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SEPS_METMP
ID   SEPS_METMP              Reviewed;         537 AA.
AC   Q6LZE1;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=O-phosphoserine--tRNA(Cys) ligase {ECO:0000255|HAMAP-Rule:MF_01674};
DE            Short=O-phosphoserine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_01674};
DE            EC=6.1.1.27 {ECO:0000255|HAMAP-Rule:MF_01674};
DE   AltName: Full=Non-canonical O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000255|HAMAP-Rule:MF_01674};
DE   AltName: Full=O-phosphoseryl-tRNA(Cys) synthetase {ECO:0000255|HAMAP-Rule:MF_01674};
DE            Short=SepRS {ECO:0000255|HAMAP-Rule:MF_01674};
GN   Name=sepS {ECO:0000255|HAMAP-Rule:MF_01674}; OrderedLocusNames=MMP0688;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: Catalyzes the attachment of O-phosphoserine (Sep) to
CC       tRNA(Cys). {ECO:0000255|HAMAP-Rule:MF_01674}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + O-phospho-L-serine + tRNA(Cys) = AMP + diphosphate + O-
CC         phospho-L-seryl-tRNA(Cys); Xref=Rhea:RHEA:25678, Rhea:RHEA-COMP:9661,
CC         Rhea:RHEA-COMP:9719, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57524, ChEBI:CHEBI:78442, ChEBI:CHEBI:78551,
CC         ChEBI:CHEBI:456215; EC=6.1.1.27; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_01674};
CC   -!- SUBUNIT: Homotetramer. Interacts with SepCysS. {ECO:0000255|HAMAP-
CC       Rule:MF_01674}.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase family.
CC       O-phosphoseryl-tRNA(Cys) synthetase subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_01674}.
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DR   EMBL; BX950229; CAF30244.1; -; Genomic_DNA.
DR   RefSeq; WP_011170632.1; NC_005791.1.
DR   PDB; 2ODR; X-ray; 3.23 A; A/B/C/D=1-537.
DR   PDBsum; 2ODR; -.
DR   AlphaFoldDB; Q6LZE1; -.
DR   SMR; Q6LZE1; -.
DR   DIP; DIP-60876N; -.
DR   STRING; 267377.MMP0688; -.
DR   EnsemblBacteria; CAF30244; CAF30244; MMP0688.
DR   GeneID; 2762711; -.
DR   KEGG; mmp:MMP0688; -.
DR   PATRIC; fig|267377.15.peg.705; -.
DR   eggNOG; arCOG00411; Archaea.
DR   HOGENOM; CLU_506822_0_0_2; -.
DR   OMA; RSHMTSG; -.
DR   OrthoDB; 6499at2157; -.
DR   BioCyc; MMAR267377:MMP_RS03605-MON; -.
DR   BRENDA; 6.1.1.27; 3262.
DR   EvolutionaryTrace; Q6LZE1; -.
DR   Proteomes; UP000000590; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0043816; F:phosphoserine-tRNA(Cys) ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000049; F:tRNA binding; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   GO; GO:0043039; P:tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.930.10; -; 1.
DR   HAMAP; MF_01674; Sep_tRNA_synth; 1.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR045864; aa-tRNA-synth_II/BPL/LPL.
DR   InterPro; IPR005246; O-Pseryl-tRNA(Cys)_ligase.
DR   InterPro; IPR002319; Phenylalanyl-tRNA_Synthase.
DR   InterPro; IPR041590; SepRS_C.
DR   PANTHER; PTHR11538:SF38; PTHR11538:SF38; 1.
DR   Pfam; PF18006; SepRS_C; 1.
DR   Pfam; PF01409; tRNA-synt_2d; 1.
DR   SUPFAM; SSF55681; SSF55681; 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; Ligase;
KW   Nucleotide-binding; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..537
FT                   /note="O-phosphoserine--tRNA(Cys) ligase"
FT                   /id="PRO_0000363750"
FT   BINDING         186..188
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         231..233
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         273..274
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         317
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   HELIX           5..13
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           15..22
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           23..25
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   TURN            31..33
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           35..37
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           47..61
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          71..74
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           75..82
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           83..85
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           86..91
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          94..98
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          180..183
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           188..198
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   TURN            199..201
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          206..215
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          227..237
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           243..255
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   TURN            256..258
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          262..266
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          280..286
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   TURN            287..290
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          291..301
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           303..308
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          315..321
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           322..329
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           335..339
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           341..343
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           350..354
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          357..360
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           366..381
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          427..431
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           450..459
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          460..466
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           467..481
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   STRAND          505..507
FT                   /evidence="ECO:0007829|PDB:2ODR"
FT   HELIX           509..517
FT                   /evidence="ECO:0007829|PDB:2ODR"
SQ   SEQUENCE   537 AA;  61148 MW;  3AB053C02E6571AB CRC64;
     MFKREEIIEM ANKDFEKAWI ETKDLIKAKK INESYPRIKP VFGKTHPVND TIENLRQAYL
     RMGFEEYINP VIVDERDIYK QFGPEAMAVL DRCFYLAGLP RPDVGLSDEK ISQIEKLGIK
     VSEHKESLQK ILHGYKKGTL DGDDLVLEIS NALEISSEMG LKILEDVFPE FKDLTAVSSK
     LTLRSHMTSG WFLTVSDLMN KKPLPFKLFS IDRCFRREQK EDKSHLMTYH SASCAIAGEG
     VDINDGKAIA EGLLSQFGFT NFKFIPDEKK SKYYTPETQT EVYAYHPKLK EWLEVATFGV
     YSPVALSKYG IDVPVMNLGL GVERLAMISG NFADVREMVY PQFYEHKLND RNVASMVKLD
     KVPVMDEIYD LTKELIESCV KNKDLKSPCE LAIEKTFSFG KTKKNVKINI FEKEEGKNLL
     GPSILNEIYV YDGNVIGIPE SFDGVKEEFK DFLEKGKSEG VATGIRYIDA LCFKITSKLE
     EAFVSNTTEF KVKVPIVRSL SDINLKIDDI ALKQIMSKNK VIDVRGPVFL NVEVKIE
 
 
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