ID   DTDA_CALMQ              Reviewed;         269 AA.
AC   A8MCV2;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   04-DEC-2007, sequence version 1.
DT   25-MAY-2022, entry version 60.
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=Cmaq_0773;
OS   Caldivirga maquilingensis (strain ATCC 700844 / DSM 13496 / JCM 10307 /
OS   IC-167).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Caldivirga.
OX   NCBI_TaxID=397948;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700844 / DSM 13496 / JCM 10307 / IC-167;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Saunders E., Brettin T., Bruce D., Detter J.C.,
RA   Han C., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ivanova N., Biddle J.F., Zhang Z., Fitz-Gibbon S.T., Lowe T.M.,
RA   Saltikov C., House C.H., Richardson P.;
RT   "Complete sequence of Caldivirga maquilingensis IC-167.";
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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; CP000852; ABW01608.1; -; Genomic_DNA.
DR   RefSeq; WP_012185827.1; NC_009954.1.
DR   AlphaFoldDB; A8MCV2; -.
DR   SMR; A8MCV2; -.
DR   STRING; 397948.Cmaq_0773; -.
DR   EnsemblBacteria; ABW01608; ABW01608; Cmaq_0773.
DR   GeneID; 5708529; -.
DR   KEGG; cma:Cmaq_0773; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_056464_1_0_2; -.
DR   OMA; CYEATHH; -.
DR   OrthoDB; 84039at2157; -.
DR   Proteomes; UP000001137; 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.
DR   PIRSF; PIRSF016210; UCP016210; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Metal-binding; Reference proteome; Zinc.
FT   CHAIN           1..269
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345206"
SQ   SEQUENCE   269 AA;  30373 MW;  6FB5F597DCDD6B3D CRC64;
     MKIGLIVSRV DEASIGIWSM LKGMVKFKEI NTNEYSSDLA LALVSDKDIV YVDEADEWAR
     VNDIDLLLFL SRHEMKNPKP LITFHTPGNW TNDVELGGKP GQVAISEPRV LTNLFREAYR
     RIGELNGYSV TLEATHHGPF VDKPVVFVEI GSTSNEWRDP KAQEFLASLV FDLLNNTDKY
     INDGKDAAVS IGDLHYTTLV NHIINGEYDV GHMVPKYIKP TPTIIKMAVE RNTVRPRIGI
     IHWKSLDAES RVMSEKELSN LGLTVIKRR