|PROSITE documentation PDOC50151 [for PROSITE entry PS50151]|
In prokaryote, nucleotide excision repair, DNA damage recognition and processing are achieved by the action of the uvrA, uvrB, and uvrC gene products . UvrB and uvrC share a common domain of around 35 amino acids, the so called UVR domain. This domain in uvrB can interact with the homologous domain in uvrC. The crystal structure of Escherichia coli uvrB and uvrC dimer  revealed that the interaction is made throughout a coiled coil structure (see <PDB:1QOJ>). This interaction is important for the incision of the damaged strand .
A conserved region similar to the UVR domain is also found in the ATP-binding subunit of bacterial and chloroplastic Clp proteases, which suggest that the UVR domain is not only involved in the interaction between uvrB and uvrC.
The profile we developed covers the whole domain.Note:
Because of the short size of the domain it is not possible to pick-up all UVR domains with a statistically significant score.Last update:
April 2002 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|1||Authors||Van Houten B. Snowden A.|
|Title||Mechanism of action of the Escherichia coli UvrABC nuclease: clues to the damage recognition problem.|
|2||Authors||Sohi M. Alexandrovich A. Moolenaar G. Visse R. Goosen N. Vernede X. Fontecilla-Camps J.C. Champness J. Sanderson M.R.|
|Title||Crystal structure of Escherichia coli UvrB C-terminal domain, and a model for UvrB-uvrC interaction.|
|Source||FEBS Lett. 465:161-164(2000).|
|3||Authors||Moolenaar G.F. Franken K.L. Dijkstra D.M. Thomas-Oates J.E. Visse R. van de Putte P. Goosen N.|
|Title||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.|
|Source||J. Biol. Chem. 270:30508-30515(1995).|