ID X0CSC3_FUSOX Unreviewed; 651 AA.
AC X0CSC3;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=FOQG_02385 {ECO:0000313|EMBL:EXK97051.1};
OS Fusarium oxysporum f. sp. raphani 54005.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1089458 {ECO:0000313|EMBL:EXK97051.1, ECO:0000313|Proteomes:UP000030663};
RN [1] {ECO:0000313|EMBL:EXK97051.1, ECO:0000313|Proteomes:UP000030663}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=54005 {ECO:0000313|EMBL:EXK97051.1,
RC ECO:0000313|Proteomes:UP000030663};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Fusarium oxysporum PHW815.";
RL Submitted (NOV-2011) to the EMBL/GenBank/DDBJ databases.
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; JH658364; EXK97051.1; -; Genomic_DNA.
DR AlphaFoldDB; X0CSC3; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_016134_0_0_1; -.
DR Proteomes; UP000030663; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000293; F:ferric-chelate reductase activity; IEA:UniProt.
DR GO; GO:0000041; P:transition metal ion transport; IEA:UniProt.
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; 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 PANTHER; PTHR32361; FERRIC/CUPRIC REDUCTASE TRANSMEMBRANE COMPONENT; 1.
DR PANTHER; PTHR32361:SF3; REDUCTASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_6G13750)-RELATED; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
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 PROSITE; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
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 Reference proteome {ECO:0000313|Proteomes:UP000030663};
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 55..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 213..232
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 339..452
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 536..556
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 651 AA; 72715 MW; 690A354AC37ADEF4 CRC64;
MVSLNQLDAR HIQNMSEAKI LEPHWGYADR ALPCTNDKGS CEYLDLVYYA HDLGMLYSGI
LWATILAVFF LWAILRHVGK PSSPAITLGV NPKAGLAKVR SSLSSLTRQY LLPDACRTIF
GRTTRFQVAV MLSLVGYLTV WSFVGMTYQK WVTPVKDMPG VYNTRTTLGP WSDRVGILAY
ALTPLSVLLA SRESVLSLIT GVPYQSFIFL HRWLGYIIFL QGSLHTIAWT VVEVRLYQPQ
PKVAAEWIVQ EYMIWGVVAM ILLLLMFIGS TPWGIRATGY EFFRKSHYVL AMVYIGACWG
HWKQLKCFLL PSLLFWFADR GFRLLRTAYL HYHHLPSGKM GFQAAQAVIT RFPDAEHGDI
LRFDLENDQD PWKIGQHYFL CFTESSIWQS HPFTPINAPV VEKGVVKHSY IMRAKGGETK
KMAELAAKKL TISERATTSV ILTGAYGETT MDHVAPDTNI VCVAGGTGIA YVLPVLLELA
RSPISRDRKI ELIWAIRHAA DAEWVQEEMD LLQQAQKALN LKIRVYATRD SSSSSKLQVS
DEKDVTDATR QLGSSSSSDV IEEGCACGTD VPVAKIGNGI VDEDRHPNLS KLISDFVSNT
ITGPTTVFAS GPGGMISDLR TIVAGCNSGN KVWNGNERFD VKLVCDDRLE W
//
