InterPro : IPR005140

Name  eRF1 domain 1/Pelota-like Short Name  eRF1_1_Pelota
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 for which the precise molecular function is unknown. Many of them are fromArchaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification.
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

1 Child Features

Id Name Short Name Type
IPR024049 Peptide Chain Release Factor eRF1/aRF1, N-terminal Release_factor_eRF1/aRF1_N Domain

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

0 Parent Features

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)