1 Contains
| DB identifier | Type | Name |
|---|---|---|
| IPR018394 | Conserved_site | Cryptochrome/DNA photolyase, class 1 conserved site, C-terminal |
| Type: | Domain | Name: | Cryptochrome/photolyase FAD-binding domain |
| Description: | This entry represents a multi-helical domain found C-terminal in cryptochrome proteins and DNA photolyases. It acts as a FAD-binding domain [].Photolyases and cryptochromes are related flavoproteins that bind FAD. Photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers. Cryptochromes are blue light photoreceptors that mediate blue light-induced gene expression. They function as photoreceptors in plants and circadian clock components in animals [, ]. DNA photolyases are DNA repair enzymes that repair mismatched pyrimidine dimers induced by exposure to ultra-violet light. They bind to UV-damaged DNA containing pyrimidine dimers and, upon absorbing a near-UV photon (300 to 500 nm), they catalyse dimer splitting, breaking the cyclobutane ring joining the two pyrimidines of the dimer so as to split them into the constituent monomers; this process is called photoreactivation. DNA photolyases require two choromophore-cofactors for their activity. All monomers contain a reduced FAD moiety, and, in addition, either a reduced pterin or 8-hydroxy-5-diazaflavin as a second chromophore. Either chromophore may act as the primary photon acceptor, peak absorptions occurring in the blue region of the spectrum and in the UV-B region, at a wavelength around 290nm [, ]. | Short Name: | Cryptochr/Photolyase_FAD-bd |
| DB identifier | Type | Name |
|---|---|---|
| IPR018394 | Conserved_site | Cryptochrome/DNA photolyase, class 1 conserved site, C-terminal |
