The domain within your query sequence starts at position 271 and ends at position 370; the E-value for the eRF1_3 domain shown below is 4.9e-28.

AAGEVKALDDFYKMLQHEPDRAFYGLKQVERANEALAIDTLLISDELFRHQDVATRSRYV
RLVDSVKENAGTVRIFSSLHVSGEQLGQLTGVAAILRFPV

eRF1_3

eRF1_3
PFAM accession number:PF03465
Interpro abstract (IPR005142):

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 but this awaits experimental verification.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry eRF1_3