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:
"Neutral Protease Domain 2
".
FunFam 1: Aminopeptidase
There are 4 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 |
|---|---|---|
|
Membrane alanyl aminopeptidase.
[EC: 3.4.11.2]
Release of an N-terminal amino acid, Xaa-|-Yaa- from a peptide, amide or arylamide. Xaa is preferably Ala, but may be most amino acids including Pro (slow action). When a terminal hydrophobic residue is followed by a prolyl residue, the two may be released as an intact Xaa-Pro dipeptide.
|
27 |
A0A024RC61
A0A024RC61
A0A178UWR6
A0A178UWR6
B8BAI7
B8BAI7
B8BAI7
I1QIF7
I1QIF7
I1QIF7 (17 more...) |
|
Glutamyl aminopeptidase.
[EC: 3.4.11.7]
Release of N-terminal glutamate (and to a lesser extent aspartate) from a peptide.
|
8 | P16406 P16406 P50123 Q07075 Q32LQ0 Q52JJ6 Q52JJ6 Q95334 |
|
Cytosol alanyl aminopeptidase.
[EC: 3.4.11.14]
Release of an N-terminal amino acid, preferentially alanine, from a wide range of peptides, amides and arylamides.
|
5 | K7CGL0 K7CGL0 P55786 P55786 Q11011 |
|
Aminopeptidase Ey.
[EC: 3.4.11.20]
Differs from other aminopeptidases in broad specificity for amino acids in the P1 position and the ability to hydrolyze peptides of four or five residues that contain Pro in the P1' position.
|
1 | O57579 |
