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CATH Superfamily 3.40.50.200

Peptidase S8/S53 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:

"
Peptidase S8/S53 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.
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FunFam 10195: 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
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.
 18 A0A099KJE8 A0A099KJE8 A0A099KKQ8 A0A099KKQ8 B9RC06 B9RC06 B9S3C2 B9S3C2 B9SE30 B9SE30
(8 more...)
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.
 8 A0A151QQD5 A0A151QQD5 A0A151RCR7 A0A151RCR7 A0A151RCR7 A0A151RCR7 A0A151RD84 A0A151RD84
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 4 B9RDI2 B9RDI2 B9T5M7 B9T5M7
Site-1 protease. [EC: 3.4.21.112]
Processes precursors containing basic and hydrophobic/aliphatic residues at P4 and P2, respectively, with a relatively relaxed acceptance of amino acids at P1 and P3.
  • Cleaves sterol regulatory element-binding proteins (SREBPs) and thereby initiates a process by which the active fragments of the SREBPs translocate to the nucleus and activate genes controlling the synthesis and uptake of cholesterol and unsaturated fatty acids into the bloodstream.
  • The enzyme also processes pro-brain-derived neurotrophic factor and undergoes autocatalytic activation in the endoplasmic reticulum through sequential cleavages.
  • The enzyme can also process the unfolded protein response stress factor ATF6 at an Arg-His-Lys-Lys-|- site, and the envelope glycoprotein of the highly infectious Lassa virus and Crimean Congo hemorrhagic fever virus at Arg-Arg-Lys-Lys-|-.
  • Belongs to peptidase family S8A.
 2 A0A0B2RC14 A0A0B2RC14