ID W7LJZ0_GIBM7 Unreviewed; 715 AA.
AC W7LJZ0;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=Cryptochrome DASH {ECO:0000256|RuleBase:RU367151};
GN ORFNames=FVEG_02442 {ECO:0000313|EMBL:EWG39713.1};
OS Gibberella moniliformis (strain M3125 / FGSC 7600) (Maize ear and stalk rot
OS fungus) (Fusarium verticillioides).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium fujikuroi species complex.
OX NCBI_TaxID=334819 {ECO:0000313|EMBL:EWG39713.1, ECO:0000313|Proteomes:UP000009096};
RN [1] {ECO:0000313|EMBL:EWG39713.1, ECO:0000313|Proteomes:UP000009096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M3125 / FGSC 7600 {ECO:0000313|Proteomes:UP000009096};
RX PubMed=20237561; DOI=10.1038/nature08850;
RA Ma L.J., van der Does H.C., Borkovich K.A., Coleman J.J., Daboussi M.J.,
RA Di Pietro A., Dufresne M., Freitag M., Grabherr M., Henrissat B.,
RA Houterman P.M., Kang S., Shim W.B., Woloshuk C., Xie X., Xu J.R.,
RA Antoniw J., Baker S.E., Bluhm B.H., Breakspear A., Brown D.W.,
RA Butchko R.A., Chapman S., Coulson R., Coutinho P.M., Danchin E.G.,
RA Diener A., Gale L.R., Gardiner D.M., Goff S., Hammond-Kosack K.E.,
RA Hilburn K., Hua-Van A., Jonkers W., Kazan K., Kodira C.D., Koehrsen M.,
RA Kumar L., Lee Y.H., Li L., Manners J.M., Miranda-Saavedra D., Mukherjee M.,
RA Park G., Park J., Park S.Y., Proctor R.H., Regev A., Ruiz-Roldan M.C.,
RA Sain D., Sakthikumar S., Sykes S., Schwartz D.C., Turgeon B.G.,
RA Wapinski I., Yoder O., Young S., Zeng Q., Zhou S., Galagan J., Cuomo C.A.,
RA Kistler H.C., Rep M.;
RT "Comparative genomics reveals mobile pathogenicity chromosomes in
RT Fusarium.";
RL Nature 464:367-373(2010).
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}.
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DR EMBL; DS022243; EWG39713.1; -; Genomic_DNA.
DR RefSeq; XP_018745904.1; XM_018889699.1.
DR AlphaFoldDB; W7LJZ0; -.
DR STRING; 334819.W7LJZ0; -.
DR EnsemblFungi; FVEG_02442T0; FVEG_02442T0; FVEG_02442.
DR GeneID; 30060650; -.
DR KEGG; fvr:FVEG_02442; -.
DR VEuPathDB; FungiDB:FVEG_02442; -.
DR eggNOG; KOG0133; Eukaryota.
DR HOGENOM; CLU_010348_6_1_1; -.
DR OMA; LIFELLW; -.
DR OrthoDB; 124765at2759; -.
DR Proteomes; UP000009096; Chromosome 6.
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}; Reference proteome {ECO:0000313|Proteomes:UP000009096}.
FT DOMAIN 5..164
FT /note="Photolyase/cryptochrome alpha/beta"
FT /evidence="ECO:0000259|PROSITE:PS51645"
FT REGION 186..225
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 557..715
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 592..606
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..652
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..686
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 687..702
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 297..301
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT BINDING 466..468
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-1"
FT SITE 384
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 453
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
FT SITE 476
FT /note="Electron transfer via tryptophanyl radical"
FT /evidence="ECO:0000256|PIRSR:PIRSR602081-2"
SQ SEQUENCE 715 AA; 81498 MW; 2422CBBC18909B38 CRC64;
MAGNKLLVYL LRRDLRAIDN PILHHLATSD HGFTHLLPIY ILPPHQIETS GFVAEGKKSP
YPEARSQVGR FWRCGPARAK FQAESIWDVK QSLEDISSGM LVRVGNFDNV LKHLIKSLHD
EHQSVDTVWM TEEVSKEEVD DQNAVASVCS ENNINFKLWQ DEKYYIDDRD TGLNDPKDLP
DVFTTFRKTQ EPLRERPRTS LPRPQAGSLP PFPSSWAPPQ EPPFQIPDNY NDFEQRLLQP
INSMVTDPPA YPEDARSAHP FKGGENPAWD RLYHLIKSGS MTTYQETRNG LLGTDYSTKL
SAYLALGSIS ARCIHEELVK FEDGQEQSYS RAMGFGQGEN EGTKAVRFEL LWRDYMRLCT
MKFGSRLFKL DGFKGASGKY DKKWKTALKE EAEADQDPSP EELGDIIERF LRGTTGMGLI
DASQRELYHT GYTSNRARQN VASFFAKHLG IDWRYGAEWY EAMLVDYDVS SNWANWQYVA
GVGNDPRGDA RIFNPIKQAF DYDNNGRYVR TWVPEVKDIE RLENAFQVWT TGDDELIKYG
IIDDIMVTHP IKRIDFQVDR KPRGPRRPYR WRRGGPGRGG RRGGGPGNGS GDYNDSRRSY
HNGPPSPESD RQFYHGGELY MQNGGQPRNG WSQRGNQTSW RGNSNGHGPN NHGPSSGRGG
HMAPFRGNGF QRGFNTNYFN APPPRQYMTN PNWPPQQFPP QAYHHQLPPH LGPHV
//
