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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 45878: Coagulation factor X isoform 1

There are 6 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.
 29 A0A061IQ22 A0A061IQ22 A0A061IR16 A0A061IR16 A0N065 A6MFK7 A6MFK8 B5G6G5 H2Q7T9 O19045
(19 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.
 12 P08709 P22457 P70375 P98139 Q2F9P2 Q2F9P4 Q542C2 Q804X0 Q804X1 Q804X2
(2 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.
 11 A0A061HZH1 P00740 P00741 P16293 P16294 P16296 P19540 Q6SA95 Q804W8 Q804X6
(1 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.
 9 B7QMR1 P00745 P04070 P31394 P33587 Q28278 Q28661 Q804X5 Q9GLP2
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.
 2 A0A0P5CPS6 B7QMR1
Complement factor I. [EC: 3.4.21.45]
Inactivates complement subcomponents C3b, iC3b and C4b by proteolytic cleavage.
  • Cleavage of complement subcomponent C3b requires its binding to cofactor H or complement receptor CR1; cleavage of iC3b requires complement receptor CR1; cleavage of C4b requires C4b-binding protein.
  • Belongs to peptidase family S1.
 1 B7QMR1