| Type: | Conserved_site | Name: | Cryptochrome/DNA photolyase, class 1 conserved site, C-terminal |
| Description: | Deoxyribodipyrimidine photolyase (DNA photolyase) [] is a DNArepair enzyme. It binds to UV-damaged DNA containing pyrimidine dimers and, upon absorbing a near-UV photon (300 to 500 nm), breaks the cyclobutane ring joining the two pyrimidines of the dimer. DNA photolyase is an enzyme that requires two choromophore-cofactors for its activity: a reduced FADH2 and either 5,10-methenyltetrahydrofolate (5,10-MTFH) or an oxidized 8-hydroxy-5-deazaflavin (8-HDF) derivative (F420). The folate or deazaflavin chromophore appears to function as an antenna, while the FADH2 chromophore is thought to be responsible for electron transfer.On the basis of sequence similarities DNA photolyases can be grouped into two classes []. The first class contains enzymes from eubacteria, the halophilic archaebacteria Halobacterium salinarium(Halobacterium halobium), fungi and plants. Class 1 enzymes bind either 5,10-MTHF (Escherichia coli, fungi, etc.) or 8-HDF (Streptomyces griseus, Halobacterium halobium) [, ]. The second class contains DNA photolyases from higher eukaryotes, methanobacteria and eubacteria.This family also includes plant cryptochromes 1 (CRY1) and 2 (CRY2), which are blue light photoreceptors that mediate blue light-induced geneexpression. | Short Name: | DNA_photolyase_1_CS_C |
