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InterPro: IPR001328 Peptidyl-tRNA hydrolase

Protein matches Help

UniProtKB

Matches:

1843 proteins

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

Accession

IPR001328 Pept_tRNA_hydro

Type

Family

Signatures Help

Database	ID	Name	Proteins
Gene3D	G3DSA:3.40.50.1470	Pept_tRNA_hydro	1789
Pfam	PF01195	Pept_tRNA_hydro	1810
PANTHER	PTHR17224	Pept_tRNA_hydro	1827
SuperFamily	SSF53178	Pept_tRNA_hydro	1833
TIGRFAMs	TIGR00447	pth	1708
Signatures in BioMart

InterPro Relationships Help

Contains

IPR018171 Peptidyl-tRNA hydrolase, conserved site

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

PDBe-motif: PS01195 , PS01196

Enzyme: EC:3.1.1.29

PROSITE doc: PDOC00920

PANDIT: PF01195

Blocks: IPB001328

Taxonomic coverage Help

Overlapping InterPro entries Help

IPR001328

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