View in Gene3D

CATH Superfamily 3.40.390.10

Collagenase (Catalytic Domain)

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:

"
Collagenase (Catalytic 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.
« Back to all FunFams

FunFam 13317: Neutral protease 2 homolog AN7962

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
Deuterolysin. [EC: 3.4.24.39]
Preferential cleavage of bonds with hydrophobic residues in P1'; also 3-Asn-|-Gln-4 and 8-Gly-|-Ser-9 bonds in insulin B chain.
  • Proteolytic activity found in Penicillium roqueforti, P.caseicolum, Aspergillus sojae and A.oryzae.
  • Optimum pH of 5 for digesting various proteins.
  • Strong action on protamine and histones.
  • Insensitive to phosphoramidon.
  • A distinct A.sojae endopeptidase is larger and has neutral pH optimum.
  • Belongs to peptidase family M35.
  • Formerly EC 3.4.24.4.
 495 A0A010R8L4 A0A010RHC3 A0A010RHV4 A0A010S3Z0 A0A010S7E9 A0A014QV51 A0A022VMB1 A0A022VQ39 A0A022VWU8 A0A022VXR0
(485 more...)
Peptidyl-Lys metalloendopeptidase. [EC: 3.4.24.20]
Preferential cleavage in proteins: -Xaa-|-Lys- (in which Xaa may be Pro).
  • From the honey fungus Armillaria mellea.
  • A similar specificity is shown by Myxobacter sp. AL-1 proteinase II (endoproteinase Lys-C).
  • Formerly EC 3.4.99.30 and EC 3.4.99.32.
 36 A0A077SD93 A0A0B4LCF0 A0A0B7F0Q3 A0A0B7F1B4 A0A0B7F2U4 A0A0B7F3S8 A0A0B7F5Y0 A0A0B7FPR2 A0A0B7FQI5 A0A0B7FU75
(26 more...)
Cellulase. [EC: 3.2.1.4]
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
  • Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
 1 A0A136KTG5