ID   GUX1_TRIVI     STANDARD;      PRT;   514 AA.
AC   P19355; O93832;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   21-MAR-2006, entry version 51.
DE   Exoglucanase 1 precursor (EC 3.2.1.91) (Exoglucanase I)
DE   (Exocellobiohydrolase) (1,4-beta-cellobiohydrolase).
GN   Name=cbh1;
OS   Trichoderma viride.
OC   Eukaryota; Fungi; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; mitosporic Hypocreales; Trichoderma;
OC   Tricoderma viride species complex.
OX   NCBI_TaxID=5547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=91016856; PubMed=2216737;
RA   Cheng C., Tsukagoshi N., Udaka S.;
RT   "Nucleotide sequence of the cellobiohydrolase gene from Trichoderma
RT   viride.";
RL   Nucleic Acids Res. 18:5559-5559(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=MC300-1;
RA   Watanabe M.;
RL   Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases.
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: 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 CBM1 (fungal-type carbohydrate-binding)
CC       domain.
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DR   EMBL; X53931; CAA37878.1; -; Genomic_DNA.
DR   EMBL; AB021656; BAA36215.1; -; Genomic_DNA.
DR   PIR; S11439; S11439.
DR   HSSP; P00725; 6CEL.
DR   SMR; P19355; 18-451.
DR   InterPro; IPR000254; CBD_fun.
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   PRINTS; PR00734; GLHYDRLASE7.
DR   ProDom; PD001821; CBD_fungal; 1.
DR   ProDom; PD186135; Glyco_hydro_7; 1.
DR   SMART; SM00236; fCBD; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein;
KW   Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL        1     17
FT   CHAIN        18    514       Exoglucanase 1.
FT                                /FTId=PRO_0000007928.
FT   DOMAIN      478    514       CBM1.
FT   REGION       18    453       Catalytic.
FT   REGION      454    478       Linker.
FT   ACT_SITE    229    229       Nucleophile (By similarity).
FT   ACT_SITE    234    234       Proton donor (By similarity).
FT   CARBOHYD     62     62       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD     81     81       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    287    287       N-linked (GlcNAc...) (Potential).
FT   DISULFID     21     89       By similarity.
FT   DISULFID     36     42       By similarity.
FT   DISULFID     67     88       By similarity.
FT   DISULFID     78     84       By similarity.
FT   DISULFID    155    414       By similarity.
FT   DISULFID    189    227       By similarity.
FT   DISULFID    193    226       By similarity.
FT   DISULFID    247    273       By similarity.
FT   DISULFID    255    260       By similarity.
FT   DISULFID    278    348       By similarity.
FT   DISULFID    486    503       By similarity.
FT   DISULFID    497    513       By similarity.
FT   CONFLICT    173    173       S -> T (in Ref. 1).
FT   CONFLICT    256    256       D -> E (in Ref. 1).
FT   CONFLICT    401    401       N -> D (in Ref. 1).
FT   CONFLICT    414    414       C -> S (in Ref. 1).
FT   CONFLICT    449    449       S -> P (in Ref. 1).
FT   CONFLICT    462    462       Missing (in Ref. 1).
FT   CONFLICT    466    466       R -> P (in Ref. 1).
FT   CONFLICT    492    492       S -> I (in Ref. 1).
SQ   SEQUENCE   514 AA;  54002 MW;  C5B1FB734C9CDAF5 CRC64;
     MYQKLALISA FLATARAQSA CTLQAETHPP LTWQKCSSGG TCTQQTGSVV IDANWRWTHA
     TNSSTNCYDG NTWSSTLCPD NETCAKNCCL DGAAYASTYG VTTSADSLSI GFVTQSAQKN
     VGARLYLMAS DTTYQEFTLL GNEFSFDVDV SQLPCGLNGA LYFVSMDADG GVSKYPTNTA
     GAKYGTGYCD SQCPRDLKFI NGQANVEGWE PSSNNANTGI GGHGSCCSEM DIWEANSISE
     ALTPHPCTTV GQEICDGDSC GGTYSGDRYG GTCDPDGCDW NPYRLGNTSF YGPGSSFTLD
     TTKKLTVVTQ FETSGAINRY YVQNGVTFQQ PNAELGDYSG NSLDDDYCAA EEAEFGGSSF
     SDKGGLTQFK KATSGGMVLV MSLWDDYYAN MLWLDSTYPT NETSSTPGAV RGSCSTSSGV
     PAQLESNSPN AKVVYSNIKF GPIGSTGNSS GGNPPGGNPP GTTTTRRPAT STGSSPGPTQ
     THYGQCGGIG YSGPTVCASG STCQVLNPYY SQCL
//