ID B9WAP5_CANDC Unreviewed; 552 AA.
AC B9WAP5;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE SubName: Full=Oxidoreductase, putative {ECO:0000313|EMBL:CAX43465.1};
GN OrderedLocusNames=Cd36_16860 {ECO:0000313|CGD:CAL0000161350};
GN ORFNames=CD36_16860 {ECO:0000313|EMBL:CAX43465.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX43465.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX43465.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FM992689; CAX43465.1; -; Genomic_DNA.
DR RefSeq; XP_002418165.1; XM_002418120.1.
DR AlphaFoldDB; B9WAP5; -.
DR GeneID; 8045729; -.
DR KEGG; cdu:CD36_16860; -.
DR CGD; CAL0000161350; Cd36_16860.
DR VEuPathDB; FungiDB:CD36_16860; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006937_7_0_1; -.
DR OrthoDB; 49786at2759; -.
DR Proteomes; UP000002605; Chromosome 2.
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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR42877; -; 1.
DR PANTHER; PTHR42877:SF5; L-ORNITHINE N(5)-OXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE 4: Predicted;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 271..292
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 552 AA; 63033 MW; F37620FBC48F4C20 CRC64;
MSTITLTRES HKNPAKFRIN HQDELDILGP HRKDRYAIND KLPTITTTSK LAIIGAGFGG
MAGAIKTMEK YDEHDIQIFE RHDNFGGTWY ANTYPGCASD IPALWYSFSF ALTSNWSRIQ
PPQYEMEEYL LRVADKFKLK EKTRFQTEIN KVEWDDVNGQ WTLFAHDVKT GQRIIHKSKL
LLACHGGLVH PLHFDAKGLD NFKGDYMHSA LWDHSVDFRG KKVVVVGNGC SANQAVPALL
NDPQYSVGSL TQISRSKHYI MRPLPKVIYT LYRLFSFNYF TMYFFRLMFI FFSELKVPLF
KGGGVVSNFV RKVTTEASVQ YIKEVAPEKY HDKLIPDYKI GCKRLIFDYN YVPSLKDPRI
DIKTEGVAKV VEDGVVLESG EHIEADIIVA CTGYNLSKSH FNFEIVGRNG ADITQLWKEE
GASAYRTLLI KHCPNLWTIG GTNSITGHAS VVMGIENGVD YFLKTAKPVF QGKAKSVQIK
DEAYDNWLTT LQKEINKSVF GTPFGGCVSW YSGAKVNSVS YPWSQLHYWW KTQFPTYSDL
KYEPLTENKK RR
//
