DTD2_DANRE
ID DTD2_DANRE Reviewed; 160 AA.
AC Q68EL2;
DT 31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=D-aminoacyl-tRNA deacylase 2 {ECO:0000305};
DE EC=3.1.1.96 {ECO:0000269|PubMed:29410408};
DE AltName: Full=Animalia-specific tRNA deacylase {ECO:0000303|PubMed:29410408};
DE Short=ATD {ECO:0000303|PubMed:29410408};
DE AltName: Full=D-tyrosyl-tRNA deacylase 2 {ECO:0000305};
DE AltName: Full=L-alanyl-tRNA deacylase {ECO:0000305|PubMed:29410408};
GN Name=dtd2; ORFNames=zgc:100795;
OS Danio rerio (Zebrafish) (Brachydanio rerio).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Ostariophysi; Cypriniformes;
OC Danionidae; Danioninae; Danio.
OX NCBI_TaxID=7955;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Embryo;
RG NIH - Zebrafish Gene Collection (ZGC) project;
RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=29410408; DOI=10.1038/s41467-017-02204-w;
RA Kuncha S.K., Mazeed M., Singh R., Kattula B., Routh S.B.,
RA Sankaranarayanan R.;
RT "A chiral selectivity relaxed paralog of DTD for proofreading tRNA
RT mischarging in Animalia.";
RL Nat. Commun. 9:511-511(2018).
CC -!- FUNCTION: Deacylates mischarged D-aminoacyl-tRNAs (By similarity). Also
CC deacylates mischarged glycyl-tRNA(Ala), protecting cells against
CC glycine mischarging by AlaRS (By similarity). Probably acts by
CC rejecting L-amino acids from its binding site rather than specific
CC recognition of D-amino acids (By similarity). Catalyzes the hydrolysis
CC of D-tyrosyl-tRNA(Tyr), has no activity on correctly charged L-tyrosyl-
CC tRNA(Tyr) (By similarity). By recycling D-aminoacyl-tRNA to D-amino
CC acids and free tRNA molecules, this enzyme counteracts the toxicity
CC associated with the formation of D-aminoacyl-tRNA entities in vivo and
CC helps enforce protein L-homochirality. In contrast to DTD1, deacylates
CC L-Ala mischarged on tRNA(Thr)(G4.U69) by alanine-tRNA ligase AARS
CC (PubMed:29410408). Can deacylate L-Ala due to a relaxed specificity for
CC substrate chirality caused by the trans conformation of the Gly-Pro
CC motif in the active site (PubMed:29410408). Also hydrolyzes correctly
CC charged, achiral, glycyl-tRNA(Gly) in vitro, although in vivo
CC eef1a1a/EF-Tu may protect cognate achiral glycyl-tRNA(Gly) from DTD2-
CC mediated deacetylation (By similarity). {ECO:0000250|UniProtKB:Q8BHA3,
CC ECO:0000269|PubMed:29410408}.
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:0000269|PubMed:29410408};
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:0000269|PubMed:29410408};
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:0000250|UniProtKB:Q8BHA3};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + L-alanyl-tRNA(Thr) = H(+) + L-alanine + tRNA(Thr);
CC Xref=Rhea:RHEA:17793, Rhea:RHEA-COMP:9670, Rhea:RHEA-COMP:14576,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:78442, ChEBI:CHEBI:78497;
CC Evidence={ECO:0000269|PubMed:29410408};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q8BHA3}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- DOMAIN: A Gly-transPro motif from one monomer fits into the active site
CC of the other monomer to allow specific chiral rejection of most L-amino
CC acids except L-Ala. The trans conformation of the motif is maintained
CC by Arg-143. {ECO:0000250|UniProtKB:Q8BHA3}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000305}.
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DR EMBL; BC080214; AAH80214.1; -; mRNA.
DR RefSeq; NP_001004011.1; NM_001004011.2.
DR AlphaFoldDB; Q68EL2; -.
DR SMR; Q68EL2; -.
DR STRING; 7955.ENSDARP00000120242; -.
DR PaxDb; Q68EL2; -.
DR GeneID; 445510; -.
DR KEGG; dre:445510; -.
DR CTD; 112487; -.
DR ZFIN; ZDB-GENE-040822-45; dtd2.
DR eggNOG; KOG3323; Eukaryota.
DR InParanoid; Q68EL2; -.
DR OrthoDB; 1170114at2759; -.
DR PhylomeDB; Q68EL2; -.
DR PRO; PR:Q68EL2; -.
DR Proteomes; UP000000437; Genome assembly.
DR Proteomes; UP000814640; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0106105; F:Ala-tRNA(Thr) hydrolase activity; IDA:UniProtKB.
DR GO; GO:0051500; F:D-tyrosyl-tRNA(Tyr) deacylase activity; IBA:GO_Central.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR GO; GO:0106074; P:aminoacyl-tRNA metabolism involved in translational fidelity; IDA:UniProtKB.
DR GO; GO:0006399; P:tRNA metabolic process; IBA:GO_Central.
DR Gene3D; 3.50.80.10; -; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR PANTHER; PTHR10472; PTHR10472; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; SSF69500; 1.
PE 1: Evidence at protein level;
KW Cytoplasm; Hydrolase; Reference proteome; RNA-binding; tRNA-binding.
FT CHAIN 1..160
FT /note="D-aminoacyl-tRNA deacylase 2"
FT /id="PRO_0000254051"
FT MOTIF 152..153
FT /note="Gly-transPro motif, allows the protein to recognize
FT chirality of D-amino acids"
FT /evidence="ECO:0000250|UniProtKB:Q8BHA3"
SQ SEQUENCE 160 AA; 17847 MW; EC85396F80C603CD CRC64;
MKARVVLQQC LHARLQVKPP DEESEAEWVE VNRGMVIYIC FFKGATEDLI PKMVNTLLNV
KLCETESGKF TSVLQLPGSV LIVPQATLGG KPKGRGMQYH GNIGKDEGLK LYETFVSLCQ
SELSSCKNSD ILTEVKHGTY GNRQVLKLDT NGPYTHLMEF
