ID   SYC_ANADE               Reviewed;         481 AA.
AC   Q2IQG7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 23.
DE   RecName: Full=Cysteinyl-tRNA synthetase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteine--tRNA ligase;
DE            Short=CysRS;
GN   Name=cysS; OrderedLocusNames=Adeh_1273;
OS   Anaeromyxobacter dehalogenans (strain 2CP-C).
OC   Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC   Cystobacterineae; Myxococcaceae; Anaeromyxobacter.
OX   NCBI_TaxID=290397;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
RA   Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M.,
RA   Kyrpides N., Anderson I., Sanford R.A., Ritalahti K.M., Thomas H.S.,
RA   Kirby J.R., Zhulin I.B., Loeffler F.E., Richardson P.;
RT   "Complete sequence of Anaeromyxobacter dehalogenans 2CP-C.";
RL   Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000251; ABC81047.1; -; Genomic_DNA.
DR   RefSeq; YP_464484.1; -.
DR   GeneID; 3888706; -.
DR   GenomeReviews; CP000251_GR; Adeh_1273.
DR   KEGG; ade:Adeh_1273; -.
DR   HOGENOM; Q2IQG7; -.
DR   OMA; Q2IQG7; VLWKAAK.
DR   BioCyc; ADEH290397:ADEH_1273-MON; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0004817; F:cysteine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00041; -; 1.
DR   InterPro; IPR001412; aa-tRNA-synth_I_CS.
DR   InterPro; IPR015804; Cys-tRNA-synt_Ia_C.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR   InterPro; IPR015803; Cys-tRNA-synt_Ia_N.
DR   InterPro; IPR002308; Cys-tRNA-synth_1a.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Gene3D; G3DSA:3.40.50.620; Rossmann-like_a/b/a_fold; 1.
DR   PANTHER; PTHR10890; Cys_tRNA-synt_1a; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   TIGRFAMs; TIGR00435; cysS; 1.
DR   PROSITE; PS00178; AA_TRNA_LIGASE_I; FALSE_NEG.
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    481       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000240887.
FT   MOTIF        31     41       "HIGH" region.
FT   MOTIF       272    276       "KMSKS" region.
FT   METAL        29     29       Zinc (By similarity).
FT   METAL       210    210       Zinc (By similarity).
FT   METAL       235    235       Zinc (By similarity).
FT   METAL       239    239       Zinc (By similarity).
FT   BINDING     275    275       ATP (By similarity).
SQ   SEQUENCE   481 AA;  53174 MW;  190A70B0FFE8E0B1 CRC64;
     MSIQVHDTLT AQKRELVPLE PGKLRLYVCG PTVYDYSHLG HARCYVVWDV VVRHLRARGL
     EVRFVRNFTD VDDKIIQRAN ERGEDPIALA SRFADAFHED MDALGNLRPD VEPRVSGHIP
     EIVALIARLV ERGFAYAPGN GDVYYAVRKF PEYGRLSKRN LDDLIAGARV EPGEAKRDPL
     DFALWKAAKP GEPAWDSPWG KGRPGWHIEC SAMTQKHLGA PIDLHAGGKD LVFPHHTNEI
     AQSVAATSDG LHAEDFARYW MHNGFVQIDD EKMSKSLGNF FTIRDVLARF DGEALRFFLL
     GTHYRRDFNF SDQVLAEAER RLSALYETVE KAERLGAGVE PGAEPAFVER ARAALDDDFN
     TPQVLGIVAE AFTEANALAD RKGKKSPEEK ARLAAFARGA RAVGAVLGIL GRPPAQALSA
     IRDRAAARRG IDGSEVERLI AERAAARAAK DFARSDAIRD GLLARGVVLM DGPQGTTWKV
     E
//