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Database: UniProt/TrEMBL
Entry: E4SZE2_LACDN
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ID   E4SZE2_LACDN            Unreviewed;       432 AA.
AC   E4SZE2;
DT   08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT   08-FEB-2011, sequence version 1.
DT   14-MAY-2014, entry version 26.
DE   RecName: Full=Asparagine--tRNA ligase;
DE            EC=6.1.1.22;
DE   AltName: Full=Asparaginyl-tRNA synthetase;
GN   Name=asnS; Synonyms=asnC; OrderedLocusNames=LDBND_0899;
OS   Lactobacillus delbrueckii subsp. bulgaricus (strain ND02).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=767455;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ND02;
RA   Chen W., Zhang H., Sun Z., Chen X., Guo Z., Wang J., Wu L., Zhang X.,
RA   Zhou Z., Sun T., Wang L., Meng H.;
RT   "Complete genome sequence of Lactobacillus delbrueckii subsp.
RT   bulgaricus strain ND02.";
RL   Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: ATP + L-asparagine + tRNA(Asn) = AMP +
CC       diphosphate + L-asparaginyl-tRNA(Asn).
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; CP002341; ADQ60942.1; -; Genomic_DNA.
DR   RefSeq; YP_004033919.1; NC_014727.1.
DR   EnsemblBacteria; ADQ60942; ADQ60942; LDBND_0899.
DR   GeneID; 9990584; -.
DR   KEGG; lde:LDBND_0899; -.
DR   PATRIC; 43081178; VBILacDel160915_0903.
DR   HOGENOM; HOG000226034; -.
DR   KO; K01893; -.
DR   OMA; EMIRATY; -.
DR   BioCyc; LDEL767455:GHXE-942-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004816; F:asparagine-tRNA ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006421; P:asparaginyl-tRNA aminoacylation; IEA:InterPro.
DR   Gene3D; 2.40.50.140; -; 1.
DR   HAMAP; MF_00534; Asn_tRNA_synth; 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; IPR004522; Asn-tRNA-ligase.
DR   InterPro; IPR002312; Asp/Asn-tRNA-synth_IIb.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   PANTHER; PTHR22594; PTHR22594; 1.
DR   PANTHER; PTHR22594:SF16; PTHR22594:SF16; 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   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.
SQ   SEQUENCE   432 AA;  50014 MW;  8AC545D5E76FEC52 CRC64;
     MTELISIRES AKHVDEEVRM HVWLTDKRSS GKIVFLQLRD GTAFFQGVVR KNDVSEEVFE
     AAKGLRQEAS FYLTGTIHED ARSHFGYEIQ ISDLEVVSNN EGYPITNKEH GIDFLLDHRH
     LWLRSRRPFA IMQIRNRIFK ATVDFFENEG FVKFDAPLLM HSAPEGTTEL FHIDYFDHDA
     YLSQSGQLYG EVGAEAFGKI FTFGPTFRAE ASKTRRHLTE FWMMEPEMAW MHQDESLDLQ
     ERFLSYVVGQ VLEHCEYELS ILGRDLDKLR PAAEGNYTRL SYDDAVKMLQ EAGKDFKWGD
     DFGAPDEAFL SEQFDRPFFI VNYPVAIKPF YMKKNPENPL TYLCADVEAP EGYGEIMGGS
     EREADYDTLK AQIEEAGLNL DDYSWYLDLR KYGSVPHSGF GMGFERVIAW ICKLDHVREA
     VPFPRMIKRM QP
//
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