ID A0A0E0A0E4_9ORYZ Unreviewed; 829 AA.
AC A0A0E0A0E4;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
DE RecName: Full=EF-hand domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza glumipatula.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40148 {ECO:0000313|EnsemblPlants:OGLUM05G20660.2};
RN [1] {ECO:0000313|EnsemblPlants:OGLUM05G20660.2}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A., Panaud O., Oliveira A.C.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OGLUM05G20660.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-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; A0A0E0A0E4; -.
DR STRING; 40148.A0A0E0A0E4; -.
DR EnsemblPlants; OGLUM05G20660.2; OGLUM05G20660.2; OGLUM05G20660.
DR Gramene; OGLUM05G20660.2; OGLUM05G20660.2; OGLUM05G20660.
DR eggNOG; KOG0039; Eukaryota.
DR Proteomes; UP000026961; Unassembled WGS sequence.
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 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:UP000026961};
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 292..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 431..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 471..493
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 646..663
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 500..640
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 829 AA; 93502 MW; BE6350F4B4D42C4B CRC64;
MAGDYVDVPL GGGGQSTLPP VAPLKKQPSR LASGMKRLAS MVPDTMKLKR THSSAQPALR
GLRFLDKTSA GKDGWKNVEK RFDEMSADGR LPQESFAKCI GMADSKEFAS EVFVALARRR
SIKPEDGITK EQLKEFWEEL TDQNFDSRLR IFFDMCDKNG DGQLTEDEVK EVIVLSAAAN
KLAKLKSHAA TYASLIMEEL DPDHRGYIEV PRHEIISLFF DKQQHTDMLV SMQIWQLETL
LRGMVTAQGP PEKVKLASAS LARTMVPSSH RSPMQRRFNK TVDFIHENWK RIWVLSLWAI
LNIALFMYKF VQYSRRDAFQ VMGYCVCIAK GAAETLKLNM AVILLPVCRN TLTRLRSTAL
SKVVPFDDNI NFHKVIALTI AIGAATHTLA HVTCDFPRLV SCPRDKFEAT LGPYFNYVQP
TYSSLVASTP GWTGILMILI MSFSFTLATH SFRRSVVKLP SPLHHLAGFN AFWYAHHLLV
IAYILLVLHS YFIFLTKQWY NRTTWMFLAV PVLFYSCERT IRRVRESSYG VTVIKAAIYP
GNVLSIHMNK PSSFKYKSGM HPFSITSAPG DDYLSVHIRT LGDWTTELRN LFGKACEAQV
SSKKATLARL ETTIIADGLK EETCFPKVFI DGPFGAPAQN YKKYDILLLI GLGIGATPFI
SILKDLLNNI KSNGDVQSTH DAELGCTFKS NGPGRAYFYW VTREQGSFEW FKGVMNDVAE
SDHDNVIEMH NYLTSVYEEG DARSALIAMV QSLQHAKNGV DIVSGSKIRT HFARPNWRKV
FSDLANAHQN SRIGVFYCGS PTLTKMLRDL SLEFSQTTTT RFHFHKENF
//
