ID   SYC_AYWBP               Reviewed;         438 AA.
AC   Q2NIP7;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-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=AYWB_579;
OS   Aster yellows witches'-broom phytoplasma (strain AYWB).
OC   Bacteria; Tenericutes; Mollicutes; Acholeplasmatales;
OC   Acholeplasmataceae; Candidatus Phytoplasma;
OC   Candidatus Phytoplasma asteris.
OX   NCBI_TaxID=322098;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16672622; DOI=10.1128/JB.188.10.3682-3696.2006;
RA   Bai X., Zhang J., Ewing A., Miller S.A., Jancso Radek A.,
RA   Shevchenko D.V., Tsukerman K., Walunas T., Lapidus A., Campbell J.W.,
RA   Hogenhout S.A.;
RT   "Living with genome instability: the adaptation of phytoplasmas to
RT   diverse environments of their insect and plant hosts.";
RL   J. Bacteriol. 188:3682-3696(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.
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP000061; ABC65696.1; -; Genomic_DNA.
DR   RefSeq; YP_456775.1; -.
DR   GeneID; 3866072; -.
DR   GenomeReviews; CP000061_GR; AYWB_579.
DR   KEGG; ayw:AYWB_579; -.
DR   HOGENOM; Q2NIP7; -.
DR   OMA; Q2NIP7; GWHTECA.
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; 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; 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    438       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000240889.
FT   MOTIF        30     40       "HIGH" region.
FT   MOTIF       264    268       "KMSKS" region.
FT   METAL        28     28       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   438 AA;  52036 MW;  F7B7480930083EF0 CRC64;
     MLQIYNSLTR KKEFFKPDHP PQINIYVCGP TVYNHLHLGN TRPLIFFDTV KRYLEMLKFK
     VYYVVNITDI DDKIIETSLK NQVLEKDLAN KYIKSFNNLL ETLNIQTINF KPQATQYINS
     MILYIQTLLD QGFAYFTDQG IYFRVSKITD YGKLKKQDLS QLKQNVRKQL DPQKEFPGDF
     ILWKKTSQGI TYPSPWFAGR PGWHTECATM IEQLFKLPLD IHGGGTDLKF PHHENEIAQT
     HAHSHQKLAN FFMHVERLDY QNQKMSKSLG NIIWCKDLLK QYNPCIIKFL ILSTHYRKPI
     NFSYDLMEQT QQKYKKITYF LTKNNFYLKV NHFFCQTLDQ DIMQLFHQLM QDDFATHKVI
     DLMEQIIKRA HQTQILDKLS QFQNSLLLIL NTLVIAIPFN KPTKKDLQTY FLWQDARKCR
     DFIQADILRK QLLDKGFI
//