Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

P05066

- PHR_YEAST

UniProt

P05066 - PHR_YEAST

Protein

Deoxyribodipyrimidine photo-lyase, mitochondrial

Gene

PHR1

Organism
Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
    • Align
    • Format
    • Add to basket
    • History
      Entry version 142 (01 Oct 2014)
      Sequence version 1 (13 Aug 1987)
      Previous versions | rss
    • Help video
    • Feedback
    • Comment

    Functioni

    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.

    Catalytic activityi

    Cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in DNA).

    Cofactori

    Binds 1 FAD per subunit.
    Binds 1 5,10-methenyltetrahydrofolate non-covalently per subunit.

    Absorptioni

    Abs(max)=377 nm

    Has a fluorescence excitation maximum at 390 nm and an emission maximum at 475 nm.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei326 – 3261FADBy similarity
    Sitei416 – 4161Electron transfer via tryptophanyl radicalBy similarity
    Sitei469 – 4691Electron transfer via tryptophanyl radicalBy similarity
    Sitei492 – 4921Electron transfer via tryptophanyl radicalBy similarity
    Binding sitei514 – 5141DNABy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi338 – 3425FADBy similarity
    Nucleotide bindingi482 – 4843FADBy similarity

    GO - Molecular functioni

    1. deoxyribodipyrimidine photo-lyase activity Source: SGD
    2. DNA binding Source: UniProtKB-KW
    3. mRNA binding Source: SGD
    4. nucleotide binding Source: UniProtKB-KW

    GO - Biological processi

    1. photoreactive repair Source: SGD
    2. protein-chromophore linkage Source: UniProtKB-KW

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    DNA damage, DNA repair

    Keywords - Ligandi

    Chromophore, DNA-binding, FAD, Flavoprotein, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciYEAST:G3O-33848-MONOMER.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Deoxyribodipyrimidine photo-lyase, mitochondrial (EC:4.1.99.3)
    Alternative name(s):
    DNA photolyase
    Photoreactivating enzyme
    Gene namesi
    Name:PHR1
    Ordered Locus Names:YOR386W
    OrganismiSaccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
    Taxonomic identifieri559292 [NCBI]
    Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaSaccharomycotinaSaccharomycetesSaccharomycetalesSaccharomycetaceaeSaccharomyces
    ProteomesiUP000002311: Chromosome XV

    Organism-specific databases

    CYGDiYOR386w.
    SGDiS000005913. PHR1.

    Subcellular locationi

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi387 – 3871W → A: Reduces substrate binding 100-fold. Reduces quantum yield for dimer photolysis 3-fold. 1 Publication
    Mutagenesisi463 – 4631K → A: Reduces substrate binding 100-fold. 1 Publication
    Mutagenesisi507 – 5071R → A: Reduces substrate binding 100-fold. 1 Publication
    Mutagenesisi517 – 5171K → A: Reduces substrate binding 10-fold.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini? – 565Deoxyribodipyrimidine photo-lyase, mitochondrialPRO_0000024051
    Transit peptidei1 – ?Mitochondrion

    Proteomic databases

    MaxQBiP05066.
    PaxDbiP05066.
    PeptideAtlasiP05066.

    Expressioni

    Gene expression databases

    GenevestigatoriP05066.

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Protein-protein interaction databases

    BioGridi34767. 14 interactions.
    DIPiDIP-6327N.
    IntActiP05066. 14 interactions.
    MINTiMINT-688138.
    STRINGi4932.YOR386W.

    Structurei

    3D structure databases

    ProteinModelPortaliP05066.
    SMRiP05066. Positions 75-562.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini75 – 226152Photolyase/cryptochrome alpha/betaAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni384 – 3918Interaction with DNABy similarity
    Regioni451 – 4522Interaction with DNABy similarity

    Sequence similaritiesi

    Belongs to the DNA photolyase class-1 family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0415.
    GeneTreeiENSGT00500000044813.
    HOGENOMiHOG000245621.
    KOiK01669.
    OMAiYIRAFVP.
    OrthoDBiEOG7K3TWX.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR002081. Cryptochrome/DNA_photolyase_1.
    IPR018394. DNA_photolyase_1_CS_C.
    IPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PfamiPF00875. DNA_photolyase. 1 hit.
    PF03441. FAD_binding_7. 1 hit.
    [Graphical view]
    PRINTSiPR00147. DNAPHOTLYASE.
    SUPFAMiSSF48173. SSF48173. 1 hit.
    SSF52425. SSF52425. 1 hit.
    PROSITEiPS00394. DNA_PHOTOLYASES_1_1. 1 hit.
    PS00691. DNA_PHOTOLYASES_1_2. 1 hit.
    PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P05066-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKRTVISSSN AYASKRSRLD IEHDFEQYHS LNKKYYPRPI TRTGANQFNN    50
    KSRAKPMEIV EKLQKKQKTS FENVSTVMHW FRNDLRLYDN VGLYKSVALF 100
    QQLRQKNAKA KLYAVYVINE DDWRAHMDSG WKLMFIMGAL KNLQQSLAEL 150
    HIPLLLWEFH TPKSTLSNSK EFVEFFKEKC MNVSSGTGTI ITANIEYQTD 200
    ELYRDIRLLE NEDHRLQLKY YHDSCIVAPG LITTDRGTNY SVFTPWYKKW 250
    VLYVNNYKKS TSEICHLHII EPLKYNETFE LKPFQYSLPD EFLQYIPKSK 300
    WCLPDVSEEA ALSRLKDFLG TKSSKYNNEK DMLYLGGTSG LSVYITTGRI 350
    STRLIVNQAF QSCNGQIMSK ALKDNSSTQN FIKEVAWRDF YRHCMCNWPY 400
    TSMGMPYRLD TLDIKWENNP VAFEKWCTGN TGIPIVDAIM RKLLYTGYIN 450
    NRSRMITASF LSKNLLIDWR WGERWFMKHL IDGDSSSNVG GWGFCSSTGI 500
    DAQPYFRVFN MDIQAKKYDP QMIFVKQWVP ELISSENKRP ENYPKPLVDL 550
    KHSRERALKV YKDAM 565
    Length:565
    Mass (Da):66,274
    Last modified:August 13, 1987 - v1
    Checksum:iCD4FC3DA6128B97C
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti77 – 771V → A in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti165 – 1651T → S in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti169 – 1691S → T in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti200 – 2001D → S in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti351 – 3511S → R in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti365 – 3651G → E in AAA34875. (PubMed:3000886)Curated
    Sequence conflicti473 – 4731E → K in AAA34875. (PubMed:3000886)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03183 Genomic DNA. Translation: CAA26944.1.
    M11578 Genomic DNA. Translation: AAA34875.1.
    Z75294 Genomic DNA. Translation: CAA99718.1.
    BK006948 Genomic DNA. Translation: DAA11145.1.
    PIRiS67298.
    RefSeqiNP_015031.1. NM_001183806.1.

