ID   DTDA_METHJ              Reviewed;         442 AA.
AC   Q2FPX3;
DT   22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   25-MAY-2022, entry version 73.
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=Mhun_0661;
OS   Methanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 /
OS   JF-1).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanomicrobiales; Methanospirillaceae; Methanospirillum.
OX   NCBI_TaxID=323259;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27890 / DSM 864 / NBRC 100397 / JF-1;
RX   PubMed=26744606; DOI=10.1186/s40793-015-0124-8;
RA   Gunsalus R.P., Cook L.E., Crable B., Rohlin L., McDonald E., Mouttaki H.,
RA   Sieber J.R., Poweleit N., Zhou H., Lapidus A.L., Daligault H.E., Land M.,
RA   Gilna P., Ivanova N., Kyrpides N., Culley D.E., McInerney M.J.;
RT   "Complete genome sequence of Methanospirillum hungatei type strain JF1.";
RL   Stand. Genomic Sci. 11:2-2(2016).
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; CP000254; ABD40417.1; -; Genomic_DNA.
DR   RefSeq; WP_011447701.1; NC_007796.1.
DR   AlphaFoldDB; Q2FPX3; -.
DR   SMR; Q2FPX3; -.
DR   STRING; 323259.Mhun_0661; -.
DR   EnsemblBacteria; ABD40417; ABD40417; Mhun_0661.
DR   GeneID; 3923578; -.
DR   KEGG; mhu:Mhun_0661; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_610619_0_0_2; -.
DR   OMA; MECTHHG; -.
DR   OrthoDB; 25601at2157; -.
DR   Proteomes; UP000001941; 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..442
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000345224"
SQ   SEQUENCE   442 AA;  48825 MW;  0A694E67744F24EF CRC64;
     MTPKEQSPTT LLISSRKDPA GSLIHEELYS FLEDDKRAHS HIRHWHAEER LIYLDGPSLP
     HDADRILFLS RHASERPRPV LTVHVTGNFG SADYGGRPNT LTPAATGLMH ALINRLIIHA
     PEGYEVMYEA THHGPTDIPL PSCFIELGST EKEWNDRIAA RAVAQAVLDA LLMDTSSVIP
     LAGFGGTHYA QRQTEITKLT RGGFGHIMPT RDIPHLTDAL FQDIISSTGA FAIYIDGKSM
     SGKEERMITG LADKHTIPIL GQGDLMRLFD LPFSEYMSIR NLAESLIPGS SIVLHTILEM
     PAPVSLTIPG ELVDEVMKVA AEEFISALDS FPIVHMTGRG KACHPVFITD AAFSGRISDE
     LIHLCVTLLQ DRYTCSFEGD SLIIKKLRFD PKKAKNLGIP SGPLYSELMA GKPVEVGDSV
     IYPEMVMTET EKRIHIPQRQ AR