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Database: UniProt
Entry: A0A093YE14_9PEZI
LinkDB: A0A093YE14_9PEZI
Original site: A0A093YE14_9PEZI 
ID   A0A093YE14_9PEZI        Unreviewed;       382 AA.
AC   A0A093YE14;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=Monooxygenase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=O988_04978 {ECO:0000313|EMBL:KFX97184.1};
OS   Pseudogymnoascus sp. VKM F-3808.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX   NCBI_TaxID=1391699 {ECO:0000313|EMBL:KFX97184.1, ECO:0000313|Proteomes:UP000029329};
RN   [1] {ECO:0000313|EMBL:KFX97184.1, ECO:0000313|Proteomes:UP000029329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VKM F-3808 {ECO:0000313|EMBL:KFX97184.1,
RC   ECO:0000313|Proteomes:UP000029329};
RA   Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA   Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA   Ozerskaya S.M.;
RT   "Population genomics of a fungus Geomyces pannorum provides evidence of
RT   horizontal gene transfer but not of sexual reproduction.";
RL   Submitted (JUL-2014) 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:KFX97184.1}.
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DR   EMBL; JPJR01000952; KFX97184.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093YE14; -.
DR   STRING; 1391699.A0A093YE14; -.
DR   HOGENOM; CLU_006909_8_1_1; -.
DR   Proteomes; UP000029329; 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   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|ARBA:ARBA00022827};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000029329}.
SQ   SEQUENCE   382 AA;  43042 MW;  EEC6321A623A3F17 CRC64;
     MRQQTAVVIG AGSSGLSMLK TLREDGFKVT CYERRAQVGG LWAYTDDKSM TSALPNSATS
     ANISKYTCGM SDFPMPDKYP HYLNQPQFQE YMESYATHFD MLRDIVFNAT VKQASRNEDD
     SKWRLDFVVN GERRVEEYDK VVFCHGYQTK ANMPVFDGAE KFEGEILHSQ GFRMSDKYKG
     KKVVVVGVSS TASDTILALL PVASKVYLSH RRGTLIIPKW RNGFPPDLTV TWRRRQIGFA
     LQRAFPNIAK WCLDQGIKYM MKQTWGKLDP AWRLLPTPSL TLTPRALSGA VIPALKDGSL
     TSLHGINRFL GPKSIEFADG TIVDDIDAVV CATGYKADFS ALPFLEKSRP PNYSGPEITR
     LWMNLFPPNE QRVSWRPSNT YG
//
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