InterPro

This group of metallopeptidases belong to MEROPS peptidase family M24 (clan MG), subfamily M24A.

Methionine aminopeptidase (EC:3.4.11.18) (MAP) catalyses the hydrolytic cleavage of the N-terminal methionine from newly synthesised polypeptides if the penultimate amino acid is small, with different tolerance to Val and Thr at this position [PMID: 20521764]. All MAP studied to date are monomeric proteins that require cobalt ions for activity. Two subfamilies of MAP enzymes are known to exist [PMID: 7644482, PMID: 8772380]. While being evolutionary related, they only share a limited amount of sequence similarity mostly clustered around the residues shown, in the Escherichia coli MAP [PMID: 8471602], to be involved in cobalt-binding. The first family consists of enzymes from prokaryotes as well as eukaryotic MAP-1 (IPR002467), while the second group is made up of archaeal MAP and eukaryotic MAP-2 [PMID: 9399590] and includes proteins which do not seem to be MAP, but that are clearly evolutionary related such as mouse proliferation-associated protein 1 and fission yeast curved DNA-binding protein.