ID   A0A135RQK3_9PEZI        Unreviewed;       568 AA.
AC   A0A135RQK3;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   27-MAR-2024, entry version 17.
DE   SubName: Full=Fungal cellulose binding domain-containing protein {ECO:0000313|EMBL:KXH25984.1};
GN   ORFNames=CNYM01_01825 {ECO:0000313|EMBL:KXH25984.1};
OS   Colletotrichum nymphaeae SA-01.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC   Colletotrichum acutatum species complex.
OX   NCBI_TaxID=1460502 {ECO:0000313|EMBL:KXH25984.1, ECO:0000313|Proteomes:UP000070054};
RN   [1] {ECO:0000313|EMBL:KXH25984.1, ECO:0000313|Proteomes:UP000070054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-01 {ECO:0000313|EMBL:KXH25984.1,
RC   ECO:0000313|Proteomes:UP000070054};
RA   Baroncelli R., Thon M.R.;
RT   "The genome sequence of Colletotrichum nymphaeae SA-01.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|PIRSR:PIRSR000137-2};
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:KXH25984.1}.
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DR   EMBL; JEMN01001831; KXH25984.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A135RQK3; -.
DR   Proteomes; UP000070054; 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; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR012132; GMC_OxRdtase.
DR   InterPro; IPR000172; GMC_OxRdtase_N.
DR   InterPro; IPR007867; GMC_OxRtase_C.
DR   PANTHER; PTHR47190:SF2; CELLOBIOSE DEHYDROGENASE (AFU_ORTHOLOGUE AFUA_2G17620); 1.
DR   PANTHER; PTHR47190; DEHYDROGENASE, PUTATIVE-RELATED; 1.
DR   Pfam; PF05199; GMC_oxred_C; 1.
DR   Pfam; PF00732; GMC_oxred_N; 1.
DR   PIRSF; PIRSF000137; Alcohol_oxidase; 1.
DR   PRINTS; PR00411; PNDRDTASEI.
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.
PE   3: Inferred from homology;
KW   FAD {ECO:0000256|PIRSR:PIRSR000137-2, ECO:0000256|RuleBase:RU003968};
KW   Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..568
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007801052"
FT   DOMAIN          112..135
FT                   /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT                   /evidence="ECO:0000259|PROSITE:PS00623"
FT   BINDING         114
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         241
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
FT   BINDING         548..549
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR000137-2"
SQ   SEQUENCE   568 AA;  61028 MW;  2DB906133F7A86C5 CRC64;
     MIMKFFSGFM ALALTQLSMT LLAATVPDHT YDYIVVGRGP GGIVTADKLS ASGKSVLLIE
     RGPPSSFRWG GRRRGAWLEN SNLTRFDVPG LYGHIWQDSA GIKCQDVVPM AGCVLGGGSA
     INAGLWFKPQ SLDWDTQFPD GWKAKDLSAA TDRAFRRVPW TDVPSKDGVL YNRQTNDLIT
     KGLVENGWIS VKANNEPDAK RRTVSQSEYF YQHGERGGLL ETYLVSAAAR GNFKLWTNTL
     VTRVERRGDS VTGVQVESAG DGGYNGTVKL AAGGRVILSA GVFGSAKILF RSGIGPKDQL
     ETVQKVEGDI LIDSAQWIDL PVGYNLDDHV NTNILFEHPD IANYDFNSAY NNPSPDDAAA
     YLSNRSGILA QAAPNINPIF WDAVKGDDGI ERWFQWTSYV GGPQTGKTYN TSGMAAALGL
     GKTSRGRATI NSSLIIDVSV LPYFNDEGNH DFEAVVTTVS GVVKAISSIP GATMIGPAPG
     QDVRDYVQKL AVDIGRTANH WVGTTRLGTD SALEGGKSVV DLNAQVYGTK NLHVVDAGIL
     NGIFTANPQA GIVIAAEKVA EDIIRLHG
//