ID   SPSS_METVS              Reviewed;         381 AA.
AC   A6UPN9;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=O-phospho-L-seryl-tRNA:Cys-tRNA synthase {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 {ECO:0000255|HAMAP-Rule:MF_01675};
DE            Short=SepCysS {ECO:0000255|HAMAP-Rule:MF_01675};
GN   OrderedLocusNames=Mevan_0554;
OS   Methanococcus vannielii (strain ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148
OS   / SB).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=406327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35089 / DSM 1224 / JCM 13029 / OCM 148 / SB;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Anderson I.,
RA   Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT   "Complete sequence of Methanococcus vannielii SB.";
RL   Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000742; ABR54461.1; -; Genomic_DNA.
DR   RefSeq; WP_011972364.1; NC_009634.1.
DR   AlphaFoldDB; A6UPN9; -.
DR   SMR; A6UPN9; -.
DR   STRING; 406327.Mevan_0554; -.
DR   EnsemblBacteria; ABR54461; ABR54461; Mevan_0554.
DR   GeneID; 5325981; -.
DR   KEGG; mvn:Mevan_0554; -.
DR   eggNOG; arCOG00091; Archaea.
DR   HOGENOM; CLU_060476_0_0_2; -.
DR   OMA; HKSMAAS; -.
DR   OrthoDB; 24071at2157; -.
DR   Proteomes; UP000001107; 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; Transferase.
FT   CHAIN           1..381
FT                   /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT                   /id="PRO_0000359452"
FT   BINDING         86..87
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         192
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   BINDING         215..217
FT                   /ligand="pyridoxal 5'-phosphate"
FT                   /ligand_id="ChEBI:CHEBI:597326"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT   MOD_RES         218
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ   SEQUENCE   381 AA;  43015 MW;  C666C475461DACFF CRC64;
     MDINIDKYKN ITRNLERDIV NLNPIQRGGI LPTEAKKVIY EYWDGYSVCD YCSGRLDKIE
     TPPINEFLDD MSKFLGMDIT RPTHGARESK YAVMNAICKK GDYVVLDGNS HYTSYVALER
     ANLNYVKTDV EEYPNFRVIP KSYAEKIDEL EDSGKNIGLI LLTHVDGSYG NVSDVSKVGK
     IAKSKGYPLL LNCAYSVGRM PVDGKKLNVD FIAASGHKSM AASGPCGLLS INAEYEDEIL
     KTSKVNVVKE LQMLGCTSRG IPILSLMASF PHIIERVKNW NLELEKTRKV VFEFEKLGFI
     ALGEKPRNHD IIRFETPVLD KIAEKDKRRG FFFYEELKKR GIGGIRRGVT KEFKMSVYGL
     TGMQVDYIID CIKSIVLENA N