ID D4DFN1_TRIVH Unreviewed; 490 AA.
AC D4DFN1;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 13-SEP-2023, entry version 45.
DE SubName: Full=FAD dependent oxidoreductase, putative {ECO:0000313|EMBL:EFE39389.1};
GN ORFNames=TRV_05982 {ECO:0000313|EMBL:EFE39389.1};
OS Trichophyton verrucosum (strain HKI 0517).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX NCBI_TaxID=663202 {ECO:0000313|EMBL:EFE39389.1, ECO:0000313|Proteomes:UP000008383};
RN [1] {ECO:0000313|Proteomes:UP000008383}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HKI 0517 {ECO:0000313|Proteomes:UP000008383};
RX PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT "Comparative and functional genomics provide insights into the
RT pathogenicity of dermatophytic fungi.";
RL Genome Biol. 12:R7.1-R7.16(2011).
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:EFE39389.1}.
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; ACYE01000339; EFE39389.1; -; Genomic_DNA.
DR RefSeq; XP_003020013.1; XM_003019967.1.
DR AlphaFoldDB; D4DFN1; -.
DR GeneID; 9580182; -.
DR KEGG; tve:TRV_05982; -.
DR HOGENOM; CLU_006909_5_0_1; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000008383; 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; IPR000960; Flavin_mOase.
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 PIRSF; PIRSF000332; FMO; 3.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002}.
SQ SEQUENCE 490 AA; 54854 MW; DFEF30A4A6ACC8DB CRC64;
MTRATPPVRK VAIIGAGACG LVAAKPRYLL AEQCFEQIDI FEQRNHVGGV WNLTPPEGKG
QAVTVIPSED PNTPLEIPFW HRGSKSSKKE AIFLSPLYDG LETNIPHGLM QFSDLSFPDQ
TQLFPPFEAV LEYLREYSQD VEHLIQFQVQ VVDIKPKDTS LGTWAVTRKD LVSGVLQTDV
YDAVVIANGH YNVPYVPSIP GISAWKEAYP QGIIHSKLYF DSTPYKDKKV VIVGNSASGL
DIGGQINKVC QQPLISSVKS ESYFLSGVAS DRKEYPPIAE FMPPESHTRA IRFSNGEIIE
NVDVVLFCTG YLYSFPFLSG LDMPVVSDGG RTLHVYQHLF YIEQPTLVFP GLHQKVIPFV
QAENQCAAFA RVWSGRLNLP SKKEMYEWEN SNVEARGPGK AFHALAYPLD ADYLNEMHDW
VASAKPRPGL ANGGHGKWGI RWGEKERWIR SKFTLIKREY AALGEKRRAC LTLEDLGFDF
EASKATEEKN
//
