ID G2WV78_VERDV Unreviewed; 485 AA.
AC G2WV78;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE SubName: Full=Thiol-specific monooxygenase {ECO:0000313|EMBL:EGY20203.1};
GN ORFNames=VDAG_02219 {ECO:0000313|EMBL:EGY20203.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY20203.1, ECO:0000313|Proteomes:UP000001611};
RN [1] {ECO:0000313|Proteomes:UP000001611}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VdLs.17 / ATCC MYA-4575 / FGSC 10137
RC {ECO:0000313|Proteomes:UP000001611};
RX PubMed=21829347; DOI=10.1371/journal.ppat.1002137;
RA Klosterman S.J., Subbarao K.V., Kang S., Veronese P., Gold S.E.,
RA Thomma B.P.H.J., Chen Z., Henrissat B., Lee Y.-H., Park J.,
RA Garcia-Pedrajas M.D., Barbara D.J., Anchieta A., de Jonge R., Santhanam P.,
RA Maruthachalam K., Atallah Z., Amyotte S.G., Paz Z., Inderbitzin P.,
RA Hayes R.J., Heiman D.I., Young S., Zeng Q., Engels R., Galagan J.,
RA Cuomo C.A., Dobinson K.F., Ma L.-J.;
RT "Comparative genomics yields insights into niche adaptation of plant
RT vascular wilt pathogens.";
RL PLoS Pathog. 7:E1002137-E1002137(2011).
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; DS572697; EGY20203.1; -; Genomic_DNA.
DR RefSeq; XP_009656543.1; XM_009658248.1.
DR AlphaFoldDB; G2WV78; -.
DR EnsemblFungi; EGY20203; EGY20203; VDAG_02219.
DR GeneID; 20703682; -.
DR KEGG; vda:VDAG_02219; -.
DR eggNOG; KOG1399; Eukaryota.
DR HOGENOM; CLU_006909_5_3_1; -.
DR InParanoid; G2WV78; -.
DR OMA; GHYNIPW; -.
DR OrthoDB; 2453855at2759; -.
DR Proteomes; UP000001611; Chromosome 7.
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; 1.
DR PIRSF; PIRSF000332; FMO; 3.
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:EGY20203.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000001611}.
SQ SEQUENCE 485 AA; 54495 MW; 84559E2B6887F869 CRC64;
MTTTARRVAV IGAGPSGAIA TDALVKEQAF DTIRVFDRRG AIGGTWVYTP HLPAKIPSLR
DLIAGNADHA VPIPAQLPAE TSKTERVNNH QTRFSDSALH ENLHSNIIPS IMSFTQEPFP
DKLSERTLAK YGPRAPFRHR EVVREWVQEI FVRNGNDKLL ELNTTVERAV KNEQQEWVLT
LRKETPGKDY WWEERFDALI VASGHYNVPW IPDIPGIVDF DRVVIVGGSI SSHEVLHEIL
PKAKKPVYAA LRGDPVPAFG WAPFTHPHIV VKNEITRFDP GTGTLFFADG SYLDDVDHVI
FGTGYTFSLP FLPDVQAKIK QANRRLPGVF QHTFSIDDPS LAFIGMLGGG FTFRVYEWQA
VAVARLLAGR ARPLPPRSEQ LEWEQKRVAE LKGGKNYYSI ALDYVGFFEY LRYIAGDPTP
GTTGRVLPPF DKASLAIWTG MVATKIKGFE EDARKAELEI RSQQEHETQQ RLREIIGNWS
PRAKL
//
