ID W2KQ06_PHYPR Unreviewed; 871 AA.
AC W2KQ06;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=L917_13494 {ECO:0000313|EMBL:ETL87248.1};
OS Phytophthora parasitica (Potato buckeye rot agent).
OC Eukaryota; Sar; Stramenopiles; Oomycota; Peronosporales; Peronosporaceae;
OC Phytophthora.
OX NCBI_TaxID=4792 {ECO:0000313|EMBL:ETL87248.1};
RN [1] {ECO:0000313|EMBL:ETL87248.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CHvinca01 {ECO:0000313|EMBL:ETL87248.1};
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 CHvinca01.";
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; KI681103; ETL87248.1; -; Genomic_DNA.
DR AlphaFoldDB; W2KQ06; -.
DR EnsemblProtists; ETL87248; ETL87248; L917_13494.
DR VEuPathDB; FungiDB:PPTG_14837; -.
DR Proteomes; UP000054423; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR Gene3D; 1.10.238.10; EF-hand; 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; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR002048; EF_hand_dom.
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 PRINTS; PR00466; GP91PHOX.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 1.
DR SUPFAM; SSF47473; EF-hand; 1.
DR SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
DR PROSITE; PS51384; FAD_FR; 1.
PE 4: Predicted;
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW NADP {ECO:0000256|ARBA:ARBA00022857};
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 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 390..410
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 495..514
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 526..543
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 549..568
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 244..279
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 575..681
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 117..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 871 AA; 99163 MW; 4A8E35885E939CCD CRC64;
MDRSRKDPGH GKPKNELKIT PAKTQALIDV STPSPHAPRF GDKTTPMMST MVNMNQNPPL
RKPAATNFMD SSKFVSMNST TTHAVGNCRS HNRRSRRRRA NVDAMMRSNM VRQSLTLPAS
SVSSASSAAH KKCRVAPPAG KDDMYGPPPG SDVETVPIPG DCNFEQKYNV AMSMDEKAFT
PMEKLEALRD AMGNFTDKDG YIERETFSQA FEVDGNEFDG YATSTGTIDG NAILIDAVMK
LGVNAQEKLR FIFDTLDPDN TGYVVEEQIV QLLESNFSSA KIDVVGMEFR TVAKLMFRKA
RVQNDAMTFK QFCGVFEPYV TASYHLEEAK PVYSAPIRPK SKFGQWYSDN KLRIWWLFFY
FIVNNIAFWV KWFMYEVDPA IGWGLRIARA NAQVAMLNCV FVLLPMCRSI TQVMKRSKLL
WRIIPFDDHI AFHKISGSVL LIAGLIHTIA HVFNEIYLYL IATPDEVKRS IFVTRHVSTF
VNGERPPFTT MLQALPVWTG VILLVITCIS FPLAAIPKFR QGRFNLFWYS HMLFGPFLIV
LAFHGATSWL ARCSAYIWIT PPFLIYLIER RFRYAKMFAA PVRIMEAIEL DGTVALFVEK
PRRFVYRPGM YLYLNCPQVS SHEWHPFTIS SAPGDNYISI HIRVCGDWTD AISRVIADCH
ACNLQYPDVY LDGPVGAPTQ DYHRYKTVIC IGGGIGVTPF ASILKDVVHL WEDNRCHNCN
HIRHPSSFQI QKLYFHWVTR GQESLSWFEG TMKQITEMDR DNVIETHQYL STVVLGGEEN
TSQLKMFQEF VHEQTGKDFV SGMDTKQLTH FGRPDWDKIF AEARAKHPGE EVGVFCCGPH
ELEDVLYNAC KKYSSSKAER TIFDFHSEKF A
//
