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Database: UniProt/SWISS-PROT
Entry: PHR_NEUCR
LinkDB: PHR_NEUCR
Original site: PHR_NEUCR 
ID   PHR_NEUCR               Reviewed;         615 AA.
AC   P27526; Q7RVL4;
DT   01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT   19-MAR-2014, sequence version 2.
DT   19-MAR-2014, entry version 103.
DE   RecName: Full=Deoxyribodipyrimidine photo-lyase;
DE            EC=4.1.99.3;
DE   AltName: Full=DNA photolyase;
DE   AltName: Full=Photoreactivating enzyme;
GN   Name=phr; ORFNames=NCU08626;
OS   Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM
OS   1257 / FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Sordariomycetidae; Sordariales; Sordariaceae;
OC   Neurospora.
OX   NCBI_TaxID=367110;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1833725; DOI=10.1093/nar/19.19.5359;
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=ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987;
RX   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.B., 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.W., 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).
CC   -!- FUNCTION: Involved in repair of UV radiation-induced DNA damage.
CC       Catalyzes the light-dependent monomerization (300-600 nm) of
CC       cyclobutyl pyrimidine dimers (in cis-syn configuration), which are
CC       formed between adjacent bases on the same DNA strand upon exposure
CC       to ultraviolet radiation.
CC   -!- CATALYTIC ACTIVITY: Cyclobutadipyrimidine (in DNA) = 2 pyrimidine
CC       residues (in DNA).
CC   -!- COFACTOR: Binds 1 FAD per subunit.
CC   -!- COFACTOR: Binds 1 5,10-methenyltetrahydrofolate non-covalently per
CC       subunit.
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC   -!- SIMILARITY: Contains 1 photolyase/cryptochrome alpha/beta domain.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA41549.1; Type=Erroneous initiation; Note=Translation N-terminally shortened;
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DR   EMBL; X58713; CAA41549.1; ALT_INIT; Genomic_DNA.
DR   EMBL; CM002236; EAA35598.2; -; Genomic_DNA.
DR   PIR; S18667; S18667.
DR   RefSeq; XP_964834.1; XM_959741.1.
DR   UniGene; Ncr.24426; -.
DR   ProteinModelPortal; P27526; -.
DR   STRING; 5141.NCU08626.1; -.
DR   EnsemblFungi; EFNCRT00000008644; EFNCRP00000008626; EFNCRG00000008630.
DR   GeneID; 3880994; -.
DR   KEGG; ncr:NCU08626; -.
DR   eggNOG; COG0415; -.
DR   HOGENOM; HOG000245621; -.
DR   KO; K01669; -.
DR   OMA; NGTRENG; -.
DR   OrthoDB; EOG7K3TWX; -.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0018298; P:protein-chromophore linkage; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR   InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR005101; Photolyase_FAD-bd/Cryptochr_C.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   Pfam; PF00875; DNA_photolyase; 1.
DR   Pfam; PF03441; FAD_binding_7; 1.
DR   PRINTS; PR00147; DNAPHOTLYASE.
DR   SUPFAM; SSF48173; SSF48173; 1.
DR   SUPFAM; SSF52425; SSF52425; 1.
DR   PROSITE; PS00394; DNA_PHOTOLYASES_1_1; 1.
DR   PROSITE; PS00691; DNA_PHOTOLYASES_1_2; 1.
DR   PROSITE; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE   3: Inferred from homology;
KW   Chromophore; Complete proteome; DNA damage; DNA repair; DNA-binding;
KW   FAD; Flavoprotein; Lyase; Nucleotide-binding; Reference proteome.
FT   CHAIN         1    615       Deoxyribodipyrimidine photo-lyase.
FT                                /FTId=PRO_0000085116.
FT   DOMAIN      108    249       Photolyase/cryptochrome alpha/beta.
FT   NP_BIND     364    368       FAD (By similarity).
FT   NP_BIND     505    507       FAD (By similarity).
FT   REGION      407    414       Interaction with DNA (By similarity).
FT   REGION      474    475       Interaction with DNA (By similarity).
FT   BINDING     352    352       FAD (By similarity).
FT   BINDING     356    356       DNA (By similarity).
FT   BINDING     537    537       DNA (By similarity).
FT   SITE        439    439       Electron transfer via tryptophanyl
FT                                radical (By similarity).
FT   SITE        492    492       Electron transfer via tryptophanyl
FT                                radical (By similarity).
FT   SITE        515    515       Electron transfer via tryptophanyl
FT                                radical (By similarity).
SQ   SEQUENCE   615 AA;  69972 MW;  90D7AAD9B0176026 CRC64;
     MAPSKRKASA PPQTSHVNGN PSADKKRKTT TDAPPTNPNT SSDPLRAPHP FYKDSETHGI
     VLRKFYPHEM SNARAQAYND NELPRPIETL SAALAETAAL RKSLPVRQAV VHWFKMDLRL
     HDNRSLWLAS QKAKEAGVPL ICLYVLSPED LEAHLRAPIR VDFMLRTLEV LKTDLEDLGI
     PLWVETVEKR KEVPTKIKEL MKSWGASHLF CAMEYEVDEL RREAKLVKLL AEGEKGEKMA
     ADVVHDTCVV MPGALQSGSG GQYAVYSPWF RAWIKHIEEN PECLEIYEKP GPNPPGTKEK
     HENLFACSIP EAPEGKRLRD DEKARYHSLW PAGEHEALKR LEKFCDEAIG KYAERRNIPA
     MQGTSNLSVH FASGTLSART AIRTARDRNN TKKLNGGNEG IQRWISEVAW RDFYKHVLVH
     WPYVCMNKPF KPTYSNIEWS YNVDHFHAWT QGRTGFPIID AAMRQVLSTG YMHNRLRMIV
     ASFLAKDLLV DWRMGERYFM EHLIDGDFAS NNGGWGFAAS VGVDPQPYFR VFNPLLQSEK
     FDPDGDYIRK WVEELRDLPE LKGGKGGEIH DPYGRGSEKV KKKLEEKGYP RPIVEHSGAR
     DRALDAYKRG LARDL
//
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