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Database: UniProt
Entry: G3JSI3_CORMM
LinkDB: G3JSI3_CORMM
Original site: G3JSI3_CORMM 
ID   G3JSI3_CORMM            Unreviewed;       746 AA.
AC   G3JSI3;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   SubName: Full=FAD dependent oxidoreductase {ECO:0000313|EMBL:EGX88775.1};
GN   ORFNames=CCM_08821 {ECO:0000313|EMBL:EGX88775.1};
OS   Cordyceps militaris (strain CM01) (Caterpillar fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Cordycipitaceae; Cordyceps.
OX   NCBI_TaxID=983644 {ECO:0000313|EMBL:EGX88775.1, ECO:0000313|Proteomes:UP000001610};
RN   [1] {ECO:0000313|EMBL:EGX88775.1, ECO:0000313|Proteomes:UP000001610}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CM01 {ECO:0000313|EMBL:EGX88775.1,
RC   ECO:0000313|Proteomes:UP000001610};
RX   PubMed=22112802; DOI=10.1186/gb-2011-12-11-r116;
RA   Zheng P., Xia Y., Xiao G., Xiong C., Hu X., Zhang S., Zheng H., Huang Y.,
RA   Zhou Y., Wang S., Zhao G.P., Liu X., St Leger R.J., Wang C.;
RT   "Genome sequence of the insect pathogenic fungus Cordyceps militaris, a
RT   valued traditional Chinese medicine.";
RL   Genome Biol. 12:RESEARCH116.1-RESEARCH116.21(2011).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; JH126405; EGX88775.1; -; Genomic_DNA.
DR   RefSeq; XP_006674020.1; XM_006673957.1.
DR   AlphaFoldDB; G3JSI3; -.
DR   GeneID; 18170826; -.
DR   KEGG; cmt:CCM_08821; -.
DR   VEuPathDB; FungiDB:CCM_08821; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   HOGENOM; CLU_023116_0_0_1; -.
DR   InParanoid; G3JSI3; -.
DR   OMA; GQFPMGD; -.
DR   OrthoDB; 1557755at2759; -.
DR   Proteomes; UP000001610; 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; IPR045632; DUF6314.
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; PF19834; DUF6314; 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:UP000001610}.
FT   DOMAIN          569..746
FT                   /note="DUF6314"
FT                   /evidence="ECO:0000259|Pfam:PF19834"
SQ   SEQUENCE   746 AA;  83440 MW;  71CB8E2D6DD028CA CRC64;
     MSLRRNAPWT AMAKSVCIVG AGPAGLAVAK TLLHSAPQGD FRVTVFDAQQ DVGGLWPTFK
     EDVGRQIHPL MLANQSRHSM HFSDLAWEDK TPQLPPAWML GRYLHRYAEK YLSGRPDFQL
     KLKTRVVRTE KDDEGWSVTV RSDDGDQTTR FDRLVVASGY FGDPIIPKAL KENATIPVIH
     SCQYRDLQSL LGCSGKGGKI LVAGGQMSGV EIAATISTHL SNEINSPDES AIPNIEKYSI
     HHVSPRHPWV IPLYTTPEPK WKAPPFLPQD FSSWNRNNRP VPFTDTQGHI PEERAKMVHE
     RLTVSLGPRQ MIDTRETGSN SLDRSLPPYV SCSDWYCDFE RSGFITVHNG RLESLAGSTA
     KLADSSIEDV AAVVLATGFS PAPCVSFLPK DVLSTLGYSP VHPSLLLALA FHATHHPDVP
     DLGFVGFYRG AFWGVIQMQA RFLAALWSSE GPSDTLREKL ARDTSIQRTL NLRDDPRQAQ
     FHMGDYPFLL QEFAEALSLD INPPLAVDTP HLTTNGLPLD MIAPCRYSPA NEDGEDNANA
     KTLMHNAEVV LKDALTTPRF VSRAVFRSLL GTWKLERDLR SKLPTHPSGH FSGTAQFLLR
     ATTKEGVQCV IKEGISPPYE DGESLEYLYI EDGEFKTDQG FGFPATRRYI YRYDEASGAI
     TVWFAKPDDN KRVDYFFHEI EFQDPPASGG GHQRWWPAKS GHLCIDDYYN VNYNFVFDAV
     NLERWVCAYT VNGPEKDYTI CGTYTR
//
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