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 2711: Putative cryptochrome DASH, mitochondrial

There are 3 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
Deoxyribodipyrimidine photo-lyase. [EC: 4.1.99.3]
Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).
  • A flavoprotein containing a second chromophore group.
  • Catalyzes the reactivation by light of irradiated DNA.
  • A similar reactivation of irradiated RNA is probably due to a separate enzyme.
65 A0A073CGB8 A0A076NU56 A0A0B2PRF6 A0A0D2KU34 A0A0E3ZMW6 A0A0H3AJW5 A0A0H3Q2V2 A0A0H6LK67 A0A0K9V1G6 A0A0P7Z3Y1
(55 more...)
TRNA (guanine(46)-N(7))-methyltransferase. [EC: 2.1.1.33]
S-adenosyl-L-methionine + guanine(46) in tRNA = S-adenosyl-L-homocysteine + N(7)-methylguanine(46) in tRNA.
  • The enzyme specifically methylates guanine(46) at N(7) in tRNA.
2 A0A078CZD7 A0A0D3DCZ7
(6-4)DNA photolyase. [EC: 4.1.99.13]
(6-4) photoproduct (in DNA) = 2 pyrimidine residues (in DNA).
  • The overall repair reaction consists of two distinct steps, one of which is light-independent and the other one light-dependent.
  • In the initial light-independent step, a 6-iminium ion is thought to be generated via proton transfer induced by two histidines highly conserved among the (6-4) photolyases.
  • This intermediate spontaneously rearranges to form an oxetane intermediate by intramolecular nucleophilic attack.
  • In the subsequent light-driven reaction, one electron is believed to be transferred from the fully reduced FAD cofactor (FADH(-)) to the oxetane intermediate thus forming a neutral FADH radical and an anionic oxetane radical, which spontaneously fractures.
  • The excess electron is then back-transferred to the flavin radical restoring the fully reduced flavin cofactor and a pair of pyrimidine bases.
2 O48652 Q0E2Y1