ID A0A165B162_9APHY Unreviewed; 664 AA.
AC A0A165B162;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0000313|EMBL:KZT00032.1};
GN ORFNames=LAESUDRAFT_577900 {ECO:0000313|EMBL:KZT00032.1};
OS Laetiporus sulphureus 93-53.
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Laetiporus.
OX NCBI_TaxID=1314785 {ECO:0000313|EMBL:KZT00032.1, ECO:0000313|Proteomes:UP000076871};
RN [1] {ECO:0000313|EMBL:KZT00032.1, ECO:0000313|Proteomes:UP000076871}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=93-53 {ECO:0000313|EMBL:KZT00032.1,
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; KV427700; KZT00032.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A165B162; -.
DR STRING; 1314785.A0A165B162; -.
DR InParanoid; A0A165B162; -.
DR OrthoDB; 1612588at2759; -.
DR Proteomes; UP000076871; 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; 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:SF110; DUF6314 DOMAIN-CONTAINING PROTEIN; 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00370; FMOXYGENASE.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000076871}.
SQ SEQUENCE 664 AA; 73297 MW; 9FA67975E232CEA3 CRC64;
MSNCQNLKAV IFEASPSLGG IWSPDHPHHR PLMTTNICRH TCTFSDVPWP ADAGRERKDL
FRYSGDMGHF LDVYAQTYVD KADVRLNTKV ASVDYQDGKW MVKSVSTQQD GNSVAHVEVF
HYLIIATGFF SSPYIPDLPG IDNFPVLEHS AMFKDPDAYL DKTVAVVGGS LSAVEIAGAL
SPYARKVHHI TPRPFYVSPL YTPTNSSAMP SFLPWDLLSY NRTDLNGRRT EAINPTPAAN
RSTHAYFQSL FPNNLLPSFE FDTSTPAQVG MSELYRGGIQ TGIVQTYLAR LAAVDTTTGE
LVLSTGDRID RPDVVIMCTG YNIVLPYLSQ SARDAISFQP NNRSVPFLSH RLVLHPDLPN
AGFVGMYRGS YYGVIELQAR YLAAIFSGAQ SWPSDDEMKE GVALEESVRE ASSKSGIQFP
HGDYAGLFES YADLLGIPMS DATYVVAANY PLEVTHDVEE IRLDTESAFT LMTSGTWVRG
AAFRSWAGQW QVDRTVHSAS QPAMNGQFVG FGTFLMRPMT GPLTGPGAMT EAVIREYLYH
ERGVFISATG ESAEEQRTAV YRYDPASDTI AVWSVVRADY EQPPDEDQTD SWQHNIEAVS
RDSPNESSFA EQHGSDGWCA IGRGSEVAVL ASYKFVFNGA EVTQFEIRDS SSEGVVSETT
FTRP
//
