ID G2Y7D7_BOTF4 Unreviewed; 330 AA.
AC G2Y7D7;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
GN ORFNames=BofuT4P277000014001 {ECO:0000313|EMBL:CCD48539.1};
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:CCD48539.1, 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 -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000966, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FQ790293; CCD48539.1; -; Genomic_DNA.
DR AlphaFoldDB; G2Y7D7; -.
DR STRING; 999810.G2Y7D7; -.
DR eggNOG; ENOG502RXA6; Eukaryota.
DR HOGENOM; CLU_045022_1_0_1; -.
DR InParanoid; G2Y7D7; -.
DR Proteomes; UP000008177; Unplaced contigs.
DR GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR036908; RlpA-like_sf.
DR PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:CCD48539.1};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000008177};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..330
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003439932"
FT DOMAIN 294..330
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 242..264
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 34
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
SQ SEQUENCE 330 AA; 33430 MW; BAD1CA987B798B5F CRC64;
MKANLVISAL FSSLLPTIIH AQSSGTGTTT RYWDCCKASC GWSKKATLAT GSNPVGSCDI
SNNPLTDYNA VSYCASSSGT AFMCGAQTPW AVSDTLSYGF AATTISGGTE ASWCCACYQL
TFTSGPVAGK QMIVQATNTG GDLGSNQFDL AIPGGGFGIF DACTHQYPST PASAWGARYG
GLSDRTQCAS LPAALQPGCY WRFDWFLNAD NPGVTFKQVA CPAALTAKSG CVRANDAIDE
TPTGPSAVPT WTSGSGGSGS TSSAAVSTSK STSVGATIST SSTTTSAASG GTGTPIARYA
QCGGIGYSGS TTCASPYTCS VLNAYYSQCV
//
