ID   PTH_SACI4               Reviewed;         120 AA.
AC   C3MYS2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   16-JUN-2009, sequence version 1.
DT   10-JUN-2026, entry version 78.
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};
GN   OrderedLocusNames=M1425_1962;
OS   Saccharolobus islandicus (strain M.14.25 / Kamchatka #1) (Sulfolobus
OS   islandicus).
OC   Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Saccharolobus.
OX   NCBI_TaxID=427317;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M.14.25 / Kamchatka #1;
RX   PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA   Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT   "Biogeography of the Sulfolobus islandicus pan-genome.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
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 = an N-acyl-L-amino
CC         acid + a tRNA + 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; CP001400; ACP38706.1; -; Genomic_DNA.
DR   RefSeq; WP_012711933.1; NC_012588.1.
DR   AlphaFoldDB; C3MYS2; -.
DR   SMR; C3MYS2; -.
DR   GeneID; 15298345; -.
DR   KEGG; sia:M1425_1962; -.
DR   HOGENOM; CLU_073661_2_2_2; -.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004045; F:peptidyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd02430; PTH2; 1.
DR   FunFam; 3.40.1490.10:FF:000001; Peptidyl-tRNA hydrolase 2; 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   NCBIfam; NF003314; PRK04322.1; 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.
FT   CHAIN           1..120
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_1000212317"
SQ   SEQUENCE   120 AA;  13147 MW;  076EDE7E014F58A3 CRC64;
     MVKMVIVVRS DIKMGKGKMA AQVAHAAVTL VISIINSNNS RWKEWLNEWL QQGQPKIVVK
     ANSLDEIILR SKKAETMNLP FSIIEDAGKT QLEPGTITCL GIGPAPENLI DPITGDLKLL
//