ID A0A023GL55_9ACAR Unreviewed; 541 AA. AC A0A023GL55; DT 11-JUN-2014, integrated into UniProtKB/TrEMBL. DT 11-JUN-2014, sequence version 1. DT 09-DEC-2015, entry version 9. 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 -!- 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}. 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; GBBM01000802; JAC34616.1; -; mRNA. DR GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell. 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-EC. DR GO; GO:0050661; F:NADP binding; IEA:InterPro. DR Gene3D; 3.50.50.60; -; 2. DR InterPro; IPR012143; DiMe-aniline_mOase. DR InterPro; IPR023753; FAD/NAD-binding_dom. 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|SAAS:SAAS00315531}; KW Flavoprotein {ECO:0000256|PIRNR:PIRNR000332, KW ECO:0000256|SAAS:SAAS00315515}; 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|SAAS:SAAS00315513, ECO:0000313|EMBL:JAC34616.1}; KW NADP {ECO:0000256|PIRNR:PIRNR000332}; KW Oxidoreductase {ECO:0000256|PIRNR:PIRNR000332, KW ECO:0000256|SAAS:SAAS00315533}; 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 //