SYC_STAXY
ID SYC_STAXY Reviewed; 118 AA.
AC P77986;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
DE Flags: Fragment;
GN Name=cysS;
OS Staphylococcus xylosus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1288;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DSM 20267 / Isolate C2A;
RX PubMed=9084146; DOI=10.1111/j.1574-6968.1997.tb10286.x;
RA Fiegler H., Brueckner R.;
RT "Identification of the serine acetyltransferase gene of Staphylococcus
RT xylosus.";
RL FEMS Microbiol. Lett. 148:181-187(1997).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-cysteine + tRNA(Cys) = AMP + diphosphate + L-
CC cysteinyl-tRNA(Cys); Xref=Rhea:RHEA:17773, Rhea:RHEA-COMP:9661,
CC Rhea:RHEA-COMP:9679, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:35235, ChEBI:CHEBI:78442, ChEBI:CHEBI:78517,
CC ChEBI:CHEBI:456215; EC=6.1.1.16;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250};
CC Note=Binds 1 zinc ion per subunit. {ECO:0000250};
CC -!- SUBUNIT: Monomer. {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase family.
CC {ECO:0000305}.
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DR EMBL; Y07614; CAA68888.1; -; Genomic_DNA.
DR AlphaFoldDB; P77986; -.
DR SMR; P77986; -.
DR STRING; 1288.SXYLSMQ121_2235; -.
DR eggNOG; COG0215; Bacteria.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR InterPro; IPR032678; tRNA-synt_1_cat_dom.
DR PANTHER; PTHR10890; PTHR10890; 1.
DR Pfam; PF01406; tRNA-synt_1e; 1.
DR PRINTS; PR00983; TRNASYNTHCYS.
PE 3: Inferred from homology;
KW Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase; Metal-binding;
KW Nucleotide-binding; Protein biosynthesis; Zinc.
FT CHAIN 1..>118
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159485"
FT MOTIF 30..40
FT /note="'HIGH' region"
FT BINDING 28
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT NON_TER 118
SQ SEQUENCE 118 AA; 13846 MW; 377CCA9EFF515C1C CRC64;
MITLYNTLTR QKETFEPIEP GKVKMYVCGP TVYNYIHIGN ARPAINYDVV RRYFEYQGYE
VIYVSNFTDV DDKLIKRSKE LDESVETITD RYIKAFYEDV GALNVKKATS NPRVMNHM