}. FT HELIX 216 218 {ECO:0000244|PDB:2C4E}. FT STRAND 220 223 {ECO:0000244|PDB:2C4E}. FT STRAND 228 231 {ECO:0000244|PDB:2C4E}. FT HELIX 245 258 {ECO:0000244|PDB:2C4E}. FT HELIX 263 277 {ECO:0000244|PDB:2C4E}. FT STRAND 280 284 {ECO:0000244|PDB:2C4E}. FT HELIX 290 299 {ECO:0000244|PDB:2C4E}. SQ SEQUENCE 302 AA; 33920 MW; 6A535606CC7D3260 CRC64; MGGKMEKITC VGHTALDYIF NVEKFPEPNT SIQIPSARKY YGGAAANTAV GIKKLGVNSE LLSCVGYDFK NSGYERYLKN LDINISKLYY SEEEETPKAW IFTDKDNNQI TFFLWGAAKH YKELNPPNFN TEIVHIATGD PEFNLKCAKK AYGNNLVSFD PGQDLPQYSK EMLLEIIEHT NFLFMNKHEF ERASNLLNFE IDDYLERVDA LIVTKGSKGS VIYTKDKKIE IPCIKAGKVI DPTGAGDSYR AGFLSAYVKG YDLEKCGLIG AATASFVVEA KGCQTNLPTW DKVVERLEKH RI // ID Y418_METJA Reviewed; 257 AA. AC Q57861; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0418; GN OrderedLocusNames=MJ0418; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98416.1; -; Genomic_DNA. DR PIR; B64352; B64352. DR ProteinModelPortal; Q57861; -. DR STRING; 243232.MJ_0418; -. DR EnsemblBacteria; AAB98416; AAB98416; MJ_0418. DR KEGG; mja:MJ_0418; -. DR eggNOG; arCOG03414; Archaea. DR eggNOG; ENOG410YBIU; LUCA. DR InParanoid; Q57861; -. DR OMA; EMYKCAW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR021586; Tscrpt_reg_TrmB_C. DR Pfam; PF11495; Regulator_TrmB; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 257 Uncharacterized protein MJ0418. FT /FTId=PRO_0000106864. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 257 AA; 28765 MW; CFEAA1AA6AB38000 CRC64; MIIMKKIGIL EIVVILSILI TSVSLAYKFY SNNGNDYEFD GNQMYKCAWV CEKILNKNFP LNATIIGKWT LSKKPFNGEV KIYDAKGGTL YAIYNGTPIT IGGELAYQED IAAKKIILHP IGKSIIFYEL NPIEGKSFRD IANEIENTTK NFNGLNIVDV IVEGSMGVDS KTYTPVERQK IMNNLDVDIK KGLGLYFVDY GIIINGKIHL NTLKNLDNYI NSSNISTSKL TIYVVVNNSI DEIPNKIKEN YAIITLG // ID Y427_METJA Reviewed; 160 AA. AC Q57870; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0427; GN OrderedLocusNames=MJ0427; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98420.1; -; Genomic_DNA. DR PIR; C64353; C64353. DR STRING; 243232.MJ_0427; -. DR EnsemblBacteria; AAB98420; AAB98420; MJ_0427. DR KEGG; mja:MJ_0427; -. DR eggNOG; arCOG08291; Archaea. DR eggNOG; ENOG4110ZWQ; LUCA. DR OMA; SCINALK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 160 Uncharacterized protein MJ0427. FT /FTId=PRO_0000106872. SQ SEQUENCE 160 AA; 20088 MW; 41557230A5D06B9F CRC64; MMERMHNLNN VYLKECIHFL DSCINALKEF DLRTFISRFY YGMLYLLNAF EFYIRENIED WHNKDRYANF SKKIRNFLMD LKLYRHASDY ILSPRLEHGK HYEEHWEEFK ESYLKLKFFH YLHILRQELY SYRHNQLIAI IIEKLEIIEK LLKLYIMLEE // ID Y434_METJA Reviewed; 222 AA. AC Q57876; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Gamma-glutamylcyclotransferase and UPF0331 family protein MJ0434; DE Includes: DE RecName: Full=Gamma-glutamylcyclotransferase family protein MJ0434; DE Includes: DE RecName: Full=UPF0331 family protein MJ0434; GN OrderedLocusNames=MJ0434; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: In the N-terminal section; belongs to the UPF0331 CC family. {ECO:0000305}. CC -!- SIMILARITY: In the C-terminal section; belongs to the gamma- CC glutamylcyclotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98422.1; -; Genomic_DNA. DR PIR; B64354; B64354. DR ProteinModelPortal; Q57876; -. DR STRING; 243232.MJ_0434; -. DR EnsemblBacteria; AAB98422; AAB98422; MJ_0434. DR KEGG; mja:MJ_0434; -. DR eggNOG; arCOG05024; Archaea. DR eggNOG; arCOG05099; Archaea. DR eggNOG; ENOG410ZJ0D; LUCA. DR InParanoid; Q57876; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.10.490.10; -; 1. DR InterPro; IPR009288; AIG2-like. DR InterPro; IPR013024; Butirosin_synth_BtrG-like. DR InterPro; IPR008201; DUF86. DR Pfam; PF01934; DUF86; 1. DR Pfam; PF06094; GGACT; 1. DR SUPFAM; SSF110857; SSF110857; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 222 Gamma-glutamylcyclotransferase and FT UPF0331 family protein MJ0434. FT /FTId=PRO_0000158262. SQ SEQUENCE 222 AA; 26742 MW; F0FA33F1634D1A11 CRC64; MRKDVKIYLN HILESIELIE EYTKDKTEDD FFTSKFLQDA VIRRIEIIGE AIKNLPMEFR EKYNHIPWKE FAEMRDILIR KYFGVDLGLT WEVVKKDIPK LKEEILKIME ELDKNKNNKY NVFAYGELMK KERLLELINR VPKMIEGRVY GYEKFFDETI GYYGARKKEG SYIDGIILLD ITDKELGIFD DYEDLDVYYI REKTTAVSED GRKYDVYIYL RK // ID Y447_METJA Reviewed; 161 AA. AC Q57889; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0447; GN OrderedLocusNames=MJ0447; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98447.1; -; Genomic_DNA. DR PIR; G64355; G64355. DR STRING; 243232.MJ_0447; -. DR PRIDE; Q57889; -. DR EnsemblBacteria; AAB98447; AAB98447; MJ_0447. DR KEGG; mja:MJ_0447; -. DR eggNOG; arCOG09632; Archaea. DR eggNOG; ENOG4110ZMX; LUCA. DR OMA; NREWRWK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 161 Uncharacterized protein MJ0447. FT /FTId=PRO_0000106879. SQ SEQUENCE 161 AA; 19125 MW; 13DDED5CC33A10BB CRC64; MNLNIKEIKQ KINEWKNREW RWKGKGKIEI RFVCLIERAE SFKELVDNLE IIICEYEKIK QLIEDKDIKE IAKLNLFCGN NVYEEMLKDI LSSNKFISLT ISFDENIAYV KYMERGKEEV VYLDGKSAYK ALQILKNRYE NILKKQISII EDAIPLTIPS Q // ID Y453_METJA Reviewed; 107 AA. AC Q57895; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 65. DE RecName: Full=Uncharacterized protein MJ0453; GN OrderedLocusNames=MJ0453; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98442.1; -; Genomic_DNA. DR PIR; E64356; E64356. DR ProteinModelPortal; Q57895; -. DR STRING; 243232.MJ_0453; -. DR EnsemblBacteria; AAB98442; AAB98442; MJ_0453. DR KEGG; mja:MJ_0453; -. DR eggNOG; arCOG04844; Archaea. DR eggNOG; COG4033; LUCA. DR InParanoid; Q57895; -. DR OMA; NIREFNP; -. DR PhylomeDB; Q57895; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR012031; UCP006577. DR Pfam; PF08979; DUF1894; 1. DR PIRSF; PIRSF006577; UCP006577; 1. DR ProDom; PD028584; UCP006577; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 107 Uncharacterized protein MJ0453. FT /FTId=PRO_0000106883. SQ SEQUENCE 107 AA; 12603 MW; 4E3723628AEF3F8F CRC64; MGCIDKLNYE ILYKGGFKEC AEYIRKNFKN IKEMEAGYEI FEGIFLIGIP PIPVAYEDNY VIFPYTKPCY GTFVLKINLD EINKDKKEEK KEKDKGKKGL LSRLKFW // ID Y486_METJA Reviewed; 322 AA. AC Q57910; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 89. DE RecName: Full=Uncharacterized protein MJ0486 {ECO:0000305}; GN OrderedLocusNames=MJ0486; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000250|UniProtKB:Q9X0Z6}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000250|UniProtKB:Q9X0Z6}; CC -!- SIMILARITY: Belongs to the radical SAM superfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98477.1; -; Genomic_DNA. DR PIR; F64360; F64360. DR ProteinModelPortal; Q57910; -. DR STRING; 243232.MJ_0486; -. DR DNASU; 1451348; -. DR EnsemblBacteria; AAB98477; AAB98477; MJ_0486. DR KEGG; mja:MJ_0486; -. DR eggNOG; arCOG01362; Archaea. DR eggNOG; COG1242; LUCA. DR InParanoid; Q57910; -. DR KO; K07139; -. DR OMA; GGCTYCN; -. DR PhylomeDB; Q57910; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033588; C:Elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016573; P:histone acetylation; IBA:GOC. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR032432; Radical_SAM_C. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR InterPro; IPR005911; YhcC-like. DR PANTHER; PTHR11135:SF1; PTHR11135:SF1; 1. DR Pfam; PF04055; Radical_SAM; 1. DR Pfam; PF16199; Radical_SAM_C; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01212; TIGR01212; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 322 Uncharacterized protein MJ0486. FT /FTId=PRO_0000106893. FT METAL 50 50 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:Q9X0Z6}. FT METAL 58 58 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:Q9X0Z6}. FT METAL 61 61 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000250|UniProtKB:Q9X0Z6}. SQ SEQUENCE 322 AA; 37390 MW; F3D074B32180B805 CRC64; MVVIMLNYDD IKIIDEIYSE GYLFAQYGIY IKKKFKQKIF KIPVDIGLGC PHKKNGGCIF CPEMGRPISV KYCSAKIPLK EQIKKQMENQ KKKGFKKFYI YFYPGTNTYA PAEKLKEIWD FSLSYKEVIG LSIGTRPDCL EKEKLDILAE YVENGYDIWI DLGVQSMHQK TLEILNRGHD VSDIIKAIKD CHKRGIKVCG HVILGLPGES WKEMMETAKI LSLLEIEAVK IYPLVVVKGT KLEEMYWKGE YRTLDENQYI SLVCDFLEHL SPYVLIQRLS KDKVPESIKV SPEWYLGRLK IMNKVSEILK KRGTKQGARF FR // ID Y504_METJA Reviewed; 196 AA. AC Q57927; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0504; GN OrderedLocusNames=MJ0504; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98495.1; -; Genomic_DNA. DR PIR; H64362; H64362. DR ProteinModelPortal; Q57927; -. DR SMR; Q57927; 1-189. DR STRING; 243232.MJ_0504; -. DR EnsemblBacteria; AAB98495; AAB98495; MJ_0504. DR KEGG; mja:MJ_0504; -. DR eggNOG; arCOG04343; Archaea. DR eggNOG; COG1751; LUCA. DR InParanoid; Q57927; -. DR KO; K09126; -. DR OMA; QGVKVCY; -. DR PhylomeDB; Q57927; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.1380.30; -; 1. DR InterPro; IPR015074; DUF1867. DR InterPro; IPR023161; PK-like_domain. DR InterPro; IPR015795; Pyrv_Knase_C. DR Pfam; PF02887; PK_C; 1. DR PIRSF; PIRSF016138; UCP016138; 1. DR ProDom; PD022619; DUF1867; 1. DR SUPFAM; SSF52935; SSF52935; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 196 Uncharacterized protein MJ0504. FT /FTId=PRO_0000106903. SQ SEQUENCE 196 AA; 21452 MW; F994E98F4670196B CRC64; MKLFDYPGIQ NTDETLKIAV ERAKKGDIKS IVVASSTGYT AKKLLDLLEK EGLDLNVVVV TYHQGFHGED TISMDKEVEE ELKKRGAKVF RGSHALSGVE RGISNKLGGY GPVQVIAETL RTFGQGVKVC YEITIMACDA GLIKAKEEVI AIGGTGRGAD TAMVIKPANM NTFFNIEARE ILCMPRIKKK VKEDDE // ID Y515_METJA Reviewed; 380 AA. AC Q57935; DT 16-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ0515; GN OrderedLocusNames=MJ0515; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the complex I 49 kDa subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98504.1; -; Genomic_DNA. DR PIR; C64364; C64364. DR ProteinModelPortal; Q57935; -. DR STRING; 243232.MJ_0515; -. DR EnsemblBacteria; AAB98504; AAB98504; MJ_0515. DR KEGG; mja:MJ_0515; -. DR eggNOG; arCOG01547; Archaea. DR eggNOG; COG3261; LUCA. DR InParanoid; Q57935; -. DR KO; K14106; -. DR OMA; GEWRNEA; -. DR PhylomeDB; Q57935; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008901; F:ferredoxin hydrogenase activity; IEA:InterPro. DR GO; GO:0051287; F:NAD binding; IEA:InterPro. DR GO; GO:0016151; F:nickel cation binding; IEA:InterPro. DR GO; GO:0016651; F:oxidoreductase activity, acting on NAD(P)H; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR Gene3D; 1.10.645.10; -; 2. DR InterPro; IPR001135; NADH_Q_OxRdtase_suD. DR InterPro; IPR014029; NADH_UbQ_OxRdtase_49kDa_CS. DR InterPro; IPR001501; Ni-dep_hyd_lsu. DR InterPro; IPR018194; Ni-dep_hyd_lsu_Ni_BS. DR InterPro; IPR029014; NiFe_Hase-like. DR Pfam; PF00346; Complex1_49kDa; 2. DR Pfam; PF00374; NiFeSe_Hases; 1. DR SUPFAM; SSF56762; SSF56762; 1. DR PROSITE; PS00535; COMPLEX1_49K; 1. DR PROSITE; PS00507; NI_HGENASE_L_1; 1. PE 3: Inferred from homology; KW Complete proteome; Oxidoreductase; Reference proteome. FT CHAIN 1 380 Uncharacterized protein MJ0515. FT /FTId=PRO_0000118627. SQ SEQUENCE 380 AA; 43638 MW; 3EAD16D67834A76F CRC64; MSENMATIPI GPIHPVLKEP LRIKLVLDGE KPVDAEIEMG YVHRGIEKIM EGKHCHKGIH LAERVCGICS YVHTMTFAEC IEHISKIEIP DKAKYLRVVT CELERIHSHL IASAVYNLSI EHETLAMWLL NVREIIMDLM EMITGNRVNM GYNVIGGVRR DINREMMDEI YKKLDIFEDE LKNIIEVFET GPLIALRSKE IGILPYHEVM RTRAVGPICR GSGLPESDWR LRHSTYQELK FKPVWREEGD NFARMMVRHE EIIESVRLIR EALEHYEECS GDIRVKAEIK GGKGEWRNEA PRGEVTYRME ITDGGIIKRI MIRTPTVMNL EAYKYMLKTC PTVADAVSAY TSIDPCVSCT ERCIVAVKDG KEIPISIKFR // ID Y516_METJA Reviewed; 148 AA. AC Q57936; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 2. DT 11-NOV-2015, entry version 95. DE RecName: Full=Uncharacterized protein MJ0516; GN OrderedLocusNames=MJ0516; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. {ECO:0000305}; CC -!- SIMILARITY: Belongs to the complex I 20 kDa subunit family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98505.1; -; Genomic_DNA. DR ProteinModelPortal; Q57936; -. DR STRING; 243232.MJ_0516; -. DR EnsemblBacteria; AAB98505; AAB98505; MJ_0516. DR KEGG; mja:MJ_0516; -. DR eggNOG; ENOG4102T9N; Archaea. DR eggNOG; COG3260; LUCA. DR InParanoid; Q57936; -. DR KO; K14105; -. DR OMA; AKIPGCP; -. DR PhylomeDB; Q57936; -. DR BRENDA; 2.7.1.78; 5244. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008137; F:NADH dehydrogenase (ubiquinone) activity; IEA:InterPro. DR GO; GO:0048038; F:quinone binding; IEA:InterPro. DR Gene3D; 3.40.50.700; -; 1. DR InterPro; IPR006137; NADH_UbQ_OxRdtase-like_20kDa. DR InterPro; IPR006138; NADH_UQ_OxRdtase_20Kd_su. DR Pfam; PF01058; Oxidored_q6; 1. DR PROSITE; PS01150; COMPLEX1_20K; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 148 Uncharacterized protein MJ0516. FT /FTId=PRO_0000118783. FT METAL 21 21 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 24 24 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 88 88 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 117 117 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 148 AA; 16276 MW; 6EF752B2509B9C94 CRC64; MMKELFRKRS IHVCVVNTGG CNGCDIEIVA CLAPRYDIEQ YGIYVHNNPR EADVLLVTGP VTLQWAERLK EIYEKTPEPK IVVAVGACAL SGGIFKEGHV VGGVDKVIPV DAKIPGCPPR PSEIIETILK VAPKAIAMRE KRLKNKDE // ID Y517_METJA Reviewed; 140 AA. AC Q57937; DT 22-AUG-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0517; GN OrderedLocusNames=MJ0517; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98506.1; -; Genomic_DNA. DR PIR; E64364; E64364. DR ProteinModelPortal; Q57937; -. DR STRING; 243232.MJ_0517; -. DR EnsemblBacteria; AAB98506; AAB98506; MJ_0517. DR KEGG; mja:MJ_0517; -. DR eggNOG; arCOG04835; Archaea. DR eggNOG; COG4084; LUCA. DR KO; K14104; -. DR OMA; GCLGRKV; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.3070.10; -; 1. DR InterPro; IPR012056; NiFe-hyd_3_EhaM. DR Pfam; PF09218; DUF1959; 1. DR SUPFAM; SSF101332; SSF101332; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 140 Uncharacterized protein MJ0517. FT /FTId=PRO_0000106907. SQ SEQUENCE 140 AA; 16386 MW; 2FE6B33714CE0486 CRC64; MVIMTEIVDI DKKYVENSLK QKMNVLKDNR FLMDDVFIPI AKALKIEVEE VIEIFAKKLD FASCYELHAY AEQAKMGCLG RKVDIDLGLC WLSDFFGLIK KEEADLIRKK VVESYLLYKK PYKEALEEGR QMIIKLLKEE // ID Y523_METJA Reviewed; 234 AA. AC Q57943; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0523; GN OrderedLocusNames=MJ0523; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98515.1; -; Genomic_DNA. DR PIR; C64365; C64365. DR ProteinModelPortal; Q57943; -. DR STRING; 243232.MJ_0523; -. DR EnsemblBacteria; AAB98515; AAB98515; MJ_0523. DR KEGG; mja:MJ_0523; -. DR eggNOG; arCOG04832; Archaea. DR eggNOG; COG4036; LUCA. DR KO; K14098; -. DR OMA; NMILLTD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019212; DUF2105_membrane. DR InterPro; IPR011311; Prd_NiFe_hyd_3_EhaG. DR Pfam; PF09878; DUF2105; 1. DR PIRSF; PIRSF019136; EhaG; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 234 Uncharacterized protein MJ0523. FT /FTId=PRO_0000106912. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 52 72 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. FT TRANSMEM 207 227 Helical. {ECO:0000255}. SQ SEQUENCE 234 AA; 25584 MW; EBEFD2D776D1B56C CRC64; MGEMENIIYS IYHPTILVGF AIGILSLLAI GFQKNDLHAL ILTDVVECAM LIIIAGVGTD LAEALILPGL VVSLAELLAV SEVLITRKYL KSKRPKPKSY KLFEEFKLPL YTGELKYDIH MEILKTSPKF LAIILIVYGA ILSGFTGGAV IATGLLFYAL SQRVIGVEIS EELKTMWEGI SGLSGIAWAL WIFGFIGFFV FPDKWLLCLL MAGLGLVIKV GSKLGLIGYI GEVR // ID Y555_METJA Reviewed; 350 AA. AC Q57975; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Putative aminopeptidase MJ0555; DE EC=3.4.11.-; GN OrderedLocusNames=MJ0555; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250}; CC Note=Binds 2 divalent metal cations per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98546.1; -; Genomic_DNA. DR PIR; C64369; C64369. DR ProteinModelPortal; Q57975; -. DR STRING; 243232.MJ_0555; -. DR EnsemblBacteria; AAB98546; AAB98546; MJ_0555. DR KEGG; mja:MJ_0555; -. DR eggNOG; arCOG01518; Archaea. DR eggNOG; COG1363; LUCA. DR InParanoid; Q57975; -. DR KO; K01179; -. DR OMA; ICHPTIV; -. DR PhylomeDB; Q57975; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW. DR Gene3D; 2.40.30.40; -; 1. DR InterPro; IPR008007; Peptidase_M42. DR InterPro; IPR023367; Peptidase_M42_dom2. DR Pfam; PF05343; Peptidase_M42; 1. DR PIRSF; PIRSF001123; PepA_GA; 1. PE 3: Inferred from homology; KW Aminopeptidase; Complete proteome; Hydrolase; Metal-binding; KW Metalloprotease; Protease; Reference proteome. FT CHAIN 1 350 Putative aminopeptidase MJ0555. FT /FTId=PRO_0000071660. FT ACT_SITE 207 207 Proton acceptor. {ECO:0000250}. FT METAL 62 62 Divalent metal cation 1. {ECO:0000250}. FT METAL 175 175 Divalent metal cation 1. {ECO:0000250}. FT METAL 175 175 Divalent metal cation 2. {ECO:0000250}. FT METAL 208 208 Divalent metal cation 2. {ECO:0000250}. FT METAL 230 230 Divalent metal cation 1. {ECO:0000250}. FT METAL 321 321 Divalent metal cation 2. {ECO:0000250}. SQ SEQUENCE 350 AA; 38622 MW; 9D4942EF5528955B CRC64; MSVVEYLKKL SKLHGISGRE DSVREFMKKE LEKYCDSVEI DNFGNLIAKR GNKGKKIMIA AHMDEIGLMV KYIDDNGFLK FTKIGGIYDP TILNQKVVVH GSKGDLIGVL GSKPPHRMKE EEKTKIIKYE DMFIDIGAES REEAIEMGVN IGTWVSFLSE VYDLGKNRLT GKAFDDRVGC AVLLEVMKRL SEEDIDCQVY AVGTVQEEVG LKGARVSAFK INPDVAIALD VTIAGDHPGI KKEDAPVDLG KGPVVGIVDA SGRGLIAHPK VLDMIKAVSE KYKIDVQWEV GEGGTTDATA IHLTREGIPT GVISVPARYI HTPVEVIDKR DLEKTVELVY NCIKEVNNFF // ID Y560_METJA Reviewed; 138 AA. AC Q57980; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0560; GN OrderedLocusNames=MJ0560; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98559.1; -; Genomic_DNA. DR PIR; H64369; H64369. DR EnsemblBacteria; AAB98559; AAB98559; MJ_0560. DR KEGG; mja:MJ_0560; -. DR OMA; CIDFKNV; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Uncharacterized protein MJ0560. FT /FTId=PRO_0000106931. SQ SEQUENCE 138 AA; 16470 MW; 752B2B7E63EA9721 CRC64; MMIMKFVRLE FISYEESYDF EFMAPDDITE DKFIDDLSDA IVKSINWEYI KGYFQEEDEL GMEILPNLID CIDFKNVNVE MEKKGYKPIK YDIIVYAGAW SYFNPKKLSI IDFHETGELT KLEKAIQEKL KRLKTDIY // ID Y574_METJA Reviewed; 93 AA. AC Q57994; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0574; GN OrderedLocusNames=MJ0574; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98574.1; -; Genomic_DNA. DR PIR; F64371; F64371. DR STRING; 243232.MJ_0574; -. DR EnsemblBacteria; AAB98574; AAB98574; MJ_0574. DR KEGG; mja:MJ_0574; -. DR OMA; GFMFFGF; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR027379; CLS_N. DR Pfam; PF13396; PLDc_N; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 93 Uncharacterized protein MJ0574. FT /FTId=PRO_0000106937. FT TRANSMEM 17 37 Helical. {ECO:0000255}. FT TRANSMEM 54 74 Helical. {ECO:0000255}. FT COMPBIAS 33 39 Poly-Ile. SQ SEQUENCE 93 AA; 10446 MW; 60CF4CE6406EB6EF CRC64; MWPCPIGFGM VGFPIFGFFF MGLFFVIGIA VFIIIIITIV DILKRDALDT LEKILWILVV WFLGIIGAII YYLLSKRNSK SKGDNNGKNI GSN // ID Y585_METJA Reviewed; 205 AA. AC Q58005; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0585; GN OrderedLocusNames=MJ0585; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98583.1; -; Genomic_DNA. DR PIR; A64373; A64373. DR STRING; 243232.MJ_0585; -. DR EnsemblBacteria; AAB98583; AAB98583; MJ_0585. DR KEGG; mja:MJ_0585; -. DR eggNOG; arCOG00368; Archaea. DR eggNOG; COG0419; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 205 Uncharacterized protein MJ0585. FT /FTId=PRO_0000106945. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 130 150 Helical. {ECO:0000255}. FT TRANSMEM 151 171 Helical. {ECO:0000255}. FT TRANSMEM 182 202 Helical. {ECO:0000255}. SQ SEQUENCE 205 AA; 24327 MW; 9D235C9F16E52A61 CRC64; MKKLAFLILL IVFSNLSLVN AIDDNISNYS KEINELTVKL KELESKNPND ERIEEYKEKL KQLIEKQHEL KSQNLKYNET LAYIQSEEYW KMQEEIWEYN NKVMKWFIAI SILILGIILA TLWILRKDKF LLFLAIFGLI VPFLQFKIPN WLFNILALPL FVYIKFIVPE CAEGSFYYSP LITIPISMYG WILIGLAVKF IIKKY // ID Y586_METJA Reviewed; 170 AA. AC Q58006; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0586; GN OrderedLocusNames=MJ0586; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98578.1; -; Genomic_DNA. DR PIR; B64373; B64373. DR ProteinModelPortal; Q58006; -. DR STRING; 243232.MJ_0586; -. DR EnsemblBacteria; AAB98578; AAB98578; MJ_0586. DR KEGG; mja:MJ_0586; -. DR eggNOG; arCOG01863; Archaea. DR eggNOG; COG1813; LUCA. DR InParanoid; Q58006; -. DR KO; K03627; -. DR OMA; EICGAEI; -. DR PhylomeDB; Q58006; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR004451; CHP00270. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR TIGRFAMs; TIGR00270; TIGR00270; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 170 Uncharacterized HTH-type transcriptional FT regulator MJ0586. FT /FTId=PRO_0000149791. FT DOMAIN 90 144 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 101 120 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 170 AA; 19671 MW; 3EC953BDC7FEA6EA CRC64; MRDSIMQMCE LCGKLTDKLY KVIIEGSEMN VCKECAKFGK SPKTYSRLGK KTIIGKGTIT TNKQVKKPIK RRRDIFDTLP MLREDYGDVI REAREKRGLS IEELAKKLKM KASTLQKFER YELEPNEKEI KILEKELKIS LTESIGEETS YYGGRDEDGF TLGDFIKIKK // ID Y638_METJA Reviewed; 225 AA. AC Q58055; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0638; GN OrderedLocusNames=MJ0638; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98634.1; -; Genomic_DNA. DR PIR; F64379; F64379. DR ProteinModelPortal; Q58055; -. DR STRING; 243232.MJ_0638; -. DR EnsemblBacteria; AAB98634; AAB98634; MJ_0638. DR KEGG; mja:MJ_0638; -. DR eggNOG; arCOG01789; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q58055; -. DR OMA; CINVLEH; -. DR PhylomeDB; Q58055; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR013216; Methyltransf_11. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF08241; Methyltransf_11; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 225 Uncharacterized protein MJ0638. FT /FTId=PRO_0000106965. SQ SEQUENCE 225 AA; 26695 MW; 672B812CA1E93E8A CRC64; MKEVKDFYDK WEPEDFPNYI KLLMNFADEL IFEEISLLLK KFENKKDFLV LDCGCGFGAF YNLTKDFNTI YLDISLNLLK RFKLKERKIC ANILHLPFKD NTFDLVLCIN VLEHVNYLKA LNEIRRILKN KGKLIVVVVN KDSLIKEEIF NDFKIFHKPL SIKDFEIDGF KIVYSNSVYF LPSIFKISPP IILSKIIEYW KPVDKKLSKI FKNKGQFLII EMVKE // ID Y639_METJA Reviewed; 109 AA. AC Q58056; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0639; GN OrderedLocusNames=MJ0639; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98635.1; -; Genomic_DNA. DR PIR; G64379; G64379. DR STRING; 243232.MJ_0639; -. DR EnsemblBacteria; AAB98635; AAB98635; MJ_0639. DR KEGG; mja:MJ_0639; -. DR eggNOG; arCOG05044; Archaea. DR eggNOG; ENOG410YYQG; LUCA. DR OMA; CYYRSGF; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 109 Uncharacterized protein MJ0639. FT /FTId=PRO_0000106966. FT COMPBIAS 75 90 Glu-rich. FT COMPBIAS 87 94 Lys-rich. SQ SEQUENCE 109 AA; 12890 MW; 8364B35BD3C629EF CRC64; MWLLIFNIIF NGETMKLAVD AVFYVREGFN FEKAFKEVLK ILGEDVKILS VEYPELALIS ENGYYYRCGF MLDKELREEL SGEEINKIKE KIKKLFEDEI IYTLTCEIL // ID Y642_METJA Reviewed; 333 AA. AC Q58059; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 75. DE RecName: Full=Uncharacterized protein MJ0642; GN OrderedLocusNames=MJ0642; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00344}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98644.1; -; Genomic_DNA. DR PIR; B64380; B64380. DR ProteinModelPortal; Q58059; -. DR STRING; 243232.MJ_0642; -. DR EnsemblBacteria; AAB98644; AAB98644; MJ_0642. DR KEGG; mja:MJ_0642; -. DR eggNOG; arCOG03417; Archaea. DR eggNOG; COG0614; LUCA. DR InParanoid; Q58059; -. DR KO; K02016; -. DR OMA; YLFENVE; -. DR PhylomeDB; Q58059; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 333 Uncharacterized protein MJ0642. FT /FTId=PRO_0000106968. FT DOMAIN 45 318 Fe/B12 periplasmic-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00344}. SQ SEQUENCE 333 AA; 40006 MW; 1EF47CDE74593BDF CRC64; MITMALNFYK YYSRQIKYAL HFNILNNSII DAENKYINFQ KPLKNVIVSD SMFIDTAYLL KIKKMIKSIK GVFWADFVLK KYYPLYSDYL KGKISNVGTD GKINYGEILN INPDMIFLID WNIFNPLSKW LDKNNIPYTK TGNYKEPKFL GKMEWIKFYA SFYNKYKKAE KVFNKIIEEK RRILKSLNSR SIKYKPVVAF FGYHKNQPYI YGKSHYIPNW IREIKGNYLF ENVEGTNYHY IDRKIFNSRA KYADVCILDT MGEDIDIKEL LKNNPHFLKF RAYKNKRFYI TTKDYLKFET LKCSEVMEEY VKIIHPKIYQ NGDNDLKYFI KVV // ID Y646_METJA Reviewed; 164 AA. AC Q58062; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=UPF0305 protein MJ0646 {ECO:0000255|HAMAP-Rule:MF_00763}; GN OrderedLocusNames=MJ0646; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0305 family. {ECO:0000255|HAMAP- CC Rule:MF_00763}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98640.1; -; Genomic_DNA. DR PIR; F64380; F64380. DR ProteinModelPortal; Q58062; -. DR STRING; 243232.MJ_0646; -. DR EnsemblBacteria; AAB98640; AAB98640; MJ_0646. DR KEGG; mja:MJ_0646; -. DR eggNOG; arCOG03215; Archaea. DR eggNOG; COG4066; LUCA. DR OMA; DIMMIRS; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00763; UPF0305; 1. DR InterPro; IPR019215; DUF2115. DR Pfam; PF09888; DUF2115; 1. DR PIRSF; PIRSF004959; UCP004959; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 164 UPF0305 protein MJ0646. FT /FTId=PRO_0000141703. SQ SEQUENCE 164 AA; 19895 MW; 8BF99216F5B7A702 CRC64; MKARELFEKL KKELNNFSIY DIMMIRSFIE KDAKYLPPQY KNHYVEAMMK YLIETFNEIR KKSVDEIQDE EIDEEKLNEM LNRIERFRKY YTPDEERFIN LSKILCPYLA FIAKKPLHPE YLTFPGNVKI IKKGNNYYCP VKNKQLNEYS LCEFCVCKSI DELK // ID Y653_METJA Reviewed; 194 AA. AC Q58069; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0653; GN OrderedLocusNames=MJ0653; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98648.1; -; Genomic_DNA. DR PIR; E64381; E64381. DR ProteinModelPortal; Q58069; -. DR STRING; 243232.MJ_0653; -. DR EnsemblBacteria; AAB98648; AAB98648; MJ_0653. DR KEGG; mja:MJ_0653; -. DR eggNOG; arCOG00606; Archaea. DR eggNOG; COG0517; LUCA. DR InParanoid; Q58069; -. DR OMA; MATHGIK; -. DR PhylomeDB; Q58069; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 194 Uncharacterized protein MJ0653. FT /FTId=PRO_0000106972. FT DOMAIN 13 72 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 78 133 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT COMPBIAS 187 194 Glu-rich. SQ SEQUENCE 194 AA; 21723 MW; 33921320EF82E5DC CRC64; MKIACDIPVS EVMSFPVIKA TKNMSIYDIA NIMTENNIGA VVIVENNKPI GIVTERDIVK RVVSKNLKPK DVLAEEVMSK KIITIPQNAS ITEAAKIMAT HGIKRLPVVK DGELVGIVTQ SDIVRVSPEL LEIVIEYASI TPEEKEVISL DTDEFSEEYI NGICENCGYQ GRVRLYQGRY LCDECIEEFE EKEE // ID Y674_METJA Reviewed; 338 AA. AC Q58087; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0674; GN OrderedLocusNames=MJ0674; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98668.1; -; Genomic_DNA. DR PIR; B64384; B64384. DR ProteinModelPortal; Q58087; -. DR EnsemblBacteria; AAB98668; AAB98668; MJ_0674. DR KEGG; mja:MJ_0674; -. DR eggNOG; arCOG00934; Archaea. DR eggNOG; COG1313; LUCA. DR InParanoid; Q58087; -. DR KO; K04070; -. DR OMA; RNINHVG; -. DR PhylomeDB; Q58087; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 338 Uncharacterized protein MJ0674. FT /FTId=PRO_0000106984. FT METAL 129 129 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 133 133 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 136 136 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 338 AA; 40020 MW; 96923543AEB9C705 CRC64; MKLGRYLAVS KDLAPAKFII AKCIEVEEFK GLELNELWEI HNKVLKKVDF DNFDFNDLEY VKPNLLDLKV EIAKNIFKNC HFCEHRCYVN RETERGFCRI KESYYSTEFL HLGEERVLVP SHTIFFCGCN FKCVFCQNWD ISQVYFDKTI PNHCIPYNPK EMAKIIKHKR DYSKNVNFVG GDPTPHLLSI LKTLSYLDKN IPVVWNSNMY LTVEGMHLLK GVVDVYLTDF KFGNNECGER LSKVKNYFDI IKRNHLLIKD EEVIIRHLVM PNHLDCCTEK IFDFISKNLD NAVVNVMFQY RPEYKAKEYP DINRRLTYEE IEKALELAEK YNLDLIYD // ID Y686_METJA Reviewed; 580 AA. AC Q58099; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0686; GN OrderedLocusNames=MJ0686; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98681.1; -; Genomic_DNA. DR PIR; F64385; F64385. DR ProteinModelPortal; Q58099; -. DR STRING; 243232.MJ_0686; -. DR EnsemblBacteria; AAB98681; AAB98681; MJ_0686. DR KEGG; mja:MJ_0686; -. DR eggNOG; arCOG05223; Archaea. DR eggNOG; COG1479; LUCA. DR eggNOG; COG3472; LUCA. DR InParanoid; Q58099; -. DR OMA; QRDFVWE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004919; DUF262. DR Pfam; PF03235; DUF262; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 580 Uncharacterized protein MJ0686. FT /FTId=PRO_0000106989. SQ SEQUENCE 580 AA; 68393 MW; C23CA146575B2506 CRC64; MELSHDTKNL LDLVKKAYEG EVALPDFQRN FVWTRQDIEE LIKSLLENMF IGTFLIQEIN PENPPFGTIY IRGAEELNPN ITLRKPRILV LDGQQRLTSL FYAIYSPNFP LKNTTKPYAF FIDLNKLVED DIDNSVFSLS KDCRQYKALL NEDNSFDIEK LKEKRFFPLT FLSNSNKFYK IWYKHFSEIF PEEVFNYMHN ILEYKVPTLI LGLSYNDKPE QVVVLFERIN KTGIKLSPYD LLVARFYKFI KLREKWAEAF ENNIRIKNFA GDVEDTKVPY MFIQALALSK GMSIKSRDLI KIDNSILNDE SWNRVVDIAE NKVFQRIFDI SEYGIADIKK WNPYTPTITM MLAFFLKHDI PDMDKVNKWY WSSVFSERYS GSTESKMMKD FKEVSQWIEN NNKIPEVVEN LKIEIQYGAY SLKKVKSSGS SKYKGVFNLI FKNKPMDFYK PDNIAYYKLE DHHIFPKGFL RNKGISNEYI DSVLNKTPIL DETNKKISKK SPSKYVKEMI EIQKNKGLSE DEAVNKVKEI LKGHFINEEM FEILRNTDDS LSKDEIEENF NRFIELREKL ILEKILELIS // ID Y691_METJA Reviewed; 109 AA. AC Q58103; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=DNA-binding protein MJ0691 {ECO:0000255|HAMAP-Rule:MF_00026}; GN OrderedLocusNames=MJ0691; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the PDCD5 family. {ECO:0000255|HAMAP- CC Rule:MF_00026}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98686.1; -; Genomic_DNA. DR PIR; C64386; C64386. DR ProteinModelPortal; Q58103; -. DR STRING; 243232.MJ_0691; -. DR EnsemblBacteria; AAB98686; AAB98686; MJ_0691. DR KEGG; mja:MJ_0691; -. DR eggNOG; arCOG04179; Archaea. DR eggNOG; COG2118; LUCA. DR InParanoid; Q58103; -. DR KO; K06875; -. DR OMA; IREPIDD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP. DR Gene3D; 1.10.8.140; -; 1. DR HAMAP; MF_00026; dsDNA_bind; 1. DR InterPro; IPR022889; DNA_bind_arc. DR InterPro; IPR002836; PDCD5-related. DR PANTHER; PTHR10840; PTHR10840; 1. DR Pfam; PF01984; dsDNA_bind; 1. DR PIRSF; PIRSF015730; TFAR19; 1. DR SUPFAM; SSF46950; SSF46950; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome. FT CHAIN 1 109 DNA-binding protein MJ0691. FT /FTId=PRO_0000121555. SQ SEQUENCE 109 AA; 12892 MW; DAB41A2366B8822C CRC64; MDVEEIKRKK LLELQKKLAE QQQQEEALLE AEMQKRALLR KILTPEARER LERIRLARPE FAEAVEVQLI QLAQLGRLPI PLSDEDFKAL LERISALTKR KREIKIVRK // ID Y725_METJA Reviewed; 261 AA. AC Q58135; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0725; GN OrderedLocusNames=MJ0725; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the FrhB family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98721.1; -; Genomic_DNA. DR PIR; E64390; E64390. DR STRING; 243232.MJ_0725; -. DR EnsemblBacteria; AAB98721; AAB98721; MJ_0725. DR KEGG; mja:MJ_0725; -. DR eggNOG; arCOG02651; Archaea. DR eggNOG; COG1035; LUCA. DR InParanoid; Q58135; -. DR KO; K00441; -. DR OMA; NEEINKC; -. DR PhylomeDB; Q58135; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR007525; FrhB_FdhB_C. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. PE 3: Inferred from homology; KW Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome. FT CHAIN 1 261 Uncharacterized protein MJ0725. FT /FTId=PRO_0000159227. SQ SEQUENCE 261 AA; 29017 MW; 10D8066AB1458133 CRC64; MKYLSAKSKL NIDAQDGGFT TTLLSYCLEN GILDAVVVVG DKNWKPVAYL ATTPTELLKS TKSKYSISPN NKLLEYATEN YDKVGLVGLP CHILGGLQFD LTLKVGLFCT KNFYYDTIKS IIKERFGVNI DEVAKMNITK GKFVVETLKK KGFAGTEKVV YEIPIKEIEK LCNLGCRVCT DFSAKYADVS VGSVGSEDGW NTVIVRNKMV EDIINEMAEK GLIEVKETVD IKAIEKLENI KKKNEEINKC SAYFAVCPAL F // ID Y729_METJA Reviewed; 124 AA. AC Q58139; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0729; GN OrderedLocusNames=MJ0729; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 2 CBS domains. {ECO:0000255|PROSITE- CC ProRule:PRU00703}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98725.1; -; Genomic_DNA. DR PIR; A64391; A64391. DR ProteinModelPortal; Q58139; -. DR STRING; 243232.MJ_0729; -. DR EnsemblBacteria; AAB98725; AAB98725; MJ_0729. DR KEGG; mja:MJ_0729; -. DR eggNOG; arCOG00629; Archaea. DR eggNOG; ENOG410YKT4; LUCA. DR OMA; DLLTGCK; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR000644; CBS_dom. DR Pfam; PF00571; CBS; 2. DR SMART; SM00116; CBS; 2. DR PROSITE; PS51371; CBS; 2. PE 3: Inferred from homology; KW CBS domain; Complete proteome; Reference proteome; Repeat. FT CHAIN 1 124 Uncharacterized protein MJ0729. FT /FTId=PRO_0000107005. FT DOMAIN 10 67 CBS 1. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. FT DOMAIN 70 124 CBS 2. {ECO:0000255|PROSITE- FT ProRule:PRU00703}. SQ SEQUENCE 124 AA; 14303 MW; 1C0AAF097936B34A CRC64; MMIMKVKEVM NKDFIKISPN DIGGEVVQTL YKEKKNYAPV IEDGKLVGWI TALDLLIGCK HSKIEDLMLL IDEIKILKEN DEVTDELIDE IIKNEDIAYP VINDRDEVVG TLSVFDLLKY YKNR // ID Y755_METJA Reviewed; 342 AA. AC Q58165; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0755; DE Flags: Precursor; GN OrderedLocusNames=MJ0755; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98748.1; -; Genomic_DNA. DR PIR; C64394; C64394. DR ProteinModelPortal; Q58165; -. DR STRING; 243232.MJ_0755; -. DR EnsemblBacteria; AAB98748; AAB98748; MJ_0755. DR KEGG; mja:MJ_0755; -. DR eggNOG; arCOG00388; Archaea. DR eggNOG; COG2247; LUCA. DR OMA; RINGSDR; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 18 {ECO:0000255}. FT CHAIN 19 342 Uncharacterized protein MJ0755. FT /FTId=PRO_0000013995. SQ SEQUENCE 342 AA; 38778 MW; BD25220A7EEAD85C CRC64; MWKKLMLLLL MAIPLVSAVA IPSISATDVV LVSDNCADQC TALEVADALN ATVITTEWGI YNESLIDEIL ALNPDKVIII GGPLAVVENY TTALENVGIT VERIGGSNRY ETNANVTLRF QNQFRYAFGN NTTVCVCHGF DDIALNETMG LIKNGTCLVL LTNGVNLSVE PQKLQLRINK VEIIENPICP FCNYSKLMLK LQKNGLKIEI KQIPKVKVKL MLQNRIRIME RRILMLKRMG VNVTDLEEKL KEVEQLMEQN RYQEAYRIMV QLQEEQMVRV KLHLHPMWSK MKRGKIQENK NASHIYHQNI NNLTNELNTS RGGIGGINAP HIYHQRINST IQ // ID Y756_METJA Reviewed; 136 AA. AC Q58166; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0756; DE Flags: Precursor; GN OrderedLocusNames=MJ0756; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98757.1; -; Genomic_DNA. DR PIR; D64394; D64394. DR STRING; 243232.MJ_0756; -. DR EnsemblBacteria; AAB98757; AAB98757; MJ_0756. DR KEGG; mja:MJ_0756; -. DR eggNOG; arCOG07800; Archaea. DR eggNOG; ENOG41111PA; LUCA. DR OMA; ENTDINP; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 19 {ECO:0000255}. FT CHAIN 20 136 Uncharacterized protein MJ0756. FT /FTId=PRO_0000013996. SQ SEQUENCE 136 AA; 15370 MW; A501A6B7D97F2BD0 CRC64; MKKLLMVILG IALIGMAYAF PPWMAYQTQT TENTDINPVD ILKTAEVVQH TTPFGYNLSH LEIDGKIVGV LWKDVDLSKL EVGEPFNTPF GEKYPLYYDR ELVGFIFTNH PASHYGYGMR GGYGCHCHCG CCCWQQ // ID Y792_METJA Reviewed; 89 AA. AC Q58202; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0792; GN OrderedLocusNames=MJ0792; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98789.1; -; Genomic_DNA. DR PIR; H64398; H64398. DR STRING; 243232.MJ_0792; -. DR EnsemblBacteria; AAB98789; AAB98789; MJ_0792. DR KEGG; mja:MJ_0792; -. DR eggNOG; arCOG09673; Archaea. DR eggNOG; ENOG410ZDC0; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 89 Uncharacterized protein MJ0792. FT /FTId=PRO_0000107042. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. SQ SEQUENCE 89 AA; 9084 MW; 06D02F0D9ED983BB CRC64; MKFLEKGVYK IFGAVILVSM IGALVAEPIA LGDAGLYYQY YVGDIDTAQQ CYLVAADSAI TGAAISAALG PAGLASGVFT VVFSTTVLA // ID Y80A_METJA Reviewed; 138 AA. AC P81321; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 50. DE RecName: Full=Uncharacterized protein MJ0808.1; GN OrderedLocusNames=MJ0808.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98820.1; -; Genomic_DNA. DR EnsemblBacteria; AAB98820; AAB98820; MJ_0808.1. DR KEGG; mja:MJ_0808.1; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Uncharacterized protein MJ0808.1. FT /FTId=PRO_0000107058. SQ SEQUENCE 138 AA; 16750 MW; DA087F74CA5A064D CRC64; MLKEIKNDYD KIREKMTQKI QELNQQITQI KKQIQIIEQN NLSDQQNQTI QKIKRQIYSI EFDILRVESN RSNMIYSKTF EDMCEYLDSH SGIGRIFAES FMREIEKNIQ LMKQLVMMED QIIKIKQEIR MIEKDLKI // ID Y820_METJA Reviewed; 47 AA. AC Q58230; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 70. DE RecName: Full=Putative uncharacterized protein MJ0820; GN OrderedLocusNames=MJ0820; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC -!