ID   SYD_ARTS2               Reviewed;         596 AA.
AC   A0JXA1;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   16-JUN-2009, entry version 22.
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=Arth_2291;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Micrococcineae; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
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., Chertkov O., Thompson S., Brettin T., Bruce D., Han C.,
RA   Tapia R., Gilna P., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Mikhailova N., Beasley F., Chen W., Jerke K.,
RA   Nakatsu C.H., Richardson P.;
RT   "Complete sequence of chromosome 1 of Arthrobacter sp. FB24.";
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.
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DR   EMBL; CP000454; ABK03671.1; -; Genomic_DNA.
DR   RefSeq; YP_831771.1; -.
DR   GeneID; 4445334; -.
DR   GenomeReviews; CP000454_GR; Arth_2291.
DR   KEGG; art:Arth_2291; -.
DR   TIGR; Arth_2291; -.
DR   OMA; A0JXA1; 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; IPR004365; NA_bd_OB_tRNA-helicase.
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    596       Aspartyl-tRNA synthetase.
FT                                /FTId=PRO_1000006633.
SQ   SEQUENCE   596 AA;  65331 MW;  C92073621960756E CRC64;
     MLRTHDLGSL RSEHIGQTVT LAGWVGRRRD HGGVAFVDLR DASGVSQVVV REEEVFHGLR
     NEYVLQVIGT VSQRPEGNEN PALATGQIEV IAEKVTILNT SDPLPFQIDE HVEVGEEARL
     KHRYLDLRRP GPARNMRLRS EANRVARELL HRDGYVEIET PTLTRSTPEG ARDFVVPARL
     APGSWYALPQ SPQLFKQLLQ VGGFEKYYQI ARCYRDEDFR ADRQPEFTQL DIEASFVEQD
     DIISLGESIV KALWQLIDVE IPTPIQRITY ADAMARYGSD KPDLRFGLEL TELTEFFKDT
     NFGVFKAPYV GAVVMPGGAS QARRALDAWQ EWAKQRGAKG LAYVLFKEDG ELAGPVAKNL
     TDTERAGLAD AVGAKPGDCI FFAAGEKTPS RALLGAARVE IGHRTGLINP ADWAFCWVVD
     APMFEPAAAA VASGDVAVGA GQWTAVHHAF TSPKPEFMDS FDKDPESALS YAYDIVCNGN
     EIGGGSIRIH ERDVQERVFE LMGLDKADAE TKFGFLLEGF KFGAPPHGGI AFGWDRVVAL
     LAGVESIRDV IAFPKSGGGY DPLTQAPAPI TAQQRKEAGV DFKPEAKKAD PGATKA
//