ID A0A1R1XL23_9FUNG Unreviewed; 121 AA.
AC A0A1R1XL23;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=AYI70_g7335 {ECO:0000313|EMBL:OMJ15341.1};
OS Smittium culicis.
OC Eukaryota; Fungi; Fungi incertae sedis; Zoopagomycota; Kickxellomycotina;
OC Harpellomycetes; Harpellales; Legeriomycetaceae; Smittium.
OX NCBI_TaxID=133412 {ECO:0000313|EMBL:OMJ15341.1, ECO:0000313|Proteomes:UP000187283};
RN [1] {ECO:0000313|EMBL:OMJ15341.1, ECO:0000313|Proteomes:UP000187283}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GSMNP {ECO:0000313|EMBL:OMJ15341.1,
RC ECO:0000313|Proteomes:UP000187283};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) 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:OMJ15341.1}.
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DR EMBL; LSSN01002711; OMJ15341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R1XL23; -.
DR STRING; 133412.A0A1R1XL23; -.
DR Proteomes; UP000187283; 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 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:UP000187283};
KW RNA-binding {ECO:0000256|RuleBase:RU003470};
KW tRNA-binding {ECO:0000256|RuleBase:RU003470}.
SQ SEQUENCE 121 AA; 13412 MW; 0C6482147FB1C29D CRC64;
MLALIGISVR DTENDIDFMS EQLLNAPIFD GPEKKASVLE SNLEILCVSQ FTLLGKTVKG
NKPDFHDAMK GSQSRPMFDR LISQLRARLG EKSVQTGEFG AMMEVSLEND GPMTFQIDSE
N
//
