eRF1_1 | |
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| SMART ACC: | SM001194 |
| Description: | The release factor eRF1 terminates protein biosynthesis by recognising stop codons at the A site of the ribosome and stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known (PUBMED:10676813). The overall shape 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 tip of domain 2 suggests that the Gln residue coordinates a water molecule to mediate the hydrolytic activity at the peptidyl transferase centre. A conserved groove on domain 1, 80 A from the GGQ motif, is proposed to form the codon recognition site (PUBMED:10676813). This family also includes other proteins for which the precise molecular function is unknown. Many of them are from Archaebacteria. These proteins may also be involved in translation termination but this awaits experimental verification. |
| InterPro ACC: | IPR005140 |
| InterPro abstract: | 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 stimulating peptidyl-tRNA bond hydrolysis at the peptidyl transferase centre. The crystal structure of human eRF1 is known [ PUBMED:10676813 ]. The overall shape and dimensions … expand |
| Family alignment: | View the Family alignment or the Alignment consensus sequence |
| There are 5 259 eRF1_1 domains in 5 257 proteins in SMART's NRDB database. | |
Taxonomic distribution of proteins containing eRF1_1 domains
The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing eRF1_1 domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.
Predicted cellular role
| Cellular role: | Translation |
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Relevant references for this domain
Primary literature for the eRF1_1 domain is listed below. Automatically-derived, secondary literature is also available.
KEGG pathways involving proteins which contain this domain
This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a eRF1_1 domain which could be assigned to a KEGG orthologous group, and not all proteins containing eRF1_1 domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.