(data stored in ACNUC7421 zone)

SWISSPROT: DTDA_SULIK

ID   DTDA_SULIK              Reviewed;         237 AA.
AC   C4KJG8;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   07-JUL-2009, sequence version 1.
DT   07-JUN-2017, entry version 40.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000255|HAMAP-Rule:MF_00562};
DE            EC=3.1.1.96 {ECO:0000255|HAMAP-Rule:MF_00562};
DE   AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN   Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562};
GN   OrderedLocusNames=M164_0052;
OS   Sulfolobus islandicus (strain M.16.4 / Kamchatka #3).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=426118;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.16.4 / Kamchatka #3;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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_00562}.
CC   -!- CATALYTIC ACTIVITY: A D-aminoacyl-tRNA + H(2)O = a D-amino acid +
CC       tRNA. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC       Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00562};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- SIMILARITY: Belongs to the DtdA deacylase family.
CC       {ECO:0000255|HAMAP-Rule:MF_00562}.
DR   EMBL; CP001402; ACR40688.1; -; Genomic_DNA.
DR   RefSeq; WP_012710231.1; NC_012726.1.
DR   SMR; C4KJG8; -.
DR   EnsemblBacteria; ACR40688; ACR40688; M164_0052.
DR   GeneID; 8759891; -.
DR   KEGG; sid:M164_0052; -.
DR   HOGENOM; HOG000107871; -.
DR   KO; K09716; -.
DR   OMA; CYEATHH; -.
DR   OrthoDB; POG093Z07LR; -.
DR   BioCyc; SISL426118:GI01-52-MONOMER; -.
DR   Proteomes; UP000001479; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:InterPro.
DR   HAMAP; MF_00562; Deacylase_DtdA; 1.
DR   InterPro; IPR018033; Deacylase_DtdA_archaea.
DR   InterPro; IPR007508; DtdA.
DR   Pfam; PF04414; tRNA_deacylase; 1.
DR   PIRSF; PIRSF016210; UCP016210; 1.
PE   3: Inferred from homology;
DR   PRODOM; C4KJG8.
DR   SWISS-2DPAGE; C4KJG8.
KW   Complete proteome; Hydrolase; Metal-binding; Zinc.
FT   CHAIN         1    237       D-aminoacyl-tRNA deacylase.
FT                                /FTId=PRO_1000212045.
SQ   SEQUENCE   237 AA;  26762 MW;  D31B42FFCE46FA95 CRC64;
     MDIKLVYSTS DPVGLTIKKL GYSFEEIDED VTDFHYKNGE AIVIFSRHES KASIPSLTVH
     YPGNPSEEVM GGEPKKLGIA YPRLLTSILR EIKKIDLDIE KTMEATHHGP TYQNVPVIFV
     EIGSDKTYWT NERIVRTLVD STLKGIDKVD ETDCRDYISG FGGPHYSKLF TKLADESCIG
     HVISKHYVDK LDDKVIIQAI ANSVNNINKV VIDSLNLKQR ERIIAALKSF DIHIQLR
//

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