ID   GUN1_HYPRU              Reviewed;          15 AA.
AC   P85218;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   11-DEC-2019, entry version 22.
DE   RecName: Full=Endoglucanase 1;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta-D-glucanase 1;
DE   Flags: Fragment;
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1]
RP   PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RC   STRAIN=MTCC 167 {ECO:0000269|Ref.1};
RA   Chaudhary N., Sharma B.C.;
RT   "Purification, characterization and N-terminal sequence analysis of novel
RT   endo-beta-1,4-D-glucanase from Trichoderma viride.";
RL   Submitted (JUL-2007) to UniProtKB.
CC   -!- FUNCTION: Has endoglucanase activity on carboxymethylcellulose (CMC).
CC       {ECO:0000269|Ref.1}.
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:0000269|Ref.1};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 5.0. {ECO:0000269|Ref.1};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|Ref.1}.
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DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Direct protein sequencing;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Secreted.
FT   CHAIN           1..>15
FT                   /note="Endoglucanase 1"
FT                   /id="PRO_0000315940"
FT   NON_TER         15
FT                   /evidence="ECO:0000303|Ref.1"
SQ   SEQUENCE   15 AA;  1759 MW;  0ED77433D6F953B4 CRC64;
     SYPNKQPYGP SGFWM