ID A0A2G5IAG6_CERBT Unreviewed; 609 AA.
AC A0A2G5IAG6;
DT 31-JAN-2018, integrated into UniProtKB/TrEMBL.
DT 31-JAN-2018, sequence version 1.
DT 13-SEP-2023, entry version 21.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
GN ORFNames=CB0940_01502 {ECO:0000313|EMBL:PIB01837.1};
OS Cercospora beticola (Sugarbeet leaf spot fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Cercospora.
OX NCBI_TaxID=122368 {ECO:0000313|EMBL:PIB01837.1, ECO:0000313|Proteomes:UP000230605};
RN [1] {ECO:0000313|EMBL:PIB01837.1, ECO:0000313|Proteomes:UP000230605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=09-40 {ECO:0000313|EMBL:PIB01837.1,
RC ECO:0000313|Proteomes:UP000230605};
RA De Jonge R., Ebert M.K., Suttle J.C., Jurick Ii W.M., Secor G.A.,
RA Thomma B.P., Van De Peer Y., Bolton M.D.;
RT "The cercosporin biosynthetic gene cluster was horizontally transferred to
RT several fungal lineages and shown to be expanded in Cercospora beticola
RT based on microsynteny with recipient genomes.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: May have a photoreceptor function.
CC {ECO:0000256|RuleBase:RU367151}.
CC -!- COFACTOR:
CC Name=(6R)-5,10-methylene-5,6,7,8-tetrahydrofolate;
CC Xref=ChEBI:CHEBI:15636; Evidence={ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 5,10-methenyltetrahydrofolate (MTHF) per subunit.
CC {ECO:0000256|RuleBase:RU367151};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC Note=Binds 1 FAD per subunit. {ECO:0000256|PIRSR:PIRSR602081-1,
CC ECO:0000256|RuleBase:RU367151};
CC -!- SIMILARITY: Belongs to the DNA photolyase class-1 family.
CC {ECO:0000256|ARBA:ARBA00005862, ECO:0000256|RuleBase:RU367151}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PIB01837.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; LKMD01000100; PIB01837.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2G5IAG6; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000230605; Chromosome 1.
DR GO; GO:0003913; F:DNA photolyase activity; IEA:InterPro.
DR GO; GO:0006281; P:DNA repair; IEA:InterPro.
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; IPR014133; Cry_DASH.
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; IPR006050; DNA_photolyase_N.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR NCBIfam; TIGR02765; crypto_DASH; 1.
DR PANTHER; PTHR11455; CRYPTOCHROME; 1.
DR PANTHER; PTHR11455:SF22; CRYPTOCHROME DASH; 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; PS51645; PHR_CRY_ALPHA_BETA; 1.
PE 3: Inferred from homology;
KW Chromophore {ECO:0000256|RuleBase:RU367151};
KW FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRSR:PIRSR602081-1};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|PIRSR:PIRSR602081-
KW 1}.
FT DOMAIN 6..171
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 249..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 581..609
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 291
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 304..308
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 475..477
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
SQ SEQUENCE 609 AA; 68780 MW; AA7A67978FB21F9E CRC64;
MAGAQRVLVY LLRRDLRLAD NPIFNEIAKL NAQSKKPFTH VLPVYVYPAE QVEVSGFLAP
GQEKSPYKEA RSRVGNFWRC GTHRVKFLAE SVWDLKKDLQ KVQSDLIIRI GSVKDAVESI
LEGFRGKEGA ELHGLWMTSE EGWEEQNEEE AVKAMIEKDG KEFKLWVDEK YYIDDRDIPF
KDSRELPDVF TTYRKMVEPL RDAPRKELPK PEQLLPLPDH IPNQAAPFKI PSSYDEVLAA
LKKPLEEKPV DIKGPPKLPQ DAKSAHPFVG GSKAGHERVD HLIESGSMSS YKDTRNGLLG
LDFSTKLSAW LALGCISARQ VHWKLLDFEN GKGSRAQAAD GYGKGENKGT AAVRFELLWR
DYMRLCTRKF GMRLFFIDGY RGDADAVNKF ISSPYTHSTN KKNKKGVDDE NTRRVVERFL
NGTTGTGLID ASQRELWLTG WTSNRARQNV ASYLSKHLGI DWRLGAEWYE SNLIDYDVSS
NWGNWQYVAG VGNDPRGDAR VFNPVKQAVD YDTNGEYVRT WVPELRDVGR GEGGQQQGGG
DSMESLMGVF QAWRVPPEEK KRLGLEGVEF VESPLIRIDF SVNRRGGGRP RGRGRGRGGR
GGDRGRRGQ
//
