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CATH Superfamily 1.20.142.10

Poly(ADP-ribose) polymerase, regulatory domain

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:

"
Poly(ADP-ribose) polymerase, regulatory domain
".

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 408: Poly [ADP-ribose] polymerase 1

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
NAD(+) ADP-ribosyltransferase. [EC: 2.4.2.30]
NAD(+) + (ADP-D-ribosyl)(n)-acceptor = nicotinamide + (ADP-D- ribosyl)(n+1)-acceptor.
  • The ADP-D-ribosyl group of NAD(+) is transferred to an acceptor carboxy group on a histone or the enzyme itself, and further ADP- ribosyl groups are transferred to the 2'-position of the terminal adenosine moiety, building up a polymer with an average chain length of 20-30 units.
 1599 A0A010R3N3 A0A014PFX3 A0A014QVK2 A0A015K5T5 A0A016W4D1 A0A016W4D6 A0A016W4I1 A0A016W4I9 A0A017SBJ6 A0A022R9L7
(1589 more...)
Uracil-DNA glycosylase. [EC: 3.2.2.27]
Hydrolyzes single-stranded DNA or mismatched double-stranded DNA and polynucleotides, releasing free uracil.
  • Uracil-DNA glycosylases are widespread enzymes that are found in all living organisms.
  • Uracil-DNA glycosylase (EC 3.2.2.27) and double-stranded uracil-DNA glycosylase (EC 3.2.2.28) form a central part of the DNA-repair machinery since they initiate the DNA base-excision repair pathway by hydrolyzing the N-glycosidic bond between uracil and the deoxyribose sugar thereby catalyzing the removal of mis-incorporated uracil from DNA.
 1 L8H564