ID   SEPS_METTH              Reviewed;         532 AA.
AC   O27545;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 125.
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=MTH_1501;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB85976.1; -; Genomic_DNA.
DR   PIR; C69067; C69067.
DR   RefSeq; WP_010877111.1; NC_000916.1.
DR   AlphaFoldDB; O27545; -.
DR   SMR; O27545; -.
DR   STRING; 187420.MTH_1501; -.
DR   EnsemblBacteria; AAB85976; AAB85976; MTH_1501.
DR   GeneID; 1471770; -.
DR   KEGG; mth:MTH_1501; -.
DR   PATRIC; fig|187420.15.peg.1464; -.
DR   HOGENOM; CLU_506822_0_0_2; -.
DR   OMA; RSHMTSG; -.
DR   Proteomes; UP000005223; 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..532
FT                   /note="O-phosphoserine--tRNA(Cys) ligase"
FT                   /id="PRO_0000363747"
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   532 AA;  61027 MW;  15A011BC4129C95A CRC64;
     MKRKDIVKLS RRDFERAWLE SGKSLRKPHH DMQYPRLRFE TGKSHVLYDT IWMIREAYLR
     LGFSEMVNPL LIDEEHIYRQ FGPEAPAVLD RCFYLGGLPR PDIGLGTGRI QMIEDMGIDV
     SDEKLENLKE VFRSYKKGDL SGDDLVLEVS NALEVESHDG LRVLERVFPE IRDLKPVSGR
     TTLRSHMTSG WFISLQNIHD RYRMPLKLFS IDRCFRREQK EDSSHLMTYH SASCVVVDHE
     VPLDVGKAVA EGLLEHLGFS RFRFRPDEKK SKYYIPGTQT EVYAYHPLLK EWVEVATFGL
     YSPIALSMYG IDQEVMNLGV GVERVAMILN QASDVREMVY PQIYGEWRLS DRDIAEMLRI
     NLHPVTSDGR MLMEKIVKTW RAHADAPSPC SFEVYSGEFL GRRIEVSALE VEENTRLLGP
     AVWNTVYIHD GNILGVPPGT ELDSELITRA RKEGLNTGIT YMEALAAEAA YRIEEMVVSG
     AEEVEVRSTI ARSLSDLNLT LEDTAMRYIT GKNREIDLRG PLFSTIRCRL RG