ID   PTH_METKA               Reviewed;         116 AA.
AC   Q8TV04;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   25-MAY-2022, entry version 93.
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=MK1597;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02810.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TV04; -.
DR   SMR; Q8TV04; -.
DR   STRING; 190192.MK1597; -.
DR   EnsemblBacteria; AAM02810; AAM02810; MK1597.
DR   KEGG; mka:MK1597; -.
DR   PATRIC; fig|190192.8.peg.1758; -.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   OMA; GHAAVEC; -.
DR   Proteomes; UP000001826; 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..116
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000120293"
SQ   SEQUENCE   116 AA;  12871 MW;  D9556F87E16102CF CRC64;
     MYKQVIVVRG DLKLSRGKLA AQVAHASLGA FLRAKESGAP VEEWLREGQK KVVLKCKDKE
     ELLELHELAK RRGLPSFLVR DAGLTELEPG TVTCLGIGPE REEEIDRVTG DLPLLR