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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 46566: Coagulation factor XII (Hageman factor)

There are 4 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.
 74 A0A096NZY9 A0A096NZY9 A0A0D9RIP2 A0A0D9RIP2 A0A0F7G8J1 A0A0F7G8J1 A0A0K2A1W0 A0A0K2A1W0 A0A1A6HIS2 A0A1A6HIS2
(64 more...)
Hepsin. [EC: 3.4.21.106]
Cleavage after basic amino-acid residues, with Arg strongly preferred to Lys.
  • This type-II membrane-associated serine peptidase has been implicated in cell growth and development.
  • The enzyme has been shown to activate blood coagulation factor VII by cleavage of the 152-Arg-|-Ile-153 peptide bound in BHK cells, thus indicating a possible role in the initiation of blood coagulation.
  • There is no cleavage after aromatic or aliphatic residues.
  • The occupancy of the S2 site is an absolute requirement for catalysis and a basic residue at that site is preferred to an aliphatic residue.
  • The nature of the residue at S3 also affects hydrolysis, with Gln being much more favorable than Ala.
  • Belongs to peptidase family S1A.
 14 A0A061HUY7 A0A061HUY7 A0A140VJK9 A0A140VJK9 H2QG15 H2QG15 O35453 O35453 P05981 P05981
(4 more...)
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.
 2 P00748 P00748
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
 2 E0VJE5 E0VJE5
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