ID   SYD_BLOPB               Reviewed;         574 AA.
AC   Q492L1;
DT   16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   16-JUN-2009, entry version 27.
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=BPEN_467;
OS   Blochmannia pennsylvanicus (strain BPEN).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacteriales;
OC   Enterobacteriaceae; ant endosymbionts; Candidatus Blochmannia.
OX   NCBI_TaxID=291272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16077009; DOI=10.1101/gr.3771305;
RA   Degnan P.H., Lazarus A.B., Wernegreen J.J.;
RT   "Genome sequence of Blochmannia pennsylvanicus indicates parallel
RT   evolutionary trends among bacterial mutualists of insects.";
RL   Genome Res. 15:1023-1033(2005).
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; CP000016; AAZ41086.1; -; Genomic_DNA.
DR   RefSeq; YP_277962.1; -.
DR   GeneID; 3562963; -.
DR   GenomeReviews; CP000016_GR; BPEN_467.
DR   KEGG; bpn:BPEN_467; -.
DR   HOGENOM; Q492L1; -.
DR   OMA; Q492L1; VDRRRDH.
DR   BioCyc; CBLO291272:BPEN_467-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    574       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_0000235509.
SQ   SEQUENCE   574 AA;  66034 MW;  4DBCFE93C0CD6A0F CRC64;
     MRTAYCGQLN LSHVGLEVTL CGWINKYRNF GGLIFIDLRD REGCIQVCFD VYQNKEVCIS
     AAKLKQEFCI QLIGMVRARP KNQINSNIST GAVEVVAKKF SILNISDPLP LDISKNNIEE
     NRLKYRYLDL RRSIMFDRIK TRSRIMSIVH RFMELEGFLN IETPMLTKVT PEGSRDYIVP
     SRLHAGKNYA LPQSPQIFKQ LLMVSGFDRY YQITKCFRDE DLRADRQPEF TQIDIETSFM
     TTQKIRELME IFIRIIWREI LNVELGVFSQ FTYSEVMQRF GSDAPDLRNP IEMFDVSYLF
     NSTQNRLSFI RANNIGVQAI AMKVPNGRQL TQKQIDEYIY YSKQCGLKEL LWVKVQFSDN
     DITKKEIQGS VTNFIDNLTL DIILNKTNIK SNDILFVGFN DNKNQFITKM LSALRLKLGN
     DLCLIKKDSW APLWIIDFPM FKKNCHGEYT SMHHMFTSPK NCDVQMLKKD PLLVISEAYD
     MVINGCEIGS GSARIHSFDM QQAVFNILGI TQNDQKKKFG YFMDALKYGA PPHAGLAFGL
     DRIAMLLTGS KNIREVIAFP KTTASVDIMA NAPD
//