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InterPro: IPR018171 Peptidyl-tRNA hydrolase, conserved site

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1764 proteins

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Detailed:	sorted by AC,	sorted by name,	of known structure	proteins with splice variants
Table:	For all matching proteins,	of known structure
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Accession List
Matches in BioMart

Accession

IPR018171 Pept_tRNA_hydro_CS

Type

Conserved_site

Signatures Help

Database	ID	Name	Proteins
PROSITE pattern	PS01195	PEPT_TRNA_HYDROL_1	1508
PROSITE pattern	PS01196	PEPT_TRNA_HYDROL_2	1510
Signatures in BioMart

InterPro Relationships Help

Found in

IPR001328 Peptidyl-tRNA hydrolase

GO Term annotation Help

Process

GO:0006412 translation

Function

GO:0004045 aminoacyl-tRNA hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

Peptidyl-tRNA hydrolase (EC:3.1.1.29) (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 to be evolutionary related to a yeast protein [3].

Structural links Help

PDB - click here

SCOP: c.56.3.1

CATH: 3.40.50.1470

Database links Help

Enzyme: EC:3.1.1.29

CluSTr: ALLvsALL:5054:40.1

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR018171

Numbers of overlapping proteins

Average numbers of overlapping amino acids

Example proteins Help

P38876 Peptidyl-tRNA hydrolase

Q10LI6 CRS2-like protein, chloroplastic

Q6NLS8 Peptidyl-tRNA hydrolase, mitochondrial

Q86Y79 Probable peptidyl-tRNA hydrolase

Q8BW00 Probable peptidyl-tRNA hydrolase

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR018171	Peptidyl-tRNA hydrolase, conserved site
IPR001328	Peptidyl-tRNA hydrolase
	SWISS-MODEL
	ModBase

Publications Open in usermanual
1.	Garcia-Villegas MR, De La Vega FM, Galindo JM, Segura M, Buckingham RH, Guarneros G. Peptidyl-tRNA hydrolase is involved in lambda inhibition of host protein synthesis. EMBO J. 10 3549-55 1991 [PubMed: 1833189] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=1833189&action=stream&blobtype=pdf
2.	De La Vega FM, Galindo JM, Old IG, Guarneros G. Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of Escherichia coli. Gene 169 97-100 1996 [PubMed: 8635758] http://dx.doi.org/10.1016/0378-1119(95)00823-3
3.	Ouzounis C, Bork P, Casari G, Sander C. New protein functions in yeast chromosome VIII. Protein Sci. 4 2424-8 1995 [PubMed: 8563640] http://ukpmc.ac.uk/picrender.cgi?tool=EBI&pubmedid=8563640&action=stream&blobtype=pdf

Additional Reading Open in usermanual
	Ostheimer GJ, Hadjivassiliou H, Hadjivasiliou H, Kloer DP, Barkan A, Matthews BW. Structural analysis of the group II intron splicing factor CRS2 yields insights into its protein and RNA interaction surfaces. J. Mol. Biol. 345 2005 51-68 [PubMed: 15567410] http://dx.doi.org/10.1016/j.jmb.2004.10.032
	Selvaraj M, Roy S, Singh NS, Sangeetha R, Varshney U, Vijayan M. Structural plasticity and enzyme action: crystal structures of mycobacterium tuberculosis peptidyl-tRNA hydrolase. J. Mol. Biol. 372 2007 186-93 [PubMed: 17619020] http://dx.doi.org/10.1016/j.jmb.2007.06.053
	Schmitt E, Mechulam Y, Fromant M, Plateau P, Blanquet S. Crystal structure at 1.2 A resolution and active site mapping of Escherichia coli peptidyl-tRNA hydrolase. EMBO J. 16 1997 4760-9 [PubMed: 9303320] http://dx.doi.org/10.1093/emboj/16.15.4760

InterPro 23.1