- CAUTION: Could be the product of a pseudogene. MJ0821, MJ0820 and CC MJ0819 respectively represent the N-terminal, central and C- CC terminal sections of other members of this family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98832.1; -; Genomic_DNA. DR PIR; D64402; D64402. DR STRING; 243232.MJ_0820; -. DR EnsemblBacteria; AAB98832; AAB98832; MJ_0820. DR KEGG; mja:MJ_0820; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR InterPro; IPR011579; ATPase_dom. DR Pfam; PF01637; ATPase_2; 1. PE 5: Uncertain; KW Complete proteome; Reference proteome. FT CHAIN 1 47 Putative uncharacterized protein MJ0820. FT /FTId=PRO_0000184682. SQ SEQUENCE 47 AA; 5565 MW; AB1B30CCE652247B CRC64; MDDFDKETAI KFMDFLAEEI LNKKLSEDEK ELIYSYVGGK PINRNCY // ID Y827_METJA Reviewed; 199 AA. AC Q58237; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 85. DE RecName: Full=Uncharacterized protein MJ0827; GN OrderedLocusNames=MJ0827; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the band 7/mec-2 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98826.1; -; Genomic_DNA. DR PIR; C64403; C64403. DR ProteinModelPortal; Q58237; -. DR STRING; 243232.MJ_0827; -. DR PRIDE; Q58237; -. DR EnsemblBacteria; AAB98826; AAB98826; MJ_0827. DR KEGG; mja:MJ_0827; -. DR eggNOG; arCOG01915; Archaea. DR eggNOG; COG0330; LUCA. DR InParanoid; Q58237; -. DR OMA; WGIHVER; -. DR PhylomeDB; Q58237; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR001107; Band_7. DR InterPro; IPR018080; Band_7/stomatin-like_CS. DR InterPro; IPR001972; Stomatin_fam. DR PANTHER; PTHR10264; PTHR10264; 1. DR Pfam; PF01145; Band_7; 1. DR PRINTS; PR00721; STOMATIN. DR SMART; SM00244; PHB; 1. DR SUPFAM; SSF117892; SSF117892; 1. DR PROSITE; PS01270; BAND_7; 1. PE 3: Inferred from homology; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 199 Uncharacterized protein MJ0827. FT /FTId=PRO_0000094064. FT TRANSMEM 7 27 Helical. {ECO:0000255}. SQ SEQUENCE 199 AA; 22809 MW; 2545CE07DD54337E CRC64; MKVNDMFWFW LILGIIALFI IVKAIVIVNQ YEGGLIFRLG RVIGKLKPGI NIIIPFLDVP VKVDMRTRVT DIPPQEMITK DNAVVKVDAV VYYRVIDVEK AILEVEDYEY AIINLAQTTL RAIIGSMELD EVLNKREYIN SKLLEILDRE TDAWGVRIEK VEVKEIDPPE DIKNAMAQQM KAERLKRAAI LEAEGEKPE // ID Y830_METJA Reviewed; 252 AA. AC Q58240; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0830; GN OrderedLocusNames=MJ0830; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To Synechocystis PCC 6803 slr1717. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98829.1; -; Genomic_DNA. DR PIR; F64403; F64403. DR ProteinModelPortal; Q58240; -. DR STRING; 243232.MJ_0830; -. DR DNASU; 1451713; -. DR EnsemblBacteria; AAB98829; AAB98829; MJ_0830. DR KEGG; mja:MJ_0830; -. DR eggNOG; arCOG00043; Archaea. DR eggNOG; COG1606; LUCA. DR InParanoid; Q58240; -. DR KO; K06864; -. DR OMA; LVTRIPY; -. DR PhylomeDB; Q58240; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR005232; CHP00268. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR PIRSF; PIRSF006661; PP-lp_UCP006661; 1. DR TIGRFAMs; TIGR00268; TIGR00268; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 252 Uncharacterized protein MJ0830. FT /FTId=PRO_0000107066. SQ SEQUENCE 252 AA; 29736 MW; 2F4A13CCBEC1D470 CRC64; MVFLKKLIKL KNNLKEKFKN KKIIIAYSGG IDSLLLSILL SEITETLCIF IKTPYISEWS LNNAIINAKK YNLNLKVIKI DKIIKNVPER CYLCKKMFFE ILTKEKEKYN YDVVVDGTNY DDLFEDRPGL RAKEEFNIGS PFADFKIGKK DILEIAKELN INIPPKETCL LTRFEFNREI SIEDLKKIEE LEEFLRNYVK GAIRVRDYKN LAVIEIEDDL SKIINEKEEI IKKFKDYGFK KVCINLEIYR SY // ID Y831_METJA Reviewed; 432 AA. AC Q58241; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0831; GN OrderedLocusNames=MJ0831; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0977. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98830.1; -; Genomic_DNA. DR PIR; G64403; G64403. DR ProteinModelPortal; Q58241; -. DR STRING; 243232.MJ_0831; -. DR EnsemblBacteria; AAB98830; AAB98830; MJ_0831. DR KEGG; mja:MJ_0831; -. DR eggNOG; arCOG00427; Archaea. DR eggNOG; COG0608; LUCA. DR InParanoid; Q58241; -. DR KO; K07463; -. DR OMA; AVGDMQE; -. DR PhylomeDB; Q58241; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR InterPro; IPR003156; DHHA1_dom. DR Pfam; PF02272; DHHA1; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 432 Uncharacterized protein MJ0831. FT /FTId=PRO_0000107067. SQ SEQUENCE 432 AA; 48835 MW; 0EB95D188D2B41F3 CRC64; MMEKLKEIEK VTKAIKEKIL NHYGYIRVIT HHDTDGLSSG GILAKMLMRT NKLFHLTVVE HLSKEVIEKL AKENEVNKPL FIFADMGSGQ IEEIIKHNFN AIILDHHPPV IKDSFINENI IQLNPHIFGV DGSREITASG VCYLVAREFG YYDLSVLAIV GIIGDMQYNP LLGLNKFIVN EAREYRYVKI MNDIVYNIYD VEIYKAIAYC TKPYIPDLAS EGKAFKFLKD IGIDPNKKQL DDTDKKKLLS AIIFKYPKIE NLLIDRYLIE HKVRDAFLLS EMLNAVGRNG LFAVGIGICL EDDECIKIGN QILWEYKKNL INELKSVKLK KLNNIYYFEG KKGMIGIIAS ILVDDKPVIG YHIEGDIAKF SARGNRDLVN RGLNLSVAMA VAKEFGGNGG GHDVASGAVV SKDKVQEFLK RVDEIIGEQL RR // ID Y888_METJA Reviewed; 206 AA. AC Q58298; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 84. DE RecName: Full=Probable metallo-hydrolase MJ0888; DE EC=3.-.-.-; GN OrderedLocusNames=MJ0888; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000250}; CC -!- SIMILARITY: Belongs to the metallo-beta-lactamase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98892.1; -; Genomic_DNA. DR PIR; H64410; H64410. DR ProteinModelPortal; Q58298; -. DR STRING; 243232.MJ_0888; -. DR EnsemblBacteria; AAB98892; AAB98892; MJ_0888. DR KEGG; mja:MJ_0888; -. DR eggNOG; arCOG00504; Archaea. DR eggNOG; COG0491; LUCA. DR InParanoid; Q58298; -. DR OMA; CHYDHTA; -. DR PhylomeDB; Q58298; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.60.15.10; -; 1. DR InterPro; IPR001279; Metallo-B-lactamas. DR Pfam; PF00753; Lactamase_B; 1. DR SMART; SM00849; Lactamase_B; 1. DR SUPFAM; SSF56281; SSF56281; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome; Zinc. FT CHAIN 1 206 Probable metallo-hydrolase MJ0888. FT /FTId=PRO_0000107092. FT METAL 55 55 Zinc 1. {ECO:0000250}. FT METAL 57 57 Zinc 1. {ECO:0000250}. FT METAL 59 59 Zinc 2. {ECO:0000250}. FT METAL 60 60 Zinc 2. {ECO:0000250}. FT METAL 130 130 Zinc 1. {ECO:0000250}. FT METAL 147 147 Zinc 1. {ECO:0000250}. FT METAL 147 147 Zinc 2. {ECO:0000250}. FT METAL 190 190 Zinc 2. {ECO:0000250}. SQ SEQUENCE 206 AA; 23229 MW; AC2C59FF1E80840E CRC64; MILKLNGYGY SSNSYLIIGK KNILIDPGTS GTFNILMEEL ERNGIKDIDL IINTHCHFDH TSADYLIEEY FNCPTIIEDK EVKHLKNGDE VTVSSLFGAK LNPPKEIIPL SEIEEELKSY GLEIIRTPGH TYGSISIIYE NSLITGDTIF AYGVGRWDLP TGDVIQLRNS INLLERIANE RNIDKLYPGH GEIGDRMAFS YAKLFI // ID Y890_METJA Reviewed; 137 AA. AC Q58300; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=UPF0148 protein MJ0890; GN OrderedLocusNames=MJ0890; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0148 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98906.1; -; Genomic_DNA. DR PIR; B64411; B64411. DR ProteinModelPortal; Q58300; -. DR STRING; 243232.MJ_0890; -. DR EnsemblBacteria; AAB98906; AAB98906; MJ_0890. DR KEGG; mja:MJ_0890; -. DR eggNOG; arCOG00578; Archaea. DR eggNOG; COG1645; LUCA. DR InParanoid; Q58300; -. DR KO; K07143; -. DR OMA; AKMLGKH; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_00343; UPF0148; 1. DR InterPro; IPR009563; SSSCA1. DR InterPro; IPR022954; UPF0148. DR Pfam; PF06677; Auto_anti-p27; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 137 UPF0148 protein MJ0890. FT /FTId=PRO_0000159857. FT COMPBIAS 131 135 Lys-rich. SQ SEQUENCE 137 AA; 15914 MW; B0EEAC8A4245C0C8 CRC64; MIKTVIDNLC YNFGENMKND DAIKVLSNEL LKGAKMLSTH CSKCGCPLFE KDGKIYCPIC EKLKNKETIE KGENEKEIKN EIERKKSEIN EILDLNKVVM DKINYLVMKL KEEDEVSRIR EIAEAIYVLI KLKKKIE // ID Y908_METJA Reviewed; 1232 AA. AC Q58318; DT 14-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0908; GN OrderedLocusNames=MJ0908; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the Mg-chelatase subunit H family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98910.1; -; Genomic_DNA. DR PIR; D64413; D64413. DR ProteinModelPortal; Q58318; -. DR STRING; 243232.MJ_0908; -. DR PRIDE; Q58318; -. DR EnsemblBacteria; AAB98910; AAB98910; MJ_0908. DR KEGG; mja:MJ_0908; -. DR eggNOG; arCOG03022; Archaea. DR eggNOG; COG1429; LUCA. DR InParanoid; Q58318; -. DR KO; K02230; -. DR OMA; WETGQAM; -. DR PhylomeDB; Q58318; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051116; F:cobaltochelatase activity; IEA:InterPro. DR GO; GO:0016851; F:magnesium chelatase activity; IEA:InterPro. DR GO; GO:0015995; P:chlorophyll biosynthetic process; IEA:InterPro. DR GO; GO:0009236; P:cobalamin biosynthetic process; IEA:InterPro. DR InterPro; IPR011771; BchH. DR InterPro; IPR011953; Cobalto_CobN. DR InterPro; IPR003672; CobN/Mg_chltase. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF02514; CobN-Mg_chel; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR TIGRFAMs; TIGR02025; BchH; 1. DR TIGRFAMs; TIGR02257; cobalto_cobN; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 1232 Uncharacterized protein MJ0908. FT /FTId=PRO_0000219887. SQ SEQUENCE 1232 AA; 142644 MW; 89722AEF2AE22158 CRC64; MVILMIKIGF VSTIDSDDLV FEEAYKEIKK YGIEFKILDY KCSRKEFEEF LEFIKEANIV FTKLMGGKNA FKYYDELAEF CKRHNIPFLP LPTISEIHPD LEKDRTVDDD VKNKVVKYLG YEGVYNYKNL LLYLANRFGN LNVEYEEPRP MPWQGIYYKG KYFETLDDYL NYLKELGRDL DKPIIGVLFY RNWFVANNID YVNDLIDIIE NKGAIPIAVF SSHLKNELGS IGTLETFKRF FYKDGKPIVH ALINTTMFTL SMGVKAELLK DEPEFLKELN VPILQGIIST GFIEDWKKSV SGLNPIDLII GMAMPEFDGA IIHFPIGGKE KIKDGEVGVP IIKYRAIRDR AEKIVDLALR YANLKLKSNK DKKIAIIFHN YPPRNDKIAS AFGLDSPESV VNILKEMKKR GFIVDEIPKN GTELIKKMLN YATNDKRFLT EEMIKKAVGK VKKEDYEKWF NSLSEKVKQE LIKNWGAIPG DVMNFDGELI IPGIINGNVF ISVQPPRGFG ENPSAIYHSP DLPPTHYYIA FYKWIKDVFK ADAIMHIGKH GNLEWLPGKC VGLSNECYPD ICMELPNIYP FIVNNPGEGT QAKRRSYATI ISHLIPPMTI SDLYGDLVEL EKSIDDYYET ENKEKKEFLK KEILKKIKEL KLDEDLLDGK VIDEEINDEN FEKLLNKIHD YLETLKNRQI NDGLHIMGVP LEGDKLVNML FMIIRYQFNY LEILAEILDY SWEELNENKG KYHKILDEIN EIGLNLLKEY MQYNFDENKI DELKTVKINS KLRDVLKTVS TIYKNLMKVD EEIINAVNAL EGFYIPPRVA GAPTKDINCL PTGRNFYSCN PQEIPTKSAY EMGKKLAEDL INKYLKEEGK YPEYIGVIVW GSPTMRTKGD DIGEILYLLG VKPVWNKMGR VVGLEVIPLE ELGRPRIDVT LRISGLFRDT FPNVVELIDE AIKMVANLDE PDEMNYVKKH YREEVEEKIK KGIDEKTAKE TSLYRIFSDK PGCYGAGVSH LIDEKNWESI EDFAKVYVEW GGYAYGKGYY GVEAKEEFIN RLSKIELTVK NEDSQEWDIF EGDDFNSYHG GLIASVTYYS GKKPVSYVGD TSNPNDIRTK HLKEEGKEIF RTKIMNPKWI EGMKRHGYKG AADFSKYVDH MFAWDATSGI IDDWMYEKIA EKYVFDKDME EFFKENNPYA LLNITERLLE AIERGMWKAD EEMKEKLRKK YLEIEGMIEE KL // ID Y912_METJA Reviewed; 243 AA. AC Q58322; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized protein MJ0912; GN OrderedLocusNames=MJ0912; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98917.1; -; Genomic_DNA. DR PIR; H64413; H64413. DR ProteinModelPortal; Q58322; -. DR STRING; 243232.MJ_0912; -. DR EnsemblBacteria; AAB98917; AAB98917; MJ_0912. DR KEGG; mja:MJ_0912; -. DR eggNOG; arCOG01143; Archaea. DR eggNOG; COG0639; LUCA. DR InParanoid; Q58322; -. DR OMA; RAPLDEY; -. DR PhylomeDB; Q58322; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.60.21.10; -; 1. DR InterPro; IPR024654; Calcineurin-like_PHP_lpxH. DR InterPro; IPR029052; Metallo-depent_PP-like. DR InterPro; IPR011152; Pesterase_MJ0912. DR InterPro; IPR000979; Phosphodiesterase_MJ0936/Vps29. DR PANTHER; PTHR11124; PTHR11124; 3. DR Pfam; PF12850; Metallophos_2; 1. DR PIRSF; PIRSF000883; Pesterase_MJ0912; 1. DR SUPFAM; SSF56300; SSF56300; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 243 Uncharacterized protein MJ0912. FT /FTId=PRO_0000107101. SQ SEQUENCE 243 AA; 27819 MW; 98B27C4E23E6C136 CRC64; MVKSMIAVIS DIHSNLEALN AVLNDIKNRG IKKIFCLGDI VGYGANPNEC VELIRDLNCL SVVGNHDYGV LGKESLDYFN KYGAIAILWT KKVIKNENLK FLDSLPLIIE ENIKGKKVIF SHANPKHPEI WEYLFPDYVD DVFNYGDLIF VGHSHIPFVN SEEGNLLLHE GKIYLDEDKK YLINPGSVGQ PRDGINKASY CIFDEKDFKI EIVRVEYDIK KAYEKIVKNR LPEWLGERLF LGR // ID Y923_METJA Reviewed; 297 AA. AC Q58333; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0923; GN OrderedLocusNames=MJ0923; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98936.1; -; Genomic_DNA. DR PIR; C64415; C64415. DR EnsemblBacteria; AAB98936; AAB98936; MJ_0923. DR KEGG; mja:MJ_0923; -. DR eggNOG; arCOG06562; Archaea. DR eggNOG; ENOG4111ME3; LUCA. DR OMA; GREVFYY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 297 Uncharacterized protein MJ0923. FT /FTId=PRO_0000107108. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. FT TRANSMEM 110 130 Helical. {ECO:0000255}. FT TRANSMEM 135 155 Helical. {ECO:0000255}. FT TRANSMEM 163 183 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. SQ SEQUENCE 297 AA; 34083 MW; 8ECEF68FFBD70D24 CRC64; MEIFKLLRKD RKMLFLMFIG TVSFLFIFIP FLKFQMIGSS HKINAYPSLS AVCGLLLGPI YGFFAVMLVT LIYFFLNPKA FYFGIYSLIP PTLAVISAGA LSEGKWKYSA IILIVGLLLF YLTDVGRVAF YYPYLSTLAL LLILIFREKI SKLLFSKDWK KMIVGATILS FSSVMTDHLY GSILGIVYLH LPAEDYISVI PLFIKERLIM TVIGAFFVIF AIEISKCFLK NATKLKEKLL KSYIDKEIKI NCKNMLNVDE ELLKKYNVKI PSEEEQKEIL KTLVEVVVFN NDKDENR // ID Y924_METJA Reviewed; 263 AA. AC Q58334; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized ATP-binding protein MJ0924; GN OrderedLocusNames=MJ0924; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0547 and MJ0169. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98928.1; -; Genomic_DNA. DR PIR; D64415; D64415. DR ProteinModelPortal; Q58334; -. DR STRING; 243232.MJ_0924; -. DR EnsemblBacteria; AAB98928; AAB98928; MJ_0924. DR KEGG; mja:MJ_0924; -. DR eggNOG; arCOG00589; Archaea. DR eggNOG; COG0455; LUCA. DR OMA; QSYAKKE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 263 Uncharacterized ATP-binding protein FT MJ0924. FT /FTId=PRO_0000107109. FT NP_BIND 16 23 ATP. {ECO:0000255}. FT COMPBIAS 27 34 Poly-Ala. SQ SEQUENCE 263 AA; 29130 MW; EF2020594D327CA0 CRC64; MDYRWIQMKV ITFSIAKGGT GKTIITANAA AALAKKGKKI LLIDGDVGSK SLSHLLNVKS NIFLADIIEE ERPIKDAIVN TPIENIELLA VGKSLADYLK FDINILKRFK ELGDYDYVFI DAPSTSSGVE TYLALGLSDY FIPVLDYTAF GPSLQGAINT IVIGKNYLES TPAGFIINKA EDLPESVIND IKKILGLECI SIIHKNSLVE QSYAKKEIVY LTSSDKKFVE EIDKIVDALE KLKEVKERDI PKVIEKIKES TLL // ID Y938_METJA Reviewed; 250 AA. AC Q58348; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 84. DE RecName: Full=UPF0014 membrane protein MJ0938; GN OrderedLocusNames=MJ0938; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0014 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98943.1; -; Genomic_DNA. DR PIR; B64417; B64417. DR ProteinModelPortal; Q58348; -. DR STRING; 243232.MJ_0938; -. DR EnsemblBacteria; AAB98943; AAB98943; MJ_0938. DR KEGG; mja:MJ_0938; -. DR eggNOG; arCOG04953; Archaea. DR eggNOG; COG0390; LUCA. DR InParanoid; Q58348; -. DR KO; K02069; -. DR OMA; APIMASM; -. DR PhylomeDB; Q58348; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central. DR GO; GO:0015075; F:ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0034220; P:ion transmembrane transport; IBA:GOC. DR InterPro; IPR005226; UPF0014_fam. DR PANTHER; PTHR30028:SF0; PTHR30028:SF0; 1. DR Pfam; PF03649; UPF0014; 1. DR TIGRFAMs; TIGR00245; TIGR00245; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 250 UPF0014 membrane protein MJ0938. FT /FTId=PRO_0000217860. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 95 115 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 195 215 Helical. {ECO:0000255}. FT TRANSMEM 222 242 Helical. {ECO:0000255}. SQ SEQUENCE 250 AA; 27984 MW; 320012908D9C7F22 CRC64; MIIKVMVMLL IELTYAFIFV IIAVLIAYRE KLGIEKKILY VSILALIQLF ILGFVLLYIF SFGMVGAFLM IGVMITLASY LIMREINLKN KTKLFICLFI TFLTTTIVSL AVLTIPKVVK FEPIYVIPLM GMVIGNTMNT IHLALDKIID MVKSERDILW GYLALGATEI EALRPFIKNA VKSAVIPQMN RTKSVGVIFI PGAMVGMLLS GANPIYAAEI QIIIMWMILS SAVISGILIC YLMYKEIIRA // ID Y940_METJA Reviewed; 318 AA. AC Q58350; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 93. DE RecName: Full=TPR repeat-containing protein MJ0940; GN OrderedLocusNames=MJ0940; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 8 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98944.1; -; Genomic_DNA. DR PIR; D64417; D64417. DR ProteinModelPortal; Q58350; -. DR STRING; 243232.MJ_0940; -. DR EnsemblBacteria; AAB98944; AAB98944; MJ_0940. DR KEGG; mja:MJ_0940; -. DR eggNOG; arCOG03038; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q58350; -. DR OMA; KFATAFF; -. DR PhylomeDB; Q58350; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 2. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00515; TPR_1; 2. DR Pfam; PF13181; TPR_8; 1. DR SMART; SM00028; TPR; 8. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 7. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 318 TPR repeat-containing protein MJ0940. FT /FTId=PRO_0000106458. FT REPEAT 17 50 TPR 1. FT REPEAT 84 117 TPR 2. FT REPEAT 119 151 TPR 3. FT REPEAT 152 185 TPR 4. FT REPEAT 186 219 TPR 5. FT REPEAT 221 254 TPR 6. FT REPEAT 255 288 TPR 7. FT REPEAT 289 318 TPR 8. SQ SEQUENCE 318 AA; 36861 MW; 3CA9BCBFF71B4047 CRC64; MEIKNKKLKE TSDVLLSLTY LIKSYEYRDR GNLLESLYYL DKALELNPDF KFAKFLKAIS LAILGDINKS IECLEDITSN SNDPVAYALL GQLYELLGNF DNALECYEKS LGIEEKFATA FFLKVLCLGL SGKYDELLKC CDRLISFAPN FIPAYIIKAN MLRKLGRYEE ALACVNKVLE LKENDTNAIY LKALILNRIG NCDEALKYYE KLIDELNVTW IEVIREAIYL SFLFNKLDKA EKYIEMGLKL RPDDASLWYF KGKLYEKQNK FEEALKYYNK AIQLMPHHTK ALLAKARVLE KLGRIEESIE CYNKALDR // ID Y951_METJA Reviewed; 355 AA. AC Q58361; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=UPF0348 protein MJ0951; GN OrderedLocusNames=MJ0951; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0348 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98952.1; -; Genomic_DNA. DR PIR; G64418; G64418. DR PDB; 3GMI; X-ray; 1.91 A; A=1-355. DR PDBsum; 3GMI; -. DR ProteinModelPortal; Q58361; -. DR STRING; 243232.MJ_0951; -. DR DNASU; 1451848; -. DR EnsemblBacteria; AAB98952; AAB98952; MJ_0951. DR KEGG; mja:MJ_0951; -. DR eggNOG; arCOG03224; Archaea. DR eggNOG; COG1323; LUCA. DR InParanoid; Q58361; -. DR OMA; FTEYNPL; -. DR EvolutionaryTrace; Q58361; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR032266; HIGH_NTase1_ass. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR008513; UPF0348. DR Pfam; PF05636; HIGH_NTase1; 1. DR Pfam; PF16581; HIGH_NTase1_ass; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 355 UPF0348 protein MJ0951. FT /FTId=PRO_0000147199. FT HELIX 1 26 {ECO:0000244|PDB:3GMI}. FT HELIX 30 47 {ECO:0000244|PDB:3GMI}. FT STRAND 52 56 {ECO:0000244|PDB:3GMI}. FT HELIX 64 74 {ECO:0000244|PDB:3GMI}. FT STRAND 76 83 {ECO:0000244|PDB:3GMI}. FT STRAND 93 95 {ECO:0000244|PDB:3GMI}. FT HELIX 100 110 {ECO:0000244|PDB:3GMI}. FT STRAND 113 117 {ECO:0000244|PDB:3GMI}. FT HELIX 121 123 {ECO:0000244|PDB:3GMI}. FT HELIX 126 140 {ECO:0000244|PDB:3GMI}. FT STRAND 144 149 {ECO:0000244|PDB:3GMI}. FT HELIX 153 163 {ECO:0000244|PDB:3GMI}. FT STRAND 168 171 {ECO:0000244|PDB:3GMI}. FT STRAND 174 177 {ECO:0000244|PDB:3GMI}. FT TURN 178 180 {ECO:0000244|PDB:3GMI}. FT STRAND 183 186 {ECO:0000244|PDB:3GMI}. FT HELIX 190 192 {ECO:0000244|PDB:3GMI}. FT HELIX 193 207 {ECO:0000244|PDB:3GMI}. FT STRAND 215 220 {ECO:0000244|PDB:3GMI}. FT HELIX 227 235 {ECO:0000244|PDB:3GMI}. FT HELIX 239 241 {ECO:0000244|PDB:3GMI}. FT HELIX 243 245 {ECO:0000244|PDB:3GMI}. FT HELIX 248 259 {ECO:0000244|PDB:3GMI}. FT HELIX 264 266 {ECO:0000244|PDB:3GMI}. FT HELIX 272 281 {ECO:0000244|PDB:3GMI}. FT HELIX 284 286 {ECO:0000244|PDB:3GMI}. FT HELIX 290 299 {ECO:0000244|PDB:3GMI}. FT HELIX 305 311 {ECO:0000244|PDB:3GMI}. FT HELIX 318 330 {ECO:0000244|PDB:3GMI}. FT HELIX 334 343 {ECO:0000244|PDB:3GMI}. FT STRAND 350 353 {ECO:0000244|PDB:3GMI}. SQ SEQUENCE 355 AA; 41322 MW; 2F683FE81FFE22FA CRC64; MLIGEIMDLN LKNFLEDREE IIRDAKRKDE KSFKDFKKIV EEIKERENKD KIVCDFTEYN PLHKGHKYAL EKGKEHGIFI SVLPGPLERS GRGIPYFLNR YIRAEMAIRA GADIVVEGPP MGIMGSGQYM RCLIKMFYSL GAEIIPRGYI PEKTMEKVID CINKGYHIQV KPYKIICIET GEILGEKLNI DNYVIASMSQ MIYKLNREGL KFNPKFVFVK RLEGISGTKI REAIFSGKFE DIKNMLPKTT LSILKELYDN GKLNELILKR FEDRILETAN EYDLYEYLPS NVAEILEKKR PFNNIEEIKN SLPYGFSRHF RERILSKLEA RIPNETLSKY INNYPAKIKI LAVKL // ID Y953_METJA Reviewed; 100 AA. AC Q58363; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0953; GN OrderedLocusNames=MJ0953; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98958.1; -; Genomic_DNA. DR PIR; A64419; A64419. DR STRING; 243232.MJ_0953; -. DR EnsemblBacteria; AAB98958; AAB98958; MJ_0953. DR KEGG; mja:MJ_0953; -. DR eggNOG; arCOG03099; Archaea. DR eggNOG; COG1863; LUCA. DR InParanoid; Q58363; -. DR KO; K14110; -. DR OMA; IIPFEPY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0008324; F:cation transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR002758; Cation_antiport_E. DR Pfam; PF01899; MNHE; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 100 Uncharacterized protein MJ0953. FT /FTId=PRO_0000107119. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. SQ SEQUENCE 100 AA; 11192 MW; 1E73563CF1336F91 CRC64; MRLLGVIGYL AVLIKAICES WVDVVKRSIN GEIHPQVIEI ESIINNPTGL VLLSWSITAT PGTLVIDLIP EERKLKVAVI SPRSREDIVP FEPYIKKIFD // ID Y971_METJA Reviewed; 365 AA. AC Q58381; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 97. DE RecName: Full=Uncharacterized protein MJ0971; GN OrderedLocusNames=MJ0971; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To S.solfataricus C04034. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98976.1; -; Genomic_DNA. DR PIR; C64421; C64421. DR ProteinModelPortal; Q58381; -. DR STRING; 243232.MJ_0971; -. DR MEROPS; M50.A07; -. DR EnsemblBacteria; AAB98976; AAB98976; MJ_0971. DR KEGG; mja:MJ_0971; -. DR eggNOG; arCOG04064; Archaea. DR eggNOG; COG0750; LUCA. DR InParanoid; Q58381; -. DR OMA; IPWIPGI; -. DR PhylomeDB; Q58381; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004222; F:metalloendopeptidase activity; IBA:GO_Central. DR GO; GO:0031293; P:membrane protein intracellular domain proteolysis; IBA:GO_Central. DR Gene3D; 2.30.42.10; -; 1. DR InterPro; IPR001193; MBTPS2. DR InterPro; IPR001478; PDZ. DR InterPro; IPR008915; Peptidase_M50. DR PANTHER; PTHR13325; PTHR13325; 1. DR Pfam; PF13180; PDZ_2; 1. DR Pfam; PF02163; Peptidase_M50; 1. DR PRINTS; PR01000; SREBPS2PTASE. DR SUPFAM; SSF50156; SSF50156; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 365 Uncharacterized protein MJ0971. FT /FTId=PRO_0000107124. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 60 80 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 141 161 Helical. {ECO:0000255}. FT TRANSMEM 171 191 Helical. {ECO:0000255}. FT TRANSMEM 280 300 Helical. {ECO:0000255}. SQ SEQUENCE 365 AA; 41082 MW; F1608E3149691942 CRC64; MNMDTSKVIL IVAIIIWIIL YSIRDSINLK TYGGIFGILR TKLGLKTIEK LGKYKIWQKI GIISIPICVI LGFFMLLNII DMSIRLLSGT LPKEAAKPVV FLFGDVIPWI PGIIALLIAI SVHELAHGIF AKSFGIKVKS SGILLLLGLP LGAFVELGDE FKTADKKIRG AIASAGPLAN LIIFLTSIPL LSFSYTLPTE LKIIDVKEPA SEFLQKGDII YEINGKKINS LEDFKEFAKT IEPKKEYEIK ILRDNKILTY KIVSSNEGKL GIMVSPTKNT ALFINTIYWT YWFNFLLALF NLLPAMPLDG FHVWNAFPEL LKERKNRFIS KVGQILELFI NEKTLGSITL LVWWVILGSI LYSMW // ID Y986_METJA Reviewed; 75 AA. AC Q58393; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-JAN-1998, sequence version 2. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MJ0986; GN OrderedLocusNames=MJ0986; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98995.1; -; Genomic_DNA. DR PIR; B64423; B64423. DR EnsemblBacteria; AAB98995; AAB98995; MJ_0986. DR KEGG; mja:MJ_0986; -. DR eggNOG; arCOG07514; Archaea. DR eggNOG; ENOG410XZ7U; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 75 Uncharacterized protein MJ0986. FT /FTId=PRO_0000107130. SQ SEQUENCE 75 AA; 8731 MW; 2C32908691499D11 CRC64; MCLICVLGEY IMTQREKDNN IKRVQVTFTK SQWELIENFR GILGQTDAEI VRTIVLTWLS EKSIITTIKK EIGDK // ID Y992_METJA Reviewed; 177 AA. AC Q58399; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0992; GN OrderedLocusNames=MJ0992; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0628. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98997.1; -; Genomic_DNA. DR PIR; H64423; H64423. DR ProteinModelPortal; Q58399; -. DR STRING; 243232.MJ_0992; -. DR EnsemblBacteria; AAB98997; AAB98997; MJ_0992. DR KEGG; mja:MJ_0992; -. DR eggNOG; arCOG06576; Archaea. DR eggNOG; ENOG410ZEY3; LUCA. DR InParanoid; Q58399; -. DR OMA; HENITFF; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 177 Uncharacterized protein MJ0992. FT /FTId=PRO_0000107135. SQ SEQUENCE 177 AA; 20903 MW; E5FE519F740853C5 CRC64; MFNIDEFKEI AEKLPTFKSL PNEGKYRTAI GRYYYCIFLK LREIVKEIEQ DREDGIYELL NSGKAHKALP AYFRTLSDKI RVDNLKNDLI TLAEALEDLR KLRNMCDYDV DVSISFTKVI EAEIDIEIIE QTITNLSYQK PKSKTKIVGL KNVLEYFKDK DNLPTYNEVI NIMYRRR // ID YE1A_METJA Reviewed; 145 AA. AC P81328; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1417.1; GN OrderedLocusNames=MJ1417.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99431.1; -; Genomic_DNA. DR ProteinModelPortal; P81328; -. DR STRING; 243232.MJ_1417.1; -. DR EnsemblBacteria; AAB99431; AAB99431; MJ_1417.1. DR KEGG; mja:MJ_1417.1; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 145 Uncharacterized protein MJ1417.1. FT /FTId=PRO_0000107316. FT TRANSMEM 97 117 Helical. {ECO:0000255}. SQ SEQUENCE 145 AA; 17308 MW; A37763D64BAD99C6 CRC64; MYLIWIIGGG QKDLTNKILD EIKKLYEQLD EIKDKNINSS NVQLNEFMRQ NVNMLKELNQ KIDKYLENNN EILKEMEKYV KEDIEHKNRM ERKLKQISML LLIVIIAIGL TISYMVILNN EYLSTQLFNY IQIAIQYLKS LLSNY // ID Y3524_METJA Reviewed; 259 AA. AC Q60283; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 75. DE RecName: Full=Uncharacterized protein MJECL24; GN OrderedLocusNames=MJECL24; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ParA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37095.1; -; Genomic_DNA. DR PIR; G64512; G64512. DR ProteinModelPortal; Q60283; -. DR EnsemblBacteria; AAC37095; AAC37095; MJ_ECL24. DR KEGG; mja:MJECL24; -. DR HOGENOM; HOG000019422; -. DR InParanoid; Q60283; -. DR KO; K03496; -. DR OMA; NEVATHG; -. DR PhylomeDB; Q60283; -. DR Proteomes; UP000000805; Plasmid large ECE. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR025669; AAA_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13614; AAA_31; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 259 Uncharacterized protein MJECL24. FT /FTId=PRO_0000201991. SQ SEQUENCE 259 AA; 29031 MW; C637DF1BFF78EFAC CRC64; MVVISIANQK GGVGKTTIAL NLSFTLAEKG YDTLVIDLDP QFNLSFGILG MKLLDYADKN IGILLSKNSV KKKEIEESII KINDKLDLIP SHLQLSAVEK MLVNAYAREM KLKNIINQIK ENYDYIIIDN APSLGLFLIN SLVASDYIII PCEPSYFSIA GVQLMLDTVE EIKESNLNPK LKVLGFIFNK YSKQSKIPQK RLEQLKQLYP NIPVIGVIPR TITVEKAERE GKPVFKFDAN NPASVAFSEL AEWVIENVK // ID Y3528_METJA Reviewed; 1272 AA. AC Q60287; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJECL28; GN OrderedLocusNames=MJECL28; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37099.1; -; Genomic_DNA. DR PIR; C64513; C64513. DR ProteinModelPortal; Q60287; -. DR EnsemblBacteria; AAC37099; AAC37099; MJ_ECL28. DR KEGG; mja:MJECL28; -. DR OMA; KRINIAY; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF04851; ResIII; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 1272 Uncharacterized protein MJECL28. FT /FTId=PRO_0000107514. SQ SEQUENCE 1272 AA; 149439 MW; 88E7AE8C48629DEA CRC64; MNNILSNSIK SLRYWDDQTV KAIFDKYQIN VSGIYNISDD ILESDLKLHI AQLLFLIVKH KEEFSVYLGE THLEKILKKL VKQFKYLEIR FLGKFKGKKQ FFIDISDLHV DNILEKTEEI IKLIKKQYEY IKKQKKRRLD GVYVGIAPRK EKRGDAGAAT AWSYIAFDFD VEEWKTNKMP TEEEIMEKLI KYLSKFVEKD ILPHKVAFTG GGLRFILYPE RPILEEELIL LRMIAEDLGA DIAMYDLARV DRLVGTYNYK EKYGSPRPCV TIAQLTDEED IEKLLTPIIL YEKFGIIENY KEFEVLFNEK REELYNKRGL NNITTTINRL IKKPNLNKTI LQDINKRIYK WLYTIQDKLT KKLGKRWIEK LLSYLGIDYK YGKNGTRLDL WSLFFDDGKN PDCSIYINEG YNAVMVDFHD PNMRFIALAG LWMIKEFRDK IIEFLKLHNI NPKPSTYRTV REIMNELLDR ETIKIEAEGY LPKEAIIKAY QLSIEQGVPV FLKADTGRGK TYTLTRNTRE IKEVFKKHAI AVAFPYKIQV LQVGAGLHAD GVVVPMYYED GKKLDKNTIH YLTIGTYDQV ENMLNDLCYD TYKGEKIQVA NEEDILLAID EAHDLVIQKE FRKRAITGVK KCIDRAGGCV LLTATPELIN LNNYPVIEVE FKDEKKLFER CSIHIAKNII GEFCEYILLM FRQGWIKNAV VLVDNKKMIE NIKYTLELYG FNKPIYVITR ETVGIDKASK MIINEEKVPE EGLILATRVI SEGVNIKNHV DLVWALYCKS ATTIRQFIAR CRNGGGELIV TAPFKEREEE PMIIDYNAMI EMFKENYKLL KEYLETDIEV LKELDKNYKK VLISQIQNAI YYDEEKKDWV LDEDEIAHIY NSLLEAHITR DYKLLKEYLE KTTGYEFAIK TIKELKESKL DKFLKYNYLE YLEKVSAKHI IIAFKEYGVN EIKNALEYNN YKKFKDCRDE YTPQLIKKHS KRINRSINVL KDVYNIPEVI EVYNLMLNKG KDDDKKSNLD ENTIKKCLEE INEYKKIVKE INENEDRKTK KIYHIDLKLL EEHKDKLSTL ARIIEELILK TFLCPPSKWG KIQRIIRAVW NIVVGEDDER LDRRKLGLRS LVAKVLIKVR DFAIERQKFK IRELIEVIKE ECGFTLTLDE VRRLIRAIFN CVIRGVKKLG ENAVVEIKEL NKEFKTLYEI IKQNINSNSV EKCEKVIEKK IEENGGEILE MELYELIVEK LKFVEEVFYK ALEKLKKLGV IYEPKPGLLR IT // ID Y3535_METJA Reviewed; 630 AA. AC Q60291; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 80. DE RecName: Full=Uncharacterized protein MJECL35; GN OrderedLocusNames=MJECL35; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OG Plasmid large ECE. OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 Toprim domain. {ECO:0000255|PROSITE- CC ProRule:PRU00995}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77118; AAC37104.1; -; Genomic_DNA. DR PIR; B64514; B64514. DR ProteinModelPortal; Q60291; -. DR EnsemblBacteria; AAC37104; AAC37104; MJ_ECL35. DR KEGG; mja:MJECL35; -. DR HOGENOM; HOG000155272; -. DR InParanoid; Q60291; -. DR OMA; PGYFLFS; -. DR Proteomes; UP000000805; Plasmid large ECE. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000731; P:DNA synthesis involved in DNA repair; IBA:GO_Central. DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR006171; Toprim_domain. DR SMART; SM00493; TOPRIM; 1. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS50880; TOPRIM; 1. PE 3: Inferred from homology; KW Complete proteome; Plasmid; Reference proteome. FT CHAIN 1 630 Uncharacterized protein MJECL35. FT /FTId=PRO_0000107519. FT DOMAIN 412 507 Toprim. {ECO:0000255|PROSITE- FT ProRule:PRU00995}. SQ SEQUENCE 630 AA; 72441 MW; FD8EAE30D2F5B58E CRC64; MKIEQVKIEN FRSIYDLTVE FGKVTVLIGK NSSGKTSILN VIRIIFENLD TNSTEKNLNI TTITEQNLKD QIRRLWFYTY QNYPIKLAVW LNFDEGEGDK LREVCGLESN VKKAYIEVSI ESNNNQIIWK LQNVIIFGYV SETSKIAKEA LKKMKEIHSK VTGHNIESKT GDSLVPCVIV ESGTIKNKDV FNIFIDLIKN KICYVNTFPE IYKMVNIPIK GLFAHPMVSS ELINVIKNTI KDFARLRMLY DCLREIKGSV DTYEQPDRTE ILTKSYEGMS LNYELFGSGD QIIDGILASI ISKGKHHIFL IEEPEIHLHP AYIRRLARVL EDLANNLNVQ LIIVTHSPDF IATLKDKRFV IGVRKDSIKI NFEGYPTELL ATRIFYPFRG SRLSESLARD LGVVPGYFLF SDVAILVEGN SDRIILQGYI DLLIEQLKNL PKFSYIIIPY AQRSLKEMIK VFKEDYGIKV FLIADNDEEG LKNVKIAKDM GLRENFEVFI IEKKDILGYI KPEDFILALD ELLRECLKDK YEEVLQDEEI KSIIDEIKIF GACKNEEGKN EKDLLHKLSG KLFTVLKNVD EEFIITLGWD SGRSIERYLK CKIAEKIVSR LTEVPEDIKK IILNIDSELG // ID Y390_METJA Reviewed; 130 AA. AC Q57835; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0390; GN OrderedLocusNames=MJ0390; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98381.1; -; Genomic_DNA. DR PIR; F64348; F64348. DR STRING; 243232.MJ_0390; -. DR EnsemblBacteria; AAB98381; AAB98381; MJ_0390. DR KEGG; mja:MJ_0390; -. DR eggNOG; arCOG08287; Archaea. DR eggNOG; ENOG41110P2; LUCA. DR OMA; DIYLGDK; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 130 Uncharacterized protein MJ0390. FT /FTId=PRO_0000106851. FT COMPBIAS 57 77 Asn/Lys-rich. FT COMPBIAS 92 129 Ile/Lys-rich. SQ SEQUENCE 130 AA; 14973 MW; 5854471834A81D73 CRC64; MEEKIILSIQ NPEDVLISYV DIYLGDKNVS LEVLSKDTAK INLPFDKDEG EGEIVVKIKY KTLPHYKNNN NKKEVKKQDY KNLTQTLNEI TKKTTNRKDN DIIIADSKPV SLDGLKKEEK KKKLNDIIIV // ID Y401_METJA Reviewed; 66 AA. AC Q57844; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0401; GN OrderedLocusNames=MJ0401; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98394.1; -; Genomic_DNA. DR PIR; A64350; A64350. DR ProteinModelPortal; Q57844; -. DR STRING; 243232.MJ_0401; -. DR EnsemblBacteria; AAB98394; AAB98394; MJ_0401. DR KEGG; mja:MJ_0401; -. DR eggNOG; arCOG06573; Archaea. DR eggNOG; ENOG410Y768; LUCA. DR OMA; EVPYGVP; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR004039; Rubredoxin-type_fold. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 66 Uncharacterized protein MJ0401. FT /FTId=PRO_0000106853. FT COMPBIAS 43 65 Arg/Gly-rich. SQ SEQUENCE 66 AA; 7416 MW; 69E0B0E5B8CF5B94 CRC64; MEMKRFLCAK CQKVIEVPYG VPKPDVCPYC GAPATFIHRI DAGGRGLGPG RGRRCGMRMM GRFRRE // ID Y403_METJA Reviewed; 287 AA. AC Q57846; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=MEMO1 family protein MJ0403 {ECO:0000255|HAMAP-Rule:MF_00055}; GN OrderedLocusNames=MJ0403; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MEMO1 family. {ECO:0000255|HAMAP- CC Rule:MF_00055}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98390.1; -; Genomic_DNA. DR PIR; C64350; C64350. DR ProteinModelPortal; Q57846; -. DR STRING; 243232.MJ_0403; -. DR EnsemblBacteria; AAB98390; AAB98390; MJ_0403. DR KEGG; mja:MJ_0403; -. DR eggNOG; arCOG01728; Archaea. DR eggNOG; COG1355; LUCA. DR InParanoid; Q57846; -. DR KO; K06990; -. DR OMA; ISMCGYG; -. DR PhylomeDB; Q57846; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008198; F:ferrous iron binding; IEA:InterPro. DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro. DR GO; GO:0006725; P:cellular aromatic compound metabolic process; IEA:InterPro. DR HAMAP; MF_00055; MEMO1; 1. DR InterPro; IPR002737; MEMO1_fam. DR InterPro; IPR004183; Xdiol_dOase_suB. DR PANTHER; PTHR11060; PTHR11060; 1. DR Pfam; PF01875; Memo; 1. DR SUPFAM; SSF53213; SSF53213; 1. DR TIGRFAMs; TIGR04336; AmmeMemoSam_B; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 287 MEMO1 family protein MJ0403. FT /FTId=PRO_0000134379. SQ SEQUENCE 287 AA; 32097 MW; D788000C3E6B8834 CRC64; MNKIRYPAVA GLFYPSHPDE LIDMIEQCYL HKFGPKSMPV HGTYEKPIGL LCPHAGYVYS GPIQAHSYYE LSKRVDALEE TTVVILGPNH TGLGSGVSVM DGIWRTPLGD VKCDEEFVEE LWRKCEIVDL DETAHLNEHS IEVQLPFLKH LELLNIAKFK IVPICMMFQD YETAVEVGYF IAKIAKELNR RIVVIASSDL THYEPQEIAS KKDAIVIKDI LEMNEKELYE DVVNYNISMC GYGPVIAMLK AMKTLGAEKA KLLAYATSGD ITGDYSAVVG YASAIVE // ID Y421_METJA Reviewed; 360 AA. AC Q57864; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0421; GN OrderedLocusNames=MJ0421; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 THUMP domain. {ECO:0000255|PROSITE- CC ProRule:PRU00529}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98409.1; -; Genomic_DNA. DR PIR; E64352; E64352. DR ProteinModelPortal; Q57864; -. DR STRING; 243232.MJ_0421; -. DR EnsemblBacteria; AAB98409; AAB98409; MJ_0421. DR KEGG; mja:MJ_0421; -. DR eggNOG; arCOG00056; Archaea. DR eggNOG; COG1818; LUCA. DR InParanoid; Q57864; -. DR KO; K06963; -. DR OMA; GLFRFAD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003723; F:RNA binding; IEA:InterPro. DR InterPro; IPR029028; Alpha/beta_knot_MTases. DR InterPro; IPR025849; SPOUT_MTase_fused_to_THUMP. DR InterPro; IPR004114; THUMP_dom. DR Pfam; PF14419; SPOUT_MTase_2; 1. DR Pfam; PF02926; THUMP; 1. DR SMART; SM00981; THUMP; 1. DR SUPFAM; SSF75217; SSF75217; 1. DR PROSITE; PS51165; THUMP; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 360 Uncharacterized protein MJ0421. FT /FTId=PRO_0000106867. FT DOMAIN 45 148 THUMP. {ECO:0000255|PROSITE- FT ProRule:PRU00529}. SQ SEQUENCE 360 AA; 41397 MW; 6C268E2E09D2753B CRC64; MKFIIKTQKG FENIVVNNLK EIVDDFNYIV SPDGYQGIVI VESDEDIEDK ILQIPEVERV LKVYFETETD FDKIVNLAEK IKDYIKEDET FAVETKKRGK HDFSSTDINI VLGAKIKDLT NASVDLNNPD KVVHVEVFKN KTYVSITPGE KFKKYTKEKR NARELFKKVV IVQMPYLGEK IVCKRFGEAI GRAAQGFEVK ELIIAPKEKV DAYELMEFIK GVKIGQHSRY EIQKRAYPFE IKLVPVTVQD LYQVVRDKRR DNRLLIITDP KGDELSKIKD KLAYDLRKKR EIIVFCGSRE GIPRGLFRFA DYIVDLAPHM TFATEHAIPA ALIALWGVYS GEDLENSSKE EKTESNSNGE // ID Y423_METJA Reviewed; 59 AA. AC Q57866; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=Uncharacterized ATP-binding protein MJ0423; GN OrderedLocusNames=MJ0423; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98411.1; -; Genomic_DNA. DR PIR; G64352; G64352. DR ProteinModelPortal; Q57866; -. DR STRING; 243232.MJ_0423; -. DR EnsemblBacteria; AAB98411; AAB98411; MJ_0423. DR KEGG; mja:MJ_0423; -. DR eggNOG; arCOG03166; Archaea. DR eggNOG; COG1672; LUCA. DR KO; K06921; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01637; ATPase_2; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 59 Uncharacterized ATP-binding protein FT MJ0423. FT /FTId=PRO_0000106868. FT NP_BIND 33 40 ATP. {ECO:0000255}. FT COMPBIAS 12 23 Glu-rich. SQ SEQUENCE 59 AA; 7209 MW; 8DFBC8C9CBD610EA CRC64; MYGIVMFVNR KEELEFLERK WNENKANLII LYGRRRVGKT MLIKKFLENK KIKRASIFC // ID Y441_METJA Reviewed; 267 AA. AC Q57883; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=UPF0721 transmembrane protein MJ0441; GN OrderedLocusNames=MJ0441; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the UPF0721 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98428.1; -; Genomic_DNA. DR PIR; A64355; A64355. DR ProteinModelPortal; Q57883; -. DR STRING; 243232.MJ_0441; -. DR EnsemblBacteria; AAB98428; AAB98428; MJ_0441. DR KEGG; mja:MJ_0441; -. DR eggNOG; arCOG02050; Archaea. DR eggNOG; COG0730; LUCA. DR InParanoid; Q57883; -. DR KO; K07090; -. DR OMA; LPFRHAV; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002781; TM_pro_TauE-like. DR PANTHER; PTHR30269; PTHR30269; 1. DR Pfam; PF01925; TauE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 267 UPF0721 transmembrane protein MJ0441. FT /FTId=PRO_0000106878. