ID   SYD_ALCBS               Reviewed;         587 AA.
AC   Q0VRK1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   05-SEP-2006, sequence version 1.
DT   16-JUN-2009, entry version 28.
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=ABO_0749;
OS   Alcanivorax borkumensis (strain SK2 / ATCC 700651 / DSM 11573).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC   Alcanivoracaceae; Alcanivorax.
OX   NCBI_TaxID=393595;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16878126; DOI=10.1038/nbt1232;
RA   Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T.,
RA   Brecht M., Buhrmester J., Chernikova T.N., Denaro R., Ferrer M.,
RA   Gertler C., Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N.,
RA   Lang S., Linke B., McHardy A.C., Meyer F., Nechitaylo T., Puehler A.,
RA   Regenhardt D., Rupp O., Sabirova J.S., Selbitschka W., Yakimov M.M.,
RA   Timmis K.N., Vorhoelter F.-J., Weidner S., Kaiser O., Golyshin P.N.;
RT   "Genome sequence of the ubiquitous hydrocarbon-degrading marine
RT   bacterium Alcanivorax borkumensis.";
RL   Nat. Biotechnol. 24:997-1004(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 (By similarity).
CC   -!- SIMILARITY: Belongs to the class-II aminoacyl-tRNA synthetase
CC       family.
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DR   EMBL; AM286690; CAL16197.1; -; Genomic_DNA.
DR   RefSeq; YP_692469.1; -.
DR   GeneID; 4213839; -.
DR   GenomeReviews; AM286690_GR; ABO_0749.
DR   KEGG; abo:ABO_0749; -.
DR   NMPDR; fig|393595.12.peg.752; -.
DR   HOGENOM; Q0VRK1; -.
DR   OMA; Q0VRK1; VDRRRDH.
DR   BioCyc; ABOR393595:ABO_0749-MON; -.
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    587       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006630.
SQ   SEQUENCE   587 AA;  65330 MW;  991D56D498DD71AC CRC64;
     MRSHYCGDLR ASHDGETVEL CGWVSRRRDH GGVIFLDLRD RNGLVQVVFD PDTVDAFALA
     DKVRSEYVVR LSGRVRMRDE SVRNNKMATG DIEVLGKELT ILNEAETPPF ELDAHSAAGE
     EVRLKYRYMD LRRPDVLKNF QFRSRLTHVV RAFLEGEGFM DVETPILTRA TPEGARDYLV
     PSRTHPGSFF ALPQSPQLFK QLLMVAGFDR YYQIAKCFRD EDLRADRQPE FTQIDLEASF
     VEEEDIMGIT ERMVRSVFKE LLSVDLPDFP RMPFSEAMQR FGSDKPDLRI ALELIDIADL
     LAGVDFKVFS GPANDPKGRV AAMRVPGGCS LSRKDIDGYT KFVSIYGAKG LAYIKVNDLA
     AGAEGLQSPI LKFLTEDAIK GILERTGAET GDLIFFGADK AKIVNEALGA LRVKVGHDLN
     LVEGEWAPLW VVDFPMFEED EGQYHALHHP FTMPSCSAEE LKSNPGEALS RAYDMVLNGT
     ELGGGSIRIH SPAMQRTVFE ALGISDEEAE EKFGFLLDGL KYGAPPHGGL AFGLDRMVML
     MTGCESIRDV IAFPKTQTAA CTMTNAPSPV DNKQLREVGV QVRKEEG
//