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FAD-binding domain-containing protein
deoxyribodipyrimidine photo-lyase
This domain binds a light harvesting cofactor. [1]. 9360600. Crystal structure of DNA photolyase from Anacystis nidulans. Tamada T, Kitadokoro K, Higuchi Y, Inaka K, Yasui A, de Ruiter PE, Eker AP, Miki K. Nat Struct Biol 1997;4:887-891. (from Pfam)
cryptochrome/photolyase family protein
cryptochrome/photolyase family protein may act as a DNA photolyase such as deoxyribodipyrimidine photo-lyase, which is involved in repair of UV radiation-induced DNA damage by catalyzing the light-dependent monomerization of cyclobutyl pyrimidine dimers. Photolyases and cryptochromes are related flavoproteins; while photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers, cryptochromes do not repair DNA and are presumed to act instead in some other (possibly unknown) process such as entraining circadian rhythms. They may show weak photolyase activity in vitro but have not been shown to affect DNA repair in vivo. Rather, DASH family cryptochromes have been shown to bind RNA or DNA, and seem likely to act in light-responsive regulatory processes.
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