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 87 107 Helical. {ECO:0000255}. FT TRANSMEM 158 178 Helical. {ECO:0000255}. FT TRANSMEM 185 205 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. SQ SEQUENCE 267 AA; 28980 MW; 08EF7F36D198FCF0 CRC64; MVIKLEFEFL LLLPLLIIVG FIVGILGSLF GIGGGFLVAP ILTFIFDYFG IPDGVKFAVG TSLFVVFINS IISIFRHAKI KNINWKASIT IGIISLVFSY FSGFLVVNFI DSAILKKLFG IFLIANAIYM AKSHHIDKIS DREDKLEPFI LCGVITGFLS GLFGIGGGIV IIPILAMAKY PVKRAVAISV GVIPLTSIGG LISYLTANTE GYIYNIGYVS IPIALIMAIP IIYSSKLGIK INQKISPKHL RIMLSSILGV MGLFMLL // ID Y489_METJA Reviewed; 268 AA. AC Q57913; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0489; GN OrderedLocusNames=MJ0489; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98480.1; -; Genomic_DNA. DR PIR; A64361; A64361. DR ProteinModelPortal; Q57913; -. DR STRING; 243232.MJ_0489; -. DR EnsemblBacteria; AAB98480; AAB98480; MJ_0489. DR KEGG; mja:MJ_0489; -. DR eggNOG; arCOG04864; Archaea. DR eggNOG; COG4017; LUCA. DR OMA; MKYGITE; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR009573; DUF1188. DR Pfam; PF06690; DUF1188; 1. DR PIRSF; PIRSF019265; DUF1188; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 268 Uncharacterized protein MJ0489. FT /FTId=PRO_0000106895. SQ SEQUENCE 268 AA; 30532 MW; 1A24C6D66FA955A6 CRC64; MGCGIMKYGI TEMVKTIDTK TRVVDVTNEI AKKKYQAIRD FLEGEEFKEV VIFGVYLWGN YTAQMLSKYA DKVYLVDIHE FMKGFVPNNN SIKFLNLNEF KLKFIRGEVN PDLIVDLTGL GGIEPEFLAK FNPKVFIVED PKGVFDVDIY EADNTYKRTA PFIEKAKVGV LKTYRKARVS KTSGTMTLTI DTIVDASREI TSLDGVLYAI PNLRYYEGIL FHENDIHKFL SEISQPAITI STLNDVLDEA EEILSNNINL IYSFVEEL // ID Y531_METJA Reviewed; 170 AA. AC Q57951; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Universal stress protein MJ0531; DE Short=USP MJ0531; GN OrderedLocusNames=MJ0531; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the universal stress protein A family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98522.1; -; Genomic_DNA. DR PIR; C64366; C64366. DR ProteinModelPortal; Q57951; -. DR STRING; 243232.MJ_0531; -. DR EnsemblBacteria; AAB98522; AAB98522; MJ_0531. DR KEGG; mja:MJ_0531; -. DR eggNOG; arCOG02053; Archaea. DR eggNOG; COG0589; LUCA. DR InParanoid; Q57951; -. DR OMA; NAHCPVL; -. DR PhylomeDB; Q57951; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006950; P:response to stress; IEA:InterPro. DR Gene3D; 3.40.50.620; -; 1. DR InterPro; IPR014729; Rossmann-like_a/b/a_fold. DR InterPro; IPR006015; Universal_stress_UspA. DR InterPro; IPR006016; UspA. DR Pfam; PF00582; Usp; 1. DR PIRSF; PIRSF006276; UspA; 1. DR PRINTS; PR01438; UNVRSLSTRESS. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 170 Universal stress protein MJ0531. FT /FTId=PRO_0000147445. SQ SEQUENCE 170 AA; 18890 MW; D992BD538494964A CRC64; MKKVFILLAL KYYILNSIIR NGENLYKKIV IPTDGSDVSL EAAKHAINIA KEFDAEVYAI YVVDVSPFVG LPAEGSWELI SELLKEEGQE ALKKVKKMAE EWGVKIHTEM LEGVPANEIV EFAEKKKADL IVMGTTGKTG LERILLGSVA ERVIKNAHCP VLVVKKPKKE // ID Y535_METJA Reviewed; 343 AA. AC Q57955; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ0535; GN OrderedLocusNames=MJ0535; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative deacetylase. {ECO:0000250}. CC -!- SIMILARITY: Belongs to the histone deacetylase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98526.1; -; Genomic_DNA. DR PIR; G64366; G64366. DR ProteinModelPortal; Q57955; -. DR STRING; 243232.MJ_0535; -. DR EnsemblBacteria; AAB98526; AAB98526; MJ_0535. DR KEGG; mja:MJ_0535; -. DR eggNOG; arCOG00324; Archaea. DR eggNOG; COG0123; LUCA. DR InParanoid; Q57955; -. DR OMA; HIDIHQD; -. DR PhylomeDB; Q57955; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.800.20; -; 1. DR InterPro; IPR000286; His_deacetylse. DR InterPro; IPR023801; His_deacetylse_dom. DR PANTHER; PTHR10625; PTHR10625; 1. DR Pfam; PF00850; Hist_deacetyl; 1. DR PRINTS; PR01270; HDASUPER. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Reference proteome. FT CHAIN 1 343 Uncharacterized protein MJ0535. FT /FTId=PRO_0000114745. SQ SEQUENCE 343 AA; 38174 MW; 8848EDB757FDC233 CRC64; MVSIMPKILY NPEVLGHKPK SYHVENPERV LTILNSLKSN GFDDIVLIEG KSTINEILEI HSRDYVYSII NLSKSFNYYD GDTYLCDRTL DAALTAFKLA KEAVKLALKD RDLYFALTRP PGHHAGISGR ALGAMSNGFC IFNNIAGAAR LAKNYMKKVI IIDFDVHHGN GTQEIFWNDN RVIHIDFHQR GIYPGTGDIL DIGGEEAKGT KINLPFPAHS TDADYIFAWN EIVEPILNYF SPDTVLVSAG FDAFINDGLA SMDLTETFYR FVGAKLSGYS VTAVLEGGYS IGLKYAPPAF LDGYVDAKDV LDNLEDYTVI NSNEVKSMVK NVKKIIGEYL DIF // ID Y550_METJA Reviewed; 365 AA. AC Q57970; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized protein MJ0550; GN OrderedLocusNames=MJ0550; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98542.1; -; Genomic_DNA. DR PIR; F64368; F64368. DR ProteinModelPortal; Q57970; -. DR STRING; 243232.MJ_0550; -. DR EnsemblBacteria; AAB98542; AAB98542; MJ_0550. DR KEGG; mja:MJ_0550; -. DR eggNOG; arCOG01360; Archaea. DR eggNOG; COG1244; LUCA. DR InParanoid; Q57970; -. DR KO; K06936; -. DR OMA; NKYFDFA; -. DR PhylomeDB; Q57970; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0033588; C:Elongator holoenzyme complex; IBA:GO_Central. DR GO; GO:0004402; F:histone acetyltransferase activity; IBA:GO_Central. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR GO; GO:0016573; P:histone acetylation; IBA:GOC. DR GO; GO:0006357; P:regulation of transcription from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0006368; P:transcription elongation from RNA polymerase II promoter; IBA:GO_Central. DR GO; GO:0002098; P:tRNA wobble uridine modification; IBA:GO_Central. DR Gene3D; 3.80.30.20; -; 1. DR InterPro; IPR005909; CHP01210. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023404; rSAM_horseshoe. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004954; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR01210; TIGR01210; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 365 Uncharacterized protein MJ0550. FT /FTId=PRO_0000106927. SQ SEQUENCE 365 AA; 42518 MW; ED684F9589D77411 CRC64; MNQIINDNYR EFLKKLRERH LKKRKVKDKN KPIAVWMQDD IYRDFSIGKS LTIILRTEGC YYAKEGGCLM CSYLMDSSPE KITAENIINQ FNYAIEKYKE KIKDLKDFSV KIFTSGSFLD DREVPKEARN YIFKKLSEFD NLKEVAIESR PEFIDEDKLN EIRKYLDVNV EIGVGIESFN EEIREKAINK GITNEQIIRA IELAKNYNIG IKAYLLIKPL FITEKEAIYD SISSANKCIE LGCSRISFCP ATVHKGSVME FFFNKNQYRP PFLWSIIEIL KEVKKSNPKA LIMCDTSGVG SERGAHNLYN CKCNKLIKER LERFTLTQDI NVLNVECECK NIWNAYIEVE NKNIVPLGDE RKLLL // ID Y554_METJA Reviewed; 152 AA. AC Q57974; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0554; GN OrderedLocusNames=MJ0554; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0129 and MJ0587. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98545.1; -; Genomic_DNA. DR PIR; B64369; B64369. DR ProteinModelPortal; Q57974; -. DR DNASU; 1451419; -. DR EnsemblBacteria; AAB98545; AAB98545; MJ_0554. DR KEGG; mja:MJ_0554; -. DR PhylomeDB; Q57974; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 152 Uncharacterized protein MJ0554. FT /FTId=PRO_0000106928. FT TRANSMEM 15 35 Helical. {ECO:0000255}. FT TRANSMEM 43 63 Helical. {ECO:0000255}. FT TRANSMEM 117 137 Helical. {ECO:0000255}. SQ SEQUENCE 152 AA; 17434 MW; 4408E3CA5E03EB2F CRC64; MVNEHKAHAS FMFKIINVFV SFGFNLILGI LIYDIFFNID ENLVVACILI AMPIIAFLIL ILTGGVHKEL TYLQIYDKYK LMCEFIREIT ISTITSELAT IATMILYQLQ NPIKTITFLL LLIAFLAFGL IFTKLLIDAY FITLKKLKSL KE // ID Y612_METJA Reviewed; 446 AA. AC Q58029; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 96. DE RecName: Full=Probable arogenate/prephenate dehydrogenase; DE EC=1.3.1.-; GN OrderedLocusNames=MJ0612; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 prephenate/arogenate dehydrogenase domain. CC {ECO:0000255|PROSITE-ProRule:PRU00522}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98605.1; -; Genomic_DNA. DR PIR; D64376; D64376. DR ProteinModelPortal; Q58029; -. DR STRING; 243232.MJ_0612; -. DR EnsemblBacteria; AAB98605; AAB98605; MJ_0612. DR KEGG; mja:MJ_0612; -. DR eggNOG; arCOG00245; Archaea. DR eggNOG; COG0287; LUCA. DR eggNOG; COG4937; LUCA. DR InParanoid; Q58029; -. DR KO; K04517; -. DR OMA; RIIGQNP; -. DR PhylomeDB; Q58029; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro. DR GO; GO:0070403; F:NAD+ binding; IBA:GO_Central. DR GO; GO:0004826; F:phenylalanine-tRNA ligase activity; IEA:InterPro. DR GO; GO:0004665; F:prephenate dehydrogenase (NADP+) activity; IBA:GO_Central. DR GO; GO:0008977; F:prephenate dehydrogenase activity; IBA:GO_Central. DR GO; GO:0000049; F:tRNA binding; IEA:InterPro. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GO_Central. DR GO; GO:0006432; P:phenylalanyl-tRNA aminoacylation; IEA:InterPro. DR GO; GO:0008033; P:tRNA processing; IEA:InterPro. DR GO; GO:0006571; P:tyrosine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.30.70.380; -; 1. DR Gene3D; 3.40.50.720; -; 1. DR InterPro; IPR008927; 6-PGluconate_DH_C-like. DR InterPro; IPR016040; NAD(P)-bd_dom. DR InterPro; IPR005121; PheS_beta_Fdx_antiC-bd. DR InterPro; IPR008299; Prep_DH/arog_DH. DR InterPro; IPR003099; Prephen_DH. DR Pfam; PF03147; FDX-ACB; 1. DR Pfam; PF02153; PDH; 1. DR PIRSF; PIRSF006549; PDH_arog_dh_reg; 1. DR SMART; SM00896; FDX-ACB; 1. DR SUPFAM; SSF48179; SSF48179; 1. DR SUPFAM; SSF51735; SSF51735; 1. DR SUPFAM; SSF54991; SSF54991; 1. DR PROSITE; PS51176; PDH_ADH; 1. PE 3: Inferred from homology; KW Complete proteome; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 446 Probable arogenate/prephenate FT dehydrogenase. FT /FTId=PRO_0000119199. FT DOMAIN 6 288 Prephenate/arogenate dehydrogenase. FT {ECO:0000255|PROSITE-ProRule:PRU00522}. SQ SEQUENCE 446 AA; 50888 MW; 5968C24E2C9AC2DB CRC64; MKNTNLTISI IGGTDGLGKW FARYLKNKGF NVIVTGRDIE KGKNVEKELG VEFTNNNIEA AKKGDIVIVA VPINVTERVI KEVAPHVREG CLLMDITSIK EIPSKAMEEH VKEGVTVIPT HPMFGPSTPS LLRQVVILTP SEKHKNTEWF NKVYNFLKKE GAKVIVIPPE KHDRIMGIVQ GLTHFAFISL GATLKELNVD IKESRKFASP IYELMISIIG RIIGQNPYLY ADIQMFNPRI KEIHETFINQ CKEISEIVKN KDREGFVKIM KEAAKHFGSE AKRGAYYSDK AVFALTSEIE KLNKLIGKDV AVKNINSNVV HFGVLKDIED DYLILNKNGK EQKFNILRVE VFAGDELSKL KKKHLEKKYI DVSVLFKKDV DEEVILNLLK KMFDIEIIDV YEGEKIEEGY KSITFRIYGY NKDELKNIEK EFLKIIKNIG GKERFK // ID Y614_METJA Reviewed; 130 AA. AC Q58031; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0614; GN OrderedLocusNames=MJ0614; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98608.1; -; Genomic_DNA. DR PIR; F64376; F64376. DR STRING; 243232.MJ_0614; -. DR EnsemblBacteria; AAB98608; AAB98608; MJ_0614. DR KEGG; mja:MJ_0614; -. DR eggNOG; arCOG04850; Archaea. DR eggNOG; COG1417; LUCA. DR OMA; KIEPIVA; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002572; DUF22. DR Pfam; PF01629; DUF22; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 130 Uncharacterized protein MJ0614. FT /FTId=PRO_0000106959. SQ SEQUENCE 130 AA; 14873 MW; 311EF0525908896F CRC64; MVMFMVFRIL GRMTKIEKEI KEEEAKYDLI IKNEAKIEPI VAEEDMEFKQ GDIKPIRIKK IKIPPMSVLL ICPYGRHRVG HVVAVGEEVP MPIDVEREVD MAMFACGFEG EVKKGDLIGM LLILAAEKRE // ID Y627_METJA Reviewed; 117 AA. AC Q58044; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 61. DE RecName: Full=Uncharacterized protein MJ0627; GN OrderedLocusNames=MJ0627; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98626.1; -; Genomic_DNA. DR PIR; C64378; C64378. DR STRING; 243232.MJ_0627; -. DR EnsemblBacteria; AAB98626; AAB98626; MJ_0627. DR KEGG; mja:MJ_0627; -. DR OMA; IFKISEQ; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 117 Uncharacterized protein MJ0627. FT /FTId=PRO_0000106961. SQ SEQUENCE 117 AA; 13866 MW; AECD137581B92706 CRC64; MEIDVKSPDL IINTIRGNEK IYFDKSIFEE SLDNKFEIIQ YLMKILERFL KIYDNHIKEI KLLIDSENHP EPHLIVVIKF KNKENIFKIS EQIENKIYEN PKSKNVLVYP ITGGTDV // ID Y629_METJA Reviewed; 214 AA. AC Q58046; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=UPF0111 protein MJ0629; GN OrderedLocusNames=MJ0629; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0111 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98621.1; -; Genomic_DNA. DR PIR; E64378; E64378. DR ProteinModelPortal; Q58046; -. DR STRING; 243232.MJ_0629; -. DR EnsemblBacteria; AAB98621; AAB98621; MJ_0629. DR KEGG; mja:MJ_0629; -. DR eggNOG; arCOG02640; Archaea. DR eggNOG; COG1392; LUCA. DR InParanoid; Q58046; -. DR KO; K07220; -. DR OMA; PNMRREL; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR002727; DUF47. DR InterPro; IPR018445; Put_Phosphate_transp_reg. DR Pfam; PF01865; PhoU_div; 1. DR TIGRFAMs; TIGR00153; TIGR00153; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 214 UPF0111 protein MJ0629. FT /FTId=PRO_0000154913. SQ SEQUENCE 214 AA; 25428 MW; EB6895CCC79C4AD9 CRC64; MDVITMSIFL FERDNEKSVI DNLRLLIQMS LKSIELLKDY MNSKDEKILK EIIKIEEEGD ETTKNIRINL EKAFLPNMRR ELSRSAELLD ETLDSLKHAA MLYELLKEEF DEYLKNEIDL VLMITVDMFQ HLDRVLDVIE KGGDLDPIIK EIKDKEKFID DVYQNRIYKY LINLEVESFW EGKILCDFID NIVNISDYIE DVADELHIIY LHTK // ID Y640_METJA Reviewed; 324 AA. AC Q58057; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0640; GN OrderedLocusNames=MJ0640; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98632.1; -; Genomic_DNA. DR PIR; H64379; H64379. DR ProteinModelPortal; Q58057; -. DR STRING; 243232.MJ_0640; -. DR EnsemblBacteria; AAB98632; AAB98632; MJ_0640. DR KEGG; mja:MJ_0640; -. DR eggNOG; arCOG00640; Archaea. DR eggNOG; COG2144; LUCA. DR InParanoid; Q58057; -. DR KO; K07123; -. DR OMA; AADGIWG; -. DR PhylomeDB; Q58057; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.1330.10; -; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR017668; Methan_mark_2. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR011413; UCP036540_AIR. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036540; UCP036540_AIR; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR03267; methan_mark_2; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 324 Uncharacterized protein MJ0640. FT /FTId=PRO_0000106967. SQ SEQUENCE 324 AA; 35805 MW; 9DDA077ED84982EE CRC64; MNLKKVVNEI RNFEGILRKI AIKDVVETFD FNDEDYEFDI IVDFGDDAAV IGIDGDNAIL LAADGIWGKL LEADPWWAGY CSVLVNCKDI AAMGGKCVGM TNIISIKDKD ICREVLKGVK DGVKKFGVPM VGGHTHPDAM CNVLDVSITG IAKKDCILRS DNAKIGDKII FAYDLVGQIY KSFPLNWDTT TMKSKKLVRA QMDALVQIAE NKLANSCKDI SNPGAIGTLG MLLEVSRKGG VVDITKIPKP EEIDLIHWLK VYPGSGYVLT AKEENFKEIK DIFEDVEMTA EICGEVIAEK KLYITDGENK EVVFDFEKEF ICGC // ID Y662_METJA Reviewed; 239 AA. AC Q58076; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 87. DE RecName: Full=Uncharacterized protein MJ0662; GN OrderedLocusNames=MJ0662; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98659.1; -; Genomic_DNA. DR PIR; F64382; F64382. DR ProteinModelPortal; Q58076; -. DR STRING; 243232.MJ_0662; -. DR EnsemblBacteria; AAB98659; AAB98659; MJ_0662. DR KEGG; mja:MJ_0662; -. DR eggNOG; arCOG03951; Archaea. DR eggNOG; ENOG4111QDF; LUCA. DR InParanoid; Q58076; -. DR OMA; WGGLMWY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 1.20.144.10; -; 1. DR InterPro; IPR026841; Aur1/Ipt1. DR InterPro; IPR000326; P_Acid_Pase_2/haloperoxidase. DR Pfam; PF14378; PAP2_3; 1. DR SMART; SM00014; acidPPc; 1. DR SUPFAM; SSF48317; SSF48317; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 239 Uncharacterized protein MJ0662. FT /FTId=PRO_0000106979. FT TRANSMEM 9 29 Helical. {ECO:0000255}. FT TRANSMEM 65 85 Helical. {ECO:0000255}. FT TRANSMEM 94 114 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. SQ SEQUENCE 239 AA; 27769 MW; D66F091DB1B0AA61 CRC64; MDKRILVRLA IYPIAYVLWG GLMWYSQIIT PLDVTNLLLK LPLCNKEFYI FLQSLPNIVI EFFKIIYLYG FSSMIIGGIA YYLFIKRDFL KSDIILIDLA LGWLFAGLIY TFVVVKSPFQ VGVAKDLINM HYFWIFTKPT YEIPSLHTAY SFLLALHFKD EKPLNYIYFA LAILIPISTL IMGMHWIVDV ITGVLYGYII YKFPKTIHIK ISKALDFLAG HIKPCILCGK CKERETHEK // ID Y664_METJA Reviewed; 301 AA. AC Q58078; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0664; GN OrderedLocusNames=MJ0664; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98660.1; -; Genomic_DNA. DR PIR; H64382; H64382. DR ProteinModelPortal; Q58078; -. DR STRING; 243232.MJ_0664; -. DR EnsemblBacteria; AAB98660; AAB98660; MJ_0664. DR KEGG; mja:MJ_0664; -. DR eggNOG; arCOG05045; Archaea. DR eggNOG; COG0551; LUCA. DR OMA; ANRDYNW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005694; C:chromosome; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0003916; F:DNA topoisomerase activity; IEA:InterPro. DR GO; GO:0006265; P:DNA topological change; IEA:InterPro. DR InterPro; IPR013498; Topo_IA_Znf. DR Pfam; PF01396; zf-C4_Topoisom; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 301 Uncharacterized protein MJ0664. FT /FTId=PRO_0000106980. SQ SEQUENCE 301 AA; 35495 MW; CF1D742AB59F1CD2 CRC64; MKNLVLRRDN MGEVLNELFE ILSKDLHFNA TKLNSETYEQ NWKVPEGFIS IIGIENAKMP VFYYGITNSY KKEFEIKKVI SPKGQKQIFA RIYYIFDRRD IIEKEKYVVA NAFNGLLLLI KFDKTEFIEK AIEMLTKGYE EDNFIKEVLN NIKEKNMFDN IDETIRFVAN RDYNWLIGRI KYNMGILEYS GQGYYLIPIK TNMQITPGIK INNGRVIIDL ENSHLFKNFI VYVDTINNKI IYNKERLCNK NPAILDIMSK IDDNTCPWCG AKLRVVRTKK GEFLGCTNYP NCLYRRFPKK N // ID Y714_METJA Reviewed; 118 AA. AC Q58124; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0714; GN OrderedLocusNames=MJ0714; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0310 and MJ1340. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98709.1; -; Genomic_DNA. DR PIR; B64389; B64389. DR ProteinModelPortal; Q58124; -. DR STRING; 243232.MJ_0714; -. DR EnsemblBacteria; AAB98709; AAB98709; MJ_0714. DR KEGG; mja:MJ_0714; -. DR eggNOG; arCOG02603; Archaea. DR eggNOG; COG2018; LUCA. DR InParanoid; Q58124; -. DR KO; K07131; -. DR OMA; EYENGIM; -. DR PhylomeDB; Q58124; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR004942; Roadblock/LAMTOR2_dom. DR Pfam; PF03259; Robl_LC7; 1. DR SMART; SM00960; Robl_LC7; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 118 Uncharacterized protein MJ0714. FT /FTId=PRO_0000107000. SQ SEQUENCE 118 AA; 12345 MW; D6380D2D6E0CFD0E CRC64; MVESMIDRVL LELNRTDGVK GSMVVGKDGL VIASQLPGNV DAELVGAMAS AAFGAAERTS SEIGLSGLEQ TMIEGEHGKT LMVDAGEGIL VVLTDAKVNL GLIRITMKRA ADKIKAMF // ID Y718_METJA Reviewed; 402 AA. AC Q58128; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Putative uncharacterized transporter MJ0718; GN OrderedLocusNames=MJ0718; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the chromate ion transporter (CHR) CC (TC 2.A.51) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98712.1; -; Genomic_DNA. DR PIR; F64389; F64389. DR ProteinModelPortal; Q58128; -. DR STRING; 243232.MJ_0718; -. DR DNASU; 1451595; -. DR EnsemblBacteria; AAB98712; AAB98712; MJ_0718. DR KEGG; mja:MJ_0718; -. DR eggNOG; arCOG06434; Archaea. DR eggNOG; COG2059; LUCA. DR InParanoid; Q58128; -. DR KO; K07240; -. DR OMA; VMHRIIV; -. DR PhylomeDB; Q58128; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015109; F:chromate transmembrane transporter activity; IEA:InterPro. DR InterPro; IPR014047; Chr_Tranpt_l_chain. DR InterPro; IPR003370; Chromate_transpt. DR Pfam; PF02417; Chromate_transp; 2. DR PIRSF; PIRSF004810; ChrA; 1. DR TIGRFAMs; TIGR00937; 2A51; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 402 Putative uncharacterized transporter FT MJ0718. FT /FTId=PRO_0000107003. FT TRANSMEM 26 46 Helical. {ECO:0000255}. FT TRANSMEM 67 87 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. FT TRANSMEM 213 233 Helical. {ECO:0000255}. FT TRANSMEM 235 255 Helical. {ECO:0000255}. FT TRANSMEM 289 309 Helical. {ECO:0000255}. FT TRANSMEM 312 332 Helical. {ECO:0000255}. FT TRANSMEM 338 358 Helical. {ECO:0000255}. FT TRANSMEM 360 380 Helical. {ECO:0000255}. FT TRANSMEM 381 401 Helical. {ECO:0000255}. SQ SEQUENCE 402 AA; 45132 MW; A35EBADB62CF9C8B CRC64; MMMHPMNKTN KRDKMEKRNN PSALNIFMSF LKLGMVAFGG PTAIAYVREM VVDEKKWMDE KSFNNGVALA QIIPGASVMQ VAAYVGFYLR GIVGAFAAFM AYALPAFLIM LFLTIIYMHV KSLPKTVSIF EALRIIVVSL AANGTLNFSK KNIRTIGDVF LLLISALLFI LKFSPFIVIF VSIFIGFLMY RRDITKLSLK IDIPREKLRI YKYVAYLLFG VFLFNLILYM IDSKLFLLST LMMKVDVFAF GGGYGSVPFM LHEVVDKYNL MDAKTFMDGI ALGQITPGPI VITATFVGYI VGGFIGSIIS TISVFTPSFI ILLSSIPIFD SLKHNTIFKN ILHMILVSFV GLLVAVTIRF ALLVDWSIQA LIIFIVSFLL LYKKYNMLLV VLLSLVLGYL IL // ID Y719_METJA Reviewed; 600 AA. AC Q58129; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 104. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0719; GN OrderedLocusNames=MJ0719; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC -!- SIMILARITY: Contains 2 ABC transporter domains. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98713.1; -; Genomic_DNA. DR PIR; G64389; G64389. DR ProteinModelPortal; Q58129; -. DR SMR; Q58129; 13-597. DR STRING; 243232.MJ_0719; -. DR EnsemblBacteria; AAB98713; AAB98713; MJ_0719. DR KEGG; mja:MJ_0719; -. DR eggNOG; arCOG00187; Archaea. DR eggNOG; COG1245; LUCA. DR InParanoid; Q58129; -. DR KO; K06174; -. DR OMA; AYKPQYI; -. DR PhylomeDB; Q58129; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR013283; ABCE. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR007209; RNaseL-inhib_metal-bd_dom. DR PANTHER; PTHR19248; PTHR19248; 1. DR Pfam; PF00005; ABC_tran; 2. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF04068; RLI; 1. DR PRINTS; PR01868; ABCEFAMILY. DR SMART; SM00382; AAA; 2. DR SUPFAM; SSF52540; SSF52540; 2. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 2. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 2. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Repeat; Transport. FT CHAIN 1 600 Uncharacterized ABC transporter ATP- FT binding protein MJ0719. FT /FTId=PRO_0000093220. FT DOMAIN 14 44 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 53 82 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 77 318 ABC transporter 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT DOMAIN 348 563 ABC transporter 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 117 124 ATP 1. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 380 387 ATP 2. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. SQ SEQUENCE 600 AA; 68019 MW; 07BC8DF6107B354C CRC64; MKLGFYLLGG DFMRLAIIDY DRCQPKKCSM ECMKYCPGVR MGEKTIEIDE NTGKPVISEV LCSGCGICVK RCPFKAISII GLPEELSEDK IVHSYGQNRF KLFGLVIPRD GVVGIIGQNG IGKSTVLRIL AGELIPNLGK HDKEPNYDDV IKYFRGTELQ EYFEKLKNKG VKAIHKVQYV DILPKVVKGK VGDLLKKVDE KGKFDEVVEK LELKNILDRE LSQLSGGELQ RVAIAAAYLR NGDIYFFDEP SSWLDIRQRF NAARLIRELN KVVVVEHDLI VLDYLSDYIH IMYGVPSAYG IVSMPKSVRV GINEYLYGEL REENIRFRKE PIIFEKRAVI DFKNRPILLS YSSMKKTLGD FKLEVSGGTI YKGEVIGILG PNGIGKTTFV KLLAGVIKPD EGEVIKEGDI KVSYKPQYIT PDYDGTVEDL LSSITNIHTS YYKSEIINPL QLEKLLDREV RELSGGELQR VAIAACLSRD ADIYLLDEPS AFLDVEQRLR VSKVIRRIAD EKEAGMFVVD HDILFQDYIS DRFIVFSGEP GKFGVGSSPM NKRDGANKFL KEMQITFRRD PETGRPRANK EGSQRDIMQK EKGEYYYVDE // ID Y752_METJA Reviewed; 76 AA. AC Q58162; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0752; GN OrderedLocusNames=MJ0752; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0857 N-terminal region. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98754.1; -; Genomic_DNA. DR PIR; H64393; H64393. DR STRING; 243232.MJ_0752; -. DR EnsemblBacteria; AAB98754; AAB98754; MJ_0752. DR KEGG; mja:MJ_0752; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR KO; K07496; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 76 Uncharacterized protein MJ0752. FT /FTId=PRO_0000107014. SQ SEQUENCE 76 AA; 9186 MW; ABDC436ED6ECC4F8 CRC64; MMEVIKAIEF KYYSDVVELI YDFKEMVNFC IDKAMELGIT SYAKLRKAIY NEWKEKWYPK YHTHYCHSAC RVATSI // ID Y754_METJA Reviewed; 185 AA. AC Q58164; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0754; GN OrderedLocusNames=MJ0754; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98756.1; -; Genomic_DNA. DR PIR; B64394; B64394. DR PDB; 3Q4N; X-ray; 2.88 A; A/B=1-185. DR PDB; 3Q4O; X-ray; 1.34 A; A=11-185. DR PDB; 3Q4Q; X-ray; 1.75 A; A=11-185. DR PDB; 3Q4R; X-ray; 1.60 A; A=11-185. DR PDBsum; 3Q4N; -. DR PDBsum; 3Q4O; -. DR PDBsum; 3Q4Q; -. DR PDBsum; 3Q4R; -. DR ProteinModelPortal; Q58164; -. DR STRING; 243232.MJ_0754; -. DR DNASU; 1451631; -. DR EnsemblBacteria; AAB98756; AAB98756; MJ_0754. DR KEGG; mja:MJ_0754; -. DR eggNOG; arCOG03957; Archaea. DR eggNOG; COG4902; LUCA. DR InParanoid; Q58164; -. DR OMA; YITSAYF; -. DR PhylomeDB; Q58164; -. DR EvolutionaryTrace; Q58164; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.20.1260.10; -; 1. DR InterPro; IPR019243; DUF2202. DR InterPro; IPR009078; Ferritin-like_SF. DR InterPro; IPR012347; Ferritin-rel. DR Pfam; PF09968; DUF2202; 1. DR SUPFAM; SSF47240; SSF47240; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 185 Uncharacterized protein MJ0754. FT /FTId=PRO_0000107015. FT HELIX 15 42 {ECO:0000244|PDB:3Q4O}. FT HELIX 45 67 {ECO:0000244|PDB:3Q4O}. FT HELIX 85 98 {ECO:0000244|PDB:3Q4O}. FT HELIX 102 124 {ECO:0000244|PDB:3Q4O}. FT HELIX 130 156 {ECO:0000244|PDB:3Q4O}. FT STRAND 164 166 {ECO:0000244|PDB:3Q4O}. FT HELIX 168 175 {ECO:0000244|PDB:3Q4O}. SQ SEQUENCE 185 AA; 21766 MW; 2CE5EC9D424895F6 CRC64; MLEYISSLPK QPISEEEKEG LIEMREEEKL ARDVYLTLYN KWKLQIFKNI AESEQTHMDA VKYLLEKYNI PDPVKNDSIG VFSNPKFEEL YKKLVEKGDK SEVDALKVGA TIEDLDIADL EKWINKTDNE DIKFVYENLM KGSRNHMRAF VRMLNNYGSN YTPQYISKEE YEEIISSSTE RGMNR // ID Y758_METJA Reviewed; 159 AA. AC Q58168; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0758; GN OrderedLocusNames=MJ0758; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98758.1; -; Genomic_DNA. DR PIR; F64394; F64394. DR ProteinModelPortal; Q58168; -. DR STRING; 243232.MJ_0758; -. DR EnsemblBacteria; AAB98758; AAB98758; MJ_0758. DR KEGG; mja:MJ_0758; -. DR eggNOG; arCOG08262; Archaea. DR eggNOG; ENOG4112CCR; LUCA. DR OMA; CPFMYLL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 159 Uncharacterized protein MJ0758. FT /FTId=PRO_0000107017. SQ SEQUENCE 159 AA; 18245 MW; 99ABB8A49BBD2F56 CRC64; MVCSRGIFGI DIMNKKGIDS LFVSALYYSI NKAIYDVMGD GGKVLGRRAS YEMIKLLKDL GFIKENMSNE EIKNLFVNTF GLSEDLNIVE EDKKVIFEVI NPTLDLFLKK LMEENLKPYV CPFMYLLSEI YSVSNNCRLM LSDVVPETEE KVKLIFKKV // ID Y762_METJA Reviewed; 342 AA. AC Q58172; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized transporter MJ0762; GN OrderedLocusNames=MJ0762; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the tellurite-resistance/dicarboxylate CC transporter (TDT) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98753.1; -; Genomic_DNA. DR PIR; B64395; B64395. DR ProteinModelPortal; Q58172; -. DR STRING; 243232.MJ_0762; -. DR TCDB; 2.A.16.4.4; the telurite-resistance/dicarboxylate transporter (tdt) family. DR EnsemblBacteria; AAB98753; AAB98753; MJ_0762. DR KEGG; mja:MJ_0762; -. DR eggNOG; arCOG04355; Archaea. DR eggNOG; COG1275; LUCA. DR InParanoid; Q58172; -. DR OMA; PAFVGCS; -. DR PhylomeDB; Q58172; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR011552; TehA/Mae1. DR InterPro; IPR004695; Voltage-dep_anion_channel. DR Pfam; PF03595; SLAC1; 1. DR TIGRFAMs; TIGR00816; tdt; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 342 Uncharacterized transporter MJ0762. FT /FTId=PRO_0000107020. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 39 59 Helical. {ECO:0000255}. FT TRANSMEM 79 99 Helical. {ECO:0000255}. FT TRANSMEM 108 128 Helical. {ECO:0000255}. FT TRANSMEM 142 162 Helical. {ECO:0000255}. FT TRANSMEM 175 195 Helical. {ECO:0000255}. FT TRANSMEM 207 227 Helical. {ECO:0000255}. FT TRANSMEM 242 262 Helical. {ECO:0000255}. FT TRANSMEM 276 296 Helical. {ECO:0000255}. FT TRANSMEM 304 324 Helical. {ECO:0000255}. SQ SEQUENCE 342 AA; 39535 MW; 08EFEC3E2C4955D8 CRC64; MQSYIKNFES SWFAAVMGTG VLAVTSLFYS EYLPILKDIS FLLFYFNILL FFVFLMLWIL RWVKYPKNMI AELKHPVLSS FSPTVAVAML VLGIDFILIK NNLFLGKIFW VFGAIGMFLF SLIVPFYMFK SESIKLDHVN PGWYIPPVGL IVIPIAGSLI MPHLTGVWHE LTVLINYFGW GAGFFLYLAL LAVVIYRFIL HHPLPSAMAP TVWINLGPIG AGIVALINMV NNSPFITIKE PFYIFSFIFW GFGLWWSLMA IIMTLYYVKK LKLPYAMSWW AFIFPLGVYI ASTHLVYKIF GFEIVDYIGF GLYWLLFFFW IVTLIKTINK VYSGELFKDK IN // ID Y770_METJA Reviewed; 223 AA. AC Q58180; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0770; GN OrderedLocusNames=MJ0770; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98775.1; -; Genomic_DNA. DR PIR; B64396; B64396. DR ProteinModelPortal; Q58180; -. DR STRING; 243232.MJ_0770; -. DR EnsemblBacteria; AAB98775; AAB98775; MJ_0770. DR KEGG; mja:MJ_0770; -. DR eggNOG; arCOG06578; Archaea. DR eggNOG; COG0582; LUCA. DR InParanoid; Q58180; -. DR OMA; HYGINTH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0015074; P:DNA integration; IEA:InterPro. DR GO; GO:0006310; P:DNA recombination; IEA:InterPro. DR Gene3D; 1.10.443.10; -; 1. DR InterPro; IPR011010; DNA_brk_join_enz. DR InterPro; IPR013762; Integrase-like_cat. DR InterPro; IPR002104; Integrase_catalytic. DR Pfam; PF00589; Phage_integrase; 1. DR SUPFAM; SSF56349; SSF56349; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 223 Uncharacterized protein MJ0770. FT /FTId=PRO_0000107025. SQ SEQUENCE 223 AA; 26733 MW; 739C8CE50FF67B5B CRC64; MMIWDWNLSK PSESIKKHSG TWDKGIDYKQ TYKMFKEDLQ KLKNKELLYE DDYKRIAYLI TFLFQLRNGC RIWEAIAGMI NIAINIDNLN WNERITVKVR TQKRKDWEFR ELIIPKCIKK EDIEMVRDVF LDIKKEIDEK LTMDEKLKAK KKIVKRFGAW LYKNYGINTH SLRYAYVTYL GEHGIPAQVL AKITKHKNIN YIETYTQSRL AKEILKNIGD LDD // ID Y772_METJA Reviewed; 353 AA. AC Q58182; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 09-DEC-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0772; GN OrderedLocusNames=MJ0772; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98776.1; -; Genomic_DNA. DR PIR; D64396; D64396. DR ProteinModelPortal; Q58182; -. DR STRING; 243232.MJ_0772; -. DR EnsemblBacteria; AAB98776; AAB98776; MJ_0772. DR KEGG; mja:MJ_0772; -. DR eggNOG; arCOG05049; Archaea. DR eggNOG; ENOG410YBNG; LUCA. DR OMA; YRAKKAW; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 353 Uncharacterized protein MJ0772. FT /FTId=PRO_0000107026. SQ SEQUENCE 353 AA; 42478 MW; 06843C680B4EA752 CRC64; MKIIKAVPEE FLNGLYLIPT DRGNLLELDE NGNFEVVNNI AIIRVLATPN LKKAIAKIVY QIKDKYYLFK NHKKANWLKN LLEYMNNKIE FDKYYRAKKA WYRGIGDLFR NIRKWEFEKV VGKIISLLKV LNPIVVFDVH DIRKWHYRKS FINFVKELRK NSISVVIRYP IDCHEEIREI FPEGILNTKA TIRYFAKVHG YYISDRVAEY LLKITNGNLE TIYLILRHSK REIKNLRELK IPWLRILPYI VDSKYRKLVE VIIELRKFKV EDITYKVNYK LSTIYRYLDE LVELGILTKI KHKGKVRFKI RLNRNILLTL LKKSKNNYLH WFSIFLLDSI PWDIQIFEFS KSI // ID Y774_METJA Reviewed; 409 AA. AC Q58184; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 100. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0774; GN OrderedLocusNames=MJ0774; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH arsR-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00340}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98778.1; -; Genomic_DNA. DR PIR; F64396; F64396. DR ProteinModelPortal; Q58184; -. DR STRING; 243232.MJ_0774; -. DR EnsemblBacteria; AAB98778; AAB98778; MJ_0774. DR KEGG; mja:MJ_0774; -. DR eggNOG; arCOG00472; Archaea. DR eggNOG; COG0640; LUCA. DR InParanoid; Q58184; -. DR OMA; MTCSESI; -. DR PhylomeDB; Q58184; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0003700; F:transcription factor activity, sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR001845; HTH_ArsR_DNA-bd_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01022; HTH_5; 1. DR SMART; SM00382; AAA; 1. DR SMART; SM00418; HTH_ARSR; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS50987; HTH_ARSR_2; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 409 Uncharacterized HTH-type transcriptional FT regulator MJ0774. FT /FTId=PRO_0000160633. FT DOMAIN 305 409 HTH arsR-type. {ECO:0000255|PROSITE- FT ProRule:PRU00340}. SQ SEQUENCE 409 AA; 46329 MW; 34AF708F87D7BE43 CRC64; MDPIEFIQKS ASSIASTMHK LKLKYNPFSE KPIRGNTKFF VGRVSELREI GEILGSALHG SVANAAIVGT KGIGKSSMLN IIYYATKKQG HWVVEMTASQ VTPRQFLIQL LYNILTENII TMSGTIKSDY MEHSSRILDM YRKLNNYGDK VPIHYPRERI ERDLEYLINE VKSPDKLCII LIDEADQFAK KSCLSLLQFF HSFLYEEGIL TFMAGSPTLM DDLTKISPPI KDRIPKIINM PPLSKDESYD LIRRRLEDAH IDGAEEFEPF TEEAIHKIVE ECDGIPRKII MTCSESISIA IRKGLTKIDE KVVKEAMHSL GISVGHQILN HLTPAQSEIV RAMAELGGSA TVTQLAEYLK KSPSTIGTHL SDIYEMGYIY KEREGNNVYY KLSKELRDVL IGEDDELEM // ID Y788_METJA Reviewed; 79 AA. AC Q58198; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 59. DE RecName: Full=Uncharacterized protein MJ0788; GN OrderedLocusNames=MJ0788; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98787.1; -; Genomic_DNA. DR PIR; D64398; D64398. DR ProteinModelPortal; Q58198; -. DR STRING; 243232.MJ_0788; -. DR EnsemblBacteria; AAB98787; AAB98787; MJ_0788. DR KEGG; mja:MJ_0788; -. DR eggNOG; arCOG06614; Archaea. DR eggNOG; ENOG410YY6V; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 79 Uncharacterized protein MJ0788. FT /FTId=PRO_0000107039. FT COMPBIAS 33 47 Glu-rich. SQ SEQUENCE 79 AA; 9582 MW; 5DDF8E58CDAF1865 CRC64; MVKLMDIDEF LNYLSNATKE NFKKTKHFEI RIELREDNIP NEEELFEILT KNKPVGILKQ KDDKFLRYIM SLMKNMMLL // ID Y793_METJA Reviewed; 178 AA. AC Q58203; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 86. DE RecName: Full=Uncharacterized protein MJ0793; GN OrderedLocusNames=MJ0793; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0706 and Synechocystis PCC 6803 CC slr1478. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98796.1; -; Genomic_DNA. DR PIR; A64399; A64399. DR ProteinModelPortal; Q58203; -. DR STRING; 243232.MJ_0793; -. DR DNASU; 1451673; -. DR EnsemblBacteria; AAB98796; AAB98796; MJ_0793. DR KEGG; mja:MJ_0793; -. DR eggNOG; arCOG01996; Archaea. DR eggNOG; COG1300; LUCA. DR InParanoid; Q58203; -. DR OMA; IFEIAAF; -. DR PhylomeDB; Q58203; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002798; SpoIIM-like. DR Pfam; PF01944; SpoIIM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 178 Uncharacterized protein MJ0793. FT /FTId=PRO_0000107044. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 101 121 Helical. {ECO:0000255}. FT TRANSMEM 150 170 Helical. {ECO:0000255}. SQ SEQUENCE 178 AA; 19804 MW; 95B9049D585D12AA CRC64; MKIPIILTLM LFSLGFIFGF ISINNLSKIN DKDLSNYIPN IQFNFPSILT NNLKVIFLML AGSITFGLST FINLIFNGFN VGVLIGSISL TNEPLKLITA LILPHGIFEI SAMLISAVAG FKIPYKVTLY LLDKKEKPLT EEDIKDFLKL SLISIILIVI AAFIEVYITP KIATYLLT // ID Y799_METJA Reviewed; 296 AA. AC Q58209; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0799; GN OrderedLocusNames=MJ0799; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To Synechocystis PCC 6803 sll0787 and M.jannaschii CC MJ0640. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98794.1; -; Genomic_DNA. DR PIR; G64399; G64399. DR ProteinModelPortal; Q58209; -. DR STRING; 243232.MJ_0799; -. DR EnsemblBacteria; AAB98794; AAB98794; MJ_0799. DR KEGG; mja:MJ_0799; -. DR eggNOG; arCOG00642; Archaea. DR eggNOG; COG2144; LUCA. DR KO; K07123; -. DR OMA; NMEGPYP; -. DR PhylomeDB; Q58209; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0009030; F:thiamine-phosphate kinase activity; IEA:InterPro. DR GO; GO:0009228; P:thiamine biosynthetic process; IEA:InterPro. DR Gene3D; 3.30.1330.10; -; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR016188; PurM-like_N. DR InterPro; IPR006283; ThiL. DR InterPro; IPR011414; UCP036541_AIR. DR PANTHER; PTHR30270; PTHR30270; 1. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF036541; UCP036541_AIR; 1. DR SUPFAM; SSF56042; SSF56042; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 296 Uncharacterized protein MJ0799. FT /FTId=PRO_0000107050. SQ SEQUENCE 296 AA; 33054 MW; 7590A47A898F0B22 CRC64; MKMENFEYEL KMAIEHILET NYPRKAFWHF DDLIDDLKSG IKAGDDAVVI KNMVINMEGP YPLKLGAKTA LIHTACDVVA MGAEPKFALN AIQAKNEDEI KLAVDGLRKQ SIGLNIPIIG GNTQTVEELK SCISVAVFGE LIDENLIIKD GGAKDGDLLI MLGDPVEGDV GERIYKAKKK FDTYLEILEN GIKINACKDA SRGGWLGNLL EMLIKAKKGA EIKSLPYPRA TRYLGTYIIA VPEEEYEKVV DIALKNKCPV VLFGRILEKP KLIIGTKEYI SENKMLELIK KFPYKY // ID Y79A_METJA Reviewed; 162 AA. AC P81313; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0792.1; GN OrderedLocusNames=MJ0792.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98800.1; -; Genomic_DNA. DR ProteinModelPortal; P81313; -. DR STRING; 243232.MJ_0792.1; -. DR EnsemblBacteria; AAB98800; AAB98800; MJ_0792.1. DR KEGG; mja:MJ_0792.1; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 162 Uncharacterized protein MJ0792.1. FT /FTId=PRO_0000107043. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 50 70 Helical. {ECO:0000255}. FT TRANSMEM 96 116 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. SQ SEQUENCE 162 AA; 18866 MW; 4057E5A837BEB01C CRC64; MNFEKKLNGI LSFTYLALVL CLVMPFMLIL VLDTTFTFNK FNLNFVYRQI VELIVLSIFA GFITSFALYN KICRISTEEL KRDILENNGL KTIFKIAQYE VMVSIFYSLL LLIILLNKQL LYYGFTAIFQ IFFTFCAIFV PLFIFGSLVC RTILLHKIRG TT // ID Y804_METJA Reviewed; 286 AA. AC Q58214; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0804; GN OrderedLocusNames=MJ0804; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98804.1; -; Genomic_DNA. DR PIR; D64400; D64400. DR ProteinModelPortal; Q58214; -. DR STRING; 243232.MJ_0804; -. DR EnsemblBacteria; AAB98804; AAB98804; MJ_0804. DR KEGG; mja:MJ_0804; -. DR eggNOG; arCOG00955; Archaea. DR eggNOG; COG0535; LUCA. DR InParanoid; Q58214; -. DR OMA; CIFCYSN; -. DR PhylomeDB; Q58214; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR004154; Anticodon-bd. