ID A0A024UVM6_9STRA Unreviewed; 708 AA.
AC A0A024UVM6;
DT 09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT 09-JUL-2014, sequence version 1.
DT 27-MAR-2024, entry version 35.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=H310_00409 {ECO:0000313|EMBL:ETW10000.1};
OS Aphanomyces invadans.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Saprolegniales; Saprolegniaceae;
OC Aphanomyces.
OX NCBI_TaxID=157072 {ECO:0000313|EMBL:ETW10000.1};
RN [1] {ECO:0000313|EMBL:ETW10000.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJM9701 {ECO:0000313|EMBL:ETW10000.1};
RG The Broad Institute Genomics Platform;
RA Russ C., Tyler B., van West P., Dieguez-Uribeondo J., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L., Chapman S.B.,
RA Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M., Howarth C.,
RA Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C., Pearson M.,
RA Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S., Wortman J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Aphanomyces invadans NJM9701.";
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KI913952; ETW10000.1; -; Genomic_DNA.
DR RefSeq; XP_008861411.1; XM_008863189.1.
DR AlphaFoldDB; A0A024UVM6; -.
DR STRING; 157072.A0A024UVM6; -.
DR EnsemblFungi; H310_00409-t26_1; H310_00409-t26_1-p1; H310_00409.
DR EnsemblProtists; ETW10000; ETW10000; H310_00409.
DR GeneID; 20077459; -.
DR VEuPathDB; FungiDB:H310_00409; -.
DR eggNOG; KOG0039; Eukaryota.
DR OrthoDB; 54846at2759; -.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; 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; 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:SF69; METALLOREDUCTASE AIM14-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 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 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}.
FT TRANSMEM 44..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 137..161
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 173..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..238
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 304..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 599..615
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 336..446
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 708 AA; 79586 MW; 22DD851CB4D328A3 CRC64;
MQTSPRKSIK SFQAASTPVG FDNKPAPVTG ASSRWGVVLV AVNWMVGALL AFAIVSPIGI
QVVAIYRNNL ALKWNSWFNI DPKDKNRFAR GKEMLPVSYF FLFFVVPVVV AAVLFSLAKA
HYRMGVTYWL HIKPRCLHRL VSVGEILFVL AAVAGNVLVF YHSYMFQLSL KKPVLKVVGI
SLAFSGLYNM VFLALPATRH CFWMEWLNLP WARAVKYHRW FGAATIAMFF VHFAVFFVEF
ANNGALAHEL LPCFKCDIGV EGSMGKDAWI NVFGELSLLC MLIMGATAFP YVRRNYYATF
KATHWLFIPA ALFAVMHYEQ IIVWIYVSMV LYIVNRMYSS STVAHPVALD TAAALPGHVT
QLTFKCSTNY LPGDIVYVQV PSISTVQWHP FSIASTPLHT PGQLTVYIKA LGHWTSQVHD
YVKQCEAQGV EPVVYMDAGY TPPTPMSLSY SSVVFIGGGI GVTPLMGQIM HLLHARPHQD
VYLVWHVKTV EMVSQFQGWL HELEDVAERH RGRLSLHLHV TQQDIAEVSI EHDEPTHKFQ
LSKSSTEPRP YSHLSTTRKL VMLLLAFFVS GALLFYVRYQ QKISTYKPSL WPLQRFVEFS
IVIVGSFFAY GVALIRPGKQ PVAATALQMR ANTTAVPLTN DEFVRHFNVK YERANWEELF
GEIKAGHSST DLRSVGVYVS GPNALTAAIE AVTANDALYD VHHEVFEL
//