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CATH Superfamily 2.30.29.30

Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)

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:

"
Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB)
".

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 22143: Dynamin 2, isoform CRA_b

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
Dynamin GTPase. [EC: 3.6.5.5]
GTP + H(2)O = GDP + phosphate.
  • An enzyme with a molecular mass of about 100 kDa that is involved in endocytosis and is instrumental in pinching off membrane vesicles.
  • Formerly EC 3.6.1.50.
 42 A0A061I6R1 A0A061I6R1 A0A061I7K3 A0A061I7K3 A0A0J9YUN4 A0A0J9YUN4 A4V4I8 A4V4I8 A6H7I5 A6H7I5
(32 more...)
Transferred entry: 3.6.5.5. [EC: 3.6.1.50]
    		4 Q6ZTU8 Q6ZTU8 Q6ZV85 Q6ZV85
    Protein-serine/threonine phosphatase. [EC: 3.1.3.16]
    [a protein]-serine/threonine phosphate + H(2)O = [a protein]- serine/threonine + phosphate.
    • A group of enzymes removing the serine- or threonine-bound phosphate group from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase (cf. EC 3.1.3.48).
    • The spleen enzyme also acts on phenolic phosphates and phosphamides (cf. EC 3.9.1.1).
    		 2 A0A1B0CY18 A0A1B0CY18
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