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UvrB interaction domain
This domain is found in the UvrB protein where it interacts with the UvrA protein [2]. [1]. 18158267. Crystal structure of Bacillus stearothermophilus UvrA provides insight into ATP-modulated dimerization, UvrB interaction, and DNA binding. Pakotiprapha D, Inuzuka Y, Bowman BR, Moolenaar GF, Goosen N, Jeruzalmi D, Verdine GL;. Mol Cell. 2008;29:122-133. [2]. 19287003. A structural model for the damage-sensing complex in bacterial nucleotide excision repair. Pakotiprapha D, Liu Y, Verdine GL, Jeruzalmi D;. J Biol Chem. 2009;284:12837-12844. (from Pfam)
Ultra-violet resistance protein B
This domain family is found in bacteria, archaea and eukaryotes, and is approximately 40 amino acids in length. The family is found in association with Pfam:PF00271, Pfam:PF02151, Pfam:PF04851. There are two conserved sequence motifs: YAD and RRR. This family is the C terminal region of the UvrB protein which conveys mutational resistance against UV light to various different species. [1]. 7721686. A promoter associated with the neisserial repeat can be used to transcribe the uvrB gene from Neisseria gonorrhoeae. Black CG, Fyfe JA, Davies JK;. J Bacteriol. 1995;177:1952-1958. (from Pfam)
DEAD/DEAH box helicase family protein
UvrB/UvrC motif-containing protein
helicase-related protein
The Prosite family is restricted to DEAD/H helicases, whereas this domain family is found in a wide variety of helicases and helicase related proteins. It may be that this is not an autonomously folding unit, but an integral part of the helicase. (from Pfam)
excinuclease ABC subunit UvrB
excinuclease ABC subunit B is part of the UvrABC repair system, which catalyzes the recognition and processing of DNA lesions
The UvrABC repair system catalyzes the recognition and processing of DNA lesions. The beta-hairpin of the Uvr-B subunit is inserted between the strands, where it probes for the presence of a lesion
All proteins in this family for wich functions are known are DNA helicases that function in the nucleotide excision repair and are endonucleases that make the 3' incision next to DNA damage. They are part of a pathway requiring UvrA, UvrB, UvrC, and UvrD homologs. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University)
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