The domain within your query sequence starts at position 359 and ends at position 561; the E-value for the Peptidase_M28 domain shown below is 1.2e-18.
NVIGTLKGALEPDRYVILGGHRDAWVFGGIDPQSGAAVVHEIVRSFGTLKKKGRRPRRTI LFASWDAEEFGLLGSTEWAEEHSRLLQERGVAYINADSSIEGNYTLRVDCTPLMYSLVYN LTKELQSPDEGFEGKSLYDSWKEKSPSPEFIGMPRISKLGSGNDFEVFFQRLGIASGRAR YTKNWKTNKVSSYPLYHSVYETY
Peptidase_M28 |
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PFAM accession number: | PF04389 |
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Interpro abstract (IPR007484): | 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 electrophillic 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) ]. This domain is found in metallopeptidases belonging to the MEROPS peptidase family M28 (aminopeptidase Y, clan MH) [ (PUBMED:7674922) ]. They also contain a transferrin receptor-like dimerisation domain ( IPR007365 ) and a protease-associated PA domain ( IPR003137 ). |
This is a PFAM domain. For full annotation and more information, please see the PFAM entry Peptidase_M28