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CATH Superfamily 2.40.70.10

Acid Proteases

The name of this superfamily has been modified since the most recent official CATH+ release (v4_2_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 23181: Aspartyl protease family protein

There are 5 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
Gastricsin. [EC: 3.4.23.3]
More restricted specificity than pepsin A, but shows preferential cleavage at Tyr-|-Xaa bonds. High activity on hemoglobin.
  • Formed from progastricsin, apparently in the gastric juice of most vertebrates.
  • In addition to the fundus, progastricsin is also secreted in antrum and proximal duodenum.
  • Seminal plasma contains a zymogen that is immunologically identical with progastricsin.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.22.
 8 B9RG92 B9RG92 B9RM62 B9RM62 B9S098 B9S098 B9SCN7 B9SCN7
Pepsin A. [EC: 3.4.23.1]
Preferential cleavage: hydrophobic, preferably aromatic, residues in P1 and P1' positions. Cleaves 1-Phe-|-Val-2, 4-Gln-|-His-5, 13-Glu-|-Ala-14, 14-Ala-|-Leu-15, 15-Leu-|-Tyr-16, 16-Tyr-|-Leu-17, 23-Gly-|-Phe-24, 24-Phe-|-Phe-25 and 25-Phe-|-Tyr-26 bonds in the B chain of insulin.
  • The predominant endopeptidase in the gastric juice of vertebrates, formed from pepsinogen A by limited proteolysis.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.1.
 6 B9R734 B9R734 B9RNR8 B9RNR8 B9SG33 B9SG33
Nepenthesin. [EC: 3.4.23.12]
Similar to pepsin, but also cleaves on either side of Asp and at Lys-|-Arg.
  • From the insectivorous plants Nepenthes sp. (secretions) and Drosera peltata (ground-up leaves).
  • Aspartic endopeptidases are probably present in many other plants, including lotus and sorghum.
  • Formerly EC 3.4.99.4.
 4 Q766C2 Q766C2 Q766C3 Q766C3
Proteasome endopeptidase complex. [EC: 3.4.25.1]
Cleavage of peptide bonds with very broad specificity.
  • A 20-S protein composed of 28 subunits arranged in four rings of seven.
  • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
  • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
  • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
  • Terminal apertures restrict access of substrates to the active sites.
  • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
  • Belongs to peptidase family T1.
  • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
 2 A0A1E5WFF7 A0A1E5WFF7
Gly-Xaa carboxypeptidase. [EC: 3.4.17.4]
Release of a C-terminal amino acid from a peptide in which glycine is the penultimate amino acid, e.g. Z-Gly-|-Leu.
  • Belongs to peptidase family M20A.
  • Formerly EC 3.4.2.3, EC 3.4.12.8 and EC 3.4.17.9.
 2 A0A0M3R844 A0A0M3R844