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CATH Superfamily 1.10.472.10

Cyclin-like

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:

"
Cyclin-like
".

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 9852: G2/mitotic-specific cyclin F variant

There are 10 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
NAD(+) ADP-ribosyltransferase. [EC: 2.4.2.30]
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.
  • The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
 6 A0A195ET12 A0A195ET12 E2B9H6 E2B9H6 F4W5N2 F4W5N2
[RNA-polymerase]-subunit kinase. [EC: 2.7.11.23]
ATP + [DNA-directed RNA polymerase] = ADP + [DNA-directed RNA polymerase] phosphate.
  • Appears to be distinct from other protein phosphokinases.
  • Brings about multiple phosphorylation of the unique C-terminal repeat domain of the largest subunit of eukaryotic EC 2.7.7.6.
  • Does not phosphorylate casein, phosvitin or histone.
  • Formerly EC 2.7.1.141.
 4 G0QML9 G0QML9 G0QSS3 G0QSS3
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 G0QZ51 G0QZ51
Histone-lysine N-methyltransferase. [EC: 2.1.1.43]
S-adenosyl-L-methionine + L-lysine-[histone] = S-adenosyl-L-homocysteine + N(6)-methyl-L-lysine-[histone].
    		 2 A0A0F8ACY8 A0A0F8ACY8
    Transferred entry: 1.6.5.11. [EC: 1.6.99.5]
      		2 G0QYN6 G0QYN6
      DNA helicase. [EC: 3.6.4.12]
      ATP + H(2)O = ADP + phosphate.
      • DNA helicases utilize the energy from ATP hydrolysis to unwind double-stranded DNA.
      • Some of them unwind duplex DNA with a 3' to 5' polarity (1,3,5,8), other show 5' to 3' polarity (10,11,12,13) or unwind DNA in both directions (14,15).
      • Some helicases unwind DNA as well as RNA (4,9).
      • May be identical with EC 3.6.4.13 (RNA helicase).
      		 2 A0A1E5VMF4 A0A1E5VMF4
      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 G0QNF9 G0QNF9
      RING-type E3 ubiquitin transferase. [EC: 2.3.2.27]
      S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)- ubiquitinyl-[acceptor protein]-L-lysine.
      • The RING domain of E3 ubiquitin transferase serves as a mediator bringing the ubiquitin-charged E2 ubiquitin-conjugating enzyme and the acceptor protein together to enable the direct transfer of ubiquitin through the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin an the epsilon-amino group of an L-lysine residue of the acceptor protein.
      • The RING-E3 domain does not form a catalytic thioester intermediate with ubiquitin (unlike the HECT domain, EC 2.3.2.26).
      • RING-type ubiquitin transferases may occur as single-chain enzymes but also in dimeric forms or in multi-subunit assemblies.
      • Formerly EC 6.3.2.19 and EC 6.3.2.21.
      		 2 A5C7C9 A5C7C9
      Picornain 3C. [EC: 3.4.22.28]
      Selective cleavage of Gln-|-Gly bond in the poliovirus polyprotein. In other picornavirus reactions Glu may be substituted for Gln, and Ser or Thr for Gly.
      • From entero-, rhino-, aphto- and cardioviruses.
      • Larger than the homologous virus picornain 2A.
      • Belongs to peptidase family C3.
      		 2 G0QZ51 G0QZ51
      Phosphoserine transaminase. [EC: 2.6.1.52]
      (1) O-phospho-L-serine + 2-oxoglutarate = 3-phosphonooxypyruvate + L-glutamate. (2) 4-phosphonooxy-L-threonine + 2-oxoglutarate = (3R)-3-hydroxy-2-oxo-4- phosphonooxybutanoate + L-glutamate.
      • Catalyzes the second step in the phosphorylated pathway of serine biosynthesis in Escherichia coli.
      • Also catalyzes the third step in the biosynthesis of the coenzyme pyridoxal 5'-phosphate in E.coli (using reaction 2 above).
      • In E.coli, pyridoxal 5'-phosphate is synthesized de novo by a pathway that involves EC 1.2.1.72, EC 1.1.1.290, EC 2.6.1.52, EC 1.1.1.262, EC 2.6.99.2 and EC 1.4.3.5 (with pyridoxine 5'-phosphate as substrate).
      • Pyridoxal phosphate is the cofactor for both activities and therefore seems to be involved in its own biosynthesis.
      • Non-phosphorylated forms of serine and threonine are not substrates.
      		 2 A0A1J7GXQ7 A0A1J7GXQ7
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