ID   PTH_METJA               Reviewed;         115 AA.
AC   Q60363;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   25-MAY-2022, entry version 119.
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}; Synonyms=pth2;
GN   OrderedLocusNames=MJ0051;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
RN   [2]
RP   PARTIAL PROTEIN SEQUENCE, FUNCTION, AND CHARACTERIZATION.
RX   PubMed=12475929; DOI=10.1073/pnas.222659199;
RA   Rosas-Sandoval G., Ambrogelly A., Rinehart J., Wei D., Cruz-Vera L.R.,
RA   Graham D.E., Stetter K.O., Guarneros G., Soell D.;
RT   "Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase
RT   are nonessential in yeast.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:16707-16712(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, ECO:0000269|PubMed:12475929}.
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.
CC   -!- SIMILARITY: Belongs to the PTH2 family. {ECO:0000255|HAMAP-
CC       Rule:MF_00628}.
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DR   EMBL; L77117; AAB98032.1; -; Genomic_DNA.
DR   PIR; C64306; C64306.
DR   RefSeq; WP_010869543.1; NC_000909.1.
DR   PDB; 2ZV3; X-ray; 2.10 A; A/B/C/D/E/F/G/H/I=1-115.
DR   PDBsum; 2ZV3; -.
DR   AlphaFoldDB; Q60363; -.
DR   SMR; Q60363; -.
DR   STRING; 243232.MJ_0051; -.
DR   EnsemblBacteria; AAB98032; AAB98032; MJ_0051.
DR   GeneID; 1450890; -.
DR   KEGG; mja:MJ_0051; -.
DR   eggNOG; arCOG04228; Archaea.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   InParanoid; Q60363; -.
DR   OMA; GHAAVEC; -.
DR   OrthoDB; 115947at2157; -.
DR   PhylomeDB; Q60363; -.
DR   BRENDA; 3.1.1.29; 3260.
DR   EvolutionaryTrace; Q60363; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Direct protein sequencing; Hydrolase;
KW   Reference proteome.
FT   CHAIN           1..115
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000120292"
FT   STRAND          2..11
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   HELIX           15..36
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   HELIX           38..46
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   STRAND          51..58
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   HELIX           59..72
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   STRAND          76..81
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   STRAND          91..100
FT                   /evidence="ECO:0007829|PDB:2ZV3"
FT   HELIX           102..109
FT                   /evidence="ECO:0007829|PDB:2ZV3"
SQ   SEQUENCE   115 AA;  12670 MW;  FFBC33D185B4A8A2 CRC64;
     MKMVVVIRND LGMGKGKMVA QGGHAIIEAF LDAKRKNPRA VDEWLREGQK KVVVKVNSEK
     ELIDIYNKAR SEGLPCSIIR DAGHTQLEPG TLTAVAIGPE KDEKIDKITG HLKLL