The domain within your query sequence starts at position 231 and ends at position 430; the E-value for the Peptidase_M16_C domain shown below is 4.1e-43.

KIDREVLHSYLKNYYTPDRMVLAGVGVEHEHLVECARKYLVGAEPAWGAPGTVDVDRSVA
QYTGGIIKVERDMSNVSLGPTPIPELTHIMVGLESCSFLEDDFIPFAVLNMMMGGGGSFS
AGGPGKGMFSRLYLNVLNRHHWMYNATSYHHSYEDTGLLCIHASADPRQVREMVEIITKE
FILMGRTVDLVELERAKTQL

Peptidase_M16_C

Peptidase_M16_C
PFAM accession number:PF05193
Interpro abstract (IPR007863):

These metallopeptidases belong to MEROPS peptidase family M16 (clan ME). They include proteins, which are classified as non-peptidase homologues either have been found experimentally to be without peptidase activity, or lack amino acid residues that are believed to be essential for the catalytic activity.

The peptidases in this group of sequences include:

  • Insulinase, insulin-degrading enzyme (EC 3.4.24.56)
  • Mitochondrial processing peptidase alpha subunit, (Alpha-MPP, EC 3.4.24.64)
  • Pitrlysin, Protease III precursor (EC 3.4.24.55)
  • Nardilysin, (EC 3.4.24.61)
  • Ubiquinol-cytochrome C reductase complex core protein I,mitochondrial precursor (EC 1.10.2.2)
  • Coenzyme PQQ synthesis protein F (EC 3.4.99)

These proteins do not share many regions of sequence similarity; the most noticeable is in the N-terminal section. This region includes a conserved histidine followed, two residues later by a glutamate and another histidine. In pitrilysin, it has been shown [(PUBMED:7990931)] that this H-x-x-E-H motif is involved in enzymatic activity; the two histidines bind zinc and the glutamate is necessary for catalytic activity. The mitochondrial processing peptidase consists of two structurally related domains. One is the active peptidase whereas the other, the C-terminal region, is inactive. The two domains hold the substrate like a clamp [(PUBMED:11470436)].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M16_C