Summary: DNA photolyase
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This is the Wikipedia entry entitled "DNA photolyase". More...
DNA photolyase Edit Wikipedia article
| Identifiers | |||||||||
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| Symbol | DNA_photolyase | ||||||||
| Pfam | PF00875 | ||||||||
| InterPro | IPR006050 | ||||||||
| PROSITE | PDOC00331 | ||||||||
| SCOP | 1qnf | ||||||||
| SUPERFAMILY | 1qnf | ||||||||
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DNA photolyase is an evolutionary conserved protein domain. This domain binds a light harvesting cofactor.[1]
Deoxyribodipyrimidine photolyase (DNA photolyase) is a DNA repair enzyme. It binds to UV-damaged DNA containing pyrimidine dimers and, upon absorbing a near-UV photon (300 to 500 nm), breaks the cyclobutane ring joining the two pyrimidines of the dimer. DNA photolyase is an enzyme that requires two chromophore-cofactors for its activity: a reduced FADH2 and either 5,10-methenyltetrahydrofolate (5,10-MTFH) or an oxidized 8-hydroxy-5-deazaflavin (8-HDF) derivative (F420). The folate or deazaflavin chromophore appears to function as an antenna, while the FADH2 chromophore is thought to be responsible for electron transfer. On the basis of sequence similarities DNA photolyases can be grouped into two classes. The first class contains enzymes from Gram-negative and Gram-positive bacteria, the halophilic archaebacteria Halobacterium halobium, fungi and plants. Class 1 enzymes bind either 5,10-MTHF (E. coli, fungi, etc.) or 8-HDF (S. griseus, H. halobium).
Proteins containing this domain also include Arabidopsis thaliana cryptochromes 1 (CRY1) and 2 (CRY2), which are blue light photoreceptors that mediate blue light-induced gene expression.
[edit] Examples
Human proteins containing this domain include:
[edit] References
- ^ Tamada T, Kitadokoro K, Higuchi Y, Inaka K, Yasui A, de Ruiter PE, Eker AP, Miki K (November 1997). "Crystal structure of DNA photolyase from Anacystis nidulans". Nat. Struct. Biol. 4 (11): 887–91. doi:10.1038/nsb1197-887. PMID 9360600.
This article incorporates text from the public domain Pfam and InterPro IPR005101
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DNA photolyase Provide feedback
This domain binds a light harvesting cofactor.
Literature references
-
Tamada T, Kitadokoro K, Higuchi Y, Inaka K, Yasui A, de Ruiter PE, Eker AP, Miki K , Nat Struct Biol 1997;4:887-891.: Crystal structure of DNA photolyase from Anacystis nidulans. PUBMED:9360600 EPMC:9360600
External database links
| HOMSTRAD: | DNA_photolyase |
| PANDIT: | PF00875 |
| PROSITE: | PDOC00832 PDOC00331 |
| Pseudofam: | PF00875 |
| SCOP: | 1qnf |
| SYSTERS: | DNA_photolyase |
This tab holds annotation information from the InterPro database.
InterPro entry IPR006050
DNA photolyases are enzymes that bind to DNA containing pyrimidine dimers: on absorption of visible light, they catalyse dimer splitting into the constituent monomers, a process called photoreactivation [PUBMED:6325459]. This is a DNA repair mechanism, repairing mismatched pyrimidine dimers induced by exposure to ultra-violet light [PUBMED:3000886]. The precise mechanisms involved in substrate binding, conversion of light energy to the mechanical energy needed to rupture the cyclobutane ring, and subsequent release of the product are uncertain [PUBMED:6325459]. Analysis of DNA lyases has revealed the presence of an intrinsic chromophore, all monomers containing a reduced FAD moiety, and, in addition, either a reduced pterin or 8-hydroxy-5-diazaflavin as a second chromophore [PUBMED:3000886, PUBMED:2110564]. 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 [PUBMED:2110564].
This domain binds a light harvesting cofactor.
