ID   SYC_AZOSE               Reviewed;         461 AA.
AC   Q5P1H8;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   16-JUN-2009, entry version 31.
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=AZOSEA27110; ORFNames=ebA4792;
OS   Azoarcus sp. (strain EbN1) (Aromatoleum aromaticum (strain EbN1)).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC   Rhodocyclaceae; Aromatoleum.
OX   NCBI_TaxID=76114;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA   Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA   Reinhardt R.;
RT   "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT   bacterium, strain EbN1.";
RL   Arch. Microbiol. 183:27-36(2005).
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; CR555306; CAI08836.1; -; Genomic_DNA.
DR   RefSeq; YP_159737.1; -.
DR   GeneID; 3180031; -.
DR   GenomeReviews; CR555306_GR; AZOSEA27110.
DR   KEGG; eba:ebA4792; -.
DR   NMPDR; fig|76114.4.peg.2608; -.
DR   HOGENOM; Q5P1H8; -.
DR   OMA; Q5P1H8; VLWKAAK.
DR   BioCyc; ASP76114:EBA4792-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    461       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000159342.
FT   MOTIF        30     40       "HIGH" region.
FT   MOTIF       269    273       "KMSKS" region.
FT   METAL        28     28       Zinc (By similarity).
FT   METAL       212    212       Zinc (By similarity).
FT   METAL       237    237       Zinc (By similarity).
FT   METAL       241    241       Zinc (By similarity).
FT   BINDING     272    272       ATP (By similarity).
SQ   SEQUENCE   461 AA;  51978 MW;  4BEC8BF9DBEA7612 CRC64;
     MLHIHNTLTR RKEAFVPIAP GKVRMYVCGM TVYDYCHLGH ARVMVVFDMV ARWLRASGFE
     LTYVRNITDI DDKIIRRAGE KGESIRTLTD RFIAAMHEDA DALGVLRPDH EPRATEYVMQ
     MQSLIGRLRD KGLAYVAGNR DVCYSVRKFD SYGRFSGKSL DELRAGERVE VAGDKQDPLD
     FVLWKHARTD EPDEVKWASP WGAGRPGWHI ECSAMSSDLL GEQFDIHGGG QDLQFPHHEN
     EIAQSEGAHG HTFVNYWMHN GFVRVDDEKM SKSLGNFFTI RDVLERFDPE VVRFFILRAH
     YRSPLNYSDA HLEDARQALT RLYTALRNVQ PSDAQVDWDE PHAMRFRAAM DDDFNTAEAV
     AVLFELANEA NRSGSAATAA QLKGLGGVLG LLAREPASFL QGRMAGEPDK GEGVAIESMI
     ERRALAKKSK DYAEADRIRA QLLASGIVLE DTPHGTVWRR A
//