HMM Summary Page: TIGR02414

Functionaminopeptidase N
Gene SymbolpepN
Trusted Cutoff718.20
Domain Trusted Cutoff718.20
Noise Cutoff403.85
Domain Noise Cutoff403.85
Isology Typeequivalog
EC Number3.4.11.2
HMM Length868
Mainrole CategoryProtein fate
Subrole CategoryDegradation of proteins, peptides, and glycopeptides
Gene Ontology TermGO:0004177: aminopeptidase activity molecular_function
GO:0006508: proteolysis biological_process
GO:0008237: metallopeptidase activity molecular_function
AuthorHaft DH
Entry DateDec 23 2004 10:57AM
Last ModifiedFeb 14 2011 3:27PM
CommentThe M1 family of zinc metallopeptidases contains a number of distinct, well-separated clades of proteins with aminopeptidase activity. Several are designated aminopeptidase N, EC, 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.
ReferencesDR SWISSPROT; P04825; Escherichia coli DR PFAM; PF01433; Peptidase family M1 RM 14663077 RT PepN is the major aminopeptidase in Escherichia coli: insights on substrate specificity and role during sodium-salicylate-induced stress. RA Chandu D, Nandi D. RL Microbiology. 2003 Dec;149(Pt 12):3437-47.