ID   SYN_BAUCH               Reviewed;         467 AA.
AC   Q1LT63;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2006, sequence version 1.
DT   16-JUN-2009, entry version 29.
DE   RecName: Full=Asparaginyl-tRNA synthetase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparagine--tRNA ligase;
DE            Short=AsnRS;
GN   Name=asnS; OrderedLocusNames=BCI_0408;
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-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
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; CP000238; ABF13990.1; -; Genomic_DNA.
DR   RefSeq; YP_588851.1; -.
DR   GeneID; 4056737; -.
DR   GenomeReviews; CP000238_GR; BCI_0408.
DR   KEGG; bci:BCI_0408; -.
DR   HOGENOM; Q1LT63; -.
DR   OMA; Q1LT63; LQKKRHS.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:HAMAP.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:HAMAP.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:InterPro.
DR   HAMAP; MF_00534; -; 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; IPR004522; Asn-tRNA-synth_IIb.
DR   InterPro; IPR002312; Asp-tRNA-synth_IIb.
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   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   TIGRFAMs; TIGR00457; asnS; 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    467       Asparaginyl-tRNA synthetase.
FT                                /FTId=PRO_1000051380.
SQ   SEQUENCE   467 AA;  53150 MW;  79F9BDE893AFFDF6 CRC64;
     MIILPIAKIL QGIILAADHE VIVQGWVRTR RDSKAGISFL SIYDGSCLDS LQVIINHDLP
     NYKSDVLHLT TGCSVVITGS IVTSIGVGQH FEIQAKNIKV LGWVKNPETY PITAKKHSLE
     FLREVAHLRP RTNIIGAVTR VRHTLAQAIH RFMHIEGFFW VSTPLITTFN CEGAGEMFRV
     STLDLENLPY TSKGKINYEK DFFGKEAFLT VSGQLNGESY ACALSKIYTF GPTFRAENSN
     TSRHLAEFWM VEPEVAFANL TDIAILAEKM LKYIFNAILI ERVDDINFFA EQINKNIIKR
     LEQFISSNFA QIDYTEAIDI LQNCKQKFDH TVFWGMDLFA EHERYLADKH FQAPVVVTNY
     PKDIKAFYMR INDDGKTVAA MDVLAPGIGE IIGGSQREER LAKLDQRLAD RGLNIEDYWW
     YRDLRSYGTV PHSGFGLGLE RLMIYITGMH NIRDVIPFPR NPRQASF
//