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:

"
tricorn interacting facor f3 domain
".

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 1: Leucyl-cystinyl aminopeptidase

There are 3 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.
  • Is not activated by heavy metal ions.
  • Belongs to peptidase family M1.
  • Formerly EC 3.4.1.2, EC 3.4.3.5 and EC 3.4.13.6.
11 A0A024RC61 A0A024RC61 P15144 P15144 P15145 P15541 P15684 P79098 P79143 P79171
(1 more...)
Cystinyl aminopeptidase. [EC: 3.4.11.3]
Release of an N-terminal amino acid, Cys-|-Xaa-, in which the half- cystine residue is involved in a disulfide loop, notably in oxytocin or vasopressin. Hydrolysis rates on a range of aminoacyl arylamides exceed that for the cystinyl derivative, however.
  • Belongs to peptidase family M1.
3 P97629 Q8C129 Q9UIQ6
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.
  • From the plasma fraction of chicken egg yolk.
  • Belongs to peptidase family M1.
1 O57579
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