ID   GUX3_AGABI     STANDARD;      PRT;   438 AA.
AC   P49075;
DT   01-FEB-1996 (Rel. 33, Created)
DT   01-FEB-1996 (Rel. 33, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Exoglucanase 3 precursor (EC 3.2.1.91) (Exocellobiohydrolase 3) (1,4-
DE   beta-cellobiohydrolase 3).
GN   Name=cel3;
OS   Agaricus bisporus (Common mushroom).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Agaricales; Agaricaceae; Agaricus.
OX   NCBI_TaxID=5341;
RN   [1]
RP   NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 255-277 AND 331-351.
RC   STRAIN=D649;
RX   MEDLINE=94368092; PubMed=8085821;
RA   Chow C.-M., Yague E., Raguz S., Wood D.A., Thurston C.F.;
RT   "The cel3 gene of Agaricus bisporus codes for a modular cellulase and
RT   is transcriptionally regulated by the carbon source.";
RL   Appl. Environ. Microbiol. 60:2779-2785(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Mycelium;
RX   MEDLINE=96269930; PubMed=8662210;
RA   Yague E., Chow C.-M., Challen M.P., Thurston C.F.;
RT   "Correlation of exons with functional domains and folding regions in a
RT   cellulase from Agaricus bisporus.";
RL   Curr. Genet. 30:56-61(1996).
CC   -!- FUNCTION: Shows enzymatic activity towards crystalline cellulose.
CC       At long reaction times. It is also able to degrade carboxymethyl
CC       cellulose and barley B-glucan.
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 6 (cellulase B)
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; L24519; AAA50607.1; -.
DR   EMBL; L24520; AAA50608.1; -.
DR   EMBL; Z34007; CAA83971.1; -.
DR   PIR; S70602; S70602.
DR   HSSP; P00725; 1AZ6.
DR   InterPro; IPR000254; CBD_fungal.
DR   InterPro; IPR001524; Glyco_hydro_6.
DR   InterPro; IPR011253; Glyco_hydro_6-lk.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   ProDom; PD001821; CBD_fungal; 1.
DR   ProDom; PD003733; Glyco_hydro_6; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBD_FUNGAL; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1.
KW   Cellulose degradation; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Signal.
FT   SIGNAL        1     20       Potential.
FT   CHAIN        21    438       Exoglucanase 3.
FT   DOMAIN       21     59       Cellulose-binding (By similarity).
FT   DOMAIN       60     87       Linker.
FT   DOMAIN       88    438       Catalytic.
FT   ACT_SITE    215    215       Proton donor (By similarity).
FT   ACT_SITE    393    393       Nucleophile (By similarity).
FT   DISULFID     28     45       By similarity.
FT   DISULFID     39     55       By similarity.
FT   DISULFID    170    229       By similarity.
FT   DISULFID    360    407       By similarity.
FT   VARIANT     133    133       V -> T.
FT   VARIANT     152    152       R -> Q.
FT   VARIANT     244    244       V -> I.
FT   VARIANT     248    248       N -> D.
FT   VARIANT     398    398       N -> S.
SQ   SEQUENCE   438 AA;  46210 MW;  002C973544893794 CRC64;
     MFKFAALLAL ASLVPGFVQA QSPVWGQCGG NGWTGPTTCA SGSTCVKQND FYSQCLPNNQ
     APPSTTTQPG TTPPATTTSG GTGPTSGAGN PYTGKTVWLS PFYADEVAQA AADISNPSLA
     TKAASVAKIP TFVWFDTVAK VPDLGGYLAD ARSKNQLVQI VVYDLPDRDC AALASNGEFS
     LANDGLNKYK NYVDQIAAQI KQFPDVSVVA VIEPDSLANL VTNLNVQKCA NAQSAYKEGV
     IYAVQKLNAV GVTMYIDAGH AGWLGWPANL SPAAQLFAQI YRDAGSPRNL RGIATNVANF
     NALRASSPDP ITQGNSNYDE IHYIEALAPM LSNAGFPAHF IVDQGRSGVQ NIRDQWGDWC
     NVKGAGFGQR PTTNTGSSLI DAIVWVKPGG ECDGTSDNSS PRFDSHCSLS DAHQPAPEAG
     TWFQAYFETL VANANPAL
//