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Database: UniProt
Entry: A0A2K1QZU2_9PEZI
LinkDB: A0A2K1QZU2_9PEZI
Original site: A0A2K1QZU2_9PEZI 
ID   A0A2K1QZU2_9PEZI        Unreviewed;       446 AA.
AC   A0A2K1QZU2;
DT   28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT   28-MAR-2018, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:PNS20556.1};
GN   ORFNames=CAC42_6006 {ECO:0000313|EMBL:PNS20556.1};
OS   Sphaceloma murrayae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Myriangiales; Elsinoaceae; Sphaceloma.
OX   NCBI_TaxID=2082308 {ECO:0000313|EMBL:PNS20556.1, ECO:0000313|Proteomes:UP000243797};
RN   [1] {ECO:0000313|EMBL:PNS20556.1, ECO:0000313|Proteomes:UP000243797}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQ-2017a {ECO:0000313|EMBL:PNS20556.1,
RC   ECO:0000313|Proteomes:UP000243797};
RA   Cheng Q.;
RT   "Draft genome sequence of a variant of Elsinoe murrayae.";
RL   Submitted (JUN-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:PNS20556.1}.
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DR   EMBL; NKHZ01000025; PNS20556.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2K1QZU2; -.
DR   STRING; 2082308.A0A2K1QZU2; -.
DR   InParanoid; A0A2K1QZU2; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000243797; 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; 4.
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:PNS20556.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000243797}.
FT   REGION          62..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  50456 MW;  E105188499BBF97C CRC64;
     MPSARSRVFN ISSIAVIGAG PSGIAAAKSL LAENAFQRID IIEQRSKISG LWAYDPSYKR
     PDQAYPIPQT NPDADPNAAS RPATYLSPVY DRLETNIPRG LMGFSDLDWP KDAYLFPKHD
     TVTEYIENYS KSVRHLIKFG TKLISAAPED DEDDTSGWRV TLEAADRTQH HCHYDAIVAA
     TGHFNKVLLI GNGASGVDIA SQIRQFCRPP LLQSSRSPSM FLSSTSSTLL ELPEVTALDP
     TTRTAHFANG HSETNIDALL FCTGYFYSFP WLRVSPHPIT DGLRVHHTYQ HLFYRPRPTL
     VFPVLQQRVI PFPMAEVQAA VFARIWSGRL ALPSDAEMTT WEQRQIEESG DGKGFHLLKF
     PKDAEYINMM SDWAMTAVDA EQGRRPPRWG QREFWLRERF AEIRKQYGEL GERRWEVKSV
     GEMGFDFDAW KRQRGGQGED ELATSR
//
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