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00729; Elp3; 1. DR SUPFAM; SSF52954; SSF52954; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 286 Uncharacterized protein MJ0804. FT /FTId=PRO_0000107054. FT METAL 50 50 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 54 54 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 57 57 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 286 AA; 32920 MW; CACC47C3A3B4E63A CRC64; MIVLRNEICD KLENIAKILK FVRHCIGCEG INLEIENPQH HPSIELTQKC NLNCIYCYSR LKTVKRGIYG NLEEAETVTI SQYGEPLLDL EGVKKAIEFC KDLGLRVDLQ TNGTLLNEEI IKELKDLGLD LIMISLSSFS REKYKLLTGK DYFNRVLNNI KIASKYLHTI VRSIYIPGFN DNELLNLAKE LNNYADEIMV HQLISYKENE NLLKNAGIDL NNLGRIRDLL LIVDEMQKNA PKINVTIKGC LLVQLKEMDG FILNNITYDV FSEVPDIKRE HRPLPW // ID Y812_METJA Reviewed; 373 AA. AC Q58222; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0812; GN OrderedLocusNames=MJ0812; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98811.1; -; Genomic_DNA. DR PIR; D64401; D64401. DR ProteinModelPortal; Q58222; -. DR STRING; 243232.MJ_0812; -. DR EnsemblBacteria; AAB98811; AAB98811; MJ_0812. DR KEGG; mja:MJ_0812; -. DR eggNOG; arCOG00436; Archaea. DR eggNOG; COG0714; LUCA. DR InParanoid; Q58222; -. DR KO; K03924; -. DR OMA; TRFTEPD; -. DR PhylomeDB; Q58222; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011704; ATPase_dyneun-rel_AAA. DR InterPro; IPR001270; ClpA/B. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF07728; AAA_5; 1. DR PRINTS; PR00300; CLPPROTEASEA. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 373 Uncharacterized protein MJ0812. FT /FTId=PRO_0000107060. SQ SEQUENCE 373 AA; 43183 MW; D7168B1717DDB6AD CRC64; MLEKIREELN SYFLERREEI DIALTSILAN EHTVFLGNPG VAKSQLIRAI ASHINANYFE KLITRFTTED ELFGPLSIKE LKDNDRFVRK TSGYLPTAEI AFLDEVFKAN SSILNALLSI INERIYHNGD RIEKVPLISL FGASNELPEE NELLAFYDRF LFRKVVRGIR SYENLSKLID LEEEYKPKTI IDVEDVKKMQ NEALKVDISN IKDDLIKIKL SLESEGIRIS DRRFKKSVKA VKCFAYLNGK EKADENDLDI LRHIYWNEPD EFYKVSVEIF KISNHFAGFA LEQREILDSL MNEIKKINKD RIKLGGIEYR KCLEILGKLN SMSITLKDVK NKAIEANKPY ELVEDVLKEV EGFKKYVEGL LKG // ID Y818_METJA Reviewed; 203 AA. AC Q58228; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0818; GN OrderedLocusNames=MJ0818; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98819.1; -; Genomic_DNA. DR PIR; B64402; B64402. DR ProteinModelPortal; Q58228; -. DR STRING; 243232.MJ_0818; -. DR EnsemblBacteria; AAB98819; AAB98819; MJ_0818. DR KEGG; mja:MJ_0818; -. DR eggNOG; arCOG05052; Archaea. DR eggNOG; COG4085; LUCA. DR KO; K06931; -. DR OMA; SYCEKRD; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0008168; F:methyltransferase activity; IEA:InterPro. DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro. DR GO; GO:0006281; P:DNA repair; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 2.40.50.140; -; 1. DR Gene3D; 3.40.10.10; -; 1. DR InterPro; IPR004026; Ada_DNA_repair_Zn-bd. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR004365; NA-bd_OB_tRNA. DR InterPro; IPR016798; UCP021980_OB-fold. DR Pfam; PF01336; tRNA_anti-codon; 1. DR PIRSF; PIRSF021980; UCP021980_RNA-bd; 1. DR SUPFAM; SSF50249; SSF50249; 1. DR SUPFAM; SSF57884; SSF57884; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 203 Uncharacterized protein MJ0818. FT /FTId=PRO_0000107062. SQ SEQUENCE 203 AA; 23754 MW; 4715370D01BB0A9E CRC64; MKLTEKNITL FALTCFVIIS TTWLFLNPIQ PKEKHIAEIK EGDYVVIKGY IQEMYVKRDK YRHVINISRI VINDGTGNLD VVAFGKTREE LLTYILSYNP MIKEGDYIEV KGRVTLYKGK YEIILNNIKD FKLLKKNNFE RDIYLSPTPT GIYASKYGKK YHTSKNCPYG KRLKEENIIY FYSEDDAKAL GYEKCKWCEE HGG // ID Y857_METJA Reviewed; 274 AA. AC Q58267; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0857; GN OrderedLocusNames=MJ0857; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98863.1; -; Genomic_DNA. DR PIR; A64407; A64407. DR STRING; 243232.MJ_0857; -. DR EnsemblBacteria; AAB98863; AAB98863; MJ_0857. DR KEGG; mja:MJ_0857; -. DR eggNOG; arCOG00679; Archaea. DR eggNOG; COG0675; LUCA. DR InParanoid; Q58267; -. DR KO; K07496; -. DR OMA; VRIATHR; -. DR PhylomeDB; Q58267; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 274 Uncharacterized protein MJ0857. FT /FTId=PRO_0000107082. SQ SEQUENCE 274 AA; 31704 MW; 7C0149CC545F597E CRC64; MPKTIKLTKT IALKSKPLTK TKIKIIENTI ESYKEVLSIA LDFGLKNNRK SHRKIREGIY EEIKSKLPKL PTHYIYTASQ DASTRIKSFI AMKKRDKAYT SKPKIKNISL WLDDVLTNYR DFKNNIEKLF LIDKEGKKTL HLRLSTPNGR IVIPLKPHKQ FFKLLNEGWG IKAGFKLRLN KEDGTITVLI PLEKEITIND SYKTVYALDF NLDNITYGNF ENIELIKTDL GKLTEKYSNI MTNIQEKFSF KGIHKQDKPL KRKGFILLKN SVGG // ID Y882_METJA Reviewed; 197 AA. AC Q58292; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 94. DE RecName: Full=Probable S-adenosylmethionine-dependent methyltransferase MJ0882; DE EC=2.1.1.-; GN OrderedLocusNames=MJ0882; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS) OF 4-197, AND RP S-ADENOSYLMETHIONINE BINDING. RX PubMed=12836702; DOI=10.1023/A:1021279113558; RA Huang L., Hung L., Odell M., Yokota H., Kim R., Kim S.H.; RT "Structure-based experimental confirmation of biochemical function to RT a methyltransferase, MJ0882, from hyperthermophile Methanococcus RT jannaschii."; RL J. Struct. Funct. Genomics 2:121-127(2002). CC -!- FUNCTION: Probable methyltransferase that uses S- CC adenosylmethionine as the methyl donor. Binds neither NAD nor NADP CC in vitro. CC -!- SIMILARITY: Belongs to the methyltransferase superfamily. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98886.1; -; Genomic_DNA. DR PIR; B64410; B64410. DR PDB; 1DUS; X-ray; 1.80 A; A=4-197. DR PDBsum; 1DUS; -. DR ProteinModelPortal; Q58292; -. DR SMR; Q58292; 4-197. DR STRING; 243232.MJ_0882; -. DR EnsemblBacteria; AAB98886; AAB98886; MJ_0882. DR KEGG; mja:MJ_0882; -. DR eggNOG; arCOG00110; Archaea. DR eggNOG; COG2813; LUCA. DR InParanoid; Q58292; -. DR OMA; ITNPPIR; -. DR PhylomeDB; Q58292; -. DR EvolutionaryTrace; Q58292; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008168; F:methyltransferase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Methyltransferase; KW Reference proteome; S-adenosyl-L-methionine; Transferase. FT CHAIN 1 197 Probable S-adenosylmethionine-dependent FT methyltransferase MJ0882. FT /FTId=PRO_0000157176. FT REGION 63 67 S-adenosyl-L-methionine binding. FT {ECO:0000305}. FT REGION 129 132 Substrate binding. {ECO:0000250}. FT BINDING 84 84 S-adenosyl-L-methionine. {ECO:0000305}. FT BINDING 129 129 S-adenosyl-L-methionine. {ECO:0000305}. FT STRAND 14 21 {ECO:0000244|PDB:1DUS}. FT STRAND 24 31 {ECO:0000244|PDB:1DUS}. FT TURN 35 38 {ECO:0000244|PDB:1DUS}. FT HELIX 42 50 {ECO:0000244|PDB:1DUS}. FT STRAND 58 62 {ECO:0000244|PDB:1DUS}. FT HELIX 68 73 {ECO:0000244|PDB:1DUS}. FT HELIX 74 76 {ECO:0000244|PDB:1DUS}. FT STRAND 77 85 {ECO:0000244|PDB:1DUS}. FT HELIX 87 99 {ECO:0000244|PDB:1DUS}. FT STRAND 107 111 {ECO:0000244|PDB:1DUS}. FT TURN 114 117 {ECO:0000244|PDB:1DUS}. FT STRAND 123 128 {ECO:0000244|PDB:1DUS}. FT HELIX 136 149 {ECO:0000244|PDB:1DUS}. FT STRAND 150 162 {ECO:0000244|PDB:1DUS}. FT HELIX 164 177 {ECO:0000244|PDB:1DUS}. FT STRAND 181 186 {ECO:0000244|PDB:1DUS}. FT STRAND 189 195 {ECO:0000244|PDB:1DUS}. SQ SEQUENCE 197 AA; 22244 MW; F4E108E500ABEB28 CRC64; MHYFSEKPTT KSDVKIVEDI LRGKKLKFKT DSGVFSYGKV DKGTKILVEN VVVDKDDDIL DLGCGYGVIG IALADEVKST TMADINRRAI KLAKENIKLN NLDNYDIRVV HSDLYENVKD RKYNKIITNP PIRAGKEVLH RIIEEGKELL KDNGEIWVVI QTKQGAKSLA KYMKDVFGNV ETVTIKGGYR VLKSKKL // ID Y920_METJA Reviewed; 185 AA. AC Q58330; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ0920; GN OrderedLocusNames=MJ0920; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 G (guanine nucleotide-binding) domain. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98924.1; -; Genomic_DNA. DR PIR; H64414; H64414. DR ProteinModelPortal; Q58330; -. DR STRING; 243232.MJ_0920; -. DR EnsemblBacteria; AAB98924; AAB98924; MJ_0920. DR KEGG; mja:MJ_0920; -. DR eggNOG; arCOG00354; Archaea. DR eggNOG; COG1100; LUCA. DR InParanoid; Q58330; -. DR KO; K06883; -. DR OMA; VGGTTKM; -. DR PhylomeDB; Q58330; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005525; F:GTP binding; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR006073; GTP_binding_domain. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR005225; Small_GTP-bd_dom. DR Pfam; PF01926; MMR_HSR1; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR00231; small_GTP; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 185 Uncharacterized protein MJ0920. FT /FTId=PRO_0000107105. FT DOMAIN 17 137 G. SQ SEQUENCE 185 AA; 21241 MW; AD53E72ED4DB1FAE CRC64; MQDKEFKIAI IGPENAGKSS IMNALFGKYV SLVSEVGGTT KMPIKRYWGK LKIGRIKEEP EFVNLVFVDL GGLYTTTDKQ SPIMTPKVLE KTFEEINDSD MIIHVIDGSV GLLRSFERLH HLLKFRYQKP IIVVINKCDL LNDSDKEHLK NYVERRIKNT PIFVSAKTFE GIPELLDIII KYLKR // ID Y928_METJA Reviewed; 197 AA. AC Q58338; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 93. DE RecName: Full=Putative protein methyltransferase MJ0928; DE AltName: Full=M.MjaHemkP; GN OrderedLocusNames=MJ0928; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Putative protein methyltransferase using S-adenosyl-L- CC methionine as the methyl donor. May methylate a Gln residue in CC target proteins (By similarity). {ECO:0000250}. CC -!- SIMILARITY: Belongs to the eukaryotic/archaeal PrmC-related CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98930.1; -; Genomic_DNA. DR PIR; H64415; H64415. DR ProteinModelPortal; Q58338; -. DR STRING; 243232.MJ_0928; -. DR EnsemblBacteria; AAB98930; AAB98930; MJ_0928. DR KEGG; mja:MJ_0928; -. DR eggNOG; arCOG00109; Archaea. DR eggNOG; COG2890; LUCA. DR InParanoid; Q58338; -. DR KO; K02493; -. DR OMA; EWDDWME; -. DR PhylomeDB; Q58338; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003676; F:nucleic acid binding; IEA:InterPro. DR GO; GO:0008276; F:protein methyltransferase activity; IEA:InterPro. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR002052; DNA_methylase_N6_adenine_CS. DR InterPro; IPR004557; PrmC-related. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR007848; Small_mtfrase_dom. DR Pfam; PF05175; MTS; 1. DR SUPFAM; SSF53335; SSF53335; 1. DR TIGRFAMs; TIGR00537; hemK_rel_arch; 1. DR PROSITE; PS00092; N6_MTASE; 1. PE 3: Inferred from homology; KW Complete proteome; Methyltransferase; Reference proteome; KW S-adenosyl-L-methionine; Transferase. FT CHAIN 1 197 Putative protein methyltransferase FT MJ0928. FT /FTId=PRO_0000157177. FT REGION 42 46 S-adenosyl-L-methionine binding. FT {ECO:0000250}. FT REGION 105 108 Substrate binding. {ECO:0000250}. FT BINDING 64 64 S-adenosyl-L-methionine. {ECO:0000250}. FT BINDING 105 105 S-adenosyl-L-methionine. {ECO:0000250}. SQ SEQUENCE 197 AA; 22057 MW; 2AE2377FE86EB217 CRC64; MIIEIEGIKL KLHPEVYEPA EDSILLLKNL VDVKNKDVLE IGVGTGLISI ACAKKGAKKI VGVDINPYAV KLAKENAKLN NVNISFFESD LFENVTGKFD VILFNPPYLP TSEDEKIDSY LNFAFDGGKD GREILDRFIY ELPNYLKKGG VVQILQSSLT GEKETINKLK PLGFKVEISA RLKVPFEELM VINAWRL // ID Y944_METJA Reviewed; 120 AA. AC Q58354; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0944; GN OrderedLocusNames=MJ0944; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0361. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98954.1; -; Genomic_DNA. DR PIR; H64417; H64417. DR ProteinModelPortal; Q58354; -. DR STRING; 243232.MJ_0944; -. DR EnsemblBacteria; AAB98954; AAB98954; MJ_0944. DR KEGG; mja:MJ_0944; -. DR eggNOG; arCOG01057; Archaea. DR eggNOG; COG1733; LUCA. DR InParanoid; Q58354; -. DR OMA; HNIINAK; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR005149; Tscrpt_reg_PadR_N. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF03551; PadR; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 120 Uncharacterized protein MJ0944. FT /FTId=PRO_0000107115. SQ SEQUENCE 120 AA; 13862 MW; 3219CC06451A7B49 CRC64; MLIGILSKKY VKEILELLNE KGELHFSQIH KEIPTHMSSL NRTLNELVKL GLISKRKEDN KQALPKTYYK LTPLGKKALL LYEVEKIIEN SKNNQNIIIQ IINGKNHNII NAKIVNIHNK // ID Y948_METJA Reviewed; 191 AA. AC Q58358; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0948; GN OrderedLocusNames=MJ0948; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98956.1; -; Genomic_DNA. DR PIR; D64418; D64418. DR ProteinModelPortal; Q58358; -. DR STRING; 243232.MJ_0948; -. DR EnsemblBacteria; AAB98956; AAB98956; MJ_0948. DR KEGG; mja:MJ_0948; -. DR eggNOG; arCOG08286; Archaea. DR eggNOG; ENOG41110P3; LUCA. DR OMA; KKTCMEL; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 191 Uncharacterized protein MJ0948. FT /FTId=PRO_0000107117. SQ SEQUENCE 191 AA; 22423 MW; 8D75231083FDB216 CRC64; MIFMKNSTEY PTLVEIKDKK GEMIEKGEAK LRDLNNIRVK LNELRTSNPD DLDTIAQLEE EESHLTSEVL KLDLSIKILE VVEYIIESNI FEDYWKIIEE KIPYEELLNI VVENGLSIKK TCMELYKLAN IDDKNILKKI QNLPDDYPKE TKEDPNLQNK YLSKIISRIS RLKEFKSNLD EIVSDIISNM R // ID Y964_METJA Reviewed; 680 AA. AC Q58374; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ0964; GN OrderedLocusNames=MJ0964; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98966.1; -; Genomic_DNA. DR PIR; D64420; D64420. DR ProteinModelPortal; Q58374; -. DR STRING; 243232.MJ_0964; -. DR EnsemblBacteria; AAB98966; AAB98966; MJ_0964. DR KEGG; mja:MJ_0964; -. DR eggNOG; ENOG4102T9U; Archaea. DR eggNOG; COG0145; LUCA. DR InParanoid; Q58374; -. DR KO; K01473; -. DR OMA; VRFPFID; -. DR PhylomeDB; Q58374; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016787; F:hydrolase activity; IEA:InterPro. DR InterPro; IPR008040; Hydant_A_N. DR InterPro; IPR002821; Hydantoinase_A. DR Pfam; PF05378; Hydant_A_N; 1. DR Pfam; PF01968; Hydantoinase_A; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 680 Uncharacterized protein MJ0964. FT /FTId=PRO_0000208586. SQ SEQUENCE 680 AA; 75843 MW; D69AEA8C4F4555CD CRC64; MVMGYRVGID IGGTFTDLVY FDEYSKEFHV VKVPTTPKSP DVGAINAIET AKIEFDKINI LIHATTLGTN MFLGQEHLNP PKIALITTKG FKDVIEIGRQ RRPKLYDLFF EKPKPLIKRR DRYEVEERID ANGNIITPLN EEELQKIAEI IKKKDYEVVV ISFLHSYKNP IHEKKAREII KNLCSNVDVI TSYEINPEYK EYERTSTTVI NAYLKPLVSN YLKNFIDSLK NKGFNGKFYV MQSSGGISNI KYATERPAAF IESGPAAGAI AVAYFSKILN DNKVIGFDMG GTTAKASTII NNSPLVTNEY EVGGEVHAGR LIKGSGYPVR FPFIDLAEVS AGGGTIAWVD EGNALRVGPI SAGADPGPVC YGKGNDKPTI TDANLILGRL GEKLSGGLLK LRKDLAEKAI SKLAEKIGES VEEIAYGIIR LANTTMAKAL RIVTVERGYD PRDFVMYVFG GAGPLHGVEL AEEMEISSIL IPPSCGVFSA LGLLLADCRV DKAKSILKDI DEVDEEEIEN IFIELIEEGL KEVEGFEEIK IVKQIDVRYK GQSYELTIPW TGDLKELADN FHKKHETVYK FSSLEEDIEL VNARVTIIGL LTKPEIKCYE VKEYKPKPES YRKVYFSSGW EETAIYNRDK LKPGAIFEGP AVVEEYDSTI VIPPDYTAFV DKYGCLRIER // ID Y967_METJA Reviewed; 205 AA. AC Q58377; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Uncharacterized protein MJ0967; GN OrderedLocusNames=MJ0967; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the peptidase C56 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98972.1; -; Genomic_DNA. DR PIR; G64420; G64420. DR ProteinModelPortal; Q58377; -. DR STRING; 243232.MJ_0967; -. DR EnsemblBacteria; AAB98972; AAB98972; MJ_0967. DR KEGG; mja:MJ_0967; -. DR eggNOG; arCOG00769; Archaea. DR eggNOG; COG0693; LUCA. DR InParanoid; Q58377; -. DR KO; K05520; -. DR OMA; ICISPVV; -. DR PhylomeDB; Q58377; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0019172; F:glyoxalase III activity; IBA:GO_Central. DR GO; GO:0016798; F:hydrolase activity, acting on glycosyl bonds; IEA:InterPro. DR GO; GO:0019249; P:lactate biosynthetic process; IBA:GOC. DR GO; GO:0019243; P:methylglyoxal catabolic process to D-lactate via S-lactoyl-glutathione; IBA:GO_Central. DR Gene3D; 3.40.50.880; -; 1. DR InterPro; IPR029062; Class_I_gatase-like. DR InterPro; IPR002818; DJ-1/PfpI. DR InterPro; IPR006286; Peptidase_C56. DR Pfam; PF01965; DJ-1_PfpI; 1. DR SUPFAM; SSF52317; SSF52317; 1. DR TIGRFAMs; TIGR01382; PfpI; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 205 Uncharacterized protein MJ0967. FT /FTId=PRO_0000157847. FT COMPBIAS 174 180 Val-rich. SQ SEQUENCE 205 AA; 22542 MW; E60E6AD066ECCFB5 CRC64; MKRLAVILIT LALVSSMCIT NSNEKRENMK NAKVLMVIAP KDFRDEELFE PMAVFESNGL KVDVVSTTKG ECVGMLGNKI TVEKTIYDVN PDDYVAIVIV GGIGSKEYLW NNTKLIELVK EFYNKNKVVS AICLSPVVLA RAGILKGKKA TVYPAPEAIE ELKKAGAIYE DRGVVVDGNV ITAKSPDYAR LFGLEVLKAI EKNNE // ID Y989_METJA Reviewed; 114 AA. AC Q58396; DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0989; GN OrderedLocusNames=MJ0989; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.kandleri MK0008. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98991.1; -; Genomic_DNA. DR PIR; E64423; E64423. DR ProteinModelPortal; Q58396; -. DR STRING; 243232.MJ_0989; -. DR EnsemblBacteria; AAB98991; AAB98991; MJ_0989. DR KEGG; mja:MJ_0989; -. DR eggNOG; arCOG02068; Archaea. DR eggNOG; COG1553; LUCA. DR InParanoid; Q58396; -. DR KO; K07235; -. DR OMA; QLATMHD; -. DR PhylomeDB; Q58396; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR Pfam; PF02635; DrsE; 1. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 114 Uncharacterized protein MJ0989. FT /FTId=PRO_0000107132. SQ SEQUENCE 114 AA; 12577 MW; 2FF7A56356C0E3FB CRC64; MKFTVIITEA PYGKERAYSA LRFALTALLE GIEVNIFLLE NGVYVAKKEQ NPSEVPNYLE LLKNAIELGA VVKVCGPCCK ARGLKEEDLI EGAKLATMHD LIAFVKESDN VVTF // ID Y990_METJA Reviewed; 75 AA. AC Q58397; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=UPF0033 protein MJ0990; GN OrderedLocusNames=MJ0990; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0033 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98992.1; -; Genomic_DNA. DR PIR; F64423; F64423. DR ProteinModelPortal; Q58397; -. DR STRING; 243232.MJ_0990; -. DR EnsemblBacteria; AAB98992; AAB98992; MJ_0990. DR KEGG; mja:MJ_0990; -. DR eggNOG; arCOG02062; Archaea. DR eggNOG; COG0425; LUCA. DR InParanoid; Q58397; -. DR KO; K04085; -. DR OMA; VVGDYKP; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.110.40; -; 1. DR InterPro; IPR001455; TusA-like. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR PROSITE; PS01148; UPF0033; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 75 UPF0033 protein MJ0990. FT /FTId=PRO_0000159080. FT COMPBIAS 27 36 Glu-rich. SQ SEQUENCE 75 AA; 8465 MW; CF7009364C388539 CRC64; MVIAMKKLDV TGDICPVPVL KTKKALEELN EGEELEVVGD YKPALENIKR FAENNGYTVV LAEETESRFR IVIKK // ID YC8C_METJA Reviewed; 123 AA. AC P81320; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1288.1; GN OrderedLocusNames=MJ1288.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99300.1; -; Genomic_DNA. DR STRING; 243232.MJ_1288.1; -. DR EnsemblBacteria; AAB99300; AAB99300; MJ_1288.1. DR KEGG; mja:MJ_1288.1; -. DR eggNOG; arCOG08271; Archaea. DR eggNOG; ENOG41111FP; LUCA. DR OMA; SFTIIFQ; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 123 Uncharacterized protein MJ1288.1. FT /FTId=PRO_0000107255. FT TRANSMEM 1 21 Helical. {ECO:0000255}. SQ SEQUENCE 123 AA; 14404 MW; 3E4A5EFBD75E54B3 CRC64; MHIIAKSILL MAVSFLVIIF TSTIYSELIE IGKYRYIDKV DREITSEVMN AVVLANEGNI TLYKKINLNC KVIFENNSFT IIFQNKTYVH KFNNNIRFFK NEISDISKIS CKKVNNTYMI YIE // ID YE7B_METJA Reviewed; 129 AA. AC P81227; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ1479.1; GN OrderedLocusNames=MJ1479.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99501.1; -; Genomic_DNA. DR STRING; 243232.MJ_1479.1; -. DR EnsemblBacteria; AAB99501; AAB99501; MJ_1479.1. DR KEGG; mja:MJ_1479.1; -. DR eggNOG; arCOG05086; Archaea. DR eggNOG; COG2983; LUCA. DR KO; K09160; -. DR OMA; FPKDCPY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized protein MJ1479.1. FT /FTId=PRO_0000107362. SQ SEQUENCE 129 AA; 15505 MW; 4E41E257A58A8C69 CRC64; MSSKPLYTIL TVFNPIFIYF TKRDNLHTLR FKKDRAIKIS EELFPDELCE RCGRCCILHA YKTEDGIKTI YCEHLDPETK LCKVYKDRFK HRCLTVMEGI LAGVFPKDCP YVKNLKNYEE PWFYRHLRD // ID YF9A_METJA Reviewed; 128 AA. AC P81325; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MJ1597.1; GN OrderedLocusNames=MJ1597.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99628.1; -; Genomic_DNA. DR STRING; 243232.MJ_1597.1; -. DR EnsemblBacteria; AAB99628; AAB99628; MJ_1597.1. DR KEGG; mja:MJ_1597.1; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 128 Uncharacterized protein MJ1597.1. FT /FTId=PRO_0000107432. SQ SEQUENCE 128 AA; 15255 MW; AA298F1AE774032D CRC64; MFPFRIGLIL TTKEEYEVLN GLFQFPYRIG LILIAKILVW HWRVYLFSFP SSKRSDFNFL KQPQVKHWFI SFPSSKRSDF NLLCYCQFPY SPPKNFHPPR GLILTENEVK ELKKCLCFHP PRGLILTV // ID Y439_METJA Reviewed; 361 AA. AC Q57881; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized ATP-binding protein MJ0439; GN OrderedLocusNames=MJ0439; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SIMILARITY. RX PubMed=9045616; DOI=10.1126/science.275.5305.1489; RA Koonin E.V.; RT "Evidence for a family of archaeal ATPases."; RL Science 275:1489-1490(1997). CC -!- SIMILARITY: Belongs to the archaeal ATPase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98434.1; -; Genomic_DNA. DR PIR; G64354; G64354. DR ProteinModelPortal; Q57881; -. DR SMR; Q57881; 270-361. DR STRING; 243232.MJ_0439; -. DR DNASU; 1451299; -. DR EnsemblBacteria; AAB98434; AAB98434; MJ_0439. DR KEGG; mja:MJ_0439; -. DR eggNOG; arCOG03407; Archaea. DR eggNOG; COG1672; LUCA. DR InParanoid; Q57881; -. DR KO; K06921; -. DR OMA; WCERELT; -. DR PhylomeDB; Q57881; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR011579; ATPase_dom. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01637; ATPase_2; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 361 Uncharacterized ATP-binding protein FT MJ0439. FT /FTId=PRO_0000184668. FT NP_BIND 41 48 ATP. {ECO:0000255}. SQ SEQUENCE 361 AA; 42610 MW; 8B24E3B24F1E5D80 CRC64; MNYIYSFING DFMRFFNREK EITEILSILE GNPDLVYFVY GPLNSGKTAL ISEIINNRID KNKYVVFYIN LRGIFISKYK DFIEVLFEEY EEDRKPVEII KSLIKDVPSL CGIPTPKNTL EEILKKKTTK NVFKYITNVL MDIKKEGKQP IIIIDELQKI GDMKINGFLI YELFNYFVDL TKELHLCHVF CLSSDSLFIE QVYSEAMLKD RVDYILVDDF DKETALKFMD FLAEEILNKK LSDDEKELIY SYVGGKPILI IKVIKKLKIK GLKETLDEML RDEMQKLKYF LEDIKEKDEE SYNKIADALE IFKDSYEIED IKIPKNIREF LVKKNILFLN PQKGTLKPQS YLVWNAIKRL L // ID Y480_METJA Reviewed; 198 AA. AC Q57904; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 82. DE RecName: Full=Uncharacterized protein MJ0480; GN OrderedLocusNames=MJ0480; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98471.1; -; Genomic_DNA. DR PIR; H64359; H64359. DR PDB; 5C8J; X-ray; 3.50 A; I/J/K/L=1-198. DR PDBsum; 5C8J; -. DR STRING; 243232.MJ_0480; -. DR EnsemblBacteria; AAB98471; AAB98471; MJ_0480. DR KEGG; mja:MJ_0480; -. DR eggNOG; arCOG10126; Archaea. DR eggNOG; COG1422; LUCA. DR InParanoid; Q57904; -. DR OMA; WYILCSM; -. DR PhylomeDB; Q57904; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002809; DUF106_TM. DR Pfam; PF01956; DUF106; 1. DR SMART; SM01415; DUF106; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 198 Uncharacterized protein MJ0480. FT /FTId=PRO_0000106888. FT TRANSMEM 23 43 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 137 157 Helical. {ECO:0000255}. FT TRANSMEM 168 188 Helical. {ECO:0000255}. SQ SEQUENCE 198 AA; 23072 MW; 91CFB738E3E6BAC8 CRC64; MFGSIFDIYY KTLDAIFMPI IKVLHPALAI LIIAIIVSLI INIATKLLVD QKRVAELKKE IQEFQVKFKK MSKNPEMMEK LQEEQQRIMQ LNAELMKMSF RPMIYTWVPI ILIFIYLRHV YGFGGVYQEL NPGWNGVVVY LPIILSKILF IDFWHWLGSI FYKGGFKIVS NTALGWLGWY ILCSFATSTV LRKILGIK // ID Y481_METJA Reviewed; 98 AA. AC Q57906; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0481; GN OrderedLocusNames=MJ0481; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98472.1; -; Genomic_DNA. DR PIR; B64360; B64360. DR ProteinModelPortal; Q57906; -. DR EnsemblBacteria; AAB98472; AAB98472; MJ_0481. DR KEGG; mja:MJ_0481; -. DR eggNOG; arCOG05031; Archaea. DR eggNOG; ENOG410YR2C; LUCA. DR OMA; LFFKYQD; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020505; Uncharacterised_MJ0481. DR ProDom; PD066852; Uncharacterised_MJ0481; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 98 Uncharacterized protein MJ0481. FT /FTId=PRO_0000106889. SQ SEQUENCE 98 AA; 11218 MW; 6F31A408240C3CB3 CRC64; MYNCPYCGKD CVNEAAVNIY LKMVEKFFKY QNKGSDITFE KYPTVGEVGE CKETGGRIYL CPYCKKPFKA YYEKDKVVIT CPNCGETLCL PATNRTFC // ID Y488_METJA Reviewed; 158 AA. AC Q57912; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0488; GN OrderedLocusNames=MJ0488; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98479.1; -; Genomic_DNA. DR PIR; H64360; H64360. DR PDB; 3WB0; X-ray; 1.91 A; A/B/C/D=3-158. DR PDB; 3WB1; X-ray; 2.40 A; A/B/C/D=3-158. DR PDB; 3WB2; X-ray; 2.44 A; A/B/C/D=3-158. DR PDBsum; 3WB0; -. DR PDBsum; 3WB1; -. DR PDBsum; 3WB2; -. DR ProteinModelPortal; Q57912; -. DR STRING; 243232.MJ_0488; -. DR EnsemblBacteria; AAB98479; AAB98479; MJ_0488. DR KEGG; mja:MJ_0488; -. DR eggNOG; arCOG04863; Archaea. DR eggNOG; COG4019; LUCA. DR OMA; IMDKKGR; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.10150; -; 1. DR InterPro; IPR010254; B12-dep_deHydtase_bsu. DR InterPro; IPR012019; DUF3236. DR Pfam; PF11576; DUF3236; 1. DR PIRSF; PIRSF005018; UCP005018; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 158 Uncharacterized protein MJ0488. FT /FTId=PRO_0000106894. FT HELIX 4 17 {ECO:0000244|PDB:3WB0}. FT HELIX 25 36 {ECO:0000244|PDB:3WB0}. FT STRAND 39 44 {ECO:0000244|PDB:3WB0}. FT HELIX 48 58 {ECO:0000244|PDB:3WB0}. FT TURN 59 61 {ECO:0000244|PDB:3WB0}. FT STRAND 65 68 {ECO:0000244|PDB:3WB0}. FT HELIX 73 78 {ECO:0000244|PDB:3WB0}. FT STRAND 79 81 {ECO:0000244|PDB:3WB0}. FT HELIX 82 93 {ECO:0000244|PDB:3WB0}. FT STRAND 97 104 {ECO:0000244|PDB:3WB0}. FT STRAND 112 118 {ECO:0000244|PDB:3WB0}. FT STRAND 123 129 {ECO:0000244|PDB:3WB0}. FT HELIX 132 135 {ECO:0000244|PDB:3WB0}. FT HELIX 139 152 {ECO:0000244|PDB:3WB0}. FT TURN 153 155 {ECO:0000244|PDB:3WB0}. SQ SEQUENCE 158 AA; 17784 MW; 4BB76EAE604F7078 CRC64; MIVMEEIIKK AFIESINNIR RGDKEEELKK IQEKIVNAKK IVVATNNQKK FKVIRDIMLR VCNAEIKMLD IDTRFADLTR MPALTKGLIA LDIEKADLYI ARGRLGAPGS GSMLVILDEK GRVLTASLSP SSVIHKEDIE ERIKKELIEA LSRIGISI // ID Y492_METJA Reviewed; 95 AA. AC Q57915; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0492; GN OrderedLocusNames=MJ0492; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98488.1; -; Genomic_DNA. DR PIR; D64361; D64361. DR ProteinModelPortal; Q57915; -. DR STRING; 243232.MJ_0492; -. DR EnsemblBacteria; AAB98488; AAB98488; MJ_0492. DR KEGG; mja:MJ_0492; -. DR eggNOG; arCOG08284; Archaea. DR eggNOG; ENOG41110P4; LUCA. DR OMA; NIMKSEN; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 95 Uncharacterized protein MJ0492. FT /FTId=PRO_0000106897. FT TRANSMEM 3 23 Helical. {ECO:0000255}. SQ SEQUENCE 95 AA; 10695 MW; 7A49FD4F888A365C CRC64; MNFVIIIAIL LLGISLILAF TVLNKSKSKT TMAYKRAQEE KIDTEIKMLK NLKNNVCSGA SDEIIDNILN SENNILKEAL KNNLDDADVC KKLRR // ID Y496_METJA Reviewed; 141 AA. AC Q57919; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 62. DE RecName: Full=Uncharacterized protein MJ0496; GN OrderedLocusNames=MJ0496; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98489.1; -; Genomic_DNA. DR PIR; H64361; H64361. DR STRING; 243232.MJ_0496; -. DR EnsemblBacteria; AAB98489; AAB98489; MJ_0496. DR KEGG; mja:MJ_0496; -. DR eggNOG; arCOG05032; Archaea. DR eggNOG; ENOG410YRZ7; LUCA. DR OMA; HKEEEHS; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 141 Uncharacterized protein MJ0496. FT /FTId=PRO_0000106898. SQ SEQUENCE 141 AA; 15692 MW; DA284F11A8CEB443 CRC64; MVRVVYVVNL PYKKLGVECD GKQLILKMKS KDVEDSIKMN FESAALLKIL MEQSAVIAEK INKDFKKDKI KVHNIHDVGT VFGVDGRVSV GVLPADENRV ASILVGFHKD DKHISVVVKP KKIALLSVII TKIISENLKL D // ID Y498_METJA Reviewed; 156 AA. AC Q57921; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0498; GN OrderedLocusNames=MJ0498; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98486.1; -; Genomic_DNA. DR PIR; B64362; B64362. DR STRING; 243232.MJ_0498; -. DR EnsemblBacteria; AAB98486; AAB98486; MJ_0498. DR KEGG; mja:MJ_0498; -. DR eggNOG; arCOG04901; Archaea. DR eggNOG; COG4029; LUCA. DR InParanoid; Q57921; -. DR OMA; ETCFGAY; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR012025; UCP005642_methan. DR Pfam; PF09875; DUF2102; 1. DR PIRSF; PIRSF005642; UCP005642; 1. DR TIGRFAMs; TIGR03272; methan_mark_6; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 156 Uncharacterized protein MJ0498. FT /FTId=PRO_0000106900. SQ SEQUENCE 156 AA; 17921 MW; B514D56D41EAAAB7 CRC64; MMKKTKVIVL AENALTTPGK LVRYINTLNQ PVIVKETCFG AYIEGEEELV DKLAQEIRNY ERNRIFCKDR GYAIWDKRRC RAFRGGGPRE GFHQLEAEQA VLDKIGLALD KIDKEGIKPM EEVLAKENEL IKRETKIPVE EFKNIIEKVL GSKNEA // ID Y526_METJA Reviewed; 92 AA. AC Q57946; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0526; GN OrderedLocusNames=MJ0526; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98529.1; -; Genomic_DNA. DR PIR; F64365; F64365. DR ProteinModelPortal; Q57946; -. DR STRING; 243232.MJ_0526; -. DR EnsemblBacteria; AAB98529; AAB98529; MJ_0526. DR KEGG; mja:MJ_0526; -. DR eggNOG; arCOG04829; Archaea. DR eggNOG; COG4039; LUCA. DR KO; K14095; -. DR OMA; CYYLDIA; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR019213; DUF2108_membrane. DR InterPro; IPR011308; Prd_NiFe_hyd_3_EhaD. DR Pfam; PF09881; DUF2108; 1. DR PIRSF; PIRSF006581; EhaD; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 92 Uncharacterized protein MJ0526. FT /FTId=PRO_0000106915. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. SQ SEQUENCE 92 AA; 10077 MW; CB4935AF56AA3110 CRC64; MEVLPLVSGI CCILGGIGVI LHTNPINKII MLALLEIGMI GLIVSCYYLD IAIVSSLCEP ICTVILLLGY LKYLTTVKKK KRYGRNLPIL SK // ID Y527_METJA Reviewed; 164 AA. AC Q57947; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0527; GN OrderedLocusNames=MJ0527; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98518.1; -; Genomic_DNA. DR PIR; G64365; G64365. DR STRING; 243232.MJ_0527; -. DR EnsemblBacteria; AAB98518; AAB98518; MJ_0527. DR KEGG; mja:MJ_0527; -. DR eggNOG; arCOG04828; Archaea. DR eggNOG; COG4041; LUCA. DR KO; K14093; -. DR OMA; MGNIVCS; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011314; Prd_NiFe_hyd_3_EhaB. DR PIRSF; PIRSF019706; EhaB; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 164 Uncharacterized protein MJ0527. FT /FTId=PRO_0000106918. FT TRANSMEM 3 23 Helical. {ECO:0000255}. FT TRANSMEM 76 96 Helical. {ECO:0000255}. FT TRANSMEM 105 125 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. SQ SEQUENCE 164 AA; 17616 MW; BC24D60F9F9B4A60 CRC64; MEIVEIVKII IAGIICWLNF VLIDTYFGLP EKPGVLGAKT IGEKIRDIGG NLNGGYFMGN IVCSPDASAG TLLASIMNYL MGIEGGFIAA LLVWIGNRLC ADPGYAGTIG ALTITAIIYL LNPIIEAKYF IVGMVLAIFT IQGFEHRYAS ILLGKIAKKM NRGE // ID Y529_METJA Reviewed; 232 AA. AC Q57949; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 88. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0529; GN OrderedLocusNames=MJ0529; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98520.1; -; Genomic_DNA. DR PIR; A64366; A64366. DR ProteinModelPortal; Q57949; -. DR STRING; 243232.MJ_0529; -. DR PRIDE; Q57949; -. DR EnsemblBacteria; AAB98520; AAB98520; MJ_0529. DR KEGG; mja:MJ_0529; -. DR eggNOG; arCOG05036; Archaea. DR eggNOG; ENOG410YA97; LUCA. DR OMA; PIYSIKK; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR Pfam; PF01381; HTH_3; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 232 Uncharacterized HTH-type transcriptional FT regulator MJ0529. FT /FTId=PRO_0000149790. FT DOMAIN 39 91 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 50 69 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 232 AA; 27091 MW; 46A162ADFDE60EF1 CRC64; MAEYVFLIYL VDIKYQFREN MYKKLEIIER AILLNPQYIQ AFREKLKITQ SKLAKESGIS QSHLSMLEKG KRPATKLIAT AVTLGLLKCF SSNNVENPII ELLDALSLLK FEDTFAEFVS EIIEKGDKGY LRLIENYPVL IISKENLLNE MRSRLEVMDI ERIELSRGRI KVIGKHLDNK YVEIFLDCSD IRRLEKKFMK KTGKKVIIQV FPKDEVPPIY SINKDCVIIH CW // ID Y52A_METJA Reviewed; 82 AA. AC P81309; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 66. DE RecName: Full=Uncharacterized protein MJ0526.1; GN OrderedLocusNames=MJ0526.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH386. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98527.1; -; Genomic_DNA. DR STRING; 243232.MJ_0526.1; -. DR DNASU; 1451391; -. DR EnsemblBacteria; AAB98527; AAB98527; MJ_0526.1. DR KEGG; mja:MJ_0526.1; -. DR eggNOG; arCOG03190; Archaea. DR eggNOG; COG4040; LUCA. DR KO; K14094; -. DR OMA; LYIKSPM; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019214; DUF2109_membrane. DR InterPro; IPR011316; Prd_NiFe_hyd_3_EhaC. DR Pfam; PF09882; DUF2109; 1. DR PIRSF; PIRSF036534; EhaC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 82 Uncharacterized protein MJ0526.1. FT /FTId=PRO_0000106916. SQ SEQUENCE 82 AA; 9169 MW; 4ABFA1488DE787EA CRC64; MMDIVEIIIG FIALLMTARI FLERSRARKL LYLCCLSFCI SALIALYVDS PMGGIVAITY FICSTISSNA IAYTIEQTKH IE // ID Y558_METJA Reviewed; 261 AA. AC Q57978; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 83. DE RecName: Full=Uncharacterized protein MJ0558; GN OrderedLocusNames=MJ0558; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98552.1; -; Genomic_DNA. DR PIR; F64369; F64369. DR ProteinModelPortal; Q57978; -. DR STRING; 243232.MJ_0558; -. DR EnsemblBacteria; AAB98552; AAB98552; MJ_0558. DR KEGG; mja:MJ_0558; -. DR eggNOG; arCOG04399; Archaea. DR eggNOG; COG1497; LUCA. DR InParanoid; Q57978; -. DR KO; K07730; -. DR OMA; HQPNVRQ; -. DR PhylomeDB; Q57978; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR012318; HTH_CRP. DR InterPro; IPR012015; UCP_HTH_arc. