ID D4DAS6_TRIVH Unreviewed; 522 AA.
AC D4DAS6;
DT 18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT 18-MAY-2010, sequence version 1.
DT 24-JAN-2024, entry version 43.
DE SubName: Full=Flavin-containing monooxygenase, putative {ECO:0000313|EMBL:EFE41026.1};
GN ORFNames=TRV_04224 {ECO:0000313|EMBL:EFE41026.1};
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:EFE41026.1, 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:EFE41026.1}.
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DR EMBL; ACYE01000215; EFE41026.1; -; Genomic_DNA.
DR RefSeq; XP_003021644.1; XM_003021598.1.
DR AlphaFoldDB; D4DAS6; -.
DR GeneID; 9578605; -.
DR KEGG; tve:TRV_04224; -.
DR HOGENOM; CLU_024886_0_0_1; -.
DR OrthoDB; 1826198at2759; -.
DR Proteomes; UP000008383; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 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; PR00368; FADPNR.
DR PRINTS; PR00469; PNDRDTASEII.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:EFE41026.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 453..476
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 482..501
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 522 AA; 58487 MW; B1CB4FAFB08FCD65 CRC64;
MSLISSVGRS LAHIYSQCFI ICYTLIQDIL VYVFATNAPP PSSRNKRLRR PRVAIIGSGL
TGVSAAAHCV GHGFDVKIFE ARPKDKGLGG IWSRVNSTSS LQIHSIMFRF HPSVKWKDAY
PNQQQIKDQI VELWKTYHLD DKTVFDTPVK STRKNDQGRW VINDDEDTHG TFDGIVAAVG
SCGDPKMPTL PHQDKFTGQV YHSSELDGLD AKGKRIVVVG GGASAVEALE FAVNAGAANI
DVLSRSDKWI IPRNVVVDVL LACNIFGQET ILSFIPETLL RKLFYRDLED IAPSGKGLFT
DTPMVNSDLF ELIRAGKARW LRGDILSVEE DGISFNHRAQ GVPKSGPGHE IFVKADIIIM
ATGFIRPSLS FLPQEVFEPP YDPPNWYLQI FPPAYPSICT NNSTFVNAIG TVGNYHIGIY
TRLLLMFLID PLSRPREYLM KRWVDMTRIM KRFAPTGAFD FFTYAELLYW FVFVMVFNPF
RWKWAAFVFF GLGRVLPMAV VDKEDDAREL LGADSRSSVS GN
//