ID A0A074Y289_AURSE Unreviewed; 498 AA.
AC A0A074Y289;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN ORFNames=AUEXF2481DRAFT_454501 {ECO:0000313|EMBL:KEQ91830.1};
OS Aureobasidium subglaciale (strain EXF-2481) (Aureobasidium pullulans var.
OS subglaciale).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Dothideomycetidae; Dothideales; Saccotheciaceae; Aureobasidium.
OX NCBI_TaxID=1043005 {ECO:0000313|EMBL:KEQ91830.1, ECO:0000313|Proteomes:UP000030641};
RN [1] {ECO:0000313|EMBL:KEQ91830.1, ECO:0000313|Proteomes:UP000030641}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-2481 {ECO:0000313|EMBL:KEQ91830.1,
RC ECO:0000313|Proteomes:UP000030641};
RX PubMed=24984952;
RA Gostin Ar C., Ohm R.A., Kogej T., Sonjak S., Turk M., Zajc J., Zalar P.,
RA Grube M., Sun H., Han J., Sharma A., Chiniquy J., Ngan C.Y., Lipzen A.,
RA Barry K., Grigoriev I.V., Gunde-Cimerman N.;
RT "Genome sequencing of four Aureobasidium pullulans varieties:
RT biotechnological potential, stress tolerance, and description of new
RT species.";
RL BMC Genomics 15:549-549(2014).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KL584775; KEQ91830.1; -; Genomic_DNA.
DR RefSeq; XP_013340327.1; XM_013484873.1.
DR AlphaFoldDB; A0A074Y289; -.
DR STRING; 1043005.A0A074Y289; -.
DR GeneID; 25367944; -.
DR HOGENOM; CLU_006909_5_0_1; -.
DR InParanoid; A0A074Y289; -.
DR OMA; FMEWEHH; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000030641; 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; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00419; ADXRDTASE.
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:UP000030641}.
SQ SEQUENCE 498 AA; 56750 MW; A2DC0DE5C37180AE CRC64;
MAGKFAVKNV CIVGAGPSGV AAAKYLVAEK AFERIDVYEQ RSRVGGVWDY SPEDKTPTPD
DLPVPSVSPH TGLAKAKWLQ SGTRKALGSR IEEDSLFLSP LYDRLETNIP RTLMGYSDFD
WPQDSQLFPK HETVTQYLED YAAEIKHLIH FNTQVLDISL AGTKEHGQDI WSVKTQKVQH
NSPAEVVETK YDAIVVANGH FAVPFIPQIK GIKEWADHYP NAISHSMYYK KPEDYTNLKT
IIVGSGASGI DIAMQIMQLC KHPLLQSQKS KSFLLSDPSP KKQERDEIVE FLIQDRAVRF
ADGSVEKDID SILFCTGYFY SFPFLNNMDP PLVTSGTHVQ NLYQHLICRP HPTLCFPTLQ
QRVIPFPMAE SQSAVIARLW NNRISLPSAN DMEAWENNLL RETDGGKRDF HLLLFPKDAN
YINAMYDWSM SASDAKTKGK QPPRWGEKEY WMREKFPEIK KAFQDRGEGR YQVRTLEELG
FDFEKYKKEK PAEQRSSL
//
