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:

"
Acid Proteases
".

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: Aspartic protease

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
Yapsin 1. [EC: 3.4.23.41]
Hydrolyzes various precursor proteins with Arg or Lys in P1, and commonly Arg or Lys also in P2. The P3 amino acid is usually non-polar, but otherwise additional basic amino acids are favorable in both non- prime and prime positions.
  • Weakly inhibited by pepstatin.
  • Can partially substitute for kexin in a deficient strain of Saccharomyces cerevisiae.
  • The homologous product of the MKC7 gene (S.cerevisiae) has similar catalytic activity and has been termed yapsin 2.
  • Belongs to peptidase family A1.
50 A0A0L8VKP1 A0A0L8VKP1 A0A0L8VKP1 A0A0L8VKP1 A0A0L8VKP1 A0A0L8VKP1 A0A0L8VKP1 A7A122 A7A122 A7A122
(40 more...)
Barrierpepsin. [EC: 3.4.23.35]
Selective cleavage of 6-Leu-|-Lys-7 bond in the pheromone alpha-mating factor.
  • Belongs to peptidase family A1.
36 B5VKS5 B5VKS5 B5VKS5 B5VKS5 B5VKS5 B5VKS5 C7GSF7 C7GSF7 C7GSF7 C7GSF7
(26 more...)
Candidapepsin. [EC: 3.4.23.24]
Preferential cleavage at the carboxyl of hydrophobic amino acids, but fails to cleave 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17 and 24-Phe-|-Phe-25 of insulin B chain. Activates trypsinogen, and degrades keratin.
  • This endopeptidase from the imperfect yeast Candida albicans is inhibited by pepstatin, but not by methyl 2-diazoacetamido-hexanoate or 1,2-epoxy-3-(p-nitrophenoxy)propane.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17 and EC 3.4.23.6.
31 A0A454J8J3 C4YMJ3 C4YNQ5 C4YQ21 C4YQ21 C4YSF6 C4YSN0 C4YSN0 O42778 O42779
(21 more...)
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