InterPro : IPR005142

Name  eRF1 domain 3 Short Name  eRF1_3
Type  Domain Description  This domain is found in the release factor eRF1 which terminates protein biosynthesis by recognizing stop codons at the A site of the ribosome and stimulatingpeptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known []. The overallshape and dimensions of eRF1 resemble a tRNA molecule with domains 1, 2, and 3 of eRF1 corresponding to the anticodon loop,aminoacyl acceptor stem, and T stem of a tRNA molecule, respectively. The position of the essential GGQ motif at an exposed tipof domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyltransferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site [].This domain is also found in other proteins which may also be involved in translation termination but this awaits experimental verification.

Sequence Features

GO Displayer


InterPro protein domain ID --> Contigs



0 Child Features

0 Contains

3 Found In

Id Name Short Name Type
IPR004405 Translation release factor pelota Transl_rel_pelota Family
IPR004403 Peptide chain release factor eRF1/aRF1 Peptide_chain-rel_eRF1/aRF1 Family
IPR020918 Peptide chain release factor aRF1 Peptide_chain-rel_aRF1 Family

1 Parent Features

Id Name Short Name Type
IPR029064 50S ribosomal protein L30e-like L30e-like Domain

1 Publications

First Author Title Year Journal Volume Pages
Song H The crystal structure of human eukaryotic release factor eRF1--mechanism of stop codon recognition and peptidyl-tRNA hydrolysis. 2000 Cell 100 311-21

To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)