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CATH Superfamily 2.40.10.10

Trypsin-like serine proteases

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:

"
Trypsin-like serine proteases
".

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 46106: Transmembrane protease serine 9

There are 7 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
Plasmin. [EC: 3.4.21.7]
Preferential cleavage: Lys-|-Xaa > Arg-|-Xaa; higher selectivity than trypsin. Converts fibrin into soluble products.
  • Formed from plasminogen by proteolysis which results in multiple forms of the active plasmin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.14.
 58 A0A087XAX0 A0A087XAX0 A0A096LUY1 A0A096LUY1 A0A0F8CNM7 A0A0F8CNM7 A0A0S7KT15 A0A0S7KT15 A0A146NKH6 A0A146NKH6
(48 more...)
Enteropeptidase. [EC: 3.4.21.9]
Activation of trypsinogen by selective cleavage of 6-Lys-|-Ile-7 bond.
  • Activates trypsinogen.
  • Not inhibited by protein inhibitors of trypsin.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.8.
 26 A0A061I686 A0A061I686 A0A096NE29 A0A096NE29 E6Y432 E6Y432 E9Q6Y6 E9Q6Y6 H2QKV6 H2QKV6
(16 more...)
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
 8 B7P3F4 B7P3F4 B7PKT9 B7PKT9 B7Q228 B7Q228 E0W195 E0W195
Coagulation factor XIIa. [EC: 3.4.21.38]
Selective cleavage of Arg-|-Ile bonds in factor VII to form factor VIIa and factor XI to form factor XIa.
  • Also activates plasma prekallikrein and plasminogen.
  • Formed from the proenzyme, factor XII, by plasma kallikrein or factor XIIa.
  • Belongs to peptidase family S1.
 4 A0A061IBV4 A0A061IBV4 A0A061IEF7 A0A061IEF7
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.
 4 P98139 P98139 Q804X7 Q804X7
Limulus clotting enzyme. [EC: 3.4.21.86]
Selective cleavage of 18-Arg-|- and 47-Arg-|- bonds in coagulogen to form coagulin and fragments.
  • From the hemocyte granules of the horseshoe crabs Limulus and Tachypleus.
  • Limulus clotting enzyme is activated by factor B.
  • Belongs to peptidase family S1.
 2 B7QDI9 B7QDI9
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.
 2 A0A061IR16 A0A061IR16
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