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
//