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CATH Superfamily 3.30.70.80

Peptidase S8 propeptide/proteinase inhibitor I9

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:

"
Peptidase S8 propeptide/proteinase inhibitor I9
".

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 2822: Serine protease, subtilase family

There are 4 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
Subtilisin. [EC: 3.4.21.62]
Hydrolysis of proteins with broad specificity for peptide bonds, and a preference for a large uncharged residue in P1. Hydrolyzes peptide amides.
  • Subtilisin is a serine endopeptidase that evolved independently of chymotrypsin.
  • It contains no cysteine residues (although these are found in homologous enzymes).
  • Species variants include subtilisin BPN' (also subtilisin B, subtilopeptidase C, nagarse, nagarse proteinase, subtilisin Novo, bacterial proteinase Novo) and subtilisin Carlsberg (subtilisin A, subtilopeptidase A, alcalase Novo).
  • Similar enzymes are produced by various Bacillus subtilis strains and other Bacillus species.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16 and EC 3.4.21.14.
 69 A0A024B5D8 A0A024B5N4 A0A080UK04 A0A0A0THM5 A0A0A0TPQ7 A0A0E1LLD9 A0A0F7CA45 A0A0H3DZM5 A0A0K0HX88 A0A0K6KB79
(59 more...)
Transferred entry: 3.4.21.62, 3.4.21.63, 3.4.21.64, 3.4.21.65 and 3.4.21.67. [EC: 3.4.21.14]
    		4 A0A1L4AJA4 E3W705 E5LCP0 Q6IT79
    Pancreatic elastase. [EC: 3.4.21.36]
    Hydrolysis of proteins, including elastin. Preferential cleavage: Ala-|-Xaa.
    • Formed by activation of proelastase from mammalian pancreas by trypsin.
    • Belongs to peptidase family S1.
    • Formerly EC 3.4.4.7 and EC 3.4.21.11.
    		 2 G4Y092 H9CH13
    Neprilysin. [EC: 3.4.24.11]
    Preferential cleavage of polypeptides between hydrophobic residues, particularly with Phe or Tyr at P1'.
    • A membrane-bound glycoprotein widely distributed in animal tissues.
    • Inhibited by phosphoramidon and thiorphan.
    • Belongs to peptidase family M13.
    		 1 D9IXA7