3 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR000642 |
| GO:0005524 | IPR000642 |
| GO:0006508 | IPR000642 |
| Type: | Domain | Name: | Peptidase M41 |
| Description: | 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 []. 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 [].This group of metallopeptidases belong to MEROPS peptidase family M41 (FtsH endopeptidase family, clan MA(E)). The predicted active site residues for members of this family and thermolysin, the type example for clan MA, occur in the motif HEXXH.The peptidase M41 family belong to a larger family of zinc metalloproteases. This family includes the cell division protein FtsH, and the yeast mitochondrial respiratory chain complexesassembly protein, which is a putative ATP-dependent protease required for assembly of the mitochondrial respiratory chain and ATPase complexes. FtsH is an integral membrane protein,which seems to act as an ATP-dependent zinc metallopeptidase that binds one zinc ion. | Short Name: | Peptidase_M41 |
| GO Term | Gene Name |
|---|---|
| GO:0004222 | IPR000642 |
| GO:0005524 | IPR000642 |
| GO:0006508 | IPR000642 |
