ID   SYC_ANAVT               Reviewed;         486 AA.
AC   Q3M6R3;
DT   27-JUN-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Ava_3718;
OS   Anabaena variabilis (strain ATCC 29413 / PCC 7937).
OC   Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Anabaena.
OX   NCBI_TaxID=240292;
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., Saunders E.H., Schmutz J.,
RA   Larimer F., Land M., Kyrpides N., Mavrommatis K., Richardson P.;
RT   "Complete sequence of Anabaena variabilis ATCC 29413.";
RL   Submitted (SEP-2005) 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; CP000117; ABA23323.1; -; Genomic_DNA.
DR   RefSeq; YP_324218.1; -.
DR   GeneID; 3678922; -.
DR   GenomeReviews; CP000117_GR; Ava_3718.
DR   KEGG; ava:Ava_3718; -.
DR   NMPDR; fig|240292.3.peg.4871; -.
DR   HOGENOM; Q3M6R3; -.
DR   OMA; Q3M6R3; VLWKAAK.
DR   BioCyc; AVAR240292:AVA_3718-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    486       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000240886.
FT   MOTIF        31     41       "HIGH" region.
FT   MOTIF       271    275       "KMSKS" region.
FT   METAL        29     29       Zinc (By similarity).
FT   METAL       214    214       Zinc (By similarity).
FT   METAL       239    239       Zinc (By similarity).
FT   METAL       243    243       Zinc (By similarity).
FT   BINDING     274    274       ATP (By similarity).
SQ   SEQUENCE   486 AA;  55152 MW;  95C7EE7DFFA304C5 CRC64;
     MTLTIYNTLT RRQEPLETVE PGKVKMYCCG VTVYDYCHLG HARSYIVWDT IRRYLIWRGF
     EVKYIQNFTD IDDKILNRAK EQGSTMAEVS NRFIDAYFAD IRRLNVLDAD EYPRVTEHIP
     EIHQLIQILE EKGLAYAVGG DVYYRVERFP SYGKLSGREL EQMQAGASGR VDVEDSEPKK
     QHPFDFALWK AAKPGEPAWD SPWGQGRPGW HIECSAMIRS KLGATIDIHG GGGDLIFPHH
     ENEIAQSEAA MNQPLARYWT HNGMVMVNGQ KMSKSLGNFI TIRELLDGVG SWKGDPVNPM
     AVRLFVLQAH YRKPLDFTEE AIANAENSWK TLKEGLLFGY QYGEKLGWGQ ESAIIPELAT
     RFQELGDDDF NFSGGLAVLF ELAKELRREG NILVHEGTTK TPSDELQRQW NTLVTLGKVL
     GLEATPDDET LTQPGLSDTD IEALIEQRQA ARKNKNFSES DRIRNELQAQ GVTLIDSPQG
     TRWHRS
//