ID Q4WLJ1_ASPFU Unreviewed; 549 AA.
AC Q4WLJ1;
DT 05-JUL-2005, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2005, sequence version 1.
DT 27-MAR-2024, entry version 111.
DE SubName: Full=NADPH oxidase (NoxA), putative {ECO:0000313|EMBL:EAL89173.1};
GN ORFNames=AFUA_6G13350 {ECO:0000313|EMBL:EAL89173.1};
OS Aspergillus fumigatus (strain ATCC MYA-4609 / CBS 101355 / FGSC A1100 /
OS Af293) (Neosartorya fumigata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000313|EMBL:EAL89173.1, ECO:0000313|Proteomes:UP000002530};
RN [1] {ECO:0000313|EMBL:EAL89173.1, ECO:0000313|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000313|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.,
RA Fedorova N., Fedorova N., Feldblyum T.V., Fischer R., Fosker N., Fraser A.,
RA Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B., Haas H., Harris D., Horiuchi H.,
RA Huang J., Humphray S., Jimenez J., Keller N., Khouri H., Kitamoto K.,
RA Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafon A., Latge J.P.,
RA Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L., Mohamoud Y.,
RA Molina M., Monod M., Mouyna I., Mulligan S., Murphy L., O'Neil S.,
RA Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L., Quail M.A.,
RA Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U., Renauld H.,
RA Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M., Ronning C.M.,
RA Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C., Saunders D.,
RA Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F., Turner G.,
RA Vazquez de Aldana C.R., Weidman J., White O., Woodward J., Yu J.H.,
RA Fraser C., Galagan J.E., Asai K., Machida M., Hall N., Barrell B.,
RA Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAL89173.1}.
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DR EMBL; AAHF01000006; EAL89173.1; -; Genomic_DNA.
DR RefSeq; XP_751211.1; XM_746118.1.
DR AlphaFoldDB; Q4WLJ1; -.
DR STRING; 330879.Q4WLJ1; -.
DR EnsemblFungi; EAL89173; EAL89173; AFUA_6G13350.
DR GeneID; 3508521; -.
DR KEGG; afm:AFUA_6G13350; -.
DR VEuPathDB; FungiDB:Afu6g13350; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_3_0_1; -.
DR InParanoid; Q4WLJ1; -.
DR OMA; FTFAKEH; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005739; C:mitochondrion; IEA:UniProtKB-KW.
DR GO; GO:0043020; C:NADPH oxidase complex; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0016175; F:superoxide-generating NAD(P)H oxidase activity; IBA:GO_Central.
DR GO; GO:0006952; P:defense response; IBA:GO_Central.
DR GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
DR GO; GO:0042554; P:superoxide anion generation; IBA:GO_Central.
DR CDD; cd06186; NOX_Duox_like_FAD_NADP; 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; 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; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR11972:SF39; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF01794; Ferric_reduct; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR SFLD; SFLDS00052; Ferric_Reductase_Domain; 1.
DR SFLD; SFLDG01168; Ferric_reductase_subgroup_(FRE; 1.
DR SFLD; SFLDG01169; NADPH_oxidase_subgroup_(NOX); 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 Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000002530};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}; Transport {ECO:0000256|ARBA:ARBA00023065}.
FT TRANSMEM 14..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 52..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..116
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 136..157
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 169..188
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 238..361
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 549 AA; 63097 MW; B2A7915924C71346 CRC64;
MRHPLSSQFT GSKILFYVLF WGVHIGIFAT GWHIQASNHK LDALNALKWS VWFSRAAGLV
LTVDGTLILL PMCRNLITLA RPRIRWLPLD ESIWFHRQVA YALLIFTIIH VASHYVNFYN
IEKDKIRPVT AIQLHYTQAG GITGHVMLLC MMLMYTTSHH RIRQQSFETF WYTHHLFIPF
LLALYTHATG CFVRDTPEPT SPFAGKRFWN HCIGYQGWRW ELVGGSLYLM ERLYREIRSR
RATVITKVIR HPYDAMEIQF RKDSMKYKAG QWLFIQVPEV SNTQWHPFTI TSCPFDPYIS
IHVRQVGDFT RALGDALGCG PAQARDMEGL DPLGMYEVAL QNGQKMPKLL VDGPYGAPAE
DVFENEIAVL IGTGIGVTPW ASILKNIWHL RTGPNPPRRL RRVEFIWVCK DTSSFEWFQA
LLSSLESQSA SAAASQGSAE FLRIHTYLTQ RLDEDTAANI YLNSVGQEVD PLTELRSRTN
FGRPDFNRLF TAMRDGLHDQ TYMPGFHPAM TTEIGVYFCG PNAAARQIRE AAKRASTRDV
RFKFWKEHF
//
