ID G2X591_VERDV Unreviewed; 818 AA.
AC G2X591;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 52.
DE SubName: Full=Cellobiose dehydrogenase {ECO:0000313|EMBL:EGY14232.1};
GN ORFNames=VDAG_05396 {ECO:0000313|EMBL:EGY14232.1};
OS Verticillium dahliae (strain VdLs.17 / ATCC MYA-4575 / FGSC 10137)
OS (Verticillium wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Verticillium.
OX NCBI_TaxID=498257 {ECO:0000313|EMBL:EGY14232.1};
RN [1] {ECO:0000313|EMBL:EGY14232.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=VdLs.17 {ECO:0000313|EMBL:EGY14232.1};
RG The Broad Institute Genome Sequencing Platform;
RA Ma L.-J.J., Klosterman S.J., Subbarao K., Dobinson K., Veronese P.,
RA Kang S., Gold S.E., Young S., Jaffe D., Gnerre S., Berlin A., Heiman D.,
RA Hepburn T., Sykes S., Alvarado L., Kodira C.D., Lander E., Galagan J.,
RA Nusbaum C., Birren B.;
RT "The Genome Sequence of Verticillium dahliae VdLs.17.";
RL Submitted (MAR-2008) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the GMC oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00010790, ECO:0000256|RuleBase:RU003968}.
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DR EMBL; DS572704; EGY14232.1; -; Genomic_DNA.
DR RefSeq; XP_009650586.1; XM_009652291.1.
DR AlphaFoldDB; G2X591; -.
DR STRING; 498257.G2X591; -.
DR EnsemblFungi; EGY14232; EGY14232; VDAG_05396.
DR GeneID; 20706859; -.
DR KEGG; vda:VDAG_05396; -.
DR eggNOG; KOG1238; Eukaryota.
DR HOGENOM; CLU_011025_0_0_1; -.
DR InParanoid; G2X591; -.
DR OMA; IGYLQCA; -.
DR OrthoDB; 52047at2759; -.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
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 GO; GO:0005975; P:carbohydrate metabolic process; 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; 2.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR015920; Cellobiose_DH_cyt.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
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; PF00734; CBM_1; 1.
DR Pfam; PF16010; CDH-cyt; 1.
DR Pfam; PF05199; GMC_oxred_C; 1.
DR Pfam; PF00732; GMC_oxred_N; 1.
DR Pfam; PF13450; NAD_binding_8; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF49344; CBD9-like; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS00623; GMC_OXRED_1; 1.
PE 3: Inferred from homology;
KW FAD {ECO:0000256|RuleBase:RU003968};
KW Flavoprotein {ECO:0000256|RuleBase:RU003968};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..25
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 26..818
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003438936"
FT DOMAIN 780..816
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 229..249
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 818 AA; 87506 MW; 2303756157342571 CRC64;
MRFFSRVGAG AALLAAVPFL EGVAGQTDWT SPDTGIVYQS YTGSTGMTYG IALPTDSLTV
DATEYLGYIN CPTPAGEDQG WCGLSLMPSM TNSLLFMAHP YEGEVLTSFH FATSRESVEN
YKGQATITQI TSRVTATGFS LEYRCQNCFN WEQDGFVGGH ATTQGFIVTS WALSNKAPGN
AVCPSALVIE QHASQGINGG AITPGFTNAN YATWAQLANK VVTGNCGGGT PTSTGGAGPT
TTSVPETPVT GVPVPNTAYD YIIVGSGAGG IPLADKLSEA GHKVLLIEKG PPSSGRWGGK
RGPTWLADTN LTRFDVPGLC NEIWHDSAGI ACRDTDQMAG CVLGGGTAIN AALWWKPYAA
DWDYNFPAGW KASDVAAAQQ RVFNRIPGTT RPSRDGVISL RAGMDVLRNG LAAAGWRDTD
FNANPNAKNR TFGYTPYMYS NGERGGPMAT YLVTANARSN FKLIMNTQVR RVIRSGGHVT
GVEVEPYLDG GFQGVIPLTP VTGRVILSAG TFGSAKILLR SGIGPTDQLD VVSNSTRDGS
TMISRNQWIN LPVGYNLEDH TNTNVVLEHP SVQFYDFYTA YDGTAPYQAD IQKYLTQRSG
ILAQSAPNIG PLFFEEIRGA DNVVRQLQWT ARMEASEGEV DGTLNTVVST IPYLIDTNDK
EAVIKGIENL QRALANVPNL KWLHPAPGTT ARQYVTNMVV SPSNRRANHW IGTNKLGNQD
GRINNGDSVV DTNTRVYGTD NLFVVDASIF PGMVTANPSA YFVVAAEHAA AKILALPAGK
AQPIYQQCGG LEWRGSFQCA AGLKCVDLNP YYSQCLNS
//
