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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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
//