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CATH Superfamily 2.60.40.10

Immunoglobulins

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:

"
Immunoglobulins
".

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 7557: PKD domain containing protein

There are 14 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
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.
 336 A0A066YLV7 A0A066YLV7 A0A068N9S8 A0A068N9S8 A0A068N9W1 A0A068N9W1 A0A075R1Q2 A0A075R1Q2 A0A099KWG1 A0A099KWG1
(326 more...)
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.
 58 A0A0D8I4L5 A0A0D8I4L5 A0A0F0KEH0 A0A0F0KEH0 A0A0F0KEH0 A0A0F0KEH0 A0A0F0KQA5 A0A0F0KQA5 A0A0F2C6Q6 A0A0F2C6Q6
(48 more...)
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.
 30 A0A099K9R4 A0A099K9R4 A0A099KB29 A0A099KB29 A0A099KB29 A0A099KB29 A0A099KY20 A0A099KY20 A0A099KY20 A0A099KY20
(20 more...)
Chitinase. [EC: 3.2.1.14]
Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta- linkages in chitin and chitodextrins.
  • The enzyme binds to chitin and randomly cleaves glycosidic linkages in chitin and chitodextrins in a non-processive mode, generating chitooligosaccharides and free ends on which exo-chitinases and exo- chitodextrinases can act.
  • Activity is greatly stimulated in the presence of EC 1.14.99.53, which attacks the crystalline structure of chitin and makes the polymer more accesible to the chitinase.
  • Cf. EC 3.2.1.202.
 26 A0A0K3AVN8 A0A0K3AVN8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8 A0A1B1NEB8
(16 more...)
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.
 26 A0A099L3G1 A0A099L3G1 A0A0C5WZ32 A0A0C5WZ32 A0A108UCW8 A0A108UCW8 A0A108UD33 A0A108UD33 A0A108UD65 A0A108UD65
(16 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.
 16 A0A099K9R4 A0A099K9R4 A0A099KWG1 A0A099KWG1 A0A099KWG1 A0A099KWG1 A0A099L2J5 A0A099L2J5 A0A099LGK9 A0A099LGK9
(6 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.
 8 A0A108UCW8 A0A108UCW8 A0A108UD33 A0A108UD33 A0A108UD65 A0A108UD65 A0A108UDN9 A0A108UDN9
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
 8 A0A099KB29 A0A099KB29 A0A099KB29 A0A099KB29 A0A0P9FPX5 A0A0P9FPX5 A0A0P9FPX5 A0A0P9FPX5
Carboxypeptidase A. [EC: 3.4.17.1]
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro.
  • Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells and skeletal muscle.
  • Belongs to peptidase family M14.
  • Formerly EC 3.4.2.1 and EC 3.4.12.2.
 6 A0A099KY20 A0A099KY20 A0A099KY20 A0A099KY20 A0A099KY20 A0A099KY20
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.
 6 A0A128FGU9 A0A128FGU9 A0A128FGU9 A0A128FGU9 A1SB60 A1SB60
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.
 4 A0A099L7S2 A0A099L7S2 A0A099L7S2 A0A099L7S2
Alkaline phosphatase. [EC: 3.1.3.1]
A phosphate monoester + H(2)O = an alcohol + phosphate.
  • Active at a high pH optimum.
  • Wide specificity.
  • Also catalyzes transphosphorylations.
  • Some enzymes hydrolyze diphosphate (cf. EC 3.6.1.1).
 4 A0A0S2FDC0 A0A0S2FDC0 A0A0S2FDC0 A0A0S2FDC0
Cellulase. [EC: 3.2.1.4]
Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.
  • Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages.
 2 G2FE53 G2FE53
Licheninase. [EC: 3.2.1.73]
Hydrolysis of (1->4)-beta-D-glucosidic linkages in beta-D-glucans containing (1->3)- and (1->4)-bonds.
  • Acts on lichenin and cereal beta-D-glucans, but not on beta-D-glucans containing only 1,3- or 1,4-bonds.
 2 A0A1C9W7N6 A0A1C9W7N6
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