ID A0A061FAG0_THECC Unreviewed; 889 AA.
AC A0A061FAG0;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE SubName: Full=Respiratory burst oxidase B {ECO:0000313|EMBL:EOY11489.1};
GN ORFNames=TCM_026646 {ECO:0000313|EMBL:EOY11489.1};
OS Theobroma cacao (Cacao) (Cocoa).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Byttnerioideae; Theobroma.
OX NCBI_TaxID=3641 {ECO:0000313|EMBL:EOY11489.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY11489.1, ECO:0000313|Proteomes:UP000026915}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Matina 1-6 {ECO:0000313|Proteomes:UP000026915};
RX PubMed=23731509; DOI=10.1186/gb-2013-14-6-r53;
RA Motamayor J.C., Mockaitis K., Schmutz J., Haiminen N., Iii D.L.,
RA Cornejo O., Findley S.D., Zheng P., Utro F., Royaert S., Saski C.,
RA Jenkins J., Podicheti R., Zhao M., Scheffler B.E., Stack J.C., Feltus F.A.,
RA Mustiga G.M., Amores F., Phillips W., Marelli J.P., May G.D., Shapiro H.,
RA Ma J., Bustamante C.D., Schnell R.J., Main D., Gilbert D., Parida L.,
RA Kuhn D.N.;
RT "The genome sequence of the most widely cultivated cacao type and its use
RT to identify candidate genes regulating pod color.";
RL Genome Biol. 14:R53.1-R53.24(2013).
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; CM001883; EOY11489.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061FAG0; -.
DR STRING; 3641.A0A061FAG0; -.
DR EnsemblPlants; EOY11489; EOY11489; TCM_026646.
DR Gramene; EOY11489; EOY11489; TCM_026646.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; A0A061FAG0; -.
DR OMA; AFWYTHQ; -.
DR Proteomes; UP000026915; Chromosome 5.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016174; F:NAD(P)H oxidase H2O2-forming activity; IBA:GO_Central.
DR GO; GO:0004601; F:peroxidase activity; IEA:UniProtKB-KW.
DR GO; GO:0009408; P:response to heat; IEA:EnsemblPlants.
DR GO; GO:0009845; P:seed germination; IEA:EnsemblPlants.
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:SF64; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN B; 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; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
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:UP000026915};
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 341..360
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 481..502
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..722
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 216..251
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 576..699
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 889 AA; 101150 MW; 43C294EB6BCB543D CRC64;
MEIRHSKHES WSDTESTSSN RVGYSGPLSG PILMNNKKSS SKKSARFKDG DDEYVEITLD
IREDSVSVQN IKGGDPETAM LATRLEKRPS FGSQLSFRIR QVSQELKRMT STKAAAPFNK
VDRSKSGAAR ALQGLKFMTT KNVGSEGWSE VEKRFDELSV DGSLLKSLFG QCIGMNESKE
FASELFEALA RRRGITSSAI SKAELREFWE QISDHGFDAR LQTFFDMVDK DADGRITEEE
VKEIIALSAS ANKLSKIQES AEEYAALIME ELDKDNLGYI EIYNLETLLL QAPSQSTNLV
TDSRILSRLL SEKLVPTKER NPIKRWGRGL AYFLEDNWKR IWVLALWISI CAGLFTWKFI
QYKHRAVFDV MGYCVTTAKG AAETTKFNMA LILLPVCRNT ITWLRSRTKL GVVVPFDDNI
NFHKVVALGI AIGVGLHAGA HLTCDFPRLL HATDEEYEPM KPFFGEKRPN NYWWFVKGTE
GWTGVAMVVL MAIAYILAQP WFRRNRLNLP KPIKKLTGFN AFWYSHHLFV IVYALFIVHG
YFLYLSKKWY KKTTWMYLAV PMLLYACERL IRAFRSGYKS VKILKVAVYP GNVLSLHMSK
PQGFKYTSGQ YIFVNCAAVS PFQWHPFSIT SSPADDYLSI HIRTLGDWTS QLKALFVKVC
QPPSVNQSGL LRADIGKGEN KPRLPKLLID GPYGAPAQDY KKYDVLLLVG LGIGATPLIS
IVKDVLNNIK QQKEMEEGIE NGVKNNKRKP FATKRAYFYW VTREQGSFEW FRGVMNEVAE
YDRDRMIELH NYCTSVFEEG DARSALITML QSLHHAKSGV DIVSGTRVKT HFARPNWHKV
FKHVAVNHAN QRVGVFYCGA PGLTGELRRL AQDFSRKTST KFDFHKENF
//