ID   GUN2_TRIRE     STANDARD;      PRT;   418 AA.
AC   P07982;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1988, sequence version 1.
DT   07-FEB-2006, entry version 58.
DE   Endoglucanase EG-II precursor (EC 3.2.1.4) (Endo-1,4-beta-glucanase)
DE   (Cellulase) (EGLII).
GN   Name=egl2;
OS   Trichoderma reesei (Hypocrea jecorina).
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Hypocrea.
OX   NCBI_TaxID=51453;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
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   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 nonreducing end of the cellulose polymer chain; (3)
CC       Beta-1,4-glucosidases which hydrolyze the cellobiose and other
CC       short cello-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   InterPro; IPR000254; CBD_fun.
DR   InterPro; IPR001547; Glyco_hydro_5.
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.
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Pyrrolidone carboxylic acid; 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
//