ID A0A0N0NQY8_9EURO Unreviewed; 536 AA.
AC A0A0N0NQY8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3 {ECO:0000313|EMBL:KPI44468.1};
GN ORFNames=AB675_8428 {ECO:0000313|EMBL:KPI44468.1};
OS Phialophora attinorum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Phialophora.
OX NCBI_TaxID=1664694 {ECO:0000313|EMBL:KPI44468.1, ECO:0000313|Proteomes:UP000038010};
RN [1] {ECO:0000313|EMBL:KPI44468.1, ECO:0000313|Proteomes:UP000038010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 131958 {ECO:0000313|EMBL:KPI44468.1,
RC ECO:0000313|Proteomes:UP000038010};
RA Moreno L.F., Stielow B.J., de Hoog S., Vicente V.A., Weiss V.A.,
RA de Vries M., Cruz L.M., Souza E.M.;
RT "Draft genome of the ant-associated black yeast Phialophora attae CBS
RT 131958.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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:KPI44468.1}.
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DR EMBL; LFJN01000003; KPI44468.1; -; Genomic_DNA.
DR RefSeq; XP_018004431.1; XM_018148873.1.
DR AlphaFoldDB; A0A0N0NQY8; -.
DR GeneID; 28740753; -.
DR OrthoDB; 445965at2759; -.
DR Proteomes; UP000038010; 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; 1.
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:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
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:KPI44468.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000038010}.
SQ SEQUENCE 536 AA; 60407 MW; 9A77696EBDD7FC5C CRC64;
MGERVAVIGL GLHGVVALKN LREEGFDAVG FDKNPYIGGL WRYTTDETTL SVTQHTKTNN
SQQRLAFSDF PARYTTNYPD AREIADYIDE YAKHFNLVPH CRLGLGLHRL DRSDKSEHWD
LTLQGRDGSL VTEQFSRVLL TTGSQNRLVI PKFEGQEHFK GKIIHSRAFK DAKPFAGQRV
LLVGLSNTAG DVAAELSEVC PEVFVSHRSG VLVVERTPEG QKPTDHLATR RVNSIILTIN
RNFPRVAGYI GNIGLELKMK YAMKVKPEWG LLPAHPIANA APMMNDYFLD LSRSGRLKHS
PGISSMATDG HTINFTNGTS LSNVDTIILC TGAEPDFSFL GPSANPTLHP TPEWDNHRHN
FNHMPYPRLF RGVFPPSKHT ESLAFIGAYR GHGISAFINA DLASQAIAQV WKGNFELPPQ
AEREAWCDEH YKGMLRHLEA WRTVQVGQNA KEFERFLNEA AGNGINQKLG WGWEGWSFMF
RNWRLYRLLM DGVDGPWILR LFDSPREERG RKKWEGAEAE VWRVNGLEPP TSKKAV
//
