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Database: UniProt/SWISS-PROT
Entry: SYD_BACC4
LinkDB: SYD_BACC4
Original site: SYD_BACC4 
ID   SYD_BACC4               Reviewed;         591 AA.
AC   B7HE37;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   19-FEB-2014, entry version 39.
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
DE            Short=AspRS;
GN   Name=aspS; OrderedLocusNames=BCB4264_A4522;
OS   Bacillus cereus (strain B4264).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=405532;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4264;
RA   Dodson R.J., Durkin A.S., Rosovitz M.J., Rasko D.A., Hoffmaster A.,
RA   Ravel J., Sutton G.;
RT   "Genome sequence of Bacillus cereus B4264.";
RL   Submitted (OCT-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; CP001176; ACK62033.1; -; Genomic_DNA.
DR   RefSeq; YP_002369212.1; NC_011725.1.
DR   STRING; 405532.BCB4264_A4522; -.
DR   EnsemblBacteria; ACK62033; ACK62033; BCB4264_A4522.
DR   GeneID; 7098308; -.
DR   KEGG; bcb:BCB4264_A4522; -.
DR   PATRIC; 18880935; VBIBacCer117876_4373.
DR   eggNOG; COG0173; -.
DR   HOGENOM; HOG000275159; -.
DR   KO; K01876; -.
DR   OMA; QLDVEMS; -.
DR   OrthoDB; EOG68Q0NX; -.
DR   ProtClustDB; PRK00476; -.
DR   BioCyc; BCER405532:GI1K-4480-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   HAMAP; MF_00044_B; Asp_tRNA_synth_B; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
DR   TIGRFAMs; TIGR00459; aspS_bact; 1.
DR   PROSITE; PS50862; AA_TRNA_LIGASE_II; 1.
PE   3: Inferred from homology;
KW   Aminoacyl-tRNA synthetase; ATP-binding; Complete proteome; Cytoplasm;
KW   Ligase; Nucleotide-binding; Protein biosynthesis.
FT   CHAIN         1    591       Aspartate--tRNA ligase.
FT                                /FTId=PRO_1000198959.
SQ   SEQUENCE   591 AA;  66308 MW;  54AFCCC7C5C82B55 CRC64;
     MAERTHACGK VTVEAVGQTV QLKGWVQKRR DLGGLIFIDL RDRTGIVQVV FNPETSKEAL
     EVAETIRSEY VLHVEGTVVE RGEGAINDNM ATGRIEVQAT KVNVLNAAKT TPIIIADDTD
     ASEDVRLKYR YLDLRRPVMF NTFKMRHDVT KTIRNFLDTE EFLEVETPIL TKSTPEGARD
     YLVPSRVHDG EFYALPQSPQ LFKQLLMVGG FERYYQVARC FRDEDLRADR QPEFTQIDIE
     ASFLTQDEIL DMMERMMTKV MKDAKGVEVS APFPRMKYAD AMARYGSDKP DTRFEMELTD
     LSEFAAGCGF KVFTSAVESG GQVKAINAKG AASKYSRKDI DALTEFVKVY GAKGLAWLKV
     EEDGLKGPIA KFFGEEDANV LMSTLEATAG DLLLFVADKK SVVADSLGAL RLRLGKELEL
     IDESKFNFLW VTDWPLLEYD EDADRYFAAH HPFTMPFRED VELLETAPEK ARAQAYDLVL
     NGYELGGGSL RIYERDVQEK MFKALGFSQE EAQEQFGFLL EAFEYGTPPH GGIALGLDRL
     VMLLAGRTNL RDTIAFPKTA SASCLLTEAP SPVAEAQLEE LNLKLSLKEE K
//
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