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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_2_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 78995: cGMP-dependent protein kinase 2

There are 7 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
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.
 410 A0A016RXA8 A0A016RXD8 A0A016RXH8 A0A016RY62 A0A016RYF9 A0A023F5I7 A0A023VZ86 A0A026WC71 A0A026WUP7 A0A034VA88
(400 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.
 78 A0A023B0W2 A0A023B177 A0A023B252 A0A024W6S5 A0A024X7S0 A0A060RSZ6 A0A074T734 A0A074T7U8 A0A077TKA2 A0A077XAA0
(68 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.
 11 A0A0D2K243 A0A0F4YU22 A0A1N6LY18 A7AWS2 A7AWX2 E9QXD5 P16911 P21901 P34103 Q4MZK5
(1 more...)
Transferred entry: 2.7.11.1, 2.7.11.8, 2.7.11.9, 2.7.11.10, 2.7.11.11, 2.7.11.12, 2.7.11.13, 2.7.11.21, 2.7.11.22, 2.7.11.24, 2.7.11.25, 2.7.11.30 and 2.7.12.1. [EC: 2.7.1.37]
    		4 Q4UF82 Q695H0 Q869J9 Q869K0
    Lysophospholipase. [EC: 3.1.1.5]
    2-lysophosphatidylcholine + H(2)O = glycerophosphocholine + a carboxylate.
      		 1 G0R4B7
      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).
      		 1 A0A1I8C9M5
      Proteasome endopeptidase complex. [EC: 3.4.25.1]
      Cleavage of peptide bonds with very broad specificity.
      • A 20-S protein composed of 28 subunits arranged in four rings of seven.
      • The outer rings are composed of alpha subunits, but the beta subunits forming the inner rings are responsible for peptidase activity.
      • In eukaryotic organisms there are up to seven different types of beta subunits, three of which may carry the N-terminal threonine residues that are the nucleophiles in catalysis, and show different specificities.
      • The molecule is barrel-shaped, and the active sites are on the inner surfaces.
      • Terminal apertures restrict access of substrates to the active sites.
      • Inhibited by mercurial reagents and some inhibitors of serine endopeptidases.
      • Belongs to peptidase family T1.
      • Formerly EC 3.4.22.21, EC 3.4.24.5 and EC 3.4.99.46.
      		 1 G0QKE9
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