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CATH Superfamily 1.10.1670.10

Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)

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:

"
Helix-hairpin-Helix base-excision DNA repair enzymes (C-terminal)
".

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 5801: Probable N-glycosylase/DNA lyase

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
DNA-(apurinic or apyrimidinic site) lyase. [EC: 4.2.99.18]
The C-O-P bond 3' to the apurinic or apyrimidinic site in DNA is broken by a beta-elimination reaction, leaving a 3'-terminal unsaturated sugar and a product with a terminal 5'-phosphate.
  • 'Nicking' of the phosphodiester bond is due to a lyase-type reaction, not hydrolysis.
  • This group of enzymes was previously listed as endonucleases, under the number EC 3.1.25.2.
 64 A0A075W9Y2 A0A075W9Y2 A0A0A6QJB2 A0A0A6QJB2 A0A0A7GCJ5 A0A0A7GCJ5 A0A0B5KQK5 A0A0B5KQK5 A0A101E0C8 A0A101E0C8
(54 more...)
DNA-formamidopyrimidine glycosylase. [EC: 3.2.2.23]
Hydrolysis of DNA containing ring-opened 7-methylguanine residues, releasing 2,6-diamino-4-hydroxy-5-(N-methyl)formamidopyrimidine.
  • May play a significant role in processes leading to recovery from mutagenesis and/or cell death by alkylating agents.
  • Also involved in the GO system responsible for removing an oxidatively damaged form of guanine (7,8-dihydro-8-oxoguanine) from DNA.
 12 A0A0L1HET2 A0A0L1HET2 B3NUL4 B3NUL4 B4L6Y2 B4L6Y2 B4MA54 B4MA54 B4MJ78 B4MJ78
(2 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.
 2 D3B670 D3B670
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