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Database: UniProt
Entry: F9FGN7_FUSOF
LinkDB: F9FGN7_FUSOF
Original site: F9FGN7_FUSOF 
ID   F9FGN7_FUSOF            Unreviewed;       538 AA.
AC   F9FGN7;
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=FOXB_05566 {ECO:0000313|EMBL:EGU83917.1};
OS   Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU83917.1};
RN   [1] {ECO:0000313|EMBL:EGU83917.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fo5176 {ECO:0000313|EMBL:EGU83917.1};
RX   PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA   Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT   "A highly conserved effector in Fusarium oxysporum is required for full
RT   virulence on Arabidopsis.";
RL   Mol. Plant Microbe Interact. 25:180-190(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EGU83917.1}.
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DR   EMBL; AFQF01001763; EGU83917.1; -; Genomic_DNA.
DR   AlphaFoldDB; F9FGN7; -.
DR   STRING; 660025.F9FGN7; -.
DR   PaxDb; 5507-FOXG_09601P0; -.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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; IPR000778; Cyt_b245_heavy_chain.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF207; FERRIC REDUCTASE TRANSMEMBRANE COMPONENT 1-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   PRINTS; PR00466; GP91PHOX.
DR   SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR   SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
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   Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW   Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
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        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        103..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..200
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        207..226
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          250..367
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   538 AA;  60202 MW;  7A626E2520B060C5 CRC64;
     MTDPVIIDRY TAARVYFGSV VGLISLESLT PFSIYTFQRY NKYRRQDRNV LHWSITVWLH
     KLHSFPLSLP CLDWHVTDVA RFTTFLALNL VFSVQSNEFT ADYTLYGWLA IANAGLALLM
     ASRNNLFASL LRIPNPVLLQ YHRWIGLATV AHATAHVSFN IQHYIETKQV TTSFGNHRIQ
     VGLMAWIALV MLFLTALPIV RRRFFEVFYY THALFFIFVV GALIHASHGP EFMLPGLLLW
     GIDRAIRLAY NFRNIQVQSV EAFEGNVTKF KVKGLRTRTP GQVVWLQIPR VSFVNWHPFT
     VASAPNDPEK TATIAVRGLG GFTKAVQYAD CNSDVNQHGC ASLDSNSIMA HPLKMSLDGP
     YGVGSVSWGL LPVTVLIAGG IGITPGISIA SHIIRKAAIN VGSHSMSHIH LLWVVRDAQH
     IQWFADELTE LVKECANPDS PATLDISIFV TDGAHSAVHM SEPSHEMQGM SSPQPWSIHL
     GRPDLKQWFG QLKSKRLGMD TAVNLCGPRK LLKQARAAAC DVSDREGLFF LQEEVFEL
//
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