ID A0A0E0QJU2_ORYRU Unreviewed; 1035 AA.
AC A0A0E0QJU2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
OS Oryza rufipogon (Brownbeard rice) (Asian wild rice).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=4529 {ECO:0000313|EnsemblPlants:ORUFI08G18820.1, ECO:0000313|Proteomes:UP000008022};
RN [1] {ECO:0000313|Proteomes:UP000008022}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. W1943 {ECO:0000313|Proteomes:UP000008022};
RA Zhao Q.;
RL Submitted (JUN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:ORUFI08G18820.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (JUN-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC {ECO:0000256|ARBA:ARBA00007975}.
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DR AlphaFoldDB; A0A0E0QJU2; -.
DR STRING; 4529.A0A0E0QJU2; -.
DR EnsemblPlants; ORUFI08G18820.1; ORUFI08G18820.1; ORUFI08G18820.
DR Gramene; ORUFI08G18820.1; ORUFI08G18820.1; ORUFI08G18820.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR OMA; FNTAYSD; -.
DR Proteomes; UP000008022; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050664; F:oxidoreductase activity, acting on NAD(P)H, oxygen as acceptor; IEA:InterPro.
DR GO; GO:0004601; F:peroxidase 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; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
DR InterPro; IPR013121; Fe_red_NAD-bd_6.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR InterPro; IPR013623; NADPH_Ox.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR PANTHER; PTHR11972:SF190; OS08G0453700 PROTEIN; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR Pfam; PF08414; NADPH_Ox; 2.
DR PRINTS; PR00466; GP91PHOX.
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; PS51384; FAD_FR; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000008022};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 417..436
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 615..635
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 710..831
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 359..393
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..131
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..157
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 359..387
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1035 AA; 115160 MW; 30550FB289BA69D1 CRC64;
MWTPSRGSAS GRRATGHRRI ADYLADDRTE ASTENGSFNT AYSDELFAPT SSSAGGDGVG
GMLPAFLADQ SDLVEVMLEL DEESMVVRSV TPTTGALYGP TSLAGGGAAH TPPGSGRSLS
RCSSTSSRIR KKFAWLRSPS PAPAPRAPTP SEPPPPREAA MAARERRRIQ ARLNRSRSGA
RRALKGLRFI SRTTGSAEAA ELWTRVEHRF NALSRDGLLS RDDFGDCIGK QAKPSSMSMA
RRARTRSRDD TAYGAGIGAG MEDSKEFAVG IFDALARRRR QELERISKEE LYDFWLIVLS
ASANKLSKLK EQAEEYASLI MEELDPEDLG YIELWQLEAL LLQRDAYMNY SRPLSSGSTA
QWSQNLGGGG GGGGQQGGQG QGQGQSEGRR NDWRRRWSPR RAAARAQVAA EENWRRAWVL
ALWFAAMAGL FAWKFVQYRR TPAFRVMGYC LPTAKGAAET LKLNMALVLL PVCRNTLTWL
RSSWARFFVP FDDSITFHKV ESSSGFKWAP PGRSNQCSVA GEPAGTEDPR PGRLRVKAPV
IQKSPRPTGL PLSCGATIIA TAIALGICTH AGTHLACDFP RLIGSSREEY ELLLSGFFGA
SRPTYRGLLA GVEGVTGIVM VVLMVVSFTL ATRPLRKREA PRLPFPLGHL AGFNAFWYSH
HLLIVVYLLL LVHGWFMFLV TKWHQRTTWM YIAVPLMLYV GERTLRAFRS KAYAVKILKV
CLLPGNVLTI TMSKPYGFRY RSGQYIFLQC PTISPFEWHP FSITSAPGDD YISVHIQTRG
DWTQELKRIF VENYFVPSVP RRASFGALGM AEQKSPPRLL VDGPYGAPAQ DFRNYDVLLL
VGLGIGATPF ISILRDLLNN IKLADELMDL AMETSRSDDS ANSFSVSTAS SNKRRAYRTS
RAHFYWVTRE PGSFEWFKGV MNEVAEMDKK GVIELHNYLT SVYEERDARS TLLSMVQALN
HAKHGVDIVS GTRVRTHFAR PNWKEVFTRI ASKHPNSTVG VFYCGKPTLA KELKKLSLDM
SHKTTTRFHF HKEYF
//
