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CATH Superfamily 2.60.120.260

Galactose-binding domain-like

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:

"
Galactose-binding domain-like
".

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 35732: Basic extracellular subtilisin-like protease BprV

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.
 10 A0A0S2DHJ1 A0A0S2FAR0 A0A0S2FRD5 A0A0S2G793 A0A108U531 A0A108U539 A0A108UCW8 A0A108UD33 A0A108UD65 A0A108UDN9
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.
 9 A0A0S2DKV3 A0A0S2DKZ5 A0A0S2FUB3 A0A0S2FUU3 A0A0S2GAA1 A0A0S2GAG5 Q8GQZ0 Q9AQR5 W0C3W2
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.
 7 A0A0S2FRD5 A0A108U531 A0A108U539 A0A108UCW8 A0A108UD33 A0A108UD65 A0A108UDN9
Aminopeptidase S. [EC: 3.4.11.24]
Release of an N-terminal amino acid with a preference for large hydrophobic amino-terminus residues.
  • Activated by Ca(2+).
  • In the presence of Ca(2+), the best substrates are Leu-Phe, Leu-Ser, Leu-pNA (aminoacyl-p-nitroanilide), Phe-Phe-Phe and Phe-Phe.
  • Peptides with proline in the P1' position are not substrates.
  • Belongs to peptidase family M28.
  • Formerly EC 3.4.11.n1.
 7 A0A1C4LTM5 A0A1C4PWH8 E8W5Q7 G0Q6B0 G2NAM7 N0CT05 P80561
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.
 5 A0A0K3AU42 A0A1J0UU30 F2RIL8 M9TSW3 N0CT05
Thermolysin. [EC: 3.4.24.27]
Preferential cleavage: Xaa-|-Leu > Xaa-|-Phe.
  • A thermostable extracellular metalloendopeptidase containing four calcium ions.
  • Enzymes that may be species variants of thermolysin are reported from Micrococcus caseolyticus and Aspergillus oryzae.
  • Closely related but distinct enzymes are aeromonolysin, pseudolysin, bacillolysin, aureolysin and mycolysin.
  • Belongs to peptidase family M4.
  • Formerly EC 3.4.24.4.
 5 A0A0N0MXQ2 A0A0N0NDA0 A0A0N1GEL7 A0A0N1NN82 G0Q5P5
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.
 4 A0A1C4NAB6 B1W2C4 G0PR03 G0Q2F3
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.
 2 A0A108UD21 A0A108UD55
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.
 2 Q8ECN0 T2AT09
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.
 1 A0A108UD57
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