ID   A0A1M2VZU7_TRAPU        Unreviewed;       493 AA.
AC   A0A1M2VZU7;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:OJT13141.1};
GN   ORFNames=TRAPUB_10296 {ECO:0000313|EMBL:OJT13141.1};
OS   Trametes pubescens (White-rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Polyporales; Polyporaceae; Trametes.
OX   NCBI_TaxID=154538 {ECO:0000313|EMBL:OJT13141.1, ECO:0000313|Proteomes:UP000184267};
RN   [1] {ECO:0000313|EMBL:OJT13141.1, ECO:0000313|Proteomes:UP000184267}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FBCC735 {ECO:0000313|EMBL:OJT13141.1,
RC   ECO:0000313|Proteomes:UP000184267};
RA   Makela M.R., Granchi Z., Peng M., De Vries R.P., Grigoriev I., Riley R.,
RA   Hilden K.;
RT   "Genome sequence of the basidiomycete white-rot fungus Trametes
RT   pubescens.";
RL   Submitted (OCT-2016) 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:OJT13141.1}.
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DR   EMBL; MNAD01000423; OJT13141.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M2VZU7; -.
DR   STRING; 154538.A0A1M2VZU7; -.
DR   OMA; DDWEVYV; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000184267; 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   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:OJT13141.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000184267}.
SQ   SEQUENCE   493 AA;  54747 MW;  58817DB956C52702 CRC64;
     MASSSASAPH DAQEKRICVI GAGPSGLGAI KIVKDAPEFK AEKWTVTAFE ARETLGGVWN
     PAPADPSAAE PPLTALYDSL TTNTPHPLMS YTSYPFPPET PLYPPAPTVL AYLHLYAEKF
     DLLPHIRFGT SVVSLHWNTA VHKWDVIVKG SEEEHLQFDL VLVANGHYRV PRIPDTPGLE
     AWTAAGKVTH SVWYRRPEDY TGKLLVAGGG YSGMDVASET RPFAREVIHS ITRATSEDED
     GGKFKRRGRV TEYRDAAAGE VVFEDGTTES GIDHVVLATG YQFAFPFLTA PEVLPALPPR
     VPPIPEALYN STYHIFPLAK HLFPLVTSYP PSSLAFLGLP LRVAPLPLTE IQTQVALKLL
     ADPSALDLTH EATAVRARYN AFRASLQARA QVFAADETAL EVAIADAWFR FGFTEQFDYR
     DELYEFVGTE YRVPVWEREL FEQKDLLRER CRELQRKGEE GKWLKGVGAG ADPVQEWADY
     MWRVLEGKAP LEE
//