Description:
Deoxyribodipyrimidine photo-lyase, mitochondrial precursor(EC 4.1.99.3) (DNA photolyase) (Photoreactivating enzyme).
Molecular weight: 66274
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
photoreactive repair( GO:0000719 ) DNA repair( GO:0006281 )
Important dates:
13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
13-AUG-1987, sequence version 1.
07-MAR-2006, entry version 70.
Phylogenetic order:
Eukaryota Fungi Ascomycota Saccharomycotina Saccharomycetes Saccharomycetales Saccharomycetaceae Saccharomyces.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein PHR_YEAST:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X03183 | CAA26944.1 | - |
| EMBL | M11578 | AAA34875.1 | - |
| EMBL | Z75294 | CAA99718.1 | - |
| PIR | S67298 | S67298. | |
| HSSP | P00914 | 1DNP | |
| IntAct | P05066 | -.1 | |
| GermOnline | 143974 | -.1 | |
| Ensembl | YOR386W | Saccharomyces cerevisiae.1 | |
| GenomeReviews | Y13140_GR | YOR386W.1 | |
| SGD | S000005913 | PHR1. | |
| BioCyc | SCER-S28-01:SCER-S28-01-005846-MONOMER | -.1 | |
| LinkHub | P05066 | -.1 | |
| GO | GO:0005739 | C:mitochondrion | IDA. |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0003904 | F:deoxyribodipyrimidine photo-lyase activity | IDA. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0000719 | P:photoreactive repair | TAS. |
| InterPro | IPR002081 | DNA_photolyase_1. | |
| InterPro | IPR006050 | DNA_photolyase_N. | |
| InterPro | IPR006051 | FAD_bd_N. | |
| InterPro | IPR005101 | Photolyse_FAD_bd. | |
| Pfam | PF00875 | DNA_photolyase | 1. |
| Pfam | PF03441 | FAD_binding_7 | 1. |
| PRINTS | PR00147 | DNAPHOTLYASE. | |
| ProDom | PD004390 | FAD_binding_N | 1. |
| PROSITE | PS00394 | DNA_PHOTOLYASES_1_1 | 1. |
| PROSITE | PS00691 | DNA_PHOTOLYASES_1_2 | 1. |
Keywords:
Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Mitochondrion; Nuclear protein; Nucleotide-binding; Transit peptide.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=86067229; PubMed=3906569;
RA Sancar G.B.;
RT "Sequence of the Saccharomyces cerevisiae PHR1 gene and homology of
RT the PHR1 photolyase to E. coli photolyase.";
RL Nucleic Acids Res. 13:8231-8246(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=86083177; PubMed=3000886; DOI=10.1016/0378-1119(85)90190-8;
RA Yasui A., Langeveld S.A.;
RT "Homology between the photoreactivation genes of Saccharomyces
RT cerevisiae and Escherichia coli.";
RL Gene 36:349-355(1985).
RN [3]
RP CHARACTERIZATION.
RX MEDLINE=88058876; PubMed=3316199;
RA Sancar G.B., Smith F.W., Heelis P.F.;
RT "Purification of the yeast PHR1 photolyase from an Escherichia coli
RT overproducing strain and characterization of the intrinsic
RT chromophores of the enzyme.";
RL J. Biol. Chem. 262:15457-15465(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX MEDLINE=97313270; PubMed=9169874;
RA Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W.,
RA Arino J., Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R.,
RA Boyer J., Camasses A., Casamayor A., Casas C., Cheret G.,
RA Cziepluch C., Daignan-Fornier B., Dang V.-D., de Haan M., Delius H.,
RA Durand P., Fairhead C., Feldmann H., Gaillon L., Galisson F.,
RA Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E., Grivell L.A.,
RA Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J.,
RA Maarse A.C., Madania A., Mannhaupt G., Marck C., Martin R.P.,
RA Mewes H.-W., Michaux G., Paces V., Parle-McDermott A.G., Pearson B.M.,
RA Perrin A., Pettersson B., Poch O., Pohl T.M., Poirey R.,
RA Portetelle D., Pujol A., Purnelle B., Ramezani Rad M., Rechmann S.,
RA Schwager C., Schweizer M., Sor F., Sterky F., Tarassov I.A.,
RA Teodoru C., Tettelin H., Thierry A., Tobiasch E., Tzermia M.,
RA Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I., Vlcek C.,
RA Voet M., Volckaert G., Voss H., Wambutt R., Wedler H., Wiemann S.,
RA Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL Nature 387:98-102(1997).
