PTH_PHYMT
ID PTH_PHYMT Reviewed; 176 AA.
AC B3QZM3;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 64.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=ATP_00223;
OS Phytoplasma mali (strain AT).
OC Bacteria; Tenericutes; Mollicutes; Acholeplasmatales; Acholeplasmataceae;
OC Candidatus Phytoplasma; 16SrX (Apple proliferation group).
OX NCBI_TaxID=482235;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AT;
RX PubMed=18582369; DOI=10.1186/1471-2164-9-306;
RA Kube M., Schneider B., Kuhl H., Dandekar T., Heitmann K., Migdoll A.M.,
RA Reinhardt R., Seemueller E.;
RT "The linear chromosome of the plant-pathogenic mycoplasma 'Candidatus
RT Phytoplasma mali'.";
RL BMC Genomics 9:306-306(2008).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00083}.
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:0000255|HAMAP-Rule:MF_00083};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
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DR EMBL; CU469464; CAP18410.1; -; Genomic_DNA.
DR AlphaFoldDB; B3QZM3; -.
DR SMR; B3QZM3; -.
DR STRING; 37692.ATP_00223; -.
DR EnsemblBacteria; CAP18410; CAP18410; ATP_00223.
DR KEGG; pml:ATP_00223; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_1_14; -.
DR OMA; HVLSKFH; -.
DR Proteomes; UP000002020; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR CDD; cd00462; PTH; 1.
DR Gene3D; 3.40.50.1470; -; 1.
DR HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR InterPro; IPR001328; Pept_tRNA_hydro.
DR InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..176
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000118403"
SQ SEQUENCE 176 AA; 20081 MW; 8BC1B85A0ECDF5E2 CRC64;
MKLIVGLGNP GQNYQFTLHN IGFMMIDYLL NTIITDKKIV KKHNSYIYKA NVGSNLVLFV
KPQTYMNSSG HAVKKILNEY KIILNDLLVL SDDIYLPEGN YKLKLKGGHG GHNGLRNIID
CLQTKKFKRL KIGVSQDHNI SLEDYLLTPI DDKKKLMVQK SFPIISNIIK NFIQDC
