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Database: UniProt
Entry: A0A0K6GIB2_9AGAM
LinkDB: A0A0K6GIB2_9AGAM
Original site: A0A0K6GIB2_9AGAM 
ID   A0A0K6GIB2_9AGAM        Unreviewed;       480 AA.
AC   A0A0K6GIB2;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   SubName: Full=Flavin-containing monooxygenase FMO GS-OX3 {ECO:0000313|EMBL:CUA78250.1};
GN   ORFNames=RSOLAG22IIIB_13034 {ECO:0000313|EMBL:CUA78250.1};
OS   Rhizoctonia solani.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Cantharellales; Ceratobasidiaceae; Rhizoctonia.
OX   NCBI_TaxID=456999 {ECO:0000313|EMBL:CUA78250.1, ECO:0000313|Proteomes:UP000044841};
RN   [1] {ECO:0000313|EMBL:CUA78250.1, ECO:0000313|Proteomes:UP000044841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BBA 69670 {ECO:0000313|EMBL:CUA78250.1};
RA   Noorani M.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the FMO family. {ECO:0000256|ARBA:ARBA00009183}.
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DR   EMBL; CYGV01001966; CUA78250.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K6GIB2; -.
DR   Proteomes; UP000044841; Unassembled WGS sequence.
DR   GO; GO:0016020; C: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: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; 2.
DR   PRINTS; PR00370; FMOXYGENASE.
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   Membrane {ECO:0000256|SAM:Phobius};
KW   Monooxygenase {ECO:0000256|ARBA:ARBA00023033, ECO:0000313|EMBL:CUA78250.1};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000044841};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   480 AA;  54396 MW;  11CBDFC8B503314F CRC64;
     MVGTSTQSRP RRFAIVGAGG AAGLATLQVF VSELHDYIQT GEIEVVGFEQ RQDIGGIWLA
     EPRPDPSKQI WPETPTYDSL HTNIPHPIMY YPSQWAPPST PLFTDAQTVY DYMRSYADRF
     GLQQYIRFNT QVIAATWDDS TNQWNVTTRP YGDQVGKEVE SVTHYDHLLV TNGHNRRPFT
     PDVDGFEDWA ASESRSSIHS IWYRTPEPYR DHDVLVIGGG RSGADCSADL STVARKTIHS
     VRSAEDSDLG RIIQRGEISH FTPDGLVHFK NGKQEYVDRI IFATGYEYDC SFLTQLPVEE
     AHRSSDHLYN SRFHIYPLAL HTFPLRAAFP PSSLAFIGIP NGAPAFTLSE VQAKLAIRQM
     TGKVSLDFEH ELTRTLERNE ELQKKHSSPL EVARAWHKFG KGNGNPYDFL DLLLQRADDS
     ARMPKWKREF GPFGVTILVE WKKLERLGLA DSWARGVGEG GIKEWVDLMW RVVRRAKDSA
//
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