ID A0A066Y1X6_COLSU Unreviewed; 792 AA.
AC A0A066Y1X6;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Putative GMC oxidoreductase {ECO:0000313|EMBL:KDN72066.1};
GN ORFNames=CSUB01_10631 {ECO:0000313|EMBL:KDN72066.1};
OS Colletotrichum sublineola (Sorghum anthracnose fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=1173701 {ECO:0000313|EMBL:KDN72066.1, ECO:0000313|Proteomes:UP000027238};
RN [1] {ECO:0000313|Proteomes:UP000027238}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TX430BB {ECO:0000313|Proteomes:UP000027238};
RX PubMed=24926053; DOI=10.1128/genomeA.00540-14;
RA Baroncelli R., Sanz-Martin J.M., Rech G.E., Sukno S.A., Thon M.R.;
RT "Draft genome sequence of Colletotrichum sublineola, a destructive pathogen
RT of cultivated sorghum.";
RL Genome Announc. 2:E0054014-E0054014(2014).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790}.
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:KDN72066.1}.
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DR EMBL; JMSE01000063; KDN72066.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A066Y1X6; -.
DR STRING; 1173701.A0A066Y1X6; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_0_0_1; -.
DR OMA; FIHPPER; -.
DR OrthoDB; 52047at2759; -.
DR Proteomes; UP000027238; 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; PS00624; GMC_OXRED_2; 1.
PE 3: Inferred from homology;
KW Reference proteome {ECO:0000313|Proteomes:UP000027238};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..792
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5001630942"
FT DOMAIN 484..498
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 759..792
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 778..792
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 792 AA; 84282 MW; 1D514B398E61AEB9 CRC64;
MRSILSRAAA LLGLAGTTAA QLRTSAYTDP QTGIDFQNFK ADSYGYSFGV AVPETIGTDF
IGQMVVPISE KGNWGGVSLK GGMLNGLLFV AWADGKDIRT SFRIVSAYAN PSVYTENKVN
AVPIANGTFV NSTHFSYTFL CQNCINDDTS LTSDSPVLGW AFSDTSPTPA SDPAAPLNYH
SAGFGEFGLD IAAAKSAKFD TWAKYAKAAK TSPVPGNGTT TPAPGNSTIP APTTSNTTYD
VIVVGGGPAG IIAAERLAEK GVSVLLIERG PANTAPLGSK LQLPWNNSLT PYDIPALADT
MTTLPGVSFC SDTASTAGCV FGGSSSINGL NFIHPPERDW DRWPAGWNGK DVSAAASRLY
ERNPGTTAPS EDDKYYDDLT FNVLSGLLQA KGWTQVDSIA SPDKKDNVFS RPSFSIKDRL
RAGPARTYMP FAQKLPNFTL KLETKVIQVI RTGSRVTGVL VQATNGSTQI IKLNQGGKVV
LAAGAMSTPR VLWNSGIGRS DALATVKSGA ATTGVTLPDE ADWIDLPVGH NLKDHAQILL
KFKSKTNFTA YPFSAITASP IKSDLELYNR GSGPIAQGDQ RIHLWTSAKG ADGRTRYLQG
TASAMVNGIF YLRTFLTHGT SSVGELGITA SGNTVIKTKP WLVEQEDRKA MSNFIQYWLD
LAGGANSSIS YITPRATPAD IIGNDIISGD HWVGSTKMGT DDGRRNNGTA VVDLDTKVYG
TDNLFVVDAS IHPDLPTGNT QSIIMITAEH AAEKIAAFKV SGSNSTAPEE SPKCSKRSTH
RTMRSRRSAR RH
//
