ID A0A072PUX2_9EURO Unreviewed; 605 AA.
AC A0A072PUX2;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=A1O9_01842 {ECO:0000313|EMBL:KEF63864.1};
OS Exophiala aquamarina CBS 119918.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=1182545 {ECO:0000313|EMBL:KEF63864.1, ECO:0000313|Proteomes:UP000027920};
RN [1] {ECO:0000313|EMBL:KEF63864.1, ECO:0000313|Proteomes:UP000027920}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 119918 {ECO:0000313|EMBL:KEF63864.1,
RC ECO:0000313|Proteomes:UP000027920};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala aquamarina CBS 119918.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
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:KEF63864.1}.
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DR EMBL; AMGV01000001; KEF63864.1; -; Genomic_DNA.
DR RefSeq; XP_013266454.1; XM_013411000.1.
DR AlphaFoldDB; A0A072PUX2; -.
DR GeneID; 25276788; -.
DR VEuPathDB; FungiDB:A1O9_01842; -.
DR HOGENOM; CLU_006937_6_1_1; -.
DR OrthoDB; 49786at2759; -.
DR Proteomes; UP000027920; 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; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF7; FLAVIN-BINDING MONOOXYGENASE-RELATED; 1.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 3.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000027920}.
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 605 AA; 68375 MW; 470B643EBBEDDABD CRC64;
MIPSPVHSKN GTTPSLANGD LRELPERYGW PTTNGRGYII REQPAAVQRH IRVIHLGAGA
SGICFSKFAS ETLENVDFIC YDKNPDIGGT WLENRFGRFS LVSRCDFTWA RKADWSHFYS
YSEEIWQYFK DIVDTFGLRK YMKLNHEITG AEWHEDQGMW HVKVKNLDDG TEFVDRADIF
INGGGVLNSW KWPAIEGLHD FKGTLCHTAN YAAGTDLEGK RVAVIGVGSS GIQVTASIAS
KVDKLYTWVR SPTWITAGFA QKYAGPDGAN FEYSEQQKRN FAENFPDYVA HTKEIEDELN
QRFKFILNGT PEAKEAKDFS TKQMQDKLKG RQDLINMLVP TKFGVGCRRP TPGNGFLEAL
TLPHVTTFPM EMAKVTPNGF IDHQGLEHEV DAIICATGFD TSWVPRFPVK ARGLNVQDMQ
KDKPISYLSI GVPEIPNYWT VTGAYSPVGH GSFLPIIEHL MRHFMMLIKK IQTQNIRAMA
PRKEVCHAFI EHADLYLKRT AWTSGCRSWF KQGKEDGPLS IWPGSRLLFF EALAQPRYED
YNISYEGNNP FGFFGNGFTL REYDNSDLSY YLGTAENLGA LLPTSNYSSK GTDSLDRTSN
KDAEE
//
