ID A0A087STW5_AUXPR Unreviewed; 738 AA.
AC A0A087STW5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=NADPH oxidase 1 {ECO:0000313|EMBL:KFM29169.1};
GN ORFNames=F751_3250 {ECO:0000313|EMBL:KFM29169.1};
OS Auxenochlorella protothecoides (Green microalga) (Chlorella
OS protothecoides).
OC Eukaryota; Viridiplantae; Chlorophyta; core chlorophytes; Trebouxiophyceae;
OC Chlorellales; Chlorellaceae; Auxenochlorella.
OX NCBI_TaxID=3075 {ECO:0000313|EMBL:KFM29169.1, ECO:0000313|Proteomes:UP000028924};
RN [1] {ECO:0000313|EMBL:KFM29169.1, ECO:0000313|Proteomes:UP000028924}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0710 {ECO:0000313|EMBL:KFM29169.1,
RC ECO:0000313|Proteomes:UP000028924};
RX PubMed=25012212; DOI=10.1186/1471-2164-15-582;
RA Gao C., Wang Y., Shen Y., Yan D., He X., Dai J., Wu Q.;
RT "Oil accumulation mechanisms of the oleaginous microalga Chlorella
RT protothecoides revealed through its genome, transcriptomes, and
RT proteomes.";
RL BMC Genomics 15:582-582(2014).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; KL662188; KFM29169.1; -; Genomic_DNA.
DR RefSeq; XP_011402222.1; XM_011403920.1.
DR AlphaFoldDB; A0A087STW5; -.
DR GeneID; 23614641; -.
DR KEGG; apro:F751_3250; -.
DR eggNOG; KOG0039; Eukaryota.
DR OrthoDB; 2671609at2759; -.
DR Proteomes; UP000028924; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
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 InterPro; IPR013112; FAD-bd_8.
DR InterPro; IPR013130; Fe3_Rdtase_TM_dom.
DR InterPro; IPR039261; FNR_nucleotide-bd.
DR PANTHER; PTHR11972:SF69; METALLOREDUCTASE AIM14-RELATED; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000028924};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 45..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 156..175
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..217
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 267..285
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 291..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 556..580
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 600..626
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 161..282
FT /note="Ferric oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01794"
FT DOMAIN 326..396
FT /note="FAD-binding 8"
FT /evidence="ECO:0000259|Pfam:PF08022"
FT REGION 507..530
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 738 AA; 83363 MW; 1EDC8EE4B9BAB3DF CRC64;
MWCQYFWYEG FEKIYGASMA RLGLVYTYGA GLDPPVKSLD MYDSFYILFL WVPLGGGALF
MILAQRLPNQ AKPGWMRRTQ ALGRRVMQYQ LPPHGFWIKQ TGGMSVLDVL MLVIVLLLNL
MWFCVGMKNF NDEHAAMRLA GIRTVEEVWQ LRLEWAGLYF GVLLFIDVWL LLLPIPQSSF
LQDLSGMDYH QMIRWHRWMG HITMIVTTIH GLLYFIFWGI THQFWTMFTD WSKDSSINYL
AGSISWFFGL ALWLTSMEWC RRGFWEVYYR FHIVCFFGFM FFAYVHYSGS WIYFSPGLLL
WFIDLVLRAG SYPNTTTVAN CGVSASEEVV TLQIQASKRA HGCPLHDIYL LFPTISRWQW
HPFTISHQSP DGVLTVRIKR FGGWTESLLN KLKNREPLPI RASCPQYNAP HRWRQDEVAV
VLAGGIASTA VLSVLSDLVA RRAQGKATGP RRVFFVWAAR HAVEFCVLDL SVAAASMSSD
GWLSTSLFYT GKEPLLAANQ HEKLDSLEKV SSHGSESGSE PRAGGAAKAK PLTFPRASPF
WWNRARRMQP QTTGPWHLAI VTGLVFFGGF VGQALSYSWY GEWQTHYQSL GEALPYNPFF
WKQAAVNCIV FCVIALGFPF LVAVFLPNLY WRDTRAGSTG EEQMAAFDGV WDPSSMGCEL
QGQEVVIPGS EAGIPIASGR PDIVAVLQGA AKETGARHIG VYVAGPEPMS RDAQIATCQL
NSTKGGAFFD FHKMAGML
//
