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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 10202: Alkaline serine protease Alp1

There are 9 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
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.
 54 A0A075UR29 A0A075V0K3 A0A084FWX1 A0A084G2A1 A0A084G9F4 A0A089X196 A0A099KVU4 A0A0M9AFU5 A0A0N0N2B9 A0A0N0NH05
(44 more...)
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.
 25 A0A084FW16 A0A084FWX1 A0A084G077 A0A084G2A1 A0A084G9F4 A0A084G9J0 A0A084GDZ9 A0A0D9MQC0 A0A0F8B185 A0A0F8D9T1
(15 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.
 12 A0A084GDZ9 A0A0F6N3V8 A0A1D8NQQ9 A2QTZ2 A4FQG6 B3PIU6 D1MGZ7 F9XA84 P09230 T2AT09
(2 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.
 11 A0A084FW16 A0A084FWX1 A0A084G9F4 A0A0D2KJ52 A0A0F4YZ35 A3LY46 B7XHI1 B8MD40 B9WJU6 P09232
(1 more...)
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.
 7 A0A084FWX1 A0A084G2A1 A0A084G9F4 D7CWJ6 J7LFA2 P06873 S2DAU2
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
    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
    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.
    		 1 G0B138
    Aminopeptidase Y. [EC: 3.4.11.15]
    Preferentially, release of N-terminal lysine.
    • Inhibited by Zn(2+) and Mn(2+).
    • Hydrolyzes L-lysyl-4-nitroanilide and, more slowly, L-arginyl-4- nitroanilide.
    • Belongs to peptidase family M28B.
    		 1 A0A0H5CTQ3