PTH_THEAC
ID PTH_THEAC Reviewed; 117 AA.
AC Q9HLW6;
DT 29-AUG-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 25-MAY-2022, entry version 107.
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=Ta0108;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
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; AL445063; CAC11256.1; -; Genomic_DNA.
DR RefSeq; WP_010900535.1; NC_002578.1.
DR PDB; 1RLK; X-ray; 1.95 A; A=1-117.
DR PDBsum; 1RLK; -.
DR AlphaFoldDB; Q9HLW6; -.
DR SMR; Q9HLW6; -.
DR STRING; 273075.Ta0108; -.
DR EnsemblBacteria; CAC11256; CAC11256; CAC11256.
DR GeneID; 1455762; -.
DR KEGG; tac:Ta0108; -.
DR eggNOG; arCOG04228; Archaea.
DR HOGENOM; CLU_073661_2_2_2; -.
DR OMA; GHAAVEC; -.
DR OrthoDB; 115947at2157; -.
DR EvolutionaryTrace; Q9HLW6; -.
DR Proteomes; UP000001024; 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 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT CHAIN 1..117
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000120306"
FT STRAND 3..11
FT /evidence="ECO:0007829|PDB:1RLK"
FT HELIX 17..38
FT /evidence="ECO:0007829|PDB:1RLK"
FT HELIX 40..48
FT /evidence="ECO:0007829|PDB:1RLK"
FT STRAND 53..60
FT /evidence="ECO:0007829|PDB:1RLK"
FT HELIX 61..74
FT /evidence="ECO:0007829|PDB:1RLK"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:1RLK"
FT STRAND 86..90
FT /evidence="ECO:0007829|PDB:1RLK"
FT STRAND 94..103
FT /evidence="ECO:0007829|PDB:1RLK"
FT HELIX 104..111
FT /evidence="ECO:0007829|PDB:1RLK"
SQ SEQUENCE 117 AA; 13170 MW; DDC40D79EEB05B7E CRC64;
MVKKMVIAVR KDLDMGKGKI AAQVAHAAVT CAIRSMKINR DVFNEWYDEG QRKIVVKVND
LDEIMEIKRM ADSMGIVNEI VQDRGYTQVE PGTITCIGLG PDEEEKLDKI TGKYKLL
