ID   SEPS_METM7              Reviewed;         537 AA.
AC   A6VJZ5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
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=MmarC7_1715;
OS   Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=426368;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C7 / ATCC BAA-1331;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus maripaludis C7.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000745; ABR66771.1; -; Genomic_DNA.
DR   RefSeq; WP_012068231.1; NC_009637.1.
DR   AlphaFoldDB; A6VJZ5; -.
DR   SMR; A6VJZ5; -.
DR   STRING; 426368.MmarC7_1715; -.
DR   EnsemblBacteria; ABR66771; ABR66771; MmarC7_1715.
DR   GeneID; 5328918; -.
DR   KEGG; mmz:MmarC7_1715; -.
DR   eggNOG; arCOG00411; Archaea.
DR   HOGENOM; CLU_506822_0_0_2; -.
DR   OMA; RSHMTSG; -.
DR   OrthoDB; 6499at2157; -.
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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..537
FT                   /note="O-phosphoserine--tRNA(Cys) ligase"
FT                   /id="PRO_0000363753"
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"
SQ   SEQUENCE   537 AA;  61132 MW;  80C3BE1045501692 CRC64;
     MFKREEIIEM ANKDFEKAWI ETKDLIKAKK VNESYPRIKP VFGKTHPVND TIENLRQAYL
     RMGFEEYINP VIVDERDIYK QFGPEAMAVL DRCFYLAGLP RPDVGLSDEK ISQIEKLGIK
     VSEHKESLQK ILHGYKKGTL DGDDLVLEIS NALEISSEMG LKILEEVFPE FKDLTAVSSK
     LTLRSHMTSG WFLTVSDLMN KKPLPFKLFS IDRCFRREQK EDKSHLMTYH SASCAIAGEG
     VDINDGKAIA EGLLSQFGFT NFKFIPDEKK SKYYTPETQT EVYAYHPKLK EWLEVATFGV
     YSPVALSKYG IDVPVMNLGL GVERLAMISG NFADVREMVY PQFYEHKLDD RAVASMVKLD
     KVPVMDEIYD LTKELIDSCV KNKDLKSPCE LTIEKTFSFG KTKKNVKINI FEKEEGKNLL
     GPSILNEIYV YDGNVIGIPE SFDGVKEEFK EFLEKGKSEG VATSIRYIDA LCFKLTSKLE
     EAIVTNTSEF KVKVPIVRSL SDINLKIDDI ALKQIMSKNK VIDVRGPVFL NVEVKIE