ID   SYD_BAUCH               Reviewed;         589 AA.
AC   Q1LTF0;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-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=BCI_0315;
OS   Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Candidatus Baumannia.
OX   NCBI_TaxID=374463;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA   Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L.,
RA   Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L.,
RA   Moran N.A., Eisen J.A.;
RT   "Metabolic complementarity and genomics of the dual bacterial
RT   symbiosis of sharpshooters.";
RL   PLoS Biol. 4:1079-1092(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; CP000238; ABF14266.1; -; Genomic_DNA.
DR   RefSeq; YP_588764.1; -.
DR   GeneID; 4056450; -.
DR   GenomeReviews; CP000238_GR; BCI_0315.
DR   KEGG; bci:BCI_0315; -.
DR   HOGENOM; Q1LTF0; -.
DR   OMA; Q1LTF0; 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    589       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006639.
SQ   SEQUENCE   589 AA;  67501 MW;  52E7422E511E9BF2 CRC64;
     MRTIYCGQLN KSHLGQEVIL CGWVYRYRNL GRLIFIELSD REGRVQVVFD LTHPSIFSNA
     AKLRNDFCIQ LHGIVRTRLD KQINYNITTG EIEVLATNLT ILNSSQPLPL DINFHNNEEQ
     RLKFRYLDLR NPEMAQRLKL RAKITSLVRH FMEKKGFLDI ETPMLTKTTP EGARDYLVPS
     RVHKGQFYAL PQSPQLFKQL LMISGFDRYY QIVKCFRDED LRADRQPEFT QIDVEASFIN
     AEQICKIMED LVRHLWREIQ EVELENFQYM SYTAAMYRFG SDKPDLRNPI EIVDVVDLVK
     NTTCTILADI AKDIKNRVVA LRVPNGAKLS LNDIKKYEKY IQTYGIKFII WMKVYQGKDG
     VKTTQSSITK YLLPEDIMSI IERTGACDGD ILFFAAGNNN IINNVMGALR IKLGCDLKLN
     RENSWAPLWI VDFPMFEKDD EGNLHAVHHP FTAPKNIDIP TLLQYPLKAK ANAYDMVING
     YEVGSGSVRI HCAELQQTIF SILGMTRNEQ SSKFGFFIDA LKYGAPPHAG FAFGLDRLVM
     LLTSTENIRD VIAFPKTTTA IDLMTEAPSI GNTIALKELS IEILDKNKI
//