ID A0A066X4T7_COLSU Unreviewed; 515 AA.
AC A0A066X4T7;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Putative monooxygenase {ECO:0000313|EMBL:KDN64153.1};
GN ORFNames=CSUB01_02746 {ECO:0000313|EMBL:KDN64153.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN64153.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN64153.1}.
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DR EMBL; JMSE01001156; KDN64153.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066X4T7; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_024886_0_0_1; -.
DR OMA; SEKWIIP; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000027238; 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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF62; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G14280); 1.
DR Pfam; PF00743; FMO-like; 1.
DR PRINTS; PR00469; PNDRDTASEII.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:KDN64153.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 27..515
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001629864"
SQ SEQUENCE 515 AA; 58598 MW; FCF961F455EC8F7F CRC64;
MPSESRMENP FFHPFLFLFQ LWQWFADKIF SPTPPEPSTR LSRPKIAVIG AGITGVTSAA
HCIGHGFDVV IFEAGGRENL GGIWSKVNNS SSLQIHSMMF RFHPSVKWER GYPDRQQILS
QVKQLWHKYG LETRTKFNTP VEKVYQDEKG RWVINNTANG HFEGIIAAVG TCGEPKMPRL
PGIEDFKGHV YHSSQLTGKN AKGKKMVVIG GGASAVEALE FAVDEEAEKT YILSRSDKWI
IPRNPIVNIL LALNILGQET RLSWIPETLL RKFFYRDLQE IAPYDKGIYM DTPMVNSQVM
DTIRSGRAEW IRCDIEGFTA DGVIVNRRAQ GVPKGGPGRR QVVPADIIVM ATGYKRPSLD
FLPEDCFTEP YRPPNWYLQT FPPAHPSISA INCTYVAAIG TVGNWHIGIY TRILLMFLID
PMTRPHPFWM KAWIEMTKLL KSAAPTGAFD FFTYLELIWW FAFSVTFNPF RWKWAFFVFF
GLGFMLPKKV VEVESRIRNG MGFQDEVGRD VGHSI
//
