ID A0A3M2S334_9HYPO Unreviewed; 366 AA.
AC A0A3M2S334;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=CDV36_008418 {ECO:0000313|EMBL:RMJ11951.1};
OS Fusarium kuroshium.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium solani species complex.
OX NCBI_TaxID=2010991 {ECO:0000313|EMBL:RMJ11951.1, ECO:0000313|Proteomes:UP000277212};
RN [1] {ECO:0000313|EMBL:RMJ11951.1, ECO:0000313|Proteomes:UP000277212}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UCR3666 {ECO:0000313|EMBL:RMJ11951.1};
RA Stajich J.E., Carrillo J., Kijimoto T., Eskalen A., O'Donnell K.,
RA Kasson M.;
RT "Comparative genomic analysis of Ambrosia Fusariam Clade fungi.";
RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases.
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 -!- 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:RMJ11951.1}.
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DR EMBL; NKUJ01000151; RMJ11951.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3M2S334; -.
DR STRING; 2010991.A0A3M2S334; -.
DR Proteomes; UP000277212; Unassembled WGS sequence.
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 CDD; cd22278; DPBB_GH45_endoglucanase; 1.
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};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000277212};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 21..366
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5018109442"
FT DOMAIN 325..364
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 224..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 227..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 29
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
SQ SEQUENCE 366 AA; 37761 MW; E1219514B487702C CRC64;
MRSSTLIALA GPLAVRAASG NGHSTRYWDC CKPSCSWADK ASVSAPALTC DKNDNPISDA
NAKSGCDGGS AFACTNYSPW AVNDNLAYGF AATKLSGGSE ATWCCACYSL TFTTGPVKGK
TMVVQSTNTG GDLGENHFDL QMPGGGVGIF DGCSSQFGGS GLGGAQYGGI SARSDCDSFP
ELLKDGCYWR FDWFENADNP DFTFEQVQCP KALTDISGCT RDDDSSFPAF SGDTSSSGSS
SGSGSSSKAS TSKAAVQTQK TQAPATEQKS TQVQQQPSNV QTQVQSSASQ PQQTQAPVQE
PATSKTTKAT AKASATKSAA ASAQSAVAAW YQCGGSKSAY PDGNLPCASG STCVQHNEYY
SQCVPN
//