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR PIRSF; PIRSF004955; HTH_arch; 1. DR SMART; SM00419; HTH_CRP; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 261 Uncharacterized protein MJ0558. FT /FTId=PRO_0000106930. SQ SEQUENCE 261 AA; 29206 MW; 706AD20896269F4F CRC64; MKKRNITEFQ VLSEIIRKQP HIKQKEIAEN LGITVQAVSE HIRNLVKEGY VKSRGRGEYV VTEKGLRKLK NWISEFKDYL DEINTAVYRY KDIWPAIADE DVKDGETVYL FMKNGLLYAS KQPKGEAKAK ALYGGKKGED IAICEIKGII DVPKGKVIVF RIPPEVVGGS RAVDFNLIKE NIDNLDDYVI ATMGTVAYVV ACKLGLKPDI RFAVPEAIVN ACNRGCNVIA LITGKMAEKV IKKLDNAKIS YTVLDATKEN K // ID Y573_METJA Reviewed; 189 AA. AC Q57993; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0573; GN OrderedLocusNames=MJ0573; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the OsmC/Ohr family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98573.1; -; Genomic_DNA. DR PIR; E64371; E64371. DR ProteinModelPortal; Q57993; -. DR STRING; 243232.MJ_0573; -. DR EnsemblBacteria; AAB98573; AAB98573; MJ_0573. DR KEGG; mja:MJ_0573; -. DR eggNOG; arCOG03686; Archaea. DR eggNOG; COG1765; LUCA. DR InParanoid; Q57993; -. DR OMA; EMAPKMM; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0006979; P:response to oxidative stress; IEA:InterPro. DR Gene3D; 3.30.300.20; -; 1. DR InterPro; IPR015946; KH_dom-like_a/b. DR InterPro; IPR003718; OsmC/Ohr_fam. DR Pfam; PF02566; OsmC; 1. DR SUPFAM; SSF82784; SSF82784; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 189 Uncharacterized protein MJ0573. FT /FTId=PRO_0000172734. SQ SEQUENCE 189 AA; 21198 MW; 47173D93ADBEDF69 CRC64; MNPEMIMEMM NSDIAKEMAP KMMPKMMPLA LEKFLQYIPE NERKEFIARI VDIIVSKDEN KEVSAEYLDM FEALLNVKGL KIHSRGGKGA IKEKISPMDL FLAGLCGCVC IAVGNTLKAN NIDAEIKVDG KVEKSFEEGK IKKVIINIYV KVDGDIDKEK LKKLVLEGSK KCLISNSISC EIEKNVILE // ID Y580_METJA Reviewed; 118 AA. AC Q58000; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0580; GN OrderedLocusNames=MJ0580; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98571.1; -; Genomic_DNA. DR PIR; D64372; D64372. DR ProteinModelPortal; Q58000; -. DR STRING; 243232.MJ_0580; -. DR EnsemblBacteria; AAB98571; AAB98571; MJ_0580. DR KEGG; mja:MJ_0580; -. DR eggNOG; arCOG02734; Archaea. DR eggNOG; COG1433; LUCA. DR InParanoid; Q58000; -. DR OMA; IVQNIGP; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.420.130; -; 1. DR InterPro; IPR003731; Di-Nase_FeMo-co_biosynth. DR Pfam; PF02579; Nitro_FeMo-Co; 1. DR SUPFAM; SSF53146; SSF53146; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 118 Uncharacterized protein MJ0580. FT /FTId=PRO_0000106941. SQ SEQUENCE 118 AA; 13139 MW; 71B7E11FF73E0C1F CRC64; MTKILKVKLM KIALPIDNNR LSPHFGRCEK FMIVEIENGE IKNKEIIENT ARNGMHGVGT TSASLIANMG VNAIIVQNIG PKAYSVFKQL GIDVYKANTT SIDECIKLFL EGKLEKFE // ID Y609_METJA Reviewed; 435 AA. AC Q58026; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Uncharacterized protein MJ0609; GN OrderedLocusNames=MJ0609; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98602.1; -; Genomic_DNA. DR PIR; A64376; A64376. DR PDB; 3GI8; X-ray; 2.59 A; C=1-435. DR PDB; 3GI9; X-ray; 2.48 A; C=1-435. DR PDB; 3GIA; X-ray; 2.32 A; A=1-435. DR PDBsum; 3GI8; -. DR PDBsum; 3GI9; -. DR PDBsum; 3GIA; -. DR ProteinModelPortal; Q58026; -. DR STRING; 243232.MJ_0609; -. DR TCDB; 2.A.3.6.3; the amino acid-polyamine-organocation (apc) family. DR EnsemblBacteria; AAB98602; AAB98602; MJ_0609. DR KEGG; mja:MJ_0609; -. DR eggNOG; arCOG00009; Archaea. DR eggNOG; COG0531; LUCA. DR InParanoid; Q58026; -. DR OMA; YSWINVM; -. DR PhylomeDB; Q58026; -. DR EvolutionaryTrace; Q58026; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0015297; F:antiporter activity; IBA:GO_Central. DR GO; GO:0015179; F:L-amino acid transmembrane transporter activity; IBA:GO_Central. DR GO; GO:1902475; P:L-alpha-amino acid transmembrane transport; IBA:GOC. DR GO; GO:0015807; P:L-amino acid transport; IBA:GOC. DR InterPro; IPR002293; AA/rel_permease1. DR PANTHER; PTHR11785; PTHR11785; 1. DR Pfam; PF13520; AA_permease_2; 1. DR PIRSF; PIRSF006060; AA_transporter; 1. PE 1: Evidence at protein level; KW 3D-structure; Cell membrane; Complete proteome; Membrane; KW Reference proteome; Transmembrane; Transmembrane helix. FT CHAIN 1 435 Uncharacterized protein MJ0609. FT /FTId=PRO_0000106956. FT TRANSMEM 14 34 Helical. {ECO:0000255}. FT TRANSMEM 44 64 Helical. {ECO:0000255}. FT TRANSMEM 84 104 Helical. {ECO:0000255}. FT TRANSMEM 123 143 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TRANSMEM 224 244 Helical. {ECO:0000255}. FT TRANSMEM 267 287 Helical. {ECO:0000255}. FT TRANSMEM 324 344 Helical. {ECO:0000255}. FT TRANSMEM 346 366 Helical. {ECO:0000255}. FT TRANSMEM 375 395 Helical. {ECO:0000255}. FT TRANSMEM 400 420 Helical. {ECO:0000255}. FT HELIX 10 25 {ECO:0000244|PDB:3GIA}. FT TURN 26 28 {ECO:0000244|PDB:3GIA}. FT HELIX 30 37 {ECO:0000244|PDB:3GIA}. FT HELIX 38 40 {ECO:0000244|PDB:3GIA}. FT HELIX 41 63 {ECO:0000244|PDB:3GIA}. FT TURN 69 71 {ECO:0000244|PDB:3GIA}. FT HELIX 72 80 {ECO:0000244|PDB:3GIA}. FT HELIX 84 115 {ECO:0000244|PDB:3GIA}. FT HELIX 122 142 {ECO:0000244|PDB:3GIA}. FT HELIX 144 172 {ECO:0000244|PDB:3GIA}. FT HELIX 175 177 {ECO:0000244|PDB:3GIA}. FT HELIX 184 196 {ECO:0000244|PDB:3GIA}. FT HELIX 197 203 {ECO:0000244|PDB:3GIA}. FT HELIX 204 208 {ECO:0000244|PDB:3GIA}. FT HELIX 209 213 {ECO:0000244|PDB:3GIA}. FT STRAND 214 216 {ECO:0000244|PDB:3GIA}. FT HELIX 217 244 {ECO:0000244|PDB:3GIA}. FT HELIX 249 254 {ECO:0000244|PDB:3GIA}. FT HELIX 256 258 {ECO:0000244|PDB:3GIA}. FT HELIX 259 292 {ECO:0000244|PDB:3GIA}. FT TURN 293 295 {ECO:0000244|PDB:3GIA}. FT HELIX 296 305 {ECO:0000244|PDB:3GIA}. FT STRAND 310 312 {ECO:0000244|PDB:3GI9}. FT HELIX 322 337 {ECO:0000244|PDB:3GIA}. FT HELIX 340 364 {ECO:0000244|PDB:3GIA}. FT HELIX 366 369 {ECO:0000244|PDB:3GIA}. FT HELIX 373 397 {ECO:0000244|PDB:3GIA}. FT HELIX 399 423 {ECO:0000244|PDB:3GIA}. FT HELIX 429 431 {ECO:0000244|PDB:3GIA}. FT TURN 432 434 {ECO:0000244|PDB:3GIA}. SQ SEQUENCE 435 AA; 47358 MW; 3F289E21FC56CF97 CRC64; MELKNKKLSL WEAVSMAVGV MIGASIFSIF GVGAKIAGRN LPETFILSGI YALLVAYSYT KLGAKIVSNA GPIAFIHKAI GDNIITGALS ILLWMSYVIS IALFAKGFAG YFLPLINAPI NTFNIAITEI GIVAFFTALN FFGSKAVGRA EFFIVLVKLL ILGLFIFAGL ITIHPSYVIP DLAPSAVSGM IFASAIFFLS YMGFGVITNA SEHIENPKKN VPRAIFISIL IVMFVYVGVA ISAIGNLPID ELIKASENAL AVAAKPFLGN LGFLLISIGA LFSISSAMNA TIYGGANVAY SLAKDGELPE FFERKVWFKS TEGLYITSAL GVLFALLFNM EGVASITSAV FMVIYLFVIL SHYILIDEVG GRKEIVIFSF IVVLGVFLLL LYYQWITNRF VFYGIIATFI GVLIFEIIYR KVTKRTFSNN MYVKS // ID Y672_METJA Reviewed; 432 AA. AC Q58086; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 101. DE RecName: Full=Uncharacterized transporter MJ0672; GN OrderedLocusNames=MJ0672; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the CitM (TC 2.A.11) transporter family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98666.1; -; Genomic_DNA. DR PIR; H64383; H64383. DR ProteinModelPortal; Q58086; -. DR STRING; 243232.MJ_0672; -. DR TCDB; 2.A.47.5.1; the divalent anion:na(+) symporter (dass) family. DR EnsemblBacteria; AAB98666; AAB98666; MJ_0672. DR KEGG; mja:MJ_0672; -. DR eggNOG; arCOG00237; Archaea. DR eggNOG; COG0471; LUCA. DR InParanoid; Q58086; -. DR KO; K14445; -. DR OMA; LFIIPSR; -. DR PhylomeDB; Q58086; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IBA:GO_Central. DR GO; GO:0098656; P:anion transmembrane transport; IBA:GO_Central. DR GO; GO:0006814; P:sodium ion transport; IEA:InterPro. DR InterPro; IPR001898; Na/sul_symport. DR InterPro; IPR031312; Na/sul_symport_CS. DR Pfam; PF00939; Na_sulph_symp; 1. DR TIGRFAMs; TIGR00785; dass; 1. DR PROSITE; PS01271; NA_SULFATE; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 432 Uncharacterized transporter MJ0672. FT /FTId=PRO_0000172507. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 29 49 Helical. {ECO:0000255}. FT TRANSMEM 68 88 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 156 176 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 241 261 Helical. {ECO:0000255}. FT TRANSMEM 266 286 Helical. {ECO:0000255}. FT TRANSMEM 291 311 Helical. {ECO:0000255}. FT TRANSMEM 326 346 Helical. {ECO:0000255}. FT TRANSMEM 358 378 Helical. {ECO:0000255}. FT TRANSMEM 379 399 Helical. {ECO:0000255}. FT TRANSMEM 412 432 Helical. {ECO:0000255}. SQ SEQUENCE 432 AA; 47542 MW; A24BF9E64475CB74 CRC64; MRLSKEFIGL GIITASLIFG SSLPDIYKGI VILIVAGCLW FFELLPLPVT SLAIPIMAVF LGIFNLKEAL TYFAHPIIFL FLGGFMLAQA LKNHNLDKFI AYKLLNYGKD FKTTCFLMFL SAYFLSMWIS NTSATLILLP IALGLLHKKT GKLRDFLLLG VAYSASIGGI ATIIGSPPNA IASSYLDYGF FSWFKVGFPI SLLLFLICTL TLYIYFKKWI PKEDIAIQAR MELSRNAYKL LVIFVLIASL WIISDYLSEI FNVQYFDSVI AIFAIILLFV FNLVEVNDFK KIDWGTLILF GGALCLGGVI VKSGANTFLS EKLIAILGNL TPIVLLFLVV TITIILTNFI SNTGLTGIIV PILFGVSLGI PKEILILAVG MSASCSFILP VGTPPNAIVY SEGVKKEEMM KIGMILSILS AAVITLYSIL YL // ID Y676_METJA Reviewed; 335 AA. AC Q58089; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Putative hydrogenase expression/formation protein MJ0676; GN OrderedLocusNames=MJ0676; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HypE family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98671.1; -; Genomic_DNA. DR PIR; D64384; D64384. DR ProteinModelPortal; Q58089; -. DR SMR; Q58089; 39-331. DR STRING; 243232.MJ_0676; -. DR EnsemblBacteria; AAB98671; AAB98671; MJ_0676. DR KEGG; mja:MJ_0676; -. DR eggNOG; arCOG00636; Archaea. DR eggNOG; COG0309; LUCA. DR InParanoid; Q58089; -. DR KO; K04655; -. DR OMA; DPIPRVC; -. DR PhylomeDB; Q58089; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.1330.10; -; 1. DR Gene3D; 3.90.650.10; -; 1. DR InterPro; IPR010918; AIR_synth_C_dom. DR InterPro; IPR011854; HypE. DR InterPro; IPR016188; PurM-like_N. DR Pfam; PF00586; AIRS; 1. DR Pfam; PF02769; AIRS_C; 1. DR PIRSF; PIRSF005644; Hdrgns_mtr_HypE; 1. DR SUPFAM; SSF56042; SSF56042; 1. DR TIGRFAMs; TIGR02124; hypE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 335 Putative hydrogenase expression/formation FT protein MJ0676. FT /FTId=PRO_0000201462. SQ SEQUENCE 335 AA; 35813 MW; 1676B351C033A964 CRC64; MKITRMHGAG GKVMQELIKD VILKNLEITS VNGGIGLESL DDSATIPIGD KEIVFTVDGH TVKPIFFPGG DIGRLAVSGT VNDLAVMGAK PLALSLSLII PEGFNLEDLE KIVKSINETS KEAEVAIITG DTKVSDGVDD IIISTAGIGI VDRGKAIRDC NVQEGDAIIV SGNIGEHGLA ILLSREGFDF ETNIKSDVAP INKLIERVLE EGIQINAMKD PTRGGLADAL NEMAEKSNIG ITIFEDKIPI SDEVQSICDI LGLDPLTIAN EGKVVMAVKK EDAERCLEIL REHPLGKNAE IIGYATKEHK GVIIETIVGR RIVDMPIGDP IPRVC // ID Y683_METJA Reviewed; 259 AA. AC Q58096; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0683; GN OrderedLocusNames=MJ0683; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98678.1; -; Genomic_DNA. DR PIR; C64385; C64385. DR ProteinModelPortal; Q58096; -. DR STRING; 243232.MJ_0683; -. DR EnsemblBacteria; AAB98678; AAB98678; MJ_0683. DR KEGG; mja:MJ_0683; -. DR eggNOG; arCOG01290; Archaea. DR eggNOG; COG1533; LUCA. DR InParanoid; Q58096; -. DR OMA; CYASFMK; -. DR PhylomeDB; Q58096; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 259 Uncharacterized protein MJ0683. FT /FTId=PRO_0000106987. FT METAL 34 34 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 38 38 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 41 41 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 259 AA; 30385 MW; 15CB7E77D2CF756C CRC64; MNSKIEIIKI KAKKPINPTK IPGAKYVINQ YIGCQYACKY CYARFMCKWY NYGKWGSWVV VKENLPDLIK NKHIKGKIYM SSVSDAYRPI EKDFKLTRNI LKNIDKRAEL SILTKSDLVL RDMDLFKKFS SIEVGLTINN FEGNLKKDIE PFSPSNEKRI DALKTLYENG IKNYAFISPI IPDLIDVEYI IGETKPFTNF YYFEFLNLKA SREFKHYLEQ NYPESYEIIS NKTAFKRYID EVINTIKKKD IAIKGICVH // ID Y696_METJA Reviewed; 182 AA. AC Q58107; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0696; GN OrderedLocusNames=MJ0696; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0803. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98697.1; -; Genomic_DNA. DR PIR; H64386; H64386. DR ProteinModelPortal; Q58107; -. DR STRING; 243232.MJ_0696; -. DR EnsemblBacteria; AAB98697; AAB98697; MJ_0696. DR KEGG; mja:MJ_0696; -. DR eggNOG; arCOG09672; Archaea. DR eggNOG; ENOG41110S3; LUCA. DR OMA; ILTICTI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR009328; DUF986. DR Pfam; PF06173; DUF986; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 182 Uncharacterized protein MJ0696. FT /FTId=PRO_0000106993. FT TRANSMEM 58 78 Helical. {ECO:0000255}. FT TRANSMEM 81 101 Helical. {ECO:0000255}. SQ SEQUENCE 182 AA; 21487 MW; 62D4DD70A40952AB CRC64; MESILFIAIA FLINSFISYK ITNMQPKIKS RIFKRVKMHY LNLIEGKKAE FDKKAMPILF GFMIIALISF NILLYVVYNC PVSITSIIAE ILIIISMIII WKAFNKEISV YLCDDGIYYS NKFISWKNIE NVKKDDGFIV LFGKKKKILG RKLYLLQRIY LKYDEEIENI IKNQIEKFRD KA // ID Y737_METJA Reviewed; 61 AA. AC Q58147; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0737; GN OrderedLocusNames=MJ0737; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 rubredoxin-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00241}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98732.1; -; Genomic_DNA. DR PIR; A64392; A64392. DR ProteinModelPortal; Q58147; -. DR STRING; 243232.MJ_0737; -. DR EnsemblBacteria; AAB98732; AAB98732; MJ_0737. DR KEGG; mja:MJ_0737; -. DR eggNOG; arCOG05047; Archaea. DR eggNOG; COG1773; LUCA. DR OMA; VTCYTPE; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005506; F:iron ion binding; IEA:InterPro. DR Gene3D; 2.20.28.10; -; 1. DR InterPro; IPR024934; Rubredoxin-like_dom. DR InterPro; IPR004039; Rubredoxin-type_fold. DR PROSITE; PS50903; RUBREDOXIN_LIKE; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 61 Uncharacterized protein MJ0737. FT /FTId=PRO_0000135074. FT DOMAIN 1 46 Rubredoxin-like. {ECO:0000255|PROSITE- FT ProRule:PRU00241}. SQ SEQUENCE 61 AA; 7051 MW; EB62A73AF9D15587 CRC64; MPWWKCSNCG YVFEAEKPPE RCPNCGEKCT FYDVSCYTPE CGFKGYDPKL VARTPNQESK M // ID Y778_METJA Reviewed; 169 AA. AC Q58188; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 84. DE RecName: Full=Uncharacterized protein MJ0778; GN OrderedLocusNames=MJ0778; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98768.1; -; Genomic_DNA. DR PIR; B64397; B64397. DR ProteinModelPortal; Q58188; -. DR STRING; 243232.MJ_0778; -. DR DNASU; 1451655; -. DR EnsemblBacteria; AAB98768; AAB98768; MJ_0778. DR KEGG; mja:MJ_0778; -. DR eggNOG; arCOG01858; Archaea. DR eggNOG; COG1418; LUCA. DR InParanoid; Q58188; -. DR KO; K06950; -. DR OMA; DHGIIGS; -. DR PhylomeDB; Q58188; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.3210.10; -; 1. DR InterPro; IPR004454; HD-related. DR InterPro; IPR003607; HD/PDEase_dom. DR InterPro; IPR006674; HD_domain. DR InterPro; IPR006675; HDIG_dom. DR Pfam; PF01966; HD; 1. DR SMART; SM00471; HDc; 1. DR TIGRFAMs; TIGR00277; HDIG; 1. DR TIGRFAMs; TIGR00295; TIGR00295; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 169 Uncharacterized protein MJ0778. FT /FTId=PRO_0000107029. SQ SEQUENCE 169 AA; 18940 MW; 912EC4EAB768C8F2 CRC64; MEFEKALSIL KNLCSENVVE HCLAVSEYAY ELALAIKNKG YEVDVELVRL GGLLHDIGRS RTHGIEHGVV GAEILRELGF DEKLALIAER HIGAGITKEE AIELGLPPKD YLPITLEEKI VAHADNLIFG TKRVEIDDVI KKFEKRLGKN HPSIKRIILL NDEINNLLK // ID Y786_METJA Reviewed; 186 AA. AC Q58196; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0786; GN OrderedLocusNames=MJ0786; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98786.1; -; Genomic_DNA. DR PIR; B64398; B64398. DR ProteinModelPortal; Q58196; -. DR STRING; 243232.MJ_0786; -. DR EnsemblBacteria; AAB98786; AAB98786; MJ_0786. DR KEGG; mja:MJ_0786; -. DR eggNOG; arCOG02614; Archaea. DR eggNOG; ENOG4111RNX; LUCA. DR InParanoid; Q58196; -. DR KO; K06024; -. DR OMA; ILIIPDY; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 186 Uncharacterized protein MJ0786. FT /FTId=PRO_0000107036. SQ SEQUENCE 186 AA; 21628 MW; 769D5413D99977F7 CRC64; MIRGTMKIGI TKMYKEIADL IGLEEYEIVN PYNTKVDCDF LIISKGYKER VKKLNPESEI FEVKSATFMD LIKSLEELKK LGIGKEGKID KSIEFLKNKE KEIKKLVKDL NVKVNPKTEF IRKVVEDLGL EISDNGILII PDYLFDGKNI ENIIILKTHN YDLGLVERIE DRYLQIIQSI QKYLNK // ID Y794_METJA Reviewed; 141 AA. AC Q58204; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0794; GN OrderedLocusNames=MJ0794; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98797.1; -; Genomic_DNA. DR PIR; B64399; B64399. DR ProteinModelPortal; Q58204; -. DR STRING; 243232.MJ_0794; -. DR EnsemblBacteria; AAB98797; AAB98797; MJ_0794. DR KEGG; mja:MJ_0794; -. DR eggNOG; arCOG02054; Archaea. DR eggNOG; COG2881; LUCA. DR InParanoid; Q58204; -. DR OMA; YMREISQ; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR006977; Yip1. DR Pfam; PF04893; Yip1; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 141 Uncharacterized protein MJ0794. FT /FTId=PRO_0000107045. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. SQ SEQUENCE 141 AA; 15935 MW; 39CD0EA926BDC08C CRC64; MILMNLIEAL TNPDTFFKKL SQKEISLKEP FLIVLIFSIL IAISAYISTS IIYKIFPPQY QQVLAFTKII ALISTFIGGI VAWLIIAGFM HLISMIFKGE GSFKKTLSFT GYGFLPNIVG ALITIPIAYY MREISQQEMR L // ID Y807_METJA Reviewed; 184 AA. AC Q58217; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Putative lyase MJ0807; DE EC=4.1.-.-; GN OrderedLocusNames=MJ0807; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the chorismate pyruvate-lyase type 2 CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98807.1; -; Genomic_DNA. DR PIR; G64400; G64400. DR ProteinModelPortal; Q58217; -. DR STRING; 243232.MJ_0807; -. DR EnsemblBacteria; AAB98807; AAB98807; MJ_0807. DR KEGG; mja:MJ_0807; -. DR eggNOG; arCOG01031; Archaea. DR eggNOG; COG3161; LUCA. DR InParanoid; Q58217; -. DR OMA; QRTYNII; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.1410.10; -; 1. DR InterPro; IPR028978; Chorismate_lyase_/UTRA_dom. DR InterPro; IPR002800; DUF98. DR Pfam; PF01947; DUF98; 1. DR SUPFAM; SSF64288; SSF64288; 1. PE 3: Inferred from homology; KW Complete proteome; Lyase; Reference proteome. FT CHAIN 1 184 Putative lyase MJ0807. FT /FTId=PRO_0000107056. SQ SEQUENCE 184 AA; 21548 MW; 086471223FBE61D6 CRC64; MQKTKLRLIF MIIYKEIAKL NKTFPLLNEE KILLGTDGSV TNILEILFEG ECRVETINQK IVANTNYREV ILKVNNIPLV YAVSKTPFKN IEEENLREEI KRDLLSADIP IGKIIRKHNL ETRREIKYIG IAEIDDYLKS LLKTNYSRLP KRTYNIIYKN KVLMEITEIF AVRGKLVKNT YSID // ID Y808_METJA Reviewed; 333 AA. AC Q58218; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 86. DE RecName: Full=Uncharacterized protein MJ0808; GN OrderedLocusNames=MJ0808; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98808.1; -; Genomic_DNA. DR PIR; H64400; H64400. DR ProteinModelPortal; Q58218; -. DR STRING; 243232.MJ_0808; -. DR EnsemblBacteria; AAB98808; AAB98808; MJ_0808. DR KEGG; mja:MJ_0808; -. DR eggNOG; arCOG00946; Archaea. DR eggNOG; COG1180; LUCA. DR InParanoid; Q58218; -. DR KO; K04069; -. DR OMA; PYIDAMN; -. DR PhylomeDB; Q58218; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR027596; AmmeMemoSam_rS. DR InterPro; IPR016431; Pyrv-formate_lyase-activ_prd. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. DR PIRSF; PIRSF004869; PflX_prd; 1. DR TIGRFAMs; TIGR04337; AmmeMemoSam_rS; 1. PE 4: Predicted; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 333 Uncharacterized protein MJ0808. FT /FTId=PRO_0000107057. FT METAL 82 82 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 86 86 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 89 89 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 333 AA; 38337 MW; C31C2477F6050893 CRC64; MREAMFYEKL DDNKVRCHIC PRHCIIKEGE RGFCWNRENI NGVLYAVGYG KVCSLAIDPI EKKPLFHFYP TTQVVSLAIG GCNFRCLHCQ NWTISQFPPD EIPYREMTPE EIVEVAIRYN CPGISYTYTE PTVYYEFMYD TSVIARENGM FNVMITNGYI EKEPLKALPV DAMNIDIKGN ADFYKKVCKA TLEPVLETCK LAKKLGIWVE VTNLIVPNYN DNIDDLLFII HFVRDELGRE TPLHFSRFHP DYKLTDVPPT PIETLEMARN LAIEEGLKYV YIGNVPGHEG ENTYCPNCGA LLIERYIFNA KIINLDVETK RCKICGEKID IVL // ID Y809_METJA Reviewed; 167 AA. AC Q58219; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 78. DE RecName: Full=Acylphosphatase-like protein MJ0809; GN OrderedLocusNames=MJ0809; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 acylphosphatase-like domain. CC {ECO:0000255|PROSITE-ProRule:PRU00520}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98817.1; -; Genomic_DNA. DR PIR; A64401; A64401. DR ProteinModelPortal; Q58219; -. DR STRING; 243232.MJ_0809; -. DR EnsemblBacteria; AAB98817; AAB98817; MJ_0809. DR KEGG; mja:MJ_0809; -. DR eggNOG; arCOG01674; Archaea. DR eggNOG; COG1254; LUCA. DR InParanoid; Q58219; -. DR OMA; EHTRILN; -. DR PhylomeDB; Q58219; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016743; F:carboxyl- or carbamoyltransferase activity; IBA:GO_Central. DR GO; GO:0008270; F:zinc ion binding; IBA:GO_Central. DR GO; GO:0051604; P:protein maturation; IBA:GO_Central. DR InterPro; IPR001792; Acylphosphatase-like_dom. DR InterPro; IPR017968; Acylphosphatase_CS. DR Pfam; PF00708; Acylphosphatase; 1. DR SUPFAM; SSF54975; SSF54975; 1. DR PROSITE; PS00150; ACYLPHOSPHATASE_1; 1. DR PROSITE; PS51160; ACYLPHOSPHATASE_3; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 167 Acylphosphatase-like protein MJ0809. FT /FTId=PRO_0000158563. FT DOMAIN 8 106 Acylphosphatase-like. FT {ECO:0000255|PROSITE-ProRule:PRU00520}. SQ SEQUENCE 167 AA; 19723 MW; DD998FE1329C0042 CRC64; MVIIMPTTYE LKIYGKVQHV GFRDRIENIG KGLGINGIIY NYKDGTVRIL ANFDDEEDKE LFKKYIERLE KKDKLIEIEK IEEKRLNTYI EFPEGISRLS SDDILELNKK LDEGVKYIKL IFAELEEHKK VLLEIKDMHV KTVEILSEHT RILNEIKDTL KDIKDKL // ID Y828_METJA Reviewed; 66 AA. AC Q58238; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MJ0828; GN OrderedLocusNames=MJ0828; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98827.1; -; Genomic_DNA. DR PIR; D64403; D64403. DR STRING; 243232.MJ_0828; -. DR EnsemblBacteria; AAB98827; AAB98827; MJ_0828. DR KEGG; mja:MJ_0828; -. DR eggNOG; arCOG01915; Archaea. DR eggNOG; COG0330; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 66 Uncharacterized protein MJ0828. FT /FTId=PRO_0000107065. SQ SEQUENCE 66 AA; 7485 MW; C1C9DF3595FFA7CD CRC64; MRIEAEGQAK AIQIVAEAAR QYFKDEAQLY KALEVANNVL KDNAKYVISE NILDVVRNFI KKDKSA // ID Y858_METJA Reviewed; 113 AA. AC Q58268; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0858; GN OrderedLocusNames=MJ0858; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98864.1; -; Genomic_DNA. DR PIR; B64407; B64407. DR ProteinModelPortal; Q58268; -. DR STRING; 243232.MJ_0858; -. DR EnsemblBacteria; AAB98864; AAB98864; MJ_0858. DR KEGG; mja:MJ_0858; -. DR eggNOG; arCOG04905; Archaea. DR eggNOG; COG4009; LUCA. DR OMA; TTSYQAY; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.160.120; -; 1. DR InterPro; IPR008032; DUF749. DR InterPro; IPR016458; UCP005648_Ca-bd. DR Pfam; PF05370; DUF749; 1. DR PIRSF; PIRSF005648; UCP005648_Ca-bd; 1. DR SUPFAM; SSF75412; SSF75412; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 113 Uncharacterized protein MJ0858. FT /FTId=PRO_0000107083. SQ SEQUENCE 113 AA; 13335 MW; D2FE8B783DBCB0AB CRC64; MNDKNVEFVA TLISILTVKE ALNSEMENFV KVRAAIDKRE LKDDDKVAIF NINSTTSYQV FFIDKDTNIE ELKEEFKKMN VRINYDSEQV LKRYIERLRI QNNSKPISNN NKQ // ID Y866_METJA Reviewed; 129 AA. AC Q58276; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 83. DE RecName: Full=Uncharacterized HIT-like protein MJ0866; GN OrderedLocusNames=MJ0866; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP SEQUENCE REVISION. RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RL Submitted (FEB-1998) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Contains 1 HIT domain. {ECO:0000255|PROSITE- CC ProRule:PRU00464}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98871.1; -; Genomic_DNA. DR PIR; B64408; B64408. DR ProteinModelPortal; Q58276; -. DR STRING; 243232.MJ_0866; -. DR EnsemblBacteria; AAB98871; AAB98871; MJ_0866. DR KEGG; mja:MJ_0866; -. DR eggNOG; arCOG00419; Archaea. DR eggNOG; COG0537; LUCA. DR InParanoid; Q58276; -. DR KO; K02503; -. DR OMA; DDELCNF; -. DR PhylomeDB; Q58276; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR Gene3D; 3.30.428.10; -; 1. DR InterPro; IPR019808; Histidine_triad_CS. DR InterPro; IPR001310; Histidine_triad_HIT. DR InterPro; IPR011146; HIT-like. DR PANTHER; PTHR23089; PTHR23089; 1. DR Pfam; PF01230; HIT; 1. DR PRINTS; PR00332; HISTRIAD. DR SUPFAM; SSF54197; SSF54197; 1. DR PROSITE; PS00892; HIT_1; 1. DR PROSITE; PS51084; HIT_2; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 129 Uncharacterized HIT-like protein MJ0866. FT /FTId=PRO_0000109834. FT DOMAIN 3 109 HIT. {ECO:0000255|PROSITE- FT ProRule:PRU00464}. FT MOTIF 94 98 Histidine triad motif. SQ SEQUENCE 129 AA; 14749 MW; DEC95012CEF4339C CRC64; MCIFCKIING EIPAKVVYED EHVLAFLDIN PRNKGHTLVV PKKHYERFDE MPDDELCNFI KGVKKTVEVL KKLGFDGYNI VNNNGRVAGQ EVNHVHFHII PRYEGDGEVV KFGEVKNVDL DEVLKEIKG // ID Y870_METJA Reviewed; 620 AA. AC Q58280; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 100. DE RecName: Full=Uncharacterized protein MJ0870; GN OrderedLocusNames=MJ0870; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the nitrite and sulfite reductase 4Fe-4S CC domain family. {ECO:0000305}. CC -!- SIMILARITY: Contains 3 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98876.1; -; Genomic_DNA. DR PIR; F64408; F64408. DR ProteinModelPortal; Q58280; -. DR STRING; 243232.MJ_0870; -. DR EnsemblBacteria; AAB98876; AAB98876; MJ_0870. DR KEGG; mja:MJ_0870; -. DR eggNOG; arCOG02650; Archaea. DR eggNOG; COG1035; LUCA. DR eggNOG; COG2221; LUCA. DR InParanoid; Q58280; -. DR KO; K00441; -. DR OMA; YFPYLAK; -. DR BRENDA; 1.8.98.3; 3260. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0020037; F:heme binding; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR007516; Co_F420_Hydgase/DH_bsu_N. DR InterPro; IPR007525; FrhB_FdhB_C. DR InterPro; IPR005117; NiRdtase/SiRdtase_haem-b_fer. DR InterPro; IPR006067; NO2/SO3_Rdtase_4Fe4S_dom. DR InterPro; IPR006066; NO2/SO3_Rdtase_FeS/sirohaem_BS. DR Pfam; PF00037; Fer4; 2. DR Pfam; PF04432; FrhB_FdhB_C; 1. DR Pfam; PF04422; FrhB_FdhB_N; 1. DR Pfam; PF01077; NIR_SIR; 1. DR Pfam; PF03460; NIR_SIR_ferr; 1. DR PRINTS; PR00397; SIROHAEM. DR SUPFAM; SSF55124; SSF55124; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 2. DR PROSITE; PS51379; 4FE4S_FER_2; 3. DR PROSITE; PS00365; NIR_SIR; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Heme; Iron; Iron-sulfur; Metal-binding; KW Oxidoreductase; Reference proteome; Repeat. FT CHAIN 1 620 Uncharacterized protein MJ0870. FT /FTId=PRO_0000199970. FT DOMAIN 6 35 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 486 515 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 515 544 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 428 428 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 434 434 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 468 468 Iron-sulfur (4Fe-4S). {ECO:0000250}. FT METAL 472 472 Iron (siroheme axial ligand). FT {ECO:0000250}. FT METAL 472 472 Iron-sulfur (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 620 AA; 69794 MW; 9D71D2580D7D0BA8 CRC64; MYEWKLNEIV DSGVCARCGT CTIVCPNGIL TFDERPKLID ECLRKGHGMC FEVCPRVSSA KYQIKIREKF YEKYYYAKSD IEGQDGGVVT AFLKYLLENG KIDGAIVVGD ECWKPVSLVV QNAEDLLKTA KSKYAISTLD ALRKAGEMGL EKVAVVGLPC QINGLRKLQY FPYHAKHDLE LGRNGKPVKL PKIEYLIGLF CTEKFRYDNM KEVLSKHGID IEKVEKFDIK KGKLLVYVNG EKKEFDLKEF EICSGCKMCR DFDAEMADVS VGCVGSPDGY STIIIRTEKG EEIKNAVELK EGVNLEEIEK LRQLKLKRFK KEVERRRENN EYVSFYWTAD YGGIGKRADG TYFIRVRAKP GGWYKPEEIK EILDIAEEYN AKIKVTDRAG YELHGISGFD VEDIVLRLRE KGLLTGSEGP LVRATLACPG GGNCSSGLVD TTELARIIED NFKERPAPYK FKIAISGCPN GCVRPQVHDI GIAGVKYPKV NEEKCNGCGR CAEVCKVEAI DIRGETSYTN YNVCVGCGKC IKNCPNEARE VKEEGYLVYV GGKTGREVVE GVKMKLMSVD EIINFIDKVL VVYGKYAEKP QRERLAAVMK RVGYGKFLEE VKELMKKEIC // ID Y872_METJA Reviewed; 391 AA. AC Q58282; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 10-MAY-2004, sequence version 2. DT 17-FEB-2016, entry version 85. DE RecName: Full=Uncharacterized lipoprotein MJ0872; DE Flags: Precursor; GN OrderedLocusNames=MJ0872; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE- CC ProRule:PRU00303}; Lipid-anchor {ECO:0000255|PROSITE- CC ProRule:PRU00303}. CC -!- SIMILARITY: Contains 1 Fe/B12 periplasmic-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00344}. CC -!- SEQUENCE CAUTION: CC Sequence=AAB98880.1; Type=Erroneous initiation; Evidence={ECO:0000305}; CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98880.1; ALT_INIT; Genomic_DNA. DR PIR; H64408; H64408. DR ProteinModelPortal; Q58282; -. DR STRING; 243232.MJ_0872; -. DR EnsemblBacteria; AAB98880; AAB98880; MJ_0872. DR KEGG; mja:MJ_0872; -. DR eggNOG; arCOG03417; Archaea. DR eggNOG; COG0614; LUCA. DR InParanoid; Q58282; -. DR KO; K02016; -. DR OMA; EPTYMGR; -. DR PhylomeDB; Q58282; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0030288; C:outer membrane-bounded periplasmic space; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0036094; F:small molecule binding; IBA:GO_Central. DR GO; GO:0006810; P:transport; IBA:GO_Central. DR InterPro; IPR002491; ABC_transptr_periplasmic_BD. DR Pfam; PF01497; Peripla_BP_2; 1. DR PROSITE; PS50983; FE_B12_PBP; 1. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Lipoprotein; Membrane; KW Reference proteome; Signal. FT SIGNAL 1 20 {ECO:0000255|PROSITE-ProRule:PRU00303}. FT CHAIN 21 390 Uncharacterized lipoprotein MJ0872. FT /FTId=PRO_0000014004. FT DOMAIN 104 377 Fe/B12 periplasmic-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00344}. FT LIPID 21 21 S-archaeol cysteine. {ECO:0000255}. SQ SEQUENCE 391 AA; 44910 MW; C063343A4AF51CA4 CRC64; MRKLFLLSIL MIGVIVAFAG CVEESKTTTQ LQQTTQSESQ KAETQPKLGV NVVRYAETFK LYPHWDEGYC VVADSVGNKF VLVEGNAKAP NISDGKIIKV PVKRIVTDFY CPIISAADIL NAYHHTIVGA PKYAVEKSPK LKELFDEGKV VDIGSPSKGV NYELIVNLTP DIVFLGDWKS EDVVEEKLKE LGVTVSRFYT YQEPTYMGRV EWIKFAAAFW GSNAYKKADK WFENVVKVRE NILKKVQNVT NEPTVVIFSW SKTKNMPGIY GNDSYYSKMI AEFKGKNVFD DYNRGYQYVD KETFYERAMN ADVVILIWFY GDVKTKEDLL KINPNFAEFK AFKTGRFYVS HPDYYVWEAR DPAGYMMDFA KMIHPELFGG DDDLKYYYKI K // ID Y905_METJA Reviewed; 111 AA. AC Q58315; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0905; GN OrderedLocusNames=MJ0905; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98915.1; -; Genomic_DNA. DR PIR; A64413; A64413. DR ProteinModelPortal; Q58315; -. DR STRING; 243232.MJ_0905; -. DR EnsemblBacteria; AAB98915; AAB98915; MJ_0905. DR KEGG; mja:MJ_0905; -. DR eggNOG; arCOG03422; Archaea. DR eggNOG; COG3373; LUCA. DR InParanoid; Q58315; -. DR KO; K09745; -. DR OMA; YYRLTEY; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR010863; DUF1495. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF07381; DUF1495; 1. DR SUPFAM; SSF46785; SSF46785; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 111 Uncharacterized protein MJ0905. FT /FTId=PRO_0000107097. SQ SEQUENCE 111 AA; 12873 MW; AF34D2852F85715F CRC64; MSLAFIDPMI IRSLNKSKLR KKILYLLYKM YPHGIYLSEI SRRVRSDPSN VLGCLKGMNG RYNGHFSLIE LGLVECVERG GVKIYKLTDY GKKIVEVLKD QDSDFIESLR W // ID Y911_METJA Reviewed; 365 AA. AC Q58321; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 86. DE RecName: Full=Magnesium-chelatase subunit ChlI homolog; GN OrderedLocusNames=MJ0911; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the Mg-chelatase subunits D/I family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98913.1; -; Genomic_DNA. DR PIR; G64413; G64413. DR ProteinModelPortal; Q58321; -. DR SMR; Q58321; 7-323. DR STRING; 243232.MJ_0911; -. DR EnsemblBacteria; AAB98913; AAB98913; MJ_0911. DR KEGG; mja:MJ_0911; -. DR eggNOG; arCOG00438; Archaea. DR eggNOG; COG1239; LUCA. DR InParanoid; Q58321; -. DR KO; K03405; -. DR OMA; RAFEPGL; -. DR PhylomeDB; Q58321; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR000523; Mg_chelatse_chII_dom. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01078; Mg_chelatase; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 365 Magnesium-chelatase subunit ChlI homolog. FT /FTId=PRO_0000206875. FT NP_BIND 40 47 ATP. {ECO:0000255}. SQ SEQUENCE 365 AA; 41677 MW; CB0046955E1881E3 CRC64; MMIMQYIYPF TAIVGQEKMK KALILNAINP KIGGVLIRGE KGTAKSTAVR ALADLLPEIE IVEGCPFNCD PNGNLCDICK EKKKRGELKT TKKKMKVVNL PIGATEDRVI GTLDIEKAIK EGIKALEPGI LAEANRNILY IDEVNLLDDH IIDVLLDAAA MGWNIIEREG VKIKHPSRFI LVGTMNPEEG ELRPQILDRF GLMVDVEGLN DVKDRVEVIK RVEEFNENPE AFYKKFEEEQ NKLRERIIKA RELLNKVEIS DDLLEFISKV CIELGIQTNR ADITVVRTAK ALAAYNGRTY VTIDDVKEAM ELALPHRMRR KPFEPPQLNK EKLEQMINEF KQQNNKDNEE KEEHKDDDVK KNMMK // ID Y934_METJA Reviewed; 209 AA. AC Q58344; DT 10-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 91. DE RecName: Full=Uncharacterized polyferredoxin-like protein MJ0934; GN OrderedLocusNames=MJ0934; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 6 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98939.1; -; Genomic_DNA. DR PIR; F64416; F64416. DR ProteinModelPortal; Q58344; -. DR STRING; 243232.MJ_0934; -. DR EnsemblBacteria; AAB98939; AAB98939; MJ_0934. DR KEGG; mja:MJ_0934; -. DR eggNOG; arCOG02184; Archaea. DR eggNOG; ENOG410XW3B; LUCA. DR InParanoid; Q58344; -. DR OMA; SCIFCKD; -. DR PhylomeDB; Q58344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR InterPro; IPR009051; Helical_ferredxn. DR Pfam; PF00037; Fer4; 1. DR Pfam; PF13237; Fer4_10; 1. DR Pfam; PF13187; Fer4_9; 1. DR SUPFAM; SSF46548; SSF46548; 1. DR PROSITE; PS00198; 4FE4S_FER_1; 5. DR PROSITE; PS51379; 4FE4S_FER_2; 6. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Electron transport; Iron; Iron-sulfur; KW Metal-binding; Reference proteome; Repeat; Transport. FT CHAIN 1 209 Uncharacterized polyferredoxin-like FT protein MJ0934. FT /FTId=PRO_0000159151. FT DOMAIN 38 67 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 63 92 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 90 119 4Fe-4S ferredoxin-type 3. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 122 151 4Fe-4S ferredoxin-type 4. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 145 174 4Fe-4S ferredoxin-type 5. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 179 209 4Fe-4S ferredoxin-type 6. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 47 47 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 50 50 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 53 53 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 57 57 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 72 72 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 75 75 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 78 78 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 82 82 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 99 99 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 102 102 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 105 105 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 109 109 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 154 154 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 157 157 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 160 160 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 164 164 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 188 188 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 191 191 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 194 194 Iron-sulfur (4Fe-4S). {ECO:0000255}. FT METAL 198 198 Iron-sulfur (4Fe-4S). {ECO:0000255}. SQ SEQUENCE 209 AA; 23567 MW; 755EDCFF8077D54B CRC64; MRFMEEEFYK IFKGAGLIKT LIRSIFLTNR NKFSKPSKTK PIQLTECIGC GLCVDVCPTN AIKIFSFRET ICSVCGTCVD VCPNNAIIKD RFTIDADKCT KCGVCVLFCP IPIIKKEIPK PKTPVILKDR CNSCGLCECE AIDIINKEIN PEKCKLCLSC IEKCPLQAIL TPDEYINSLI VKVDIDSCIF CRECEEICPI RGNYEHRES // ID Y945_METJA Reviewed; 224 AA. AC Q58355; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0945; GN OrderedLocusNames=MJ0945; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98955.1; -; Genomic_DNA. DR PIR; A64418; A64418. DR ProteinModelPortal; Q58355; -. DR STRING; 243232.MJ_0945; -. DR PRIDE; Q58355; -. DR EnsemblBacteria; AAB98955; AAB98955; MJ_0945. DR KEGG; mja:MJ_0945; -. DR eggNOG; arCOG08285; Archaea. DR eggNOG; ENOG410Z3KA; LUCA. DR InParanoid; Q58355; -. DR OMA; GTDFYRY; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR InterPro; IPR010496; DUF1080. DR Pfam; PF06439; DUF1080; 1. PE 4: Predicted; KW Complete proteome; Membrane; Reference proteome; Transmembrane; KW Transmembrane helix. FT CHAIN 1 224 Uncharacterized protein MJ0945. FT /FTId=PRO_0000107116. FT TRANSMEM 21 41 Helical. {ECO:0000255}. SQ SEQUENCE 224 AA; 25416 MW; 1E9FF7E32C025DA9 CRC64; MLLRQYINVP RLGEIMNLKE LTVILIIPIV YLGVCGCFEI VPKSFYDNFS SYNVGDKAPF GEWKVKEGGF KIEAILSEDK KTLNKVAVPI NNGIIYIDKN YTDFKFIVDI KRLEESDSPK IYFRLINNAN AGYYIDIEGF DRGYVLYKFN GTKVEKLAES YDAAPAGTDF YRYEVVAKDN KIIFLAGGQK YIEYTDNNTP ILKGGIGIGG GRAYYDNVRV EPIE // ID Y959_METJA Reviewed; 385 AA. AC Q58369; DT 21-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized aminotransferase MJ0959; DE EC=2.6.1.-; GN OrderedLocusNames=MJ0959; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326; CC Evidence={ECO:0000250}; CC -!- SIMILARITY: Belongs to the class-V pyridoxal-phosphate-dependent CC aminotransferase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98961.1; -; Genomic_DNA. DR PIR; G64419; G64419. DR ProteinModelPortal; Q58369; -. DR STRING; 243232.MJ_0959; -. DR EnsemblBacteria; AAB98961; AAB98961; MJ_0959. DR KEGG; mja:MJ_0959; -. DR eggNOG; arCOG00082; Archaea. DR eggNOG; COG0075; LUCA. DR InParanoid; Q58369; -. DR OMA; IFRIAHM; -. DR PhylomeDB; Q58369; -. DR BioCyc; MetaCyc:MONOMER-15919; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0008483; F:transaminase activity; IEA:UniProtKB-KW. DR Gene3D; 3.40.640.10; -; 1. DR Gene3D; 3.90.1150.10; -; 1. DR InterPro; IPR000192; Aminotrans_V_dom. DR InterPro; IPR015424; PyrdxlP-dep_Trfase. DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major_sub1. DR InterPro; IPR015422; PyrdxlP-dep_Trfase_major_sub2. DR InterPro; IPR024169; SP_NH2Trfase/AEP_transaminase. DR Pfam; PF00266; Aminotran_5; 1. DR PIRSF; PIRSF000524; SPT; 1. DR SUPFAM; SSF53383; SSF53383; 1. PE 3: Inferred from homology; KW Aminotransferase; Complete proteome; Pyridoxal phosphate; KW Reference proteome; Transferase. FT CHAIN 1 385 Uncharacterized aminotransferase MJ0959. FT /FTId=PRO_0000150343. FT MOD_RES 194 194 N6-(pyridoxal phosphate)lysine. FT {ECO:0000255}. SQ SEQUENCE 385 AA; 42413 MW; 7DA5410050D3FB1A CRC64; MKIDAVKKLL MIPGPTMVPP EVLNAMALPV IGHRTKDYSN LLEDTIEKLK KVFITENDTF LITGSGTAAM DMAISNIIKR GDKVLNIVTG NFGERFANIV KAYKGEAIRL DVEWGDMAEP EAVKEILDKY DDIKAVTVVH NETSTGARNP IKEIGEVVKD YDALYIVDTV SSLGGDYVNV DKFHIDICVT GSQKCLAAPP GLAAITVSEK AWEVIKKNDD KVGFYLDLLA YKKYYEEKKQ TPYTPSVNLT YALNVALDLV LEEGIENRVK RHERLAKATR AGLEAMGIEL FAKERARSVT VTSAKYPEGI EDSKFRGILS NKYNIVVAGG QKHLAGKIFR IGHMGICGEK EVLATLACVE LALKELGFEV KESGVEVAKE VLLKE // ID Y978_METJA Reviewed; 147 AA. AC Q58388; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0978; GN OrderedLocusNames=MJ0978; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1086 N-terminal region. