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CATH Superfamily 1.10.840.10

Ras guanine-nucleotide exchange factors catalytic domain

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:

"
Ras guanine-nucleotide exchange factors catalytic domain
".

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 1407: Rap guanine nucleotide exchange factor 4

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.
 17 A0A0P8XRP5 A0A0P8XRR5 A0A0P8XRS6 A0A0P9AHI3 A0A0Q9W4T9 A0A0Q9W4Y7 A0A0Q9XEV3 A0A0R1DR09 A0A0R1DSS7 A0A0R1DT68
(7 more...)
Succinate dehydrogenase (quinone). [EC: 1.3.5.1]
Succinate + a quinone = fumarate + a quinol.
  • The enzyme is found in the inner mitochondrial membrane in eukaryotes and the plasma membrane of many aerobic or facultative bacteria.
  • It catalyzes succinate oxidation in the citric acid cycle and transfers the electrons to quinones in the membrane, thus constituting a part of the aerobic respiratory chain (known as complex II).
  • In vivo the enzyme uses the quinone found in the organism - eukaryotic enzymes utilize ubiquinone, bacterial enzymes utilize ubiquinone or menaquinone, and archaebacterial enzymes from the Sulfolobus genus use caldariellaquinone.
  • Cf. EC 1.3.5.4.
 1 A0A084VQP5
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.
 1 B7QN35
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