ID A0A316UDI5_9BASI Unreviewed; 552 AA.
AC A0A316UDI5;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:PWN22948.1};
GN ORFNames=BCV69DRAFT_266456 {ECO:0000313|EMBL:PWN22948.1};
OS Pseudomicrostroma glucosiphilum.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Exobasidiomycetes; Microstromatales; Microstromatales incertae sedis;
OC Pseudomicrostroma.
OX NCBI_TaxID=1684307 {ECO:0000313|EMBL:PWN22948.1, ECO:0000313|Proteomes:UP000245942};
RN [1] {ECO:0000313|EMBL:PWN22948.1, ECO:0000313|Proteomes:UP000245942}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 4718 {ECO:0000313|EMBL:PWN22948.1,
RC ECO:0000313|Proteomes:UP000245942};
RX PubMed=29771364; DOI=10.1093/molbev/msy072;
RA Kijpornyongpan T., Mondo S.J., Barry K., Sandor L., Lee J., Lipzen A.,
RA Pangilinan J., LaButti K., Hainaut M., Henrissat B., Grigoriev I.V.,
RA Spatafora J.W., Aime M.C.;
RT "Broad genomic sampling reveals a smut pathogenic ancestry of the fungal
RT clade Ustilaginomycotina.";
RL Mol. Biol. Evol. 0:0-0(2018).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KZ819322; PWN22948.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A316UDI5; -.
DR STRING; 1684307.A0A316UDI5; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000245942; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:InterPro.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000245942};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 44..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 401..424
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 454..473
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 552 AA; 61577 MW; C8A7905A92CCC01E CRC64;
MAVVASLDPF GIISLIYQAI QIVISWVFSP LYPQLQQPQK PLKHVAIIGA GITGISSASH
LLGHGFDVTI FEASQDVGGI WANVNSTSGL QISSILYRFH PSVKYTKGYP KRDEILENVK
KIWKSYGLDK KTRFNQKVTS ITRHESSGDP EKGGLSRWII NGNEGDIYDG LLVCTGTCGK
PKMLDLPNQE KFMGKIVHSS HLDGVDLKDK KVLIVGGGAS GVEALELAVA KGARKPMILA
RSDKWVIPRF TVVDTVLALQ PLGRQTWLSC IPEILLRKLH YRDLEEKMAP TTPFYASTPI
VNSTALQDIR EGKADYVRGD VVELQGHSVK FNKRKRGSKP EDEGQETNYA ADVIVVATGF
EIPPLDFLPD DLFPEDYVRP NLYLQNFSIK DVSVCCTNAS FIGAVGTVGH VHIGIYARIL
AVFLMDPSTR PLPRDARLWV DGIRWIKARA PGGALSFFTY MELMIWLVSF SFFKIERLKY
FFFILLGWGF WVRQSYDEQG QVMKDKKGRL TGEPHFRWSL TKLIPFYYAK TRYAVGSSPR
IGGPSAVKVN GA
//
