ID Q6L8F6_COCMI Unreviewed; 634 AA.
AC Q6L8F6;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Photolyase {ECO:0000313|EMBL:BAD18969.1};
GN Name=PHR1 {ECO:0000313|EMBL:BAD18969.1};
OS Cochliobolus miyabeanus (Brown spot disease fungus) (Bipolaris oryzae).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=101162 {ECO:0000313|EMBL:BAD18969.1};
RN [1] {ECO:0000313|EMBL:BAD18969.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=D9/F6-69 {ECO:0000313|EMBL:BAD18969.1};
RX PubMed=15138697; DOI=10.1007/s00294-004-0507-7;
RA Kihara J., Moriwaki A., Matsuo N., Arase S., Honda Y.;
RT "Cloning, functional characterization, and near-ultraviolet radiation-
RT enhanced expression of a photolyase gene (PHR1) from the phytopathogenic
RT fungus Bipolaris oryzae.";
RL Curr. Genet. 46:37-46(2004).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862}.
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DR EMBL; AB126091; BAD18969.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6L8F6; -.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0097159; F:organic cyclic compound binding; IEA:UniProt.
DR GO; GO:0051716; P:cellular response to stimulus; IEA:UniProt.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; IEA:UniProt.
DR GO; GO:0006950; P:response to stress; IEA:UniProt.
DR Gene3D; 1.25.40.80; -; 1.
DR Gene3D; 1.10.579.10; DNA Cyclobutane Dipyrimidine Photolyase, subunit A, domain 3; 1.
DR Gene3D; 3.40.50.620; HUPs; 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; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF18; DEOXYRIBODIPYRIMIDINE PHOTO-LYASE, MITOCHONDRIAL; 1.
DR Pfam; PF00875; DNA_photolyase; 1.
DR Pfam; PF03441; FAD_binding_7; 1.
DR PRINTS; PR00147; DNAPHOTLYASE.
DR SUPFAM; SSF48173; Cryptochrome/photolyase FAD-binding domain; 1.
DR SUPFAM; SSF52425; Cryptochrome/photolyase, N-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022991};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}; Lyase {ECO:0000313|EMBL:BAD18969.1}.
FT DOMAIN 137..274
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 11..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 61..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 377
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 389..393
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 429
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 432..439
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 530..532
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 464
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 517
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 540
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 634 AA; 72768 MW; 5315C10FD341CD8B CRC64;
MPPKRKSNGI PHNVKSANKY TDASGNAPNK RSRIAKPLDK ASTNSAPLID AIVRNSKNGA
PGDAVKKEEG NFDHSRPEER AGIVDRQYYP AEMSNERCAM YNANEIPRPI AILEKTLKDT
KQRRDKIQSG NENGHGDAVM HWFKRDLRVR DNTGLSKAAE LAKSKGIGLV AVWIMSPQDW
EAHLVSPPKC DFELRSVQLL KQELEELDIP LYIETVHERK NIKKRLVEMA LEWNVKSVFC
NLEYEPDELR REERLVRMML EKGINMDPQH DDCVVPPGSL KTGTGKQYAV YTPWYRAWIA
YLHAHPHLLN ERSMPEKNPT GFREKFTKLF DSRVPDLPDC KSLTAEEKER FHHLWPAGEA
AAIDRLERFL TEKVIKYKDT RNFPALNSTG RISAHHAAGT LAARTSVRMA RDINSVKKLD
GGKEGIKGWI GEVAWRDFYR HVLVHWPYVC MNKPFKYEYT NIEWEYNDAH FEAWTQGRTG
YPIVDAAMRC LKHTGYMHNR LRMITASFLA KHLLLDWRLG EQYFITHLID GDFASNNGGW
GFSASTGVDP QPYFRIFNPW TQSEKFDEQG EFIRLWVKEL EDVQGAAIHN PYQAKGEAAK
IAKKNGYPEP IVEHKFARER CLARYKAGIG RETA
//
