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CATH Superfamily 3.90.70.10

Cysteine proteinases

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:

"
Cysteine proteinases
".

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 17146: Cathepsin B-like cysteine protease

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
Cathepsin B. [EC: 3.4.22.1]
Hydrolysis of proteins with broad specificity for peptide bonds. Preferentially cleaves -Arg-Arg-|-Xaa bonds in small molecule substrates (thus differing from cathepsin L). In addition to being an endopeptidase, shows peptidyl-dipeptidase activity, liberating C-terminal dipeptides.
  • An intracellular (lysosomal) enzyme.
  • Belongs to peptidase family C1.
 126 A0A024R374 A0A024R374 A0A074SNC2 A0A074SNC2 A0A086KP44 A0A086KP44 A0A086KWX2 A0A086KWX2 A0A086LC71 A0A086LC71
(116 more...)
Dipeptidyl-peptidase I. [EC: 3.4.14.1]
Release of an N-terminal dipeptide, Xaa-Yaa-|-Zaa-, except when Xaa is Arg or Lys, or Yaa or Zaa is Pro.
  • Also polymerizes dipeptide amides, arylamides and esters at neutral pH.
  • Cl(-)-dependent lysosomal cysteine-type peptidase.
  • Belongs to peptidase family C1.
  • Formerly EC 3.4.4.9.
 42 A0A061I6V3 A0A061I6V3 A0A061I819 A0A061I819 C1L6J5 C1L6J5 C1L6J6 C1L6J6 C1L6J7 C1L6J7
(32 more...)
Cathepsin X. [EC: 3.4.18.1]
Release of C-terminal amino acid residues with broad specificity, but lacks action on C-terminal proline. Shows weak endopeptidase activity.
  • Deamidates Z-Arg-NH(2), but shows no action on the arylamide derivatives.
  • Inhibited by thiol-blocking reagents.
  • Belongs to peptidase family C1.
 20 A0A0D2KVZ3 A0A0D2KVZ3 A0A0D2LDC0 A0A0D2LDC0 G0QL92 G0QL92 G0QL92 G0QL92 H2QKN8 H2QKN8
(10 more...)
Papain. [EC: 3.4.22.2]
Hydrolysis of proteins with broad specificity for peptide bonds, but preference for an amino acid bearing a large hydrophobic side chain at the P2 position. Does not accept Val in P1'.
  • From latex of the papaya (Carica papaya).
  • Inhibited by compound E-64 and proteins of the cystatin family.
  • Belongs to peptidase family C1.
  • Formerly EC 3.4.4.10.
 10 A0A1G4I6F7 A0A1G4I6F7 C9ZQ62 C9ZQ62 D6XHE1 D6XHE1 G0TW77 G0TW77 Q6R7Z5 Q6R7Z5
V-cath endopeptidase. [EC: 3.4.22.50]
Endopeptidase of broad specificity, hydrolyzing substrates of both cathepsin L and cathepsin B.
  • Contributes to the liquefaction of the tissues of the insect host in the late stages of infection by the baculovirus.
  • Belongs to peptidase family C1.
 4 G0QL92 G0QL92 G0QL92 G0QL92