ID A0A0E0ESK5_9ORYZ Unreviewed; 975 AA.
AC A0A0E0ESK5;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Oryza meridionalis.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Oryza.
OX NCBI_TaxID=40149 {ECO:0000313|EnsemblPlants:OMERI09G09060.1};
RN [1] {ECO:0000313|EnsemblPlants:OMERI09G09060.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=OR44 {ECO:0000313|EnsemblPlants:OMERI09G09060.1};
RA Wing R.A., Panaud O., Henry R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:OMERI09G09060.1}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- SIMILARITY: Belongs to the RBOH (TC 5.B.1.3) family.
CC {ECO:0000256|ARBA:ARBA00007975}.
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DR AlphaFoldDB; A0A0E0ESK5; -.
DR STRING; 40149.A0A0E0ESK5; -.
DR EnsemblPlants; OMERI09G09060.1; OMERI09G09060.1; OMERI09G09060.
DR Gramene; OMERI09G09060.1; OMERI09G09060.1; OMERI09G09060.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR Proteomes; UP000008021; Chromosome 9.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 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; IPR002048; EF_hand_dom.
DR InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR017927; FAD-bd_FR_type.
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:SF44; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN E; 1.
DR Pfam; PF08022; FAD_binding_8; 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; 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|SAM:Phobius}; NADP {ECO:0000256|ARBA:ARBA00022857};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00022559};
KW Peroxidase {ECO:0000256|ARBA:ARBA00022559};
KW Reference proteome {ECO:0000313|Proteomes:UP000008021};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 412..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 479..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 530..556
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 595..617
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 777..798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 252..287
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 650..771
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..39
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 116..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 24..39
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 975 AA; 108500 MW; 8C4AE580AAF003CC CRC64;
MWTPSRGSNA ARRSGHRRIA DYLADDQTTN TDTSDNESYT TAYGDEFFAA AAAAAAAAAG
SGGGGGMLPA FLADQGDLVE VMLELDEESM VVRSGGGGAR SLSRCSSTSS RIRKKFAWLR
SPSPSPSPRP PTPAELQREA AMAARERRRI QARLNRSSTG AKRALKGLRF ISRTTGTVQA
AELWRRVEDR FNSLARDGLL SRDDFGECIG MVDSKEFAVG IFDALARRRR QNLERITREE
LYDFWLQISD QSFDARLQIF FDMVDTNVDG RITREEVQEL IVLSASANKL AKLKEQAEEY
ASLIMEELDP ENLGYIELWQ LEALLLQRDS YMNYSRPLST ASGAQWSQNL GGGAAAVAAG
AAAATGGGAH AAAAARGGQQ QQQQEEGRRG GWGVRKAAAR VRVAAEENWR RAWVVALWFA
AMASLFVWKF VQYRRTPAFR VMGYCLPTAK GAAETLKLNM ALVLLPVCRN TLTWLRSSWA
RFFMIATAIV VGITLHAGNH LACDFPRLIA SGPKEYRLVA DAFGPEKPTY VGLLSGVEGI
TGVAMVVLMI VSFTLATHPF RKGEKGGSGG GAAATVLPTV ARLPSPFNRL AGFNAFWYSH
HLLGIVYALL IAHGYFLFLV RRWYLKTTWM YISVPLMLYV GERMLRALRS NAYAVKILKV
CLLPGNVLTI TMSKPYGFRY RSGQYIFLQC PTISPFEWHP FSITSAPGDD YLSVHIRTNG
DWTQELKRIF VENYFSPHLN RRASFSELGA AEPRSLPRLL VDGPYGAPAQ DFRNYDVLLL
VGLGIGATPF ISILRDLLNN IKLAEELMDL AMETSRSEDS ANSFSVSTTS SNKKRAYRTS
RAHFYWVTRE PLSFEWFKGV MNEVAEMDKK GVIELHNYLT SVYEERDART TLLSMVQALN
HAKHGVDIVS GTRVRTHFAR PNWKEVFTRI ASKHPNSTVG VFYCGAPTLA KELKNLSHEM
SHRTGTRFHF HKEYF
//
