ID   GUX2_AGABI     STANDARD;      PRT;   506 AA.
AC   Q92400;
DT   15-DEC-1998 (Rel. 37, Created)
DT   15-DEC-1998 (Rel. 37, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Exoglucanase precursor (EC 3.2.1.91) (Exocellobiohydrolase) (1,4-beta-
DE   cellobiohydrolase) (Beta-glucancellobiohydrolase).
GN   Name=cel2;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=D649;
RX   MEDLINE=97177791; PubMed=9025297;
RA   Yague E., Mehak-Zunic M., Morgan L., Wood D.A., Thurston C.F.;
RT   "Expression of CEL2 and CEL4, two proteins from Agaricus bisporus with
RT   similarity to fungal cellobiohydrolase I and beta-mannanase,
RT   respectively, is regulated by the carbon source.";
RL   Microbiology 143:239-244(1997).
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) Beta-1,4-
CC       glucosidases which hydrolyze the cellobiose and other short cello-
CC       oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of 1,4-beta-D-glucosidic linkages
CC       in cellulose and cellotetraose, releasing cellobiose from the non-
CC       reducing ends of the chains.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C)
CC       family.
CC   -!- SIMILARITY: Contains 1 fungal-type cellulose-binding (CBD) domain.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; Z50094; CAA90422.1; -.
DR   HSSP; Q09431; 1GPI.
DR   InterPro; IPR000254; CBD_fungal.
DR   InterPro; IPR008985; ConA_like_lec_gl.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   ProDom; PD001821; CBD_fungal; 1.
DR   ProDom; PD186135; Glyco_hydro_7; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBD_FUNGAL; 1.
KW   Cellulose degradation; Glycoprotein; Glycosidase; Hydrolase; Signal.
FT   SIGNAL        1     18       Potential.
FT   CHAIN        19    506       Exoglucanase.
FT   DOMAIN       19    450       Catalytic.
FT   DOMAIN      451    473       Linker.
FT   DOMAIN      474    506       Cellulose-binding (By similarity).
FT   ACT_SITE    227    227       Nucleophile (By similarity).
FT   ACT_SITE    232    232       Proton donor (By similarity).
FT   DISULFID    478    495       By similarity.
FT   DISULFID    489    505       By similarity.
FT   CARBOHYD    308    308       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    447    447       N-linked (GlcNAc...) (Potential).
SQ   SEQUENCE   506 AA;  54320 MW;  0D0390CA4E71BC55 CRC64;
     MFPRSILLAL SLTAVALGQQ VGTNMAENHP SLTWQRCTSS GCQNVNGKVT LDANWRWTHR
     INDFTNCYTG NEWDTSICPD GVTCAENCAL DGADYAGTYG VTSSGTALTL KFVTESQQKN
     IGSRLYLMAD DSNYEIFNLL NKEFTFDVDV SKLPCGLNGA LYFSEMAADG GMSSTNTAGA
     KYGTGYCDSQ CPRDIKFIDG EANSEGWEGS PNDVNAGTGN FGACCGEMDI WEANSISSAY
     TPHPCREPGL QRCEGNTCSV NDRYATECDP DGCDFNSFRM GDKSFYGPGM TVDTNQPITV
     VTQFITDNGS DNGNLQEIRR IYVQNGQVIQ NSNVNIPGID SGNSISAEFC DQAKEAFGDE
     RSFQDRGGLS GMGSALDRGM VLVLSIWDDH AVNMLWLDSD YPLDASPSQP GISRGTCSRD
     SGKPEDVEAN AGGVQVVYSN IKFGDINSTF NNNGGGGGNP SPTTTRPNSP AQTMWGQCGG
     QGWTGPTACQ SPSTCHVIND FYSQCF
//