Protein Domain : Methionine aminopeptidase, archaeal IPR028595

Type	Family
Description	Methionine aminopeptidase ( ) (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 [ ]. All MAP studied to date are monomeric proteins that require cobalt ions for activity. Two subfamilies of MAP enzymes are known to exist [, ]. While being evolutionary related, they only share a limited amount of sequence similarity mostly clustered around the residues shown, in the Escherichia coli MAP [], to be involved in cobalt-binding. The first family consists of enzymes from prokaryotes as well as eukaryotic MAP-1 (), while the second group is made up of archaeal MAP and eukaryotic MAP-2 and includes proteins which do not seem to be MAP, but that are clearly evolutionary related such as mouse proliferation-associated protein1 and fission yeast curved DNA-binding protein. This entry represents the archaeal MAP, which belongs to the subfamily two [ ].
Short Name	MetAP_archaeal