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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 10223: Extracellular alkaline serine protease

There are 12 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.
 414 A0A024B5D8 A0A024B5D8 A0A024B5N4 A0A024B5N4 A0A062V4N2 A0A062V4N2 A0A062VA58 A0A062VA58 A0A068N5T9 A0A068N5T9
(404 more...)
Thermitase. [EC: 3.4.21.66]
Hydrolysis of proteins, including collagen.
  • From Thermoactinomyces vulgaris containing a single Cys, near the active site His, and inhibited by p-mercuribenzoate.
  • The N-terminal extension of the polypeptide chain relative to subtilisin contributes to calcium-binding and the high thermostability.
  • The amino acid composition and properties of the thermostable enzyme from Streptomyces rectus var. proteolyticus are closely similar.
  • Belongs to peptidase family S8.
  • Formerly EC 3.4.4.16.
 190 A0A091A1E8 A0A091A1E8 A0A099L7S2 A0A099L7S2 A0A0A3VVT9 A0A0A3VVT9 A0A0B5NDQ4 A0A0B5NDQ4 A0A0D1NWU9 A0A0D1NWU9
(180 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]
    		10 A0A1L4AJA4 A0A1L4AJA4 E3W705 E3W705 E5LCP0 E5LCP0 Q56700 Q56700 Q6IT79 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.
    		 4 G4Y092 G4Y092 H9CH13 H9CH13
    Lactocepin. [EC: 3.4.21.96]
    Endopeptidase activity with very broad specificity, although some subsite preference have been noted, e.g. large hydrophobic residues in the P1 and P4 positions, and Pro in the P2 position. Best known for its action on caseins, although it has been shown to hydrolyze hemoglobin and oxidized insulin B-chain.
    • Responsible for the hydrolysis of casein in milk and the provision of peptides essential for cell growth.
    • Specificity differences between lactocepins from different starter strains may be partly responsible for imparating different flavor qualities to cheese.
    • Belongs to peptidase family S8.
    		 4 A0A0K6LSQ7 A0A0K6LSQ7 A0A0U0C460 A0A0U0C460
    Xanthomonalisin. [EC: 3.4.21.101]
    Cleavage of casein.
    • Secreted by the bacterium Xanthomonas sp.
    • Belongs to peptidase family S53.
    • Formerly EC 3.4.23.33.
    		 2 A0A099L7S2 A0A099L7S2
    Glutamyl endopeptidase. [EC: 3.4.21.19]
    Preferential cleavage: Glu-|-Xaa, Asp-|-Xaa.
    • In appropriate buffer the specificity is restricted to Glu-|-Xaa.
    • Bonds involving bulky side-chains of hydrophobic amino acids are cleaved at a lower rate.
    • Belongs to peptidase family S1B.
    		 2 S5VEF0 S5VEF0
    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.
    		 2 D9IXA7 D9IXA7
    Furin. [EC: 3.4.21.75]
    Release of mature proteins from their proproteins by cleavage of -Arg- Xaa-Yaa-Arg-|-Zaa- bonds, where Xaa can be any amino acid and Yaa is Arg or Lys. Releases albumin, complement component C3 and von Willebrand factor from their respective precursors.
    • Activated by calcium.
    • Belongs to peptidase family S8.
    		 2 C0QHY8 C0QHY8
    Lysyl endopeptidase. [EC: 3.4.21.50]
    Preferential cleavage: Lys-|-Xaa, including Lys-|-Pro.
    • Isolated from Achromobacter lyticus.
    • Enzymes with similar specificity are produced by Lysobacter enzymogenes (endoproteinase Lys-C) and Pseudomonas aeruginosa (Ps-1).
    • Belongs to peptidase family S1.
    		 2 A0A0S2F552 A0A0S2F552
    Methionine adenosyltransferase. [EC: 2.5.1.6]
    ATP + L-methionine + H(2)O = phosphate + diphosphate + S-adenosyl-L- methionine.
    • Formerly EC 2.4.2.13.
    		 2 A0A0C2RY34 A0A0C2RY34
    Vibriolysin. [EC: 3.4.24.25]
    Preferential cleavage of bonds with bulky hydrophobic groups in P2 and P1'. Phe at P1' is the most favored residue, which distinguished this enzyme from thermolysin.
    • Thermostable enzyme from Vibrio proteolyticus (formerly Aeromonas proteolytica).
    • Specificity related to, but distinct from, those of the thermolysin and Bacillus subtilis endopeptidase.
    • Belongs to peptidase family M4.
    • Formerly EC 3.4.24.4.
    		 2 G0JYK7 G0JYK7