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Database: UniProt
Entry: A0A0D3G8Q9_9ORYZ
LinkDB: A0A0D3G8Q9_9ORYZ
Original site: A0A0D3G8Q9_9ORYZ 
ID   A0A0D3G8Q9_9ORYZ        Unreviewed;       828 AA.
AC   A0A0D3G8Q9;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS   Oryza barthii.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=65489 {ECO:0000313|EnsemblPlants:OBART05G19600.1};
RN   [1] {ECO:0000313|EnsemblPlants:OBART05G19600.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 105608 {ECO:0000313|EnsemblPlants:OBART05G19600.1};
RX   DOI=10.1007/s12284-009-9025-z;
RA   Rounsley S., Marri P.R., Yu Y., He R., Sisneros N., Goicoechea J.L.,
RA   Lee S.J., Angelova A., Kudrna D., Luo M., Affourtit J., Desany B.,
RA   Knight J., Niazi F., Egholm M., Wing R.A.;
RT   "De novo next generation sequencing of plant genomes.";
RL   Rice 2:35-43(2009).
RN   [2] {ECO:0000313|EnsemblPlants:OBART05G19600.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC       {ECO:0000256|ARBA:ARBA00007975}.
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DR   AlphaFoldDB; A0A0D3G8Q9; -.
DR   STRING; 65489.A0A0D3G8Q9; -.
DR   PaxDb; 65489-OBART05G19600-1; -.
DR   EnsemblPlants; OBART05G19600.1; OBART05G19600.1; OBART05G19600.
DR   Gramene; OBART05G19600.1; OBART05G19600.1; OBART05G19600.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_005646_6_0_1; -.
DR   Proteomes; UP000026960; Chromosome 5.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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; IPR018247; EF_Hand_1_Ca_BS.
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; IPR013623; NADPH_Ox.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   PANTHER; PTHR11972:SF133; OS05G0465800 PROTEIN; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF01794; Ferric_reduct; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   Pfam; PF08414; NADPH_Ox; 1.
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; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 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|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   NADP {ECO:0000256|ARBA:ARBA00022857};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW   Reference proteome {ECO:0000313|Proteomes:UP000026960};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        268..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        407..426
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..469
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        645..662
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          144..179
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          502..639
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   828 AA;  93407 MW;  8F4FC4A275516422 CRC64;
     MAGDYVDVPL GGGGQSTLPP VAPLKKQPSR LASGMKRLAS MVPDTMKLKR THSSAQPALR
     GLRFLDKTSA GKDGWKNVEK RFDEMSADGR LPQESFAKCI GMADSKEFAS EVFVALARRR
     SIKPEDGITK EQLKEFWEEL TDQNFDSRLR IFFDMCDKNG DGQLTEDEVK EVIVLSAAAN
     KLAKLKSHAA TYASLIMEEL DPDHRGYIEI WQLETLLRGM VTAQGPPEKV KLASASLART
     MVPSSHRSPM QRRFNKTVDF IHENWKRIWV LSLWAILNIA LFMYKFVQYS RRDAFQVMGY
     CVCIAKGAAE TLKLNMAVIL LPVCRNTLTR LRSTALSKVV PFDDNINFHK VIALTIAIGA
     ATHTLAHVTC DFPRLVSCPR DKFEATLGPY FNYVQPTYSS LVASTPGWTG ILMILIMSFS
     FTLATHSFRR SVVKLPSPLH HLAGFNAFWY AHHLLVIAYI LLVLHSYFIF LTKQWYNRTT
     WMFLAVPVLF YSCERTIRRV RESSYGVTVI KAAIYPGNVL SIHMNKPSSF KYKSGMYMFV
     KCPDVSPFEW YHLIVSVQMH PFSITSAPGD DYLSVHIRTL GDWTTELRNL FGKACEAQVS
     SKKATLARLE TTIIADGLKE ETCFPKVFID GPFGAPAQNY KKYDILLLIG LGIGATPFIS
     ILKDLLNNIK SNGDVQSTHD AELGCTFKSN GPGRAYFYWV TREQGSFEWF KGVMNDVAES
     DHDNVIEMHN YLTSVYEEGD ARSALIAMVQ SLQHAKNGVD IVSGSKIRTH FARPNWRKVF
     SDLANAHQNS RIGVFYCGSP TLTKMLRTLS LEFSQTTTTR FHFHKENF
//
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