cryptochrome/deoxyribodipyrimidine photo-lyase family protein; cryptochrome/photolyase family protein( domain architecture ID 1903185)
cryptochrome/deoxyribodipyrimidine photo-lyase family (CPF) protein is a flavoprotein that may be involved in DNA repair, circadian photoreception, and transcriptional regulation; similar to cryptochrome-1| cryptochrome/photolyase family protein may act as a DNA photolyase such as deoxyribodipyrimidine photo-lyase, which is involved in repair of UV radiation-induced DNA damage by catalyzing the light-dependent monomerization of cyclobutyl pyrimidine dimers. Photolyases and cryptochromes are related flavoproteins; while photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers, cryptochromes do not repair DNA and are presumed to act instead in some other (possibly unknown) process such as entraining circadian rhythms. They may show weak photolyase activity in vitro but have not been shown to affect DNA repair in vivo. Rather, DASH family cryptochromes have been shown to bind RNA or DNA, and seem likely to act in light-responsive regulatory processes.
cryptochrome, DASH family; Photolyases and cryptochromes are related flavoproteins. ...
5-406
5.80e-41
cryptochrome, DASH family; Photolyases and cryptochromes are related flavoproteins. Photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers. Cryptochromes do not repair DNA and are presumed to act instead in some other (possibly unknown) process such as entraining circadian rhythms. This model describes the cryptochrome DASH subfamily, one of at least five major subfamilies, which is found in plants, animals, marine bacteria, etc. Members of this family bind both folate and FAD. They may show weak photolyase activity in vitro but have not been shown to affect DNA repair in vivo. Rather, DASH family cryptochromes have been shown to bind RNA (Vibrio cholerae VC1814), or DNA, and seem likely to act in light-responsive regulatory processes. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 274288 [Multi-domain] Cd Length: 429 Bit Score: 150.99 E-value: 5.80e-41
cryptochrome, DASH family; Photolyases and cryptochromes are related flavoproteins. ...
5-406
5.80e-41
cryptochrome, DASH family; Photolyases and cryptochromes are related flavoproteins. Photolyases harness the energy of blue light to repair DNA damage by removing pyrimidine dimers. Cryptochromes do not repair DNA and are presumed to act instead in some other (possibly unknown) process such as entraining circadian rhythms. This model describes the cryptochrome DASH subfamily, one of at least five major subfamilies, which is found in plants, animals, marine bacteria, etc. Members of this family bind both folate and FAD. They may show weak photolyase activity in vitro but have not been shown to affect DNA repair in vivo. Rather, DASH family cryptochromes have been shown to bind RNA (Vibrio cholerae VC1814), or DNA, and seem likely to act in light-responsive regulatory processes. [Cellular processes, Adaptations to atypical conditions]
Pssm-ID: 274288 [Multi-domain] Cd Length: 429 Bit Score: 150.99 E-value: 5.80e-41
cryptochrome, plant family; At least five major families of cryptochomes and photolyases share ...
7-435
4.24e-38
cryptochrome, plant family; At least five major families of cryptochomes and photolyases share FAD cofactor binding, sequence homology, and the ability to react to short wavelengths of visible light. Photolysases are responsible for light-dependent DNA repair by removal of two types of uv-induced DNA dimerizations. Cryptochromes have other functions, often regulatory and often largely unknown, which may include circadian clock entrainment and control of development. Members of this subfamily are known so far only in plants; they may show some photolyase activity in vitro but appear mostly to be regulatory proteins that respond to blue light.
Pssm-ID: 131813 [Multi-domain] Cd Length: 475 Bit Score: 143.85 E-value: 4.24e-38
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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