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98993.1; -; Genomic_DNA. DR PIR; B64422; B64422. DR ProteinModelPortal; Q58388; -. DR STRING; 243232.MJ_0978; -. DR EnsemblBacteria; AAB98993; AAB98993; MJ_0978. DR KEGG; mja:MJ_0978; -. DR eggNOG; arCOG05125; Archaea. DR eggNOG; ENOG4111JNR; LUCA. DR InParanoid; Q58388; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR020209; Uncharacterised_MJ0978. DR ProDom; PD089226; Uncharacterised_MJ0978; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 147 Uncharacterized protein MJ0978. FT /FTId=PRO_0000107127. SQ SEQUENCE 147 AA; 17112 MW; 28A5962011ED2FCB CRC64; MGEIILNIRE LNLKGEVYRV VNGYAKVKFE EFGVAENMIK YKFISPWIAL NEKNYLEYKE LDEDGKKELL EKILVGNILS MSKYLDYTVE EKLKAGLLEY EDFVVKYKGN KFIGFWGEFL VNFNIPNYLG IGRKVSKGFG SVIRVEE // ID Y995_METJA Reviewed; 227 AA. AC Q58402; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0995; GN OrderedLocusNames=MJ0995; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99000.1; -; Genomic_DNA. DR PIR; C64424; C64424. DR ProteinModelPortal; Q58402; -. DR STRING; 243232.MJ_0995; -. DR EnsemblBacteria; AAB99000; AAB99000; MJ_0995. DR KEGG; mja:MJ_0995; -. DR eggNOG; arCOG06579; Archaea. DR eggNOG; ENOG410YMK8; LUCA. DR OMA; YYNGVLI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 227 Uncharacterized protein MJ0995. FT /FTId=PRO_0000107136. FT TRANSMEM 12 32 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. SQ SEQUENCE 227 AA; 26360 MW; F9D84BB3E76BB568 CRC64; MYGDYMKYMK KIVLFLIINI LPILILGLYL YANIGGAEDV KEVIENSPFK EFTYIDHKTL MMLKNDVNLK NMPEFYKESI ILINGIYIGN HGSFGIKIPL GFLIKYIPID NFKYYNGVLI KNLNEDDLGK AEMNDLVNTI PPNYKDVLIY RENYTIGIYY DLNSNKTYLI EVFRKPNNQE IDTEKLRNEL LQKTNAVDCN VVDMGDKVYV YLEFNGIDLN LINNGIT // ID YD3A_METJA Reviewed; 137 AA. AC P81327; DT 02-FEB-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 76. DE RecName: Full=Uncharacterized protein MJ1333.1; GN OrderedLocusNames=MJ1333.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 1 EamA domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99347.1; -; Genomic_DNA. DR ProteinModelPortal; P81327; -. DR STRING; 243232.MJ_1333.1; -. DR EnsemblBacteria; AAB99347; AAB99347; MJ_1333.1. DR KEGG; mja:MJ_1333.1; -. DR eggNOG; arCOG03426; Archaea. DR eggNOG; COG2510; LUCA. DR KO; K08978; -. DR OMA; YKGKASI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR000620; EamA_dom. DR Pfam; PF00892; EamA; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 137 Uncharacterized protein MJ1333.1. FT /FTId=PRO_0000107279. FT TRANSMEM 4 26 Helical. {ECO:0000255}. FT TRANSMEM 35 57 Helical. {ECO:0000255}. FT TRANSMEM 62 84 Helical. {ECO:0000255}. FT TRANSMEM 89 111 Helical. {ECO:0000255}. FT TRANSMEM 116 135 Helical. {ECO:0000255}. FT DOMAIN 13 135 EamA. SQ SEQUENCE 137 AA; 14847 MW; 61C99BEDD5157636 CRC64; MDTAIILGLL VAVFYGVGTF FAKIVCEKNP LFQWIVVNIV GIILCLIILL KYKNIIITDQ KILTYAIISA VLVVIGSLLL YYALYKGKAS IVVPLSSIGP AITVALSILF LKETLTLPQM IGIVLIIIGI ILLSISN // ID YE6A_METJA Reviewed; 154 AA. AC P81329; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1469.1; GN OrderedLocusNames=MJ1469.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99490.1; -; Genomic_DNA. DR ProteinModelPortal; P81329; -. DR STRING; 243232.MJ_1469.1; -. DR EnsemblBacteria; AAB99490; AAB99490; MJ_1469.1. DR KEGG; mja:MJ_1469.1; -. DR eggNOG; arCOG04471; Archaea. DR eggNOG; COG4083; LUCA. DR OMA; ISFIIFP; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR026432; Archaeo_ArtD. DR InterPro; IPR026392; Exo/Archaeosortase_dom. DR TIGRFAMs; TIGR04175; archaeo_artD; 1. DR TIGRFAMs; TIGR04178; exo_archaeo; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 154 Uncharacterized protein MJ1469.1. FT /FTId=PRO_0000107355. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 57 77 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 125 145 Helical. {ECO:0000255}. SQ SEQUENCE 154 AA; 18128 MW; 0CC1081E2F38B045 CRC64; MGNKNAIYIL RFLIYFFIFY YILKMLEGNI MDLLTITLSK LLNLKFYKNE IIVGKNIIEI SSPCTCSLEM ALFLGYIFGT PDVPIKYKIS YSVFGLSIIT ISNILRIILI INYSNMINYN VVHDVISFII FPIALFLNWF WIYLLKMKKI IMFK // ID Y567_METJA Reviewed; 82 AA. AC Q57987; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 75. DE RecName: Full=Uncharacterized protein MJ0567; GN OrderedLocusNames=MJ0567; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98558.1; -; Genomic_DNA. DR PIR; G64370; G64370. DR ProteinModelPortal; Q57987; -. DR STRING; 243232.MJ_0567; -. DR EnsemblBacteria; AAB98558; AAB98558; MJ_0567. DR KEGG; mja:MJ_0567; -. DR eggNOG; arCOG02102; Archaea. DR eggNOG; COG1918; LUCA. DR InParanoid; Q57987; -. DR KO; K04758; -. DR OMA; RNQNGPV; -. DR PhylomeDB; Q57987; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046914; F:transition metal ion binding; IEA:InterPro. DR InterPro; IPR007167; Fe-transptr_FeoA. DR InterPro; IPR008988; Transcriptional_repressor_C. DR Pfam; PF04023; FeoA; 1. DR SMART; SM00899; FeoA; 1. DR SUPFAM; SSF50037; SSF50037; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 82 Uncharacterized protein MJ0567. FT /FTId=PRO_0000106934. SQ SEQUENCE 82 AA; 8766 MW; 3F3810EEFC9F81CE CRC64; MYPLAFAKEG EEVIVKKIDA GCGAMQRLVS MGINIGSKLK VIRNQNGPVI ISTKGSNIAI GRGLAMKIMV EDAEYGGENE KL // ID Y596_METJA Reviewed; 141 AA. AC Q58013; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0596; GN OrderedLocusNames=MJ0596; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98596.1; -; Genomic_DNA. DR PIR; D64374; D64374. DR ProteinModelPortal; Q58013; -. DR STRING; 243232.MJ_0596; -. DR EnsemblBacteria; AAB98596; AAB98596; MJ_0596. DR KEGG; mja:MJ_0596; -. DR eggNOG; arCOG03415; Archaea. DR eggNOG; ENOG410Y478; LUCA. DR OMA; PEYLPFD; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR022620; DUF2666. DR Pfam; PF10869; DUF2666; 1. DR ProDom; PD033097; DUF2666; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 141 Uncharacterized protein MJ0596. FT /FTId=PRO_0000106949. SQ SEQUENCE 141 AA; 16433 MW; 4E2A7CC57ACBEF3D CRC64; MEDKIEFMAK HKKWFVVKKL KIDENTEDIE IARLLASIDE TVLNKIPEYL PFDMNKLYEI ADGIYQKKKG RITEEEIAEV LKKLKSPATT RKLNEITESK EGKEILKAIL NNIILERLGI QTRVSPKVIE KYIENSQSSN R // ID Y599_METJA Reviewed; 199 AA. AC Q58016; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0599; GN OrderedLocusNames=MJ0599; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98597.1; -; Genomic_DNA. DR PIR; G64374; G64374. DR STRING; 243232.MJ_0599; -. DR EnsemblBacteria; AAB98597; AAB98597; MJ_0599. DR KEGG; mja:MJ_0599; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 199 Uncharacterized protein MJ0599. FT /FTId=PRO_0000106951. SQ SEQUENCE 199 AA; 24196 MW; 52D6E8D92BF19E0A CRC64; MQIKPFEENK PYPEWDPDEP DKVPGIPNWN RNFGNIIIEF DKGTRTCYYH RKKKNKYDVE CGDYRIKITY SQKNWNKKVV YDNDAWKWLV DCLDPTEINK FLCHLCKILD MNIDKDVYDY LINNVNFSVN NNDLRALLYY FWHRAIIEDR IYSQKKGYNG RKQVIGATYE VLKELRNNQN RVYLYEKCDE IYKMAKKKL // ID Y61A_METJA Reviewed; 197 AA. AC P81310; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0611.1; GN OrderedLocusNames=MJ0611.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98609.1; -; Genomic_DNA. DR ProteinModelPortal; P81310; -. DR STRING; 243232.MJ_0611.1; -. DR EnsemblBacteria; AAB98609; AAB98609; MJ_0611.1. DR KEGG; mja:MJ_0611.1; -. DR eggNOG; arCOG07501; Archaea. DR eggNOG; COG0671; LUCA. DR InParanoid; P81310; -. DR OMA; FWKISMH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 197 Uncharacterized protein MJ0611.1. FT /FTId=PRO_0000106958. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 55 75 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 143 163 Helical. {ECO:0000255}. FT TRANSMEM 177 197 Helical. {ECO:0000255}. SQ SEQUENCE 197 AA; 23180 MW; 73FCFB65007C0692 CRC64; MESIYLGNCW TPFNWIYAIY DVLVKILSIR EIFQILSLMY LLFLYIGFLL ISKFDISLSL AFFFPCVFWI CWAKIKNETW DIPNRKNRLV PLIFTLIYLS ILAIFWKNIF IIIFLVNVLV ILIITKFWKI SMHNYGLSAM AYLIYAFTNS IWLSTIYLIL VIITGYARIY LKKHTVSQVI AGTILGISVN YILLNLI // ID Y621_METJA Reviewed; 172 AA. AC Q58038; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized HTH-type transcriptional regulator MJ0621; GN OrderedLocusNames=MJ0621; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 1 HTH cro/C1-type DNA-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00257}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98616.1; -; Genomic_DNA. DR PIR; E64377; E64377. DR ProteinModelPortal; Q58038; -. DR STRING; 243232.MJ_0621; -. DR EnsemblBacteria; AAB98616; AAB98616; MJ_0621. DR KEGG; mja:MJ_0621; -. DR eggNOG; arCOG04375; Archaea. DR eggNOG; COG4800; LUCA. DR InParanoid; Q58038; -. DR OMA; ALVCAPI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.260.40; -; 1. DR InterPro; IPR001387; Cro/C1-type_HTH. DR InterPro; IPR010982; Lambda_DNA-bd_dom. DR InterPro; IPR016472; Tscrpt_reg_MJ0621_prd. DR Pfam; PF01381; HTH_3; 1. DR PIRSF; PIRSF005978; HTH_MJ0621_prd; 1. DR SMART; SM00530; HTH_XRE; 1. DR SUPFAM; SSF47413; SSF47413; 1. DR PROSITE; PS50943; HTH_CROC1; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 172 Uncharacterized HTH-type transcriptional FT regulator MJ0621. FT /FTId=PRO_0000149792. FT DOMAIN 21 75 HTH cro/C1-type. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. FT DNA_BIND 32 51 H-T-H motif. {ECO:0000255|PROSITE- FT ProRule:PRU00257}. SQ SEQUENCE 172 AA; 19263 MW; 4519725AD4020031 CRC64; MKACERLLLK IESQEKFVEE FKRILLELGL TLKEFSEISG IPYSTLYKVI QGKDFRVSTL IKILKTIRSF EKDENIDTIA IIAARPALNK ITTRKIGING KSYLIKEYPA NSLEECIVAA VRAEREGVKG IVCAPIVSAT IEKIVNVPVA VIIPEKDAFM KALEIIAKKI NE // ID Y628_METJA Reviewed; 166 AA. AC Q58045; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0628; GN OrderedLocusNames=MJ0628; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0992. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98627.1; -; Genomic_DNA. DR PIR; D64378; D64378. DR ProteinModelPortal; Q58045; -. DR STRING; 243232.MJ_0628; -. DR EnsemblBacteria; AAB98627; AAB98627; MJ_0628. DR KEGG; mja:MJ_0628; -. DR eggNOG; arCOG06576; Archaea. DR eggNOG; ENOG410ZEY3; LUCA. DR OMA; GRYYYAS; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 166 Uncharacterized protein MJ0628. FT /FTId=PRO_0000106962. SQ SEQUENCE 166 AA; 19743 MW; 4CFA7E0536F07C50 CRC64; MGQMFNPLDF VYIAEFLEES KVDKKEAKNR TIIGRYYYAS FLFLRGILKE NLKNYNSKEA KEFLYLIELS NSHKIILDFL NVLKKEDGKF RRVYNALSIL RDLRNASDYE LESPARVKSI KEMVDFNDDY YVELSKNKYK IIVNSKSDVE NILKDRSKID KILRKI // ID Y644_METJA Reviewed; 208 AA. AC Q58060; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 13-APR-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0644; GN OrderedLocusNames=MJ0644; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98638.1; -; Genomic_DNA. DR PIR; D64380; D64380. DR ProteinModelPortal; Q58060; -. DR STRING; 243232.MJ_0644; -. DR EnsemblBacteria; AAB98638; AAB98638; MJ_0644. DR KEGG; mja:MJ_0644; -. DR eggNOG; ENOG4102TAA; Archaea. DR eggNOG; COG0684; LUCA. DR InParanoid; Q58060; -. DR KO; K08093; -. DR OMA; VVDYEAS; -. DR PhylomeDB; Q58060; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.50.30.40; -; 1. DR InterPro; IPR005493; RraA/RraA-like. DR Pfam; PF03737; Methyltransf_6; 1. DR SUPFAM; SSF89562; SSF89562; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 208 Uncharacterized protein MJ0644. FT /FTId=PRO_0000106969. SQ SEQUENCE 208 AA; 22709 MW; 422F40333C23A9D5 CRC64; MKVLLKIIVG RAMNILKNFS VPNLCDAGAK PLNGIKPILE NQKLVFGEAI TVKISYNDWG TLIKTISFAK NKFIVAEVVG EGKYETAVWG GLASLNAKIK GVRGVVIDGC VRDVEDIKAL KFPVFAKNFC PNAGKPLNLG EINVAVNCCG VIVEPGDIIV GDCNGVVVIK KESLPEIIEN AKNIKEKERK IRERILRGQD LRDVLNLE // ID Y645_METJA Reviewed; 191 AA. AC Q58061; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 90. DE RecName: Full=Uncharacterized protein MJ0645; GN OrderedLocusNames=MJ0645; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98639.1; -; Genomic_DNA. DR PIR; E64380; E64380. DR ProteinModelPortal; Q58061; -. DR STRING; 243232.MJ_0645; -. DR EnsemblBacteria; AAB98639; AAB98639; MJ_0645. DR KEGG; mja:MJ_0645; -. DR eggNOG; arCOG01091; Archaea. DR eggNOG; COG1814; LUCA. DR InParanoid; Q58061; -. DR OMA; YSGTYDG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005381; F:iron ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0005384; F:manganese ion transmembrane transporter activity; IBA:GO_Central. DR GO; GO:0030026; P:cellular manganese ion homeostasis; IBA:GO_Central. DR GO; GO:0071281; P:cellular response to iron ion; IBA:GO_Central. DR GO; GO:0006880; P:intracellular sequestering of iron ion; IBA:GO_Central. DR GO; GO:0034755; P:iron ion transmembrane transport; IBA:GOC. DR GO; GO:0071421; P:manganese ion transmembrane transport; IBA:GO_Central. DR InterPro; IPR008217; Ccc1_fam. DR InterPro; IPR006682; CHP00267. DR Pfam; PF01988; VIT1; 2. DR TIGRFAMs; TIGR00267; TIGR00267; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 191 Uncharacterized protein MJ0645. FT /FTId=PRO_0000106970. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 51 71 Helical. {ECO:0000255}. FT TRANSMEM 114 134 Helical. {ECO:0000255}. FT TRANSMEM 139 159 Helical. {ECO:0000255}. FT TRANSMEM 167 187 Helical. {ECO:0000255}. SQ SEQUENCE 191 AA; 20046 MW; 7FB368CC3B48FE2F CRC64; MLRIPRSLKS IINTINGESG TRYIVRGLID GSLSALGVVI GASGSADASV IIAAGLGGGI ANGLSNILGA FTAEKASLER ERIQKEKSLL KKNGYLKKSI IYKKAIRETM ICGLIDGIST TIGSALPVVP FFLFDIKTAL YVAIGITIAI LFILGVFIGK ISKENVIISG IKMVAGALAV AILCFMIEKA F // ID Y650_METJA Reviewed; 692 AA. AC Q57852; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1997, sequence version 2. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0650; DE Flags: Precursor; GN OrderedLocusNames=MJ0650; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98647.1; -; Genomic_DNA. DR PIR; B64381; B64381. DR STRING; 243232.MJ_0650; -. DR EnsemblBacteria; AAB98647; AAB98647; MJ_0650. DR KEGG; mja:MJ_0650; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 692 Uncharacterized protein MJ0650. FT /FTId=PRO_0000013992. SQ SEQUENCE 692 AA; 80607 MW; 25D0A91A08177188 CRC64; MVNFMKRILI FFILFLLFCG SLKAHLIFYD KDVSQLKSLG FIGDYNGKYW LISDKCKLIK YNEIPILIVP SKPLNNIEII KWDKYRESWL IITNNESISN VSSDIYLLEG KKLIHFGRFN FLIEDIDDNG DYFLVSAFCP DKKSKIFIIY NNKSIEDINK YLNIKIDDFS FPKIKYIPNG NFWLIVTTTL EGQNCLIKFN GTYGEDISPK LNIPKPPNKM GCYNIIEDVD FNGTSYLIVG KFSKYKDRCN YILSYENNRS KIYKYNFDGH FKRVSWINNS WIVEIVNFSR DNSYSYEYYA LKNGKLKRIK VGESANFTPI VWYLGTYITD IAKINDNQYL ITLKSIEDFP KYPNIGALIK LTINNSKIDK KIIYKGKGLT SIGYNGKYCL IGGKGVLLLY NGKNITDLTK RANISNSDLI SSIAYGKDCW LIGLDEVNLH YPSKSLIKFD GKKFYDLTNI SNITICKILK SNKEYILIGT KNVLIKYNGS FITIINYTNY EKYGLCYIFE AMDYNPKERY WLVGGVCLYN HPYSSDAILY KVYDNGSYES LPINDNLHKI YGDFGFALVS LIKYIPKNNS FLIKVWVGLN DHWLIYKNNT LTEFVTQKNP GSIEIDNYTL YIFNYYNTIE IYDNNKLLST VELIDIPKET VCVEEYHYKE KSSYNNYLYI LIFIILTIIA IYIVVKINKK LT // ID Y659_METJA Reviewed; 138 AA. AC Q58073; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0659; GN OrderedLocusNames=MJ0659; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98658.1; -; Genomic_DNA. DR PIR; C64382; C64382. DR ProteinModelPortal; Q58073; -. DR EnsemblBacteria; AAB98658; AAB98658; MJ_0659. DR KEGG; mja:MJ_0659; -. DR eggNOG; arCOG09670; Archaea. DR eggNOG; ENOG41111B7; LUCA. DR OMA; LIEKGYC; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 1. DR InterPro; IPR011990; TPR-like_helical_dom. DR SUPFAM; SSF48452; SSF48452; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 138 Uncharacterized protein MJ0659. FT /FTId=PRO_0000106976. SQ SEQUENCE 138 AA; 15470 MW; 96A8AE06757D563C CRC64; MVSEIIKLIE EGKIEEVLKK VEEIKGDAQL EIIALTLIEK GYCDEAVKVA EKISSFGLKD EVLRKVAIAY IENGEIDKAM ALVEKIKTET DLEKIAMKLI EIKKYREALK VAEKIKSRAI KEGILMAIIN ALLDELGK // ID Y661_METJA Reviewed; 182 AA. AC Q58075; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0661; GN OrderedLocusNames=MJ0661; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To H.pylori HP0274. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98654.1; -; Genomic_DNA. DR PIR; E64382; E64382. DR STRING; 243232.MJ_0661; -. DR EnsemblBacteria; AAB98654; AAB98654; MJ_0661. DR KEGG; mja:MJ_0661; -. DR eggNOG; arCOG02579; Archaea. DR eggNOG; COG0727; LUCA. DR InParanoid; Q58075; -. DR KO; K06940; -. DR OMA; DEEYYKH; -. DR PhylomeDB; Q58075; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR005358; Puta_zinc/iron-chelating_dom. DR Pfam; PF03692; CxxCxxCC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 182 Uncharacterized protein MJ0661. FT /FTId=PRO_0000106978. SQ SEQUENCE 182 AA; 21570 MW; 01E6F47F37008AFE CRC64; MESVRRGKLM KNKKIKFDVY LNGIAYHCIK CGFCCDAPTV TKKDLAKIAG YLKIPFDEVL KRYVRFFNGY IGELKEVGGK CIFLDKKTKK CKIYKVRPLI CRLRPYSVQV RNGKLTLTYD IWFLRYCRGL YLGDGKVEDE YFKYAELVLK YLGFEEGVDE EEFKRAKERL LEESLKYRKK KD // ID Y675_METJA Reviewed; 391 AA. AC Q58088; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 16-MAR-2016, entry version 77. DE RecName: Full=Uncharacterized protein MJ0675; GN OrderedLocusNames=MJ0675; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98669.1; -; Genomic_DNA. DR PIR; C64384; C64384. DR ProteinModelPortal; Q58088; -. DR STRING; 243232.MJ_0675; -. DR EnsemblBacteria; AAB98669; AAB98669; MJ_0675. DR KEGG; mja:MJ_0675; -. DR eggNOG; arCOG00913; Archaea. DR eggNOG; COG1568; LUCA. DR KO; K07057; -. DR OMA; IDQSFAT; -. DR PhylomeDB; Q58088; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IEA:InterPro. DR GO; GO:0006596; P:polyamine biosynthetic process; IEA:InterPro. DR Gene3D; 1.10.10.10; -; 1. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR014435; BpsA. DR InterPro; IPR002723; BpsA_C. DR InterPro; IPR029063; SAM-dependent_MTases. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR Pfam; PF01861; DUF43; 1. DR PIRSF; PIRSF005895; UCP005895_mtase; 1. DR SUPFAM; SSF46785; SSF46785; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 391 Uncharacterized protein MJ0675. FT /FTId=PRO_0000106985. SQ SEQUENCE 391 AA; 44553 MW; 08DCBF6899EC9A6B CRC64; MKIIGKIGKG KVEVNEKTKF SILLNNVAKK ADIAEGKRAV EDIIRVIYRH QPISTKKIAQ KTRLPLPIVA KVRTILEREK ILKRTERGAE LTDLGKEFAE NFLKLKYKKS LTCKTCNGRG IVLDEFFEDI LNKVRVWAKR RPLVDTTIDQ SFATPETSTY RAALMYERGD LEGKRILFVG DDDLTSLPTA LTNMAEEIAV VDIDERILKL IEKFSQKEGV KIKTIKHDLR NPLPQDLKER FDVISTDPPY TVDGLKLFLS RGIEALGKEG IAYLSYSHKP IDEWLSIQKA ITNMGFVISE LIPNFNYYEG SEIIANTTFI ARLVGKNLKI NIGDTEKIYT GLVKPVIRYY KCLKCGKIHK VGEEVKKVED LVCECGGKKF KMIKREKLKN E // ID Y678_METJA Reviewed; 320 AA. AC Q58091; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 83. DE RecName: Full=Uncharacterized protein MJ0678; GN OrderedLocusNames=MJ0678; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98673.1; -; Genomic_DNA. DR PIR; F64384; F64384. DR ProteinModelPortal; Q58091; -. DR STRING; 243232.MJ_0678; -. DR EnsemblBacteria; AAB98673; AAB98673; MJ_0678. DR KEGG; mja:MJ_0678; -. DR eggNOG; arCOG02264; Archaea. DR eggNOG; COG1808; LUCA. DR InParanoid; Q58091; -. DR OMA; IHSRITL; -. DR PhylomeDB; Q58091; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR005240; DUF389. DR Pfam; PF04087; DUF389; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 320 Uncharacterized protein MJ0678. FT /FTId=PRO_0000106986. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 131 151 Helical. {ECO:0000255}. FT TRANSMEM 169 189 Helical. {ECO:0000255}. FT TRANSMEM 200 220 Helical. {ECO:0000255}. FT TRANSMEM 228 248 Helical. {ECO:0000255}. FT TRANSMEM 260 280 Helical. {ECO:0000255}. FT TRANSMEM 299 319 Helical. {ECO:0000255}. SQ SEQUENCE 320 AA; 35674 MW; 92BBB732DFBF7705 CRC64; MKLRFIECHI PKHLFMGIDE IREWDGVIWA NVKTNGTIST IQILTTLKDS EKIVDKLKEM YGGANYRVVV FEPTMTYPPI EEEEEKEEPE RLIREELYNI ASDIANLSKE NMLMLILSTI VAIAGIYKDD VALLIASMII APLLGPNIAL SLSITVADYK LALKSIKTLI AELIFVIILS MIAGHYLPIS LDNPQIHSRI TLDFWSIIIA LSAGIAGSLS TVSNISSIAV GVMIAIALLP PLAVFGLLIG AGYVEQSFSA LILFLINMIA INLSAIVIFS AYGISPYRWW KKEEARKYTL YAILLWVTLF IAIFVLIIYH // ID Y685_METJA Reviewed; 253 AA. AC Q58098; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized ATP-binding protein MJ0685; GN OrderedLocusNames=MJ0685; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0084 and MJ0823. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98680.1; -; Genomic_DNA. DR PIR; E64385; E64385. DR ProteinModelPortal; Q58098; -. DR STRING; 243232.MJ_0685; -. DR PRIDE; Q58098; -. DR EnsemblBacteria; AAB98680; AAB98680; MJ_0685. DR KEGG; mja:MJ_0685; -. DR eggNOG; arCOG00587; Archaea. DR eggNOG; COG3640; LUCA. DR InParanoid; Q58098; -. DR KO; K07321; -. DR OMA; PEGPGCY; -. DR PhylomeDB; Q58098; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR002586; CobQ/CobB/MinD/ParA_Nub-bd_dom. DR InterPro; IPR014433; CooC. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF01656; CbiA; 1. DR PIRSF; PIRSF005647; CooC; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 4: Predicted; KW ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome. FT CHAIN 1 253 Uncharacterized ATP-binding protein FT MJ0685. FT /FTId=PRO_0000106988. FT NP_BIND 7 14 ATP. {ECO:0000255}. SQ SEQUENCE 253 AA; 28585 MW; A48824E3DC0A8E5D CRC64; MIIAVSGKGG VGKTAFTTLL IKALSKKTNS ILVVDADPDS NLPETLGVEV EKTVGDIREE LKKLVERDEI PAGMTKLDYL RSKIFEILVE TKYYDLLVMG RPEGSGCYCS VNNWLRQIID NLAKDYEFVV IDTEAGLEHL SRRTTQNVDV MIVITDASKR GLGTAKRIKK LANELEVKFK DIYVVANKVK PEYEELIDNY AKELGLNLIG KLPYNKEIAE YDLKGIPLWN LPENNEVYKK VEEIAEKIIN KKF // ID Y695_METJA Reviewed; 108 AA. AC Q58106; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 67. DE RecName: Full=Uncharacterized protein MJ0695; DE Flags: Precursor; GN OrderedLocusNames=MJ0695; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0803. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98696.1; -; Genomic_DNA. DR PIR; G64386; G64386. DR STRING; 243232.MJ_0695; -. DR EnsemblBacteria; AAB98696; AAB98696; MJ_0695. DR KEGG; mja:MJ_0695; -. DR eggNOG; arCOG10950; Archaea. DR eggNOG; ENOG41111A6; LUCA. DR OMA; FYKWDEF; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 108 Uncharacterized protein MJ0695. FT /FTId=PRO_0000013993. SQ SEQUENCE 108 AA; 13250 MW; CF0051894326A911 CRC64; MNLWEFRFGK SFLFIPNFIM KVLAFEELAL FDIFDSLINV KINIYENGIE CGFSFYKWDE FKGYKIEDKY IRLISKFPLI IRLIFVRDIY LRYDEELEGI IEKHLRQK // ID Y699_METJA Reviewed; 380 AA. AC Q58110; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 76. DE RecName: Full=Uncharacterized protein MJ0699; GN OrderedLocusNames=MJ0699; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98692.1; -; Genomic_DNA. DR PIR; C64387; C64387. DR ProteinModelPortal; Q58110; -. DR STRING; 243232.MJ_0699; -. DR EnsemblBacteria; AAB98692; AAB98692; MJ_0699. DR KEGG; mja:MJ_0699; -. DR eggNOG; arCOG00692; Archaea. DR eggNOG; COG0402; LUCA. DR InParanoid; Q58110; -. DR OMA; CPRSNLV; -. DR PhylomeDB; Q58110; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0004000; F:adenosine deaminase activity; IBA:GO_Central. DR GO; GO:0050270; F:S-adenosylhomocysteine deaminase activity; IBA:GO_Central. DR GO; GO:0019700; P:organic phosphonate catabolic process; IBA:GO_Central. DR Gene3D; 2.30.40.10; -; 1. DR InterPro; IPR006680; Amidohydro-rel. DR InterPro; IPR011059; Metal-dep_hydrolase_composite. DR InterPro; IPR032466; Metal_Hydrolase. DR Pfam; PF01979; Amidohydro_1; 1. DR SUPFAM; SSF51556; SSF51556; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 380 Uncharacterized protein MJ0699. FT /FTId=PRO_0000106994. SQ SEQUENCE 380 AA; 43053 MW; 6AC180A4A0EA7E99 CRC64; MVVFLLLKSQ FLYGEDFKLR KGTLIIEEGI IKGFTDEHNE REVIEFKGLV IPSLINAHTH IADNSIKDIG INKTLDELVK PPNGLKHRYL TECSDDLLAE GMKLGLGDMR EHGIKYFCDF RENGVRGISL LNKALKCYDY PKAIILGRPI KVDKDEIEEV LKVSNGLGLS GANEFKDDEL KLIFKIFKKF KEKDDKKLFA IHAAEHRGAV EYSLNKYGMT EVERLIDLKI KPDFIVHGTH LTDNDLELLK ENNIPVVACV RANLSFNVGM PKLNELNDNL LVGIGTDNFM ANSPSIFKEM DFIYKLYHIE PKDILRMATI NNAKILKLEN VGLVDEGFKA VFTFIKPTNA ILFSKNIIAS VVTRCEKGDV VDFSLMENEE // ID Y700_METJA Reviewed; 324 AA. AC Q58111; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 90. DE RecName: Full=Uncharacterized MscS family protein MJ0700; GN OrderedLocusNames=MJ0700; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98693.1; -; Genomic_DNA. DR PIR; D64387; D64387. DR ProteinModelPortal; Q58111; -. DR STRING; 243232.MJ_0700; -. DR EnsemblBacteria; AAB98693; AAB98693; MJ_0700. DR KEGG; mja:MJ_0700; -. DR eggNOG; arCOG01569; Archaea. DR eggNOG; COG0668; LUCA. DR InParanoid; Q58111; -. DR OMA; WIYILAR; -. DR PhylomeDB; Q58111; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0055085; P:transmembrane transport; IEA:InterPro. DR InterPro; IPR010920; LSM_dom. DR InterPro; IPR006685; MscS_channel. DR InterPro; IPR011014; MscS_channel_TM-2. DR Pfam; PF00924; MS_channel; 1. DR SUPFAM; SSF50182; SSF50182; 1. DR SUPFAM; SSF82861; SSF82861; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 324 Uncharacterized MscS family protein FT MJ0700. FT /FTId=PRO_0000110255. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 42 62 Helical. {ECO:0000255}. FT TRANSMEM 80 100 Helical. {ECO:0000255}. FT TRANSMEM 116 136 Helical. {ECO:0000255}. SQ SEQUENCE 324 AA; 37260 MW; E3A76D3F1F5BAEB4 CRC64; MIDNKLKLVI KVVLLIFLLH SLMSIFNLET YIKILAKYQN QIMIIAIIIL SGLIIVDIAS EVFKKYARTR EEKAGEYLTL NYIFKYLVYV CVTLMIFGVI YQNVSSLVVS VGLIGAAVTY ALQKPILNFA GWIIILYTRT IKIGDRIFIK NMGAGDVFDI DTQHIYLSEL TTDTFEPTGR VLIIPNSYIF TASIENLTKG SPYIWDNIVV HFTLNSNINK AEKIVFESAD EVIGNLMREL YEKWSKRKYL ISRKLSDKPV VRVGITRSSF YIKALYLVNV YEKAKIRSEI NKRILEKVNK ENDVKLAYPH IKAVIETENK FKNT // ID Y703_METJA Reviewed; 226 AA. AC Q58114; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 87. DE RecName: Full=Uncharacterized protein MJ0703; GN OrderedLocusNames=MJ0703; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HisA/HisF family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98695.1; -; Genomic_DNA. DR PIR; G64387; G64387. DR ProteinModelPortal; Q58114; -. DR STRING; 243232.MJ_0703; -. DR EnsemblBacteria; AAB98695; AAB98695; MJ_0703. DR KEGG; mja:MJ_0703; -. DR eggNOG; arCOG00616; Archaea. DR eggNOG; COG1411; LUCA. DR InParanoid; Q58114; -. DR KO; K01814; -. DR OMA; IGTTIHN; -. DR PhylomeDB; Q58114; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005622; C:intracellular; IBA:GO_Central. DR GO; GO:0003949; F:1-(5-phosphoribosyl)-5-[(5-phosphoribosylamino)methylideneamino]imidazole-4-carboxamide isomerase activity; IBA:GO_Central. DR GO; GO:0000105; P:histidine biosynthetic process; IBA:GO_Central. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR006062; His_biosynth. DR InterPro; IPR004650; HisAF-rel. DR InterPro; IPR011060; RibuloseP-bd_barrel. DR Pfam; PF00977; His_biosynth; 1. DR SUPFAM; SSF51366; SSF51366; 1. DR TIGRFAMs; TIGR00734; hisAF_rel; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 226 Uncharacterized protein MJ0703. FT /FTId=PRO_0000142292. SQ SEQUENCE 226 AA; 25067 MW; 0B26652F68FF54EE CRC64; MKIIPVIDLK DKIAVHGKSG NRDEYKPLES VICKSSNPIE VAKAYKERGA KTIYIADLNF IMGNGDNFDI IKEIDFINKI VDIGVKSRED LETIKKVLNK DDRAIVATET LKDIELLKEK DIVVSLDFKN GNLLNYSLDE ILSCVRDDTP LIILDISSVG TQRGVNAELI KYVLDKTNNP VYVGGGIKGM EDLELCYNLG VDAVLIATAI HKGVLDLEEI INKFGD // ID Y706_METJA Reviewed; 214 AA. AC Q58117; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 77. DE RecName: Full=Uncharacterized protein MJ0706; GN OrderedLocusNames=MJ0706; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98700.1; -; Genomic_DNA. DR PIR; B64388; B64388. DR ProteinModelPortal; Q58117; -. DR STRING; 243232.MJ_0706; -. DR TCDB; 9.B.98.1.5; the duf95 (duf95) family. DR DNASU; 1451574; -. DR EnsemblBacteria; AAB98700; AAB98700; MJ_0706. DR KEGG; mja:MJ_0706; -. DR eggNOG; arCOG01994; Archaea. DR eggNOG; COG1300; LUCA. DR OMA; TFRIIPH; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002798; SpoIIM-like. DR Pfam; PF01944; SpoIIM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 214 Uncharacterized protein MJ0706. FT /FTId=PRO_0000106998. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 104 124 Helical. {ECO:0000255}. FT TRANSMEM 132 152 Helical. {ECO:0000255}. FT TRANSMEM 153 173 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. SQ SEQUENCE 214 AA; 24497 MW; BA53797337D0304F CRC64; MRDAYLMMVL MDALKEIFDL KEILKSPIRN KKVILFVSLV FILSLVLLYI LVVNIKYFSY LGDIIFQNFQ KHVENLKITL NEDNLHIILA IWKNNLTVCI LNYILGIFSL FVIAVNSYIL SYVLYKFGAE SFIYLVLPHG IIEIPALILS ASGGVLFNMG LVNFLINIKF GTKREVLYYI KESLKLLILS IILFIVAGIV EGTITFKIAK IMFS // ID Y738_METJA Reviewed; 90 AA. AC Q58148; DT 27-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0738; GN OrderedLocusNames=MJ0738; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98733.1; -; Genomic_DNA. DR PIR; B64392; B64392. DR ProteinModelPortal; Q58148; -. DR STRING; 243232.MJ_0738; -. DR EnsemblBacteria; AAB98733; AAB98733; MJ_0738. DR KEGG; mja:MJ_0738; -. DR eggNOG; arCOG02797; Archaea. DR eggNOG; COG4746; LUCA. DR OMA; TNHPLYE; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.238.80; -; 1. DR InterPro; IPR024093; Uncharacterised_MTH865. DR Pfam; PF07747; MTH865; 1. DR SUPFAM; SSF69025; SSF69025; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 90 Uncharacterized protein MJ0738. FT /FTId=PRO_0000107009. SQ SEQUENCE 90 AA; 10276 MW; 121DAA6854FBF3ED CRC64; MMITTNHPLY EALRDIQEFK LRLVEYFKDK DVFPIKNKVE LAEALPCGIS LPCGEIEAAE LVKLLTDNDF PIKDPEDLAM KLANKCPIKQ // ID Y742_METJA Reviewed; 104 AA. AC Q58152; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0742; GN OrderedLocusNames=MJ0742; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ1511. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98736.1; -; Genomic_DNA. DR PIR; F64392; F64392. DR PDB; 3D7I; X-ray; 1.75 A; A/B/C=1-104. DR PDBsum; 3D7I; -. DR ProteinModelPortal; Q58152; -. DR SMR; Q58152; 7-104. DR STRING; 243232.MJ_0742; -. DR EnsemblBacteria; AAB98736; AAB98736; MJ_0742. DR KEGG; mja:MJ_0742; -. DR eggNOG; arCOG02148; Archaea. DR eggNOG; COG0599; LUCA. DR OMA; VASKCDE; -. DR PhylomeDB; Q58152; -. DR EvolutionaryTrace; Q58152; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051920; F:peroxiredoxin activity; IEA:InterPro. DR Gene3D; 1.20.1290.10; -; 1. DR InterPro; IPR029032; AhpD-like. DR InterPro; IPR003779; CMD-like. DR Pfam; PF02627; CMD; 1. DR SUPFAM; SSF69118; SSF69118; 1. PE 1: Evidence at protein level; KW 3D-structure; Complete proteome; Reference proteome. FT CHAIN 1 104 Uncharacterized protein MJ0742. FT /FTId=PRO_0000107011. FT HELIX 9 17 {ECO:0000244|PDB:3D7I}. FT HELIX 19 32 {ECO:0000244|PDB:3D7I}. FT STRAND 36 38 {ECO:0000244|PDB:3D7I}. FT HELIX 40 52 {ECO:0000244|PDB:3D7I}. FT HELIX 57 71 {ECO:0000244|PDB:3D7I}. FT HELIX 75 89 {ECO:0000244|PDB:3D7I}. FT HELIX 91 103 {ECO:0000244|PDB:3D7I}. SQ SEQUENCE 104 AA; 11703 MW; AD2E2BED3D563A82 CRC64; MKNEVFFGEG MKVVKEKYPD LYDIIVKLND TVFTGKTLDY KTQKLIAIGI VASRCDEVAI EKQMKSAMKE LGITKEEIAD VLRVVLLTSG MPAFTKAMKI LEKL // ID Y750_METJA Reviewed; 238 AA. AC Q58160; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 102. DE RecName: Full=Uncharacterized protein MJ0750; GN OrderedLocusNames=MJ0750; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Contains 2 4Fe-4S ferredoxin-type domains. CC {ECO:0000255|PROSITE-ProRule:PRU00711}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98746.1; -; Genomic_DNA. DR PIR; F64393; F64393. DR ProteinModelPortal; Q58160; -. DR STRING; 243232.MJ_0750; -. DR EnsemblBacteria; AAB98746; AAB98746; MJ_0750. DR KEGG; mja:MJ_0750; -. DR eggNOG; arCOG02772; Archaea. DR eggNOG; COG0348; LUCA. DR InParanoid; Q58160; -. DR KO; K02574; -. DR OMA; ECKSACK; -. DR PhylomeDB; Q58160; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IEA:UniProtKB-KW. DR InterPro; IPR017896; 4Fe4S_Fe-S-bd. DR InterPro; IPR017900; 4Fe4S_Fe_S_CS. DR Pfam; PF12801; Fer4_5; 3. DR PROSITE; PS00198; 4FE4S_FER_1; 1. DR PROSITE; PS51379; 4FE4S_FER_2; 2. PE 3: Inferred from homology; KW 4Fe-4S; Cell membrane; Complete proteome; Electron transport; Iron; KW Iron-sulfur; Membrane; Metal-binding; Reference proteome; Repeat; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 238 Uncharacterized protein MJ0750. FT /FTId=PRO_0000159312. FT TRANSMEM 13 33 Helical. {ECO:0000255}. FT TRANSMEM 40 60 Helical. {ECO:0000255}. FT TRANSMEM 107 127 Helical. {ECO:0000255}. FT TRANSMEM 140 160 Helical. {ECO:0000255}. FT DOMAIN 178 208 4Fe-4S ferredoxin-type 1. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT DOMAIN 204 233 4Fe-4S ferredoxin-type 2. FT {ECO:0000255|PROSITE-ProRule:PRU00711}. FT METAL 188 188 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 191 191 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 194 194 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. FT METAL 198 198 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 213 213 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 216 216 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 219 219 Iron-sulfur 2 (4Fe-4S). {ECO:0000250}. FT METAL 223 223 Iron-sulfur 1 (4Fe-4S). {ECO:0000250}. SQ SEQUENCE 238 AA; 27777 MW; 6B4F7FB996E941EF CRC64; MDKIQILRKI SQTLFFIYFV FLTSFCLCFF GIIEKFILKG SVGQLIAKLV VIVVLTLILG RVFCGWMCPL GFLFELMYKL RMKLFMKKKL PTVNEEVHNK LIYLRYVVLI LSLVLTYYLS IYAFCQVCPI GFLTNLYGTV ISLIILIFFL SLSFFVPMAF CRYFCPLGAF LSIFSIKPFF QLKTNNNCVK CKLCEFKCPM QIKITEKLDQ KECIRCFECK SSCKKDALSF SYAFKKRS // ID Y753_METJA Reviewed; 210 AA. AC Q58163; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0753; DE Flags: Precursor; GN OrderedLocusNames=MJ0753; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98755.1; -; Genomic_DNA. DR PIR; A64394; A64394. DR ProteinModelPortal; Q58163; -. DR STRING; 243232.MJ_0753; -. DR EnsemblBacteria; AAB98755; AAB98755; MJ_0753. DR KEGG; mja:MJ_0753; -. DR eggNOG; arCOG05048; Archaea. DR eggNOG; ENOG410Y003; LUCA. DR OMA; CGRYIDT; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 24 {ECO:0000255}. FT CHAIN 25 210 Uncharacterized protein MJ0753. FT /FTId=PRO_0000013994. SQ SEQUENCE 210 AA; 23606 MW; F17A00F449E214B2 CRC64; MKNMKIINKI VAILLLFSIL SLSFAWNDCP YGRVNCTYPG ECGRYIDTNH NGICDHSEPP PTTTIKTTNN EEEIKTSNVS SLELTEELIN EYVGISGKEL KSYTIKQVCD KYGISPKCLK EKLNINVPDD TTFGEIKEVY GIPPSVIKKA IVECMIEEGK IKLNTTNTID NNRDLNNNNS GNEKVGNTIL DKIVSFLFST INLRDLLFKF // ID Y760_METJA Reviewed; 275 AA. AC Q58170; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 82. DE RecName: Full=Uncharacterized protein MJ0760; GN OrderedLocusNames=MJ0760; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98751.1; -; Genomic_DNA. DR PIR; H64394; H64394. DR ProteinModelPortal; Q58170; -. DR STRING; 243232.MJ_0760; -. DR DNASU; 1451637; -. DR EnsemblBacteria; AAB98751; AAB98751; MJ_0760. DR KEGG; mja:MJ_0760; -. DR eggNOG; arCOG02066; Archaea. DR eggNOG; ENOG4102TN8; Archaea. DR eggNOG; COG0425; LUCA. DR eggNOG; COG2044; LUCA. DR KO; K07092; -. DR OMA; KPTIFLM; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.30.110.40; -; 1. DR Gene3D; 3.40.1260.10; -; 1. DR InterPro; IPR027396; DsrEFH-like. DR InterPro; IPR003787; Sulphur_relay_DrsE/F-like. DR InterPro; IPR001455; TusA-like. DR Pfam; PF02635; DrsE; 1. DR Pfam; PF01206; TusA; 1. DR SUPFAM; SSF64307; SSF64307; 1. DR SUPFAM; SSF75169; SSF75169; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 275 Uncharacterized protein MJ0760. FT /FTId=PRO_0000107019. SQ SEQUENCE 275 AA; 30542 MW; 7E81636BD7CAEFB3 CRC64; MIRMIRKFKV KGLRSPSLLI DMILNDTEEG ILVVETDGEE QIKDIEKLLK KYNLKYEVDG NVVKIYVGEI KADKTINVVG ATCPGPIMMV SDMLSKMKNG EILEIICGKN SLTDLTEGLK GMGNEIIKVE DKGDGTYRIL VKKGEKKEEK AAVTKIDELF IINTTGTGNA EKAYATFMMA DVALKMNLKP TIFLMMDGAS LALKGECDRV KHPAFPKLGD LVRDILSKGV KIYVCELSAE FRGINEKNLE EGFEIAGAPT FLNYLSKPNV RPVWL // ID Y761_METJA Reviewed; 251 AA. AC Q58171; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 87. DE RecName: Full=Uncharacterized metal-dependent hydrolase MJ0761 {ECO:0000305}; DE EC=3.1.-.- {ECO:0000305}; GN OrderedLocusNames=MJ0761; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240; CC Evidence={ECO:0000250|UniProtKB:P0AFQ7}; CC Note=Binds 2 divalent metal cations per subunit. CC {ECO:0000250|UniProtKB:P0AFQ7}; CC -!- SIMILARITY: Belongs to the TatD-type hydrolase family. