ID A0A0L9U5E7_PHAAN Unreviewed; 844 AA.
AC A0A0L9U5E7;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KOM37990.1};
GN ORFNames=LR48_Vigan03g137200 {ECO:0000313|EMBL:KOM37990.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM37990.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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 EMBL; CM003373; KOM37990.1; -; Genomic_DNA.
DR RefSeq; XP_017417628.1; XM_017562139.1.
DR AlphaFoldDB; A0A0L9U5E7; -.
DR STRING; 3914.A0A0L9U5E7; -.
DR EnsemblPlants; KOM37990; KOM37990; LR48_Vigan03g137200.
DR GeneID; 108328293; -.
DR Gramene; KOM37990; KOM37990; LR48_Vigan03g137200.
DR KEGG; var:108328293; -.
DR OMA; FTFAKEH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000053144; Chromosome 3.
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:SF54; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN J-RELATED; 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 SMART; SM00054; EFh; 2.
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:UP000053144};
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 291..308
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 375..393
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 429..452
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 472..492
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 662..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 167..202
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 526..656
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..71
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..63
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 844 AA; 96214 MW; 4BE7C98B62DDC912 CRC64;
MSSDKEGKDE SSTWILESIQ IHPADRSIRD EDDEPSPNAS PVLKSPSEGS QSNVRNRNVN
QGNGGRKMVR VESGAARGIK GLRFLDRTVT GKEADAWRSI EKRFTQHAVD GKLSKDKFGI
CMGMGPESKD FAGELYEALA RRRKICTENG ITLAEARVFW EDMTSKDLES RLQVFFDMCD
KNGDGRLSEE EVKEVIVLSA STNKLGNLKT NADGYAALIM EELDPDHNGY IEMWQLETLL
KEMVSSEDGP KKVNNTKAMN LSKAMIPSKY RTPVSKYVSK VTEFALDKWK IIWVVEIWLV
INLVLYIWKF KQYRQTGAFQ VMGYCVCFAK GAAETLKLNM ALIVLTMCRR TLTKLRESFL
SRIIPFDDNI NFHKTIAVAV VIGTLIHVMV HIFCDFPRLI SYPKDQFMAI LGDGFNYKQP
DYITLVKSIP GVTGIVMVLL MAFSFTLATH SFRKNVVKLP SPLHRLAGFN SFWYAHHLLI
VVYILLVIHG YYLFLTKEWQ KKTTWMYLVI PLSLYAFERI HPFFKGKDHR VNIIKAIVYT
GNVLALYMTK PPGFKYKSGM YIFIKCPDIS SFEWHPFSIT SAPGDEYLSV HVRTLGDWTT
ELKNKFTKVC EPHSAQTRRG SLMRMETRAP SSSFSKQGIR YPKILVKGPY GAPAQSYKNY
DVLFLIGLGI GATPMISILK DMLNHIKLGT PVEDSIQVNQ SDEAKKGPER AYFYWVTREQ
SSFEWFKGVM DDIADYDHDG IIEMHNYLTS VYEEGDARSA LIAMIQKLQH AKNGVDVVSE
SRIRTHFARP NWKKVFSQLA STHQTSRIGV FYCGSPTLTK VLKNLCQEFS LNTSTRFQFH
KENF
//
