ID A0A0D9V5C2_9ORYZ Unreviewed; 858 AA.
AC A0A0D9V5C2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G25710.5, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR01G25710.5, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR01G25710.5, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR01G25710.5}
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; A0A0D9V5C2; -.
DR EnsemblPlants; LPERR01G25710.2; LPERR01G25710.2; LPERR01G25710.
DR EnsemblPlants; LPERR01G25710.5; LPERR01G25710.5; LPERR01G25710.
DR Gramene; LPERR01G25710.2; LPERR01G25710.2; LPERR01G25710.
DR Gramene; LPERR01G25710.5; LPERR01G25710.5; LPERR01G25710.
DR HOGENOM; CLU_005646_6_0_1; -.
DR Proteomes; UP000032180; Chromosome 1.
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; 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:SF153; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN F; 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; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
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:UP000032180};
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 297..316
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 436..456
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 476..500
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..673
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 173..208
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 530..650
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..42
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 14..35
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 858 AA; 97642 MW; 9D022423CF0E44F4 CRC64;
MRGGGASADH HQRWGSASAG TTPRSLSTGS SPRGSDDRSC SDDGEELVEV TLDLQDDDTI
VLRSSALAAR AARRQRAQLD RTRSGAHKAL RGLRFISSNK ANNAWIEVQA NFDRLARDGY
LSRSDFAECI GMTESKEFAL ELFDTLSRRR RMKVDTINKE ELREIWQQIT DNSFDSRLQI
FFEMVDKNAD GRITEAEVKE IIMLSASANK LSRLKEQAEE YAALIMEELD PEGLGYIELW
QLETLLLQKD TYMNYSQALS YTSQALSQNM AGLRKKSPIR KISTTLSYYF EDNWKRLWVL
ALWIGIMAGL FAWKFMQYRN RYVFDVMGYC VTTAKGAAET LKLNMAIILL PVCRNTITWL
RSTRAARVLP FDDNINFHKT IAAAIVVGII LHAGNHLVCD FPRLIKSSDE KYAPLGQYFG
EIKPTYFTLV KGVEGITGVI MVVCMIIAFT LATRWFRRSL VKLPRPFDKL TGFNAFWYSH
HLFIIVYIAF IVHGECLYLI HVWYRRTTWM YLSVPVCLYV GERTLRFFRS GSYSVRLLKV
AIYPGNVLTL QMSKPPTFRY KSGQYMFVQC PAVSPFEWHP FSITSAPGDD YLSIHVRQLG
DWTRELKRVF AAACEPPVGG KSGLLRADET TKKTLPKLLI DGPYGSPAQD YSKYDVLLLV
GLGIGATPFI SILKDLLNNI IKMEEEEDAS TDLYPPIGRN KPHIDLGTLM TITSRPKKIL
KTTNAYFYWV TREQGSFDWF KGVMNEIADL DQRNIIEMHN YLTSVYEEGD ARSALITMLQ
ALNHAKNGVD IVSGTRVRTH FARPNWKKVL SKIASKHPYA KIGVFYCGAP VLAQELSKLC
HEFNGKCTSK FEFHKEHF
//