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98752.1; -; Genomic_DNA. DR PIR; A64395; A64395. DR ProteinModelPortal; Q58171; -. DR STRING; 243232.MJ_0761; -. DR EnsemblBacteria; AAB98752; AAB98752; MJ_0761. DR KEGG; mja:MJ_0761; -. DR eggNOG; arCOG00892; Archaea. DR eggNOG; COG1099; LUCA. DR InParanoid; Q58171; -. DR KO; K07051; -. DR OMA; ETIITCA; -. DR PhylomeDB; Q58171; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016888; F:endodeoxyribonuclease activity, producing 5'-phosphomonoesters; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR018228; DNase_TatD-rel_CS. DR InterPro; IPR032466; Metal_Hydrolase. DR InterPro; IPR001130; TatD_family. DR InterPro; IPR012022; UCP005295. DR PANTHER; PTHR10060; PTHR10060; 1. DR Pfam; PF01026; TatD_DNase; 1. DR PIRSF; PIRSF005295; UCP005295_TatD; 1. DR SUPFAM; SSF51556; SSF51556; 1. DR PROSITE; PS01137; TATD_1; 1. PE 3: Inferred from homology; KW Complete proteome; Hydrolase; Metal-binding; Reference proteome. FT CHAIN 1 251 Uncharacterized metal-dependent hydrolase FT MJ0761. FT /FTId=PRO_0000202011. FT METAL 5 5 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 7 7 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 101 101 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 101 101 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 132 132 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 163 163 Divalent metal cation 2. FT {ECO:0000250|UniProtKB:P0AFQ7}. FT METAL 209 209 Divalent metal cation 1. FT {ECO:0000250|UniProtKB:P0AFQ7}. SQ SEQUENCE 251 AA; 28838 MW; ADE2B8F498D57970 CRC64; MIDAHTHLDV RSFEDLEKMA LSGIETIITC AHDPYKMSTP EVYLDHWDRL INLEVKRGEM AGVEVKVAVG VHPMGYPKNW EVLIKKLPEF LDNENVVAIG ETGLHYLTED EKNLLREQLY LAKDYNMPII IHTPEKNKKE ALIEILKILD EVKIKDSLVM IDHINKETVD LIDRDVYVGL TVQPSMKLTH EEAAEIIKNY NKKFILSSDL GSLKADIYAL PRTKLYMKNI GVDEEKIIAS VYKNAKGFYR L // ID Y773_METJA Reviewed; 175 AA. AC Q58183; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0773; DE Flags: Precursor; GN OrderedLocusNames=MJ0773; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98777.1; -; Genomic_DNA. DR PIR; E64396; E64396. DR ProteinModelPortal; Q58183; -. DR STRING; 243232.MJ_0773; -. DR EnsemblBacteria; AAB98777; AAB98777; MJ_0773. DR KEGG; mja:MJ_0773; -. DR eggNOG; arCOG05050; Archaea. DR eggNOG; ENOG410YCHB; LUCA. DR OMA; ILHYVLI; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.10.10; -; 1. DR InterPro; IPR011991; WHTH_DNA-bd_dom. DR SUPFAM; SSF46785; SSF46785; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 33 {ECO:0000255}. FT CHAIN 34 175 Uncharacterized protein MJ0773. FT /FTId=PRO_0000013997. SQ SEQUENCE 175 AA; 20247 MW; 63EE09A737EE4F11 CRC64; MERLPYEIVS TIFRKAILHY VLIRGTTYPQ SLAENLNISK GLASSFLRLC SALNIMKRER AGHKVLYSFT SKGLAILKRL APEIFDLSFS SVFEQLPKKK IATKYYPVDK IGFEISWKED KLGGIVFSFF DSNGEHLGDV FRSNKGYWWC VICQSDTCKH IDYLKRLYKT LKNQD // ID Y779_METJA Reviewed; 299 AA. AC Q58189; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0779; GN OrderedLocusNames=MJ0779; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98769.1; -; Genomic_DNA. DR PIR; C64397; C64397. DR STRING; 243232.MJ_0779; -. DR EnsemblBacteria; AAB98769; AAB98769; MJ_0779. DR KEGG; mja:MJ_0779; -. DR eggNOG; arCOG01811; Archaea. DR eggNOG; COG2064; LUCA. DR InParanoid; Q58189; -. DR KO; K07333; -. DR OMA; NRMIITC; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR018076; T2SS_F. DR Pfam; PF00482; T2SSF; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 299 Uncharacterized protein MJ0779. FT /FTId=PRO_0000107030. FT TRANSMEM 32 52 Helical. {ECO:0000255}. FT TRANSMEM 56 76 Helical. {ECO:0000255}. FT TRANSMEM 199 219 Helical. {ECO:0000255}. FT TRANSMEM 220 240 Helical. {ECO:0000255}. FT TRANSMEM 246 266 Helical. {ECO:0000255}. FT TRANSMEM 273 293 Helical. {ECO:0000255}. SQ SEQUENCE 299 AA; 33291 MW; 2251166CDB6BFAD5 CRC64; MPKYLTTLYK RTIKRNIILF KKLGKDFDEK KFILLLIIIA AIPLLISYYL HLTLKSMIIF VVIYVGAALF IPSILYENKI ETLENNIPQA LYIMILALES GRSINEALLE VVKSNIKEVS DIFRKVLYLM ENQKLSFEES MTIVSNLYDS KVLRMLARIM IENRKYGGDL SDSLKILAKT LEDFKMYKRQ LLSVTASGLA IGFIILCGVI PAVAALLGAY LIAVSGMLSG VAPIPPVKPE DISKGFEIVQ MGTAIIGALF AIPIFGLKIG RMFLISAVTM TIGVLAYYTI LKFAPGIFS // ID Y785_METJA Reviewed; 375 AA. AC Q58195; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized protein MJ0785; GN OrderedLocusNames=MJ0785; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98782.1; -; Genomic_DNA. DR PIR; A64398; A64398. DR ProteinModelPortal; Q58195; -. DR STRING; 243232.MJ_0785; -. DR EnsemblBacteria; AAB98782; AAB98782; MJ_0785. DR KEGG; mja:MJ_0785; -. DR eggNOG; arCOG00658; Archaea. DR eggNOG; COG0502; LUCA. DR InParanoid; Q58195; -. DR KO; K01012; -. DR OMA; IPDNHPM; -. DR PhylomeDB; Q58195; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:InterPro. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR010722; BATS_dom. DR InterPro; IPR006638; Elp3/MiaB/NifB. DR InterPro; IPR007197; rSAM. DR InterPro; IPR023858; RSAM_HmdB. DR Pfam; PF06968; BATS; 1. DR Pfam; PF04055; Radical_SAM; 1. DR SMART; SM00876; BATS; 1. DR SMART; SM00729; Elp3; 1. DR TIGRFAMs; TIGR03957; rSAM_HmdB; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 375 Uncharacterized protein MJ0785. FT /FTId=PRO_0000185568. FT COMPBIAS 23 31 Glu-rich. SQ SEQUENCE 375 AA; 42810 MW; 1467DF2B76A89999 CRC64; MKYTYKISKV KISGDLMVFG KIEEEFKEFL ESRRKYNEFI KNGLIDEDEA LKLFKIDNWR DYLKLFDIAS RVRDYFKKKI EITSTIHITN ICHVNPKCLY CGFAAGTSKE GYYEPFRLTD EEIKKSAIAI EESGIKRVSC SSAHGYQGKE VIRALKIVKK YTNLEVLVNA GADLTEESIK ELKKYGIDTI CCNLETINEN LFKKVKPGEE LEDRIRVCKL VNKYDIELST GLLIGIGESY EDRVEHLFYL KNELNVGEIP IMGFNPYKGT PMENHPKCSA LEQAKTIAIT RLIFPNIRIT SPTPTIGAEL VQFALFGGAS NVATVIPKNH PMNVKGVGNP KTGNLEEVVK MIMDLGLKPK LDWRRYENYL KIYGK // ID Y787_METJA Reviewed; 504 AA. AC Q58197; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 70. DE RecName: Full=Uncharacterized protein MJ0787; GN OrderedLocusNames=MJ0787; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.thermoautotrophicum MTH1137. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98783.1; -; Genomic_DNA. DR PIR; C64398; C64398. DR ProteinModelPortal; Q58197; -. DR STRING; 243232.MJ_0787; -. DR EnsemblBacteria; AAB98783; AAB98783; MJ_0787. DR KEGG; mja:MJ_0787; -. DR eggNOG; arCOG04861; Archaea. DR eggNOG; COG4018; LUCA. DR OMA; HHGYMCG; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR016760; MonoFe_hyd_HmdC. DR Pfam; PF10113; Fibrillarin_2; 1. DR PIRSF; PIRSF019375; UCP019375; 1. DR TIGRFAMs; TIGR03958; monoFe_hyd_HmdC; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 504 Uncharacterized protein MJ0787. FT /FTId=PRO_0000107037. SQ SEQUENCE 504 AA; 56128 MW; 1F6C18C2C2655EC0 CRC64; MRELIKEAVN SLDSALELRK LIIKKLNEKK LKESDIIEIV DAVDDLSLEE IQKLGSNLRT FPMGCDLVEI AVGPCSSSLT LIQFIENCIL TDYMGFPIHI CSYAVADIAE KEGLKPIEVL KMVLENVDVP IDIDHFGMYG PMRFPKEITH CYGDCYFKGP PFKGCPRNRI HKRLIEKEKE HADEFEDWIK LASTLCINVV EEQGGEEHAA PLEEMKIVAE TAKKYGKGLE GIFHIGDGYD DLITGIKACI DLDVDVFVVE GAPFNRAKNR LKAFAKAIAV SRILVKGGVV ATNGAYEDEC RVGLRSGLNT ILTGFPLNHH GYMCGYSPKT AKRGNFGLRR VMRIIKEEIR AGNVNATFID KDMVKAIALG NRFLKGNIYP YSIGGFYLGD AHWAAIKESN LCKKLKINKT IDDISAEKVG LIGGRYISWA IAEKAEEVYI SDTDSWVEKA TIKILNEAGI NAYPCNGDDK KVLEADKAYI TTFIPNIALK ILNKLRDSKV ELLI // ID Y789_METJA Reviewed; 116 AA. AC Q58199; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 58. DE RecName: Full=Uncharacterized protein MJ0789; GN OrderedLocusNames=MJ0789; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98788.1; -; Genomic_DNA. DR PIR; E64398; E64398. DR ProteinModelPortal; Q58199; -. DR STRING; 243232.MJ_0789; -. DR EnsemblBacteria; AAB98788; AAB98788; MJ_0789. DR KEGG; mja:MJ_0789; -. DR eggNOG; arCOG05051; Archaea. DR eggNOG; ENOG41128YK; LUCA. DR OMA; IDYDYEN; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR019270; DUF2283. DR Pfam; PF10049; DUF2283; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 116 Uncharacterized protein MJ0789. FT /FTId=PRO_0000107040. SQ SEQUENCE 116 AA; 13203 MW; E00F5FD7D6EEB771 CRC64; MKVKIDYDYE NDNLLVYKEG AKSKKTLDLD DILIDFDENG DVVGIEILNA SKLFNVDKYD LLKNLIKFEA VGKITKDLIT LNIKLYLLRR KKEIIKESVV KGLNTIGLKE GEVVIG // ID Y78B_METJA Reviewed; 189 AA. AC P81231; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0785.1; GN OrderedLocusNames=MJ0785.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0795.1 and MJ1249.1. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98790.1; -; Genomic_DNA. DR ProteinModelPortal; P81231; -. DR STRING; 243232.MJ_0785.1; -. DR EnsemblBacteria; AAB98790; AAB98790; MJ_0785.1. DR KEGG; mja:MJ_0785.1; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 189 Uncharacterized protein MJ0785.1. FT /FTId=PRO_0000107035. FT TRANSMEM 20 40 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. FT TRANSMEM 100 120 Helical. {ECO:0000255}. FT TRANSMEM 126 146 Helical. {ECO:0000255}. SQ SEQUENCE 189 AA; 21527 MW; 7DB9DB3E8E954EDD CRC64; MENNKCGTMR GESVYLAYPF ILGSVIFVEF FIFGLVYLTF GLGLKTIIIT SGVILICLLP ISIILIRLFI KSIAGKNKGK LIKKYTKLKI LNKKYKILKV LLFIVGINFY LFGNLVSLNI NPYTKFVLYS ISAFFIIISI VVGDVIVEFY ENGVFINPLG FYKWGEVGKE DLNDRLILKI DKLVIECKR // ID Y790_METJA Reviewed; 229 AA. AC Q58200; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 80. DE RecName: Full=Uncharacterized protein MJ0790; GN OrderedLocusNames=MJ0790; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98784.1; -; Genomic_DNA. DR PIR; F64398; F64398. DR ProteinModelPortal; Q58200; -. DR STRING; 243232.MJ_0790; -. DR EnsemblBacteria; AAB98784; AAB98784; MJ_0790. DR KEGG; mja:MJ_0790; -. DR eggNOG; arCOG04880; Archaea. DR eggNOG; COG1988; LUCA. DR KO; K07038; -. DR OMA; GHTILGI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR007404; YdjM-like. DR Pfam; PF04307; YdjM; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 229 Uncharacterized protein MJ0790. FT /FTId=PRO_0000107041. FT TRANSMEM 8 28 Helical. {ECO:0000255}. FT TRANSMEM 49 69 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 113 133 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 162 182 Helical. {ECO:0000255}. FT TRANSMEM 208 228 Helical. {ECO:0000255}. SQ SEQUENCE 229 AA; 25893 MW; 7636AC4674E85379 CRC64; MNWKGHTILG IIFGLPFISS PEQIFLALAG ALYPDLDHDV KEDIVKRGLL ISGGIVFINI LLYFFDKHLF NVDLFILGVL ILLIYLIPYF SDHRGLTHTF WSLLFVSSIL GYLAYKLSFI SSVFAGLISL LMVTNEVLLG RVMIFAVFAW AVLDILNPNI NVNGALYYIL PVVFGYLSHL VGDTMTPAGV RAFYPLSNYK LRKKEGYILV AIWALMAVYV WKYMILSLL // ID Y796_METJA Reviewed; 235 AA. AC Q58206; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 109. DE RecName: Full=Uncharacterized ABC transporter ATP-binding protein MJ0796; GN OrderedLocusNames=MJ0796; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS). RX PubMed=11402022; DOI=10.1074/jbc.M100758200; RA Yuan Y.-R., Blecker S., Martsinkevich O., Millen L., Thomas P.J., RA Hunt J.F.; RT "The crystal structure of the MJ0796 ATP-binding cassette. RT Implications for the structural consequences of ATP hydrolysis in the RT active site of an ABC transporter."; RL J. Biol. Chem. 276:32313-32321(2001). RN [3] RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF MUTANT GLN-171. RX PubMed=12150914; DOI=10.1016/S1097-2765(02)00576-2; RA Smith P.C., Karpowich N., Millen L., Moody J.E., Rosen J., RA Thomas P.J., Hunt J.F.; RT "ATP binding to the motor domain from an ABC transporter drives RT formation of a nucleotide sandwich dimer."; RL Mol. Cell 10:139-149(2002). CC -!- SIMILARITY: Belongs to the ABC transporter superfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 ABC transporter domain. CC {ECO:0000255|PROSITE-ProRule:PRU00434}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98791.1; -; Genomic_DNA. DR PIR; D64399; D64399. DR PDB; 1F3O; X-ray; 2.70 A; A=1-235. DR PDB; 1L2T; X-ray; 1.90 A; A/B=1-235. DR PDB; 3TIF; X-ray; 1.80 A; A/B=1-235. DR PDBsum; 1F3O; -. DR PDBsum; 1L2T; -. DR PDBsum; 3TIF; -. DR ProteinModelPortal; Q58206; -. DR SMR; Q58206; 1-232. DR STRING; 243232.MJ_0796; -. DR TCDB; 3.A.1.122.14; the atp-binding cassette (abc) superfamily. DR EnsemblBacteria; AAB98791; AAB98791; MJ_0796. DR KEGG; mja:MJ_0796; -. DR eggNOG; arCOG00922; Archaea. DR eggNOG; COG1136; LUCA. DR InParanoid; Q58206; -. DR KO; K02003; -. DR OMA; HDINVAR; -. DR PhylomeDB; Q58206; -. DR BioCyc; RETL1328306-WGS:GSTH-2083-MONOMER; -. DR EvolutionaryTrace; Q58206; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016887; F:ATPase activity; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR003593; AAA+_ATPase. DR InterPro; IPR003439; ABC_transporter-like. DR InterPro; IPR017871; ABC_transporter_CS. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00005; ABC_tran; 1. DR SMART; SM00382; AAA; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00211; ABC_TRANSPORTER_1; 1. DR PROSITE; PS50893; ABC_TRANSPORTER_2; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Complete proteome; Nucleotide-binding; KW Reference proteome; Transport. FT CHAIN 1 235 Uncharacterized ABC transporter ATP- FT binding protein MJ0796. FT /FTId=PRO_0000093221. FT DOMAIN 2 235 ABC transporter. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT NP_BIND 38 45 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00434}. FT STRAND 2 13 {ECO:0000244|PDB:3TIF}. FT STRAND 16 28 {ECO:0000244|PDB:3TIF}. FT STRAND 33 37 {ECO:0000244|PDB:3TIF}. FT HELIX 44 51 {ECO:0000244|PDB:3TIF}. FT STRAND 58 64 {ECO:0000244|PDB:3TIF}. FT HELIX 74 84 {ECO:0000244|PDB:3TIF}. FT STRAND 85 88 {ECO:0000244|PDB:3TIF}. FT HELIX 100 109 {ECO:0000244|PDB:3TIF}. FT STRAND 112 114 {ECO:0000244|PDB:3TIF}. FT HELIX 118 131 {ECO:0000244|PDB:3TIF}. FT HELIX 136 138 {ECO:0000244|PDB:3TIF}. FT HELIX 143 145 {ECO:0000244|PDB:3TIF}. FT HELIX 148 160 {ECO:0000244|PDB:3TIF}. FT STRAND 165 171 {ECO:0000244|PDB:3TIF}. FT TURN 172 175 {ECO:0000244|PDB:3TIF}. FT HELIX 178 195 {ECO:0000244|PDB:3TIF}. FT STRAND 198 202 {ECO:0000244|PDB:3TIF}. FT HELIX 206 209 {ECO:0000244|PDB:3TIF}. FT STRAND 212 219 {ECO:0000244|PDB:3TIF}. FT STRAND 222 228 {ECO:0000244|PDB:3TIF}. SQ SEQUENCE 235 AA; 26566 MW; C3035AE896099E72 CRC64; MIKLKNVTKT YKMGEEIIYA LKNVNLNIKE GEFVSIMGPS GSGKSTMLNI IGCLDKPTEG EVYIDNIKTN DLDDDELTKI RRDKIGFVFQ QFNLIPLLTA LENVELPLIF KYRGAMSGEE RRKRALECLK MAELEERFAN HKPNQLSGGQ QQRVAIARAL ANNPPIILAD EPTGALDSKT GEKIMQLLKK LNEEDGKTVV VVTHDINVAR FGERIIYLKD GEVEREEKLR GFDDR // ID Y798_METJA Reviewed; 334 AA. AC Q58208; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=TPR repeat-containing protein MJ0798; GN OrderedLocusNames=MJ0798; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 7 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98793.1; -; Genomic_DNA. DR PIR; F64399; F64399. DR ProteinModelPortal; Q58208; -. DR STRING; 243232.MJ_0798; -. DR EnsemblBacteria; AAB98793; AAB98793; MJ_0798. DR KEGG; mja:MJ_0798; -. DR eggNOG; arCOG03032; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q58208; -. DR OMA; MGRIYIY; -. DR PhylomeDB; Q58208; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.10.150.160; -; 1. DR Gene3D; 1.25.40.10; -; 3. DR InterPro; IPR023114; Elongated_TPR_rpt_dom. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR001440; TPR_1. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF00515; TPR_1; 2. DR Pfam; PF13181; TPR_8; 4. DR SMART; SM00028; TPR; 6. DR PROSITE; PS50005; TPR; 6. DR PROSITE; PS50293; TPR_REGION; 2. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 334 TPR repeat-containing protein MJ0798. FT /FTId=PRO_0000106457. FT REPEAT 102 135 TPR 1. FT REPEAT 137 168 TPR 2. FT REPEAT 169 202 TPR 3. FT REPEAT 204 235 TPR 4. FT REPEAT 236 269 TPR 5. FT REPEAT 273 306 TPR 6. FT REPEAT 308 333 TPR 7. SQ SEQUENCE 334 AA; 39695 MW; 1FC759BF15E64970 CRC64; MAIKMDKNFT LEILNLLKNN VLKNRLKIGK ELTEMLIDEI DKLIETANEI SEEISKNSPN NSSLYDLRLI YNKLSTLYED IDKLLGEIEC ILSLSNKDIK NWKLWKNLGD KAYLWKAYYE ALFCYNKALE LNQNTELLCK KGYALLKLYK RDLAIKYFEK ASEKDRNNYK ALFGLGKSYY LMSDNKNSIK YFEKVLELNP NDVEALEYLG ELYYEEDCEK AINYFKKALE LKPDDIDLIL KVAFTYFKLK KYKHALKYFE KALKLNPNVF ELEQIYESMG RIYIYLGEDE KAIECFEKLK EINLYHYEIY EIIALTYEEV GNIEKAKEFY KKLV // ID Y79B_METJA Reviewed; 170 AA. AC P81233; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0795.1; GN OrderedLocusNames=MJ0795.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ1249.1, MJ0210.1 and MJ0785.1. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98801.1; -; Genomic_DNA. DR ProteinModelPortal; P81233; -. DR STRING; 243232.MJ_0795.1; -. DR EnsemblBacteria; AAB98801; AAB98801; MJ_0795.1. DR KEGG; mja:MJ_0795.1; -. DR eggNOG; arCOG09674; Archaea. DR eggNOG; ENOG41110S2; LUCA. DR OMA; NPFYFYI; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 170 Uncharacterized protein MJ0795.1. FT /FTId=PRO_0000107047. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 31 51 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. SQ SEQUENCE 170 AA; 19689 MW; CE4B561CD16C01AA CRC64; MKGINPFYFY IGMALILASI VSILLITKSI LLFILLAFGS LVGITLILIY ISRKILKIDK GRLKKEVKRI FGNRVYKILR LMLVLGYAGF IYFSGTFYNS AVLFFIFIVA FTISEFYKTY RIRIYEKGIL IEGIAFYSWE EIEKTTNKDK NQTILKIKGI PKKIVINEII // ID Y805_METJA Reviewed; 221 AA. AC Q58215; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 3. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ0805; GN OrderedLocusNames=MJ0805; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98805.1; -; Genomic_DNA. DR PIR; E64400; E64400. DR ProteinModelPortal; Q58215; -. DR STRING; 243232.MJ_0805; -. DR EnsemblBacteria; AAB98805; AAB98805; MJ_0805. DR KEGG; mja:MJ_0805; -. DR eggNOG; arCOG04875; Archaea. DR eggNOG; COG2029; LUCA. DR InParanoid; Q58215; -. DR KO; K09139; -. DR OMA; KIHLGIN; -. DR PhylomeDB; Q58215; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007162; DUF366. DR Pfam; PF04017; DUF366; 1. DR PIRSF; PIRSF006503; UCP006503; 1. DR ProDom; PD022700; DUF366; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 221 Uncharacterized protein MJ0805. FT /FTId=PRO_0000107055. SQ SEQUENCE 221 AA; 25926 MW; 6067DA093C185725 CRC64; MMYSRKFQIL KENIGLYHGD FMDFEVYDTE YMSIIFVKDR LDYTGKEIEP LWAFKTFDIQ KDSIVVFRGR MEVTTENMKD LKDIKREKDI KTPIKSEDAI NFVVEHFDVI DLKTIYLRQR LLVFIAKEVI ESYNIKLKRD GDDLYFEDKK LSVCIACKGT VSAKIHLGIN VKSKGAEHVK IIGLEDLGIK DIDKVMREIA INYAKEIDKI ERDLRKTLPL I // ID Y826_METJA Reviewed; 138 AA. AC Q58236; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 85. DE RecName: Full=Uncharacterized protein MJ0826; GN OrderedLocusNames=MJ0826; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98825.1; -; Genomic_DNA. DR PIR; B64403; B64403. DR ProteinModelPortal; Q58236; -. DR STRING; 243232.MJ_0826; -. DR EnsemblBacteria; AAB98825; AAB98825; MJ_0826. DR KEGG; mja:MJ_0826; -. DR eggNOG; arCOG01912; Archaea. DR eggNOG; COG1585; LUCA. DR InParanoid; Q58236; -. DR OMA; GLYFPAW; -. DR PhylomeDB; Q58236; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR Gene3D; 2.40.50.140; -; 1. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR002810; NfeD-like_C. DR Pfam; PF01957; NfeD; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 138 Uncharacterized protein MJ0826. FT /FTId=PRO_0000107064. FT TRANSMEM 1 21 Helical. {ECO:0000255}. FT TRANSMEM 46 66 Helical. {ECO:0000255}. SQ SEQUENCE 138 AA; 15094 MW; 24B8EA4E23E20534 CRC64; MEIGYIFILA GFLVIALEAI VPGLYFPAWG IALLIYGVVL LIIPQYAFIS AIIAGVLTII ILHKFVYGVG KEIKVGAERF VGMIGIAIED FEENGYGRIK IENQIWLAKS KDKIKNGDKV EIVGVEGVSL IVKKVEGE // ID Y876_METJA Reviewed; 351 AA. AC Q58286; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 92. DE RecName: Full=Putative ABC transporter permease protein MJ0876; GN OrderedLocusNames=MJ0876; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- FUNCTION: Probably part of a binding-protein-dependent transport CC system. Probably responsible for the translocation of the CC substrate across the membrane. CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the binding-protein-dependent transport CC system permease family. FecCD subfamily. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98879.1; -; Genomic_DNA. DR PIR; D64409; D64409. DR ProteinModelPortal; Q58286; -. DR STRING; 243232.MJ_0876; -. DR EnsemblBacteria; AAB98879; AAB98879; MJ_0876. DR KEGG; mja:MJ_0876; -. DR eggNOG; arCOG01007; Archaea. DR eggNOG; COG0609; LUCA. DR InParanoid; Q58286; -. DR KO; K02015; -. DR OMA; KTSDHRW; -. DR PhylomeDB; Q58286; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005215; F:transporter activity; IEA:InterPro. DR Gene3D; 1.10.3470.10; -; 1. DR InterPro; IPR029022; ABC_BtuC-like. DR InterPro; IPR000522; ABC_transptr_permAse. DR PANTHER; PTHR30472; PTHR30472; 1. DR Pfam; PF01032; FecCD; 1. DR SUPFAM; SSF81345; SSF81345; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix; Transport. FT CHAIN 1 351 Putative ABC transporter permease protein FT MJ0876. FT /FTId=PRO_0000060306. FT TRANSMEM 4 24 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 99 119 Helical. {ECO:0000255}. FT TRANSMEM 124 144 Helical. {ECO:0000255}. FT TRANSMEM 152 172 Helical. {ECO:0000255}. FT TRANSMEM 196 216 Helical. {ECO:0000255}. FT TRANSMEM 249 269 Helical. {ECO:0000255}. FT TRANSMEM 284 304 Helical. {ECO:0000255}. FT TRANSMEM 322 342 Helical. {ECO:0000255}. SQ SEQUENCE 351 AA; 38580 MW; 764EA88C29AD4F16 CRC64; MNKVGILLIL FILSLILPFT ALYLAGDTHL ITVKDIINFL LKGTTGNEFK DIIIKDVRLP PIIGAVLIGL TISVAGLMLQ TLFRNLLASP YTTGISSGVL MVVALVIFID SLSHLFEIFG EKSILVAGWC GGIFSMILLI IIALRVREAN GVIIVALLLS YFFMGLRAYL IANAEELKIQ EYWGFTIGSL SKITLGDVIP MTICSIIFII GVMFLIKSLN ALLFGEQYAK SFGLDIKKTR LLVLFFASFI TGAIIPYVGL IAFIGIIAPY LARPLIKTSD HRYLVPATMF LGVILMVSCH ILSLKYYLPI HYLYGINRPA SPLPIGAVLD ILGGMLVVYL VYKGEKKIKI D // ID Y880_METJA Reviewed; 308 AA. AC Q58290; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 20-JAN-2016, entry version 87. DE RecName: Full=Uncharacterized protein MJ0880; GN OrderedLocusNames=MJ0880; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0871, MJ1556 and MJ1589. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98884.1; -; Genomic_DNA. DR PIR; H64409; H64409. DR ProteinModelPortal; Q58290; -. DR STRING; 243232.MJ_0880; -. DR TCDB; 2.A.126.2.2; the fatty acid exporter (fax) family. DR EnsemblBacteria; AAB98884; AAB98884; MJ_0880. DR KEGG; mja:MJ_0880; -. DR eggNOG; arCOG00360; Archaea. DR eggNOG; COG3366; LUCA. DR InParanoid; Q58290; -. DR OMA; KPICLIS; -. DR PhylomeDB; Q58290; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011642; Gate_dom. DR Pfam; PF07670; Gate; 2. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 308 Uncharacterized protein MJ0880. FT /FTId=PRO_0000107089. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 91 111 Helical. {ECO:0000255}. FT TRANSMEM 115 135 Helical. {ECO:0000255}. FT TRANSMEM 178 198 Helical. {ECO:0000255}. FT TRANSMEM 219 239 Helical. {ECO:0000255}. FT TRANSMEM 251 271 Helical. {ECO:0000255}. FT TRANSMEM 288 308 Helical. {ECO:0000255}. SQ SEQUENCE 308 AA; 34204 MW; CF8BBA7524C83530 CRC64; MDILPYLTKI ILLSSIGITI ASIIVETNLI SKIKKITKPI CLISNLPEEC VVSLLGNFIN PTVGKSMLSG FYKENKVNEK EVIVTTIISP LPTILGESVF RVQLPLAVVI LGYKLGLIYV SLNVISGFLQ ALIGILYANI FFERRQINID NNNNEKIVFN REVIIKGFKK SLKILKKVIP MIVIFTLLIN FLIKLGLMDV VKGLFSPIFR ILDLPGEAIT VLIANLAHFS AGYTTVDILI KNGVLNEKQA LIVLLIGNII SVTMIYLKHS IGTYISLFGR FGLKLAVINY TISVMIKILL ILLLIAFF // ID Y906_METJA Reviewed; 366 AA. AC Q58316; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0906; GN OrderedLocusNames=MJ0906; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98916.1; -; Genomic_DNA. DR PIR; B64413; B64413. DR ProteinModelPortal; Q58316; -. DR STRING; 243232.MJ_0906; -. DR EnsemblBacteria; AAB98916; AAB98916; MJ_0906. DR KEGG; mja:MJ_0906; -. DR eggNOG; arCOG05058; Archaea. DR eggNOG; COG0500; LUCA. DR InParanoid; Q58316; -. DR OMA; DKDADFW; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 3.40.50.150; -; 1. DR InterPro; IPR025714; Methyltranfer_dom. DR InterPro; IPR029063; SAM-dependent_MTases. DR Pfam; PF13847; Methyltransf_31; 1. DR SUPFAM; SSF53335; SSF53335; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 366 Uncharacterized protein MJ0906. FT /FTId=PRO_0000107098. SQ SEQUENCE 366 AA; 42708 MW; 56AABFC1F3FF4727 CRC64; MKFDSAKIEN VVGGGSFEIG DDDSKILDEI ISEVINDIMP SEIKLKKKIE MIDNTIEYLS YELLVTFIKH GVEFGIFPII AKYSPKIDDI PLLVKYPNKQ FILDYIKTAL KLEILKYEDE KIKINEDFEL NIKMPKFDKI ISDYVMKYNF ITHVSRYALI SYSHPKIAIS FKKDPDIWDM ILSSPYYSLC REIASDYLKI DKGDYILDVG CGSRSPKYFI DMIYPEGHYM GVDISKGLLQ IAECRIKRLY CDSYELKNID FTKIIPKEKY DYIICSHTMI YAPSLKQFLN KMMSSIHSGG KIFISEEFIL DKNENICKEV FEFYNRLNKR FRGYYSEKDI VDILESLGYD FKIESLGNGI LVIEKI // ID Y907_METJA Reviewed; 286 AA. AC Q58317; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 88. DE RecName: Full=Uncharacterized protein MJ0907; GN OrderedLocusNames=MJ0907; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000305}; CC Note=Binds 1 [4Fe-4S] cluster. The cluster is coordinated with 3 CC cysteines and an exchangeable S-adenosyl-L-methionine. CC {ECO:0000305}; CC -!- SIMILARITY: Belongs to the radical SAM superfamily. Anaerobic CC sulfatase-maturating enzyme family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98909.1; -; Genomic_DNA. DR PIR; C64413; C64413. DR ProteinModelPortal; Q58317; -. DR STRING; 243232.MJ_0907; -. DR EnsemblBacteria; AAB98909; AAB98909; MJ_0907. DR KEGG; mja:MJ_0907; -. DR eggNOG; arCOG00945; Archaea. DR eggNOG; COG0641; LUCA. DR InParanoid; Q58317; -. DR KO; K06871; -. DR OMA; MKYLILK; -. DR PhylomeDB; Q58317; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR Gene3D; 3.20.20.70; -; 1. DR InterPro; IPR013785; Aldolase_TIM. DR InterPro; IPR000385; MoaA_NifB_PqqE_Fe-S-bd_CS. DR InterPro; IPR007197; rSAM. DR Pfam; PF04055; Radical_SAM; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Metal-binding; KW Reference proteome; S-adenosyl-L-methionine. FT CHAIN 1 286 Uncharacterized protein MJ0907. FT /FTId=PRO_0000134466. FT METAL 16 16 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 20 20 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. FT METAL 23 23 Iron-sulfur (4Fe-4S-S-AdoMet). FT {ECO:0000255}. SQ SEQUENCE 286 AA; 32947 MW; FF488030DC364F94 CRC64; MVDGMKHLIL KVTNRCNLNC IYCYANNKNN KDMDFKTAKN AIDYLLNLDN QIKIQFTGGE PLLNFNLIEK IVDYCNDNYS NCNIQYAIQT NATLINEKIA EKIKELDIKV GISIDGLEIN DILRPYKNGK PSTLDTLKGM YILKSYNIPF GITTVVTNKN LPYLEEFVKY LIAFGVKSIS FDLLKPKKKE HLTLMPNIEE FNKLLNKLGR YPIYIKNLQK RPKDKYCYLN SGDLLFVNEF GDIYLCPTLE GLSCLGNIND KNKIKLPKVK SKGCYAREFL IKTFKK // ID Y935_METJA Reviewed; 208 AA. AC Q58345; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 63. DE RecName: Full=Uncharacterized protein MJ0935; GN OrderedLocusNames=MJ0935; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98940.1; -; Genomic_DNA. DR PIR; G64416; G64416. DR ProteinModelPortal; Q58345; -. DR STRING; 243232.MJ_0935; -. DR EnsemblBacteria; AAB98940; AAB98940; MJ_0935. DR KEGG; mja:MJ_0935; -. DR eggNOG; arCOG03229; Archaea. DR eggNOG; COG2454; LUCA. DR InParanoid; Q58345; -. DR OMA; FVANHYK; -. DR PhylomeDB; Q58345; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR007368; DUF434. DR Pfam; PF04256; DUF434; 1. DR ProDom; PD019177; DUF434; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 208 Uncharacterized protein MJ0935. FT /FTId=PRO_0000107112. SQ SEQUENCE 208 AA; 24162 MW; B2F3D0027B0C1B6D CRC64; MSIEKAKEDF KYLINRGYKK DVALNFVANH YKLSKEDRLK IIRTTHSDKE IKLTKRKLKK LKDFKGKTIY IDGFNVLISL EALIKGNKIV LCDDNIYRDF ENVYGKYKIN EYSDKAISLL LEILKHYNIK AVIYLDAQVS KSGILAKKIR EKMKAFSIEG EVFCVKNCDY ELKNKEVVAT SDSVIIKSEN VKYVVDLIAE AIEYLKKK // ID Y941_METJA Reviewed; 338 AA. AC Q57711; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 3. DT 11-MAY-2016, entry version 90. DE RecName: Full=TPR repeat-containing protein MJ0941; GN OrderedLocusNames=MJ0941; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Contains 8 TPR repeats. {ECO:0000255|PROSITE- CC ProRule:PRU00339}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98947.1; -; Genomic_DNA. DR PIR; E64417; E64417. DR ProteinModelPortal; Q57711; -. DR STRING; 243232.MJ_0941; -. DR PRIDE; Q57711; -. DR EnsemblBacteria; AAB98947; AAB98947; MJ_0941. DR KEGG; mja:MJ_0941; -. DR eggNOG; arCOG03038; Archaea. DR eggNOG; COG0457; LUCA. DR InParanoid; Q57711; -. DR OMA; EAWANQA; -. DR PhylomeDB; Q57711; -. DR Proteomes; UP000000805; Chromosome. DR Gene3D; 1.25.40.10; -; 4. DR InterPro; IPR013026; TPR-contain_dom. DR InterPro; IPR011990; TPR-like_helical_dom. DR InterPro; IPR019734; TPR_repeat. DR Pfam; PF13414; TPR_11; 1. DR Pfam; PF13181; TPR_8; 2. DR SMART; SM00028; TPR; 8. DR SUPFAM; SSF48452; SSF48452; 1. DR PROSITE; PS50005; TPR; 8. DR PROSITE; PS50293; TPR_REGION; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Repeat; TPR repeat. FT CHAIN 1 338 TPR repeat-containing protein MJ0941. FT /FTId=PRO_0000106459. FT REPEAT 27 62 TPR 1. FT REPEAT 63 96 TPR 2. FT REPEAT 97 130 TPR 3. FT REPEAT 131 164 TPR 4. FT REPEAT 165 198 TPR 5. FT REPEAT 199 232 TPR 6. FT REPEAT 268 301 TPR 7. FT REPEAT 302 335 TPR 8. SQ SEQUENCE 338 AA; 39450 MW; 0A6A40E2FCDDBBE7 CRC64; MIDKIIILYF YGDMRMNRKR TPRVDTLEAV ANVLRAYREL FEGNLIKALY YVDKALELEP DFYLALFLKG LALSAKGEIK EAITTFEELL SYESKNPITW VFVGQLYGMS GNCDEALKCY NKALGIENRF LSAFLLKTIC LEFLGEYDEL LKCYNEVLTY TPNFVPMWVK KAEILRKLGR YEDALLCLNR ALELKPHDKN ALYLKGVLLK RMGKFREALE CFKKLIDELN VKWIDAIRHA VSLMLALDDL KDAERYINIG LEIRKDDVAL WYFKGELYER LGKLDEALKC YEKVIELQPH YIKALLSKAR IYERQGNIEA AIEYYNKAVE NIHKDHGE // ID Y943_METJA Reviewed; 417 AA. AC Q58353; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 74. DE RecName: Full=Uncharacterized protein MJ0943; GN OrderedLocusNames=MJ0943; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98953.1; -; Genomic_DNA. DR PIR; G64417; G64417. DR ProteinModelPortal; Q58353; -. DR EnsemblBacteria; AAB98953; AAB98953; MJ_0943. DR KEGG; mja:MJ_0943; -. DR eggNOG; arCOG03788; Archaea. DR eggNOG; ENOG410XUXB; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 417 Uncharacterized protein MJ0943. FT /FTId=PRO_0000107114. FT TRANSMEM 10 30 Helical. {ECO:0000255}. FT TRANSMEM 148 168 Helical. {ECO:0000255}. FT COMPBIAS 399 415 Pro-rich. SQ SEQUENCE 417 AA; 46355 MW; 6DF8D82E1AA8BD90 CRC64; MITMDTIRKA LVCFSILSIL VLACGCVNTP EKIDININSN TNNGENTEKP INQENQNVNN VENKKESQST QNIQSYENKE IKNQENHPLQ SNQNYEQTNG NFNEENENAM TNVGESEVNY NNEPAYNYYI EITYPDGTIP DKIEEQMLYY IKVIDPIVGG LAGIDIYVDG NYIGTLDDVY GIVECVFYEP GYHTITAEDN GKILASKTVY VEEGTAYNSG ESENYDEYDN NYESNDLQQT QTQFSEIEVY VDDIKPSNSI IITKLAMNPG FLASINGISP DIGVNIEMEN GEKINLKYVS MDVDLIIDNP NSESITIDKI ILNMFDDEGH SLGRGEVSNI VITPGENPVT VKVNIPINKM GYEILRKLSG EEVFAEISGS AYIEGSGEVP FSGEADLLPP LPTPPFPLPP LPPFPTE // ID Y956_METJA Reviewed; 260 AA. AC Q58366; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0956; GN OrderedLocusNames=MJ0956; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98969.1; -; Genomic_DNA. DR PIR; D64419; D64419. DR STRING; 243232.MJ_0956; -. DR EnsemblBacteria; AAB98969; AAB98969; MJ_0956. DR KEGG; mja:MJ_0956; -. DR eggNOG; arCOG00043; Archaea. DR eggNOG; COG1606; LUCA. DR OMA; KWIMKAN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 260 Uncharacterized protein MJ0956. FT /FTId=PRO_0000107120. SQ SEQUENCE 260 AA; 30867 MW; 80F2F8D67C8F0D49 CRC64; MHEDVWSLIK ETNHKTILYS HGMKNRVLLG YLLKLRGKYN FDFEAVTFIS DRSPKWVREE IKWIMKANDV KHRFIECGKC KISLENNGHD YHGSCVVWEG IKNFEGGVVA SSIGEHIKDK ERFLTWCNDY NLFPPFIHLN VSRERLVKEF ESLDKNLISS CYHACVFCPI LYKLGKSLIK SEIFYKKKIL TDNERKEHAL NEFYDAMKEQ DIGRMINSVK IYYNKYIREL DEPYADYIKS RDVEMFDKLV NKCKEYLGVK // ID Y961_METJA Reviewed; 762 AA. AC Q58371; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized MCM-type protein MJ0961; GN OrderedLocusNames=MJ0961; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the MCM family. {ECO:0000305}. CC -!- SIMILARITY: Contains 1 MCM domain. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98963.1; -; Genomic_DNA. DR PIR; A64420; A64420. DR ProteinModelPortal; Q58371; -. DR STRING; 243232.MJ_0961; -. DR EnsemblBacteria; AAB98963; AAB98963; MJ_0961. DR KEGG; mja:MJ_0961; -. DR eggNOG; arCOG00439; Archaea. DR eggNOG; COG1241; LUCA. DR InParanoid; Q58371; -. DR KO; K10726; -. DR OMA; EIQQPID; -. DR PhylomeDB; Q58371; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW. DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 2.40.50.140; -; 2. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR031327; MCM. DR InterPro; IPR018525; MCM_CS. DR InterPro; IPR001208; MCM_dom. DR InterPro; IPR012340; NA-bd_OB-fold. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF00493; MCM; 1. DR PRINTS; PR01657; MCMFAMILY. DR SMART; SM00350; MCM; 1. DR SUPFAM; SSF50249; SSF50249; 2. DR SUPFAM; SSF52540; SSF52540; 1. DR PROSITE; PS00847; MCM_1; 1. DR PROSITE; PS50051; MCM_2; 1. PE 3: Inferred from homology; KW ATP-binding; Cell cycle; Complete proteome; DNA replication; KW DNA-binding; Nucleotide-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 762 Uncharacterized MCM-type protein MJ0961. FT /FTId=PRO_0000194130. FT DOMAIN 334 542 MCM. FT NP_BIND 384 391 ATP. {ECO:0000255}. SQ SEQUENCE 762 AA; 87526 MW; 3323509057464C12 CRC64; MVNFDEEVFR AYYEHKIKSF IKEELSNNLI KGNIFEFDIE KFLMHFPDAC EVNDLIIERP KEIEEIILDI FKEAYVELFG EDKELEKIQI AFKNPKGCEK LIEEISAEDI NKLVKFEGNI LQAGKVNALL KKAVYYCNKR IKDENGGFLC KYTYTPCDGR VEIEIDDYFS EGEFIKDMLS PREVKKILEN KKVWDKLVEK GKIPRCVDLK ENDEVFKENL KEIKFILDEY DSIYVNIQEM EIQQPIDLMK NPEEPARSIR VFLENTPGIY AGRVNVIGRV MKREYRHNIP IYKIYIKSNY IKISESYNKI EVKDILRNEE LIETLNELGR KKNIIDILSN YLISQIKGYE LVKKAIFLQQ IKGAFKFLPD GTPLRRDSHI LLITDPGIGK STMLRRIARL FPQNAYASVT TATGGGLTAI VTREATEIGD GWVVKPGVFV RANEGTACID ELTVDKNVMK YILEAMESQT IHVNKGGINV KLPARCAVLA ACNPKRGRFD RNLTVIEQID IPAPLLSRFD LIFPLMDKPN RKSDEEIAEH ILNTHIETAT KDYKILGAID IDGITVDEKL LKYYIIYARS CAYIEENQDL YLGEFDETKL IMPYLTDKAK KMIKKYYLEM RKLGEGDNPI PITARQLEAI IRIAEMHAKA RLSDKVEDVD AEVAISIIDD CLKQVAYDPE TGTLDLDKIA GTPKSRRDKM DAVLNIIREI VSLRDDGLAP EEEIYEKAMA IGLSEKDVND ALEYLKKAGD IYNPRYGFWG LL // ID Y963_METJA Reviewed; 563 AA. AC Q58373; DT 28-NOV-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ0963; GN OrderedLocusNames=MJ0963; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the oxoprolinase family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98965.1; -; Genomic_DNA. DR PIR; C64420; C64420. DR ProteinModelPortal; Q58373; -. DR STRING; 243232.MJ_0963; -. DR EnsemblBacteria; AAB98965; AAB98965; MJ_0963. DR KEGG; mja:MJ_0963; -. DR eggNOG; arCOG01512; Archaea. DR eggNOG; COG0146; LUCA. DR InParanoid; Q58373; -. DR KO; K01474; -. DR OMA; SGCRNIR; -. DR PhylomeDB; Q58373; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003824; F:catalytic activity; IEA:InterPro. DR InterPro; IPR003692; Hydantoinase_B. DR Pfam; PF02538; Hydantoinase_B; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 563 Uncharacterized protein MJ0963. FT /FTId=PRO_0000208585. SQ SEQUENCE 563 AA; 62148 MW; 7D92D7DEAC98FE7F CRC64; MDKITVEVIK SSTSYIAEEM GIILRNTAYS PNIKDRLDFS CAILSSNGEL IAQAEHIPVH LGSMAIGVKN TVDYLKKESI EIEKDDVIIV NDPYIAGTHL NDITLLKPIF YNDEIIGYVA NKAHHVDVGG YAPGSISSNV KELYHEGLII PPSKLVINGK LNKELLNLIT SNVRVPKSTI GDLKAQIASL NIGVERILKL IEKYGDREVT EAWNKSLDYS EEYLKSKIRD INCICEAVDY LEYKDKLINI NMKIEIKNGK IKVDFTGTHR QLDAPLNAVY GVTVASTSFA LKAVIDPDLP MNHGIFRVLN IIAPEETIVN PKKPAPVSVG NVETSQRIVD VIFKALYHEF PDRVPAASNG SMNNVIIGGR GWAFYETIGG GFGGRNGKDG VDGVHANMTN TLNTPIEVIE NEYPIMILEY SLREDSGGAG KYRGGLGIRR VYKMLSDCML SIIADRIKIS PWGVNNGYSG ACGEHYVIKD GKKIPLSGKD TLYLSCGDIV EINTPGGGGY GSPYERDINL ILEDVKDEKI SIKSAYRDYK VKIIKKDDDF VVDMEETKKL RGL // ID Y979_METJA Reviewed; 197 AA. AC Q58389; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ0979; GN OrderedLocusNames=MJ0979; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98994.1; -; Genomic_DNA. DR PIR; C64422; C64422. DR EnsemblBacteria; AAB98994; AAB98994; MJ_0979. DR KEGG; mja:MJ_0979; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 197 Uncharacterized protein MJ0979. FT /FTId=PRO_0000107128. FT TRANSMEM 11 31 Helical. {ECO:0000255}. FT TRANSMEM 85 105 Helical. {ECO:0000255}. FT TRANSMEM 109 129 Helical. {ECO:0000255}. FT TRANSMEM 174 194 Helical. {ECO:0000255}. SQ SEQUENCE 197 AA; 21520 MW; B250A41C03D10A3E CRC64; MLPKKIDYIK IALIVVGIIA LFLPWLTISA STINIKTDEG IHLSVNLAPF RVSSDIKSDT NNIFVEMMMP YVKQYFDMAV KEKMSTFMMI FGIIPIILYI ASIFVDKKAV VVGAGIAGIT CASIFVVLFT VGLNSSDSGL ALTGGKEVTP IDLITGVVNE KSSYLSKDII KIQVGTGWYL TMIIGLALIA YPFIRKV // ID YB5A_METJA Reviewed; 110 AA. AC P81316; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 72. DE RecName: Full=Uncharacterized protein MJ1155.1; GN OrderedLocusNames=MJ1155.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To A.fulgidus AF1754. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99154.1; -; Genomic_DNA. DR ProteinModelPortal; P81316; -. DR STRING; 243232.MJ_1155.1; -. DR DNASU; 1452052; -. DR EnsemblBacteria; AAB99154; AAB99154; MJ_1155.1. DR KEGG; mja:MJ_1155.1; -. DR eggNOG; arCOG07899; Archaea. DR eggNOG; ENOG410Y6QR; LUCA. DR OMA; LEKWSEW; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR008407; Brnchd-chn_aa_trnsp_AzlD. DR Pfam; PF05437; AzlD; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 110 Uncharacterized protein MJ1155.1. FT /FTId=PRO_0000107193. FT TRANSMEM 5 25 Helical. {ECO:0000255}. FT TRANSMEM 62 82 Helical. {ECO:0000255}. FT TRANSMEM 90 110 Helical. {ECO:0000255}. SQ SEQUENCE 110 AA; 12498 MW; 47AFCF07E9448A17 CRC64; MDKNILAIIF VAVGTYLIRY IPIHLHSKIK NIDEKVKEIN EILIYSSTSV ISALFITSFI KFPIIFSNVL ISTISLIFAI VSYKKWNNLG ISILISVVIY YLASKFLISI // ID YC9A_METJA Reviewed; 237 AA. AC P81333; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 54. DE RecName: Full=Uncharacterized protein MJ1292.1; GN OrderedLocusNames=MJ1292.