The domain within your query sequence starts at position 76 and ends at position 226; the E-value for the Peptidase_M16 domain shown below is 1.6e-47.

RVASQNKFGQFCTVGILINSGSRYEAKYLSGIAHFLEKLAFSSTARFDSKDEILLTLEKH
GGICDCQTSRDTTMYAVSADSKGLDTVVDLLADVVLHPRLTDEEIEMTRMAVQFELEDLN
MRPDPEPLLTEMIHEAAFRENTVGLHRFCPV

Peptidase_M16

Peptidase_M16
PFAM accession number:PF00675
Interpro abstract (IPR011765):

This entry represents an N-terminal domain found in metallopeptidases and non-peptidase homologues belonging to MEROPS peptidase family M16 (clan ME), subfamilies M16A, M16B and M16C. Members of this family 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 proteins 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.

This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M16