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Database: UniProt
Entry: A0A0N4UYP5_ENTVE
LinkDB: A0A0N4UYP5_ENTVE
Original site: A0A0N4UYP5_ENTVE 
ID   A0A0N4UYP5_ENTVE        Unreviewed;       202 AA.
AC   A0A0N4UYP5;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE            EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
OS   Enterobius vermicularis (Human pinworm).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Spirurina; Oxyuridomorpha; Oxyuroidea; Oxyuridae; Enterobius.
OX   NCBI_TaxID=51028 {ECO:0000313|Proteomes:UP000038041, ECO:0000313|WBParaSite:EVEC_0000271201-mRNA-1};
RN   [1] {ECO:0000313|WBParaSite:EVEC_0000271201-mRNA-1}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (FEB-2017) to UniProtKB.
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000256|ARBA:ARBA00003043}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC         amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={ECO:0000256|ARBA:ARBA00033690};
CC   -!- SIMILARITY: Belongs to the PTH2 family.
CC       {ECO:0000256|ARBA:ARBA00038050}.
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DR   AlphaFoldDB; A0A0N4UYP5; -.
DR   WBParaSite; EVEC_0000271201-mRNA-1; EVEC_0000271201-mRNA-1; EVEC_0000271201.
DR   Proteomes; UP000038041; Unplaced.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
DR   CDD; cd02430; PTH2; 1.
DR   Gene3D; 3.40.1490.10; Bit1; 1.
DR   InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR   InterPro; IPR002833; PTH2.
DR   NCBIfam; TIGR00283; arch_pth2; 1.
DR   PANTHER; PTHR12649; PEPTIDYL-TRNA HYDROLASE 2; 1.
DR   PANTHER; PTHR12649:SF11; PEPTIDYL-TRNA HYDROLASE 2, MITOCHONDRIAL; 1.
DR   Pfam; PF01981; PTH2; 1.
DR   SUPFAM; SSF102462; Peptidyl-tRNA hydrolase II; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801}.
SQ   SEQUENCE   202 AA;  22523 MW;  ACE8F141A88734CB CRC64;
     LKIKYFLACF EVEFLCYFLW FRGTRTPKKF GIRRNSVKKF VVQFLKSGAY VGLIRNGPHK
     LPCLSKFRLQ FLSVLGFLST LASAEPHKMV FVVNMSLKMR AGKIAAQVGH ATLGVYRLAQ
     RSDKGQQALT AWRSVGEMKV VVKGDSTDHL LELFKESRDK GLFVYVVSDA GRTQIPAGSR
     TVLGIFGPSE TVDSVSGKLK LL
//
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