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 78946: Myosin light chain kinase

There are 25 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
Non-specific serine/threonine protein kinase. [EC:]
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 and EC
1314 A0A024R603 A0A024R603 A0A024V5M2 A0A024V5M2 A0A024VC36 A0A024VC36 A0A024WUB6 A0A024WUB6 A0A024WVX3 A0A024WVX3
(1304 more...)
Calcium/calmodulin-dependent protein kinase. [EC:]
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 or EC
  • Formerly EC and EC
698 A0A024V1U2 A0A024V1U2 A0A024VLX3 A0A024VLX3 A0A024W1X5 A0A024W1X5 A0A024X2P8 A0A024X2P8 A0A060RNI8 A0A060RNI8
(688 more...)
[Myosin light-chain] kinase. [EC:]
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
158 A0A061I7J0 A0A061I7J0 A0A061I8P6 A0A061I8P6 A0A061I8Z4 A0A061I8Z4 A0A074SL66 A0A074SL66 A0A074SPH1 A0A074SPH1
(148 more...)
Receptor protein-tyrosine kinase. [EC:]
ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate.
  • The receptor protein-tyrosine kinases, which can be defined as having a transmembrane domain, are a large and diverse multigene family found only in metazoans.
  • In the human genome, 58 receptor-type protein-tyrosine kinases have been identified and these are distributed into 20 subfamilies.
  • Formerly EC
(16 more...)
DNA ligase (ATP). [EC:]
ATP + (deoxyribonucleotide)(n)-3'-hydroxyl + 5'-phospho- (deoxyribonucleotide)(m) = (deoxyribonucleotide)(n+m) + AMP + diphosphate.
  • The enzyme catalyzes the ligation of DNA strands with 3'-hydroxyl and 5'-phosphate termini, forming a phosphodiester and sealing certain types of single-strand breaks in duplex DNA.
  • Catalysis occurs by a three-step mechanism, starting with the activation of the enzyme by ATP, forming a phosphoramide bond between adenylate and a lysine residue.
  • The adenylate group is then transferred to the 5'-phosphate terminus of the substrate, forming the capped structure 5'-(5'-diphosphoadenosine)-(DNA).
  • Finally, the enzyme catalyzes a nucleophilic attack of the 3'-OH terminus on the capped terminus, which results in formation of the phosphodiester bond and release of the adenylate.
  • RNA can also act as substrate, to some extent.
  • Cf. EC, EC and EC
14 A0A0N5DP64 A0A0N5DP64 A0A0V0S790 A0A0V0S790 A0A0V0S7B2 A0A0V0S7B2 A0A0V0S7H3 A0A0V0S7H3 A0A0V0S7T0 A0A0V0S7T0
(4 more...)
Dual-specificity kinase. [EC:]
ATP + a protein = ADP + a phosphoprotein.
  • This family of enzymes can phosphorylate both Ser/Thr and Tyr residues.
  • Formerly EC
Glycylpeptide N-tetradecanoyltransferase. [EC:]
Tetradecanoyl-CoA + glycylpeptide = CoA + N-tetradecanoylglycylpeptide.
  • The enzyme from Saccharomyces cerevisiae is highly specific for tetradecanoyl-CoA, and for N-terminal glycine in oligopeptides containing serine in the 5-position.
  • The enzyme from mammalian heart transfers acyl groups to a specific acceptor protein of 51 kDa.
6 A0A0Q3PK66 A0A0Q3PK66 G0QMC4 G0QMC4 G0R3S7 G0R3S7
1-acylglycerophosphocholine O-acyltransferase. [EC:]
Acyl-CoA + 1-acyl-sn-glycero-3-phosphocholine = CoA + 1,2-diacyl- sn-glycero-3-phosphocholine.
  • Acts preferentially with unsaturated acyl-CoA derivatives.
  • 1-acyl-sn-glycero-3-phosphoinositol can also act as acceptor.
NAD(P)H oxidase (H(2)O(2)-forming). [EC:]
NAD(P)H + O(2) = NAD(P)(+) + H(2)O(2).
  • When calcium is present, this transmembrane glycoprotein generates H(2)O(2) by transfering electrons from intracellular NAD(P)H to extracellular molecular oxygen.
  • The electron bridge within the enzyme contains one molecule of FAD and probably two heme groups.
  • This flavoprotein is expressed at the apical membrane of thyrocytes, and provides H(2)O(2) for the thyroid peroxidase-catalyzed biosynthesis of thyroid hormones.
2-alkenal reductase (NAD(P)(+)). [EC:]
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
Mitogen-activated protein kinase. [EC:]
ATP + a protein = ADP + a phosphoprotein.
  • Phosphorylation of specific tyrosine and threonine residues in the activation loop of this enzyme by EC is necessary for enzyme activation.
  • Once activated, the enzyme phosphorylates target substrates on serine or threonine residues followed by a proline.
  • A distinguishing feature of all MAPKs is the conserved sequence Thr- Xaa-Tyr (TXY).
  • Mitogen-activated protein kinase (MAPK) signal transduction pathways are among the most widespread mechanisms of cellular regulation.
