Protein Domain : Peptidase M18 IPR001948

Type	Family
Description	This group of metallopeptidases belong to the MEROPS peptidase family M18, (clan MH). The proteins have two catalytic zinc ions at the active site, bound by His/Asp, Asp, Glu, Asp/Glu and His. The catalysed reaction involves the release of an N-terminal aminoacid, usually neutral or hydrophobic, from a polypeptide [ ].The type example is aminopeptidase I from Saccharomyces cerevisiae (Baker's yeast), the sequence of which has been deduced, and the mature protein shown to consist of 469 amino acids []. A 45-residue presequence contains bothpositively- and negatively-charged and hydrophobic residues, which could be arranged in an N-terminal amphiphilic α-helix []. The presequence differs fromsignal sequences that direct proteins across bacterial plasma membranes and endoplasmic reticulum or into mitochondria. It is unclear how this uniquepresequence targets aminopeptidase I to yeast vacuoles, and how this sorting utilises classical protein secretory pathways [].
Short Name	Peptidase_M18