ID   SPSS1_METAR             Reviewed;         384 AA.
AC   Q0W2L3;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1 {ECO:0000255|HAMAP-Rule:MF_01675};
DE            EC=2.5.1.73 {ECO:0000255|HAMAP-Rule:MF_01675};
DE   AltName: Full=Sep-tRNA:Cys-tRNA synthase 1 {ECO:0000255|HAMAP-Rule:MF_01675};
DE            Short=SepCysS 1 {ECO:0000255|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=UNCMA_08720; ORFNames=RCIX2270;
OS   Methanocella arvoryzae (strain DSM 22066 / NBRC 105507 / MRE50).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=351160;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 22066 / NBRC 105507 / MRE50;
RX   PubMed=16857943; DOI=10.1126/science.1127062;
RA   Erkel C., Kube M., Reinhardt R., Liesack W.;
RT   "Genome of rice cluster I archaea -- the key methane producers in the rice
RT   rhizosphere.";
RL   Science 313:370-372(2006).
CC   -!- FUNCTION: Converts O-phospho-L-seryl-tRNA(Cys) (Sep-tRNA(Cys)) to L-
CC       cysteinyl-tRNA(Cys) (Cys-tRNA(Cys)). {ECO:0000255|HAMAP-Rule:MF_01675}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H(+) + hydrogen sulfide + O-phospho-L-seryl-tRNA(Cys) = L-
CC         cysteinyl-tRNA(Cys) + phosphate; Xref=Rhea:RHEA:25686, Rhea:RHEA-
CC         COMP:9679, Rhea:RHEA-COMP:9719, ChEBI:CHEBI:15378, ChEBI:CHEBI:29919,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:78517, ChEBI:CHEBI:78551; EC=2.5.1.73;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01675};
CC   -!- SUBUNIT: Homodimer. Interacts with SepRS. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
CC   -!- SIMILARITY: Belongs to the SepCysS family. {ECO:0000255|HAMAP-
CC       Rule:MF_01675}.
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DR   EMBL; AM114193; CAJ37380.1; -; Genomic_DNA.
DR   RefSeq; WP_012035201.1; NC_009464.1.
DR   AlphaFoldDB; Q0W2L3; -.
DR   SMR; Q0W2L3; -.
DR   STRING; 351160.RCIX2270; -.
DR   EnsemblBacteria; CAJ37380; CAJ37380; RCIX2270.
DR   GeneID; 5145435; -.
DR   KEGG; rci:RCIX2270; -.
DR   PATRIC; fig|351160.9.peg.903; -.
DR   eggNOG; arCOG00091; Archaea.
DR   OMA; HKSMAAS; -.
DR   OrthoDB; 24071at2157; -.
DR   Proteomes; UP000000663; Chromosome.
DR   GO; GO:0043766; F:Sep-tRNA:Cys-tRNA synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.640.10; -; 1.
DR   Gene3D; 3.90.1150.10; -; 1.
DR   HAMAP; MF_01675; Sep_Cys_tRNA_synth; 1.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   InterPro; IPR013375; Sep_Cys-tRNA_synth_arc.
DR   InterPro; IPR008829; SepSecS/SepCysS.
DR   PANTHER; PTHR43586:SF3; PTHR43586:SF3; 1.
DR   Pfam; PF05889; SepSecS; 1.
DR   SUPFAM; SSF53383; SSF53383; 1.
DR   TIGRFAMs; TIGR02539; SepCysS; 1.
PE   3: Inferred from homology;
KW   Protein biosynthesis; Pyridoxal phosphate; Reference proteome; Transferase.
FT   CHAIN           1..384
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase 1"
FT                   /id="PRO_0000359465"
FT   BINDING         88..89
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         195
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         218..220
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         221
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   384 AA;  42231 MW;  D163A392A11F366D CRC64;
     MSQDLSLQKF GFIKRDTPRT VNLDPLQTGG LLTPEAREAL LEWGDGYSVC DYCGGMLDQI
     KTPPIFDFVH KSLPSFIGMD HARVTNGARE SKFAIMHAMT SPGDWIVMDG NAHYSSIVAA
     QRARLNVKLV PKTPAPDYKI TPEAYAAAIE EVKQQSGKPP ALALLTYPDG SYGNLADAKA
     ITNLAHDFGV PIIINGAYAI GRMPFKGKDL GADFVAGSGH KSMAASGPVG VLGVNEQYAA
     KVLQKSPTHK NKEIEFLGCT ARGATIMTMI ASFPAVVERT KPESWEKEVS NARWFSEQME
     SIGMKQLGDK PHNHDLMFFE GTVFYDISQK TDRYFLYREL KEKSIHGIKP GLTKNFKLST
     LGVGREKLGF VMDTLKDIIK KYDG