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CATH Superfamily 3.90.230.10

Creatinase/methionine aminopeptidase superfamily

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Creatinase/methionine aminopeptidase superfamily
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 11: Methionine aminopeptidase

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Methionyl aminopeptidase. [EC: 3.4.11.18]
Release of N-terminal amino acids, preferentially methionine, from peptides and arylamides.
  • This membrane-bound enzyme, which is present in both prokaryotes and eukaryotes, releases the initiator methionine from nascent peptides.
  • The activity is dependent on the identity of the second, third and fourth amino acid residues of the target protein, but in general the enzyme acts only when the penultimate residue is small and uncharged (e.g. Gly, Ala, Cys, Ser, Thr, and Val).
  • Belongs to peptidase family M24A.
 12 A0A178UWL4 A0A178UWL4 Q24JL4 Q24JL4 Q4VBS4 Q6UB28 Q9CPW9 Q9FV50 Q9FV50 Q9FV51
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