GUN5_HYPJE
ID GUN5_HYPJE Reviewed; 242 AA.
AC P43317;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 101.
DE RecName: Full=Endoglucanase-5;
DE EC=3.2.1.4;
DE AltName: Full=Cellulase V;
DE AltName: Full=Endo-1,4-beta-glucanase V;
DE Short=EG V;
DE AltName: Full=Endoglucanase V;
DE Flags: Precursor;
GN Name=egl5;
OS Hypocrea jecorina (Trichoderma reesei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=51453;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 26921 / CBS 392.92 / QM9414;
RX PubMed=7984103; DOI=10.1111/j.1365-2958.1994.tb00417.x;
RA Saloheimo A., Henrissat B., Hoffren A.-M., Teleman O., Penttilae M.;
RT "A novel, small endoglucanase gene, egl5, from Trichoderma reesei isolated
RT by expression in yeast.";
RL Mol. Microbiol. 13:219-228(1994).
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000305}.
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DR EMBL; Z33381; CAA83846.1; -; Genomic_DNA.
DR PIR; S60143; S60143.
DR AlphaFoldDB; P43317; -.
DR SMR; P43317; -.
DR CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR CAZy; GH45; Glycoside Hydrolase Family 45.
DR CLAE; EGL45E_TRIRE; -.
DR VEuPathDB; FungiDB:TrQ_008031; -.
DR OMA; YNGNQQW; -.
DR BioCyc; MetaCyc:MON-16505; -.
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; -; 1.
DR InterPro; IPR035971; CBD_sf.
DR InterPro; IPR000254; Cellulose-bd_dom_fun.
DR InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR InterPro; IPR000334; Glyco_hydro_45.
DR InterPro; IPR009009; RlpA-like_DPBB.
DR InterPro; IPR036908; RlpA-like_sf.
DR Pfam; PF00734; CBM_1; 1.
DR Pfam; PF03330; DPBB_1; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR SUPFAM; SSF57180; SSF57180; 1.
DR PROSITE; PS00562; CBM1_1; 1.
DR PROSITE; PS51164; CBM1_2; 1.
DR PROSITE; PS50842; EXPANSIN_EG45; 1.
DR PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT SIGNAL 1..17
FT /evidence="ECO:0000255"
FT CHAIN 18..242
FT /note="Endoglucanase-5"
FT /id="PRO_0000008022"
FT DOMAIN 205..241
FT /note="CBM1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT REGION 18..182
FT /note="Catalytic"
FT REGION 177..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 27
FT /note="Nucleophile"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10069"
FT ACT_SITE 134
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT CARBOHYD 182
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 213..230
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
FT DISULFID 224..240
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00079"
SQ SEQUENCE 242 AA; 24411 MW; CC033FC51326C71D CRC64;
MKATLVLGSL IVGAVSAYKA TTTRYYDGQE GACGCGSSSG AFPWQLGIGN GVYTAAGSQA
LFDTAGASWC GAGCGKCYQL TSTGQAPCSS CGTGGAAGQS IIVMVTNLCP NNGNAQWCPV
VGGTNQYGYS YHFDIMAQNE IFGDNVVVDF EPIACPGQAA SDWGTCLCVG QQETDPTPVL
GNDTGSTPPG SSPPATSSSP PSGGGQQTLY GQCGGAGWTG PTTCQAPGTC KVQNQWYSQC
LP
