ID   D2VBT0_NAEGR            Unreviewed;       631 AA.
AC   D2VBT0;
DT   02-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   02-MAR-2010, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   SubName: Full=Predicted protein {ECO:0000313|EMBL:EFC45520.1};
GN   ORFNames=NAEGRDRAFT_66322 {ECO:0000313|EMBL:EFC45520.1};
OS   Naegleria gruberi (Amoeba).
OC   Eukaryota; Discoba; Heterolobosea; Tetramitia; Eutetramitia;
OC   Vahlkampfiidae; Naegleria.
OX   NCBI_TaxID=5762 {ECO:0000313|Proteomes:UP000006671};
RN   [1] {ECO:0000313|EMBL:EFC45520.1, ECO:0000313|Proteomes:UP000006671}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NEG-M {ECO:0000313|EMBL:EFC45520.1,
RC   ECO:0000313|Proteomes:UP000006671};
RX   PubMed=20211133; DOI=10.1016/j.cell.2010.01.032;
RA   Fritz-Laylin L.K., Prochnik S.E., Ginger M.L., Dacks J.B., Carpenter M.L.,
RA   Field M.C., Kuo A., Paredez A., Chapman J., Pham J., Shu S., Neupane R.,
RA   Cipriano M., Mancuso J., Tu H., Salamov A., Lindquist E., Shapiro H.,
RA   Lucas S., Grigoriev I.V., Cande W.Z., Fulton C., Rokhsar D.S., Dawson S.C.;
RT   "The genome of Naegleria gruberi illuminates early eukaryotic
RT   versatility.";
RL   Cell 140:631-642(2010).
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; GG738862; EFC45520.1; -; Genomic_DNA.
DR   RefSeq; XP_002678264.1; XM_002678218.1.
DR   AlphaFoldDB; D2VBT0; -.
DR   EnsemblProtists; EFC45520; EFC45520; NAEGRDRAFT_66322.
DR   GeneID; 8858742; -.
DR   VEuPathDB; AmoebaDB:NAEGRDRAFT_66322; -.
DR   eggNOG; KOG1399; Eukaryota.
DR   InParanoid; D2VBT0; -.
DR   OMA; DCYERET; -.
DR   OrthoDB; 2453855at2759; -.
DR   Proteomes; UP000006671; Unassembled WGS sequence.
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; 1.
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};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006671}.
SQ   SEQUENCE   631 AA;  73129 MW;  C20A872E2AD494C5 CRC64;
     MFELISSFLY EVIRYVFHVI YLIYTVWNFN HHHYPDNHNN KNSNNKYDQQ FINEQCGESN
     FPLLRSLLID SIELLKACFN FVFESFGDEK QRTFSKPSKQ KPRSVCIIGA GVSGLVSLKT
     IIHDYSDVDF ANVIVFERSE SVGGLWNCNQ AGKSKQFYEL LMESGKNLMD NIDISPMYAS
     LHTNTSRDLM GFSDFPMNEK FPDFPSCEQV NNYLKAYVEK FDLMRYVMFN TEVVSVRKKD
     KIDQATCKFF ERNHVDKLTK WIVITKNLLT NECVEREFDV VIVGNGKNTK PRLPEQFKNL
     AQTYKLGKVF HSKIYQDDYE IFRDKTVLII GSGSSGSDIA SRVALVTENT YISVQKGASL
     LPKYLDGKPI DFNVARRRYF TWLPKRIQTM ILNFFINNRL PKSKLYHPFN SNPSRNHTVG
     LSSELIVEIG FGRVKVHPPL VSFSESEIKF ENGTSLAPDY IILSTGYELH FPFLEDDILQ
     LDENKSRTTK LYEHIFHMDY PNLIFLGLPF TVHPLIVCEL QARYAISVLA GQNSIPTKEA
     IKRANQTKIT NLESISINPI KFFHREYHLD YCDKLAKLGG FFPNPFKYEN FPYFKDLIFG
     PFYGIHFRMQ GCGKLSDNQI ASILTRYKEN E
//