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:

"
Homeodomain-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 123639: Transcriptional activator DNA repair enzyme Ada

There are 2 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
Methylated-DNA--[protein]-cysteine S-methyltransferase. [EC: 2.1.1.63]
DNA (containing 6-O-methylguanine) + protein L-cysteine = DNA (without 6-O-methylguanine) + protein S-methyl-L-cysteine.
  • This protein is involved in the repair of alkylated DNA.
  • It acts only on the alkylated DNA (cf. EC 3.2.2.20 and EC 3.2.2.21).
  • This enzyme catalyzes only one turnover and therefore is not strictly catalytic.
490 A0A017IE09 A0A017IE09 A0A023Z0C8 A0A023Z0C8 A0A024KWX8 A0A024KWX8 A0A024L1L6 A0A024L1L6 A0A025CEM1 A0A025CEM1
(480 more...)
Methylphosphotriester-DNA--[protein]-cysteine S-methyltransferase. [EC: 2.1.1.n11]
DNA (containing Sp-methylphosphotriester) + protein L-cysteine = DNA (without Sp-methylphosphotriester) + protein S-methyl-L-cysteine.
  • This protein is involved in the repair of Sp diastereomers of DNA methylphosphotriester lesions.
  • This enzyme catalyzes only one turnover and therefore is not strictly catalytic.
  • The enzyme from the bacterium Escherichia coli also has the activity of EC 2.1.1.63 while the enzyme from Bacillus subtilis does not.
72 A0A069XUR9 A0A069XUR9 A0A070CNK4 A0A070CNK4 A0A070SYL0 A0A070SYL0 A0A080F968 A0A080F968 A0A0E1T3X2 A0A0E1T3X2
(62 more...)