DNA photolyase, N-terminal is an evolutionary conserved protein domain. This domain binds a light harvesting chromophore that enhanced the spectrum of photolyase or cryptochrome light absorption, i.e. an antenna.^[1] It adopts the rossmann fold.^[2]

The cofactor may be either the pterin 5,10-Methenyltetrahydrofolate (MTHF, MHF) in folate photolyases (PDB: 4U63​) or the deazaflavin 8-hydroxy-7,8-didemethyl-5-deazariboflavin (8-HDF, FO1) in deazaflavin photolyases (PDB: 3CVV, 4CDN​).^[2] The 8-HDF ligand usually binds into this domain (next to the C-terminal half), while MHF tends to bind to an outside groove of this domain.^[3] A structural signature for 8-HDF binding has been produced, highlighting amino acid residues that determine which antenna a photolyase can use.^[4] Experiments on a Thermus thermophilus protein with this domain (P61497) shows that artificial substrates can be alternatively used for a modified absorption spectra. It naturally binds FMN in a pose similar to 8-HDF.^[5] In addition, many cryptochromes, especially those from animals, bind no cofactors at this domain.^[3]

Even though few eukaryotes (and no animals) can synthesize 8-HDF on their own,^[6] many lineages nevertheless use deazaflavin photolyases. They probably receive 8-HDF from their endosymbiotic microbes.^[4] Unlike many bacterial deazaflavin photolyases that accepts FMN as well as 8-HDF, one such enzyme from the fruit fly only accepts 8-HDF.^[6]

The FeS-BCP N-terminal domain is homologous to this domain. Instead of an organic cofactor, its chromophore is an iron-sulphur cluster.^[7]

Human proteins containing this domain include:

• CRY1
• CRY2