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99310.1; -; Genomic_DNA. DR ProteinModelPortal; P81333; -. DR STRING; 243232.MJ_1292.1; -. DR EnsemblBacteria; AAB99310; AAB99310; MJ_1292.1. DR KEGG; mja:MJ_1292.1; -. DR eggNOG; arCOG05057; Archaea. DR eggNOG; ENOG410YACR; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 237 Uncharacterized protein MJ1292.1. FT /FTId=PRO_0000107259. SQ SEQUENCE 237 AA; 27349 MW; D23DCDC2A19BF286 CRC64; MGVRECVVTR IIKSRPIIAC EDVYLHNYTV FIKIRNRTQG FVKYEPIVGY PVNVTVSLKS AVPDLKDIEI WASAMDENGR LINCSKKKTI DIYGNYRKVN LEILFNDSLE GYLIIYAKTG EAVIPLYYKP IMVTYPVVFG LEYNPSDPWA NLTLSHNYQV PIKVNATIGK YSKIITIYPY KETKVPFYVG KDRNNITVSI ELLNNISTIK KFKKTFYFKK LNKIKTSINE TVVNKYN // ID YF7B_METJA Reviewed; 112 AA. AC P81248; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ1572.1; GN OrderedLocusNames=MJ1572.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99596.1; -; Genomic_DNA. DR STRING; 243232.MJ_1572.1; -. DR EnsemblBacteria; AAB99596; AAB99596; MJ_1572.1. DR KEGG; mja:MJ_1572.1; -. DR eggNOG; arCOG00555; Archaea. DR eggNOG; COG1205; LUCA. DR KO; K06877; -. DR OMA; NCNCADG; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR018973; DEAD/DEAH-box_helicase. DR Pfam; PF09369; DUF1998; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 112 Uncharacterized protein MJ1572.1. FT /FTId=PRO_0000107420. SQ SEQUENCE 112 AA; 12917 MW; 9F6AA26CD7BCE636 CRC64; MHAIEHNIIK ITPIFTYIDS REIGGYSYER FNRNLFKDKA VIFIYDGNEG GFGLAEILYE NAEKLLNKSL EHLKNCNCAD GCPLCIYSTK CGTFNEFLDK WQAIRILEKL LS // ID Y767_METJA Reviewed; 135 AA. AC Q58177; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 91. DE RecName: Full=Uncharacterized transcriptional regulator MJ0767; GN OrderedLocusNames=MJ0767; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the transcriptional regulatory CopG/NikR CC family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98762.1; -; Genomic_DNA. DR PIR; G64395; G64395. DR ProteinModelPortal; Q58177; -. DR STRING; 243232.MJ_0767; -. DR EnsemblBacteria; AAB98762; AAB98762; MJ_0767. DR KEGG; mja:MJ_0767; -. DR eggNOG; arCOG01008; Archaea. DR eggNOG; COG0864; LUCA. DR KO; K07722; -. DR OMA; TTSCGKN; -. DR PhylomeDB; Q58177; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006355; P:regulation of transcription, DNA-templated; IEA:UniProtKB-KW. DR GO; GO:0006351; P:transcription, DNA-templated; IEA:UniProtKB-KW. DR Gene3D; 1.10.1220.10; -; 1. DR InterPro; IPR013321; Arc_rbn_hlx_hlx. DR InterPro; IPR002145; CopG. DR InterPro; IPR010985; Ribbon_hlx_hlx. DR InterPro; IPR014864; TF_NikR_Ni-bd_C. DR Pfam; PF08753; NikR_C; 1. DR Pfam; PF01402; RHH_1; 1. DR SUPFAM; SSF47598; SSF47598; 1. PE 3: Inferred from homology; KW Complete proteome; DNA-binding; Reference proteome; Transcription; KW Transcription regulation. FT CHAIN 1 135 Uncharacterized transcriptional regulator FT MJ0767. FT /FTId=PRO_0000139319. SQ SEQUENCE 135 AA; 15570 MW; 4E921DFF975E031C CRC64; MVNVERISIS FPKFLLKEID EVVKKKGYSS RSELIRDAVR KYVLENNPLN KNETVSGIII VVYNPTKEAL EKMSKLYFEH NKVIKSLNQA YVTTSCGKNA KVEIFVVEGN SKDISKFYEE IEKINGKIYD KVIIF // ID Y781_METJA Reviewed; 721 AA. AC Q58191; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 111. DE RecName: Full=Uncharacterized protein MJ0781; DE Contains: DE RecName: Full=Mja klbA intein; GN OrderedLocusNames=MJ0781; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass membrane CC protein {ECO:0000305}. CC -!- PTM: This protein undergoes a protein self splicing that involves CC a post-translational excision of the intervening region (intein) CC followed by peptide ligation. {ECO:0000305}. CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98770.1; -; Genomic_DNA. DR PIR; E64397; E64397. DR PDB; 2JMZ; NMR; -; A=398-577. DR PDB; 2JNQ; NMR; -; A=398-577. DR PDBsum; 2JMZ; -. DR PDBsum; 2JNQ; -. DR ProteinModelPortal; Q58191; -. DR SMR; Q58191; 398-577. DR STRING; 243232.MJ_0781; -. DR EnsemblBacteria; AAB98770; AAB98770; MJ_0781. DR KEGG; mja:MJ_0781; -. DR eggNOG; arCOG01817; Archaea. DR eggNOG; arCOG01819; Archaea. DR eggNOG; COG1372; LUCA. DR eggNOG; COG4962; LUCA. DR InParanoid; Q58191; -. DR KO; K07332; -. DR OMA; TGHDGCS; -. DR EvolutionaryTrace; Q58191; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 2.170.16.10; -; 1. DR Gene3D; 3.40.50.300; -; 2. DR InterPro; IPR028992; Hedgehog/Intein_dom. DR InterPro; IPR003586; Hint_dom_C. DR InterPro; IPR003587; Hint_dom_N. DR InterPro; IPR030934; Intein_C. DR InterPro; IPR006141; Intein_N. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SMART; SM00305; HintC; 1. DR SMART; SM00306; HintN; 1. DR SUPFAM; SSF51294; SSF51294; 1. DR SUPFAM; SSF52540; SSF52540; 1. DR TIGRFAMs; TIGR01443; intein_Cterm; 1. DR TIGRFAMs; TIGR01445; intein_Nterm; 1. DR PROSITE; PS50818; INTEIN_C_TER; 1. DR PROSITE; PS50817; INTEIN_N_TER; 1. PE 1: Evidence at protein level; KW 3D-structure; ATP-binding; Autocatalytic cleavage; Complete proteome; KW Membrane; Nucleotide-binding; Protein splicing; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 404 Uncharacterized protein MJ0781, 1st part. FT {ECO:0000255}. FT /FTId=PRO_0000013122. FT CHAIN 405 572 Mja klbA intein. {ECO:0000255}. FT /FTId=PRO_0000013123. FT CHAIN 573 721 Uncharacterized protein MJ0781, 2nd part. FT {ECO:0000255}. FT /FTId=PRO_0000013124. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT NP_BIND 308 315 ATP. {ECO:0000255}. FT HELIX 422 432 {ECO:0000244|PDB:2JMZ}. FT TURN 434 436 {ECO:0000244|PDB:2JMZ}. FT STRAND 446 448 {ECO:0000244|PDB:2JMZ}. FT TURN 450 452 {ECO:0000244|PDB:2JMZ}. FT STRAND 455 457 {ECO:0000244|PDB:2JMZ}. FT TURN 461 464 {ECO:0000244|PDB:2JMZ}. FT STRAND 468 470 {ECO:0000244|PDB:2JMZ}. FT STRAND 473 477 {ECO:0000244|PDB:2JMZ}. FT STRAND 481 484 {ECO:0000244|PDB:2JMZ}. FT STRAND 501 506 {ECO:0000244|PDB:2JMZ}. FT STRAND 509 514 {ECO:0000244|PDB:2JMZ}. FT HELIX 515 517 {ECO:0000244|PDB:2JMZ}. FT STRAND 522 527 {ECO:0000244|PDB:2JMZ}. FT STRAND 529 536 {ECO:0000244|PDB:2JMZ}. FT STRAND 542 545 {ECO:0000244|PDB:2JMZ}. FT STRAND 549 553 {ECO:0000244|PDB:2JMZ}. FT TURN 555 557 {ECO:0000244|PDB:2JMZ}. FT STRAND 558 564 {ECO:0000244|PDB:2JMZ}. FT STRAND 568 571 {ECO:0000244|PDB:2JMZ}. SQ SEQUENCE 721 AA; 82743 MW; 13B76CEC7976F0F3 CRC64; MIIKNQLIFV NFYVILIIWW FVMGILDKIQ KKSEKIEKEK KSETVIPSDT KLKPIEPHPT INKKATVGND ETILDTYSIK IDEIEMEVVI KREEGYIYYL VPEIDKINMS LSKLTKDHLN HIKSQISDLG LIEYDQIREY LTNFSMRYNL AIPYIDSLAK FFYLVIGRLG LLEVPLNDDR LEEVMVNGYN VPVFVFHRKH QMCETNIVLD RNEVDRIIES IANLVNRPID SRVPMLDAFL PDGSRVNATT ADITMNGATL TIRKFSKNPL TVIDLINFGT LDIDTAAFLW QAVEGYFGAK PANTLIAGGT GSGKTTLLNV LSLFSMYNER IITIEDTPEL QIPHKHVIKM VTRPARPGMP EYEVTMDDLI KNALRMRPDR IFVGEVRGKE AHSLLVAMNT GHDGALAYDE PIYLSDGNII NIGEFVDKFF KKYKNSIKKE DNGFGWIDIG NENIYIKSFN KLSLIIEDKR ILRVWRKKYS GKLIKITTKN RREITLTHDH PVYISKTGEV LEINAEMVKV GDYIYIPKNN TINLDEVIKV ETVDYNGHIY DLTVEDNHTY IAGKNEGFAV SNCSGTLHAN SADEAILRLT SPPMNVPKIM LTALNFIINQ QRIRRAGKTI RRILGIVEIV KGGGEGHEFA KTTLYEYNGL KDSLERRGIC MWEEEVCEIA GITKEELLRD RENRKKVLSY LYKNNIRKLE NVSDYIMRYQ VDPEKLLRSI R // ID Y803_METJA Reviewed; 172 AA. AC Q58213; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 73. DE RecName: Full=Uncharacterized protein MJ0803; GN OrderedLocusNames=MJ0803; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0695. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98816.1; -; Genomic_DNA. DR PIR; C64400; C64400. DR STRING; 243232.MJ_0803; -. DR EnsemblBacteria; AAB98816; AAB98816; MJ_0803. DR KEGG; mja:MJ_0803; -. DR eggNOG; arCOG10950; Archaea. DR eggNOG; ENOG41111A6; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 172 Uncharacterized protein MJ0803. FT /FTId=PRO_0000107053. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 59 79 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. SQ SEQUENCE 172 AA; 20073 MW; 0D49E317D6518DB5 CRC64; MNSYGVILIS YVGLIKLALA GILCYGIYLA IKSEKNLIKD ALFVYKDNNF NVFGKKYALM IFLAFGFPIF FIGSFLYLFW EKLPEGFRFS LTFAITFFVL FIFGLLFVKY KIRVCKNGIY VGFRFITWKG FEGYKIENNK IILIGKKGVT YPVHLKYSKE LEDIIKNYLK KI // ID Y833_METJA Reviewed; 277 AA. AC Q58243; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 15-DEC-1998, sequence version 2. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MJ0833; GN OrderedLocusNames=MJ0833; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98836.1; -; Genomic_DNA. DR PIR; A64404; A64404. DR ProteinModelPortal; Q58243; -. DR STRING; 243232.MJ_0833; -. DR EnsemblBacteria; AAB98836; AAB98836; MJ_0833. DR KEGG; mja:MJ_0833; -. DR eggNOG; arCOG05054; Archaea. DR eggNOG; ENOG410YGVM; LUCA. DR OMA; WIPPYTT; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 277 Uncharacterized protein MJ0833. FT /FTId=PRO_0000107068. SQ SEQUENCE 277 AA; 31995 MW; 5EFCF35AD3AB11F8 CRC64; MFMKSLIKLI VFIVLCSLFL HSICGERTIA EMSITYKLTG EITNTNPYSI FVAVPSNITF EEKTLPKPED FLDVSTSVTQ TSGIVFYKTI FNGKEGFWIP PYTTVKINIY HYTPITYDIK IDESQENYDV VGPAVVNKVN VIDLNKLFPD AKYEGIKIGK FKLYVSGYIV KGNDTESLSI IVPAPLVIDN YDEFHKFGDD NVDIWISSYN EWYKNQMERE NIHIDNNDPL IPKMDNDVLG DDTHFKFKIF DVPAMAFTTS SNQPIRFYYI IYYKYNN // ID Y834_METJA Reviewed; 238 AA. AC Q58244; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 64. DE RecName: Full=Uncharacterized protein MJ0834; GN OrderedLocusNames=MJ0834; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98837.1; -; Genomic_DNA. DR PIR; B64404; B64404. DR ProteinModelPortal; Q58244; -. DR STRING; 243232.MJ_0834; -. DR EnsemblBacteria; AAB98837; AAB98837; MJ_0834. DR KEGG; mja:MJ_0834; -. DR eggNOG; arCOG09555; Archaea. DR eggNOG; ENOG410YHYT; LUCA. DR OMA; CQLEWIL; -. DR Proteomes; UP000000805; Chromosome. DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 238 Uncharacterized protein MJ0834. FT /FTId=PRO_0000107069. SQ SEQUENCE 238 AA; 28773 MW; 15795760AC988941 CRC64; MFMDYKYFFI TIILISIFCG CYEKSYSFVE YNRHYELNEP NNTKNPNYDQ NIFLNHDLPK TYPKMYKFPK NYYELSDKMF PDVKKRDLDT LSYILKTIKL PAYKKNYYDC SEASCQLEWI LEGYGFKTYL VYGILDTYGN SGSHMWVAVQ LDNGKMVLVE STYLCENYYC PDYAIIYKNY NLNNIVIVRD MKYIPKFYAD TPDMFLIPHN NRRFLITQLD WWNHPKNAEI KKEMFNLK // ID Y838_METJA Reviewed; 223 AA. AC Q58248; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 68. DE RecName: Full=Uncharacterized protein MJ0838; GN OrderedLocusNames=MJ0838; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: To M.jannaschii MJ0575. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98843.1; -; Genomic_DNA. DR PIR; F64404; F64404. DR STRING; 243232.MJ_0838; -. DR EnsemblBacteria; AAB98843; AAB98843; MJ_0838. DR KEGG; mja:MJ_0838; -. DR eggNOG; arCOG02469; Archaea. DR eggNOG; COG1810; LUCA. DR InParanoid; Q58248; -. DR OMA; GEGFKKQ; -. DR PhylomeDB; Q58248; -. DR Proteomes; UP000000805; Chromosome. DR InterPro; IPR003745; DUF166. DR Pfam; PF02593; DUF166; 1. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 223 Uncharacterized protein MJ0838. FT /FTId=PRO_0000107075. SQ SEQUENCE 223 AA; 25837 MW; 1F592F76C84EC37F CRC64; MKVAILTDGV YGDRAYNTIK SKFPCDFITV KYYGDFDEIT ISENTIEKLK DYDLFITYTL NPDLTYELVR KIKELNNKAF VLVGAWKGEG FKKQIESFGN AFCPYLMCDI DEDELKDYKD YLDNYPHLKE FLKYFGKPKV KLYIKNNKIE KIDVLREAPC GSTSETLKEF VGREFNDKTL IDIGLRVQHF CRAGKIRLFV EKEGKKTKAG KILVSGIQVI QIP // ID Y871_METJA Reviewed; 317 AA. AC Q58281; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 81. DE RecName: Full=Uncharacterized protein MJ0871; GN OrderedLocusNames=MJ0871; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0880, MJ1556 and MJ1589. CC {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98877.1; -; Genomic_DNA. DR PIR; G64408; G64408. DR ProteinModelPortal; Q58281; -. DR STRING; 243232.MJ_0871; -. DR EnsemblBacteria; AAB98877; AAB98877; MJ_0871. DR KEGG; mja:MJ_0871; -. DR eggNOG; arCOG00360; Archaea. DR eggNOG; COG3366; LUCA. DR InParanoid; Q58281; -. DR OMA; YLTEPAN; -. DR PhylomeDB; Q58281; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR011642; Gate_dom. DR Pfam; PF07670; Gate; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 317 Uncharacterized protein MJ0871. FT /FTId=PRO_0000107086. FT TRANSMEM 24 44 Helical. {ECO:0000255}. FT TRANSMEM 63 83 Helical. {ECO:0000255}. FT TRANSMEM 136 156 Helical. {ECO:0000255}. FT TRANSMEM 187 207 Helical. {ECO:0000255}. FT TRANSMEM 229 249 Helical. {ECO:0000255}. FT TRANSMEM 252 272 Helical. {ECO:0000255}. FT TRANSMEM 295 315 Helical. {ECO:0000255}. SQ SEQUENCE 317 AA; 35128 MW; 4F6346E8A10BCB5D CRC64; MIVVDYITPL MESMKISAYY TIRISIIVLT TVFIVNYIMS TGIMKKLSNM LSPILRRLKV NPLSISSTLA CFFSPTVGYS ILAEGLKENK VNEREVIGAS LANSFPSVLS HTFTFFIPVV VPILGHTGVL YVLIRLGVAL AKTIIGFLYL SIISEDYSFE MPEINKLNKK ENAKKSFKST IRFAKRLIPI MFFMMTLVLY LSKIGFFDYV EKFVQPITNL LNLNPNVGIL ALTEIMNVQA AIVMAGGFLN EGILSSKEVL IGLIIGNVLT FSTRYVKHSL PLHVSLFGAK LGTKIVMVNA AITLLLDIFI IAGLLLI // ID Y886_METJA Reviewed; 620 AA. AC Q58296; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 17-FEB-2016, entry version 98. DE RecName: Full=Putative molybdopterin biosynthesis protein MJ0886; GN OrderedLocusNames=MJ0886; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- PATHWAY: Cofactor biosynthesis; molybdopterin biosynthesis. CC -!- SIMILARITY: Belongs to the MoeA family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98890.1; -; Genomic_DNA. DR PIR; F64410; F64410. DR ProteinModelPortal; Q58296; -. DR STRING; 243232.MJ_0886; -. DR EnsemblBacteria; AAB98890; AAB98890; MJ_0886. DR KEGG; mja:MJ_0886; -. DR eggNOG; arCOG00217; Archaea. DR eggNOG; COG0303; LUCA. DR eggNOG; COG1910; LUCA. DR InParanoid; Q58296; -. DR KO; K03750; -. DR KO; K07219; -. DR OMA; IIGSHCI; -. DR PhylomeDB; Q58296; -. DR UniPathway; UPA00344; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0006777; P:Mo-molybdopterin cofactor biosynthetic process; IEA:UniProtKB-KW. DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IBA:GO_Central. DR Gene3D; 2.40.340.10; -; 1. DR Gene3D; 3.40.980.10; -; 1. DR InterPro; IPR001453; MoaB/Mog_dom. DR InterPro; IPR008284; MoCF_biosynth_CS. DR InterPro; IPR005111; MoeA_C_domain_IV. DR InterPro; IPR005110; MoeA_linker/N. DR InterPro; IPR024370; PBP_domain. DR Pfam; PF00994; MoCF_biosynth; 1. DR Pfam; PF03454; MoeA_C; 1. DR Pfam; PF03453; MoeA_N; 1. DR Pfam; PF12727; PBP_like; 1. DR SMART; SM00852; MoCF_biosynth; 1. DR SUPFAM; SSF53218; SSF53218; 1. DR SUPFAM; SSF63867; SSF63867; 1. DR SUPFAM; SSF63882; SSF63882; 1. DR TIGRFAMs; TIGR00177; molyb_syn; 1. DR PROSITE; PS01079; MOCF_BIOSYNTHESIS_2; 1. PE 3: Inferred from homology; KW Complete proteome; Molybdenum cofactor biosynthesis; KW Reference proteome. FT CHAIN 1 620 Putative molybdopterin biosynthesis FT protein MJ0886. FT /FTId=PRO_0000171005. SQ SEQUENCE 620 AA; 68897 MW; 9B94AAA7CA6DF0AB CRC64; MTRYLTLHSI EEAKSIINES LKKLKNEVEE VDLFNAIGRV LAEDVFSNID IPPYDRAKMD GYAVKAEDTY EADEDNPVEL KVIGSLKAGE IKDLEINNGE CVEIATGAII PKGANAVVMV EYTERDNDRV KIYRAVPPME NIQFTGSDIM AGELVLRKNT KLTPRDIGVL AAIGKSKVKV YKKLKFGIIS TGNEIISPNE QLEFGKIYDI NSYTLVSYIK TLGYDFEFFG IAKDDKEELK EKIKKALKCD IILLSGGTSA GVGDLTETAI KELGGKILVH GIKIKPGKPT IIGKIDNKLI VGLPGYPTSC LTIFDVLFGD EKNVVKAKFP VRYISAKGRV EYLPVILVKH KNGFSAYPIT KGSGAITSLS EADGYIIIDE NKEILENEDV EVHLFGDVKV GLNIIGSHCI GVDIILKEAK LLAKTINVGS LGGVLSIKRG EADIAGIHLL DEKTNTYNIP FLEKYKVKDA VLVRGYIREQ GFMFRKELGF KSIEEIIEHI YKLEFINRNK GSGTRILFDK FLKDYNINPK EIKGYNIEAK THSAVATAIA MKKADIGLGI RTVAEQYNLA FIPLANEHYD FLIRKERFND EDVQNFIKAL KTAKLPFKKP DNCGEIIWGG // ID Y889_METJA Reviewed; 469 AA. AC Q58299; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 56. DE RecName: Full=Uncharacterized protein MJ0889; GN OrderedLocusNames=MJ0889; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98905.1; -; Genomic_DNA. DR PIR; A64411; A64411. DR ProteinModelPortal; Q58299; -. DR STRING; 243232.MJ_0889; -. DR EnsemblBacteria; AAB98905; AAB98905; MJ_0889. DR KEGG; mja:MJ_0889; -. DR eggNOG; arCOG08296; Archaea. DR eggNOG; ENOG41110WT; LUCA. DR OMA; NNRYITN; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 469 Uncharacterized protein MJ0889. FT /FTId=PRO_0000107093. SQ SEQUENCE 469 AA; 53586 MW; F32A0533F531B5C6 CRC64; MVGFMIALSV SSGYLLDNNY SEYSYYILDN DEDFLVFVIC DEPNTLKCGF RISEIFSRVF CNAVYNNRYI TNLKNLIEVG IYEALENMDK FLKQKGLDYN DLNVSIAGGV YRNGKLMLFS LGNSPVFVVD KDYYLYCPFD LNKNYNLKDW KKFIKFSEVI ENPKSVVACS NKLDGKVFKF KNENNKLIAE PFKYRIIQLI NSIISNRENI DKIKEELKTD LNLKDNTPLF VASFDEKPIN DELVKVGKPK LKVRGCTPIL SKKKEETSPH IEPKIIKNMV LAFILILILI FGLFVMLSHN NLNGGNNSDI VNNSSYQVNT SKISIITVNN ENKSTNISLN PIQTVKTVSS LNNLDLNNTI TKSKNKDSLK ILVKFQVGEI SKDIKKLPIS IMFPEQGYYY ISIKSENSNL KLIDVENGEV VYKNTTLIEL FEKIDGKEKT YNLIVEYNGS EIPSEKGINI SIFEIKIIK // ID Y900_METJA Reviewed; 551 AA. AC Q58310; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 79. DE RecName: Full=Uncharacterized protein MJ0900; GN OrderedLocusNames=MJ0900; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the GSP E family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98903.1; -; Genomic_DNA. DR PIR; D64412; D64412. DR ProteinModelPortal; Q58310; -. DR STRING; 243232.MJ_0900; -. DR EnsemblBacteria; AAB98903; AAB98903; MJ_0900. DR KEGG; mja:MJ_0900; -. DR eggNOG; arCOG01817; Archaea. DR eggNOG; COG0630; LUCA. DR InParanoid; Q58310; -. DR KO; K07332; -. DR OMA; LCLEYGM; -. DR PhylomeDB; Q58310; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:InterPro. DR GO; GO:0006810; P:transport; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 1. DR InterPro; IPR027417; P-loop_NTPase. DR InterPro; IPR001482; T2SS_protein-E. DR Pfam; PF00437; T2SSE; 1. DR SUPFAM; SSF52540; SSF52540; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 551 Uncharacterized protein MJ0900. FT /FTId=PRO_0000207310. SQ SEQUENCE 551 AA; 63493 MW; 2BFC8A31CA32A1BC CRC64; MVIIMSEAEL KEAMKRNPHL RRYIENFKRT YMRIPDFMVS LSRELKELKY PNIIYPVGDP IFIHIFGTPE TKTKYIVIEP TLETAEEKLK YKMILNKILE LAPYEETPKS VEEFEEVLTR LFNACTKVTE AVGEEGFFQR IFRFADNKIK ITPEERDKFL YILKRDLIGL GNLEPIGRDP YLEDIHVIGP KNCHVVHKIF GMLPTNITWE DEIELADYLK NLGERMGRPV SDANPIVDGT LPDGSRINII YSTDVSPKGP SFTIRKFTDV PISVTQLISW GTFSTEVAAY LWLCLEYGMS IFICGETASG KTTTLNAILP FIKPNSKIFS CEDTPEVKPP HPVWQQLVTR ERGPEESRVT LFDLLRAALR SRPNYIIVGE IRSVEAAVAF QAMQTGHPVL STFHAANVRK MIQRLNGDPI NVPLTFMDNL NVALFQLAVY QRGKVLRRVV SIEEIEGYYK EVDGVVTRAV FQWEPDKDRH VFTGRNNSYV LEEKIAKAAG YEDPRDIYNE LELRARILEE MIAREIFDYY QVRDIIWAFY EKGLEGLPFP I // ID Y933_METJA Reviewed; 238 AA. AC Q58343; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 87. DE RecName: Full=Uncharacterized membrane protein MJ0933; GN OrderedLocusNames=MJ0933; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: Belongs to the TMEM19 family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98935.1; -; Genomic_DNA. DR PIR; E64416; E64416. DR ProteinModelPortal; Q58343; -. DR STRING; 243232.MJ_0933; -. DR DNASU; 1451823; -. DR EnsemblBacteria; AAB98935; AAB98935; MJ_0933. DR KEGG; mja:MJ_0933; -. DR eggNOG; arCOG02245; Archaea. DR eggNOG; COG1836; LUCA. DR InParanoid; Q58343; -. DR OMA; GILNNEH; -. DR PhylomeDB; Q58343; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR InterPro; IPR002794; DUF92_TMEM19. DR PANTHER; PTHR13353; PTHR13353; 1. DR Pfam; PF01940; DUF92; 1. DR TIGRFAMs; TIGR00297; TIGR00297; 1. PE 3: Inferred from homology; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 238 Uncharacterized membrane protein MJ0933. FT /FTId=PRO_0000107111. FT TRANSMEM 6 26 Helical. {ECO:0000255}. FT TRANSMEM 45 65 Helical. {ECO:0000255}. FT TRANSMEM 98 118 Helical. {ECO:0000255}. FT TRANSMEM 160 180 Helical. {ECO:0000255}. FT TRANSMEM 186 206 Helical. {ECO:0000255}. SQ SEQUENCE 238 AA; 25514 MW; 65BABA7106CE4780 CRC64; MEVDTMETLI RLFVSILIIC VLALMIKKSR CLDNEGVIGS SIMGFILLYF CGFKYLILLL SFFILGVLVS RVGLEKKKAK KMDETCRSLK NVLANGLIPI LFAILAIFGF NWALIGYISS IAAATSDTFS SELGILSNEK PRLITTFEVV EKGTDGAITI FGTLAGVLGA FLIGLFGYLL FGDIKIVLCG TAGGIAGNLA DSLVGALFER KGILNNEHVN LIATIVGGII GVLIYCTL // ID Y942_METJA Reviewed; 651 AA. AC Q58352; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 102. DE RecName: Full=Probable ATP-dependent helicase MJ0942; DE EC=3.6.4.12; GN OrderedLocusNames=MJ0942; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- CATALYTIC ACTIVITY: ATP + H(2)O = ADP + phosphate. CC -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. CC {ECO:0000305}. CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain. CC {ECO:0000255|PROSITE-ProRule:PRU00541}. CC -!- SIMILARITY: Contains 1 helicase C-terminal domain. CC {ECO:0000255|PROSITE-ProRule:PRU00542}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98945.1; -; Genomic_DNA. DR PIR; F64417; F64417. DR ProteinModelPortal; Q58352; -. DR STRING; 243232.MJ_0942; -. DR EnsemblBacteria; AAB98945; AAB98945; MJ_0942. DR KEGG; mja:MJ_0942; -. DR eggNOG; arCOG00770; Archaea. DR eggNOG; COG1199; LUCA. DR InParanoid; Q58352; -. DR KO; K03722; -. DR OMA; TETIDQQ; -. DR PhylomeDB; Q58352; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0008026; F:ATP-dependent helicase activity; IEA:InterPro. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:InterPro. DR Gene3D; 3.40.50.300; -; 5. DR InterPro; IPR006555; ATP-dep_Helicase_C. DR InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3. DR InterPro; IPR006935; Helicase/UvrB_N. DR InterPro; IPR014001; Helicase_ATP-bd. DR InterPro; IPR001650; Helicase_C. DR InterPro; IPR027417; P-loop_NTPase. DR Pfam; PF13307; Helicase_C_2; 1. DR Pfam; PF04851; ResIII; 1. DR SMART; SM00487; DEXDc; 1. DR SMART; SM00491; HELICc2; 1. DR SUPFAM; SSF52540; SSF52540; 4. DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1. DR PROSITE; PS51193; HELICASE_ATP_BIND_2; 1. DR PROSITE; PS51194; HELICASE_CTER; 1. PE 3: Inferred from homology; KW ATP-binding; Complete proteome; DNA-binding; Helicase; Hydrolase; KW Nucleotide-binding; Reference proteome. FT CHAIN 1 651 Probable ATP-dependent helicase MJ0942. FT /FTId=PRO_0000102009. FT DOMAIN 6 255 Helicase ATP-binding. FT {ECO:0000255|PROSITE-ProRule:PRU00541}. FT DOMAIN 449 638 Helicase C-terminal. FT {ECO:0000255|PROSITE-ProRule:PRU00542}. FT NP_BIND 41 48 ATP. {ECO:0000255|PROSITE- FT ProRule:PRU00541}. FT MOTIF 195 198 DEAH box. SQ SEQUENCE 651 AA; 75957 MW; 1E55B13938D315B2 CRC64; MEFKGYIKEK FPYPKVREPQ KRMMLKIYEC IKNKRNLIVE APTGVGKTLG YLIPALYFAE RRKRVLILTE TIDQQVRIYE DLSSLRHNLK VAFLMGKSNF ICKSKGGKAN RLYCQLNKKC LYRPNKRPIC YCGTKKQPVN LGDKVIYYCP YCTCEYQKAK IESILADIVV MNNSMFYYAK EDIEAKRDID IIICDEAHKL ESSIRNTSTI IINPELPINR LKYMAIHYAP NILKKRLDIG DENFWEIIEK YLTSRGINID ICKETIIFDG ENLSSWKYKT ELAVLGAILD AYYQINNIKN KILRFNENEE IDREELRFEI DNKALIAIEL DFIHKKKLSD LYLLEFIENI KNLRYINENY VVYRSGNSLL CEPVFVSSHL KELYGNAVVI HCSATIGNLK MHALKTGLDK AEFLILESPF PKNRKKIIAL KDGVDMKYER KDREKANKNL LKILEAINGN SLVLFKSFED LDSFYKYLKR EITKTNIKNK NIHVYEQGMD GKEAKELKER FEKIGGILLA TGRFAEGVDI PGEALVGVVI DSLPFPVPTP LILREQKILE ERFKIRGVRD AHWRAFLMTS FDRMARTLVQ MIGRLIRTEN DYGVVVIQDK RFADWVGRVM REKGYLKDNY EVMSLDMAIK YIPKFMSQFK N // ID Y950_METJA Reviewed; 233 AA. AC Q58360; DT 09-SEP-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-MAY-2016, entry version 73. DE RecName: Full=UPF0278 protein MJ0950 {ECO:0000255|HAMAP-Rule:MF_01078}; GN OrderedLocusNames=MJ0950; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the UPF0278 family. {ECO:0000255|HAMAP- CC Rule:MF_01078}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98951.1; -; Genomic_DNA. DR PIR; F64418; F64418. DR ProteinModelPortal; Q58360; -. DR STRING; 243232.MJ_0950; -. DR EnsemblBacteria; AAB98951; AAB98951; MJ_0950. DR KEGG; mja:MJ_0950; -. DR eggNOG; arCOG00720; Archaea. DR eggNOG; COG1458; LUCA. DR InParanoid; Q58360; -. DR KO; K09006; -. DR OMA; VEFYMPP; -. DR PhylomeDB; Q58360; -. DR Proteomes; UP000000805; Chromosome. DR HAMAP; MF_01078; UPF0278; 1. DR InterPro; IPR014856; PIN_ribonuclease. DR Pfam; PF08745; PIN_5; 1. DR TIGRFAMs; TIGR03875; RNA_lig_partner; 1. PE 3: Inferred from homology; KW Complete proteome; Reference proteome. FT CHAIN 1 233 UPF0278 protein MJ0950. FT /FTId=PRO_0000136079. SQ SEQUENCE 233 AA; 26940 MW; 98B903D6B9523613 CRC64; MGRGMQKQRF CLDTSAFTEP SVRKALGVKT VTELTDKVMD LIAEARIKLN ISCHIPYPTV YNELMGFLEN ENCPRDVIVK VDTWLVKKTP NRYEIKIPSE IFYEYVKDLR ERINKGMRIG EEHIIKATDM VYELSKKHPE MGKNEIINKV LSKTINTFRN KYRSALRVGT LDSAPDLDVL LLAKELDAAV VASDGGIEKW AQRLGLRFVD ASDFPFMLEE YLKHNDRHLR IKY // ID Y957_METJA Reviewed; 350 AA. AC Q58367; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ0957; GN OrderedLocusNames=MJ0957; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98970.1; -; Genomic_DNA. DR PIR; E64419; E64419. DR STRING; 243232.MJ_0957; -. DR EnsemblBacteria; AAB98970; AAB98970; MJ_0957. DR KEGG; mja:MJ_0957; -. DR eggNOG; arCOG05060; Archaea. DR eggNOG; ENOG410YUV9; LUCA. DR InParanoid; Q58367; -. DR OMA; GYIEMEV; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 350 Uncharacterized protein MJ0957. FT /FTId=PRO_0000107121. FT COMPBIAS 8 19 Lys/Pro-rich. SQ SEQUENCE 350 AA; 42001 MW; 41680EA9C26AF630 CRC64; MGDDIYIPPK PKPKPKPKPE YKYALWYFKY TNTYEKRFNG TVGDLLNRGF NYAIALEKDE GSGTPESGNL REDGEKDGKE FGEFINSELS GIKYIAQIPY YKRGMLEKLK NASKDKKQME YYINHIYLVK RTLEYWKGWI DGVIESCDSN LVGFYWNFES PGQVSWGFIT DWEIAQLSTY IKQKSNELNR KLEFIWIPYI NDIENPDNND IKRLSKYFDY VFVQPHYYIA WKYWCLWNYE KNVSEDIREY WKYQINRYNG YLTQGITKLI EVLNWIKEIP NGYIEMEVDN KIDEYKYHDL INKACDYIKA REFLTGRDIW QIRAYYFDTN IENVDKVRNG AYGIKGCKNW // ID Y958_METJA Reviewed; 426 AA. AC Q58368; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 11-NOV-2015, entry version 60. DE RecName: Full=Uncharacterized protein MJ0958; DE Flags: Precursor; GN OrderedLocusNames=MJ0958; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98971.1; -; Genomic_DNA. DR PIR; F64419; F64419. DR STRING; 243232.MJ_0958; -. DR EnsemblBacteria; AAB98971; AAB98971; MJ_0958. DR KEGG; mja:MJ_0958; -. DR eggNOG; arCOG09676; Archaea. DR eggNOG; ENOG411106S; LUCA. DR OMA; YENISWE; -. DR Proteomes; UP000000805; Chromosome. PE 3: Inferred from homology; KW Complete proteome; Reference proteome; Signal. FT SIGNAL 1 23 {ECO:0000255}. FT CHAIN 24 426 Uncharacterized protein MJ0958. FT /FTId=PRO_0000014006. SQ SEQUENCE 426 AA; 50695 MW; 25317BE81E203A99 CRC64; MKKFILFLII LLFSIYFLNV SSAEVCPFKD GFIIIYHDIG YDKLFGYTYN DSEILYFNNK NLMDITPISD YYFPELYHNI TYFECGSTNN LTILSFGYFY FPKNGDGIVF LGVLVYTTKN NKINYTEKIL WADVFYSVDD FDISPPACSP NEALLVYCYK MKADYPENIL VLINNTNITE LKKFEDDDYY TTFQHYIYQP IFIFTTYDSK AKKFYILDGR LSNTSFPLYS YYGGKIHFED NITLPKYENI SWECMDFYSI NGTLYIVMKK LNCSNINYAG WYEDYLNQKP YLLIWKNKTI KIISNCSNPY YFVKIKGGEI PIEKSYLKKI FGNKYESIRI TDLAYNNGIL LIETNENHKL HYYIVKNNSI EEIKLKNIIK LYKKKHSLWD DIKKELEPKI YWVIHNWYII VLIIAGLLWM AILWKK // ID Y993_METJA Reviewed; 358 AA. AC Q58400; DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1996, sequence version 1. DT 09-DEC-2015, entry version 82. DE RecName: Full=Putative hydrogenase expression/formation protein MJ0993; GN OrderedLocusNames=MJ0993; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SIMILARITY: Belongs to the HypD family. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB98998.1; -; Genomic_DNA. DR PIR; A64424; A64424. DR ProteinModelPortal; Q58400; -. DR STRING; 243232.MJ_0993; -. DR EnsemblBacteria; AAB98998; AAB98998; MJ_0993. DR KEGG; mja:MJ_0993; -. DR eggNOG; arCOG04428; Archaea. DR eggNOG; COG0409; LUCA. DR InParanoid; Q58400; -. DR KO; K04654; -. DR OMA; LFFHINH; -. DR PhylomeDB; Q58400; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR InterPro; IPR002780; Hyd_form_HypD. DR Pfam; PF01924; HypD; 1. DR PIRSF; PIRSF005622; Hydrgn_mat_hypD; 1. DR TIGRFAMs; TIGR00075; hypD; 1. PE 3: Inferred from homology; KW Complete proteome; Metal-binding; Reference proteome. FT CHAIN 1 358 Putative hydrogenase expression/formation FT protein MJ0993. FT /FTId=PRO_0000201454. FT METAL 61 61 {ECO:0000255}. FT METAL 64 64 {ECO:0000255}. SQ SEQUENCE 358 AA; 40142 MW; 8BE027849D879A77 CRC64; MININDRALI KKAIDKINKL AEKIDKLKIM HVCGSHEHTI CKYGIRDVLP ENITVVPGPG CPVCVTTQKE IDTAIYLADN GYVITTLGDM YRVPGSEKSL MEKQSEGCDV RIVYSISEAV KMAKKERDKK FVFVAIGFET TAPTTGAELI SLKNKDVNNF FILNCHRQTP PVMEFLLNEG VYLDAFICPG HVSTITGLKP YYGLCEKYKA PMVVAGFEPI DVLMAIIMIL KQVISGEAKV ENEYIRAVKP EGNVLAQKII NEVFESIDVP WRGFPVVKNG GFGLREKYKK FDIYEHEDIP EIKEKIPKGC ICDKILRGEK LPTDCPLFGT VCTPLNPVGS CMVSDEGTCR IFYKYRRI // ID YC8B_METJA Reviewed; 179 AA. AC P81319; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 55. DE RecName: Full=Uncharacterized protein MJ1282.2; GN OrderedLocusNames=MJ1282.2; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99299.1; -; Genomic_DNA. DR ProteinModelPortal; P81319; -. DR STRING; 243232.MJ_1282.2; -. DR EnsemblBacteria; AAB99299; AAB99299; MJ_1282.2. DR KEGG; mja:MJ_1282.2; -. DR eggNOG; arCOG08268; Archaea. DR eggNOG; ENOG411100Z; LUCA. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 179 Uncharacterized protein MJ1282.2. FT /FTId=PRO_0000107251. SQ SEQUENCE 179 AA; 20501 MW; BB9FCE006025603D CRC64; MAKDVFNNSL AENVSFINTS GYYNNSENVT YINMSMNGSF SGILYVKSSY KNYTITINES GNFVFNDTTS PIEVELLNNY SDVILNYNLN ESINNFSDTS YLILNESCKN SYFNVIYGNS PMLYVSLHDE DFNHNITIFN PQKGISSKGF VLTDIFITTP RMFYSSLNNS FEYQSWNIN // ID YE8A_METJA Reviewed; 139 AA. AC P81331; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 69. DE RecName: Full=Uncharacterized protein MJ1489.1; GN OrderedLocusNames=MJ1489.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99513.1; -; Genomic_DNA. DR STRING; 243232.MJ_1489.1; -. DR EnsemblBacteria; AAB99513; AAB99513; MJ_1489.1. DR KEGG; mja:MJ_1489.1; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 139 Uncharacterized protein MJ1489.1. FT /FTId=PRO_0000107373. FT TRANSMEM 19 39 Helical. {ECO:0000255}. FT TRANSMEM 64 84 Helical. {ECO:0000255}. FT TRANSMEM 89 109 Helical. {ECO:0000255}. SQ SEQUENCE 139 AA; 16198 MW; D6A96C7CB3989A13 CRC64; MLIAIGIMFQ PLQYPTIPCI IFMVIVGLGL LFAFQFILGY GFEMHRQITI KDRIAFRNYV VGKIFNVLVE HSYYGLLLST FNLFVYKKAI TIRLCFIFAI SIVIFWILGG KLIKKSLKLC FSWFYFFINP SISHKCNSK // ID YC4B_METJA Reviewed; 166 AA. AC P81230; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 71. DE RecName: Full=Uncharacterized protein MJ1249.1; GN OrderedLocusNames=MJ1249.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0795.1 and MJ0785.1. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99259.1; -; Genomic_DNA. DR ProteinModelPortal; P81230; -. DR STRING; 243232.MJ_1249.1; -. DR EnsemblBacteria; AAB99259; AAB99259; MJ_1249.1. DR KEGG; mja:MJ_1249.1; -. DR eggNOG; arCOG09674; Archaea. DR eggNOG; ENOG41110S2; LUCA. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 166 Uncharacterized protein MJ1249.1. FT /FTId=PRO_0000107240. FT TRANSMEM 7 27 Helical. {ECO:0000255}. FT TRANSMEM 30 50 Helical. {ECO:0000255}. FT TRANSMEM 69 89 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. SQ SEQUENCE 166 AA; 19749 MW; FEA9B13E58F3A725 CRC64; MRGINPVLFK ISFLLIILVS LILSLFYYNF LFAFLLSFIL FGITWAYCYI KIESTDKGKL LYEIKRPGIE TLRFLFILMI ISVFIKSLLH SNSFFPYISF LLSNLILGLV LFDDYILGNP TIKFYEKGVV FDRVAFYNWE ELDIKEDEGY LKIKIKYYPK EIMYKK // ID YC8A_METJA Reviewed; 254 AA. AC P81318; DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot. DT 15-JUL-1998, sequence version 1. DT 11-NOV-2015, entry version 78. DE RecName: Full=Uncharacterized protein MJ1282.1; GN OrderedLocusNames=MJ1282.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass CC membrane protein {ECO:0000305}. CC -!- SIMILARITY: To M.jannaschii MJ0902. {ECO:0000305}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99298.1; -; Genomic_DNA. DR STRING; 243232.MJ_1282.1; -. DR EnsemblBacteria; AAB99298; AAB99298; MJ_1282.1. DR KEGG; mja:MJ_1282.1; -. DR eggNOG; arCOG02298; Archaea. DR eggNOG; COG1989; LUCA. DR KO; K07991; -. DR OMA; DCKFLMG; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW. DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell. DR GO; GO:0004190; F:aspartic-type endopeptidase activity; IEA:InterPro. DR InterPro; IPR000045; Prepilin_IV_endopep_pep. DR Pfam; PF01478; Peptidase_A24; 1. PE 4: Predicted; KW Cell membrane; Complete proteome; Membrane; Reference proteome; KW Transmembrane; Transmembrane helix. FT CHAIN 1 254 Uncharacterized protein MJ1282.1. FT /FTId=PRO_0000107250. FT TRANSMEM 33 53 Helical. {ECO:0000255}. FT TRANSMEM 70 90 Helical. {ECO:0000255}. FT TRANSMEM 92 112 Helical. {ECO:0000255}. FT TRANSMEM 133 153 Helical. {ECO:0000255}. FT TRANSMEM 223 243 Helical. {ECO:0000255}. SQ SEQUENCE 254 AA; 29965 MW; 8DDFA786B5D62919 CRC64; MDLGYLYGLI CSIYGAVEDW RKREVTDFLW ISMLWVGVFI HLLYNKSLLL FFIEIFAVLF ITLSVRYEKF NKLVYIGVFL FLLSFILFKS YFALSFLVFY LIGIFLYYLN FMGGGDCKFL MGLSYLKGMF FTFIIFLNAI LFVIPYCIFI LLINLKNGNH KRLKLKNLPL LFIALKKDID KVKKFETIMG DDENLSLIPN INEEKEEKKT YKGKVWVTPQ LPFLVFICLS YILYIVSPFP LIFKVIELVI KSHF // ID YD5A_METJA Reviewed; 362 AA. AC P58018; DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot. DT 12-DEC-2006, sequence version 2. DT 17-FEB-2016, entry version 57. DE RecName: Full=Uncharacterized protein MJ1351.1; GN OrderedLocusNames=MJ1351.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). RN [2] RP IDENTIFICATION. RA Medigue C., Bocs S.; RL Unpublished observations (APR-2001). CC -!- SIMILARITY: Contains 1 glutamine amidotransferase type-2 domain. CC {ECO:0000255|PROSITE-ProRule:PRU00609}. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR ProteinModelPortal; P58018; -. DR InParanoid; P58018; -. DR OMA; SYGINKR; -. DR PhylomeDB; P58018; -. DR Proteomes; UP000000805; Chromosome. DR GO; GO:0016491; F:oxidoreductase activity; IBA:GO_Central. DR GO; GO:0006541; P:glutamine metabolic process; IEA:UniProtKB-KW. DR GO; GO:0055114; P:oxidation-reduction process; IBA:GOC. DR Gene3D; 3.60.20.10; -; 1. DR InterPro; IPR017932; GATase_2_dom. DR InterPro; IPR012375; Glu_synth_lsu_1. DR InterPro; IPR029055; Ntn_hydrolases_N. DR PIRSF; PIRSF018774; GOGAT_lg_dom1; 1. DR SUPFAM; SSF56235; SSF56235; 1. DR PROSITE; PS51278; GATASE_TYPE_2; 1. PE 3: Inferred from homology; KW Complete proteome; Glutamine amidotransferase; Reference proteome. FT INIT_MET 1 1 Removed. {ECO:0000250}. FT CHAIN 2 362 Uncharacterized protein MJ1351.1. FT /FTId=PRO_0000107290. FT DOMAIN 2 362 Glutamine amidotransferase type-2. FT {ECO:0000255|PROSITE-ProRule:PRU00609}. FT ACT_SITE 2 2 For GATase activity. {ECO:0000250}. SQ SEQUENCE 362 AA; 41487 MW; 6153A96F3D569739 CRC64; MCGIIGFMSR KKRMIKGDKI ALALDSLKER GNGKGSGYVG YGIYPTKYKD CYAFHILIDN TPKFEKIKVE VENVLEQYGT IVKDEEIPTE DGIIEKTQIP WRYFYEVDEK FADREEDVVV DIVMEINDKI DGAFVISSGK DLGVFKAVGW PDEVAKFYRI DKYEGYMWLA HARYPTNTRA WWGGAHPFNL LNWSVVHNGE ITSYGTNKRF VEMFGYKCRL LTDTEVVAYI LDLLMRKHKI PVEYALSALA PRFWDEIDKM PEEERELHTA IRLAYGGAML NGPFAIAVGT PQGLIFMNGD IEKDTTMFGL TDRIKLRPLI AAEKDDMIFI SSEESAIRRI CPDLDRVWMP DAGMPVIARP WK // ID YF1B_METJA Reviewed; 155 AA. AC P81235; DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-1998, sequence version 1. DT 11-NOV-2015, entry version 57. DE RecName: Full=Uncharacterized protein MJ1516.1; GN OrderedLocusNames=MJ1516.1; OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / OS JCM 10045 / NBRC 100440) (Methanococcus jannaschii). OC Archaea; Euryarchaeota; Methanococci; Methanococcales; OC Methanocaldococcaceae; Methanocaldococcus. OX NCBI_TaxID=243232; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440; RX PubMed=8688087; DOI=10.1126/science.273.5278.1058; RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., RA Sutton G.G., Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., RA Kerlavage A.R., Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., RA Overbeek R., Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., RA Scott J.L., Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., RA Utterback T.R., Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., RA Cotton M.D., Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., RA Klenk H.-P., Fraser C.M., Smith H.O., Woese C.R., Venter J.C.; RT "Complete genome sequence of the methanogenic archaeon, Methanococcus RT jannaschii."; RL Science 273:1058-1073(1996). CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; L77117; AAB99537.1; -; Genomic_DNA. DR ProteinModelPortal; P81235; -. DR STRING; 243232.MJ_1516.1; -. DR EnsemblBacteria; AAB99537; AAB99537; MJ_1516.1. DR KEGG; mja:MJ_1516.1; -. DR Proteomes; UP000000805; Chromosome. PE 4: Predicted; KW Complete proteome; Reference proteome. FT CHAIN 1 155 Uncharacterized protein MJ1516.1. FT /FTId=PRO_0000107388. FT COMPBIAS 53 149 Ile-rich. SQ SEQUENCE 155 AA; 17259 MW; 95AFCE3E1A99C417 CRC64; MTRSSSVDVV VRHFFLSLNI RRGRITGTPM IPYNGHNGAI EYNTNVAKNQ QKILNIIFRN PILPPNIQSF KKSNSIPNIV KTINNANTVT TSANTPIPTS PKLEEINPSI IIPIHKTENI IPPIIKKIHA IRNIITITLI MSSIKSNIIK SPPKN //