ID F9X551_ZYMTI Unreviewed; 682 AA.
AC F9X551;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=MYCGRDRAFT_69850 {ECO:0000313|EMBL:EGP89390.1};
OS Zymoseptoria tritici (strain CBS 115943 / IPO323) (Speckled leaf blotch
OS fungus) (Septoria tritici).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Zymoseptoria.
OX NCBI_TaxID=336722 {ECO:0000313|EMBL:EGP89390.1, ECO:0000313|Proteomes:UP000008062};
RN [1] {ECO:0000313|EMBL:EGP89390.1, ECO:0000313|Proteomes:UP000008062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 115943 / IPO323 {ECO:0000313|Proteomes:UP000008062};
RX PubMed=21695235; DOI=10.1371/journal.pgen.1002070;
RA Goodwin S.B., Ben M'barek S., Dhillon B., Wittenberg A.H.J., Crane C.F.,
RA Hane J.K., Foster A.J., Van der Lee T.A.J., Grimwood J., Aerts A.,
RA Antoniw J., Bailey A., Bluhm B., Bowler J., Bristow J., van der Burgt A.,
RA Canto-Canche B., Churchill A.C.L., Conde-Ferraez L., Cools H.J.,
RA Coutinho P.M., Csukai M., Dehal P., De Wit P., Donzelli B.,
RA van de Geest H.C., van Ham R.C.H.J., Hammond-Kosack K.E., Henrissat B.,
RA Kilian A., Kobayashi A.K., Koopmann E., Kourmpetis Y., Kuzniar A.,
RA Lindquist E., Lombard V., Maliepaard C., Martins N., Mehrabi R.,
RA Nap J.P.H., Ponomarenko A., Rudd J.J., Salamov A., Schmutz J.,
RA Schouten H.J., Shapiro H., Stergiopoulos I., Torriani S.F.F., Tu H.,
RA de Vries R.P., Waalwijk C., Ware S.B., Wiebenga A., Zwiers L.-H.,
RA Oliver R.P., Grigoriev I.V., Kema G.H.J.;
RT "Finished genome of the fungal wheat pathogen Mycosphaerella graminicola
RT reveals dispensome structure, chromosome plasticity, and stealth
RT pathogenesis.";
RL PLoS Genet. 7:E1002070-E1002070(2011).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
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DR EMBL; CM001198; EGP89390.1; -; Genomic_DNA.
DR RefSeq; XP_003854414.1; XM_003854366.1.
DR AlphaFoldDB; F9X551; -.
DR STRING; 336722.F9X551; -.
DR EnsemblFungi; Mycgr3T69850; Mycgr3P69850; Mycgr3G69850.
DR GeneID; 13404180; -.
DR KEGG; ztr:MYCGRDRAFT_69850; -.
DR eggNOG; KOG1158; Eukaryota.
DR HOGENOM; CLU_001570_17_5_1; -.
DR InParanoid; F9X551; -.
DR OMA; LCCGGGC; -.
DR OrthoDB; 9164at2759; -.
DR Proteomes; UP000008062; Chromosome 3.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR003097; CysJ-like_FAD-binding.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR001709; Flavoprot_Pyr_Nucl_cyt_Rdtase.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR023173; NADPH_Cyt_P450_Rdtase_alpha.
DR InterPro; IPR001433; OxRdtase_FAD/NAD-bd.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR19384:SF84; METHIONINE SYNTHASE REDUCTASE; 1.
DR PANTHER; PTHR19384; NITRIC OXIDE SYNTHASE-RELATED; 1.
DR Pfam; PF00667; FAD_binding_1; 1.
DR Pfam; PF00175; NAD_binding_1; 1.
DR PRINTS; PR00371; FPNCR.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008062}.
FT DOMAIN 249..553
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 71..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..96
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 682 AA; 75089 MW; 2D971F511D60303A CRC64;
MSAALQESGV RRHSFSHFGD AATTYRHTSI PYTATSHPDN PIPSEPKDII AGMRIPLEDS
VRLSNMATIR TRSSGESLQG DTSDSDTPST PLTEHSDADG SFVRMSKLSL ETSTKPPRKR
RASTTYASNV DDIRRLIGTG GGTKFLQKYC CGEGCCMIES LPLHTDETAY APIITPSNDA
YRFLNLNLRS LSLDTELTKI PEVQESKVSF AALRRASIEE KFPDEAHHRH DAEAVKSYPP
TYMKPHPPYE IFNAPLYDAR ELTKPGAEKR TFHFDIDVTD YPAEGGVDFK VGGAVGVCPP
NDPEVVEDIM NQLGVPRFLR DKAVRLQTTG GRWPTIWGDE ESRELVTTRR EVLTWTVDIS
STAPTKPLLR LLAEHASEPN EKKILEYVCS AQGQATFCDL RTGPHITVQQ LLRAFPSSKP
PLESLCAVLT QLMPRFYSLS NDPHVSSARE GLAGRRLIEI AVTIHETPNY SGTKRSGVGS
GFMERIARAF IEAEGAAPKD SPPSTAGRAL NLSVPMFRGL MSNPLSREFA SDGPMVLIGA
GVGMAPFRGF ILNRLKNANC ANKIWLIQGI RDSMLDEIYR GELGAHESEI KKVVQSRAQK
MLPPKVAKYV QDEVRLQADI VWFVINALDG RIFVCGSTSG MGEGVESALV DVAMDKGNLD
EETARQFWEG KKAGGQYIAE TW
//
