The domain within your query sequence starts at position 631 and ends at position 913; the E-value for the Peptidase_M16_M domain shown below is 1e-91.

EFHYQEQTDPVEYVENMCENMQLYPRQDFLTGDQLLFEYKPEVIAEALNQLVPQKANLVL
LSGANEGRCDLKEKWFGTQYSIEDIENSWTELWKSNFDLNPDLHLPAENKYIATDFTLKA
FDCPETEYPAKIVNTAQGCLWYKKDNKFKIPKAYIRFHLISPLIQKSAANVVLFDIFVNI
LTHNLAEPAYEADVAQLEYKLVAGEHGLIIRVKGFNHKLPLLFQLIIDYLTEFSSTPAVF
TMITEQLKKTYFNILIKPETLAKDVRLLILEYSRWSMIDKYQA

Peptidase_M16_M

Peptidase_M16_M
PFAM accession number:PF16187
Interpro abstract (IPR032632):

This is the third domain of some M16 peptidases, such as insulin-degrading-enzyme in eukaryotes or protease 3 from bacteria [(PUBMED:8099278)]. Insulin-degrading enzymes - insulysin - are zinc metallopeptidases that metabolise several bioactive peptides, including insulin and the amyloid-beta-peptide. The tertiary structure of insulin-degrading enzymes resembles a clamshell composed of four structurally similar domains arranged to enclose a large central chamber. Substrates must enter the chamber, and it is likely that a hinge-like conformational change allows substrate binding and product release. Triphosphates are found to dock between the inner surfaces of the non-catalytic domains three and four [(PUBMED:22049080)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M16_M