ID   PTH_METMP               Reviewed;         116 AA.
AC   P61234;
DT   10-MAY-2004, integrated into UniProtKB/Swiss-Prot.
DT   10-MAY-2004, sequence version 1.
DT   27-MAR-2024, entry version 99.
DE   RecName: Full=Peptidyl-tRNA hydrolase;
DE            Short=PTH;
DE            EC=3.1.1.29;
GN   Name=pth; OrderedLocusNames=MMP0609;
OS   Methanococcus maripaludis (strain S2 / LL).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=267377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S2 / LL;
RX   PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA   Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA   Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA   Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA   Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA   Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA   Olson M.V., Leigh J.A.;
RT   "Complete genome sequence of the genetically tractable hydrogenotrophic
RT   methanogen Methanococcus maripaludis.";
RL   J. Bacteriol. 186:6956-6969(2004).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis. {ECO:0000250}.
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;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000305}.
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DR   EMBL; BX950229; CAF30165.1; -; Genomic_DNA.
DR   RefSeq; WP_011170553.1; NC_005791.1.
DR   AlphaFoldDB; P61234; -.
DR   SMR; P61234; -.
DR   STRING; 267377.MMP0609; -.
DR   EnsemblBacteria; CAF30165; CAF30165; MMP0609.
DR   GeneID; 2762305; -.
DR   KEGG; mmp:MMP0609; -.
DR   PATRIC; fig|267377.15.peg.623; -.
DR   eggNOG; arCOG04228; Archaea.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   OrthoDB; 6075at2157; -.
DR   Proteomes; UP000000590; 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; Bit1; 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   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.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..116
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000120295"
SQ   SEQUENCE   116 AA;  12705 MW;  4D6A38D39886DF25 CRC64;
     MYEQAIVIRN DLKMGKGKMA AQACHASIQA FLHAQKISSS AVSGWMNEGQ KKVVLKVNSE
     KELLEIFKNV NIEGLPCSLI RDAGRTQIEP GSLTAVGIGP EKEEKISKVK KDLKLL
//