ID G2YP77_BOTF4 Unreviewed; 823 AA.
AC G2YP77;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 49.
DE SubName: Full=Similar to cellobiose dehydrogenase {ECO:0000313|EMBL:CCD53425.1};
GN ORFNames=BofuT4_P134700.1 {ECO:0000313|EMBL:CCD53425.1};
OS Botryotinia fuckeliana (strain T4) (Noble rot fungus) (Botrytis cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=999810 {ECO:0000313|EMBL:CCD53425.1, ECO:0000313|Proteomes:UP000008177};
RN [1] {ECO:0000313|Proteomes:UP000008177}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T4 {ECO:0000313|Proteomes:UP000008177};
RX PubMed=21876677; DOI=.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Guldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; FQ790347; CCD53425.1; -; Genomic_DNA.
DR AlphaFoldDB; G2YP77; -.
DR SMR; G2YP77; -.
DR STRING; 999810.G2YP77; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_0_0_1; -.
DR InParanoid; G2YP77; -.
DR Proteomes; UP000008177; Unplaced contigs.
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:UP000008177};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..823
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003440990"
FT DOMAIN 312..335
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00623"
FT DOMAIN 483..497
FT /note="Glucose-methanol-choline oxidoreductase N-terminal"
FT /evidence="ECO:0000259|PROSITE:PS00624"
FT REGION 798..823
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 823 AA; 85023 MW; A089B8334EEDAE1C CRC64;
MRTSLLTLGF AARALAQTAA SYVDANTGIT FEGATDTTGF QFGMAMEANA TSDFIGQIVF
PSTAGSGYGG VSLTGSMVGS MLIVAWPSGT DVIASLRETS GYTSPGAYAN ATAQLLPIAK
GTFVNSTHMS YTFLCQACIG NTYTLAAGAS QVVVGWALGN GTVTNAASAT GATFSYHGTG
YGDFGIQTAN AANDNYATWA AMASAASASN TTASTTTTTC SNTTVSTSNS TYDYIIAGAG
PAGIIVAERL AESGASVLML ERGNVSTYAT GGRSTVSWND TVTQYDVPSM SYYLTSASVS
DEYCTDTASM AGCILGGGTM VNALMFVRPQ EADFDDKWPT GWKWTDVSAS ADRLYERNPG
TTNPTSNSQR YDQSVWNILS SFLGNLGWSE VDAIKSPNSK TLAYSHPPWD IQDGLRAGPV
KSYYPLATAM NNFKAQLNTK VVRGIRSTTN STTFSGVEVE NTSTGVRQII NLNAGGKLIL
ASGAMSTPRI LINSGIGPTD QITTVKNGSS CVTLPAESDW INLPVGKNLK DHPIFTLTFN
VTGAMASNST SMVSTDFTSP STANIDLFAQ QTGPLVQSGQ RLNFWTSLNT TSGTKYFQGT
CNSPAAGQVR IKLYLTHGLT SSGVLGITSS GATEFTTNPW MNTADDQSAM ETMIDYFLNA
AKNSTMLTPS DSTITGSSLV SSGTYVTGDH YTGTAIMGET NDGTSVVDTN TQVWGTDNLF
VVDASIHPDM PTGNTQAIIM VAAEQAAQKI LALAGETISA ASTTASSSAS SGSSVASAPA
VSSAAASASA VSGATTSASS AAASASSGDD DDDTCPFGYE LDE
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