Description:
Deoxyribodipyrimidine photo-lyase (EC 4.1.99.3) (DNA photolyase)(Photoreactivating enzyme).
Molecular weight: 73076
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
01-AUG-1992, sequence version 1.
07-FEB-2006, entry version 49.
Phylogenetic order:
Eukaryota Fungi Ascomycota Pezizomycotina Sordariomycetes Sordariomycetidae Sordariales Sordariaceae Neurospora.
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_NEUCR:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | X58713 | CAA41549.1 | - |
| EMBL | AABX01000019 | EAA35598.1 | - |
| PIR | S18667 | S18667. | |
| HSSP | P00914 | 1DNP | |
| BioCyc | NCRA-XX3-01:NCRA-XX3-01-003485-MONOMER | -.1 | |
| 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; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase; Nucleotide-binding.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX MEDLINE=92020228; PubMed=1833725;
RA Yajima H., Inoue H., Oikawa A., Yasui A.;
RT "Cloning and functional characterization of a eucaryotic DNA
RT photolyase gene from Neurospora crassa.";
RL Nucleic Acids Res. 19:5359-5362(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=74-OR23-1A / FGSC 987;
RX MEDLINE=22598136; PubMed=12712197; DOI=10.1038/nature01554;
RA Galagan J.E., Calvo S.E., Borkovich K.A., Selker E.U., Read N.D.,
RA Jaffe D., FitzHugh W., Ma L.-J., Smirnov S., Purcell S., Rehman B.,
RA Elkins T., Engels R., Wang S., Nielsen C.B., Butler J., Endrizzi M.,
RA Qui D., Ianakiev P., Bell-Pedersen D., Nelson M.A.,
RA Werner-Washburne M., Selitrennikoff C.P., Kinsey J.A., Braun E.L.,
RA Zelter A., Schulte U., Kothe G.O., Jedd G., Mewes H.-W., Staben C.,
RA Marcotte E., Greenberg D., Roy A., Foley K., Naylor J.,
RA Stange-Thomann N., Barrett R., Gnerre S., Kamal M., Kamvysselis M.,
RA Mauceli E., Bielke C., Rudd S., Frishman D., Krystofova S.,
RA Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S., Cogoni C.,
RA Macino G., Catcheside D.E.A., Li W., Pratt R.J., Osmani S.A.,
RA DeSouza C.P.C., Glass N.L., Orbach M.J., Berglund J.A., Voelker R.,
RA Yarden O., Plamann M., Seiler S., Dunlap J.C., Radford A., Aramayo R.,
RA Natvig D.O., Alex L.A., Mannhaupt G., Ebbole D.J., Freitag M.,
RA Paulsen I., Sachs M.S., Lander E.S., Nusbaum C., Birren B.W.;
RT "The genome sequence of the filamentous fungus Neurospora crassa.";
RL Nature 422:859-868(2003).
Feature:
CHAIN 1 642 Deoxyribodipyrimidine photo-lyase.
/FTId=PRO_0000085116.
NP_BIND 391 395 FAD (By similarity).
NP_BIND 532 534 FAD (By similarity).
REGION 434 441 Interaction with DNA (By similarity).
REGION 501 502 Interaction with DNA (By similarity).
BINDING 379 379 FAD (By similarity).
BINDING 383 383 DNA (By similarity).
BINDING 564 564 DNA (By similarity).
SITE 466 466 Electron transfer via tryptophanyl
radical (By similarity).
SITE 519 519 Electron transfer via tryptophanyl
radical (By similarity).
SITE 542 542 Electron transfer via tryptophanyl
radical (By similarity).
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.
-!- SUBUNIT: Monomer.
-!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
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Sequence length: 642
MFRTIRTLTP TTSVFPPTSL HFKLKTTMAP SKRKASAPPQ TSHVNGNPSA DKKRKTTTDA
PPTNPNTSSD PLRAPHPFYK DSETHGIVLR KFYPHEMSNA RAQAYNDNEL PRPIETLSAA
LAETAALRKS LPVRQAVVHW FKMDLRLHDN RSLWLASQKA KEAGVPLICL YVLSPEDLEA
HLRAPIRVDF MLRTLEVLKT DLEDLGIPLW VETVEKRKEV PTKIKELMKS WGASHLFCAM
EYEVDELRRE AKLVKLLAEG EKGEKMAADV VHDTCVVMPG ALQSGSGGQY AVYSPWFRAW
IKHIEENPEC LEIYEKPGPN PPGTKEKHEN LFACSIPEAP EGKRLRDDEK ARYHSLWPAG
EHEALKRLEK FCDEAIGKYA ERRNIPAMQG TSNLSVHFAS GTLSARTAIR TARDRNNTKK
LNGGNEGIQR WISEVAWRDF YKHVLVHWPY VCMNKPFKPT YSNIEWSYNV DHFHAWTQGR
TGFPIIDAAM RQVLSTGYMH NRLRMIVASF LAKDLLVDWR MGERYFMEHL IDGDFASNNG
GWGFAASVGV DPQPYFRVFN PLLQSEKFDP DGDYIRKWVE ELRDLPELKG GKGGEIHDPY
GRGSEKVKKK LEEKGYPRPI VEHSGARDRA LDAYKRGLAR DL