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   03-AUG-2022, entry version 138.
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 1257 /
OS   FGSC 987).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Sordariomycetidae; Sordariales; Sordariaceae; 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 photolyase
RT   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., Werner-Washburne M.,
RA   Selitrennikoff C.P., Kinsey J.A., Braun E.L., Zelter A., Schulte U.,
RA   Kothe G.O., Jedd G., Mewes H.-W., Staben C., Marcotte E., Greenberg D.,
RA   Roy A., Foley K., Naylor J., Stange-Thomann N., Barrett R., Gnerre S.,
RA   Kamal M., Kamvysselis M., Mauceli E.W., Bielke C., Rudd S., Frishman D.,
RA   Krystofova S., Rasmussen C., Metzenberg R.L., Perkins D.D., Kroken S.,
RA   Cogoni C., 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., Paulsen I.,
RA   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 cyclobutyl
CC       pyrimidine dimers (in cis-syn configuration), which are formed between
CC       adjacent bases on the same DNA strand upon exposure to ultraviolet
CC       radiation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cyclobutadipyrimidine (in DNA) = 2 pyrimidine residues (in
CC         DNA).; EC=4.1.99.3;
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC       Note=Binds 1 FAD per subunit.;
CC   -!- COFACTOR:
CC       Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC         Xref=ChEBI:CHEBI:15636;
CC       Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) non-covalently per
CC       subunit.;
CC   -!- SUBUNIT: Monomer.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA41549.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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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_964834.2; XM_959741.2.
DR   AlphaFoldDB; P27526; -.
DR   SMR; P27526; -.
DR   STRING; 5141.EFNCRP00000008626; -.
DR   EnsemblFungi; EAA35598; EAA35598; NCU08626.
DR   GeneID; 3880994; -.
DR   KEGG; ncr:NCU08626; -.
DR   VEuPathDB; FungiDB:NCU08626; -.
DR   HOGENOM; CLU_010348_2_1_1; -.
DR   InParanoid; P27526; -.
DR   Proteomes; UP000001805; Chromosome 1, Linkage Group I.
DR   GO; GO:0003904; F:deoxyribodipyrimidine photo-lyase activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0071949; F:FAD binding; IBA:GO_Central.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0009416; P:response to light stimulus; IBA:GO_Central.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR036134; Crypto/Photolyase_FAD-like_sf.
DR   InterPro; IPR036155; Crypto/Photolyase_N_sf.
DR   InterPro; IPR005101; Cryptochr/Photolyase_FAD-bd.
DR   InterPro; IPR002081; Cryptochrome/DNA_photolyase_1.
DR   InterPro; IPR018394; DNA_photolyase_1_CS_C.
DR   InterPro; IPR006050; DNA_photolyase_N.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR11455; PTHR11455; 1.
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; DNA damage; DNA repair; DNA-binding; FAD; Flavoprotein; Lyase;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..615
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085116"
FT   DOMAIN          108..249
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          1..53
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          407..414
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          474..475
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         356
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   BINDING         364..368
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         505..507
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         537
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   SITE            439
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            492
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            515
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
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