ID D3UNA2_LISSS Unreviewed; 591 AA.
AC D3UNA2;
DT 20-APR-2010, integrated into UniProtKB/TrEMBL.
DT 20-APR-2010, sequence version 1.
DT 01-MAY-2013, entry version 26.
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 -!- 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 BioCyc; LSEE683837:GI10-2025-MONOMER; -.
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 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_dom.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR004365; NA-bd_OB_tRNA-helicase.
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; 1.
DR PRINTS; PR01042; TRNASYNTHASP.
DR SUPFAM; SSF50249; Nucleic_acid_OB; 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.
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
//
