The domain within your query sequence starts at position 136 and ends at position 268; the E-value for the eRF1_2 domain shown below is 1.1e-38.
DVAAVVMQEGLAHVCLVTPSMTLTRAKVEVNIPRKRKGNCSQHDRALERFYEQVVQAIQR HINFEVVKCVLVASPGFVREQFCDYMFQQAVKTDNKVLLENRSKFLQVHASSGHKYSLKE ALCDPTVASRLSD
eRF1_2 |
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PFAM accession number: | PF03464 |
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Interpro abstract (IPR005141): | 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 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 domain is also found in other proteins which may also be involved in translation termination |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry eRF1_2