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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 10269: Serine protease, subtilase family

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
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.
 168 A0A045IZ89 A0A045IZ89 A0A083W9F7 A0A083W9F7 A0A087AYR0 A0A087AYR0 A0A0D6HAC9 A0A0D6HAC9 A0A0D6JKP3 A0A0D6JKP3
(158 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.
 16 A0A099KMG7 A0A099KMG7 A0A0E2Z4Y7 A0A0E2Z4Y7 A0A0G3Y3E5 A0A0G3Y3E5 A0A1B1LGC7 A0A1B1LGC7 F4L0Y2 F4L0Y2
(6 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.
 2 D2Q5F6 D2Q5F6
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