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CATH Superfamily 3.30.200.20

Phosphorylase Kinase; domain 1

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:

"
Phosphorylase Kinase; 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 281: Ndr Ser/Thr kinase-like protein

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
Non-specific serine/threonine protein kinase. [EC: 2.7.11.1]
ATP + a protein = ADP + a phosphoprotein.
  • This is a heterogeneous group of serine/threonine protein kinases that do not have an activating compound and are either non-specific or their specificity has not been analyzed to date.
  • Formerly EC 2.7.1.37 and EC 2.7.1.70.
 94 A0A024RD18 A0A024RD18 A0A061IGF4 A0A061IGF4 A0A068WA44 A0A068WA44 A0A0B2P9H8 A0A0B2P9H8 A0A0B2PBR6 A0A0B2PBR6
(84 more...)
Protein kinase C. [EC: 2.7.11.13]
ATP + a protein = ADP + a phosphoprotein.
  • A family of serine- and threonine-specific protein kinases that depend on lipids for activity.
  • They can be activated by calcium but have a requirement for the second messenger diacylglycerol.
  • Members of this group of enzymes phosphorylate a wide variety of protein targets and are known to be involved in diverse cell- signaling pathways.
  • Members of the protein kinase C family also serve as major receptors for phorbol esters, a class of tumor promoters.
  • Formerly EC 2.7.1.37.
 18 A0A0B2PU18 A0A0B2PU18 B7PIM9 B7PIM9 B7QDT6 B7QDT6 B9R7B8 B9R7B8 B9RK53 B9RK53
(8 more...)
CAMP-dependent protein kinase. [EC: 2.7.11.11]
ATP + a protein = ADP + a phosphoprotein.
  • cAMP is required to activate this enzyme.
  • The inactive holoenzyme of cAMP-dependent protein kinase is a tetramer composed of two regulatory (R) and two catalytic (C) subunits.
  • cAMP causes the dissociation of the inactive holoenzyme into a dimer of regulatory subunits bound to four cAMP molecules and two free monomeric catalytic subunits (i.e. R(2)C(2) + 4 cAMP = R(2)(cAMP)(4) + 2 C).
  • Formerly EC 2.7.1.37.
 2 A0A0A1U5A6 A0A0A1U5A6
CGMP-dependent protein kinase. [EC: 2.7.11.12]
ATP + a protein = ADP + a phosphoprotein.
  • cGMP is required to activate this enzyme.
  • The enzyme occurs as a dimer in higher eukaryotes.
  • The C-terminal region of each polypeptide chain contains the catalytic domain that includes the ATP and protein substrate binding sites.
  • This domain catalyzes the phosphorylation by ATP to specific serine or threonine residues in protein substrates.
  • The enzyme also has two allosteric cGMP-binding sites (sites A and B).
  • Binding of cGMP causes a conformational change that is associated with activation of the kinase.
  • Formerly EC 2.7.1.37.
 2 A0A0A1U248 A0A0A1U248
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