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Database: UniProt
Entry: A0A067Q028_9AGAM
LinkDB: A0A067Q028_9AGAM
Original site: A0A067Q028_9AGAM 
ID   A0A067Q028_9AGAM        Unreviewed;       455 AA.
AC   A0A067Q028;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=JAAARDRAFT_36352 {ECO:0000313|EMBL:KDQ56872.1};
OS   Jaapia argillacea MUCL 33604.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Jaapiales; Jaapiaceae; Jaapia.
OX   NCBI_TaxID=933084 {ECO:0000313|EMBL:KDQ56872.1, ECO:0000313|Proteomes:UP000027265};
RN   [1] {ECO:0000313|Proteomes:UP000027265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MUCL 33604 {ECO:0000313|Proteomes:UP000027265};
RX   PubMed=24958869; DOI=10.1073/pnas.1400592111;
RA   Riley R., Salamov A.A., Brown D.W., Nagy L.G., Floudas D., Held B.W.,
RA   Levasseur A., Lombard V., Morin E., Otillar R., Lindquist E.A., Sun H.,
RA   LaButti K.M., Schmutz J., Jabbour D., Luo H., Baker S.E., Pisabarro A.G.,
RA   Walton J.D., Blanchette R.A., Henrissat B., Martin F., Cullen D.,
RA   Hibbett D.S., Grigoriev I.V.;
RT   "Extensive sampling of basidiomycete genomes demonstrates inadequacy of the
RT   white-rot/brown-rot paradigm for wood decay fungi.";
RL   Proc. Natl. Acad. Sci. U.S.A. 111:9923-9928(2014).
CC   -!- SIMILARITY: Belongs to the paxM FAD-dependent monooxygenase family.
CC       {ECO:0000256|ARBA:ARBA00007992}.
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DR   EMBL; KL197721; KDQ56872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A067Q028; -.
DR   STRING; 933084.A0A067Q028; -.
DR   HOGENOM; CLU_009665_6_3_1; -.
DR   InParanoid; A0A067Q028; -.
DR   OrthoDB; 1947085at2759; -.
DR   Proteomes; UP000027265; 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:UP000027265}.
FT   DOMAIN          8..178
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          297..382
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   455 AA;  50546 MW;  4205F69DEFB7E2D3 CRC64;
     MGSIEPKLKV AICGGGIAGL ISAIVLSKCS DLEVHLFEAA HQFNEIGAGI ATFPRVWKIM
     ESIGVDKDLV EVASSRSESG DPEELAFRFR KSDQQEGLTF HELTTFGGFH SFHRAEFQQA
     ILKNLPSSCH THFNKRLTTY TEPSTDSPII LSFQDGTTST CDVLLGADGI KSAVRRTMLE
     NQIAQASPEE SRELLERVPP MWSGTVAYRG LIPRPILEAK WPKHQAFNFA MNYMGQDRHI
     VVYPISRGQI INVVAFCSKP HLEGTTFDGP SVVNVTKAEM LAEFSNWEPE VQALLDCIEH
     PSRWAVHALR SLQSYISGRV ALLGDAAHAM TPHQGSGAGQ AIEDAYILSA LLTDPLCTRA
     TLRNTLEIYN TVRLPMANRI LEGSRSNGMM YEFNSPGYSQ DELHSKEEIG WDMGKLKQLG
     EEFESRWMWA WTTTAEGDKQ EALKMLSDAC DRHGQ
//
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