    Genome annotation databases

    EnsemblFungiiYOR386W; YOR386W; YOR386W.
    GeneIDi854568.
    KEGGisce:YOR386W.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X03183 Genomic DNA. Translation: CAA26944.1 .
    M11578 Genomic DNA. Translation: AAA34875.1 .
    Z75294 Genomic DNA. Translation: CAA99718.1 .
    BK006948 Genomic DNA. Translation: DAA11145.1 .
    PIRi S67298.
    RefSeqi NP_015031.1. NM_001183806.1.

    3D structure databases

    ProteinModelPortali P05066.
    SMRi P05066. Positions 75-562.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 34767. 14 interactions.
    DIPi DIP-6327N.
    IntActi P05066. 14 interactions.
    MINTi MINT-688138.
    STRINGi 4932.YOR386W.

    Proteomic databases

    MaxQBi P05066.
    PaxDbi P05066.
    PeptideAtlasi P05066.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblFungii YOR386W ; YOR386W ; YOR386W .
    GeneIDi 854568.
    KEGGi sce:YOR386W.

    Organism-specific databases

    CYGDi YOR386w.
    SGDi S000005913. PHR1.

    Phylogenomic databases

    eggNOGi COG0415.
    GeneTreei ENSGT00500000044813.
    HOGENOMi HOG000245621.
    KOi K01669.
    OMAi YIRAFVP.
    OrthoDBi EOG7K3TWX.

    Enzyme and pathway databases

    BioCyci YEAST:G3O-33848-MONOMER.

    Miscellaneous databases

    NextBioi 977015.
    PROi P05066.

    Gene expression databases

    Genevestigatori P05066.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    InterProi IPR002081. Cryptochrome/DNA_photolyase_1.
    IPR018394. DNA_photolyase_1_CS_C.
    IPR006050. DNA_photolyase_N.
    IPR005101. Photolyase_FAD-bd/Cryptochr_C.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF00875. DNA_photolyase. 1 hit.
    PF03441. FAD_binding_7. 1 hit.
    [Graphical view ]
    PRINTSi PR00147. DNAPHOTLYASE.
    SUPFAMi SSF48173. SSF48173. 1 hit.
    SSF52425. SSF52425. 1 hit.
    PROSITEi PS00394. DNA_PHOTOLYASES_1_1. 1 hit.
    PS00691. DNA_PHOTOLYASES_1_2. 1 hit.
    PS51645. PHR_CRY_ALPHA_BETA. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence of the Saccharomyces cerevisiae PHR1 gene and homology of the PHR1 photolyase to E. coli photolyase."
      Sancar G.B.
      Nucleic Acids Res. 13:8231-8246(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Homology between the photoreactivation genes of Saccharomyces cerevisiae and Escherichia coli."
      Yasui A., Langeveld S.A.
      Gene 36:349-355(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "Purification of the yeast PHR1 photolyase from an Escherichia coli overproducing strain and characterization of the intrinsic chromophores of the enzyme."
      Sancar G.B., Smith F.W., Heelis P.F.
      J. Biol. Chem. 262:15457-15465(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV."
      Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A., Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B., Dang V.-D.
      , de Haan M., Delius H., Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U., Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B., Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A., Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.
      Nature 387:98-102(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 204508 / S288c.
    5. Cited for: GENOME REANNOTATION.
      Strain: ATCC 204508 / S288c.
    6. "The role of conserved amino acids in substrate binding and discrimination by photolyase."
      Baer M.E., Sancar G.B.
      J. Biol. Chem. 268:16717-16724(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TRP-387; LYS-463 AND ARG-507.
    7. Cited for: LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
    8. "Light-driven enzymatic catalysis of DNA repair: a review of recent biophysical studies on photolyase."
      Weber S.
      Biochim. Biophys. Acta 1707:1-23(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: REVIEW.

    Entry informationi

    Entry nameiPHR_YEAST
    AccessioniPrimary (citable) accession number: P05066
    Secondary accession number(s): D6W379
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 13, 1987
    Last sequence update: August 13, 1987
    Last modified: October 1, 2014
    This is version 142 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programFungal Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    There are only 150-300 molecules of photolyase per yeast cell.
    Present with 688 molecules/cell in log phase SD medium.1 Publication

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. SIMILARITY comments
      Index of protein domains and families
    2. Yeast
      Yeast (Saccharomyces cerevisiae): entries, gene names and cross-references to SGD
    3. Yeast chromosome XV
      Yeast (Saccharomyces cerevisiae) chromosome XV: entries and gene names

    External Data

    Dasty 3