ID A0A061GSV8_THECC Unreviewed; 971 AA.
AC A0A061GSV8;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE SubName: Full=Respiratory burst oxidase protein E {ECO:0000313|EMBL:EOY30174.1};
GN ORFNames=TCM_037473 {ECO:0000313|EMBL:EOY30174.1};
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:EOY30174.1, ECO:0000313|Proteomes:UP000026915};
RN [1] {ECO:0000313|EMBL:EOY30174.1, 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; CM001887; EOY30174.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A061GSV8; -.
DR STRING; 3641.A0A061GSV8; -.
DR EnsemblPlants; EOY30174; EOY30174; TCM_037473.
DR Gramene; EOY30174; EOY30174; TCM_037473.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_6_0_1; -.
DR InParanoid; A0A061GSV8; -.
DR OMA; CRSEHYS; -.
DR Proteomes; UP000026915; Chromosome 9.
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 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:SF44; RESPIRATORY BURST OXIDASE HOMOLOG PROTEIN E; 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: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 406..425
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 539..566
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 586..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 282..317
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT DOMAIN 640..761
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 971 AA; 110266 MW; 0A17DAE7055F5231 CRC64;
MESPRSFSMG NDKVPVRCGF QITQEFRAWK EESGLMKSPA SFHSFGRSSS KLSNYSRSFD
LPDDLEDLSA DDYGVGGAML PIFLSDLQRN NQQDLVEVTL ELENDSIVFC SVTPSTPPIT
DQKEASSVTA SSGILGRSLS ATSRIRRKFA WLKSGSSSRA SSSAENDQDR RITARDERRI
KAKLQRTKSS AQRALRGLRF ISKTTGANDA EEMWRRVESR FESLAKDGLL AREDFGDCIG
MVDSKEFAVG IFDALARRRR QRMGKITKEE LHDFWLQISD QSFDARLQIF FDMADSNEDG
RVTREEVQEL IMLSASANKL SKLKEQAEEY ASLIMEELDP ENFGYIELWQ LETLLLQRDN
YMNNSRPLST TSVAWSQNIS SARPKNMFRR VCFALRCLVL ENWRRGWILL LWMMAMATLF
AWKFMQYKNR AAFQVMGYCL CTAKGAAETL KLNMALILLP VCRNTLTWLR STKARSFVPF
DDNINFHKII ACAIAIGVLV HAGSHLSCDF IRLTRSSPEK FALIASDFSH GKRPTYLELL
TGVLGVTGIS MVIFMAIAFI LATSHFRRNV LRLPAPFNRL TGFNAFWYSH HLLGLVYVLL
VIHGTFLFLA HKWYQRSTWM YISAPLLLYM GERSVRTCRS EHYSVKIFKV SVLPGNVFSM
VMSKPPGFKY KSGQYIFLQC PSISPFEWHP FSITSAPGDE CLSVHIRTVG DWTQELKRVF
TDVNDSPFVI GRARFGQPGH IDQNGQPKLL VDGPYGAPAQ DYRNYDVLLL AGLGIGATPF
ISILRDLLNN SRAEDQMSST TEMTRSDDSW NSLASSNFTA KSSSTNGGKK KPQRTRNAYF
YWVTREPGSF EWFKGVMDEV AEMDHKGQIE LHNYLTSVYE EGDARSTLIT MVQALNHAKH
GVDILSGTRV RTHFARPNWK EVFSKIASKH PHATVGVFYC GMPVLAKELK KLSRELSHKT
STRFEFHKEY F
//
