ID   SYD_BORA1               Reviewed;         596 AA.
AC   Q2L1K6;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   16-JUN-2009, entry version 25.
DE   RecName: Full=Aspartyl-tRNA synthetase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartate--tRNA ligase;
DE            Short=AspRS;
GN   Name=aspS; OrderedLocusNames=BAV0115;
OS   Bordetella avium (strain 197N).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=360910;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16885469; DOI=10.1128/JB.01927-05;
RA   Sebaihia M., Preston A., Maskell D.J., Kuzmiak H., Connell T.D.,
RA   King N.D., Orndorff P.E., Miyamoto D.M., Thomson N.R., Harris D.,
RA   Goble A., Lord A., Murphy L., Quail M.A., Rutter S., Squares R.,
RA   Squares S., Woodward J., Parkhill J., Temple L.M.;
RT   "Comparison of the genome sequence of the poultry pathogen Bordetella
RT   avium with those of B. bronchiseptica, B. pertussis, and B.
RT   parapertussis reveals extensive diversity in surface structures
RT   associated with host interaction.";
RL   J. Bacteriol. 188:6002-6015(2006).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate + tRNA(Asp) = AMP +
CC       diphosphate + L-aspartyl-tRNA(Asp).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM167904; CAJ47721.1; -; Genomic_DNA.
DR   RefSeq; YP_784653.1; -.
DR   GeneID; 6264502; -.
DR   GenomeReviews; AM167904_GR; BAV0115.
DR   KEGG; bav:BAV0115; -.
DR   NMPDR; fig|521.1.peg.1263; -.
DR   HOGENOM; Q2L1K6; -.
DR   OMA; Q2L1K6; VDRRRDH.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:HAMAP.
DR   HAMAP; MF_00044; -; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II_cons-reg.
DR   InterPro; IPR002312; Asp-tRNA-synth_IIb.
DR   InterPro; IPR004524; Asp-tRNA-synth_IIb_bac/mt.
DR   InterPro; IPR018153; Asp-tRNA-synth_IIb_C_bac/mt.
DR   InterPro; IPR004115; GAD.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA_bd_OB_tRNA-helicase.
DR   Gene3D; G3DSA:2.40.50.140; OB_NA_bd_sub; 1.
DR   PANTHER; PTHR22594; aa-tRNA-synt_II; 1.
DR   PANTHER; PTHR22594:SF5; AspS_bac; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
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    596       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_0000235510.
SQ   SEQUENCE   596 AA;  67155 MW;  62CD2B48A18794CB CRC64;
     MRTCYTGQVC RDHLGQTVTL YGWVNRRRDH GGVIFIDLRD RTGLAQIVFD PDNAGAFGTA
     ERLRNEFCVR VTGLVRERPQ GTTNAELASG EVEVLCRDVE ILNPSVTPPF QLDDDNLSET
     TRLTHRVLDL RRPQMQRNLM LRYRVSIEVR KFLDQLGFID IETPMLTKST PEGARDYLVP
     SRVNAGHFFA LPQSPQLFKQ MLMVSGFDRY YQITKCFRDE DLRADRQPEF TQIDCETSFL
     TETEIRAVFE SMIRHVFKVV QNVDLPDPFP IMTWTEAMAR FGSDKPDMRV NLEFTDVADI
     MRDVDFKVFA SAATTQGSRV VALRVPGGGE LSRSEIDAYT QFVGIYGAKG LAYIKVNDVA
     KGREGLQSPI VKNLHDAALA ELVKRTGAQD GDIIFFGADR AKVVNDALGA LRVKIGHSEF
     GKKTGLFSGG WRPLWVVDFP MFEYDEEEGR YTAAHHPFTS PKDGHEDFLE TDPSQAFAKA
     YDMVLNGWEI GGGSVRIHRE EVQSKVFRAL KIGPDEAREK FGFLLDALQY GAPPHGGIAF
     GLDRIVTMMT GADSIRDVIA FPKTQRAQDL LTQAPSSVDD KQLRELHIRL RNTEVK
//