The domain within your query sequence starts at position 23 and ends at position 187; the E-value for the DNA_photolyase domain shown below is 2.4e-50.



PFAM accession number:PF00875
Interpro abstract (IPR006050):

The photolyase/cryptochrome family consists of flavoproteins that perform various functions using blue-light photons as an energie source. It is present in all three domains of life, that is, archaea, eubacteria, and eukaryotes, and hence has arisen very early during evolution to protect genomes against the genotoxic effects of ultraviolet light originating from the sun. The photolyase/cryptochrome family is divided into two major groups: photolyases and cryptochromes. Photolyases repair cytotoxic and mutagenic UV-induced photolesions in DNA in many species from bacteria to plants and animals by using a light-dependent repair mechanism. It involves light absorption, electron transfer from an excited reduced and deprotanated FADH(-) to the flipped-out photolesion, followed by the fragmentation of the photolesions. Cryptochromes are highly related proteins that generally no longer repair damaged DNA, but function as photoreceptors. Cryptochromes regulate growth and development in plants and the circadian clock in animals [ (PUBMED:12535521) (PUBMED:19074258) (PUBMED:9487120) (PUBMED:19570997) (PUBMED:21892138) (PUBMED:22170053) (PUBMED:22325881) ].

Both photolyases and cryptochromes have a bilobal architecture consisting of two domains: an N-terminal alpha/beta domain that may contain a light- harvesting chromophore to additionally broaden their activity spectra and a C- terminal alpha-helical catalytic domain comprising the light-sensitive FAD cofactor. Diverse classes of antenna chromophores likes 5,10- methenyltetrahydrofolate (MTHF), 8-hydroxydeazaflavin, FMN or FAD have been identified in some photolyase/cryptochrome to broaden their activity spectra, whereas many others apparently lack any bound antenna chromophores.

This entry represents the photolyase/cryptochrome alpha/beta domain. It adopts a dinucleotide binding fold with a five-stranded parallel beta sheet flanked on both sides by alpha helices [ (PUBMED:12535521) (PUBMED:21892138) ].

This is a PFAM domain. For full annotation and more information, please see the PFAM entry DNA_photolyase