SPSS_METMJ
ID SPSS_METMJ Reviewed; 392 AA.
AC A3CVZ3;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 20-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
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=Memar_1614;
OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoculleus.
OX NCBI_TaxID=368407;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35101 / DSM 1498 / JR1;
RX PubMed=21304656; DOI=10.4056/sigs.32535;
RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C.,
RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981
RT type strain JR1.";
RL Stand. Genomic Sci. 1:189-196(2009).
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; CP000562; ABN57543.1; -; Genomic_DNA.
DR RefSeq; WP_011844454.1; NC_009051.1.
DR AlphaFoldDB; A3CVZ3; -.
DR SMR; A3CVZ3; -.
DR STRING; 368407.Memar_1614; -.
DR EnsemblBacteria; ABN57543; ABN57543; Memar_1614.
DR GeneID; 4848208; -.
DR KEGG; mem:Memar_1614; -.
DR eggNOG; arCOG00091; Archaea.
DR HOGENOM; CLU_060476_0_0_2; -.
DR OMA; HKSMAAS; -.
DR OrthoDB; 24071at2157; -.
DR Proteomes; UP000002146; 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..392
FT /note="O-phospho-L-seryl-tRNA:Cys-tRNA synthase"
FT /id="PRO_0000359455"
FT BINDING 85..86
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 190
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT BINDING 213..215
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
FT MOD_RES 216
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01675"
SQ SEQUENCE 392 AA; 42896 MW; EEFF83A1CE7406DF CRC64;
MKCAVDIESR DVEEMYINID PIQAGGRLTV DAMKAAISFA DGYSVCDNCR SPFRLDYIQK
PPIAQFHADL AAWLNMDTAR VVPGARRGFQ AVASTYVEKG DPVIVTSLAH YTEFVAVEEA
GGIPLEVPKD EKNHITPDAA AEKIEAVILE FSKTPPLLFI DHVDYQFGNV HDVAAITKVA
HQYDIPVLVN GAYSVGIMPV DGKALGADFV VGSGHKSMAA PAPSGVLATT NEHAERVFRT
TQAKGDVTGR TFGIKEVEMM GCTLMGVTVV GMMASFPHVK ERVKHWDTEV AHSQAVVDAL
LSIEGTKVLS DYPRQHTLTR IDTRESFDKV AQQHKKRGFF LSSDLKKRGI TGVIPGSTRV
WKFNTFGLTE KQIRHVGESF VEIARENGLN IV