ID   DTDA_HALWD              Reviewed;         521 AA.
AC   Q18KS1;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   22-JUL-2008, sequence version 2.
DT   25-MAY-2022, entry version 78.
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=HQ_1244A;
OS   Haloquadratum walsbyi (strain DSM 16790 / HBSQ001).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC   Haloferacaceae; Haloquadratum.
OX   NCBI_TaxID=362976;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16790 / HBSQ001;
RX   PubMed=16820047; DOI=10.1186/1471-2164-7-169;
RA   Bolhuis H., Palm P., Wende A., Falb M., Rampp M., Rodriguez-Valera F.,
RA   Pfeiffer F., Oesterhelt D.;
RT   "The genome of the square archaeon Haloquadratum walsbyi: life at the
RT   limits of water activity.";
RL   BMC Genomics 7:169-169(2006).
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; AM180088; CAJ51373.2; -; Genomic_DNA.
DR   RefSeq; WP_048066919.1; NC_008212.1.
DR   AlphaFoldDB; Q18KS1; -.
DR   SMR; Q18KS1; -.
DR   STRING; 362976.HQ_1244A; -.
DR   EnsemblBacteria; CAJ51373; CAJ51373; HQ_1244A.
DR   GeneID; 4192205; -.
DR   KEGG; hwa:HQ_1244A; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_610619_0_0_2; -.
DR   Proteomes; UP000001975; Chromosome.
DR   GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-UniRule.
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.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..521
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345210"
FT   REGION          323..353
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          499..521
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   521 AA;  56102 MW;  49B270D637E2C8FB CRC64;
     MIGLVVSSAD TASVTISDQL HELVEWESHR DAAGDEYEQY DDFEMRTIDE WHLEAENASE
     LFSTTPQIIA FLSRHSGDTG PLLTTHFTGN FGPAEYGGEP GSFAQACPMI QQTLLEAFDR
     YAPSKYDVGI ECTHHGPTTV GAPSLFVELG SSKAEWNDPD GAHAVAQAIL ELSGEDAPAN
     VETDRTVVGF GGGHYAPRFE RIIRETDWVV GHIGADWALD SMGAPAANRD IINHAVTASD
     ADVALVADDR PELTKVISQA DIRVVQERWL RETTGVSRPM VSALENALVP IASGLRLGTP
     ATEYDPATSD EFVITDRHTD NDAVGTVHTK DSTDIDTGTN HNVDAERTES EDSHNIRDAI
     DRADADAVVL AFPTSLMETI SGIDIETTNQ VFSEHTLAFE TTEGGTRPTG RMIVSDYLSV
     ESITHALIDI LKLKYDRVER TDETLRVRRQ VFDPAKAATL DVPEGPAFGR LAAGESVTVA
     GRTIDPEAVH TTETVTFPVF STSSSSSSSS SSSSSSSSSS S