  • Mammalian MAPK pathways can be recruited by a wide variety of stimuli including hormones (e.g. insulin and growth hormone), mitogens (e.g. epidermal growth factor and platelet-derived growth factor), vasoactive peptides (e.g. angiotensin-II and endothelin), inflammatory cytokines of the tumor necrosis factor (TNF) family and environmental stresses such as osmotic shock, ionizing radiation and ischemeic injury.
  • Formerly EC
4 A0A182MX20 A0A182MX20 D8T5Z2 D8T5Z2
Deleted entry. [EC:]
    2 G0QWH8 G0QWH8
    NAD(P)H-hydrate epimerase. [EC:]
    (1) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide = (6S)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide. (2) (6R)-6-beta-hydroxy-1,4,5,6-tetrahydronicotinamide-adenine dinucleotide phosphate = (6S)-6-beta-hydroxy-1,4,5,6- tetrahydronicotinamide-adenine dinucleotide phosphate.
    • The enzyme can use either (R)-NADH-hydrate or (R)-NADPH-hydrate as a substrate.
    • Its physiological role is to convert the (R) forms to the (S) forms, which could then be restored to active dinucleotides by EC
    2 A0A1J7H833 A0A1J7H833
    Transferred entry:, and [EC:]
      2 G0QQZ4 G0QQZ4
      Transferred entry: [EC:]
        2 Q4UEA3 Q4UEA3
        Exodeoxyribonuclease V. [EC:]
        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 G0QQZ4 G0QQZ4
        Calpain-3. [EC:]
        Broad endopeptidase activity.
        • Activated by autoproteolytic cleavage of insertion sequence 1 (IS1), which allows substrates and inhibitors gain access to the active site.
        • Substrates include the protein itself and connectin/titin.
        • Belongs to peptidase family C2.
        2 G0QVX6 G0QVX6
        Peptidylprolyl isomerase. [EC:]
        Peptidylproline (omega=180) = peptidylproline (omega=0).
        • The first type of this enzyme found proved to be the protein cyclophilin, which binds the immunosuppressant cyclosporin A.
        • Other distinct families of the enzyme exist, one being FK-506 binding proteins (FKBP) and another that includes parvulin from Escherichia coli.
        • The three families are structurally unrelated and can be distinguished by being inhibited by cyclosporin A, FK-506 and 5-hydroxy-1,4-naphthoquinone, respectively.
        2 G0QJA9 G0QJA9
        Elongation factor 4. [EC: 3.6.5.n1]
        GTP + H(2)O = GDP + phosphate.
        • The enzyme is required for accurate and efficient protein synthesis under certain stress conditions.
        • May act as a fidelity factor of the translation reaction, by catalyzing a one-codon backward translocation of tRNAs on improperly translocated ribosomes.
        • Back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex, thus giving elongation factor G a second chance to translocate the tRNAs correctly.
        • Binds to ribosomes in a GTP-dependent manner.
        2 A0A151Z6W9 A0A151Z6W9
        Calpain-2. [EC:]
        Broad endopeptidase specificity.
        • Cytosolic in animal cells.
        • The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC
        • Belongs to peptidase family C2.
        • Formerly EC and EC
        2 G0QYQ5 G0QYQ5
        NADH:ubiquinone reductase (H(+)-translocating). [EC:]
        NADH + ubiquinone + 5 H(+)(In) = NAD(+) + ubiquinol + 4 H(+)(Out).
        • The complex is present in mitochondria and aerobic bacteria.
        • Breakdown of the complex can release EC
        • In photosynthetic bacteria, reversed electron transport through this enzyme can reduce NAD(+) to NADH.
        2 G0R1D6 G0R1D6
        Calpain-1. [EC:]
        Broad endopeptidase specificity.
        • Cytosolic in animal cells.
        • The active enzyme molecule is a heterodimer in which the large subunit contains the peptidase unit, and the small subunit is also a component of EC
        • Belongs to peptidase family C2.
        • Formerly EC and EC
        2 G0QW93 G0QW93
        Ferredoxin--NADP(+) reductase. [EC:]
        2 reduced ferredoxin + NADP(+) + H(+) = 2 oxidized ferredoxin + NADPH.
        • In chloroplasts and cyanobacteria the enzyme acts on plant-type [2Fe- 2S] ferredoxins, but in other bacteria it can also reduce bacterial 2[4Fe-4S] ferredoxins and flavodoxin.
        • Formerly EC and EC
        2 A0A1J7GX28 A0A1J7GX28
        Protein kinase C. [EC:]
        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 E0VY30 E0VY30
        Transketolase. [EC:]
        Sedoheptulose 7-phosphate + D-glyceraldehyde 3-phosphate = D-ribose 5-phosphate + D-xylulose 5-phosphate.
        • Wide specificity for both reactants, e.g. converts hydroxypyruvate and R-CHO into CO(2) and R-CHOH-CO-CH(2)OH.
        • The enzyme from the bacterium Alcaligenes faecalis shows high activity with D-erythrose 4-phosphate as acceptor.
        2 G0R2J9 G0R2J9