ID A0A0L7R959_9HYME Unreviewed; 159 AA.
AC A0A0L7R959;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 13-SEP-2023, entry version 30.
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};
GN ORFNames=WH47_09281 {ECO:0000313|EMBL:KOC67364.1};
OS Habropoda laboriosa.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Apoidea;
OC Anthophila; Apidae; Habropoda.
OX NCBI_TaxID=597456 {ECO:0000313|EMBL:KOC67364.1, ECO:0000313|Proteomes:UP000053825};
RN [1] {ECO:0000313|EMBL:KOC67364.1, ECO:0000313|Proteomes:UP000053825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0110345459 {ECO:0000313|EMBL:KOC67364.1};
RA Pan H., Kapheim K.;
RT "The genome of Habropoda laboriosa.";
RL Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
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 EMBL; KQ414628; KOC67364.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0L7R959; -.
DR STRING; 597456.A0A0L7R959; -.
DR Proteomes; UP000053825; Unassembled WGS sequence.
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: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:UP000053825};
KW RNA-binding {ECO:0000256|RuleBase:RU003470};
KW tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ SEQUENCE 159 AA; 18035 MW; 97BC915A02C77B45 CRC64;
MKAVIQRVAK ASVSVDGELI SSIENGLCVL IGIKRDDSKE DINYIVKKIL NTKIFENNNK
KWGASVMDKQ YEILCISQFT LYYNLKGNKL DFHRAMPAQE SEPFYNNFLA ELRKKYKPEL
IKDGKFGALM EVNIQNSGPV TLEIESPVKS NILNESNEA
//
