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Peptidase M1 N-terminal domain
This domain is found at the N-terminus of aminopeptidases from the M1 family. (from Pfam)
aminopeptidase N C-terminal domain-containing protein
This presumed domain is functionally uncharacterised. This domain is found in bacteria, archaea and eukaryotes. (from Pfam)
DUF3458 domain-containing protein
This presumed domain is functionally uncharacterised. This domain is found in bacteria, archaea and eukaryotes. The domain has an Ig-like fold. This domain is found associated with Pfam:PF01433. (from Pfam)
M1 family aminopeptidase
The M1 family metalloproteases in this family are zinc-dependent enzymes with aminopeptidase activity.
M1 family metallopeptidase
M1 family metallopeptidase is a zinc-dependent metallopeptidase that functions as an aminopeptidase and contains an HEXXH motif as part of its active site; such as aminopeptidase N, which is a type II integral membrane protease that preferentially cleaves neutral amino acids from the N-terminus of oligopeptides
aminopeptidase N
The M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, EC 3.4.11.2, after the Escherichia coli enzyme, suggesting a similar activity profile (see SP|P04825 for a description of catalytic activity). This family consists of all aminopeptidases closely related to E. coli PepN and presumed to have similar (not identical) function. Nearly all are found in Proteobacteria, but members are found also in Cyanobacteria, plants, and apicomplexan parasites. This family differs greatly in sequence from the family of aminopeptidases typified by Streptomyces lividans PepN (TIGR02412), from the membrane bound aminopeptidase N family in animals, etc.
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