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Database: UniProt/TrEMBL
Entry: D3UNA2_LISSS
LinkDB: D3UNA2_LISSS
Original site: D3UNA2_LISSS 
ID   D3UNA2_LISSS            Unreviewed;       591 AA.
AC   D3UNA2;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   11-JUN-2014, entry version 32.
DE   RecName: Full=Aspartate--tRNA ligase;
DE            EC=6.1.1.12;
DE   AltName: Full=Aspartyl-tRNA synthetase;
GN   Name=aspS; OrderedLocusNames=lse_1434;
OS   Listeria seeligeri serovar 1/2b (strain ATCC 35967 / DSM 20751 / CIP
OS   100100 / SLCC 3954).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=683837;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35967 / DSM 20751 / CIP 100100 / SLCC 3954;
RX   PubMed=20061480; DOI=10.1128/JB.01415-09;
RA   Steinweg C., Kuenne C.T., Billion A., Mraheil M.A., Domann E.,
RA   Ghai R., Barbuddhe S.B., Karst U., Goesmann A., Puhler A.,
RA   Weisshaar B., Wehland J., Lampidis R., Kreft J., Goebel W.,
RA   Chakraborty T., Hain T.;
RT   "Complete genome sequence of Listeria seeligeri, a nonpathogenic
RT   member of the genus Listeria.";
RL   J. Bacteriol. 192:1473-1474(2010).
CC   -!- FUNCTION: Catalyzes the attachment of glutamate to tRNA(Asp) in a
CC       two-step reaction: aspartate is first activated by ATP to form
CC       Asp-AMP and then transferred to the acceptor end of tRNA(Asp) (By
CC       similarity).
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; FN557490; CBH27585.1; -; Genomic_DNA.
DR   RefSeq; YP_003464671.1; NC_013891.1.
DR   EnsemblBacteria; CBH27585; CBH27585; lse_1434.
DR   GeneID; 9082185; -.
DR   KEGG; lsg:lse_1434; -.
DR   PATRIC; 32262767; VBILisSee138575_1430.
DR   HOGENOM; HOG000275160; -.
DR   KO; K01876; -.
DR   OMA; LTTEPHK; -.
DR   BioCyc; LSEE683837:GI10-1457-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004815; F:aspartate-tRNA ligase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006422; P:aspartyl-tRNA aminoacylation; IEA:UniProtKB-HAMAP.
DR   Gene3D; 2.40.50.140; -; 1.
DR   Gene3D; 3.30.1360.30; -; 1.
DR   HAMAP; MF_00044_B; Asp_tRNA_synth_B; 1.
DR   InterPro; IPR004364; aa-tRNA-synt_II.
DR   InterPro; IPR018150; aa-tRNA-synt_II-like.
DR   InterPro; IPR006195; aa-tRNA-synth_II.
DR   InterPro; IPR004524; Asp-tRNA-ligase_IIb_bac/mt.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR004115; GAD-like.
DR   InterPro; IPR029351; GAD_dom.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF5; PTHR22594:SF5; 1.
DR   Pfam; PF02938; GAD; 1.
DR   Pfam; PF00152; tRNA-synt_2; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   PRINTS; PR01042; TRNASYNTHASP.
DR   SUPFAM; SSF50249; SSF50249; 1.
DR   SUPFAM; SSF55261; SSF55261; 1.
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   NP_BIND     222    224       ATP (By similarity){EA13}.
FT   NP_BIND     536    539       ATP (By similarity){EA13}.
FT   REGION      200    203       Aspartate (By similarity).
FT   BINDING     176    176       Aspartate (By similarity){EA13}.
FT   BINDING     222    222       Aspartate (By similarity){EA13}.
FT   BINDING     231    231       ATP (By similarity){EA13}.
FT   BINDING     450    450       Aspartate (By similarity){EA13}.
FT   BINDING     484    484       ATP (By similarity){EA13}.
FT   BINDING     491    491       Aspartate (By similarity){EA13}.
SQ   SEQUENCE   591 AA;  66220 MW;  88F0486744219E55 CRC64;
     MEKRTSYCGE LNETHIGQNV ILHGWVQKRR DLGGLIFIDL RDREGIIQVV FNPETSKEAL
     AIADSVRNEF VVTIKGKVSA RSENAINEKL ATGKIEISAE EITILNTSKT PPFYIEDGVN
     VSDELRLKYR YLDLRRPEMN NIFKMRHTVT RTFRNKLDAL GFFDIETPYL TKSTPEGARD
     YLVPSRVYPG NFYALPQSPQ ILKQLLMTAG FDKYYQIVRC FRDEDLRGDR QPEFTQIDLE
     TSFLTKEEIQ TITEDMLIDV VKEAKNITIQ KPFPRMTYKE AMDRFGSDKP DIRFGLELQN
     VSEVVKDVDF KVFQSAVENG GEVKAINAKG AATNFSRKDL DALGVFVANY GAKGLAWLKV
     EAGELKGPIA KFFQAEKAQE LMAALQAEDG DLLLFAADKA EVVAASLGAL RNKLGKELAL
     INEEELAFLW VTDWPLFEYD EEAGRYVSAH HPFTLPKEED IPLLETDSSK VMAEAYDIVL
     NGYEIGGGSL RIYKKEVQES MFRALGFTDE AASEQFGFLM EALEYGTPPH GGIALGLDRI
     VMILAGRNNL RDTIAFPKTG SAVDPLTNAP GEVSEAQLAE LKLATVKKES N
//
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