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Database: UniProt
Entry: J3KZU2_ORYBR
LinkDB: J3KZU2_ORYBR
Original site: J3KZU2_ORYBR 
ID   J3KZU2_ORYBR            Unreviewed;       905 AA.
AC   J3KZU2;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EnsemblPlants:OB01G24980.1};
GN   Name=102718495 {ECO:0000313|EnsemblPlants:OB01G24980.1};
OS   Oryza brachyantha (malo sina).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX   NCBI_TaxID=4533 {ECO:0000313|EnsemblPlants:OB01G24980.1};
RN   [1] {ECO:0000313|EnsemblPlants:OB01G24980.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IRGC 101232 {ECO:0000313|EnsemblPlants:OB01G24980.1};
RX   PubMed=23481403;
RA   Chen J., Huang Q., Gao D., Wang J., Lang Y., Liu T., Li B., Bai Z.,
RA   Luis Goicoechea J., Liang C., Chen C., Zhang W., Sun S., Liao Y., Zhang X.,
RA   Yang L., Song C., Wang M., Shi J., Liu G., Liu J., Zhou H., Zhou W., Yu Q.,
RA   An N., Chen Y., Cai Q., Wang B., Liu B., Min J., Huang Y., Wu H., Li Z.,
RA   Zhang Y., Yin Y., Song W., Jiang J., Jackson S.A., Wing R.A., Wang J.,
RA   Chen M.;
RT   "Whole-genome sequencing of Oryza brachyantha reveals mechanisms underlying
RT   Oryza genome evolution.";
RL   Nat. Commun. 4:1595-1595(2013).
RN   [2] {ECO:0000313|EnsemblPlants:OB01G24980.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (APR-2013) 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   RefSeq; XP_006644164.1; XM_006644101.2.
DR   AlphaFoldDB; J3KZU2; -.
DR   STRING; 4533.J3KZU2; -.
DR   EnsemblPlants; OB01G24980.1; OB01G24980.1; OB01G24980.
DR   GeneID; 102718495; -.
DR   Gramene; OB01G24980.1; OB01G24980.1; OB01G24980.
DR   KEGG; obr:102718495; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   HOGENOM; CLU_005646_6_0_1; -.
DR   OMA; ENETHEQ; -.
DR   OrthoDB; 367877at2759; -.
DR   Proteomes; UP000006038; Chromosome 1.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005509; F:calcium ion binding; IEA:EnsemblPlants.
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   GO; GO:0043621; F:protein self-association; IEA:EnsemblPlants.
DR   CDD; cd00051; EFh; 1.
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:SF64; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN B; 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:UP000006038};
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        356..375
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        497..517
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        537..561
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          229..264
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   DOMAIN          587..715
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
FT   REGION          1..47
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          72..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        11..43
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        94..123
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   905 AA;  101921 MW;  51513F1AE881ED8C CRC64;
     MADLEAGTVA ATDLGNSTST RSQDDASSLI PNSGNLGSSN RSTKTARFKD DDELVEITLD
     VQRDSVAIQE VRGVDEGGSG HGAGFDGLPL VSPSSRSGKL TSKLRQVTNG LKMKSSSKKA
     PPQAQLSERR ARKRLDRTKS SAAVALKGLQ FVNAKVGNDG WAAVEKRFNQ LQVDGVLLRS
     RFGKCIGMDG SDEFAMQMFD ALARKRGIVK QVLTKDELKD FFEQLTDQGF DNRLRTFFDM
     VDKNADGRLT AEEVKEIIAL SASANKLSKI KERADEYTAL IMEELDPRNL GYIEMEDLEE
     LLLQSPSEAV ARSTNTHSSK LSKALSMKLA SNKEMSPMRH YWQQFMYFLE ENWKRSWVMT
     LWLSICIGLF IWKFMQYRNR AVFKIMGYCV TTAKGAAETL KFNMALVLLP VCRNTITWIR
     SKTQIGAVVP FNDNINFHKV IAAGVAVGVA LHAGAHLTCD FPRLLHASDA QYEPMKPFFG
     EKRPPNYWWF VKGTEGWTGV VMVVLMAIAF VLAQPWFRRN KLKDSNPLKK MTGFNAFWFT
     HHLFVIVYTL LFVHGICLYL SRDWYKKTTW MYLSVPVLLY VSERILRLFR SHDAVGIQKV
     AVYPGNVLAL YMSKPPGFRY RSGQYIFIKC SAVSPYEWHP FSITSAPGDD YLSVHIRTRG
     DWTSRLRTVF SEACRPSTEG ESGLLRADLS KAITNDKARF PKLLVDGPYG APAQDYREYD
     VLLLIGLGIG ATPLISIVKD VLNHIQGGGS VGATEPEVSS KAKKRPFMTK RAYFYWVTRE
     EGSFEWFRGV MNEVAEKDKG GVIELHNHCS SVYQEGDARS ALIHMLQELQ HAKKGVDILS
     GTSVKTHFAR PNWRSVFKKV AVSHENQRVG VFYCGEPVLV PQLRQLSADF THKTNTKFEF
     HKENF
//
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