ID A0A395P0S9_TRIAR Unreviewed; 485 AA.
AC A0A395P0S9;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 12.
DE SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:RFU81965.1};
GN ORFNames=TARUN_227 {ECO:0000313|EMBL:RFU81965.1};
OS Trichoderma arundinaceum.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=490622 {ECO:0000313|EMBL:RFU81965.1, ECO:0000313|Proteomes:UP000266272};
RN [1] {ECO:0000313|EMBL:RFU81965.1, ECO:0000313|Proteomes:UP000266272}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 40837 {ECO:0000313|EMBL:RFU81965.1,
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 -!- 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:RFU81965.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; PXOA01000014; RFU81965.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A395P0S9; -.
DR Proteomes; UP000266272; 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; 2.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR Pfam; PF13450; NAD_binding_8; 1.
DR PRINTS; PR00419; ADXRDTASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 2.
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:RFU81965.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000266272}.
SQ SEQUENCE 485 AA; 54621 MW; 2C2D7AA85AFEFB4A CRC64;
MGSVWSRPAV SAAASSSTAL PAKQQRQLFH VKKVAIVGAG PAGLAAARYL RAQGAVDSIT
IFEQQDEVGG VWYYSGLAPK EVPVPQQNPF WGPEPSIWPE GAPAPVFPSP MYERLHANIP
GCLMGFHDWK FSSDAWVFPK REEIQEYLVR YAEDLRHLIK FRHQVTQVDL ETRDGRDQWH
LEAASTLNDD QVVRETYDAV VIANGHYSVP FIPAIKNIQE FNKAHPSIIR HSKQYRKNDL
FKGKKVVVVG NGPSGLDIAL QINEVAARTL MSVRHATSPD KISHIGCEEV PEIVEFLPDQ
RGVLFKDGST ETDIDYIVFC TGFLFGYPFL PNLNHKIITS GRGVHGLYQH LFLIQHPTLV
FPALNMKSVP WPLAESQAAV FSAVWSNDLE LPSNEEMEQW STELEEREGE ALHIFPALGD
DGKYINEFYD WAKKATHVGK EPPRWDGELF WQREISMEAK IKFEEEGCKA KTLAELGFVY
EPAKE
//
