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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 78738: Non-specific serine/threonine protein kinase

There are 6 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
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.
 108 A0A034WNK9 A0A034WNK9 A0A088ALM0 A0A088ALM0 A0A094LCL8 A0A094LCL8 A0A0A1WL53 A0A0A1WL53 A0A0A1XQ29 A0A0A1XQ29
(98 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.
 106 A0A024R6N2 A0A024R6N2 A0A061HTY7 A0A061HTY7 A0A061HYW8 A0A061HYW8 A0A061I1R3 A0A061I1R3 A0A061I429 A0A061I429
(96 more...)
2-alkenal reductase (NAD(P)(+)). [EC: 1.3.1.74]
A n-alkanal + NAD(P)(+) = an alk-2-enal + NAD(P)H.
  • Highly specific for 4-hydroxynon-2-enal and non-2-enal.
  • Alk-2-enals of shorter chain have lower affinities.
  • Exhibits high activities also for alk-2-enones such as but-3-en-2-one and pent-3-en-2-one.
  • Inactive with cyclohex-2-en-1-one and 12-oxophytodienoic acid.
  • Involved in the detoxification of alpha,beta-unsaturated aldehydes and ketones (cf. EC 1.3.1.102).
 4 B7Q4S9 B7Q4S9 E0W264 E0W264
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 G0QM88 G0QM88
H(+)-transporting two-sector ATPase. [EC: 3.6.3.14]
ATP + H(2)O + H(+)(In) = ADP + phosphate + H(+)(Out).
  • A multisubunit non-phosphorylated ATPase that is involved in the transport of ions.
  • Large enzymes of mitochondria, chloroplasts and bacteria with a membrane sector (F(o), V(o), A(o)) and a cytoplasmic-compartment sector (F(1), V(1), A(1)).
  • The F-type enzymes of the inner mitochondrial and thylakoid membranes act as ATP synthases.
  • All of the enzymes included here operate in a rotational mode, where the extramembrane sector (containing 3 alpha- and 3 beta-subunits) is connected via the delta-subunit to the membrane sector by several smaller subunits.
  • Within this complex, the gamma- and epsilon-subunits, as well as the 9-12 c subunits rotate by consecutive 120 degree angles and perform parts of ATP synthesis.
  • This movement is driven by the H(+) electrochemical potential gradient.
  • The V-type (in vacuoles and clathrin-coated vesicles) and A-type (archaeal) enzymes have a similar structure but, under physiological conditions, they pump H(+) rather than synthesize ATP.
  • Formerly EC 3.6.1.34.
 2 G0QM88 G0QM88
UMP/CMP kinase. [EC: 2.7.4.14]
(1) ATP + (d)CMP = ADP + (d)CDP. (2) ATP + UMP = ADP + UDP.
  • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
  • dCMP can also act as acceptor.
  • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25, CMP kinase and EC 2.7.4.22, UMP kinase.
  • This eukaryotic enzyme is a bifunctional enzyme that catalyzes the phosphorylation of both CMP and UMP with similar efficiency.
  • dCMP can also act as acceptor.
  • Different from the monofunctional prokaryotic enzymes EC 2.7.4.25 and EC 2.7.4.22.
  • Formerly EC 2.7.4.5.
 2 A0A0B2RKP9 A0A0B2RKP9