The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Mannose-Binding Protein A, subunit A
".

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

There are 2 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
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.
2 P28175 Q26422
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.
1 Q9C823