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. Author manuscript; available in PMC: 2018 Oct 1.
Published in final edited form as: Photochem Photobiol. 2017 Jan 27;93(1):112–127. doi: 10.1111/php.12663

Figure 1.

Figure 1.

The domain structure of CRYs and CRY-interacting proteins. (a) Schematic diagram showing domains in CRY1 and CRY2. MTHF, 5-methyltetrahydrofolate; FAD, flavin adenine dinucleotide; PHR, photolyase homology region domain; CCE, C-terminal extension domain; NC80, 80 residues without C-terminal tail in CCE domain; CT, C-terminal tail. (b) Schematic of CRY-interacting proteins showing the functional domains and CRY-binding sites. RING, RING finger domain; CC, coiled-coil domain; WD40, WD40 repeat; kinase-related, protein kinase-like domain; bHLH, basic helix–loop–helix domain, APB, active phytochrome B binding motif. The gray lines at the bottom of each diagram represent the CRY-binding regions. The binding domains of CRYs are also shown underneath each gray line. The asterisk indicates that CRY2 binds PIF5 with a mutation in the APB motif.