ID   SYD_BRASB               Reviewed;         590 AA.
AC   A5EIE6;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-JUN-2007, sequence version 1.
DT   16-JUN-2009, entry version 17.
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=BBta_3864;
OS   Bradyrhizobium sp. (strain BTAi1 / ATCC BAA-1182).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium.
OX   NCBI_TaxID=288000;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=17540897; DOI=10.1126/science.1139548;
RA   Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.-C.,
RA   Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA   Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S.,
RA   Rouy Z., Mangenot S., Segurens B., Dossat C., Franck W.L.,
RA   Chang W.-S., Saunders E., Bruce D., Richardson P., Normand P.,
RA   Dreyfus B., Pignol D., Stacey G., Emerich D., Vermeglio A.,
RA   Medigue C., Sadowsky M.;
RT   "Legumes symbioses: absence of nod genes in photosynthetic
RT   bradyrhizobia.";
RL   Science 316:1307-1312(2007).
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; CP000494; ABQ35940.1; -; Genomic_DNA.
DR   RefSeq; YP_001239846.1; -.
DR   GeneID; 5150013; -.
DR   GenomeReviews; CP000494_GR; BBta_3864.
DR   KEGG; bbt:BBta_3864; -.
DR   OMA; A5EIE6; YQLDVEM.
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    590       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006641.
SQ   SEQUENCE   590 AA;  66606 MW;  512DE030B649AF4D CRC64;
     MHRYRTHTCG ALRDSNIGET VRLSGWCHRI RDHGGVLFVD LRDHYGITQC VVDPDSKAFG
     LAEKLRSEWV VRMEGKVRRR PEGTDNAELP TGQVELYVAD IEVLGPAAEL PLPVFGEQEY
     PEDIRLKYRF LDLRREKLHQ NIMTRGAIID SMRRRMKEQG FFEFQTPILT ASSPEGARDF
     LVPSRIHPGK FYALPQAPQQ YKQLLMMSGF DRYFQIAPCF RDEDPRADRL PGEFYQLDVE
     MSFVEQEDVF AAMEPVITGV FEDFAKGKPV TKGWPRIPFA EALRKYGTDK PDLRNPIEMQ
     DVSEHFRGSG FKVFARMLED TKNQVWAIPA PGGGSRAFCD RMNSWAQGEG QPGLGYIMWR
     EGGEGAGPLA NNIGPERTAA IRTQLGTKEG DAAFFVAGDP EKFWKFAGLA RTKVGEELNL
     IDKDRFALAW IVDFPMYEYN EDDKKVDFSH NPFSMPQGGL EALQTKDPLT IKAFQYDIAC
     NGYEIASGGI RNHKPEAMVK AFEIAGYGEQ EVVDRFGGMY RAFQYGAPPH GGMAAGVDRI
     VMLLCGTTNL REISLFPMNQ QAMDLLMGAP SEATTKQLRE LHIRTNLPNK
//