ID A0A165BZJ6_9APHY Unreviewed; 640 AA.
AC A0A165BZJ6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZT01935.1};
GN ORFNames=LAESUDRAFT_763212 {ECO:0000313|EMBL:KZT01935.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT01935.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT01935.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT01935.1,
RC ECO:0000313|Proteomes:UP000076871};
RX PubMed=26659563; DOI=10.1093/molbev/msv337;
RA Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT Insights into the Origins of Lignocellulose Decay Capabilities.";
RL Mol. Biol. Evol. 33:959-970(2016).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; KV427657; KZT01935.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165BZJ6; -.
DR STRING; 1314785.A0A165BZJ6; -.
DR InParanoid; A0A165BZJ6; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000076871; 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; 2.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF00743; FMO-like; 1.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 36..56
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 537..558
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 591..610
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 73..152
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT REGION 237..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 254..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 285..299
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 640 AA; 72252 MW; 4A461ED5CCE58460 CRC64;
MSALDAERRN IDLFLQSIVS TIQDHDVKAL LSPMPFLRLV FNSIYILIQA LIIWLFKPPP
PPDKDAHIHY RGRIAVIGAG LTGVSSAAHA VAHGFDVVLF EQDDAVGGIW AHVNKTSGLQ
LNSMLYRFHP AVLWSSAFPK RDEILRENQR IWREYRLKER TRLSTRVTSV RRATLEELDN
VSEDELDPAQ QGHARWIVND GEDDVFDAVV VTVGTCGAPR WVGFKGMPPM EYIERRRTQS
EHANAGKQKQ NSTDDNEGLQ HDEEKSEVGS ESGRSNTQEP YPPVKHTQDD GESVSKEDLQ
KKKKKKKKKK GKSRGNDEQE KGDENVETFE GTLLHSSQLD DAELEGKHVV VIGSGASGVE
AIETALQRGA SDCVMIARDD KWIIPRNVVL GTLISAQPFG REMPLSFVWE KIVTAWNYHG
VEDLTPAHLG LFEGTPVVND EFLSHIRAGR CRYVRGDTQC LTRDSVRVSV RGRWSRPGDE
GEETEFPAGV VVLATGFKKP DIAFLPKDLF PEGYERPNLY LQNFATEDWS VLMTNSAYIS
AIGTVGHFHI GIYMRILLTF LMDKDSRPTP KDMKLWVDAL RFVKRGARGG ALGFFTYMEL
TIWLVLFHIF RLDRLKWLFF IMQGWGVRPV VQGERAECAD
//
