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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_3_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 5: cAMP-dependent protein kinase catalytic subunit

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
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.
 335 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0 A0A024R7J0
(325 more...)
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.
 119 A0A140VJM3 A0A140VJM3 A0A140VJM3 A0A140VJM3 A0A140VJM3 A0A2I2YA88 A0A2I2YA88 A0A2I2YA88 A0A2I2YA88 A0A2I2YA88
(109 more...)
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.
 10 A0A024R177 A0A024R177 A0A024RBU5 A0A024RBU5 O43930 O43930 P16912 P51817 P51817 Q922R0
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