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CATH Superfamily 3.40.470.10

Uracil-DNA glycosylase-like domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Uracil-DNA glycosylase-like 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.

Superfamily EC Annotations

Note: the EC figure is not being displayed for this superfamily as there are more than 100 different EC terms.

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
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.
 1173 A0A009HDJ9 A0A009I432 A0A009QEQ1 A0A009RI98 A0A009TDI7 A0A015QL79 A0A015QM57 A0A015TQD1 A0A015TWY9 A0A015UK46
(1163 more...)
Double-stranded uracil-DNA glycosylase. [EC: 3.2.2.28]
Specifically hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free uracil.
  • No activity on DNA containing a T/G mispair or single-stranded DNA containing either a site-specific uracil or 3,N(4)-ethenocytosine residue, significant role for double-stranded uracil-DNA glycosylase in mutation avoidance in non-dividing Escherichia coli.
  • 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.
 293 A0A026VB62 A0A028AA07 A0A028EDX7 A0A029HJX2 A0A029IKI0 A0A069XQQ0 A0A070FM44 A0A070T7P7 A0A070UXB2 A0A073FQ12
(283 more...)
DNA-directed DNA polymerase. [EC: 2.7.7.7]
Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).
  • Catalyzes DNA-template-directed extension of the 3'-end of a DNA strand by one nucleotide at a time.
  • Cannot initiate a chain de novo.
  • Requires a primer which may be DNA or RNA.
  • See also EC 2.7.7.49.
 6 A0A0E1NKQ0 A0A0H2YMP7 A0A384LBB7 A0A454Y7E3 O68770 P30314
Thymine-DNA glycosylase. [EC: 3.2.2.29]
Hydrolyzes mismatched double-stranded DNA and polynucleotides, releasing free thymine.
  • Thymine-DNA glycosylase is part of the DNA-repair machinery.
  • Thymine removal is fastest when it is from a G/T mismatch with a 5'-flanking C/G pair.
  • The glycosylase removes uracil from G/U, C/U, and T/U base pairs faster than it removes thymine from G/T.
 2 P56581 Q13569