ID A0A2S7PN28_9HELO Unreviewed; 884 AA.
AC A0A2S7PN28;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE SubName: Full=Flavin-binding monooxygenase protein {ECO:0000313|EMBL:PQE15680.1};
GN ORFNames=CJF30_00006109 {ECO:0000313|EMBL:PQE15680.1};
OS Rutstroemia sp. NJR-2017a BBW.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Rutstroemiaceae; Rutstroemia.
OX NCBI_TaxID=2070414 {ECO:0000313|EMBL:PQE15680.1, ECO:0000313|Proteomes:UP000238072};
RN [1] {ECO:0000313|EMBL:PQE15680.1, ECO:0000313|Proteomes:UP000238072}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NJR-2017a BBW {ECO:0000313|EMBL:PQE15680.1,
RC ECO:0000313|Proteomes:UP000238072};
RA Gaut B.S., Morton B.R., Clegg M.T., Duvall M.R.;
RL Submitted (JAN-2018) 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:PQE15680.1}.
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DR EMBL; NJPT01000044; PQE15680.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S7PN28; -.
DR STRING; 2070414.A0A2S7PN28; -.
DR Proteomes; UP000238072; 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; 1.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR020946; Flavin_mOase-like.
DR PANTHER; PTHR23023; DIMETHYLANILINE MONOOXYGENASE; 1.
DR PANTHER; PTHR23023:SF292; FLAVIN-BINDING MONOOXYGENASE-LIKE PROTEIN (AFU_ORTHOLOGUE AFUA_6G01900); 1.
DR Pfam; PF00743; FMO-like; 1.
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 Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:PQE15680.1};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000238072}.
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 572..666
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 584..601
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 625..646
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 647..666
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 884 AA; 96990 MW; 211767B55AA80948 CRC64;
MANMEHFDVV VVGAGWYGLA AAKTQLEVHP DVKMVILTDN TTIGGTWAKG RLYPGLKTNN
LYGVFEFSDF PMWTEVYRVQ PREYIPGTTV YKYLTDYAKH FNIYDKVRYE TRVLSAKHVD
AGGWILTMSK EVKDKGSETS TIFASKLIVA TGHTAEEFVP NLPGREKFSA PFFHMKYLPK
MQDTFKTAKS VCVYGGAKSA YDAAYTYASR GIHVDWIIRE SGHGPGWMSN SFVSPFKLWV
ERLTKVRFLT FMSPCIWGDN DGFGTIRNWF CKSTIGKFIS SRFWRILQAD IVTDVNWDAH
PETAKLRPWS DVKYTGTMLS ILNYETDILE LVRNGAISVH IADIKDMAGN KLSLSNGEVI
TTDAFIAATG WKHTSSIKLL PGDSNTELPE PIGSSEPSSY TTKADNEIFS KFPVLSKRPE
PRVLGIVKPE GKSNEQRDPY RLYRFMIPPV YANSRDIAYV GALTSVSVPD IAQTQALWVT
AFFDHKIPIP SDITYQTVLH SRFGKWRYPY GFGARYPDFL FDILPYIDML LKDLNLKTHR
KSNIFWELFE PYRLRDYKGL VDEWKESIKE VEAEGEPIQD RSHGSTEGAE SSSNSSKSAA
MVLIPADTKA PLPNHNRATT PDSTIPDLDP PPYTPFDSPL PTPRFPPSSS SSSQTPNIPT
SKAVSSSGAI SLLGPLRILE SVSGSSSITL SQHVTIEGPL KSSSKIVLAD DVHVQGGIKG
SSSILLDGGE GKGAVRVGEG VRASGSVELR GDVWVKGDVS ASGKVLLEGV GGAVRVGGKV
NSSSAVTVRG EVQLGDVVCS GKIVVEGGGK ECLVVDGDVS CKSGAVIDRD VQVCKNFSAK
GNVSINGRLL VKGDLTVWGN VKIQQGSELI VNGMRTVHGK LEQL
//
