ID A0A3Q1EW96_9TELE Unreviewed; 207 AA.
AC A0A3Q1EW96;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|ARBA:ARBA00013056, ECO:0000256|RuleBase:RU003470};
DE EC=3.1.1.96 {ECO:0000256|ARBA:ARBA00013056, ECO:0000256|RuleBase:RU003470};
OS Acanthochromis polyacanthus (spiny chromis).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC Ovalentaria; Pomacentridae; Acanthochromis.
OX NCBI_TaxID=80966 {ECO:0000313|Ensembl:ENSAPOP00000008553.1, ECO:0000313|Proteomes:UP000257200};
RN [1] {ECO:0000313|Ensembl:ENSAPOP00000008553.1}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00033671};
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:0000256|ARBA:ARBA00000741};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|RuleBase:RU003470}.
CC -!- SIMILARITY: Belongs to the DTD family. {ECO:0000256|ARBA:ARBA00009673,
CC ECO:0000256|RuleBase:RU003470}.
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DR AlphaFoldDB; A0A3Q1EW96; -.
DR STRING; 80966.ENSAPOP00000008553; -.
DR Ensembl; ENSAPOT00000003051.1; ENSAPOP00000008553.1; ENSAPOG00000010720.1.
DR GeneTree; ENSGT00940000153431; -.
DR InParanoid; A0A3Q1EW96; -.
DR OrthoDB; 2872788at2759; -.
DR Proteomes; UP000257200; Unplaced.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0051499; F:D-aminoacyl-tRNA deacylase activity; IEA:UniProtKB-EC.
DR GO; GO:0106026; F:Gly-tRNA(Ala) hydrolase activity; IEA:Ensembl.
DR GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR CDD; cd00563; Dtyr_deacylase; 1.
DR Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR InterPro; IPR003732; Daa-tRNA_deacyls_DTD.
DR InterPro; IPR023509; DTD-like_sf.
DR NCBIfam; TIGR00256; D-aminoacyl-tRNA deacylase; 1.
DR PANTHER; PTHR10472:SF5; D-AMINOACYL-TRNA DEACYLASE 1; 1.
DR PANTHER; PTHR10472; D-TYROSYL-TRNA TYR DEACYLASE; 1.
DR Pfam; PF02580; Tyr_Deacylase; 1.
DR SUPFAM; SSF69500; DTD-like; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|RuleBase:RU003470};
KW Hydrolase {ECO:0000256|RuleBase:RU003470};
KW Reference proteome {ECO:0000313|Proteomes:UP000257200};
KW RNA-binding {ECO:0000256|RuleBase:RU003470};
KW tRNA-binding {ECO:0000256|RuleBase:RU003470}.
FT REGION 141..207
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..158
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 207 AA; 23042 MW; C47A879DA5FA3429 CRC64;
MKAIVQRVTK ASVTVGEEQI SSIGRGLCVL LGISVEDTQK DADYIVRKIL NLRLFEDENG
RAWTKSVMDR DFEVLCVSQF TLHCVLKGNK PDFHLAMPAE LSQPFYNSIL ENMRSTYKPE
LIKDGKFGAK MQVNIQNDGP VTIELTSPTG PTDPKQLSKQ EKQQQRKEKT RSKGPSDSSR
DKGALRSRQD PNASSGAEGD VSSEREP
//
