ID C5LDC1_PERM5 Unreviewed; 702 AA.
AC C5LDC1;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE SubName: Full=Dimethylaniline monooxygenase, putative {ECO:0000313|EMBL:EER05253.1};
GN ORFNames=Pmar_PMAR027894 {ECO:0000313|EMBL:EER05253.1};
OS Perkinsus marinus (strain ATCC 50983 / TXsc).
OC Eukaryota; Sar; Alveolata; Perkinsozoa; Perkinsea; Perkinsida; Perkinsidae;
OC Perkinsus.
OX NCBI_TaxID=423536 {ECO:0000313|Proteomes:UP000007800};
RN [1] {ECO:0000313|EMBL:EER05253.1, ECO:0000313|Proteomes:UP000007800}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50983 / TXsc {ECO:0000313|Proteomes:UP000007800};
RA El-Sayed N., Caler E., Inman J., Amedeo P., Hass B., Wortman J.;
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR EMBL; GG680969; EER05253.1; -; Genomic_DNA.
DR RefSeq; XP_002773437.1; XM_002773391.1.
DR AlphaFoldDB; C5LDC1; -.
DR EnsemblProtists; EER05253; EER05253; Pmar_PMAR027894.
DR GeneID; 9050820; -.
DR InParanoid; C5LDC1; -.
DR OrthoDB; 6048at2759; -.
DR Proteomes; UP000007800; 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 CDD; cd00170; SEC14; 1.
DR Gene3D; 3.40.525.10; CRAL-TRIO lipid binding domain; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR Gene3D; 2.60.120.680; GOLD domain; 1.
DR InterPro; IPR001251; CRAL-TRIO_dom.
DR InterPro; IPR036865; CRAL-TRIO_dom_sf.
DR InterPro; IPR036273; CRAL/TRIO_N_dom_sf.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF266; FLAVIN-CONTAINING MONOOXYGENASE; 1.
DR Pfam; PF00650; CRAL_TRIO; 1.
DR Pfam; PF00743; FMO-like; 1.
DR SMART; SM00516; SEC14; 1.
DR SUPFAM; SSF52087; CRAL/TRIO domain; 1.
DR SUPFAM; SSF46938; CRAL/TRIO N-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS50191; CRAL_TRIO; 1.
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:EER05253.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000007800}.
FT DOMAIN 462..628
FT /note="CRAL-TRIO"
FT /evidence="ECO:0000259|PROSITE:PS50191"
SQ SEQUENCE 702 AA; 78568 MW; 51332DC95C72F5D6 CRC64;
MADCTSRSTA EKVCIIGGGV SGLVTLRTLL AEGFDVTLLE ARSRVGGVWA TGYVGQGAQS
PSWFYEFSEF PVGDRYPLFM KKEDLCSYID DYVSHFELAS YIHCNVVVTH LHNVNDKAWR
VVPEGTYERI ATGEIRAKQA TIEEFTKEGI LLSTGEQIAC DAVVLGTGFE AAMEILPVEC
RNSLICDNGE GPWLYRHIVH PEYMHLGFVG WASTNISIST STLQALWLAG FWRGRISPSM
QDMKCDIAKY RKWALEHIPP TPQRPCTTFL YIDLYHDQLV EDLGVSKYLH GGIFDDFKLY
YPATYRPLVV AEENSSRRTV IDCGFNLDGL TKKQHMTIGR SNPVIRRAAD DVIIPSEVKA
SEETALLLLK DLLVDTIAQY PLHESMPDVF GLMRLLMFLR VAKNDAHIAA KRFKEFLAWR
QMRKVDEIRK NILEKKLTFD DIPHIDKVTY YLPFNPCLRD AVGEPLRAKD GSFIYCERLG
MIETNGFIAE VSDDEFMEMF IYLSELGQLL IHDVYERTKE LSSFILVIDV GGAPTASWAN
PKLCKAVVNR MGSAGKLRES YYPGQVSKVC FLNAPWIFDT FFKLLRSFLS KASLSKVTIC
RPGEQTIMSL VDPMNIPAFL GGSCESPLGQ VPETGRLLND RFGLGTGGAV ETVTIAKGES
LRIPLTAVKK GDVVSWAFGV EAQEILFGVE IQTLKDGEMT SE
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