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: 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.
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FunFam 47551: RuvB-like helicase 2, putative

There are 4 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
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).
5160 A0A010R3F4 A0A010R3F4 A0A010S768 A0A010S768 A0A014P8Z5 A0A014P8Z5 A0A014PMP3 A0A014PMP3 A0A015IZV9 A0A015IZV9
(5150 more...)
Endopeptidase La. [EC: 3.4.21.53]
Hydrolysis of proteins in presence of ATP.
  • ATP hydrolysis is linked with peptide bond hydrolysis.
  • Vanadate inhibits both reactions.
  • A similar enzyme occurs in animal mitochondria.
  • Belongs to peptidase family S16.
28 A0A0G4CBS8 A0A0G4CBS8 A0A0K6K7Q9 A0A0K6K7Q9 A0A0K6KSM8 A0A0K6KSM8 A0A0K6LJP1 A0A0K6LJP1 A0A0T8PJR7 A0A0T8PJR7
(18 more...)
Homoaconitate hydratase. [EC: 4.2.1.36]
(1R,2S)-1-hydroxybutane-1,2,4-tricarboxylate = (Z)-but-1-ene-1,2,4- tricarboxylate + H(2)O.
  • The enzyme from the hyperthermophilic eubacterium Thermus thermophilus can catalyze the reaction shown above but cannot catalyze the previously described reaction, i.e. formation of homocitrate by hydration of cis-homoaconitate.
  • The enzyme responsible for the conversion of cis-homoaconitate into homocitrate in T.thermophilus is unknown at present but the reaction can be catalyzed in vitro using EC 4.2.1.3 from pig.
2 A0A168DI61 A0A168DI61
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 T1JDV2 T1JDV2