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CATH Superfamily 3.20.20.150

Divalent-metal-dependent TIM barrel enzymes

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:

"
Divalent-metal-dependent TIM barrel enzymes
".

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 31: Probable endonuclease 4

There are 1 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
Deoxyribonuclease IV. [EC: 3.1.21.2]
Endonucleolytic cleavage to 5'-phosphooligonucleotide end-products.
  • The enzyme is an apurinic/apyrimidinic (AP) site endonuclease that primes DNA repair synthesis at AP sites.
  • It specifically cleaves the DNA backbone at AP sites and also removes 3' DNA-blocking groups such as 3' phosphates, 3' phosphoglycolates, and 3' alpha,beta-unsaturated aldehydes that arise from oxidative base damage and the activity of combined glycosylase/lyase enzymes.
  • It is also the only known repair enzyme that is able to cleave the DNA backbone 5' of the oxidative lesion alpha-deoxyadenosine.
  • The enzyme has a strong preference for single-stranded DNA.
  • Formerly EC 3.1.4.30.
 4 D6EIZ3 D6EIZ3 Q9S2N2 Q9S2N2
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