ID A0A0A2VCU1_BEABA Unreviewed; 736 AA.
AC A0A0A2VCU1;
DT 04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT 04-FEB-2015, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 3 {ECO:0000313|EMBL:KGQ05373.1};
GN ORFNames=BBAD15_g9376 {ECO:0000313|EMBL:KGQ05373.1};
OS Beauveria bassiana D1-5.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Cordycipitaceae; Beauveria.
OX NCBI_TaxID=1245745 {ECO:0000313|EMBL:KGQ05373.1, ECO:0000313|Proteomes:UP000030106};
RN [1] {ECO:0000313|EMBL:KGQ05373.1, ECO:0000313|Proteomes:UP000030106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1-5 {ECO:0000313|EMBL:KGQ05373.1,
RC ECO:0000313|Proteomes:UP000030106};
RA Li Q., Wang L., Zhang Z., Wang Q., Ren J., Wang M., Xu W., Wang J., Lu Y.,
RA Du Q., Sun Z.;
RT "Genome sequencing and analysis of entomopathogenic fungi Beauveria
RT bassiana D1-5.";
RL Submitted (OCT-2012) 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:KGQ05373.1}.
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DR EMBL; ANFO01000951; KGQ05373.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0A2VCU1; -.
DR STRING; 1245745.A0A0A2VCU1; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_023116_0_0_1; -.
DR Proteomes; UP000030106; 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; IPR045632; DUF6314.
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:SF110; DUF6314 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF19834; DUF6314; 1.
DR Pfam; PF00743; FMO-like; 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, ECO:0000313|EMBL:KGQ05373.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000030106}.
FT DOMAIN 558..736
FT /note="DUF6314"
FT /evidence="ECO:0000259|Pfam:PF19834"
SQ SEQUENCE 736 AA; 82088 MW; A5A1475CEA0307AA CRC64;
MAKSVCIIGA GPAGLAIAKT LLHNAPQGDF CVTVFDAQPN VGGLWPTDKD DAGRQIHPLM
RTNQSRHSMH FSDLAWDDET PQLPRAWMVG QYLERYAEKY LHGRLNFQLR LKTRVTRTER
DGEGWNVTVR SDKGDETARF DRLVVASGYF GEPVVPKTMK EYSTAPVIHS SYYRDLKSLL
GTSGRGGKIV VAGGQMSGVE IAATIGTHLS EEINSPDQSS IPNIENYEIH HVSPRHPWVI
PLHTTPEPKW KAPPFLPHDF SSYNKNNRPV PFTDTHGHIT EERAKIVHER LLGALGPRQM
IGSETANTDG LDRSSLPYVS CSDWYCDFVR SGFITVHDSR LESLAGSTAK LTESEIDDVA
AVVLATGFDP EPCISFLPND VLSTLKYSPA HPALLLALSF HGTHHPEVPN LGFVGFYRGA
FWGVIQMQAR FLTALWSSKG PSATLRDKLA RDSCIQRTLN LRDDPRQSQF PMGDYQFLMQ
DFAEALSLEI SPPQAVDAPS LTTNGLPLEI FAPCRFSPPN EDGQHNANAK KLNNDAAAVL
KAALTTPRFV SRAVFRSLLG TWKLERTLTS KLPTHPSGHF SGTAQFLLRK TTKEGVQCAI
AEESVASVCR DGESYEYLYI EDGDFQTDQG FGFRATRRYI YRYDEASDRI SVWFAKPDDN
KRVDYLFHRI EFEDPPAGSG GHPHGWPAKS GHLCIDDYYN VKYNFVFDAV NVESWVCAYT
VNGPQKDYTI HGTYTR
//
