ID   GUN5_TRIRF              Reviewed;         242 AA.
AC   P43317;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 112.
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   Trichoderma reesei (Filamentous fungus) (Hypocrea jecorina).
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   GlyCosmos; P43317; 1 site, No reported glycans.
DR   VEuPathDB; FungiDB:TrQ_008031; -.
DR   OMA; MAQNEIF; -.
DR   BioCyc; MetaCyc:MONOMER-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:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR000254; CBD.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR007112; Expansin/allergen_DPBB_dom.
DR   InterPro; IPR000334; Glyco_hydro_45.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF22514; EXPB1_D1; 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; 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   COMPBIAS        184..201
FT                   /note="Low complexity"
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
//