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PCRF domain-containing protein
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)
peptide chain release factor-like protein
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)
peptide chain release factor 2
The bacterial peptide chain release factor 2 (RF-2), product of the prfB gene, recognizes the stop codons UGA and UAA during protein translation, and it is the only release factor to recognize UGA. In about 80 percent of known bacterial species, a +1 frameshift must occur at a UGA stop codon about 25 amino acids from the N-terminus, or translation is aborted by a premature termination. RF-2 can therefore regulate its own production by readthrough only when RF-2 is insufficient.
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