ID   GUN2_TRIRE              Reviewed;         418 AA.
AC   P07982;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   16-JUN-2009, entry version 76.
DE   RecName: Full=Endoglucanase EG-II;
DE            Short=EGLII;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta-glucanase;
DE   AltName: Full=Cellulase;
DE   Flags: Precursor;
GN   Name=egl2;
OS   Trichoderma reesei (Hypocrea jecorina).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
OC   Sordariomycetes; Hypocreomycetidae; Hypocreales; Hypocreaceae;
OC   Hypocrea.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 22-58, AND
RP   PYROGLUTAMATE FORMATION AT GLN-22.
RC   STRAIN=VTT-D-80133;
RX   MEDLINE=88255850; PubMed=3384334; DOI=10.1016/0378-1119(88)90541-0;
RA   Saloheimo M., Lehtovaara P., Penttilae M., Teeri T.T., Staahlberg J.,
RA   Johansson G., Pettersson G., Clayssens M., Tomme P., Knowles J.K.C.;
RT   "EGIII, a new endoglucanase from Trichoderma reesei: the
RT   characterization of both gene and enzyme.";
RL   Gene 63:11-21(1988).
RN   [2]
RP   PROTEIN SEQUENCE OF 87-99.
RX   PubMed=3356188; DOI=10.1111/j.1432-1033.1988.tb13982.x;
RA   Stahlberg J., Johansson G., Pettersson G.;
RT   "A binding-site-deficient, catalytically active, core protein of
RT   endoglucanase III from the culture filtrate of Trichoderma reesei.";
RL   Eur. J. Biochem. 173:179-183(1988).
RN   [3]
RP   ACTIVE SITE GLU-350.
RX   MEDLINE=93131031; PubMed=8093602; DOI=10.1016/0014-5793(93)81202-B;
RA   Macarron R., van Beeumen J., Henrissat B., de la Mata I.,
RA   Claeyssens M.;
RT   "Identification of an essential glutamate residue in the active site
RT   of endoglucanase III from Trichoderma reesei.";
RL   FEBS Lett. 316:137-140(1993).
CC   -!- FUNCTION: The biological conversion of cellulose to glucose
CC       generally requires three types of hydrolytic enzymes: (1)
CC       Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2)
CC       Exocellobiohydrolases that cut the dissaccharide cellobiose from
CC       the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-
CC       glucosidases which hydrolyze the cellobiose and other short cello-
CC       oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding)
CC       domain.
CC   -!- CAUTION: Was originally called endoglucanase EG-III.
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DR   EMBL; M19373; AAA34213.1; -; Genomic_DNA.
DR   PIR; S28372; S28372.
DR   HSSP; P00725; 2CBH.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   BRENDA; 3.2.1.4; 280374.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR000254; CBD_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR013781; Glyco_hydro_sg_catalytic.
DR   Gene3D; G3DSA:3.20.20.80; Glyco_hydro_cat; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   ProDom; PD001821; CBD_fungal; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation;
KW   Direct protein sequencing; Disulfide bond; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Pyrrolidone carboxylic acid;
KW   Signal.
FT   SIGNAL        1     21
FT   CHAIN        22    418       Endoglucanase EG-II.
FT                                /FTId=PRO_0000007874.
FT   DOMAIN       22     57       CBM1.
FT   REGION       58     91       Linker.
FT   REGION       92    418       Catalytic.
FT   ACT_SITE    239    239       Proton donor (By similarity).
FT   ACT_SITE    350    350       Nucleophile.
FT   MOD_RES      22     22       Pyrrolidone carboxylic acid.
FT   CARBOHYD    124    124       N-linked (GlcNAc...) (Potential).
FT   DISULFID     29     46       By similarity.
FT   DISULFID     40     56       By similarity.
SQ   SEQUENCE   418 AA;  44227 MW;  26A492D55237A49B CRC64;
     MNKSVAPLLL AASILYGGAV AQQTVWGQCG GIGWSGPTNC APGSACSTLN PYYAQCIPGA
     TTITTSTRPP SGPTTTTRAT STSSSTPPTS SGVRFAGVNI AGFDFGCTTD GTCVTSKVYP
     PLKNFTGSNN YPDGIGQMQH FVNEDGMTIF RLPVGWQYLV NNNLGGNLDS TSISKYDQLV
     QGCLSLGAYC IVDIHNYARW NGGIIGQGGP TNAQFTSLWS QLASKYASQS RVWFGIMNEP
     HDVNINTWAA TVQEVVTAIR NAGATSQFIS LPGNDWQSAG AFISDGSAAA LSQVTNPDGS
     TTNLIFDVHK YLDSDNSGTH AECTTNNIDG AFSPLATWLR QNNRQAILTE TGGGNVQSCI
     QDMCQQIQYL NQNSDVYLGY VGWGAGSFDS TYVLTETPTS SGNSWTDTSL VSSCLARK
//