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Database: UniProt
Entry: A0A2P7YNJ1_9ASCO
LinkDB: A0A2P7YNJ1_9ASCO
Original site: A0A2P7YNJ1_9ASCO 
ID   A0A2P7YNJ1_9ASCO        Unreviewed;       151 AA.
AC   A0A2P7YNJ1;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=D-aminoacyl-tRNA deacylase {ECO:0000256|ARBA:ARBA00020007, ECO:0000256|RuleBase:RU003470};
DE            EC=3.1.1.96 {ECO:0000256|ARBA:ARBA00013056, ECO:0000256|RuleBase:RU003470};
GN   ORFNames=C7M61_003238 {ECO:0000313|EMBL:PSK37534.1};
OS   [Candida] pseudohaemulonii.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Metschnikowiaceae; Metschnikowiaceae incertae sedis;
OC   Candida/Metschnikowiaceae.
OX   NCBI_TaxID=418784 {ECO:0000313|EMBL:PSK37534.1, ECO:0000313|Proteomes:UP000241107};
RN   [1] {ECO:0000313|EMBL:PSK37534.1, ECO:0000313|Proteomes:UP000241107}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B12108 {ECO:0000313|EMBL:PSK37534.1,
RC   ECO:0000313|Proteomes:UP000241107};
RA   Munoz J.F., Gade L.G., Chow N.A., Litvintseva A.P., Loparev V.N.,
RA   Cuomo C.A.;
RT   "Candida pseudohaemulonii genome assembly and annotation.";
RL   Submitted (MAR-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PSK37534.1}.
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DR   EMBL; PYFQ01000008; PSK37534.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7YNJ1; -.
DR   STRING; 418784.A0A2P7YNJ1; -.
DR   EnsemblFungi; C7M61_003238_t1; PSK37534.1; C7M61_003238.
DR   VEuPathDB; FungiDB:C7M61_003238; -.
DR   OrthoDB; 2872788at2759; -.
DR   Proteomes; UP000241107; 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   Gene3D; 3.50.80.10; D-tyrosyl-tRNA(Tyr) deacylase; 1.
DR   HAMAP; MF_00518; Deacylase_Dtd; 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:UP000241107};
KW   RNA-binding {ECO:0000256|RuleBase:RU003470};
KW   tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ   SEQUENCE   151 AA;  17013 MW;  607B071FC92A3D37 CRC64;
     MRAVIQRVKR ASVTVDGEVV SSIGKGLVVF VAVKKGDVWD EFKKFSLKIE NLRIFDDENG
     KMWARSLRQL TDHELLLVSQ FTLYGDMRKG TRPDLHLSAK ADEARATYDR FVETCRDLLG
     KERVKDGVFG AMMDVELVND GPVTLTFDGA D
//
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