ID   A0A010QVV7_9PEZI        Unreviewed;       813 AA.
AC   A0A010QVV7;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 34.
DE   SubName: Full=GMC oxidoreductase {ECO:0000313|EMBL:EXF84317.1};
GN   ORFNames=CFIO01_08348 {ECO:0000313|EMBL:EXF84317.1};
OS   Colletotrichum fioriniae PJ7.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1445577 {ECO:0000313|EMBL:EXF84317.1, ECO:0000313|Proteomes:UP000020467};
RN   [1] {ECO:0000313|EMBL:EXF84317.1, ECO:0000313|Proteomes:UP000020467}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PJ7 {ECO:0000313|EMBL:EXF84317.1,
RC   ECO:0000313|Proteomes:UP000020467};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum fioriniae PJ7.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC       {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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:EXF84317.1}.
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DR   EMBL; JARH01000184; EXF84317.1; -; Genomic_DNA.
DR   RefSeq; XP_007592061.1; XM_007591999.1.
DR   AlphaFoldDB; A0A010QVV7; -.
DR   STRING; 1445577.A0A010QVV7; -.
DR   KEGG; cfj:CFIO01_08348; -.
DR   eggNOG; KOG1238; Eukaryota.
DR   HOGENOM; CLU_011025_0_0_1; -.
DR   OrthoDB; 52047at2759; -.
DR   Proteomes; UP000020467; 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   CDD; cd09630; CDH_like_cytochrome; 1.
DR   Gene3D; 2.60.40.1210; Cellobiose dehydrogenase, cytochrome domain; 1.
DR   Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR015920; Cellobiose_DH_cyt.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   PANTHER; PTHR47190:SF5; PX DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF16010; CDH-cyt; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   SUPFAM; SSF49344; CBD9-like; 1.
DR   SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR   SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR   PROSITE; PS00623; GMC_OXRED_1; 1.
DR   PROSITE; PS00624; GMC_OXRED_2; 1.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Reference proteome {ECO:0000313|Proteomes:UP000020467};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..813
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5001456372"
FT   DOMAIN          312..335
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   DOMAIN          479..493
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00624"
FT   REGION          745..813
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        745..793
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   813 AA;  84094 MW;  547D8F2E4500F9AB CRC64;
     MFKSLLTTGL LAAAAVAQQT TSYVDSATGI TFQRYTETSG FSFGVALPST VGKDFIGQIS
     APITAGWASV SLGGPMANKL LVVAWPNGDS IQTSIRKASG YSNPDVVTDS GITLKPIESG
     TSVNATAFTY TFVCEGCITG DTTTFTGTSD TTTFGWAYST TALSDTTSAS VALNYHGAGF
     GLFGANLASA KSADYATWAA KASDAVSTPG TGNGTSPSVP ANITTTISNT TYDYIVAGGG
     AAGLIVAERL AESGKSVLLL ERGGASLASS GGKATVDWNS TVTQYDVPAM GYYLSTAKET
     SEYCTDTASQ AGCILGGSTM VNAMMWVKPP AHDFDDKWPT GWKWSSVEES ANKLYERTPG
     TILASKDGKR YDQGAYDVMS QWLAGNGFSE VDALAEPDKK QAVFTHPPWL IENGMRGGPV
     RDYLPLAQAL PNFKLQLNAK VIRAIRNGTT ISGVEIETAT NVRQIINLKS GGAAILAAGA
     LSSPRILFNS GIGPKEQIQT VQNGTAQVTL PSEAQWIDLP VGQNLKDHPI FTVNFKTKST
     LNSLASTAFT APSQTDVDQF AQGSGLLSQA GQRLNFWTSV EGSDGGKRYV QGTVNSPAND
     TIRVKVYLTH GLTSVGALGI SADGSTKLTT EPYLTTAEDK EAITSFMNQL IQYASKSNST
     LTLSGNVTAE SLISEHTTGS HFVGSAVMGS TNDGNSVVDT KTKVWGTDNL YVVDASIHPD
     LPTGNTQAIV MVAAEHAAAQ ILGAGSATNS GSESSSGSGS GSGSGTGSGS GTGSGSGTGS
     GSGSGSGSGS TGCKRSVKRL ERLQRFRRAH HSF
//