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CATH Superfamily 1.10.510.10

Transferase(Phosphotransferase) domain 1

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:

"
Transferase(Phosphotransferase) domain 1
".

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 231: Cyclin-dependent kinase 1

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
[RNA-polymerase]-subunit kinase. [EC: 2.7.11.23]
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
  • Appears to be distinct from other protein phosphokinases.
  • Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6.
  • Does not phosphorylate casein, phosvitin or histone.
  • Formerly EC 2.7.1.141.
 89 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A1L8FE96 A0A1L8FE96 A0A1U7QMR3 A0A1U7QMR3 A0A1U7QMR3
(79 more...)
Cyclin-dependent kinase. [EC: 2.7.11.22]
ATP + a protein = ADP + a phosphoprotein.
  • Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin.
  • It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
  • Formerly EC 2.7.1.37.
 89 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A0J9TKI8 A0A1L8FE96 A0A1L8FE96 A0A1U7QMR3 A0A1U7QMR3 A0A1U7QMR3
(79 more...)
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