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 47558: Probable inactive serine protease 37

There are 3 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
Venombin A. [EC: 3.4.21.74]
Selective cleavage of Arg-|-Xaa bond in fibrinogen, to form fibrin, and release fibrinopeptide A. The specificity of further degradation of fibrinogen varies with species origin of the enzyme.
  • A somewhat thrombin-like enzyme from venoms of snakes of the viper/rattlesnake group.
  • Species variants of the enzyme include ancrod from Agkistrodon rhodostoma (Malayan pit viper), batroxobin from Bothrops atrox (South American pit viper) and crotalase from Crotalus adamanteus (Eastern diamondback rattlesnake).
  • Does not require activation by calcium.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.21.28, EC 3.4.21.29 and EC 3.4.21.30.
22 A0A0F7Z2N9 A0A0F7Z2N9 F8S114 F8S114 J3S3W5 J3S3W5 P04971 P04971 P05620 P05620
(12 more...)
Trypsin. [EC: 3.4.21.4]
Preferential cleavage: Arg-|-Xaa, Lys-|-Xaa.
  • Belongs to peptidase family S1.
  • Formerly EC 3.4.4.4.
10 A0A061IL07 A0A061IL07 A0A061IMT3 A0A061IMT3 P35030 P35030 Q6IE06 Q6IE06 Q8BW11 Q8BW11
Snake venom factor V activator. [EC: 3.4.21.95]
Fully activates human clotting factor V by a single cleavage at the 1545- Trp-Tyr-Leu-Arg-|-Ser-Asn-Asn-Gly-1552 bond. Cattle, but not rabbit, factor V is cleaved, and no other proteins of the clotting system are attacked. Esterase activity is observed on Bz-Arg-OEt and Tos-Arg-OMe, and amidase activity on Phe-pipecolyl-Arg-NHPhNO(2).
  • Inhibited by diisopropyl fluorophosphate.
  • Belongs to peptidase family S1.
6 P18964 P18964 P18965 P18965 Q9PT41 Q9PT41