RN [5]
RP MUTAGENESIS OF TRP-387; LYS-463 AND ARG-507.
RA Baer M.E., Sancar G.B.;
RT "The role of conserved amino acids in substrate binding and
RT discrimination by photolyase.";
RL J. Biol. Chem. 268:16717-16724(1993).
RN [6]
RP LEVEL OF PROTEIN EXPRESSION.
RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A.,
RA Dephoure N., O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [7]
RP REVIEW.
RX PubMed=15721603; DOI=10.1016/j.bbabio.2004.02.010;
RA Weber S.;
RT "Light-driven enzymatic catalysis of DNA repair: a review of recent
RT biophysical studies on photolyase.";
RL Biochim. Biophys. Acta 1707:1-23(2005).
Feature:
TRANSIT 1 ? Mitochondrion.
CHAIN ? 565 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000024051.
NP_BIND 338 342 FAD (By similarity).
NP_BIND 482 484 FAD (By similarity).
REGION 384 391 Interaction with DNA (By similarity).
REGION 451 452 Interaction with DNA (By similarity).
BINDING 326 326 FAD (By similarity).
BINDING 514 514 DNA (By similarity).
SITE 416 416 Electron transfer via tryptophanyl
radical (By similarity).
SITE 469 469 Electron transfer via tryptophanyl
radical (By similarity).
SITE 492 492 Electron transfer via tryptophanyl
radical (By similarity).
MUTAGEN 387 387 W->A: Reduces substrate binding 100-fold.
Reduces quantum yield for dimer
photolysis 3-fold.
MUTAGEN 463 463 K->A: Reduces substrate binding 100-fold.
MUTAGEN 507 507 R->A: Reduces substrate binding 100-fold.
MUTAGEN 517 517 K->A: Reduces substrate binding 10-fold.
CONFLICT 77 77 V -> A (in Ref. 2).
CONFLICT 165 165 T -> S (in Ref. 2).
CONFLICT 169 169 S -> T (in Ref. 2).
CONFLICT 200 200 D -> S (in Ref. 2).
CONFLICT 351 351 S -> R (in Ref. 2).
CONFLICT 365 365 G -> E (in Ref. 2).
CONFLICT 473 473 E -> K (in Ref. 2).
Comments:
-!- 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.
-!- CATALYTIC ACTIVITY: Cyclobutadipyrimidine (in DNA) = 2 pyrimidine
residues (in DNA).
-!- COFACTOR: Binds 1 FAD per subunit.
-!- COFACTOR: Binds 1 5,10-methenyltetrahydrofolate noncovalently per
subunit.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Absorption:
Abs(max)=377 nm;
Note=Has a fluorescence excitation maximum at 390 nm and an
emission maximum at 475 nm;
-!- SUBUNIT: Monomer (By similarity).
-!- INTERACTION:
P15179:MSD1; NbExp=1; IntAct=EBI-13385, EBI-18659;
-!- SUBCELLULAR LOCATION: Nuclear and mitochondrial.
-!- MISCELLANEOUS: There are only 150-300 molecules of photolyase per
yeast cell.
-!- MISCELLANEOUS: Present with 688 molecules/cell.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
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Sequence length: 565
MKRTVISSSN AYASKRSRLD IEHDFEQYHS LNKKYYPRPI TRTGANQFNN KSRAKPMEIV
EKLQKKQKTS FENVSTVMHW FRNDLRLYDN VGLYKSVALF QQLRQKNAKA KLYAVYVINE
DDWRAHMDSG WKLMFIMGAL KNLQQSLAEL HIPLLLWEFH TPKSTLSNSK EFVEFFKEKC
MNVSSGTGTI ITANIEYQTD ELYRDIRLLE NEDHRLQLKY YHDSCIVAPG LITTDRGTNY
SVFTPWYKKW VLYVNNYKKS TSEICHLHII EPLKYNETFE LKPFQYSLPD EFLQYIPKSK
WCLPDVSEEA ALSRLKDFLG TKSSKYNNEK DMLYLGGTSG LSVYITTGRI STRLIVNQAF
QSCNGQIMSK ALKDNSSTQN FIKEVAWRDF YRHCMCNWPY TSMGMPYRLD TLDIKWENNP
VAFEKWCTGN TGIPIVDAIM RKLLYTGYIN NRSRMITASF LSKNLLIDWR WGERWFMKHL
IDGDSSSNVG GWGFCSSTGI DAQPYFRVFN MDIQAKKYDP QMIFVKQWVP ELISSENKRP
ENYPKPLVDL KHSRERALKV YKDAM