ID   A0A023GL55_9ACAR        Unreviewed;       541 AA.
AC   A0A023GL55;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   10-OCT-2018, entry version 21.
DE   RecName: Full=Dimethylaniline monooxygenase [N-oxide-forming] {ECO:0000256|PIRNR:PIRNR000332};
DE            EC=1.14.13.8 {ECO:0000256|PIRNR:PIRNR000332};
OS   Amblyomma triste.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida;
OC   Acari; Parasitiformes; Ixodida; Ixodoidea; Ixodidae; Amblyomminae;
OC   Amblyomma.
OX   NCBI_TaxID=251400 {ECO:0000313|EMBL:JAC34616.1};
RN   [1] {ECO:0000313|EMBL:JAC34616.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Mato Grasso do Sul {ECO:0000313|EMBL:JAC34616.1};
RC   TISSUE=Salivary glands {ECO:0000313|EMBL:JAC34616.1};
RA   Garcia G.R., Gardinassi L.G., Ribeiro J.M., Anatriello E.,
RA   Ferreira B.R., Moreira H.N., Mafra C., Olegario M.M., Szabo P.J.,
RA   Miranda-Santos I.K., Maruyama S.R.;
RT   "The sialotranscriptome of Amblyomma triste, Amblyomma parvum and
RT   Amblyomma cajennense ticks, uncovered by 454-based RNA-seq.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: N,N-dimethylaniline + NADPH + O(2) = N,N-
CC       dimethylaniline N-oxide + NADP(+) + H(2)O.
CC       {ECO:0000256|PIRNR:PIRNR000332}.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRNR:PIRNR000332,
CC         ECO:0000256|RuleBase:RU361177};
CC   -!- SUBCELLULAR LOCATION: Microsome membrane
CC       {ECO:0000256|PIRNR:PIRNR000332}. Endoplasmic reticulum membrane
CC       {ECO:0000256|PIRNR:PIRNR000332}.
CC   -!- SIMILARITY: Belongs to the FMO family.
CC       {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177,
CC       ECO:0000256|SAAS:SAAS00859851}.
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DR   EMBL; GBBM01000802; JAC34616.1; -; mRNA.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0016021; C:integral component of 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:UniProtKB-UniRule.
DR   GO; GO:0050661; F:NADP binding; IEA:InterPro.
DR   Gene3D; 3.50.50.60; -; 2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000960; Flavin_mOase.
DR   InterPro; IPR020946; Flavin_mOase-like.
DR   InterPro; IPR002257; Flavin_mOase_5.
DR   Pfam; PF00743; FMO-like; 1.
DR   PIRSF; PIRSF000332; FMO; 1.
DR   PRINTS; PR00370; FMOXYGENASE.
DR   PRINTS; PR01125; FMOXYGENASE5.
DR   SUPFAM; SSF51905; SSF51905; 2.
PE   2: Evidence at transcript level;
KW   Endoplasmic reticulum {ECO:0000256|PIRNR:PIRNR000332};
KW   FAD {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|RuleBase:RU361177,
KW   ECO:0000256|SAAS:SAAS00867217};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR000332,
KW   ECO:0000256|RuleBase:RU361177, ECO:0000256|SAAS:SAAS00867206};
KW   Membrane {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|SAM:Phobius};
KW   Microsome {ECO:0000256|PIRNR:PIRNR000332};
KW   Monooxygenase {ECO:0000256|PIRNR:PIRNR000332,
KW   ECO:0000256|RuleBase:RU361177, ECO:0000256|SAAS:SAAS00859857,
KW   ECO:0000313|EMBL:JAC34616.1};
KW   NADP {ECO:0000256|PIRNR:PIRNR000332, ECO:0000256|SAAS:SAAS00859858};
KW   Oxidoreductase {ECO:0000256|PIRNR:PIRNR000332,
KW   ECO:0000256|RuleBase:RU361177, ECO:0000256|SAAS:SAAS00867215};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    514    534       Helical. {ECO:0000256|SAM:Phobius}.
SQ   SEQUENCE   541 AA;  61544 MW;  165500E50F7EA1D2 CRC64;
     MSEARGRVCV VGAGSSGLTT ARQMLDYGFD VVLYERSGDV GGLWAYHDDD VEGQASVMRT
     TIINTSKEMS AFSDFPPPKD LPNYMHNTKM LGYFRSYADH FGVTKYVKTR HDVVQVTPAA
     DYDKTGRWDV VVRDLETNTD RTETFEAVAV CVGHHVYPNV PSFKGQEKFR GRVLHTHSLK
     NADKFRDHRV AVVGIGNSAV DAVVDVSHVA IETYLSTRRG AWVAKRVGPN GMPIDIFLST
     RLKNYLMHML PESVSNDYVE NILNGFFNHE VYGIKPKHRY NAQHPTVNDA LPNLILSGKV
     QVKKNVVEFT EEGVLFEGDN KVTQLDDVIL ATGYQIKFPF LPKDVVSVVD NQVQLYKYVF
     PPHLKHPTMA IIGLIQPIGA IFPIAELQAR WMAELLTKKR SLPSEEAMHE NIRKKLAAMR
     RRYVDSPRHT IQVDWIDYMD ELASQIGARP NMIKYLLTDY ELFRALLGPC VPYQFRLEGP
     HRWPGARQAI LDSRSRVMYP LNDRCSSFRR KDKGHFTFFN VCAFFFVLAV AYIFSGLRQH
     S
//