ID   F6IQ50_9SPHN            Unreviewed;       483 AA.
AC   F6IQ50;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   03-APR-2013, entry version 14.
DE   RecName: Full=Cysteine--tRNA ligase;
DE            EC=6.1.1.16;
DE   AltName: Full=Cysteinyl-tRNA synthetase;
GN   Name=cysS; ORFNames=PP1Y_AT27754;
OS   Novosphingobium sp. PP1Y.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Novosphingobium.
OX   NCBI_TaxID=702113;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=PP1Y;
RA   D'Argenio V., Petrillo M., Cantiello P., Naso B., Cozzuto L.,
RA   Notomista E., Paolella G., Di Donato A., Salvatore F.;
RT   "De Novo Sequencing and Assembly of the Whole Genome of
RT   Novosphingobium sp. Strain PP1Y.";
RL   J. Bacteriol. 193:4296-4296(2011).
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 (By similarity).
CC   -!- SIMILARITY: Belongs to the class-I aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; FR856862; CCA93552.1; -; Genomic_DNA.
DR   RefSeq; YP_004535370.1; NC_015580.1.
DR   ProteinModelPortal; F6IQ50; -.
DR   EnsemblBacteria; CCA93552; CCA93552; PP1Y_AT27754.
DR   GeneID; 10716108; -.
DR   KEGG; npp:PP1Y_AT27754; -.
DR   KO; K01883; -.
DR   BioCyc; NSP702113:GJD2-2627-MONOMER; -.
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:HAMAP.
DR   GO; GO:0006423; P:cysteinyl-tRNA aminoacylation; IEA:HAMAP.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00041; Cys_tRNA_synth; 1; -.
DR   InterPro; IPR015803; Cys-tRNA-ligase.
DR   InterPro; IPR015273; Cys-tRNA-synt_Ia_DALR.
DR   InterPro; IPR024909; Cys-tRNA/MSH_ligase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR009080; tRNAsynth_1a_anticodon-bd.
DR   PANTHER; PTHR10890; PTHR10890; 1.
DR   Pfam; PF09190; DALR_2; 1.
DR   Pfam; PF01406; tRNA-synt_1e; 1.
DR   PRINTS; PR00983; TRNASYNTHCYS.
DR   SMART; SM00840; DALR_2; 1.
DR   SUPFAM; SSF47323; tRNAsyn_1a_bind; 1.
DR   TIGRFAMs; TIGR00435; cysS; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Cytoplasm; Ligase;
KW   Metal-binding; Nucleotide-binding; Protein biosynthesis; Zinc.
FT   MOTIF        35     45       "HIGH" region (By similarity).
FT   MOTIF       288    292       "KMSKS" region (By similarity).
FT   METAL        33     33       Zinc (By similarity).
FT   METAL       223    223       Zinc (By similarity).
FT   METAL       248    248       Zinc (By similarity).
FT   METAL       252    252       Zinc (By similarity).
FT   BINDING     291    291       ATP (By similarity).
SQ   SEQUENCE   483 AA;  53505 MW;  FF63EB2EBFF0EDCC CRC64;
     MTDAHALTLF NSLTRQLEPF QPVHEGEARV YSCGPTVYNY PHIGNMRAYV FADILGRTLS
     HKGYKLTHVI NITDVGHLTD DADAGEDKME KMAAEKAQSI WDIARHYTEA YWTDIAALNI
     RQPAQWSVAT EYVPQMIEFA KQIADKHCYE IDSGLYFDVS TVADYGRLAR AVTEEGEGRI
     EAVDGKRNAA DFAIWRKTPV GEKRQMEWDS PWGPGAPGWH LECSVMSGKL LGFPFDIHTG
     GIDHREIHHP NEIAQNQAFC CTNGLDIPAN SGARVWMHNN FLVERSGKMS KSSGEFLRLQ
     LLIDKGYHPL AYRMMCLQAH YRSELEFSWD GLGAALTRLK RMIMAAERLA GVEAGSPSHP
     KLAAMVETFE KAMSEDLNTP VALTALEDVL AAKKVDPAAK RAVVEAMDAV LGLDLFGTSR
     ADLRLRPKSA VISETEIEAA LAARKDARAA KDFAASDALR DELAAKGVEV MDGDPLGWEW
     KLG
//