InterPro : IPR005101

Name  DNA photolyase, FAD-binding/Cryptochrome, C-terminal Short Name  Photolyase_FAD-bd/Cryptochr_C
Type  Domain Description  This entry represents a multi-helical domain composed of two all-alpha subdomains that is found as the C-terminal domain in cryptochrome proteins, as well as at the N-terminal of DNA photolyase where it acts as a FAD-binding domain (the N-terminal of DNA photolyase binds a light-harvesting cofactor).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 (CRY1 and CRY2) are blue light photoreceptors that mediate blue light-induced gene expression [, ].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 [, ].
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Sequence Features

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Proteins

InterPro protein domain ID --> Contigs

 

Other

0 Child Features

1 Contains

Id Name Short Name Type
IPR018394 Cryptochrome/DNA photolyase, class 1 conserved site, C-terminal DNA_photolyase_1_CS_C Conserved_site

3 Found In

Id Name Short Name Type
IPR008148 DNA photolyase, class 2 DNA_photolyase_2 Family
IPR002081 Cryptochrome/DNA photolyase, class 1 Cryptochrome/DNA_photolyase_1 Family
IPR019947 Deoxyribodipyrimidine photo-lyase, 8-HDF type Photolyase_8HDF Family

0 Parent Features

4 Publications

First Author Title Year Journal Volume Pages
Park HW Crystal structure of DNA photolyase from Escherichia coli. 1995 Science 268 1866-72
Brudler R Identification of a new cryptochrome class. Structure, function, and evolution. 2003 Mol Cell 11 59-67
Kort R DNA apophotolyase from Anacystis nidulans: 1.8 A structure, 8-HDF reconstitution and X-ray-induced FAD reduction. 2004 Acta Crystallogr D Biol Crystallogr 60 1205-13
Brautigam CA Structure of the photolyase-like domain of cryptochrome 1 from Arabidopsis thaliana. 2004 Proc Natl Acad Sci U S A 101 12142-7



To cite PlanMine, please refer to the following publication:

Rozanski, A., Moon, H., Brandl, H., Martín-Durán, J. M., Grohme, M., Hüttner, K., Bartscherer, K., Henry, I., & Rink, J. C.
PlanMine 3.0—improvements to a mineable resource of flatworm biology and biodiversity
Nucleic Acids Research, gky1070. doi:10.1093/nar/gky1070 (2018)