Gene Ontology
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
| Molecular function | DNA photolyase activity (GO:0003913) |
| Biological process | DNA repair (GO:0006281) |
Domain organisation
Below is a listing of the unique domain organisations or architectures in which this domain is found. More...
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Pfam Clan
This family is a member of clan HUP (CL0039), which contains the following 26 members:
Arginosuc_synth Asn_synthase ATP-sulfurylase ATP_bind_3 ATP_bind_4 Citrate_ly_lig CTP_transf_2 DNA_photolyase ETF FAD_syn HIGH_NTase1 NAD_synthase Pantoate_ligase PAPS_reduct QueC ThiI tRNA-synt_1 tRNA-synt_1_2 tRNA-synt_1b tRNA-synt_1c tRNA-synt_1d tRNA-synt_1e tRNA-synt_1f tRNA-synt_1g tRNA_Me_trans UspAlignments
We store a range of different sequence alignments for families. As well as the seed alignment from which the family is built, we provide the full alignment, generated by searching the sequence database using the family HMM. We also generate alignments using four representative proteomes (RP) sets, the NCBI sequence database, and our metagenomics sequence database. More...
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We make a range of alignments for each Pfam-A family. You can see a description of each above. You can view these alignments in various ways but please note that some types of alignment are never generated while others may not be available for all families, most commonly because the alignments are too large to handle.
| Seed (143) |
Full (3841) |
Representative proteomes | NCBI (3283) |
Meta (3027) |
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| RP15 (406) |
RP35 (772) |
RP55 (1048) |
RP75 (1233) |
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| PP/heatmap | 1 | |||||||
| Pfam viewer | ||||||||
1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key:
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We make all of our alignments available in Stockholm format. You can download them here as raw, plain text files or as gzip-compressed files.
| Seed (143) |
Full (3841) |
Representative proteomes | NCBI (3283) |
Meta (3027) |
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|---|---|---|---|---|---|---|---|---|
| RP15 (406) |
RP35 (772) |
RP55 (1048) |
RP75 (1233) |
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| Raw Stockholm | ||||||||
| Gzipped | ||||||||
You can also download a FASTA format file containing the full-length sequences for all sequences in the full alignment.
External links
MyHits provides a collection of tools to handle multiple sequence alignments. For example, one can refine a seed alignment (sequence addition or removal, re-alignment or manual edition) and then search databases for remote homologs using HMMER3.
HMM logo
HMM logos is one way of visualising profile HMMs. Logos provide a quick overview of the properties of an HMM in a graphical form. You can see a more detailed description of HMM logos and find out how you can interpret them here. More...
Trees
This page displays the phylogenetic tree for this family's seed alignment. We use FastTree to calculate neighbour join trees with a local bootstrap based on 100 resamples (shown next to the tree nodes). FastTree calculates approximately-maximum-likelihood phylogenetic trees from our seed alignment.
Note: You can also download the data file for the tree.
Curation and family details
This section shows the detailed information about the Pfam family. You can see the definitions of many of the terms in this section in the glossary and a fuller explanation of the scoring system that we use in the scores section of the help pages.
Curation
| Seed source: | Pfam-B_777 (release 3.0) |
| Previous IDs: | none |
| Type: | Domain |
| Author: | Bateman A, Griffiths-Jones SR |
| Number in seed: | 143 |
| Number in full: | 3841 |
| Average length of the domain: | 163.30 aa |
| Average identity of full alignment: | 23 % |
| Average coverage of the sequence by the domain: | 33.49 % |
HMM information
| HMM build commands: |
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 23193494 -E 1000 --cpu 4 HMM pfamseq
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| Model details: |
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| Model length: | 165 | ||||||||||||
| Family (HMM) version: | 13 | ||||||||||||
| Download: | download the raw HMM for this family |
Species distribution
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Interactions
There is 1 interaction for this family. More...
FAD_binding_7Structures
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the DNA_photolyase domain has been found. There are 52 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein seqence.
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Archea
Eukaryota
Bacteria
Other sequences
Viruses
Unclassified
Viroids
Unclassified sequence