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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_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 2: Vacuolar aspartic proteinase

There are 2 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
Saccharopepsin. [EC: 3.4.23.25]
Hydrolysis of proteins with broad specificity for peptide bonds. Cleaves -Leu-Leu-|-Val-Tyr- bond in a synthetic substrate. Does not act on esters of Tyr or Arg.
  • Located in the vacuole.
  • Belongs to peptidase family A1.
  • Formerly EC 3.4.4.17, EC 3.4.23.6 and EC 3.4.23.8.
 65 A0A0J5PY94 A0A0J5PY94 A0A0J5PY94 A0A0J5PY94 A0A0L8VFV1 A0A0L8VFV1 A0A0L8VFV1 A0A0L8VFV1 A0A0L8VFV1 A0A0L8VFV1
(55 more...)
Phytepsin. [EC: 3.4.23.40]
Prefers hydrophobic residues Phe, Val, Ile, Leu, and Ala at P1 and P1', but also cleaves -Phe-|-Asp- and -Asp-|-Asp- bonds in 2S albumin from plant seeds.
  • Known particularly fron barley grain, but present in other plants also.
  • Belongs to peptidase family A1.
 4 A0A287GN26 A0A287GN26 P42210 P42210