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Database: UniProt/SWISS-PROT
Entry: SYC_CLOD6
LinkDB: SYC_CLOD6
Original site: SYC_CLOD6 
ID   SYC_CLOD6               Reviewed;         465 AA.
AC   Q18CD5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   19-FEB-2014, entry version 61.
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=CD630_00520;
OS   Clostridium difficile (strain 630).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales;
OC   Peptostreptococcaceae.
OX   NCBI_TaxID=272563;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=630;
RX   PubMed=16804543; DOI=10.1038/ng1830;
RA   Sebaihia M., Wren B.W., Mullany P., Fairweather N.F., Minton N.,
RA   Stabler R., Thomson N.R., Roberts A.P., Cerdeno-Tarraga A.M., Wang H.,
RA   Holden M.T.G., Wright A., Churcher C., Quail M.A., Baker S., Bason N.,
RA   Brooks K., Chillingworth T., Cronin A., Davis P., Dowd L., Fraser A.,
RA   Feltwell T., Hance Z., Holroyd S., Jagels K., Moule S., Mungall K.,
RA   Price C., Rabbinowitsch E., Sharp S., Simmonds M., Stevens K.,
RA   Unwin L., Whithead S., Dupuy B., Dougan G., Barrell B., Parkhill J.;
RT   "The multidrug-resistant human pathogen Clostridium difficile has a
RT   highly mobile, mosaic genome.";
RL   Nat. Genet. 38:779-786(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-cysteine + tRNA(Cys) = AMP +
CC       diphosphate + L-cysteinyl-tRNA(Cys).
CC   -!- COFACTOR: Binds 1 zinc ion per subunit (By similarity).
CC   -!- SUBUNIT: Monomer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM180355; CAJ66866.2; -; Genomic_DNA.
DR   RefSeq; YP_001086515.2; NC_009089.1.
DR   ProteinModelPortal; Q18CD5; -.
DR   STRING; 272563.CD0052; -.
DR   EnsemblBacteria; CAJ66866; CAJ66866; CD630_00520.
DR   GeneID; 4916664; -.
DR   KEGG; cdf:CD630_00520; -.
DR   PATRIC; 19438241; VBICloDif38397_0062.
DR   eggNOG; COG0215; -.
DR   HOGENOM; HOG000245250; -.
DR   KO; K01883; -.
DR   OrthoDB; EOG6RVFXC; -.
DR   ProtClustDB; PRK00260; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
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; IPR009080; tRNAsynth_1a_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;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   CHAIN         1    465       Cysteine--tRNA ligase.
FT                                /FTId=PRO_1000006582.
FT   MOTIF        29     39       "HIGH" region.
FT   MOTIF       264    268       "KMSKS" region.
FT   METAL        27     27       Zinc (By similarity).
FT   METAL       207    207       Zinc (By similarity).
FT   METAL       232    232       Zinc (By similarity).
FT   METAL       236    236       Zinc (By similarity).
FT   BINDING     267    267       ATP (By similarity).
SQ   SEQUENCE   465 AA;  53919 MW;  D3D2F468AAEAECF4 CRC64;
     MKVYNTLTRT KEEFVPLEEG KVKMYVCGPT VYNYIHIGNA RPFIIFDTLR RYLEYRGYDV
     TYVQNFTDVD DKIINRSHEE GISPEEVAAK YIKEYFVDCD GLGIKRATVH PQVTDNIQQI
     IEFIKELEDK GYAYAVNGDV YFDTNKFEGY GKLSGQKQED LEAGARIEVN DQKRHPMDFV
     LWKAKKEGEP GWDSPWGEGR PGWHIECSVM SKRYLGETID IHAGGQDLTF PHHENEIAQS
     EARSGKTFSK YWMHNGYINI NDEKMSKSKG NFFTVRDISK LYDLEIVRFF MLSAHYRNPV
     NFSDEMLNQA KAGLERLYNT KEKLEFTLSN LVESPLTEKE VELVKELDDF RQKFIDAMDD
     DVNTADAVSV IFELAKLINS NVDENSSLEF AKKCLDEFNE LTGVLNIVNK KKDTVLDKDI
     EELIQKRTDA KKNKEFQLAD DIRQQLLDMG IVLEDTRQGV KWKRI
//
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