ID A0A0V0R7K2_PSEPJ Unreviewed; 237 AA.
AC A0A0V0R7K2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260};
GN ORFNames=PPERSA_08768 {ECO:0000313|EMBL:KRX10466.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX10466.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX10466.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX10466.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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}.
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:KRX10466.1}.
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DR EMBL; LDAU01000027; KRX10466.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0R7K2; -.
DR EnsemblProtists; KRX10466; KRX10466; PPERSA_08768.
DR InParanoid; A0A0V0R7K2; -.
DR OMA; MIPANQK; -.
DR OrthoDB; 169876at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
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 Gene3D; 1.10.8.10; DNA helicase RuvA subunit, C-terminal domain; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR002833; PTH2.
DR InterPro; IPR009060; UBA-like_sf.
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.
DR SUPFAM; SSF46934; UBA-like; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937}.
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 237 AA; 26916 MW; 2013963F93CB06E9 CRC64;
MDSQAQPNKE VNKNSENQEN KEKLRQELKE FGFEESLIEK ALCFTSNQEE ALNLILTFQE
EPNFQVPQNQ KNQNEFLPQG MDQQTLAQLG NVNPNQLLNL GQNFQFGLKR PDREYKMVFL
VRMDLKMGVG KIAAQVGHSV LGAYKQIVSK IEKNNDKDLK EVLETYENYG QPKIVLKCET
KEEFLDLEQK ARNKGLNTYM VADAGRTQIE PGSLTVCAIG PGPVDAIDEV TKHLKLL
//
