ID Q0UA26_PHANO Unreviewed; 282 AA.
AC Q0UA26;
DT 05-SEP-2006, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 2.
DT 27-MAR-2024, entry version 92.
DE RecName: Full=FAD-binding FR-type domain-containing protein {ECO:0000259|PROSITE:PS51384};
GN ORFNames=SNOG_11388 {ECO:0000313|EMBL:EAT81096.2};
OS Phaeosphaeria nodorum (strain SN15 / ATCC MYA-4574 / FGSC 10173) (Glume
OS blotch fungus) (Parastagonospora nodorum).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Phaeosphaeriaceae;
OC Parastagonospora.
OX NCBI_TaxID=321614 {ECO:0000313|EMBL:EAT81096.2, ECO:0000313|Proteomes:UP000001055};
RN [1] {ECO:0000313|Proteomes:UP000001055}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN15 / ATCC MYA-4574 / FGSC 10173
RC {ECO:0000313|Proteomes:UP000001055};
RX PubMed=18024570; DOI=10.1105/tpc.107.052829;
RA Hane J.K., Lowe R.G., Solomon P.S., Tan K.C., Schoch C.L., Spatafora J.W.,
RA Crous P.W., Kodira C., Birren B.W., Galagan J.E., Torriani S.F.,
RA McDonald B.A., Oliver R.P.;
RT "Dothideomycete-plant interactions illuminated by genome sequencing and EST
RT analysis of the wheat pathogen Stagonospora nodorum.";
RL Plant Cell 19:3347-3368(2007).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CH445343; EAT81096.2; -; Genomic_DNA.
DR RefSeq; XP_001801632.1; XM_001801580.1.
DR AlphaFoldDB; Q0UA26; -.
DR STRING; 321614.Q0UA26; -.
DR EnsemblFungi; SNOT_11388; SNOT_11388; SNOG_11388.
DR GeneID; 5978540; -.
DR KEGG; pno:SNOG_11388; -.
DR VEuPathDB; FungiDB:JI435_113880; -.
DR eggNOG; KOG0039; Eukaryota.
DR HOGENOM; CLU_005646_2_0_1; -.
DR InParanoid; Q0UA26; -.
DR OrthoDB; 367877at2759; -.
DR Proteomes; UP000001055; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR InterPro; IPR000778; Cyt_b245_heavy_chain.
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:SF39; FAD-BINDING FR-TYPE DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR11972; NADPH OXIDASE; 1.
DR Pfam; PF08022; FAD_binding_8; 1.
DR Pfam; PF08030; NAD_binding_6; 1.
DR PRINTS; PR00466; GP91PHOX.
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.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 4: Predicted;
KW Electron transport {ECO:0000256|ARBA:ARBA00022982};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001055};
KW Transport {ECO:0000256|ARBA:ARBA00022982}.
FT DOMAIN 1..97
FT /note="FAD-binding FR-type"
FT /evidence="ECO:0000259|PROSITE:PS51384"
SQ SEQUENCE 282 AA; 31893 MW; 591503EA6F530100 CRC64;
MRYKPGQWLF LNCPEVSYHQ WHPFTITSCP NDPYISVHVR QVGDFTRALA DALGAGQSQS
KLYDELDPMG MYEIALQHGQ KMPSLKIDGP YGAPAEDVFE NEVAVLIGTG IGVTPWASIL
KSIYHLRLSP NPPKRLRRVE FIWVCKDTSS FEWFQTLLSS LEAQSLGGAD GDQFLRIHTY
LTQKMDANTA QNIVLNSVGT DKDPLTELKS RTNFGRPDFQ RLLSGMRDGI LDRTYMNGLE
STLRTEVGVY FCGPNVAARD IKKACKMATC QEVNFKFWKE HF
//