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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 79324: Striated muscle-specific serine/threonine-protein ...

There are 9 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.
 442 A0A026VV67 A0A026VV67 A0A034VCP3 A0A034VCP3 A0A061HVS4 A0A061HVS4 A0A087RAV3 A0A087RAV3 A0A087XC88 A0A087XC88
(432 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.
 94 A0A024RDL4 A0A024RDL4 A0A060RZR1 A0A060RZR1 A0A061I2T7 A0A061I2T7 A0A061I568 A0A061I568 A0A061I6E1 A0A061I6E1
(84 more...)
Calcium/calmodulin-dependent protein kinase. [EC: 2.7.11.17]
ATP + a protein = ADP + a phosphoprotein.
  • Requires calmodulin.
  • A wide range of proteins can act as acceptor, including vimentin, synapsin, glycogen synthase, myosin light-chains and the microtubule- associated tau protein.
  • Not identical with EC EC 2.7.11.18 or EC 2.7.11.26.
  • Formerly EC 2.7.1.120 and EC 2.7.1.123.
 64 A0A0A1UGV1 A0A0A1UGV1 A0A0D3G979 A0A0D3G979 A0A0E0A0Z7 A0A0E0A0Z7 A0A0E0HG62 A0A0E0HG62 A0A1J1H6C9 A0A1J1H6C9
(54 more...)
Phosphorylase kinase. [EC: 2.7.11.19]
2 ATP + phosphorylase b = 2 ADP + phosphorylase a.
  • Requires calmodulin for activity.
  • The enzyme phosphorylates a specific serine residue in each of the subunits of the dimeric phosphorylase b.
  • For muscle phosphorylase but not liver phosphorylase, this is accompanied by a further dimerization to form a tetrameric phosphorylase.
  • The enzyme couples muscle contraction with energy production via glycogenolysis--glycolysis by catalyzing the Ca(2+)-dependent phosphorylation and activation of glycogen phosphorylase b.
  • The gamma subunit of the tetrameric alpha-beta-gamma-delta enzyme is the catalytic subunit.
  • Formerly EC 2.7.1.38.
 50 A0A024RDL4 A0A024RDL4 A0A061IBZ2 A0A061IBZ2 A0A061ICX7 A0A061ICX7 A0A0P8XK87 A0A0P8XK87 A0A0P9BUP0 A0A0P9BUP0
(40 more...)
[Tau protein] kinase. [EC: 2.7.11.26]
ATP + [tau protein] = ADP + [tau protein] phosphate.
  • Activated by tubulin.
  • Involved in the formation of paired helical filaments, which are the main fibrous component of all fibrillary lesions in brain and are associated with Alzheimer's disease.
  • Formerly EC 2.7.1.135.
 10 A0A024RDL4 A0A024RDL4 P00518 P00518 P07934 P07934 P13286 P13286 Q16816 Q16816
[Myosin light-chain] kinase. [EC: 2.7.11.18]
ATP + [myosin light-chain] = ADP + [myosin light-chain] phosphate.
  • Requires calmodulin for activity.
  • The 20 kDa light chain from smooth muscle myosin is phosphorylated more rapidly than any other acceptor, but light chains from other myosins and myosin itself can act as acceptors, more slowly.
  • Formerly EC 2.7.1.117.
 2 Q54PB4 Q54PB4
Exodeoxyribonuclease V. [EC: 3.1.11.5]
Exonucleolytic cleavage (in the presence of ATP) in either 5'- to 3'- or 3'- to 5'-direction to yield 5'-phosphooligonucleotides.
  • Preference for double-stranded DNA.
  • Possesses DNA-dependent ATPase activity.
  • Acts endonucleolytically on single-stranded circular DNA.
  • Similar enzyme: Haemophilus influenzae ATP-dependent DNase.
 2 G0QXG5 G0QXG5
Cyclin-dependent kinase. [EC: 2.7.11.22]
ATP + a protein = ADP + a phosphoprotein.
  • Activation of cyclin-dependent kinases requires association of the enzyme with a regulatory subunit referred to as a cyclin.
  • It is the sequential activation and inactivation of cyclin-dependent kinases, through the periodic synthesis and destruction of cyclins, that provides the primary means of cell-cycle regulation.
  • Formerly EC 2.7.1.37.
 2 G0QKH9 G0QKH9
Dihydrolipoyllysine-residue (2-methylpropanoyl)transferase. [EC: 2.3.1.168]
2-methylpropanoyl-CoA + enzyme N(6)-(dihydrolipoyl)lysine = CoA + enzyme N(6)-(S-(2-methylpropanoyl)dihydrolipoyl)lysine.
  • A multimer (24-mer) of this enzyme forms the core of the multienzyme 3-methyl-2-oxobutanoate dehydrogenase complex, and binds tightly both EC 1.2.4.4 and EC 1.8.1.4.
  • The lipoyl group of this enzyme is reductively 2-methylpropanoylated by EC 1.2.4.4, and the only observed direction catalyzed by EC 2.3.1.168 is that where this 2-methylpropanoyl is passed to coenzyme A.
  • In addition to the 2-methylpropanoyl group, formed when EC 1.2.4.4 acts on the oxoacid that corresponds with valine, this enzyme also transfers the 3-methylbutanoyl and S-2-methylbutanoyl groups, donated to it when EC 1.2.4.4 acts on the oxo acids corresponding with leucine and isoleucine.
 2 B0ECW5 B0ECW5
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