(data stored in ACNUC10821 zone)

SWISSPROT: SYC_LISMF

ID   SYC_LISMF               Reviewed;         471 AA.
AC   Q724H3;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   08-MAY-2019, entry version 89.
DE   RecName: Full=Cysteine--tRNA ligase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            EC=6.1.1.16 {ECO:0000255|HAMAP-Rule:MF_00041};
DE   AltName: Full=Cysteinyl-tRNA synthetase {ECO:0000255|HAMAP-Rule:MF_00041};
DE            Short=CysRS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   Name=cysS {ECO:0000255|HAMAP-Rule:MF_00041};
GN   OrderedLocusNames=LMOf2365_0251;
OS   Listeria monocytogenes serotype 4b (strain F2365).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=265669;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F2365;
RX   PubMed=15115801; DOI=10.1093/nar/gkh562;
RA   Nelson K.E., Fouts D.E., Mongodin E.F., Ravel J., DeBoy R.T.,
RA   Kolonay J.F., Rasko D.A., Angiuoli S.V., Gill S.R., Paulsen I.T.,
RA   Peterson J.D., White O., Nelson W.C., Nierman W.C., Beanan M.J.,
RA   Brinkac L.M., Daugherty S.C., Dodson R.J., Durkin A.S., Madupu R.,
RA   Haft D.H., Selengut J., Van Aken S.E., Khouri H.M., Fedorova N.,
RA   Forberger H.A., Tran B., Kathariou S., Wonderling L.D., Uhlich G.A.,
RA   Bayles D.O., Luchansky J.B., Fraser C.M.;
RT   "Whole genome comparisons of serotype 4b and 1/2a strains of the food-
RT   borne pathogen Listeria monocytogenes reveal new insights into the
RT   core genome components of this species.";
RL   Nucleic Acids Res. 32:2386-2395(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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00041};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00041};
CC       Note=Binds 1 zinc ion per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00041};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00041}.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family. {ECO:0000255|HAMAP-Rule:MF_00041}.
DR   EMBL; AE017262; AAT03038.1; -; Genomic_DNA.
DR   RefSeq; WP_003724083.1; NC_002973.6.
DR   SMR; Q724H3; -.
DR   EnsemblBacteria; AAT03038; AAT03038; LMOf2365_0251.
DR   KEGG; lmf:LMOf2365_0251; -.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OMA; AKYWMHN; -.
DR   BioCyc; LMON265669:G1G0V-267-MONOMER; -.
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   CDD; cd00672; CysRS_core; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
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   InterPro; IPR009080; tRNAsynth_Ia_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; SSF47323; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q724H3.
DR   SWISS-2DPAGE; Q724H3.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    471       Cysteine--tRNA ligase.
FT                                /FTId=PRO_0000159422.
FT   MOTIF        31     41       "HIGH" region.
FT   MOTIF       266    270       "KMSKS" region.
FT   METAL        29     29       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       209    209       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       234    234       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   METAL       238    238       Zinc. {ECO:0000255|HAMAP-Rule:MF_00041}.
FT   BINDING     269    269       ATP. {ECO:0000255|HAMAP-Rule:MF_00041}.
SQ   SEQUENCE   471 AA;  54379 MW;  7913610887803FE4 CRC64;
     MSIQIFNTLK REKEPFKPLK DGEVKMYVCG PTVYNYIHIG NARPIIVFDT VRRYFTYRGY
     DVKFVSNFTD VDDKLIRAAN ELKLTVPEVA DRFIGAYFDD VDQLNVAKAT VNPRVTENMD
     EIIQLISTLI EKGYAYESAG DVYFRTKKFK DYGKLSGQEL SELQHGARVE YNERKQDELD
     FTLWKAAKPG EIFWESPFGN GRPGWHIECS ALAKKYLGDT IDIHAGGQDL VFPHHEDEIA
     QSEAATGKTF ANYWMHNAFL NIDGEKMSKS LGNFITLHDV LKDNDPNVIR FFMLSVHYRK
     PITLNDAILE DAKNGLERLM IAYQNIDHRI QTDDGEYVEE AHEDEWLEQL TELKQAFEDD
     MDDDFNTANA ITTFHELAKR ANIYLAKETV SINVLREFLS MMRLFAEVLG LKLENTQTDS
     LDDSEVEALI EERLQARNER NFARADEIRD ILKEKNIILE DTAQGTRFRR G
//

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