ID   GUN3_HUMIN              Reviewed;         388 AA.
AC   Q12624; Q12620;
DT   04-MAY-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   16-JUN-2009, entry version 59.
DE   RecName: Full=Endoglucanase 3;
DE            EC=3.2.1.4;
DE   AltName: Full=Endo-1,4-beta-glucanase 3;
DE   AltName: Full=Cellulase 3;
DE   Flags: Precursor;
GN   Name=CMC3;
OS   Humicola insolens.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; mitosporic Ascomycota;
OC   Humicola.
OX   NCBI_TaxID=34413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=94247364; PubMed=8190078; DOI=10.1007/BF00301060;
RA   Dalboege H., Hansen H.P.H.;
RT   "A novel method for efficient expression cloning of fungal enzyme
RT   genes.";
RL   Mol. Gen. Genet. 243:253-260(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC   STRAIN=IFO 9854;
RX   PubMed=9058960;
RA   Takashima S., Nakamura A., Masaki H., Uozumi T.;
RT   "Cloning, sequencing, and expression of a thermostable cellulase gene
RT   of Humicola grisea.";
RL   Biosci. Biotechnol. Biochem. 61:245-250(1997).
CC   -!- CATALYTIC ACTIVITY: Endohydrolysis of (1->4)-beta-D-glucosidic
CC       linkages in cellulose, lichenin and cereal beta-D-glucans.
CC   -!- BIOTECHNOLOGY: Used as a detergent cellulase. Sold under the name
CC       Celluzyme by Novozymes. This special enzyme has three effects:
CC       colour brightening, softening and removal of particulate soil. The
CC       overall effect is that it helps to preserve the nice appearance of
CC       new fabric and restores old fabric so that it looks new again.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A)
CC       family.
CC   -!- SIMILARITY: Contains 1 CBM1 (fungal-type carbohydrate-binding)
CC       domain.
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DR   EMBL; X76046; CAA53631.1; -; Genomic_DNA.
DR   EMBL; D84470; BAA12676.1; -; Genomic_DNA.
DR   PIR; JC5461; JC5461.
DR   PIR; S43920; S43920.
DR   HSSP; P00725; 1AZ6.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH5; Glycoside Hydrolase Family 5.
DR   BRENDA; 3.2.1.4; 1892.
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; FALSE_NEG.
PE   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation;
KW   Signal.
FT   SIGNAL        1     16       Potential.
FT   CHAIN        17    388       Endoglucanase 3.
FT                                /FTId=PRO_0000007863.
FT   DOMAIN       17     52       CBM1.
FT   REGION       53     91       Linker.
FT   REGION       92    388       Catalytic.
FT   ACT_SITE    215    215       Proton donor (By similarity).
FT   ACT_SITE    322    322       Nucleophile (By similarity).
FT   CARBOHYD     92     92       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    155    155       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    259    259       N-linked (GlcNAc...) (Potential).
FT   DISULFID     24     41       By similarity.
FT   DISULFID     35     51       By similarity.
FT   CONFLICT      8      8       G -> S (in Ref. 2; BAA12676).
FT   CONFLICT    340    340       T -> N (in Ref. 2; BAA12676).
SQ   SEQUENCE   388 AA;  42564 MW;  C7CF349DACC10690 CRC64;
     MKHSVLAGLF ATGALAQGGA WQQCGGVGFS GSTSCVSGYT CVYLNDWYSQ CQPQPTTLRT
     TTTPGATSTT RSAPAATSTT PAKGKFKWFG INQSCAEFGK GEYPGLWGKH FTFPSTSSIQ
     THINDGFNMF RVAFSMERLA PNQLNAAFDA NYLRNLTETV NFITGKGKYA MLDPHNFGRY
     YERIITDKAA FASFFTKLAT HFASNPLVVF DTNNEYHDMD QQLVFDLNQA AIDAIRAAGA
     TSQYIMVEGN SWTGAWTWNV TNNNLAALRD PENKLVYQMH QYLDSDGSGT STACVSTQVG
     LQRVIGATNW LRQNGKVGLL GEFAGGANSV CQQAIEGMLT HLQENSDVWT GALWWAGGPW
     WGDYIYSFEP PSGIGYTYYN SLLKKYVP
//