(data stored in ACNUC7421 zone)

SWISSPROT: DTD_PSEHT

ID   DTD_PSEHT               Reviewed;         145 AA.
AC   Q3IJ42;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   30-AUG-2017, entry version 76.
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=PSHAa0172;
OS   Pseudoalteromonas haloplanktis (strain TAC 125).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=326442;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TAC 125;
RX   PubMed=16169927; DOI=10.1101/gr.4126905;
RA   Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N.,
RA   Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G.,
RA   Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C.,
RA   Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G.,
RA   Danchin A.;
RT   "Coping with cold: the genome of the versatile marine Antarctica
RT   bacterium Pseudoalteromonas haloplanktis TAC125.";
RL   Genome Res. 15:1325-1335(2005).
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; CR954246; CAI85275.1; -; Genomic_DNA.
DR   RefSeq; WP_011326890.1; NC_007481.1.
DR   ProteinModelPortal; Q3IJ42; -.
DR   SMR; Q3IJ42; -.
DR   STRING; 326442.PSHAa0172; -.
DR   EnsemblBacteria; CAI85275; CAI85275; PSHAa0172.
DR   KEGG; pha:PSHAa0172; -.
DR   PATRIC; fig|326442.8.peg.166; -.
DR   eggNOG; ENOG4108YYA; Bacteria.
DR   eggNOG; COG1490; LUCA.
DR   HOGENOM; HOG000113982; -.
DR   KO; K07560; -.
DR   OMA; DGPVTIW; -.
DR   OrthoDB; POG091H02D0; -.
DR   Proteomes; UP000006843; Chromosome I.
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; Q3IJ42.
DR   SWISS-2DPAGE; Q3IJ42.
KW   Complete proteome; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN         1    145       D-aminoacyl-tRNA deacylase.
FT                                /FTId=PRO_0000259296.
FT   ACT_SITE     80     80       Nucleophile. {ECO:0000255|HAMAP-
FT                                Rule:MF_00518}.
SQ   SEQUENCE   145 AA;  15742 MW;  549D50C933CBE853 CRC64;
     MQGLIQRVKH AKVEINNQVV GEIGQGILVL LGVEKQDDEQ AADKLLHKIS NYRIFTDEND
     KMNLSLKDIA GELLVVSQFT LAANTKKGMR PSFSSAATPS QANELYEYFV AQAKALNLTV
     AAGEFGADMQ VSLCNDGPVT FNLAV
//

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