ID   SEPS_METLZ              Reviewed;         526 AA.
AC   A2SQV5;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 87.
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=Mlab_0537;
OS   Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX   NCBI_TaxID=410358;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43576 / DSM 4855 / Z;
RX   PubMed=21304657; DOI=10.4056/sigs.35575;
RA   Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA   Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT   "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL   Stand. Genomic Sci. 1:197-203(2009).
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; CP000559; ABN06711.1; -; Genomic_DNA.
DR   RefSeq; WP_011832912.1; NC_008942.1.
DR   AlphaFoldDB; A2SQV5; -.
DR   SMR; A2SQV5; -.
DR   STRING; 410358.Mlab_0537; -.
DR   EnsemblBacteria; ABN06711; ABN06711; Mlab_0537.
DR   GeneID; 4795209; -.
DR   KEGG; mla:Mlab_0537; -.
DR   eggNOG; arCOG00411; Archaea.
DR   HOGENOM; CLU_506822_0_0_2; -.
DR   OMA; RSHMTSG; -.
DR   OrthoDB; 6499at2157; -.
DR   Proteomes; UP000000365; 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   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Ligase; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..526
FT                   /note="O-phosphoserine--tRNA(Cys) ligase"
FT                   /id="PRO_0000363755"
FT   BINDING         189..191
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         234..236
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         276..277
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
FT   BINDING         319
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01674"
SQ   SEQUENCE   526 AA;  58870 MW;  C9BA856153DB76D4 CRC64;
     MKFDIEEFKE RRKTDFEGAW HAGPSVITPP ESSKIYPRYA YRRAKVHPIF DTIARLRAAY
     MSMGFDEAMV PVFIDEQDVY RQFGPEAAAV LDRVYYVGGL PRPNVGISRE RLDAIAEIIE
     KPLAEGTEEK LMKCLHAYKK GKFDGDDLTH EMSVALGVDD GVVVHILDTV FPEFKELAPE
     SSRTTLRSHM TSGWFISLAQ MWDKKPMPIR MFSVDRCFRR EQEEDATHLR TYHSASCIVA
     GEDVTVEEGK AVAEGLLSAF GFTEFRFQPD EKRSKYYMPE TQTEVYGKHP VHGWVEVATF
     GIYSPAALAE YGVGVPVMNL GMGVERLAMV LTQAEDVRKL SFAQLYPPVY SDTDLTKGIG
     LREEPQTAEG RRAVRAVMET AAAHAAERSP CSFPAWKGEL YGHQVEIVVE EPEENTSLLG
     PAALNEVYVR KGAVLGVPDT EKFADVKAEG VPVGISFLYS TANLALARIE EAARVGEGTS
     IQVKMSKHPS DVNLKIEEYV MRYITDNKKK LDLRGPVFMT ITSKIL