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Database: UniProt
Entry: M2Y4Q6_GALSU
LinkDB: M2Y4Q6_GALSU
Original site: M2Y4Q6_GALSU 
ID   M2Y4Q6_GALSU            Unreviewed;       775 AA.
AC   M2Y4Q6;
DT   01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   01-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   SubName: Full=NADPH oxidase {ECO:0000313|EMBL:EME30933.1};
GN   ORFNames=Gasu_17010 {ECO:0000313|EMBL:EME30933.1};
OS   Galdieria sulphuraria (Red alga).
OC   Eukaryota; Rhodophyta; Bangiophyceae; Galdieriales; Galdieriaceae;
OC   Galdieria.
OX   NCBI_TaxID=130081 {ECO:0000313|EMBL:EME30933.1, ECO:0000313|Proteomes:UP000030680};
RN   [1] {ECO:0000313|Proteomes:UP000030680}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=074W {ECO:0000313|Proteomes:UP000030680};
RX   PubMed=23471408; DOI=10.1126/science.1231707;
RA   Schonknecht G., Chen W.H., Ternes C.M., Barbier G.G., Shrestha R.P.,
RA   Stanke M., Brautigam A., Baker B.J., Banfield J.F., Garavito R.M., Carr K.,
RA   Wilkerson C., Rensing S.A., Gagneul D., Dickenson N.E., Oesterhelt C.,
RA   Lercher M.J., Weber A.P.;
RT   "Gene transfer from bacteria and archaea facilitated evolution of an
RT   extremophilic eukaryote.";
RL   Science 339:1207-1210(2013).
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DR   EMBL; KB454495; EME30933.1; -; Genomic_DNA.
DR   RefSeq; XP_005707453.1; XM_005707396.1.
DR   AlphaFoldDB; M2Y4Q6; -.
DR   STRING; 130081.M2Y4Q6; -.
DR   TCDB; 5.B.1.1.11; the phagocyte (gp91(phox)) nadph oxidase family.
DR   EnsemblPlants; EME30933; EME30933; Gasu_17010.
DR   GeneID; 17089628; -.
DR   Gramene; EME30933; EME30933; Gasu_17010.
DR   KEGG; gsl:Gasu_17010; -.
DR   eggNOG; KOG0039; Eukaryota.
DR   OMA; ENACACA; -.
DR   OrthoDB; 5489970at2759; -.
DR   Proteomes; UP000030680; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   CDD; cd06186; NOX_Duox_like_FAD_NADP; 1.
DR   Gene3D; 3.40.50.80; Nucleotide-binding domain of ferredoxin-NADP reductase (FNR) module; 2.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   InterPro; IPR013112; FAD-bd_8.
DR   InterPro; IPR017927; FAD-bd_FR_type.
DR   InterPro; IPR013121; Fe_red_NAD-bd_6.
DR   InterPro; IPR039261; FNR_nucleotide-bd.
DR   InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR   PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR   PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR   Pfam; PF08022; FAD_binding_8; 1.
DR   Pfam; PF08030; NAD_binding_6; 1.
DR   SUPFAM; SSF52343; Ferredoxin reductase-like, C-terminal NADP-linked domain; 1.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 1.
DR   PROSITE; PS51384; FAD_FR; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000030680};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..153
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        173..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        209..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        504..524
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        530..552
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        564..589
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        601..622
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          249..373
FT                   /note="FAD-binding FR-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51384"
SQ   SEQUENCE   775 AA;  87155 MW;  02C77A655B083163 CRC64;
     MTKAFYKRAS VTGNNSYRGS KDSNRFDSFL KLEAFMVNNG MLWTLLLFIA CMDIIGFLAG
     VFNMITATQQ HIITIPFLER SLPVAKGAGR VISINAALLL LTGCKATITW LRSTFVSCLL
     PIDKLMPFLH IRLYLIIAFC AALHAITQYV NYITGSFPWV FGLWTYHFPD PTVQLLITGT
     LLVILMTAIA VTAGPWIRRS VNRGYNIFWT VHIVGFSCVY PLLILHGVLL GTPDTWKYIL
     GPLVLYVIDV LYRARAVSFK GLSVVCWLNP SSEGVTELVM KRPFAYKAGQ YVQIRIPVVS
     RWEYHPLSIA SAPHEEYLRI FIKSSGDWSS LVYKVSEELQ SDSFAFSDAA SQVDARGFTI
     VNVRGPFGAP TEHVKDFSKV VLVGTGIGAT PFSSVVREYL HANSKEDQAA KRVHQTVLNL
     SQLEKPSSAL VKDTKDHNNN SPSLRKVETL LPSFFMNMTQ LAYRGIVDPF LVFFKRTSIS
     FKSENACACA FLGFFHSLSL NFMVLWMMMI AGSIRVAFVL FGYHGQYSSA IWGLVVSVII
     LFVFGFSLFI AIRSLGWKYW KTAIGVLDSL AFFIGLALFI CVFVCIASWG TKSVWTIEKV
     LNYLTFYCLI PVVGIRALLL IVNGCGGFKW KRSAKSNLKT ECSKSLHFIW VSRTVHGFHW
     FFRDFERIVS EGSSVQVQMD IFVTGVTSDI TLPENSSKIR YHIGRPQWDS LFSSMFESEE
     FIRDQEPVGV FFCGAPAVGR IVKAAANEAS LQAARRQYVT GNRCFPKIIF HKEYF
//
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