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CATH Superfamily 2.60.120.380

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: waiting to be named.

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 4706: Extracellular alkaline serine protease

There are 10 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
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.
 41 A0A090RWN3 A0A090SDP2 A0A090T886 A0A0C5VQV5 A0A0E4GFE9 A0A0H3Q5R3 A0A0H6PJE6 A0A0K9UW80 A0A0M8KIQ3 A0A0M9UGM3
(31 more...)
Bacterial leucyl aminopeptidase. [EC: 3.4.11.10]
Release of an N-terminal amino acid, preferentially leucine, but not glutamic or aspartic acids.
  • Similar aminopeptidases were isolated from Escherichia coli and Staphylococcus thermophilus.
  • Belongs to peptidase families M17 and M28.
 23 A0A085T813 A0A090IM73 A0A0E4GLE9 A0A0H3AGS2 A0A0H3Q5M6 A0A0H5T5B1 A0A0H6H2R3 A0A0H6MIT1 A0A0H6RYR3 A0A0H6V758
(13 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 A0A0P9FW33 A0A0P9FW33 A0A0Q0HIK9 A0A1E7DAL9 F6M7Z3 F6M7Z3 G0JYK7 Q480E3 Q480E3 Q488L4
(2 more...)
Pseudolysin. [EC: 3.4.24.26]
Hydrolysis of proteins including elastin, collagen types III and IV, fibronectin and immunoglobulin A, generally with bulky hydrophobic group at P1'. Insulin B chain cleavage pattern identical to that of thermolysin, but specificity differs in other respects.
  • Causes tissue damage.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 6 A0A090RWN3 A0A090SDP2 A0A090T886 A0A0C5VQV5 A0A0E4GFE9 L8D6C5
Leucyl aminopeptidase. [EC: 3.4.11.1]
Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low.
  • Is activated by heavy metal ions.
  • Belongs to peptidase family M17.
  • Formerly EC 3.4.1.1.
 6 A0A0H3Q5M6 A0A0H5T5B1 A0A0K9UYR3 A0A0X1L0N9 C3LW77 Q9KLD3
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.
 3 A0A099L7S2 A0A099L7S2 Q60106
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.
 2 G0B138 G0B138
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.
 2 A0A099L7S2 A0A099L7S2
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.
 1 A0A0K0LBG2
Microbial collagenase. [EC: 3.4.24.3]
Digestion of native collagen in the triple helical region at Xaa-|-Gly bonds. With synthetic peptides, a preference is shown for Gly at P3 and P1'; Pro and Ala at P2 and P2'; and hydroxyproline, Ala or Arg at P3'.
  • Six species of metalloendopeptidase acting on native collagen can be isolated from the medium of Clostridium histolyticum.
  • Class I has forms alpha (68 kDa), beta (115 kDa) and gamma (79 kDa); class II has delta (100 kDa), epsilon (110 kDa) and zeta (125 kDa).
  • The two classes are immunologically crossreactive, but have significantly different sequences, and different specificities such that their actions on collagen are complementary.
  • The enzymes also act as peptidyl-tripeptidases.
  • Variants of the enzyme have been purified from Bacillus cereus, Empedobacter collagenolyticum, Pseudomonas marinoglutinosa, and species of Vibrio, Vibrio B-30 (ATCC 21250) and V.alginolyticus (previously Achromobacter iophagus).
  • Also known from Streptomyces sp.
  • Belongs to peptidase family M9.
  • Formerly EC 3.4.4.19, EC 3.4.24.8 and EC 3.4.99.5.
 1 L8D8B4