ID F8Q3D7_SERL3 Unreviewed; 427 AA.
AC F8Q3D7;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
DE Flags: Fragment;
GN ORFNames=SERLA73DRAFT_56786 {ECO:0000313|EMBL:EGN97698.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
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., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
CC -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC {ECO:0000256|ARBA:ARBA00007992}.
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DR EMBL; GL945482; EGN97698.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q3D7; -.
DR STRING; 936435.F8Q3D7; -.
DR eggNOG; ENOG502SHZE; Eukaryota.
DR HOGENOM; CLU_009665_6_3_1; -.
DR InParanoid; F8Q3D7; -.
DR OMA; CHAMTPH; -.
DR OrthoDB; 1947085at2759; -.
DR Proteomes; UP000008063; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR PANTHER; PTHR46720; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR PANTHER; PTHR46720:SF3; HYDROXYLASE, PUTATIVE (AFU_ORTHOLOGUE AFUA_3G01460)-RELATED; 1.
DR Pfam; PF01494; FAD_binding_3; 2.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063}.
FT DOMAIN 6..165
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT DOMAIN 298..363
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EGN97698.1"
SQ SEQUENCE 427 AA; 46934 MW; A5CD81F903ED9858 CRC64;
RSVVVTSGAG IGGLMLAVVL GKYSDIPIDL YEAQAEITTV GAGVTVWRRT REIMIELGLY
SELSEVTTRS SDTSHPYGKP SPSIRLKFWV HLDEPSSLHR LDLVNLLIRH LPSSCTIHTM
KRLKAYARDD SGGLALALKF ADESTAITDV LIGADGIRSA TRRALFEGLA KASLPGLQNV
SEYVNAMWTG TIVYRSLIPT ENLEKLYPGN SATKNMMLVG HIVTYPVSRG ALVNVAAFYT
EAEDIGKKFE GHWVSDASEE ELLKSFENFE PEARAILQCC EKPSRWALHV TNNLPLSTSG
RVAIIGDACH AMTPHFGAGA GQAIEDAFIL GRLLSHNLTT LCNLPDVLRI YQDIRLPAVT
HISQSAAITG YMYDFMAPGY YDGEDRSDED GLEQLKDAIN KNWEWLGQTG SMDDWADAER
RLKELAS
//
