ID   GUX1_HYPRU              Reviewed;         514 AA.
AC   P19355; O93832;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 2.
DT   02-SEP-2026, entry version 114.
DE   RecName: Full=Exoglucanase 1;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase;
DE   AltName: Full=Exocellobiohydrolase;
DE   AltName: Full=Exoglucanase I;
DE   Flags: Precursor;
GN   Name=cbh1;
OS   Hypocrea rufa (Trichoderma viride).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX   NCBI_TaxID=5547;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2216737; DOI=10.1093/nar/18.18.5559;
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 generally
CC       requires three types of hydrolytic enzymes: (1) Endoglucanases which
CC       cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that
CC       cut the disaccharide cellobiose from the non-reducing end of the
CC       cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the
CC       cellobiose and other short cello-oligosaccharides to glucose.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose
CC         and cellotetraose, releasing cellobiose from the non-reducing ends of
CC         the chains.; EC=3.2.1.91;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; X53931; CAA37878.1; -; Genomic_DNA.
DR   EMBL; AB021656; BAA36215.1; -; Genomic_DNA.
DR   PIR; S11439; S11439.
DR   AlphaFoldDB; P19355; -.
DR   SMR; P19355; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   GlyCosmos; P19355; 3 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0009251; P:glucan catabolic process; IEA:UniProtKB-ARBA.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   FunFam; 2.70.100.10:FF:000001; Glucanase; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR000254; CBD.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR001722; Glyco_hydro_7.
DR   InterPro; IPR037019; Glyco_hydro_7_sf.
DR   PANTHER; PTHR33753; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 1.
DR   PANTHER; PTHR33753:SF2; GLYCOSIDE HYDROLASE FAMILY 7 PROTEIN; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00840; Glyco_hydro_7; 1.
DR   PRINTS; PR00734; GLHYDRLASE7.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Signal.
FT   SIGNAL          1..17
FT   CHAIN           18..514
FT                   /note="Exoglucanase 1"
FT                   /id="PRO_0000007928"
FT   DOMAIN          478..514
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          18..453
FT                   /note="Catalytic"
FT   REGION          401..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          444..481
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..478
FT                   /note="Linker"
FT   COMPBIAS        460..479
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        229
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        234
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        62
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        81
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        21..89
FT                   /evidence="ECO:0000250"
FT   DISULFID        36..42
FT                   /evidence="ECO:0000250"
FT   DISULFID        67..88
FT                   /evidence="ECO:0000250"
FT   DISULFID        78..84
FT                   /evidence="ECO:0000250"
FT   DISULFID        155..414
FT                   /evidence="ECO:0000250"
FT   DISULFID        189..227
FT                   /evidence="ECO:0000250"
FT   DISULFID        193..226
FT                   /evidence="ECO:0000250"
FT   DISULFID        247..273
FT                   /evidence="ECO:0000250"
FT   DISULFID        255..260
FT                   /evidence="ECO:0000250"
FT   DISULFID        278..348
FT                   /evidence="ECO:0000250"
FT   DISULFID        486..503
FT                   /evidence="ECO:0000250"
FT   DISULFID        497..513
FT                   /evidence="ECO:0000250"
FT   CONFLICT        173
FT                   /note="S -> T (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        256
FT                   /note="D -> E (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        401
FT                   /note="N -> D (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        414
FT                   /note="C -> S (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        449
FT                   /note="S -> P (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        462
FT                   /note="Missing (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        466
FT                   /note="R -> P (in Ref. 1)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        492
FT                   /note="S -> I (in Ref. 1; CAA37878)"
FT                   /evidence="ECO:0000305"
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
//