ID I6NCU5_ERECY Unreviewed; 419 AA.
AC I6NCU5;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN OrderedLocusNames=Ecym_5104 {ECO:0000313|EMBL:AET39887.1};
OS Eremothecium cymbalariae (strain CBS 270.75 / DBVPG 7215 / KCTC 17166 /
OS NRRL Y-17582) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Eremothecium.
OX NCBI_TaxID=931890 {ECO:0000313|EMBL:AET39887.1, ECO:0000313|Proteomes:UP000006790};
RN [1] {ECO:0000313|EMBL:AET39887.1, ECO:0000313|Proteomes:UP000006790}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 270.75 / DBVPG 7215 / KCTC 17166 / NRRL Y-17582
RC {ECO:0000313|Proteomes:UP000006790};
RX PubMed=22384365;
RA Wendland J., Walther A.;
RT "Genome evolution in the Eremothecium clade of the Saccharomyces complex
RT revealed by comparative genomics.";
RL G3 (Bethesda) 1:539-548(2011).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; CP002501; AET39887.1; -; Genomic_DNA.
DR RefSeq; XP_003646704.1; XM_003646656.1.
DR AlphaFoldDB; I6NCU5; -.
DR STRING; 931890.I6NCU5; -.
DR GeneID; 11470321; -.
DR KEGG; erc:Ecym_5104; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; I6NCU5; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000006790; Chromosome 5.
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; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000006790}.
SQ SEQUENCE 419 AA; 47680 MW; 9032F31F8E02E937 CRC64;
MPKNVAIIGA GPAGLGTARA LLNNTPFEVT IFEQADQIGG LWYYGNGLRD SSMYDHLETN
LMKQIMAFNG FPFPEYDPTF PSRQRVWEYL RLYFLEFIKG KAKVFLNNKV TSLEKVKEPQ
KWELRVENGQ VYTFDFVVIA NGHYVKGYTP QNIPGLDKWR AKSPEASVHS KWFTNSAYAR
GKTIVVVGNG VSGQDIANQL STVAYKVYHS VRNVSSTEWP SESVIEAVGV ITEINPETST
ITFDTGDIVH NVDQIIWATG YRYDIPFLKS YRDILFPNDG LNGADKIHNL WENLVFTRDP
TLSFPLLVKG VVTFPVAEMH GCLICQVYNG KITREEMSYG NNCQSVDIDF KSCADMDYCK
RLNEILDTHH SSRDKFEPVR WDKNMIKMRG VTAELKKLRT VELLHRAINL RKIGISYTL
//
