1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR018349 | Binding_site | Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site |
3 Ontology Annotations
| GO Term | Gene Name |
|---|---|
| GO:0004177 | IPR002468 |
| GO:0008235 | IPR002468 |
| GO:0006508 | IPR002468 |
| Type: | Family | Name: | Peptidase M24A, methionine aminopeptidase, subfamily 2 |
| Description: | This group of metallopeptidases belong to MEROPS peptidase family M24 (clan MG), subfamily M24A.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 coliMAP [], 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 protein 1 and fission yeast curved DNA-binding protein. | Short Name: | Pept_M24A_MAP2 |
| DB identifier | Type | Name |
|---|---|---|
| IPR018349 | Binding_site | Peptidase M24A, methionine aminopeptidase, subfamily 2, binding site |
| GO Term | Gene Name |
|---|---|
| GO:0004177 | IPR002468 |
| GO:0008235 | IPR002468 |
| GO:0006508 | IPR002468 |
