ID   DTDA_SACS2              Reviewed;         238 AA.
AC   Q97WI2;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2001, sequence version 1.
DT   25-MAY-2022, entry version 99.
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, ECO:0000269|PubMed:16844682};
DE   AltName: Full=D-tyrosyl-tRNA(Tyr) deacylase;
GN   Name=dtdA {ECO:0000255|HAMAP-Rule:MF_00562}; OrderedLocusNames=SSO2234;
OS   Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS   (Sulfolobus solfataricus).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=273057;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX   PubMed=11427726; DOI=10.1073/pnas.141222098;
RA   She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA   Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA   Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA   Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA   Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA   Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT   "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-5, FUNCTION, AND CATALYTIC ACTIVITY.
RX   PubMed=16844682; DOI=10.1074/jbc.m605860200;
RA   Ferri-Fioni M.-L., Fromant M., Bouin A.-P., Aubard C., Lazennec C.,
RA   Plateau P., Blanquet S.;
RT   "Identification in archaea of a novel D-Tyr-tRNATyr deacylase.";
RL   J. Biol. Chem. 281:27575-27585(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. Catalyzes the hydrolysis of D-
CC       tyrosyl-tRNA(Tyr). {ECO:0000269|PubMed:16844682}.
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         ECO:0000269|PubMed:16844682};
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-tyrosyl-tRNA(Tyr) + H2O = D-tyrosine + tRNA(Tyr);
CC         Xref=Rhea:RHEA:25347, Rhea:RHEA-COMP:9707, Rhea:RHEA-COMP:9872,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:58570, ChEBI:CHEBI:78442,
CC         ChEBI:CHEBI:78723; Evidence={ECO:0000269|PubMed:16844682};
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AE006641; AAK42404.1; -; Genomic_DNA.
DR   PIR; E90393; E90393.
DR   RefSeq; WP_009992037.1; NC_002754.1.
DR   AlphaFoldDB; Q97WI2; -.
DR   SMR; Q97WI2; -.
DR   STRING; 273057.SSO2234; -.
DR   EnsemblBacteria; AAK42404; AAK42404; SSO2234.
DR   GeneID; 44127970; -.
DR   KEGG; sso:SSO2234; -.
DR   PATRIC; fig|273057.12.peg.2331; -.
DR   eggNOG; arCOG01616; Archaea.
DR   HOGENOM; CLU_056464_1_0_2; -.
DR   InParanoid; Q97WI2; -.
DR   OMA; CYEATHH; -.
DR   PhylomeDB; Q97WI2; -.
DR   BRENDA; 3.1.1.96; 6163.
DR   Proteomes; UP000001974; 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   1: Evidence at protein level;
KW   Direct protein sequencing; Hydrolase; Metal-binding; Reference proteome;
KW   Zinc.
FT   CHAIN           1..238
FT                   /note="D-aminoacyl-tRNA deacylase"
FT                   /id="PRO_0000158974"
SQ   SEQUENCE   238 AA;  26959 MW;  4C269C09E22D369A CRC64;
     MDIKLVYSTL DPVGVTIKKL GYRFEEINED VTDFHYENGE AIVIFSRHES KAGIPSLTVH
     YPGNPSEEIM GGEPKKLGIA YPRLLTSILR EIKKIDLNIE KTMEATHHGP TYQNVPVIFV
     EVGSNETYWT NDTIVKALVD STIRSIDKVD EIDCEYYISG FGGPHYSRLF TKLADESCIG
     HVISKHYIDK LDDKVIIQTI TNSVNTINKV VIDSLNSKQK ERIIASLKKL NNINIEFR