ID J5JU80_BEAB2 Unreviewed; 219 AA.
AC J5JU80;
DT 31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 31-OCT-2012, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
GN ORFNames=BBA_05072 {ECO:0000313|EMBL:EJP66101.1};
OS Beauveria bassiana (strain ARSEF 2860) (White muscardine disease fungus)
OS (Tritirachium shiotae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=655819 {ECO:0000313|EMBL:EJP66101.1, ECO:0000313|Proteomes:UP000002762};
RN [1] {ECO:0000313|EMBL:EJP66101.1, ECO:0000313|Proteomes:UP000002762}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ARSEF 2860 {ECO:0000313|EMBL:EJP66101.1,
RC ECO:0000313|Proteomes:UP000002762};
RX PubMed=22761991; DOI=10.1038/srep00483;
RA Xiao G., Ying S.H., Zheng P., Wang Z.L., Zhang S., Xie X.Q., Shang Y.,
RA St Leger R.J., Zhao G.P., Wang C., Feng M.G.;
RT "Genomic perspectives on the evolution of fungal entomopathogenicity in
RT Beauveria bassiana.";
RL Sci. Rep. 2:483-483(2012).
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 EMBL; JH725161; EJP66101.1; -; Genomic_DNA.
DR RefSeq; XP_008598391.1; XM_008600169.1.
DR AlphaFoldDB; J5JU80; -.
DR STRING; 655819.J5JU80; -.
DR EnsemblFungi; BB8028_0004g13040.1; BB8028_0004g13040.1; BB8028_0004g13040.
DR GeneID; 19888084; -.
DR HOGENOM; CLU_073661_0_0_1; -.
DR InParanoid; J5JU80; -.
DR OrthoDB; 169876at2759; -.
DR Proteomes; UP000002762; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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, ECO:0000313|EMBL:EJP66101.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002762};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 42..69
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 219 AA; 23648 MW; A8B3A8E2BAFCCF39 CRC64;
MALDNTTVAI TTALTTFVTG YIFGLYATRG YLFSPALQAE RRANRDDPVE SEESDVDEDD
SLLDHAPNWS NAEDADVKQG LRFGAAAAAP KLKLTNEECK LVLVVRTDLG MTKGKIAAQC
SHATLACYKA LAGNPDADST ERKMLARWEK YGQAKIAVQV KSQDEMLQMC RKARGMGLTA
EVVKDAGRTQ IEAGSMTVLG VGPAPRSLID EVTGHLKLL
//
