Protein Family Models

This domain is found in peptide chain release factors. [1]. 19064930. Crystal structure of a translation termination complex formed with release factor RF2. Korostelev A, Asahara H, Lancaster L, Laurberg M, Hirschi A, Zhu J, Trakhanov S, Scott WG, Noller HF;. Proc Natl Acad Sci U S A. 2008;105:19684-19689. (from Pfam)

Date:

2024-10-16

This domain is found in peptide chain release factors such as RF-1 (Swiss:P07011) and RF-2 (Swiss:P07012), and a number of smaller proteins of unknown function such as Swiss:P40711. This domain contains the peptidyl-tRNA hydrolase activity. The domain contains a highly conserved motif GGQ, where the glutamine is thought to coordinate the water that mediates the hydrolysis. [1]. 10676813. The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. Song H, Mugnier P, Das AK, Webb HM, Evans DR, Tuite MF, Hemmings BA, Barford D;. Cell 2000;100:311-321. (from Pfam)

Date:

2024-10-16

peptide chain release factor 1 directs the termination of translation in response to the peptide chain termination codons UAG and UAA

Date:

2024-04-25

Recognizes the termination signals UAG and UAA during protein translation a specificity which is dependent on amino acid residues residing in loops of the L-shaped tRNA-like molecule of RF1

Gene:

prfA

Date:

2021-07-29

This HMM describes peptide chain release factor 1 (PrfA, RF-1), and excludes the related peptide chain release factor 2 (PrfB, RF-2). RF-1 helps recognize and terminate translation at UAA and UAG stop codons. The mitochondrial release factors are prfA-like, although not included above the trusted cutoff for this model. RF-1 does not have a translational frameshift.

Gene:

prfA

Date:

2021-04-27