PTH_METS5
ID PTH_METS5 Reviewed; 117 AA.
AC A4YD82;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 29-MAY-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00628};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00628};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00628};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00628}; OrderedLocusNames=Msed_0207;
OS Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS / TH2).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Metallosphaera.
OX NCBI_TaxID=399549;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX PubMed=18083856; DOI=10.1128/aem.02019-07;
RA Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT archaeon Metallosphaera sedula provides insights into bioleaching-
RT associated metabolism.";
RL Appl. Environ. Microbiol. 74:682-692(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_00628}.
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_00628};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00628}.
CC -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP-
CC Rule:MF_00628}.
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DR EMBL; CP000682; ABP94384.1; -; Genomic_DNA.
DR RefSeq; WP_011921352.1; NC_009440.1.
DR AlphaFoldDB; A4YD82; -.
DR SMR; A4YD82; -.
DR STRING; 399549.Msed_0207; -.
DR EnsemblBacteria; ABP94384; ABP94384; Msed_0207.
DR GeneID; 5104073; -.
DR GeneID; 59456349; -.
DR KEGG; mse:Msed_0207; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR OMA; GHAAVEC; -.
DR Proteomes; UP000000242; 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; cd02430; PTH2; 1.
DR Gene3D; 3.40.1490.10; -; 1.
DR HAMAP; MF_00628; Pept_tRNA_hydro_arch; 1.
DR InterPro; IPR023476; Pep_tRNA_hydro_II_dom_sf.
DR InterPro; IPR034759; Pept_tRNA_hydro_arch.
DR InterPro; IPR002833; PTH2.
DR PANTHER; PTHR12649; PTHR12649; 1.
DR Pfam; PF01981; PTH2; 1.
DR SUPFAM; SSF102462; SSF102462; 1.
DR TIGRFAMs; TIGR00283; arch_pth2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..117
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000072659"
SQ SEQUENCE 117 AA; 12584 MW; 7936EA406B1EBC80 CRC64;
MKMVVMVRTD INMGKGKIAA QVAHAAVSLV LDCMSRSSWR DWLDSWLHEG QPKVVVKVSS
LEDLLSRVDK ARSQGLPTTV ISDAGRTQVE PGTVTCAGIG PGPDDLIDKI TGDLKLL