ID A0A0B1S2C9_OESDE Unreviewed; 143 AA.
AC A0A0B1S2C9;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 31.
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};
DE Flags: Fragment;
GN ORFNames=OESDEN_20838 {ECO:0000313|EMBL:KHJ79513.1};
OS Oesophagostomum dentatum (Nodular worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Strongyloidea; Strongylidae; Oesophagostomum.
OX NCBI_TaxID=61180 {ECO:0000313|EMBL:KHJ79513.1, ECO:0000313|Proteomes:UP000053660};
RN [1] {ECO:0000313|EMBL:KHJ79513.1, ECO:0000313|Proteomes:UP000053660}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OD-Hann {ECO:0000313|EMBL:KHJ79513.1,
RC ECO:0000313|Proteomes:UP000053660};
RA Mitreva M.;
RT "Draft genome of the hookworm Oesophagostomum dentatum.";
RL Submitted (MAR-2014) 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; KN604665; KHJ79513.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0B1S2C9; -.
DR Proteomes; UP000053660; 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:UP000053660};
KW RNA-binding {ECO:0000256|RuleBase:RU003470};
KW tRNA-binding {ECO:0000256|RuleBase:RU003470}.
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KHJ79513.1"
SQ SEQUENCE 143 AA; 16388 MW; 67D28514D8E1F916 CRC64;
CTDLEANVNS FQISSIGRGV CVFVGISRED KDEDIEYIVR KILNVRLFAS DNKRWDKSVK
DEGLEVLCVS QFTLYGFLKG NKLDFHNSMN PEDACAFYNR FMEKLRSSYP QEKIKDGRFA
AMMNVEIVND GPVTINLDSK NRD
//
