ID   A0A1E1LQB3_9HELO        Unreviewed;      1780 AA.
AC   A0A1E1LQB3;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=Related to cholesterol oxidase {ECO:0000313|EMBL:CZT12684.1};
GN   ORFNames=RCO7_10927 {ECO:0000313|EMBL:CZT12684.1};
OS   Rhynchosporium commune.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Ploettnerulaceae; Rhynchosporium.
OX   NCBI_TaxID=914237 {ECO:0000313|EMBL:CZT12684.1, ECO:0000313|Proteomes:UP000178129};
RN   [1] {ECO:0000313|EMBL:CZT12684.1, ECO:0000313|Proteomes:UP000178129}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UK7 {ECO:0000313|EMBL:CZT12684.1,
RC   ECO:0000313|Proteomes:UP000178129};
RA   Ploux O.;
RL   Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790}.
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DR   EMBL; FJUW01000075; CZT12684.1; -; Genomic_DNA.
DR   STRING; 914237.A0A1E1LQB3; -.
DR   InParanoid; A0A1E1LQB3; -.
DR   OrthoDB; 1945480at2759; -.
DR   Proteomes; UP000178129; Unassembled WGS sequence.
DR   GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR   GO; GO:0016614; F:oxidoreductase activity, acting on CH-OH group of donors; IEA:InterPro.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 3.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR003953; FAD-binding_2.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47470; CHOLESTEROL OXIDASE; 1.
DR   PANTHER; PTHR47470:SF1; FAD-DEPENDENT OXIDOREDUCTASE 2 FAD BINDING DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00890; FAD_binding_2; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
PE   3: Inferred from homology;
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW   Reference proteome {ECO:0000313|Proteomes:UP000178129}.
FT   DOMAIN          570..618
FT                   /note="FAD-dependent oxidoreductase 2 FAD binding"
FT                   /evidence="ECO:0000259|Pfam:PF00890"
FT   DOMAIN          650..859
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00732"
FT   DOMAIN          1055..1119
FT                   /note="Glucose-methanol-choline oxidoreductase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF05199"
FT   REGION          1..33
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          462..483
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          504..557
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..23
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        542..556
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1780 AA;  198063 MW;  D01ABCB59CE2712A CRC64;
     MDERPATADT LISERDETSS DQESNHSDSS ISPELEEFDR WQATIGLKTF GEKLNAAAKA
     VFPTEIRSRY AMVNVLLAFW AEEDANSPAP IEISKLYNVF KDTFHFNVQT FRIPGESSNI
     AVSEKMSDFV NLGGNSEDDL KIVYYAGSSR VLKDKSLVWT SGRRGQKSFV EWSSVQTLLK
     QAQSDTLIFL DCAHAKTPCG NWNSDLTELV AARSFNVASK LAEPYSFTKD LIVELQDLST
     LPSFSVGNLY HNLFCRAQSR ISEQSGNDRA PIHIPLAQKK FRSIRLAVQT SGQNGCIKTS
     FKVQHLNSAG TNGFTQTPSF LHSSAVSLGE SSRMAFAIRV KDNFNVRDLS SDFFLQWLGN
     LPGTVAEVKI EAGFHSFSSL LIVSIPICMS IYMPQDSAVI SLGPITSFNQ VLNRIPGIMP
     NDLPTPKPDV WEFQNLPSPM NGATQNVNQD LNRSLRPSEI RFQKHTDTIG GKENRRPSLT
     GGFSSDVSID GSFIEPLLPN GLRHGHTLSG ELPPSLEKSH PIAAPGPHTS EPNGPQSHAH
     AKIRSYTDDP DTQKFPRISR PVELLRNSYD CIVIGSGYGG GVAASRMARA GQSVCLLERG
     KERWPGEYPS GFIDAFKNLH VSGEFAPGFL KGAMVESGDP TGLYHLICGK GQNAFVGNGL
     GGTSLLNANV FLETDSKTMK MPCWPKELRK ADSLREYYDR AADILEPETY PQDWPELPKL
     TMLERQAKAL GLGDKFKRVP QTTRFKGGPN STGVEMYPSA LTGMDCTGVN DGSKSSTLVN
     YLSDAWNWGA GMFCECEVRY IKKHPDPEEE GYLVFFAWHG SCRGAFQERL YEDLMWVHAK
     KCVFLGAGSI GTTEILLRSK KLGLSMSDKV GTGMSGNGDI LAFGYNTDTE VNAIGRQYPS
     PYKPVGPTIS GIIDCRDDHD NPLDGFVIQE GAIPKALAPL FQTMLEMMPG NQIPIGQTLL
     EKVKHSIAQQ GSRFLGPYYS KGSIERTQVY LVMSHDSNQA ILTLKDDKPV LEFLGVGRSD
     HVQYLNDILR QATQAVGGTF VNSPFYAALG QQEITVHPIG GACMSKSEFG EHGVTNHWGE
     VFTGDGKDTH HGLVVTDGAV IPTALGVNPF ATITALAERS VEHAAELRIK RKIDFETKND
     MLDLFAEPHQ YAGGKKTLQR NDTTGLRDAT SLVKATREAK ANGFGFSEVM SGYIHVGEGI
     EGDKIEDFET AAKTAKGLCE EARFFLSVKA WDTETIVNRA DHRAMLTGTF TCAGLPGSPF
     MVQRGSFHLF SVDQEAPGTR NLTYDFDMTS TDGRAFHFHG QKIVDSSVAL GPWRFWKATS
     TLYVTISESY GRKQVLGRGM MHIKPSDFLS EIFTLKSSGK SLFAKMHSTM SFMGFFARQS
     MGLFLAPFTW QQYPSVTYTG YINDTSPEHT IQIVASDGVR SLLHVWEPRN PNLKPINLFM
     IPGASVDQQI FSLPTIEVNA VNYFTRAGYR VFVSVHRICQ LMVAENDWTT YDARLDIRAC
     FEWIRKEHGH APIYTISHCM GAVAYSSGLL DGTIPAKWVK GISSSQVLMN PIWSTLNMAK
     VLAGPIPFDK LYTWLGGKWF SCSSTRDDSY FQQFVNQILR FYPDSREEMC NNVSCHRCSL
     IFGRLWNHRN LNEATHRQIN RFFGGVNMTL LHLLMQMGYR GFVTTNGPLF NDLTTEHNLR
     RLKNIPIMLF SGSDNKVLTP ESTDKSYSLM RDLFGTKHYS RHVIQGYGHL DCWMGRRAYK
     DVFPIVREEV DRVCRGEEYR YQEPDWEDDW MGWKDLPKSG
//