ID   SEPS_METPE              Reviewed;         529 AA.
AC   B8GJL9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 69.
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=Mpal_0290;
OS   Methanosphaerula palustris (strain ATCC BAA-1556 / DSM 19958 / E1-9c).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanoregulaceae; Methanosphaerula.
OX   NCBI_TaxID=521011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1556 / DSM 19958 / E1-9c;
RX   PubMed=26543115; DOI=10.1128/genomea.01280-15;
RA   Cadillo-Quiroz H., Browne P., Kyrpides N., Woyke T., Goodwin L., Detter C.,
RA   Yavitt J.B., Zinder S.H.;
RT   "Complete Genome Sequence of Methanosphaerula palustris E1-9CT, a
RT   Hydrogenotrophic Methanogen Isolated from a Minerotrophic Fen Peatland.";
RL   Genome Announc. 3:0-0(2015).
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; CP001338; ACL15673.1; -; Genomic_DNA.
DR   RefSeq; WP_012616992.1; NC_011832.1.
DR   AlphaFoldDB; B8GJL9; -.
DR   SMR; B8GJL9; -.
DR   STRING; 521011.Mpal_0290; -.
DR   EnsemblBacteria; ACL15673; ACL15673; Mpal_0290.
DR   GeneID; 7272590; -.
DR   KEGG; mpl:Mpal_0290; -.
DR   eggNOG; arCOG00411; Archaea.
DR   HOGENOM; CLU_506822_0_0_2; -.
DR   OMA; RSHMTSG; -.
DR   OrthoDB; 6499at2157; -.
DR   Proteomes; UP000002457; 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..529
FT                   /note="O-phosphoserine--tRNA(Cys) ligase"
FT                   /id="PRO_1000187330"
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   529 AA;  59307 MW;  5A2706804666C434 CRC64;
     MRFDVEAYRK RAKEDFEGAW HQGPEVLTPA GYQHRYPHLQ YQRAREHPIF AMINALRQTY
     LSLGFDECAN PVIIEEQDVY RQFGPEAMAV LDRVFYLGGL PRPNVGIARG QLDQINELLG
     REMTAETEEH LRETLHAYKK STIDGDDLTH ELAVVLETDD ARVVHILDSV FPEFRSLCPE
     SSRSTLRSHM TSGWFMTLGS IWERTPLPIK LFSVDRCFRR EQAEGPTRLM SYHSASCVIA
     GEDVTLEDGK AVSEALLSAF GYTDFRFQPD EKRSKYYMPD TQTEVYARHP VHDWVEVATF
     GMYSPSALAE YGIGVPVMNL GLGVERLAMI HYHADDVRQL THPQFFPRVL TDRELAAGIT
     LREEPASVEG RHLALAVEAV ARAHATEPGP CSFLAWEGTL FGRQVRVSVE EPEENSKLLG
     PACANEIFVY QGSVLGVPDA DKWQTVRTDG VSTGITYLGA AAAMAAARIE EAARCGQGTT
     VQVKMAKLPS DINLQIREYA MRSITDTKKK IDVRGPVFLT VRSVIPDNL