InterPro domain: IPR001943

During the process of Escherichia coli nucleotide excision repair, DNA damagerecognition and processing are achieved by the action of the uvrA, uvrB,and uvrC gene products [ 1 ]. UvrB and UvrC share a common domain of around 35amino acids, the so called UVR domain. This domain in UvrB can interact withthe homologous domain in UvrC throughout a putative coiled coil structure.This interaction is important for the incision of the damaged strand [ 2 ].

A conserved region similar to the UVR domain is also found in the ATP-binding subunit of bacterial and chloroplastic Clp ATPases [ 3 ], which suggest that the UVR domain is not only involved in the interaction between uvrB and uvrC.

1. Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem. Bioessays 15, 51-9
2. The C-terminal region of the UvrB protein of Escherichia coli contains an important determinant for UvrC binding to the preincision complex but not the catalytic site for 3'-incision. J. Biol. Chem. 270, 30508-15
3. Clp ATPases are required for stress tolerance, intracellular replication and biofilm formation in Staphylococcus aureus. Mol. Microbiol. 54, 1445-62