ID H6C9Y7_EXODN Unreviewed; 503 AA.
AC H6C9Y7;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 41.
DE SubName: Full=Dimethylaniline monooxygenase (N-oxide forming) {ECO:0000313|EMBL:EHY60798.1};
GN ORFNames=HMPREF1120_08742 {ECO:0000313|EMBL:EHY60798.1};
OS Exophiala dermatitidis (strain ATCC 34100 / CBS 525.76 / NIH/UT8656) (Black
OS yeast) (Wangiella dermatitidis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=858893 {ECO:0000313|EMBL:EHY60798.1, ECO:0000313|Proteomes:UP000007304};
RN [1] {ECO:0000313|EMBL:EHY60798.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NIH/UT8656 {ECO:0000313|EMBL:EHY60798.1};
RG The Broad Institute Genome Sequencing Platform;
RA Cuomo C., Wang Z., Hunicke-Smith S., Szanislo P.J., Earl A., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Exophiala (Wangiella) dermatitidis NIH/UT8656.";
RL Submitted (JUL-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; JH226136; EHY60798.1; -; Genomic_DNA.
DR RefSeq; XP_009161259.1; XM_009163011.1.
DR AlphaFoldDB; H6C9Y7; -.
DR GeneID; 20313381; -.
DR VEuPathDB; FungiDB:HMPREF1120_08742; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_3_1; -.
DR InParanoid; H6C9Y7; -.
DR OMA; PSYPFWN; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000007304; 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 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:EHY60798.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007304}.
FT REGION 458..488
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 503 AA; 57293 MW; 4EBABB4EE4485EFA CRC64;
MEARQIKSVA IIGAGAAGAA AAAAFGAEEC FDTIRVFERR HSAGGTWIYD KNPKTDVQLV
PGALPPDIDR PLKIPDQLPT TTAPTPKERY EQTPIYDELT TNVPAIAMSF SDIPFPYGPF
TPHWIPRQYI EGYFSSHRTD SYLVLNTTVE DVSRLPAKTS SGLDKWKLVL RQYDTVKQAD
VWWEEVFDSV IIANGHYSIP FVPPVTGLSE YLKTFPGRVS HSKTYRTPEA YRGTRVIVIG
NSASGHDITT ALVKVARLPV YQSRRSRSRW DGDEPPDGIE WKPVIKEYRN NGDVVFDDDS
VLSSVDAIIY CTGYRPSFPF WNSQANGRPL FDYRENRLIG NYLHTFLRDF PTLGIVGMPR
VLTFRSFEYQ AIALARLFAG RNAIPLPPRE VQRRWEENRA ELVRRERRKF HDIPWDNGET
MQWLRLLFEM AGLPKLEGTG RCPPILNRET RWAIENIKKY PERGSGNKEP RSRAPQDPEA
EEHTDADWVV LSADEVKDTL HLI
//
