ID W2WZI8_PHYPR Unreviewed; 781 AA.
AC W2WZI8;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 36.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=F441_10127 {ECO:0000313|EMBL:ETP15019.1};
OS Phytophthora parasitica CJ01A1.
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=1317063 {ECO:0000313|EMBL:ETP15019.1, ECO:0000313|Proteomes:UP000018958};
RN [1] {ECO:0000313|EMBL:ETP15019.1, ECO:0000313|Proteomes:UP000018958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CJ01A1 {ECO:0000313|EMBL:ETP15019.1,
RC ECO:0000313|Proteomes:UP000018958};
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., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Phytophthora parasitica CJ01A1.";
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}.
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:ETP15019.1}.
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DR EMBL; ANIX01001999; ETP15019.1; -; Genomic_DNA.
DR AlphaFoldDB; W2WZI8; -.
DR EnsemblProtists; ETP15019; ETP15019; F441_10127.
DR Proteomes; UP000018958; 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; 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; PR00410; PHEHYDRXLASE.
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 80..101
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 121..141
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 219..235
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 256..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 307..327
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 359..377
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 612..632
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 644..665
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 376..479
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 568..590
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..16
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 87519 MW; 142EADE290B2F794 CRC64;
MSARVDMERR RAPLSPPRSP DTDPDLDLLL DQDLNDDEFD RLVASRTSPK GSKRMRLLQK
PQKAAALQMM AKARRSGAKV FLKFCSAWIL FGLLWIRWPI FDLEVFPLVE AKLGDKLDVE
PFVVSVALVF PFLLAGVIFY WRQESVGSLA RWGQQLKVVQ WVKARPSIGK RFGLDAVDVV
LVSGFLLLQL NLVVGKLLID KENGKLAKAG IVVRTARAFG MNGLYAMVLS VILVARQSFL
HKFFGLSGER AARYHVLTGQ FGFIMLVLHG VLYILVWYSQ GKVEKMLFPC LAESCTPKQR
YGSTRNFFGA VAMLPLLVVA VSSMEWVRRR FFRRFIVLHC LSAGFIVFTA LHYYAASFWL
VPAIVLYGIY RTVSAFGRGK ASVMSATAMS NKVFQLELRR STTPGSDFSP GQYVYIKVDA
IGKEWHPFTI SSSPLRNRHS FVLDAKVQGP FTSQVVTLMK THQLQTVHVD GYYGSEIKLA
PHMVFVAGGS GMTPFLSVLD HLKALAELND RDEVTENSEL PRTLWIVWTC RDLEFLEAHA
ELLDAVNRCS QWKCKIWLHH THSVIGSEYD EDDDTQTEPD DLSEESSPRA QRFYPPSLER
HAFSGHNYMQ GLPLFVGTAL GCALMMMWVF RLEEFTAKSF VRRTLLPCAG ALGAVLGASA
VLYLLTRWNA RRSGDGAMGV AMGEMELEGL DIASPAAPAT PRSMPTPAQS VLSRNFLIEK
ERPDLSTRLR DVHSEIRESY GMKADVVLLV SGPANLQSDT LLLARELQSP SFKLDQKSFL
L
//