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CATH Superfamily 2.10.25.10

Laminin

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:

"
Laminin
".

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 45768: Neurogenic locus notch protein 1

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
Coagulation factor Xa. [EC: 3.4.21.6]
Selective cleavage of Arg-|-Thr and then Arg-|-Ile bonds in prothrombin to form thrombin.
  • A blood coagulation factor formed from the proenzyme factor X by limited proteolysis.
  • Factor X is a glycoprotein composed of a heavy chain and a light chain, which are generated from a precursor protein by the excision of the tripeptide RKR and held together by one or more disulfide bonds.
  • The activated factor Xa converts prothrombin to thrombin in the presence of factor Va, Ca(2+) and phospholipids.
  • Scutelarin (EC 3.4.21.60) has similar specificity, but does not require factor Va.
  • Belongs to peptidase family S1.
 78 A0A061IQ22 A0A061IQ22 A0A061IQ22 A0A061IQ22 A0A061IR16 A0A061IR16 A0A061IR16 A0A061IR16 A0N065 A0N065
(68 more...)
Coagulation factor VIIa. [EC: 3.4.21.21]
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
  • Formed from the precursor factor VII.
  • The cattle enzyme is more readily inhibited by diisopropyl fluorophosphate than the human.
  • Belongs to peptidase family S1.
 56 A0A1B1PFW7 A0A1B1PFW7 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11
(46 more...)
Coagulation factor IXa. [EC: 3.4.21.22]
Selective cleavage of Arg-|-Ile bond in factor X to form factor Xa.
  • The proenzyme factor IX is activated by EC 3.4.21.27.
  • Belongs to peptidase family S1.
 46 A0A061HZH1 A0A061HZH1 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11
(36 more...)
Receptor protein-tyrosine kinase. [EC: 2.7.10.1]
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
  • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
  • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
  • Formerly EC 2.7.1.112.
 32 B7PYC7 B7PYC7 B7PYC7 B7PYC7 B7PYC7 B7PYC7 B7Q438 B7Q438 B7Q438 B7Q438
(22 more...)
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 18 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5 E0VHU5
(8 more...)
Protein C (activated). [EC: 3.4.21.69]
Degradation of blood coagulation factors Va and VIIIa.
  • One of the gamma-carboxyglutamic acid-containing coagulation factors.
  • Formed from protein C, the proenzyme that circulates in plasma, by the action of a complex of thrombin with thrombomodulin, or by serine endopeptidases present in several snake venoms.
  • Belongs to peptidase family S1.
 18 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11
(8 more...)
Phospholipase A(2). [EC: 3.1.1.4]
Phosphatidylcholine + H(2)O = 1-acylglycerophosphocholine + a carboxylate.
  • Also acts on phosphatidylethanolamine, choline plasmalogen and phosphatides, removing the fatty acid attached to the 2-position.
 18 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11 B7PT11
(8 more...)
Limulus clotting factor C. [EC: 3.4.21.84]
Selective cleavage of 103-Arg-|-Ser-104 and 124-Ile-|-Ile-125 bonds in Limulus clotting factor B to form activated factor B. Cleavage of -Pro- Arg-|-Xaa- bonds in synthetic substrates.
  • From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus.
  • Factor C is activated by Gram-negative bacterial lipopolysaccharides and chymotrypsin.
  • Inhibited by antithrombin III.
  • Belongs to peptidase family S1.
 6 B7Q438 B7Q438 B7Q438 B7Q438 B7Q438 B7Q438
Alcohol dehydrogenase. [EC: 1.1.1.1]
(1) An alcohol + NAD(+) = an aldehyde or ketone + NADH. (2) A secondary alcohol + NAD(+) = a ketone + NADH.
  • Acts on primary or secondary alcohols or hemi-acetals with very broad specificity; however the enzyme oxidizes methanol much more poorly than ethanol.
  • The animal, but not the yeast, enzyme acts also on cyclic secondary alcohols.
 2 E0VDI8 E0VDI8
Procollagen C-endopeptidase. [EC: 3.4.24.19]
Cleavage of the C-terminal propeptide at Ala-|-Asp in type I and II procollagens and at Arg-|-Asp in type III.
  • The activity is increased by calcium and by an enhancer glycoprotein.
 2 E0VD28 E0VD28
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