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Database: UniProt
Entry: A0A0C9T643_PLICR
LinkDB: A0A0C9T643_PLICR
Original site: A0A0C9T643_PLICR 
ID   A0A0C9T643_PLICR        Unreviewed;       414 AA.
AC   A0A0C9T643;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=FAD-binding domain-containing protein {ECO:0000259|Pfam:PF01494};
GN   ORFNames=PLICRDRAFT_45592 {ECO:0000313|EMBL:KII84784.1};
OS   Plicaturopsis crispa FD-325 SS-3.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Agaricomycetidae; Amylocorticiales; Amylocorticiaceae; Plicaturopsis.
OX   NCBI_TaxID=944288 {ECO:0000313|EMBL:KII84784.1, ECO:0000313|Proteomes:UP000053263};
RN   [1] {ECO:0000313|EMBL:KII84784.1, ECO:0000313|Proteomes:UP000053263}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FD-325 SS-3 {ECO:0000313|EMBL:KII84784.1,
RC   ECO:0000313|Proteomes:UP000053263};
RG   DOE Joint Genome Institute;
RG   Mycorrhizal Genomics Consortium;
RA   Kohler A., Kuo A., Nagy L.G., Floudas D., Copeland A., Barry K.W.,
RA   Cichocki N., Veneault-Fourrey C., LaButti K., Lindquist E.A., Lipzen A.,
RA   Lundell T., Morin E., Murat C., Riley R., Ohm R., Sun H., Tunlid A.,
RA   Henrissat B., Grigoriev I.V., Hibbett D.S., Martin F.;
RT   "Evolutionary Origins and Diversification of the Mycorrhizal Mutualists.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; KN832569; KII84784.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0C9T643; -.
DR   HOGENOM; CLU_009665_4_0_1; -.
DR   OrthoDB; 5491711at2759; -.
DR   Proteomes; UP000053263; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR   GO; GO:0046677; P:response to antibiotic; IEA:InterPro.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   HAMAP; MF_00845; TetX_monooxygenase; 1.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR043683; TetX_monooxygenase.
DR   PANTHER; PTHR46972; MONOOXYGENASE ASQM-RELATED; 1.
DR   PANTHER; PTHR46972:SF1; RHODANESE DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF01494; FAD_binding_3; 2.
DR   PRINTS; PR00420; RNGMNOXGNASE.
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:UP000053263}.
FT   DOMAIN          12..230
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   DOMAIN          312..347
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
SQ   SEQUENCE   414 AA;  44721 MW;  707CF843D71A11F1 CRC64;
     MSTSSTSTYP RIAIIGGGPG GLTLARILQV NGVRATIYER ETLENPRIQG GSLDLHVESG
     IAALRAAGLF EDFKKLIRQG SQQTRIFDTD GKMHLNLDGP RGPPDDDNLG RPEIDRPVLR
     NLLLNSLDKD TVKWGHDLQT VLPNEGSGGF RLAFKDGREE TADLVIGADG AWSKIRPLLT
     PAKPVYSGTT MIELRISDID ARYPELSALA GQGTVFILSS DGKAIFPQRN GDGSVRVYAS
     LHAEEQWLDS QHAILGKEGP AAALEAIAAL FPGWSSTVLD LIRNSDQDKI TPRRIFQLPL
     PFNPWTTKPG LTVLGDAAHL MSPFAGEGVN LAMIDATDLA KAIVGVTAQP GASADALTDA
     LRGYEEVMLK RSEEMAIESA RNMDLIFGQD ALKNFLGFFA RFGLVPEGEE KPEP
//
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