Deoxyribodipyrimidine photo-lyase
Details
- Name
- Deoxyribodipyrimidine photo-lyase
- Synonyms
- 4.1.99.3
- DNA photolyase
- Photoreactivating enzyme
- Gene Name
- phr
- Organism
- Thermus thermophilus (strain HB8 / ATCC 27634 / DSM 579)
- Amino acid sequence
>lcl|BSEQ0011419|Deoxyribodipyrimidine photo-lyase MGPLLVWHRGDLRLHDHPALLEALARGPVVGLVVLDPNNLKTTPRRRAWFLENVRALREA YRARGGALWVLEGLPWEKVPEAARRLKAKAVYALTSHTPYGRYRDGRVREALPVPLHLLP APHLLPPDLPRAYRVYTPFSRLYRGAAPPLPPPEALPKGPEEGEIPREDPGLPLPEPGEE AALAGLRAFLEAKLPRYAEERDRLDGEGGSRLSPYFALGVLSPRLAAWEAERRGGEGARK WVAELLWRDFSYHLLYHFPWMAERPLDPRFQAFPWQEDEALFQAWYEGKTGVPLVDAAMR ELHATGFLSNRARMNAAQFAVKHLLLPWKRCEEAFRHLLLDGDRAVNLQGWQWAGGLGVD AAPYFRVFNPVLQGERHDPEGRWLKRWAPEYPSYAPKDPVVDLEEARRRYLRLARDLARG
- Number of residues
- 420
- Molecular Weight
- 47900.455
- Theoretical pI
- 9.66
- GO Classification
- Functionsdeoxyribodipyrimidine photo-lyase activity / DNA binding / nucleotide bindingProcessesDNA repair / protein-chromophore linkage
- General Function
- Nucleotide binding
- Specific Function
- Involved in repair of UV radiation-induced DNA damage. Catalyzes the light-dependent monomerization (300-600 nm) of cyclobutyl pyrimidine dimers (in cis-syn configuration), which are formed between adjacent bases on the same DNA strand upon exposure to ultraviolet radiation (By similarity).
- Pfam Domain Function
- Transmembrane Regions
- Not Available
- Cellular Location
- Not Available
- Gene sequence
>lcl|BSEQ0011420|Deoxyribodipyrimidine photo-lyase (phr) ATGGGCCCCCTTCTCGTCTGGCACCGGGGCGACCTCCGCCTCCACGACCACCCGGCCCTC CTGGAGGCCCTGGCCCGGGGGCCGGTGGTGGGCCTCGTGGTCCTGGACCCCAACAACCTG AAGACCACCCCGAGGCGGCGGGCCTGGTTCCTGGAAAACGTCCGGGCCCTGCGGGAGGCC TACCGGGCCCGGGGCGGGGCCCTTTGGGTCCTGGAGGGCCTCCCTTGGGAGAAGGTGCCC GAGGCGGCGAGGCGGCTTAAGGCCAAGGCCGTCTACGCCCTCACGAGCCACACCCCTTAC GGCCGCTACCGGGACGGGAGGGTGCGGGAGGCCCTCCCCGTGCCCCTCCACCTCCTCCCC GCCCCCCACCTCCTCCCCCCCGACCTCCCCCGGGCCTACCGGGTTTACACCCCCTTTAGC CGCCTCTACCGGGGGGCCGCCCCGCCCCTTCCCCCTCCCGAGGCCCTGCCCAAGGGGCCA GAGGAGGGGGAAATCCCCCGGGAAGACCCGGGGCTTCCCCTCCCCGAGCCGGGGGAGGAG GCGGCCCTCGCGGGGCTTCGGGCCTTCCTCGAGGCCAAGCTCCCCCGCTACGCCGAGGAG CGGGACCGGCTGGACGGAGAGGGGGGCTCGAGGCTCTCCCCCTACTTCGCCCTAGGGGTC CTCTCCCCCAGGCTCGCCGCCTGGGAGGCGGAAAGGCGGGGCGGGGAGGGAGCGAGGAAG TGGGTGGCGGAGCTCCTCTGGCGGGACTTCTCCTACCACCTCCTCTACCACTTCCCCTGG ATGGCGGAAAGGCCCCTGGACCCGAGGTTCCAGGCCTTCCCCTGGCAGGAGGACGAGGCC CTCTTCCAAGCTTGGTACGAGGGGAAGACGGGCGTCCCCCTGGTGGACGCCGCCATGCGG GAGCTCCACGCCACGGGCTTCCTCTCCAACCGGGCCCGGATGAACGCGGCCCAGTTCGCG GTGAAGCACCTCCTCCTCCCCTGGAAAAGGTGCGAGGAGGCCTTCCGCCACCTCCTCCTG GACGGGGACCGGGCGGTGAACCTCCAGGGCTGGCAGTGGGCGGGGGGCCTGGGGGTGGAC GCCGCCCCCTACTTCCGGGTCTTCAACCCGGTGCTCCAGGGGGAAAGGCACGACCCCGAG GGGAGGTGGCTTAAGCGCTGGGCCCCGGAATACCCCTCCTACGCCCCCAAGGACCCCGTG GTGGACCTGGAGGAGGCGAGAAGGCGCTACCTGCGCCTGGCGAGGGATCTCGCCCGAGGG TAG
- Chromosome Location
- Not Available
- Locus
- Not Available
- External Identifiers
Resource Link UniProtKB ID P61497 UniProtKB Entry Name PHR_THET8 GenBank Protein ID 15080709 GenBank Gene ID AB064548 - General References
- Torizawa T, Ueda T, Kuramitsu S, Hitomi K, Todo T, Iwai S, Morikawa K, Shimada I: Investigation of the cyclobutane pyrimidine dimer (CPD) photolyase DNA recognition mechanism by NMR analyses. J Biol Chem. 2004 Jul 30;279(31):32950-6. Epub 2004 May 28. [Article]
- Weber S: Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase. Biochim Biophys Acta. 2005 Feb 25;1707(1):1-23. [Article]
- Komori H, Masui R, Kuramitsu S, Yokoyama S, Shibata T, Inoue Y, Miki K: Crystal structure of thermostable DNA photolyase: pyrimidine-dimer recognition mechanism. Proc Natl Acad Sci U S A. 2001 Nov 20;98(24):13560-5. Epub 2001 Nov 13. [Article]