The domain within your query sequence starts at position 255 and ends at position 464; the E-value for the Reprolysin domain shown below is 1.5e-26.



PFAM accession number:PF01421
Interpro abstract (IPR001590):

Metalloproteases are the most diverse of the four main types of protease, with more than 50 families identified to date. In these enzymes, a divalent cation, usually zinc, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. The known metal ligands are His, Glu, Asp or Lys and at least one other residue is required for catalysis, which may play an electrophillic role. Of the known metalloproteases, around half contain an HEXXH motif, which has been shown in crystallographic studies to form part of the metal-binding site [(PUBMED:7674922)]. The HEXXH motif is relatively common, but can be more stringently defined for metalloproteases as 'abXHEbbHbc', where 'a' is most often valine or threonine and forms part of the S1' subsite in thermolysin and neprilysin, 'b' is an uncharged residue, and 'c' a hydrophobic residue. Proline is never found in this site, possibly because it would break the helical structure adopted by this motif in metalloproteases [(PUBMED:7674922)].

This group of metallopeptidases belong to the MEROPS peptidase family M12, subfamily M12B (adamalysin family, clan (MA(M)). The protein fold of the peptidase domain for members of this family resembles that of thermolysin, the type example for clan MA and the predicted active site residues for members of this family and thermolysin occur in the motif HEXXH [(PUBMED:7674922)].

The adamalysins are zinc dependent endopeptidases found in snake venom. There are some mammalian proteins such as P78325, and fertilin Q28472. Fertilin and closely related proteins appear to not have some active site residues and may not be active enzymes.

CD156 (also called ADAM8 (EC 3.4.24) or MS2 human) has been implicated in extravasation of leukocytes.

GO process:proteolysis (GO:0006508)
GO function:metalloendopeptidase activity (GO:0004222)

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