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Database: UniProt
Entry: B8BBA2_ORYSI
LinkDB: B8BBA2_ORYSI
Original site: B8BBA2_ORYSI 
ID   B8BBA2_ORYSI            Unreviewed;       978 AA.
AC   B8BBA2;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 79.
DE   RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN   ORFNames=OsI_29451 {ECO:0000313|EMBL:EEC83672.1};
OS   Oryza sativa subsp. indica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39946 {ECO:0000313|EMBL:EEC83672.1, ECO:0000313|Proteomes:UP000007015};
RN   [1] {ECO:0000313|EMBL:EEC83672.1, ECO:0000313|Proteomes:UP000007015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. 93-11 {ECO:0000313|Proteomes:UP000007015};
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C., Chen H., Xu Z., Li H., Huang H., Zhang F., Xu H.,
RA   Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W.,
RA   Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L.,
RA   Zheng W., Hao B., Liu S., Wang W., Yuan L., Cao M., McDermott J.,
RA   Samudrala R., Wang J., Wong G.K., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
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   EMBL; CM000133; EEC83672.1; -; Genomic_DNA.
DR   AlphaFoldDB; B8BBA2; -.
DR   STRING; 39946.B8BBA2; -.
DR   PeroxiBase; 5569; OsRboh06.
DR   EnsemblPlants; BGIOSGA028780-TA; BGIOSGA028780-PA; BGIOSGA028780.
DR   Gramene; BGIOSGA028780-TA; BGIOSGA028780-PA; BGIOSGA028780.
DR   HOGENOM; CLU_005646_6_0_1; -.
DR   OMA; FNTAYSD; -.
DR   Proteomes; UP000007015; Chromosome 8.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
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; 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:SF190; OS08G0453700 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; 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|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:UP000007015};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        418..437
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        551..578
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        598..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        780..797
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          653..774
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..395
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"
SQ   SEQUENCE   978 AA;  109234 MW;  1126CBCE394F78AA 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
     RRARARSRDD TEYGAGIGAG MEDSKEFAGG IFDALARRRR QELERISKEE LYDFWLIVLS
     ASANKLSKLK EQAEEYASLI MEELDPEDLG YIELWQLEAL LLQRDAYMNY SRPLSSGSTA
     QWSQNLGGGG GGGGGQQGGQ GQGQGQSEGR RNDWRRRWSP RRAAARAQVA AEENWRRAWV
     LALWFAAMAG LFAWKFVQYR RTPAFRVMGY CLPTAKGAAE TLKLNMALVL LPVCRNTLTW
     LRSSWARFFV PFDDSITFHK IIATAIALGI CTHAGTHLAC DFPRLIGSSR EEYELLLSGF
     FGASRPTYRG LLAGVEGVTG IVMVVLMVVS FTLATRPLRK REAPRLPFPL GHLAGFNAFW
     YSHHLLIVVY LLLLVHGWFM FLVTKWHQRT TWMYIAVPLM LYVGERTLRA FRSKAYAVKI
     LKVCLLPGNV LTITMSKPYG FRYRSGQYIF LQCPTISPFE WHPFSITSAP GDDYISVHIQ
     TRGDWTQELK RIFVENYFVP SVPRRASFGA LGMAEQKSPP RLLVDGPYGA PAQDFRNYDV
     LLLVGLGIGA TPFISILRDL LNNIKLADEL MDLAMETSRS DDSANSFSVS TASSNKRRAY
     RTSRAHFYWV TREPGSFEWF KGVMNEVAEM DKKGVIELHN YLTSVYEERD ARSTLLSMVQ
     ALNHAKHGVD IVSGTRVRTH FARPNWKEVF TRIASKHPNS TVGVFYCGKP TLAKELKKLS
     LDMSHKTTTR FHFHKEYF
//
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