ID A0A0D2D4E4_9EURO Unreviewed; 625 AA.
AC A0A0D2D4E4;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=PV06_10560 {ECO:0000313|EMBL:KIW37210.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW37210.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW37210.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW37210.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KN847345; KIW37210.1; -; Genomic_DNA.
DR RefSeq; XP_016257426.1; XM_016412118.1.
DR AlphaFoldDB; A0A0D2D4E4; -.
DR GeneID; 27362634; -.
DR VEuPathDB; FungiDB:PV06_10560; -.
DR HOGENOM; CLU_453400_0_0_1; -.
DR OrthoDB; 445965at2759; -.
DR Proteomes; UP000053342; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; 2.
DR PRINTS; PR00368; FADPNR.
DR PRINTS; PR00411; PNDRDTASEI.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 466..488
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 500..523
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 557..575
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 625 AA; 70694 MW; D460F71B1A85C6D2 CRC64;
MRRVVIVGAG PCGLVALKEM LEHGHNVMIC EQEDRLGGVF ASAVAYPNLH LTITNWAMAF
SDFPDPLRLR YSTAEEYLQY LQAYTDHFNL EPHIQYRTKV TAAKLSSKGS WSLHVRRTLG
EEVSEGNMEA DALIVATGAS QYPKAIPREL AGYNGRIIHS SQYDETFKRD VADKSLRVLV
IGGGESGADI AAELGDLSPN VSVWLRRPLC VGPRYLNKRD ELEQIQMNKT TDFPANGFLE
AATTSRMSAG QNVLAYGIFR RILWQTPVLN NTLSRMCLDS TKSAFLRNDQ ATYVTKNQRM
CEALHNGNIQ IQLSRNISST GRYCTFHRQD GTTETQQFDA IVLCTGYRVE FPWIQFSEGI
CLSSNPRSWF LHCFPPNLGH CLFFVGYTRP HQGGIPVMAE MLSRYIALLM TGARRLPVDY
TAQAHIDAKA EREYYHLSPD LDTLVDYNAF LESVARRIGC EPRLPLLATA LFNIHMATVI
LLVAQILIFD TTWSSVLSSV LLWVLSVIGF FILDNGVLLK WWFYPHWAVW YRQRGPGANP
KLLKQMLARV NLWKSTAITR GFVLLVLWSV PAYYVQRLTT IMLLVTKAML ATFGIQVERY
WGAQLLPKLY SLHDCPAHFS DIFLP
//
