ID B2WHN5_PYRTR Unreviewed; 502 AA.
AC B2WHN5;
DT 01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT 01-JUL-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
DE SubName: Full=Flavin-containing monooxygenase {ECO:0000313|EMBL:EDU42545.1};
GN ORFNames=PTRG_09494 {ECO:0000313|EMBL:EDU42545.1};
OS Pyrenophora tritici-repentis (strain Pt-1C-BFP) (Wheat tan spot fungus)
OS (Drechslera tritici-repentis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=426418 {ECO:0000313|EMBL:EDU42545.1, ECO:0000313|Proteomes:UP000001471};
RN [1] {ECO:0000313|Proteomes:UP000001471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pt-1C-BFP {ECO:0000313|Proteomes:UP000001471};
RX PubMed=23316438; DOI=10.1534/g3.112.004044;
RA Manning V.A., Pandelova I., Dhillon B., Wilhelm L.J., Goodwin S.B.,
RA Berlin A.M., Figueroa M., Freitag M., Hane J.K., Henrissat B., Holman W.H.,
RA Kodira C.D., Martin J., Oliver R.P., Robbertse B., Schackwitz W.,
RA Schwartz D.C., Spatafora J.W., Turgeon B.G., Yandava C., Young S., Zhou S.,
RA Zeng Q., Grigoriev I.V., Ma L.-J., Ciuffetti L.M.;
RT "Comparative genomics of a plant-pathogenic fungus, Pyrenophora tritici-
RT repentis, reveals transduplication and the impact of repeat elements on
RT pathogenicity and population divergence.";
RL G3 (Bethesda) 3:41-63(2013).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; DS231625; EDU42545.1; -; Genomic_DNA.
DR RefSeq; XP_001939826.1; XM_001939791.1.
DR AlphaFoldDB; B2WHN5; -.
DR EnsemblFungi; EDU42545; EDU42545; PTRG_09494.
DR GeneID; 6347784; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; B2WHN5; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000001471; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:EnsemblFungi.
DR GO; GO:0004499; F:N,N-dimethylaniline monooxygenase activity; IEA:EnsemblFungi.
DR GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR000960; Flavin_mOase.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PIRSF; PIRSF000332; FMO; 3.
DR PRINTS; PR00370; FMOXYGENASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:EDU42545.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001471}.
FT REGION 69..100
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 502 AA; 56068 MW; E3CB43A22A678CDE CRC64;
MTENERISIR ARTVAVVGAG PSGVIAAKYL RAEKAFDKID LFEQRSQAGG IWTYTGDQRD
ENLFSIPQEN PEPGVQEPEW KPKDTISSEN NHTNSINGTS KVPSFLSPMY EQLETNIPRG
LMGFQDLDWP SDSQLFPTHD TVLKYIQDYT SPVQENIHYN TQVTSITPTT PSSPTTTWTI
TTLNLLTNET ITSTYSAVII ANGHFIVPHI PSIPGISEWS SQHPGLITHS KYYRRPTDFT
AKKTIVIGNS ASGADLSKQI SSHCPQPLLW STRSTSLFSA THGSASAEDP TRRPVPPIAR
FLPDTRGVQF ADGSMEHDID AVVFATGYFY SLPFLNGVEP KLITSGERVE GTYKHLFNAV
RPTLCFLALP QRVIPFPLAE AQAAVVARVY AGRLTLPPTA TMQAWQEEVE AEMGQGRNFH
LLPFPKDAQY INEMSQWAMS AEGKDGLENA GKGKCPPVWG EWEFKCRENF PEIRRRFGER
GEERREVRDV RELGFEFGER KG
//
