ID   PTH_METBF               Reviewed;         115 AA.
AC   Q466V4;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 94.
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=Mbar_A3204;
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
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; CP000099; AAZ72088.1; -; Genomic_DNA.
DR   RefSeq; WP_011308128.1; NC_007355.1.
DR   AlphaFoldDB; Q466V4; -.
DR   SMR; Q466V4; -.
DR   STRING; 269797.Mbar_A3204; -.
DR   PRIDE; Q466V4; -.
DR   EnsemblBacteria; AAZ72088; AAZ72088; Mbar_A3204.
DR   GeneID; 3627107; -.
DR   KEGG; mba:Mbar_A3204; -.
DR   eggNOG; arCOG04228; Archaea.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   OMA; GHAAVEC; -.
DR   OrthoDB; 115947at2157; -.
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.
FT   CHAIN           1..115
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000051676"
SQ   SEQUENCE   115 AA;  12698 MW;  0C28FF9484BD7245 CRC64;
     MSEYKQCIVT REDLKLSKGK FAVQVAHAAI SASEWASKND LEKWKEGGQK KIVLKVPTLN
     DLYELKEKAR REGLPTALIQ DAGLTEIPPG TVTVLGIGPA KEELIDKVTR NLKLV