ID   SYD_ALHEH               Reviewed;         592 AA.
AC   Q0A582;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   17-OCT-2006, sequence version 1.
DT   16-JUN-2009, entry version 26.
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=Mlg_2665;
OS   Alkalilimnicola ehrlichei (strain MLHE-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Alkalilimnicola.
OX   NCBI_TaxID=187272;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Sims D., Brettin T., Bruce D., Han C., Tapia R., Gilna P.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Oremland R.S., Hoeft S.E., Switzer-Blum J., Kulp T.,
RA   King G., Tabita R., Witte B., Santini J.M., Basu P., Hollibaugh J.T.,
RA   Xie G., Stolz J.F., Richardson P.;
RT   "Complete sequence of Alkalilimnicola ehrilichei MLHE-1.";
RL   Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; CP000453; ABI58005.1; -; Genomic_DNA.
DR   RefSeq; YP_743495.1; -.
DR   GeneID; 4268798; -.
DR   GenomeReviews; CP000453_GR; Mlg_2665.
DR   KEGG; aeh:Mlg_2665; -.
DR   NMPDR; fig|187272.6.peg.2542; -.
DR   HOGENOM; Q0A582; -.
DR   OMA; Q0A582; 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    592       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006631.
SQ   SEQUENCE   592 AA;  66792 MW;  A0D5FB4D7D5337E6 CRC64;
     MRTHYCGHVS ETDLDQEVTL CGWAHRRRDH GGVIFIDLRD REGLVQVVFD PDRPETFALA
     ERVRSEFVLK VRGRVRRRPA GTENPDLPTG QVEVLGLELD LLNPAKTPPF QLDEHEQAGE
     DVRLRYRYVD LRRPEMLQRL RARARITSNL RRFLDEHGFL DIETPMLTRA TPEGARDYLV
     PSRTHPGSFF ALPQSPQLFK QLLMMAGMDR YYQIVRCFRD EDLRADRQPE FTQLDIETSF
     MDEEGIMHLT ERMMRRLFAD VLQVDLPDPF PRMGYAEAMA RFGSDKPDLR IPLELVEVAD
     LMGGVEFKVF AGPAADPRGR VAALHVPGGA GLTRKQIDDY TQFVGRYGAK GLAYIKVNDP
     AQGREGLQSP ILKFLTDEAV DGILRRTEAR AGDLIFFGAD KAKVVNDALG ALRVKLGHDL
     AMVEDEWRPL WVVDFPMFEY DEKDGRLYAL HHPFTAPNVD DPAELADKDP EQLVSRAYDM
     VLNGTELGGG SVRIHRQDMQ QAVFRLLGID EDEARAKFGF LLDALEYGAP PHGGIAFGLD
     RLVMLMTGAS SIREVMAFPK TQTAACLLTD APAEVDIAQL QELALRITKP QA
//