{PDOC50151}
{PS50151; UVR}
{BEGIN}
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* UVR domain profile *
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In   prokaryote,  nucleotide  excision  repair,  DNA  damage  recognition  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 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
[2]  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 [3].

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.

-Sequences known to belong to this class detected by the profile: a majority.
-Other sequence(s) detected in Swiss-Prot: NONE.

-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.

[ 1] Van Houten B., Snowden A.
     "Mechanism of action of the Escherichia coli UvrABC nuclease: clues to
     the damage recognition problem."
     BioEssays 15:51-59(1993).
     PubMed=8466476;
[ 2] Sohi M., Alexandrovich A., Moolenaar G., Visse R., Goosen N.,
     Vernede X., Fontecilla-Camps J.C., Champness J., Sanderson M.R.
     "Crystal structure of Escherichia coli UvrB C-terminal domain, and a
     model for UvrB-uvrC interaction."
     FEBS Lett. 465:161-164(2000).
     PubMed=10631326;
[ 3] Moolenaar G.F., Franken K.L., Dijkstra D.M., Thomas-Oates J.E.,
     Visse R., van de Putte P., Goosen N.
     "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. 270:30508-30515(1995).
     PubMed=8530482;

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