(data stored in ACNUC7421 zone)

SWISSPROT: SYC_ECO57

ID   SYC_ECO57               Reviewed;         461 AA.
AC   Q8XCT9;
DT   27-MAY-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2002, sequence version 1.
DT   05-JUL-2017, entry version 105.
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=Z0681, ECs0588;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys). {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; AE005174; AAG54883.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34011.1; -; Genomic_DNA.
DR   PIR; D90702; D90702.
DR   PIR; G85552; G85552.
DR   RefSeq; NP_308615.1; NC_002695.1.
DR   RefSeq; WP_000912351.1; NZ_MWVM01000032.1.
DR   ProteinModelPortal; Q8XCT9; -.
DR   SMR; Q8XCT9; -.
DR   STRING; 155864.Z0681; -.
DR   EnsemblBacteria; AAG54883; AAG54883; Z0681.
DR   EnsemblBacteria; BAB34011; BAB34011; BAB34011.
DR   GeneID; 916943; -.
DR   KEGG; ece:Z0681; -.
DR   KEGG; ecs:ECs0588; -.
DR   PATRIC; fig|386585.9.peg.695; -.
DR   eggNOG; ENOG4105C8N; Bacteria.
DR   eggNOG; COG0215; LUCA.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   SABIO-RK; Q8XCT9; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
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:0006423; P:cysteinyl-tRNA aminoacylation; IEA:InterPro.
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; Q8XCT9.
DR   SWISS-2DPAGE; Q8XCT9.
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    461       Cysteine--tRNA ligase.
FT                                /FTId=PRO_0000159396.
FT   MOTIF        30     40       "HIGH" region.
FT   MOTIF       266    270       "KMSKS" region.
FT   METAL        28     28       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   461 AA;  52212 MW;  81B72CBC54B4EF93 CRC64;
     MLKIFNTLTR QKEEFKPIHA GEVGMYVCGI TVYDLCHIGH GRTFVAFDVV ARYLRFLGYK
     LKYVRNITDI DDKIIKRANE NGESFVALVD RMIAEMHKDF DALNILRPDM EPRATHHIAE
     IIELTEQLIA KGHAYVADNG DVMFDVPTDP TYGVLSRQDL DQLQAGARVD VVDDKRNPMD
     FVLWKMSKEG EPSWPSPWGA GRPGWHIECS AMNCKQLGNH FDIHGGGSDL MFPHHENEIA
     QSTCAHDGQY VNYWMHSGMV MVDREKMSKS LGNFFTVRDV LKYYDAETVR YFLMSGHYRS
     QLNYSEENLK QARAALERLY TALRGTDKTV APAGGEAFEA RFIEAMDDDF NTPEAYSVLF
     DMAREVNRLK VEDMAAANAM ASHLRKLSAV LGLLEQEPEA FLQSGAQADD SEVAEIEALI
     QQRLDARKAK DWAAADAARD RLNEMGIVLE DGPQGTTWRR K
//

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