ID A0A0P7AJ94_9HYPO Unreviewed; 643 AA.
AC A0A0P7AJ94;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] 2 {ECO:0008006|Google:ProtNLM};
GN ORFNames=AK830_g8995 {ECO:0000313|EMBL:KPM37559.1};
OS Neonectria ditissima.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Neonectria.
OX NCBI_TaxID=78410 {ECO:0000313|EMBL:KPM37559.1, ECO:0000313|Proteomes:UP000050424};
RN [1] {ECO:0000313|EMBL:KPM37559.1, ECO:0000313|Proteomes:UP000050424}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R09/05 {ECO:0000313|EMBL:KPM37559.1,
RC ECO:0000313|Proteomes:UP000050424};
RA Gomez-Cortecero A., Harrison R.J., Armitage A.D.;
RT "Draft genome of a European isolate of the apple canker pathogen Neonectria
RT ditissima.";
RL Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
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:KPM37559.1}.
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DR EMBL; LKCW01000161; KPM37559.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7AJ94; -.
DR OrthoDB; 445965at2759; -.
DR Proteomes; UP000050424; 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; 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:SF304; DIMETHYLANILINE MONOOXYGENASE; 1.
DR Pfam; PF00743; FMO-like; 2.
DR PIRSF; PIRSF000332; FMO; 2.
DR PRINTS; PR00370; FMOXYGENASE.
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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000050424};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 575..601
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
SQ SEQUENCE 643 AA; 73029 MW; 3D5EDE950419C51D CRC64;
MRVAIIGGGP SGLVQLKTLL EAHQRFPVAP FEVQLFESHS KIGGIFFHHS YEDGELVSSK
FLTTFSDFRP RVDEPDFFST ERYLEYLEAY ASYYRLWPHI NLDTTVKSVR RGDSSAHVVT
YQTSDGAVVE WECDALAVCS GVHAIPHIPD IPGMERVPSV LHSSEFKTRE QFGKDKTILI
LGSGETGADI SYLAVTGDTK KVVLCHKDGW VGAPKRVPGQ KFLPWLFGAK DYDYPQLPLD
VSQVTLFDSM YVHPHVRDSM LIWDFYHFVA LPAGCWLCGG SPHGVDQFVG QIFSERFHVS
RLFLNKAWQR IHNYVSYPYR PTTWPFWTRV RRFFFNTETP PPPDRTIDIA PFPSHFSEDG
VARFPLNGRP ESERIQATEV KPDVVVLATG YLTSFPFLNT PDNDGRKAYP EAFDADVRQI
WKSDDPTVGF IGFIRPGFGA IPPLAEMQSM LFTMNLLNCI PKPLHPDDEW HYRIIHKPDA
RVSYGVEHDS YAYQLAKDMD CAPSVTEVFT IALGARKGWR LPYIWAAGAS FNAKFRLRGP
WKWEGAKDVL TGELWQTISR REGLFGNVPL SIIPMIHLGL INLFYLFYCG FWDFLAALGL
ARPIERRIEP KLIMEEMARM QEVEAKRAKL NGLGSKLNGK AMS
//
