ID   F8P8X0_SERL9            Unreviewed;       591 AA.
AC   F8P8X0;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=FAD/NAD(P)-binding domain-containing protein {ECO:0008006|Google:ProtNLM};
GN   ORFNames=SERLADRAFT_442258 {ECO:0000313|EMBL:EGO20099.1};
OS   Serpula lacrymans var. lacrymans (strain S7.9) (Dry rot fungus).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX   NCBI_TaxID=578457;
RN   [1] {ECO:0000313|EMBL:EGO20099.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S7.9 {ECO:0000313|EMBL:EGO20099.1};
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA   Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA   Coutinho P.M., Cullen D., Cullen D., Gathman A., Goodell B., Henrissat B.,
RA   Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A., Lavin J.L.,
RA   Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E., Murat C.,
RA   Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A., Salamov A.,
RA   Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A., Xie X.,
RA   Kues U., Hibbett D.S., Hoffmeister D., Hogberg N., Martin F.,
RA   Grigoriev I.V., Watkinson S.C.;
RT   "Evolution of plant cell wall degrading machinery underlies the functional
RT   diversity of forest fungi.";
RL   Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; GL945441; EGO20099.1; -; Genomic_DNA.
DR   RefSeq; XP_007322844.1; XM_007322782.1.
DR   AlphaFoldDB; F8P8X0; -.
DR   GeneID; 18815697; -.
DR   KEGG; sla:SERLADRAFT_442258; -.
DR   HOGENOM; CLU_035533_0_0_1; -.
DR   OrthoDB; 1434032at2759; -.
DR   Proteomes; UP000008064; 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; 3.
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; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
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}.
SQ   SEQUENCE   591 AA;  64917 MW;  3A6F45D147C1B3E6 CRC64;
     MAAKTVCVVG SGAAGLITAK TLLDDGFAVE ILSKDRTAGG VWAADRVYPG LYTNNVNGEY
     EFSAMPMHLQ RIKERPSGTE MRQYMEAFAD RFLNGKIRFN TQVVNIHRWD QGNNQEAVKG
     WAISVQNSDG TAEQLFYDIV VLCSGGCSLP RIPPELSSAA AQKAGFVGQV VHSFEFASRL
     DDIISAVKPI DDPNPGHVVV VGGGKSAQDI AAYLANEGRK VSIAFETADG IIAAPIPLPH
     FIRKSRQVST LIFGVSSKLS VSSLCRLLGL MATHIHLRTA LEKFLHTTWL GSKIVSGFWD
     TLSWASGKFL SIPSTSPLLT SHSLFWGIRT NDEGSPRSNG FHALVNAGKI QLVASNRVSS
     FGPDGHSVVL RDGSSVRADV VVLSTGYTSS WKGIFDEEIL RDFGLERVRN DCLSDVGIKE
     SEWQFYKTLQ NPPQLPLGNQ GQWMSSIYRG LVPARNIQRR DFAINGAVFT TSPAHIFEVS
     SHWISSYLLS DPFLRLPSSP EDALVETERV ARWVNIRNPG MLKWVNESYS SGLNFFDYAQ
     ASDDLLEDMG LPILRSGGNW FTWPFIPISS KEIKALGEER AILRASNTTR N
//