View in Gene3D

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.
« Back to all FunFams

FunFam 10257: Membrane-bound transcription factor site-1 proteas...

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
Tripeptidyl-peptidase II. [EC: 3.4.14.10]
Release of an N-terminal tripeptide from a polypeptide.
  • A cytosolic enzyme active at neutral pH.
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.14.8.
 52 A0A061IER6 A0A061IER6 A0A061ILE9 A0A061ILE9 A0A0B2QPH0 A0A0B2QPH0 A0A0B2S8E2 A0A0B2S8E2 A0A0D9RY25 A0A0D9RY25
(42 more...)
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.
 12 A0A061IER9 A0A061IER9 G4VKD8 G4VKD8 Q14703 Q14703 Q9WTZ2 Q9WTZ2 Q9WTZ3 Q9WTZ3
(2 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.
 4 B9RKQ2 B9RKQ2 E0VQL9 E0VQL9