SYC_MYCMO
ID SYC_MYCMO Reviewed; 413 AA.
AC Q6KIE2;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Cysteine--tRNA ligase;
DE EC=6.1.1.16;
DE AltName: Full=Cysteinyl-tRNA synthetase;
DE Short=CysRS;
GN Name=cysS; OrderedLocusNames=MMOB1480;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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; AE017308; AAT27634.1; -; Genomic_DNA.
DR RefSeq; WP_011264668.1; NC_006908.1.
DR AlphaFoldDB; Q6KIE2; -.
DR SMR; Q6KIE2; -.
DR STRING; 267748.MMOB1480; -.
DR EnsemblBacteria; AAT27634; AAT27634; MMOB1480.
DR KEGG; mmo:MMOB1480; -.
DR eggNOG; COG0215; Bacteria.
DR HOGENOM; CLU_013528_0_0_14; -.
DR OMA; GWHAECA; -.
DR OrthoDB; 952207at2; -.
DR Proteomes; UP000009072; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR InterPro; IPR015803; Cys-tRNA-ligase.
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; Reference proteome; Zinc.
FT CHAIN 1..413
FT /note="Cysteine--tRNA ligase"
FT /id="PRO_0000159430"
FT MOTIF 9..19
FT /note="'HIGH' region"
FT MOTIF 243..247
FT /note="'KMSKS' region"
FT BINDING 7
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 185
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 211
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 215
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250"
FT BINDING 246
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
SQ SEQUENCE 413 AA; 48254 MW; 4C71444632A71370 CRC64;
MKYIYVCGPT VYNKVHIGNM KPIMTFDLFL RGANFIEKQY LFLHNLTDID DKIIEKASKE
NKTELEISEL YSDFYLKMLD EYNINKPDYI EKVTDNINMI IEYIGLLVKK GSGYIKKGSV
YFDTTKYPEY GSISNLNLNK TLDGDDDFKN EKNNPHDFVL WKKTKVGITW KSPWSEGRPG
WHTECSALIN HIFKKDQIDI HGGGIDLIFP HNENENIQNI ALHGLSLAKK WLHVGHIKWE
NEKMSKSLNN FILADDFIEK YGNDTFRTLI LNTSFSTPIS INEEILESNK KISNKYQVTF
NQANLLIMQS KKRQNEVETQ KYLEKIAKLL ENFEFSKINF EINLQIKLFN SVVDLDAANK
LVECFKLLGF KFSSQNVSQK DLDLFLKWKI EKTNKNFKIS DKLFLELKEK KLV