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Database: UniProt
Entry: A0A2T0FFW3_9ASCO
LinkDB: A0A2T0FFW3_9ASCO
Original site: A0A2T0FFW3_9ASCO 
ID   A0A2T0FFW3_9ASCO        Unreviewed;       429 AA.
AC   A0A2T0FFW3;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:PRT53881.1};
GN   ORFNames=B9G98_01501 {ECO:0000313|EMBL:PRT53881.1};
OS   Wickerhamiella sorbophila.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Trichomonascaceae; Wickerhamiella.
OX   NCBI_TaxID=45607 {ECO:0000313|EMBL:PRT53881.1, ECO:0000313|Proteomes:UP000238350};
RN   [1] {ECO:0000313|EMBL:PRT53881.1, ECO:0000313|Proteomes:UP000238350}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DS02 {ECO:0000313|EMBL:PRT53881.1,
RC   ECO:0000313|Proteomes:UP000238350};
RA   Ahn J.O.;
RT   "Genome sequencing of [Candida] sorbophila.";
RL   Submitted (APR-2017) 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:PRT53881.1}.
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DR   EMBL; NDIQ01000001; PRT53881.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T0FFW3; -.
DR   STRING; 45607.A0A2T0FFW3; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000238350; 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; 3.
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:PRT53881.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000238350}.
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  48368 MW;  765F913B09745CE2 CRC64;
     MGSSQSTEAT ERASKSQPKG KVAIIGGGPG GAGVSRALVA RGFDVDIFES QDGFGGVWKY
     TGRGPMYRDL DTNIVAKLME YKDFPFKGSQ GYRDREDVYE YVVEYSKKYT TNVHFNTTIA
     NVLKDENSWR LIDIKGKEYE ADFIVLAAGH YNVPFTPEIE GIEEWRKVHP GTVLHSRTFD
     NPDVFENKKV VVVGNGASGL DVAIQILSVT APVSVCRRHE APSDVLFDGE NMVLKPELIK
     VDAQTQTVYY QDGSSDPADV ILFCTGYLYE FPFLREFSDG QKYPLLHPRR QRLCNLYERT
     IYLTDPTLAV VGMDKQIVPM PVSEAQGAVI ARVFAKDLTL PPLAEMVELE RRAVEVRGDG
     QSYHNLGYPN DAEWMAKLDE WVDTAPTERG FTAEKWDSEK LDLRKHSSKT KLGEFRHKID
     QSNRKRLQK
//
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