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Database: UniProt
Entry: A0A395NCM5_TRIAR
LinkDB: A0A395NCM5_TRIAR
Original site: A0A395NCM5_TRIAR 
ID   A0A395NCM5_TRIAR        Unreviewed;       612 AA.
AC   A0A395NCM5;
DT   05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT   05-DEC-2018, sequence version 1.
DT   27-MAR-2024, entry version 11.
DE   SubName: Full=Cofactor fmo1 fad enzyme {ECO:0000313|EMBL:RFU73856.1};
GN   ORFNames=TARUN_8401 {ECO:0000313|EMBL:RFU73856.1};
OS   Trichoderma arundinaceum.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU73856.1, ECO:0000313|Proteomes:UP000266272};
RN   [1] {ECO:0000313|EMBL:RFU73856.1, ECO:0000313|Proteomes:UP000266272}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU73856.1,
RC   ECO:0000313|Proteomes:UP000266272};
RX   PubMed=29649280; DOI=10.1371/journal.ppat.1006946;
RA   Proctor R.H., McCormick S.P., Kim H.S., Cardoza R.E., Stanley A.M.,
RA   Lindo L., Kelly A., Brown D.W., Lee T., Vaughan M.M., Alexander N.J.,
RA   Busman M., Gutierrez S.;
RT   "Evolution of structural diversity of trichothecenes, a family of toxins
RT   produced by plant pathogenic and entomopathogenic fungi.";
RL   PLoS Pathog. 14:e1006946-e1006946(2018).
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:RFU73856.1}.
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DR   EMBL; PXOA01000597; RFU73856.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A395NCM5; -.
DR   Proteomes; UP000266272; Unassembled WGS sequence.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR   PANTHER; PTHR23023:SF292; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G01900); 1.
DR   Pfam; PF13738; Pyr_redox_3; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
PE   4: Predicted;
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:UP000266272}.
SQ   SEQUENCE   612 AA;  68589 MW;  62BC5872D50A04B5 CRC64;
     MDSTAEQVDV VVVGAGWNGL ISAKTYLDFE PLANLIVIDE QASFGGVWSA EKIYPSLYAQ
     IKHGLFEYSF YPMKHEGITE DGYISGETIH TYLTDFAWDY DLVRRTRLRT TVKQVLRTTT
     GRWRLELENK APIECEKLIY ASGATSHPVI PAWPNDNFTS PIIHSCDTGT HLDALDKIQS
     ATVIGGAKSS YDTVFFLLKA GKRVNWIIRE DGSGPLAIMP PTLLGLANTM DVVTTRFVTL
     MGMSVMSTDG AGHQFFQRTV IGRFIVWVFW LIVNWIADRH AGYSKSENAK KLRPGPEGNG
     IFWANAGLGA ASVPLFWKTF HRGDCTVHRT DVELLCDNDR VNLKNGESFQ TDCIILCTGF
     DKSFQVFSEE LQQELGFLTA PEEADKWTKL DAEAIETVDE LLPYLKNSPF GQKKFDRETT
     AGGRKLLHGP SRHYRRLIVP KLAAQGDRSI FFPGFIHSIF TPTVSEVQAL WGVTFLLRLI
     DLPTQEEMEQ EVAEWNVWSG KRYVAQGRKH AYAIFDFLPY IDTLLGDLDI KSRRKKNWFA
     HLFAPAYPRE YNGLIDEFRQ ALAKKQDLEA TVSGTMTPLS VESETLSVGS DGLSVVSPVN
     AHNTSVKPLG FS
//
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