ID   DTDA_THEKO              Reviewed;         272 AA.
AC   Q5JH30;
DT   30-AUG-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-FEB-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
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}; OrderedLocusNames=TK1422;
OS   Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)
OS   (Pyrococcus kodakaraensis (strain KOD1)).
OC   Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC   Thermococcus.
OX   NCBI_TaxID=69014;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-918 / JCM 12380 / KOD1;
RX   PubMed=15710748; DOI=10.1101/gr.3003105;
RA   Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.;
RT   "Complete genome sequence of the hyperthermophilic archaeon Thermococcus
RT   kodakaraensis KOD1 and comparison with Pyrococcus genomes.";
RL   Genome Res. 15:352-363(2005).
CC   -!- FUNCTION: D-aminoacyl-tRNA deacylase with broad substrate specificity.
CC       By recycling D-aminoacyl-tRNA to D-amino acids and free tRNA molecules,
CC       this enzyme counteracts the toxicity associated with the formation of
CC       D-aminoacyl-tRNA entities in vivo. {ECO:0000255|HAMAP-Rule:MF_00562}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a D-aminoacyl-tRNA + H2O = a D-alpha-amino acid + a tRNA +
CC         H(+); Xref=Rhea:RHEA:13953, Rhea:RHEA-COMP:10123, Rhea:RHEA-
CC         COMP:10124, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:59871,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:79333; EC=3.1.1.96;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00562};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=glycyl-tRNA(Ala) + H2O = glycine + H(+) + tRNA(Ala);
CC         Xref=Rhea:RHEA:53744, Rhea:RHEA-COMP:9657, Rhea:RHEA-COMP:13640,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57305,
CC         ChEBI:CHEBI:78442, ChEBI:CHEBI:78522; EC=3.1.1.96;
CC         Evidence={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. {ECO:0000255|HAMAP-
CC       Rule:MF_00562}.
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DR   EMBL; AP006878; BAD85611.1; -; Genomic_DNA.
DR   RefSeq; WP_011250373.1; NC_006624.1.
DR   AlphaFoldDB; Q5JH30; -.
DR   SMR; Q5JH30; -.
DR   STRING; 69014.TK1422; -.
DR   PRIDE; Q5JH30; -.
DR   EnsemblBacteria; BAD85611; BAD85611; TK1422.
DR   GeneID; 3235448; -.
DR   KEGG; tko:TK1422; -.
DR   PATRIC; fig|69014.16.peg.1384; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_056464_1_0_2; -.
DR   InParanoid; Q5JH30; -.
DR   OMA; CYEATHH; -.
DR   OrthoDB; 84039at2157; -.
DR   PhylomeDB; Q5JH30; -.
DR   Proteomes; UP000000536; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IBA:GO_Central.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019478; P:D-amino acid catabolic process; IEA:UniProtKB-UniRule.
DR   HAMAP; MF_00562; Deacylase_DtdA; 1.
DR   InterPro; IPR018033; Deacylase_DtdA_archaea.
DR   InterPro; IPR007508; DtdA.
DR   PANTHER; PTHR34667; PTHR34667; 1.
DR   Pfam; PF04414; tRNA_deacylase; 1.
DR   PIRSF; PIRSF016210; UCP016210; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..272
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000158973"
SQ   SEQUENCE   272 AA;  30393 MW;  F37A3FF207281779 CRC64;
     MKVVMTTKVD LASMNIREKL IENFGFKEDE LLFDGNPVYQ KDDVVILTTN QEMIYYDGLD
     RAIERQTGIK PEIIAFASRH SSKQKLPALT THVTGNWGGA LYGGKDESLA IAQPSAMKLA
     LLKMNELNDL GWTVCYEATH HGPSELDVPS FFIEIGSSEE EWVNDRAGEI VAETIIYVLE
     NYQNSKFKVA VGIGGGHYAP KQTKRALQTD LAFGHIAPKY AHPLSKELLL KAIERTAERV
     DAIYVDWKGS KGETRQMARA VAEELGLEFI RD