ID   W2NYY9_PHYPR            Unreviewed;       567 AA.
AC   W2NYY9;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=L914_03324 {ECO:0000313|EMBL:ETM53183.1};
OS   Phytophthora parasitica (Potato buckeye rot agent).
OC   Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC   Phytophthora.
OX   NCBI_TaxID=4792 {ECO:0000313|EMBL:ETM53183.1};
RN   [1] {ECO:0000313|EMBL:ETM53183.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IAC_01/95 {ECO:0000313|EMBL:ETM53183.1};
RG   The Broad Institute Genomics Platform;
RA   Russ C., Tyler B., Panabieres F., Shan W., Tripathy S., Grunwald N.,
RA   Machado M., Johnson C.S., Arredondo F., Hong C., Coffey M., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Phytophthora parasitica IAC_01/95.";
RL   Submitted (NOV-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; KI691434; ETM53183.1; -; Genomic_DNA.
DR   AlphaFoldDB; W2NYY9; -.
DR   EnsemblProtists; ETM53183; ETM53183; L914_03324.
DR   VEuPathDB; FungiDB:PPTG_22174; -.
DR   Proteomes; UP000054532; Unassembled WGS sequence.
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   Gene3D; 2.40.30.10; Translation factors; 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:SF55; FERRIC REDUCTASE; 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; 2.
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   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        86..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        117..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        151..170
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        182..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        216..244
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          276..391
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   567 AA;  62757 MW;  CC5DE7FE33797762 CRC64;
     MTTPDSPKTP KADYAVMDPC MNMNTQSSLP STNDLQSVPP TTKESCSPLR KLARWWIALR
     WQLARNLFSV PLPFLTSVFD VKLGDLFIVF PICLVFIITT AIQANDREVE STGNPPTYGL
     LVVFILTVRN NSVLLALTGI SYERVLFYHK IAALITIILS GLHGFAYILA HDKGEISGEG
     DMVLTGTVAF GAMVLMFVFS LGLVRRRFFE FFLRTHWILF IVVLVFAVIH GASTALIGII
     PWGIDMAFRH AYRPRVYAQG SIIGGNKSTS QDSANFTGKS MGVIARDQVA MSALPGNVVR
     IQFPRVRKDT GQVFNYQAGQ YVFLCVPTIS SLEWHPFTIS SSPHEPMVTL HIKALGDWTS
     KLQSLIVALG GEVASPFDVL VDGPYGSVSI DIKTPTTYSH FALFSGGIGV TPMRSIVNRL
     HYEAHHEGRS SIERAHFVWS VRDRDMAQSL VVDVTGDNRG DCYFPNGIIN NVGDAFSSEI
     YLSRSERDVE AADLDRHLGS SLRYGSRPDI SATLRMVGEQ AKQNGKTRVA VLVCGPSSMV
     RDVINKSLSL SWEMKVRFDV HSEVFEF
//