ID Q0UK63_PHANO Unreviewed; 407 AA.
AC Q0UK63;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 78.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=SNOG_07851 {ECO:0000313|EMBL:EAT85317.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT85317.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000256|ARBA:ARBA00001974};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the ferric reductase (FRE) family.
CC {ECO:0000256|ARBA:ARBA00006278}.
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DR EMBL; CH445335; EAT85317.2; -; Genomic_DNA.
DR RefSeq; XP_001798178.1; XM_001798126.1.
DR AlphaFoldDB; Q0UK63; -.
DR EnsemblFungi; SNOT_07851; SNOT_07851; SNOG_07851.
DR GeneID; 5975071; -.
DR KEGG; pno:SNOG_07851; -.
DR VEuPathDB; FungiDB:JI435_078510; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_676357_0_0_1; -.
DR InParanoid; Q0UK63; -.
DR OrthoDB; 1385919at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IBA:GO_Central.
DR GO; GO:0033215; P:reductive iron assimilation; IBA:GO_Central.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 1.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR32361:SF27; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
PE 3: Inferred from homology;
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 20..37
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..158
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 170..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 210..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 234..254
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 132..249
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT DOMAIN 311..385
FT /note="Ferric reductase NAD binding"
FT /evidence="ECO:0000259|Pfam:PF08030"
SQ SEQUENCE 407 AA; 45599 MW; 7328A5A4CBD40CE8 CRC64;
MSMGMGSAAL PKLYDFPKIY WAVVGSAIGV ATLVNLYNHI LCRQRLSAAK SGTRTPAKPS
SWLTLGVATV YALTREASNY SLYIPFKKRV FRFPSVGRAS LVLANAVTLI VLCLYGLDLT
GRFTKEDVAF RCGVVTLGQV PLIFLLAGKN NIVGYLSGVS YERLNWLHRW CARTMLLTAT
IHMGYFFASW DQYKYIPYKL KNDELAWKGL AAWSVLVWIV LSSMTPIRGW NYELFVVQHL
VSFGVFLGFV YIHIPKDTKG YVWVPVALFL FDRGRFFKHA EKSSGLSDGT SKTKTVTIEG
PYGALRPLRQ FDSVVLLAGS TGATFTLPLL RDILHGWRET STSNSSSRSF FSRQTGAVAR
HVRFVWVVKS RGQLSWFGAH LSSIAADFEI LQDRLRDVKL EMGVPET
//
