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InterPro: IPR002833 Peptidyl-tRNA hydrolase, PTH2

Protein matches Help

UniProtKB

Matches:

418 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

IPR002833 Pep_tRNA_hydro_PTH2

Type

Domain

Signatures Help

Database	ID	Name	Proteins
Pfam	PF01981	PTH2	418
TIGRFAMs	TIGR00283	Pep_tRNA_hydro_PTH2	287
Signatures in BioMart

GO Term annotation Help

Process

GO:0006412 translation

Function

GO:0004045 aminoacyl-tRNA hydrolase activity

InterPro annotation

Entry Details in BioMart

Abstract

Peptidyl-tRNA hydrolases are enzymes that release tRNAs from peptidyl-tRNA during translation.

Structural links Help

PDB - click here

SCOP: c.131.1.1

CATH: 3.40.1490.10

Database links Help

Enzyme: EC:3.1.1.29

PANDIT: PF01981

Blocks: IPB002833

Pfam Clan: CL0305.1

Taxonomic coverage Help

Example proteins Help

O76387 Probable peptidyl-tRNA hydrolase 2

O97067 Probable peptidyl-tRNA hydrolase 2

P34222 Peptidyl-tRNA hydrolase 2

Q8R2Y8 Peptidyl-tRNA hydrolase 2, mitochondrial

Q9Y3E5 Peptidyl-tRNA hydrolase 2, mitochondrial

More proteins

Example Proteins Key

InterPro entry accession number/name and structure databases		Colour code
IPR002833	Peptidyl-tRNA hydrolase, PTH2
IPR009060	UBA-like
IPR000449	Ubiquitin-associated/translation elongation factor EF1B, N-terminal
IPR015940	Ubiquitin-associated/translation elongation factor EF1B, N-terminal, eukaryote
	SWISS-MODEL
	PDB Chain
	ModBase
	SCOP Domain
	CATH Domain

Publications Help

Additional Reading Open in usermanual
	Fromant M, Schmitt E, Mechulam Y, Lazennec C, Plateau P, Blanquet S. Crystal structure at 1.8 A resolution and identification of active site residues of Sulfolobus solfataricus peptidyl-tRNA hydrolase. Biochemistry 44 2005 4294-301 [PubMed: 15766258] http://dx.doi.org/10.1021/bi047711k
	Powers R, Acton TB, Chiang Y, Rajan PK, Cort JR, Kennedy MA, Liu J, Ma L, Rost B, Montelione GT. (1)H, (13)C and (15)N assignments for the Archaeglobus fulgidis protein AF2095. J. Biomol. NMR 30 2004 107-8 [PubMed: 15452442] http://dx.doi.org/10.1023/B:JNMR.0000042947.19593.80
	Powers R, Mirkovic N, Goldsmith-Fischman S, Acton TB, Chiang Y, Huang YJ, Ma L, Rajan PK, Cort JR, Kennedy MA, Liu J, Rost B, Honig B, Murray D, Montelione GT. Solution structure of Archaeglobus fulgidis peptidyl-tRNA hydrolase (Pth2) provides evidence for an extensive conserved family of Pth2 enzymes in archea, bacteria, and eukaryotes. Protein Sci. 14 2005 2849-61 [PubMed: 16251366] http://dx.doi.org/10.1110/ps.051666705
	Rosas-Sandoval G, Ambrogelly A, Rinehart J, Wei D, Cruz-Vera LR, Graham DE, Stetter KO, Guarneros G, Soll D. Orthologs of a novel archaeal and of the bacterial peptidyl-tRNA hydrolase are nonessential in yeast. Proc. Natl. Acad. Sci. U.S.A. 99 2002 16707-12 [PubMed: 12475929] http://dx.doi.org/10.1073/pnas.222659199
	De Pereda JM, Waas WF, Jan Y, Ruoslahti E, Schimmel P, Pascual J. Crystal structure of a human peptidyl-tRNA hydrolase reveals a new fold and suggests basis for a bifunctional activity. J. Biol. Chem. 279 2004 8111-5 [PubMed: 14660562] http://dx.doi.org/10.1074/jbc.M311449200

InterPro 23.1