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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 2813: Alkaline serine protease Alp1

There are 7 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
Oryzin. [EC: 3.4.21.63]
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
  • Predominant extracellular alkaline endopeptidase of the mold Aspergillus oryzae.
  • Identical or closely related enzymes are produced by A.flavus and A.sojae.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16, EC 3.4.21.14 and EC 3.4.21.15.
 24 A0A084FW16 A0A084G077 A0A084G2A1 A0A084G9F4 A0A084G9J0 A0A084GDZ9 A0A0D9MQC0 A0A0F8B185 A0A0F8D9T1 A0A0J5PVB2
(14 more...)
Cerevisin. [EC: 3.4.21.48]
Hydrolysis of proteins with broad specificity, and of Bz-Arg-OEt > Ac-Tyr-OEt. Does not hydrolyze peptide amides.
  • Contains a Cys residue near the active site His, and is inhibited by mercurials.
  • Proteinase ycaB is a similar enzyme from the yeast Candida albicans.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.22.9.
 8 A0A084FW16 A0A084G9F4 A0A0F4YZ35 A3LY46 B8MD40 B9WJU6 P09232 W1QEH5
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.
 6 A0A084GDZ9 A0A0F6N3V8 A0A1D8NQQ9 A2QTZ2 P09230 V5NDN0
Aqualysin 1. [EC: 3.4.21.111]
Exhibits low specificity toward esters of amino acids with small hydrophobic or aromatic residues at the P1 position.
  • This enzyme from the extreme thermophile, Thermus aquaticus, is an alkaline serine peptidase.
  • It has three subsites, S1, S2, and S3, in the substrate binding site.
  • The preferred amino acids at the S1 site are Ala and Phe, at the S2 site are Ala and norleucine and at the S3 site are Phe and Ile.
  • These specificities are similar to those of EC 3.4.21.62 and EC 3.4.21.64.
  • The enzyme displays broad specificity for cleavage of insulin B-chain and hydrolyzes elastin substrates such as succinyl-(Ala)(n)-p- nitroanilide (n = 1,2,3) and some peptide esters.
  • Belongs to peptidase family S8A.
 4 A0A084G2A1 A0A084G9F4 A0A0M9AFU5 P08594
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]
    		2 G3XMS1 Q00206
    Peptidase K. [EC: 3.4.21.64]
    Hydrolysis of keratin, and of other proteins with subtilisin-like specificity. Hydrolyzes peptide amides.
    • From the mold Tritirachium album Limber.
    • Contains two disulfide bridges and one free Cys near the active site His.
    • Belongs to peptidase family S8.
    • Formerly EC 3.4.4.16 and EC 3.4.21.14.
    		 2 A0A084G2A1 A0A084G9F4
    Cucumisin. [EC: 3.4.21.25]
    Hydrolysis of proteins with broad specificity.
    • From the sarcocarp of the musk melon (Cucumis melo).
    • Other endopeptidases from plants, which are less well characterized but presumably of serine-type, include euphorbain from Euphorbia cerifera, solanain from horse-nettle Solanum elaeagnifolium, hurain from Hura crepitans and tabernamontanain from Tabernamontana grandiflora.
    • Belongs to peptidase family S8.
    		 1 A0A084G9F4