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PROSITE documentation PDOC00920 [for PROSITE entry PS01196]

Peptidyl-tRNA hydrolase signatures


Peptidyl-tRNA hydrolase (EC (PTH) is a bacterial enzyme that cleaves peptidyl-tRNA or N-acyl-aminoacyl-tRNA to yield free peptides or N-acyl-amino acids and tRNA. The natural substrate for this enzyme may be peptidyl-tRNA which drop off the ribosome during protein synthesis [1,2]. Bacterial PTH has been found [2,3] to be evolutionary related to yeast hypothetical protein YHR189w.

PTH and YHR189w are proteins of about 200 amino acid residues. As signature patterns, we selected two conserved regions that each contain an histidine. The first of these regions is located in the N-terminal section, the other in the central part.

Last update:

December 2004 / Pattern and text revised.

Technical section

PROSITE methods (with tools and information) covered by this documentation:

PEPT_TRNA_HYDROL_2, PS01196; Peptidyl-tRNA hydrolase signature 2  (PATTERN)

PEPT_TRNA_HYDROL_1, PS01195; Peptidyl-tRNA hydrolase signature 1  (PATTERN)


1AuthorsGarcia-Villegas M.R. De La Vega F.M. Galindo J.M. Segura M. Buckingham R.H. Guarneros G.
SourceEMBO J. 10:3549-3555(1991).

2AuthorsDe La Vega F.M. Galindo J.M. Old I.G. Guarneros G.
SourceGene 169:97-100(1996).

3AuthorsOuzounis C. Bork P. Casari G. Sander C.
TitleNew protein functions in yeast chromosome VIII.
SourceProtein Sci. 4:2424-2428(1995).
PubMed ID8563640

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