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CATH Superfamily 2.20.70.10

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was: waiting to be named.

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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
HECT-type E3 ubiquitin transferase. [EC: 2.3.2.26]
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.
  • In the first step the enzyme transfers ubiquitin from the E2 ubiquitin-conjugating enzyme (EC 2.3.2.23) to a cysteine residue in its HECT domain (which is located in the C-terminal region), forming a thioester bond.
  • In a subsequent step the enzyme transfers the ubiquitin to an acceptor protein, resulting in the formation of an isopeptide bond between the C-terminal glycine residue of ubiquitin and the epsilon- amino group of an L-lysine residue of the acceptor protein.
  • Cf. EC 2.3.2.27 and EC 2.3.2.31.
 125 A0A024R711 A0A024R711 A0A0B4KFU5 A0A0B4KFU5 A0A0B4KFU5 A0A1L8ENB0 A0A1L8ENB0 A0A254TVI1 A0A254TVI1 A0A2I2YEM7
(115 more...)
Peptidylprolyl isomerase. [EC: 5.2.1.8]
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.
 26 A0A0A0MWZ5 A0A0B0E8R0 A0A2J8S1C9 A0A2K5CB38 A0A2K5NZD5 A0A2K5S4N8 A0A2K5ZIQ9 A0A2K6CFL7 A0A452EDY8 F8MLE4
(16 more...)
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].
    		 12 A0A0B0EBB8 A0A1H6Q9F0 E1JJN9 E9Q5F9 Q1DU03 Q2H988 Q59XV0 Q6BM04 Q6C5G5 Q7RZU4
    (2 more...)
    MRNA (2'-O-methyladenosine-N(6)-)-methyltransferase. [EC: 2.1.1.62]
    S-adenosyl-L-methionine + a 5-(N(7)-methyl 5-triphosphoguanosine)-2'-O- methyladenosine-[mRNA] = S-adenosyl-L-homocysteine + a 5-(N(7)-methyl 5-triphosphoguanosine)-N(6),2'-O-dimethyladenosine-[mRNA].
    • mRNA containing an N(6),2'-O-dimethyladenosine cap.
    		 6 A0A0R4IKJ1 A0A2R9B6G1 H2QKH7 P59114 Q542C3 Q9H4Z3
    ADP-ribose diphosphatase. [EC: 3.6.1.13]
    ADP-D-ribose + H(2)O = AMP + D-ribose 5-phosphate.
      		 2 A0A178VYY0 P93740
      FAD diphosphatase. [EC: 3.6.1.18]
      FAD + H(2)O = AMP + FMN.
      • The plant enzyme also hydrolyzes NAD(+) and NADH; the animal enzyme hydrolyzes NAD(+) and CoA at about half of the rate of hydrolysis of FAD.
      • May be identical with EC 3.6.1.9.
      		 2 A0A178VYY0 P93740
      RNA helicase. [EC: 3.6.4.13]
      ATP + H(2)O = ADP + phosphate.
      • RNA helicases utilize the energy from ATP hydrolysis to unwind RNA.
      • Some of them unwind RNA with a 3' to 5' polarity, other show 5' to 3' polarity.
      • Some helicases unwind DNA as well as RNA.
      • May be identical with EC 3.6.4.12 (DNA helicase).
      		 1 Q9LYJ9