ID A0A443HWV0_BYSSP Unreviewed; 479 AA.
AC A0A443HWV0;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 10.
DE SubName: Full=Putative dimethylaniline monooxygenase {ECO:0000313|EMBL:RWQ96224.1};
GN ORFNames=C8Q69DRAFT_506430 {ECO:0000313|EMBL:RWQ96224.1};
OS Byssochlamys spectabilis (Paecilomyces variotii).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Thermoascaceae; Paecilomyces.
OX NCBI_TaxID=264951 {ECO:0000313|EMBL:RWQ96224.1, ECO:0000313|Proteomes:UP000283841};
RN [1] {ECO:0000313|EMBL:RWQ96224.1, ECO:0000313|Proteomes:UP000283841}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 101075 {ECO:0000313|EMBL:RWQ96224.1,
RC ECO:0000313|Proteomes:UP000283841};
RX PubMed=30619145; DOI=10.3389/fmicb.2018.03058;
RA Urquhart A.S., Mondo S.J., Makela M.R., Hane J.K., Wiebenga A., He G.,
RA Mihaltcheva S., Pangilinan J., Lipzen A., Barry K., de Vries R.P.,
RA Grigoriev I.V., Idnurm A.;
RT "Genomic and genetic insights into a cosmopolitan fungus, Paecilomyces
RT variotii (Eurotiales).";
RL Front. Microbiol. 9:3058-3058(2018).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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:RWQ96224.1}.
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DR EMBL; RCNU01000004; RWQ96224.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443HWV0; -.
DR STRING; 264951.A0A443HWV0; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000283841; Unassembled WGS sequence.
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; 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:RWQ96224.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000283841}.
SQ SEQUENCE 479 AA; 54052 MW; 9E80FE266371D627 CRC64;
MGPRYRTVAV IGTGPSGLSA VRALHQEKIF DTIRVFERRD RVGGTWNYDP VPDVFPFPED
NSTSQKAKDI PARFPQFTPT AAEDTTARTG IYEGLDSNVG AKVMAFTHTP LPETNSPLSI
ERFGNSNPTR PFRVVAQWLE DLFHDYLHLV SFNTTVEKVE KVGDKWTVTL RRTGQLRHGQ
PQDYWWQEHF DAIVVASGHY NIPFIPDVPG LNEASKAHPT RFEHSKSYRS QNDYINKKVV
VVGGNVSAAD IVSEIYHLVK GPLYLSQRGK NEALQAAWDL PNVEVKPQIK NIETTPTGIN
VEFADGNKAD NVDKVIFGTG FRVSYPFLTP DPVTPNNRLA GFYQHIFKVG DPSLAIVGQV
RAGISFRVYE YQAVAVARYF AGRGKPLPSL QEQDLWEVER VQYKGPSTNF HEIKPDFKEY
FDFLVNLAGP PAPESDAYEL PPWDDKWAEI AFGVLPLKEK YWKSVRERSS KLGQQRAKL
//
