ID   PHR_STRGR               Reviewed;         455 AA.
AC   P12768;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1989, sequence version 1.
DT   03-AUG-2022, entry version 94.
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;
OS   Streptomyces griseus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1911;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2501760; DOI=10.1093/nar/17.12.4731;
RA   Kobayashi T., Takao M., Oikawa A., Yasui A.;
RT   "Molecular characterization of a gene encoding a photolyase from
RT   Streptomyces griseus.";
RL   Nucleic Acids Res. 17:4731-4744(1989).
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=coenzyme F420-(gamma-Glu)n; Xref=ChEBI:CHEBI:133980;
CC       Note=Binds 1 coenzyme F420 non-covalently per subunit.;
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC       {ECO:0000305}.
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DR   EMBL; X15060; CAA33161.1; -; Genomic_DNA.
DR   PIR; S05573; S05573.
DR   AlphaFoldDB; P12768; -.
DR   SMR; P12768; -.
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   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.
FT   CHAIN           1..455
FT                   /note="Deoxyribodipyrimidine photo-lyase"
FT                   /id="PRO_0000085111"
FT   DOMAIN          2..131
FT                   /note="Photolyase/cryptochrome alpha/beta"
FT   REGION          266..273
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   REGION          330..331
FT                   /note="Interaction with DNA"
FT                   /evidence="ECO:0000250"
FT   BINDING         219
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         231..235
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         361..363
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000250"
FT   BINDING         392
FT                   /ligand="DNA"
FT                   /ligand_id="ChEBI:CHEBI:16991"
FT                   /evidence="ECO:0000250"
FT   SITE            295
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            348
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
FT   SITE            371
FT                   /note="Electron transfer via tryptophanyl radical"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   455 AA;  50437 MW;  FEA88763DA45931A CRC64;
     MSVAVVLFTS DLRLHDNPVL RAALRDADEV VPLFVRDDAV HRAGFDAPNP LAFLADCLAA
     LDAGLRHRGG RLIVRRGEAA TEVRRVAEET GAARVHIAAG VSRYAARREQ RIREALADSG
     RELHVHDAVV TALAPGRVVP TGGKDHFAVF TPYFRRWEAE GVRGTQTAPR TVRVPDGVAS
     DPLPDRDCVE NLSPGLARGG EEAGRKLVTS WLNGPMADYE DGHDDLAGDA TSRLSPHLHF
     GTVSAAELVH RAREKGGLGG EAFVRQLAWR DFHHQVLADR PDASWSDYRP RHDRWRSDAD
     EMHAWKSGLT GYPLVDAAMR QLAHEGWMHN RARMLAASFL TKTLYVDWRE GARHFLDLLV
     DGDVANNQLN WQWVAGTGTD TRPNRVLNPV IQGKRFDARG DYVRGWVPEL AEVEGSAIHE
     PWKLQGLDRA GLDYPDPVVD LAEARARFER ARGLD