The ZnMc domain within your query sequence starts at position 131 and ends at position 273, and its E-value is 1.32e-54.

All catalytic sites are present in this domain, and marked green in the sequence below. Check the literature (PubMed 96311273 ) for details.

PERVWPDGVIPFVIGGNFTGSQRAVFRQAMRHWEKHTCVTFLERTDEDSYIVFTYRPCGCCSYVGRRGGGPQAISIGKNCDKFGIVVHELGHVIGFWHEHTRPDRDRHVSIVRENIQPGQEYNFLKMEVQEVESLGETYDFDS

ZnMc Zinc-dependent metalloprotease
SMART ACC:	SM000235
Description:	Neutral zinc metallopeptidases. This alignment represents a subset of known subfamilies. Highest similarity occurs in the HExxH zinc-binding site/ active site.
InterPro ACC:	IPR006026
InterPro abstract:	This entry includes metallopeptidases associated with MEROPS peptidase families: M7, M8, M10 and M12, all of which are members of clan MA(M). The majority of zinc-dependent metallopeptidases (with the notable exception of the carboxypeptidases) share a common pattern of primary structure [ PUBMED:2914602 expand This entry includes metallopeptidases associated with MEROPS peptidase families: M7, M8, M10 and M12, all of which are members of clan MA(M). The majority of zinc-dependent metallopeptidases (with the notable exception of the carboxypeptidases) share a common pattern of primary structure [ PUBMED:2914602 PUBMED:1894005 ] in the part of their sequence involved in the binding of zinc, and can be grouped together as a superfamily,known as the metzincins, on the basis of this sequence similarity. They can be classified into around 40 distinct families [ PUBMED:7674922 ]. Over 70 metallopeptidase families have been identified to date. In these enzymes a divalent cation, which is usually zinc but may be cobalt, manganese or copper, activates the water molecule. The metal ion is held in place by amino acid ligands, usually three in number. In some families of co-catalytic metallopeptidases, two metal ions are observed in crystal structures ligated by five amino acids, with one amino acid ligating both metal ions. The known metal ligands are His, Glu, Asp or Lys. At least one other residue is required for catalysis, which may play an electrophilic role. Many metalloproteases 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 ]. collapse
GO process:	proteolysis (GO:0006508)
GO function:	metallopeptidase activity (GO:0008237), zinc ion binding (GO:0008270)
Family alignment:	View the Family alignment or the Alignment consensus sequence
There are 34 425 ZnMc domains in 34 168 proteins in SMART's NRDB database.

Taxonomic distribution of proteins containing ZnMc domains

The tree below includes only several representative species and genera. The complete taxonomic breakdown of all proteins containing ZnMc domains can be accessed here. Click the counts or percentage values to display the corresponding proteins.

Predicted cellular role

Binding / catalysis:	Peptidase; zinc-binding

Relevant references for this domain

Primary literature for the ZnMc domain is listed below. Automatically-derived, secondary literature is also available.

KEGG pathways involving proteins which contain this domain

This information is based on the mapping of SMART genomic protein database to KEGG orthologous groups. Percentages are related to the number of proteins containing a ZnMc domain which could be assigned to a KEGG orthologous group, and not all proteins containing ZnMc domains. Please note that proteins can be included in multiple pathways, ie. the numbers below will not add to 100%.

KEGG pathways

Some of these pathways are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

KEGG orthologous groups

Some of these KOs are included in the interactive Pathways Explorer overview maps. Select an overview map and click the button below to highlight them in iPath.

3D structures in PDB containing this domain

Links to other resources describing this domain

InterPro	IPR006026