ID A0A498I5G8_MALDO Unreviewed; 812 AA.
AC A0A498I5G8;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=DVH24_023716 {ECO:0000313|EMBL:RXH77442.1};
OS Malus domestica (Apple) (Pyrus malus).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Rosales; Rosaceae; Amygdaloideae; Maleae; Malus.
OX NCBI_TaxID=3750 {ECO:0000313|EMBL:RXH77442.1, ECO:0000313|Proteomes:UP000290289};
RN [1] {ECO:0000313|EMBL:RXH77442.1, ECO:0000313|Proteomes:UP000290289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. HFTH1 {ECO:0000313|Proteomes:UP000290289};
RC TISSUE=Young leaf {ECO:0000313|EMBL:RXH77442.1};
RA Hu J.;
RT "A high-quality apple genome assembly.";
RL Submitted (OCT-2018) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RXH77442.1}.
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DR EMBL; RDQH01000340; RXH77442.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A498I5G8; -.
DR STRING; 3750.A0A498I5G8; -.
DR Proteomes; UP000290289; Chromosome 14.
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 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:SF127; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN A-LIKE; 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:UP000290289};
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 281..301
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 425..445
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 465..489
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 165..200
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 520..626
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 812 AA; 92758 MW; BD67E3E556E8F91F CRC64;
MEAHVQLQTA HQPYVSAMSP SSSSSSSSSS CSASVFPPSF SPIWTEPHDE TGVLNRQQHY
MAENGEASST AGSANEIEWL RFIDITANGG MKWKDVEEQF DRLALTRHGV EPAIKSSDFG
LCIGMQQSPE FANELLRTLR RRMDRNFDMT KCELYGYWCL MTDPRFDSRI RIYFDLCDKN
MDGRVTEKDI KQIITLSAST NKLSLTHEEA EDYAALVMKL LDTENRSYLE FPQFRTLFNV
MSLSKSSFST NHFSIRLSRL HHNFDPTEEP RSKTEILFRS YWRRAWIVLL WLIICSALFA
WKFTQYRHRA AFQVMGYCLS TAKGAAETLK FNMALILLPV CRNTITWLRK NRSINSIIPF
NDNINFHKMI AGGIVVGVIL HGGSHLACDF PRISDSDRMV FRQTIAARFG YHQPSYCEIL
ATKEVATGIA MVVLMAIAFS LATKWPRRQS PSLPKSVRNI TGYNAFWYSH HLFIPVYALL
ILHSMFLFLT NKATEKTTWM YIAVPVVLYA GERVFRAIRS GFYEVEILKA SIYPGKVLSL
KLQKPEGFRY LSGMYIFIQC PQISPFEWHP FSLTSGPEDD YLSVHIRTAG DWSYQIYSLF
QEATLSGVDG YPKVHIDGPY GAASQDHVKY DIVVLIGLGI GATPFVSILK DVVNAAKKPH
CDHSGCRECS SRKAPLKAYL YWVTREQSSF DWFRDIMKEV SISNQKQSLV EMHNFLTCVY
PEGDARSVLI STIQALHHAK NGTDFLSRTP VRTHFGRPDW FDIFSKLARG HKEERIGVFY
CGPSSAAKEL ERMCTRLSTK TSTRFVFHKE NY
//
