ID   SYC_ALHEH               Reviewed;         462 AA.
AC   Q0A7N3;
DT   29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 2.
DT   16-JUN-2009, entry version 20.
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=Mlg_1810;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-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; CP000453; ABI57154.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; YP_742644.1; -.
DR   GeneID; 4269472; -.
DR   GenomeReviews; CP000453_GR; Mlg_1810.
DR   KEGG; aeh:Mlg_1810; -.
DR   HOGENOM; Q0A7N3; -.
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    462       Cysteinyl-tRNA synthetase.
FT                                /FTId=PRO_0000332783.
FT   MOTIF        30     40       "HIGH" region.
FT   MOTIF       266    270       "KMSKS" region.
FT   METAL        28     28       Zinc (By similarity).
FT   METAL       209    209       Zinc (By similarity).
FT   METAL       234    234       Zinc (By similarity).
FT   METAL       238    238       Zinc (By similarity).
FT   BINDING     269    269       ATP (By similarity).
SQ   SEQUENCE   462 AA;  51887 MW;  F4BAC16D28FAFF0E CRC64;
     MLHIHNSLTQ RKERFEPIQP GHVRMYVCGM TVYDYCHLGH ARALVVFDMV ARYLRHLGYR
     VTFVRNITDI DDKIIRRAAE LGEPMGAVTE RFIRAMHEDA EALGVLPPDH EPRATGHIDD
     IIAMIERLVE RGHAYVADDG DVYFAVSSYP EYGKLSGERQ EDLRAGARVE VDEGKRDPVD
     FALWKAARPG EPAWPSPWGE GRPGWHIECS AMSTQVLGDH FDIHGGGLDL KFPHHENEIA
     QSECATGHPF VNYWMHNGHV RINDEKMAKS LGNFFTVREV LSEHRAEAVR LFLLSSHYRS
     PLNYSLDGLR QAQGALERLY LALRGLPEAP VPEADPQGFR ARFHAAMDDD FNTPEALAVL
     FELAREVNRL RQGDDDAGAA APGALLRVLG GVLGLLQDDP ERFLRGGDAG GDEDAEIDAL
     VARRTEARKN RDFAEADRIR DELAERGIIL EDGPQGTTWR RE
//