(data stored in ACNUC7421 zone)

SWISSPROT: DTD_SHESH

ID   DTD_SHESH               Reviewed;         145 AA.
AC   A8FPZ5;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   30-AUG-2017, entry version 61.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00518};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00518};
DE   AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN   Name=dtd {ECO:0000255|HAMAP-Rule:MF_00518};
GN   OrderedLocusNames=Ssed_0305;
OS   Shewanella sediminis (strain HAW-EB3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=425104;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HAW-EB3;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T.,
RA   Dalin E., Tice H., Pitluck S., Chertkov O., Brettin T., Bruce D.,
RA   Detter J.C., Han C., Schmutz J., Larimer F., Land M., Hauser L.,
RA   Kyrpides N., Kim E., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella sediminis HAW-EB3.";
RL   Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate
CC       specificity. By recycling D-aminoacyl-tRNA to D-amino acids and
CC       free tRNA molecules, this enzyme counteracts the toxicity
CC       associated with the formation of D-aminoacyl-tRNA entities in
CC       vivo. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid +
CC       tRNA. {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00518}.
CC   -!- SIMILARITY: Belongs to the DTD family. {ECO:0000255|HAMAP-
CC       Rule:MF_00518}.
DR   EMBL; CP000821; ABV34918.1; -; Genomic_DNA.
DR   RefSeq; WP_012004444.1; NC_009831.1.
DR   ProteinModelPortal; A8FPZ5; -.
DR   SMR; A8FPZ5; -.
DR   STRING; 425104.Ssed_0305; -.
DR   EnsemblBacteria; ABV34918; ABV34918; Ssed_0305.
DR   KEGG; sse:Ssed_0305; -.
DR   eggNOG; ENOG4108YYA; Bacteria.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113982; -.
DR   KO; K07560; -.
DR   OMA; DGPVTIW; -.
DR   OrthoDB; POG091H02D0; -.
DR   Proteomes; UP000002015; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   CDD; cd00563; Dtyr_deacylase; 1.
DR   Gene3D; 3.50.80.10; -; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 1.
DR   InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR   InterPro; IPR023509; DTD-like_dom.
DR   PANTHER; PTHR10472; PTHR10472; 1.
DR   Pfam; PF02580; Tyr_Deacylase; 1.
DR   SUPFAM; SSF69500; SSF69500; 1.
DR   TIGRFAMs; TIGR00256; TIGR00256; 1.
PE   3: Inferred from homology;
DR   PRODOM; A8FPZ5.
DR   SWISS-2DPAGE; A8FPZ5.
KW   Complete proteome; Cytoplasm; Hydrolase.
FT   CHAIN         1    145       D-aminoacyl-tRNA deacylase.
FT                                /FTId=PRO_1000081668.
FT   ACT_SITE     80     80       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   145 AA;  15578 MW;  FD350235959118E4 CRC64;
     MIALIQRVTQ AKVDVDGKTI GAIDKGLLVL LGVEREDDSF KMEKLANKVM SYRVFSDENG
     KMNLNVSQAG GALLVVSQFT LAADTGRGLR PSFSGAGTPD QAKVLYEEFV AFCRAKGMPT
     QTGEFAADMQ VSLVNDGPVT FNLQV
//

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