ID   GUX1_PENJA              Reviewed;         537 AA.
AC   Q06886;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   22-FEB-2023, entry version 100.
DE   RecName: Full=Exoglucanase 1;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase;
DE   AltName: Full=Exocellobiohydrolase I;
DE   AltName: Full=Exoglucanase I;
DE   Flags: Precursor;
GN   Name=cbh1;
OS   Penicillium janthinellum (Penicillium vitale).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX   NCBI_TaxID=5079;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   STRAIN=C41;
RX   PubMed=8440481; DOI=10.1016/0378-1119(93)90761-q;
RA   Koch A., Weigel C.T.O., Schulz G.;
RT   "Cloning, sequencing, and heterologous expression of a cellulase-encoding
RT   cDNA (cbh1) from Penicillium janthinellum.";
RL   Gene 124:57-65(1993).
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   -!- SUBCELLULAR LOCATION: Secreted.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 7 (cellulase C) family.
CC       {ECO:0000305}.
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DR   EMBL; X59054; CAA41780.1; -; mRNA.
DR   PIR; JU0150; JU0150.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   CLAE; CBH7A_PENJA; -.
DR   GlyCosmos; Q06886; 3 sites, No reported glycans.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; Glycoside hydrolase, family 7, domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
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; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE B; 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   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Disulfide bond;
KW   Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..537
FT                   /note="Exoglucanase 1"
FT                   /id="PRO_0000007923"
FT   DOMAIN          501..537
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          19..453
FT                   /note="Catalytic"
FT   REGION          454..477
FT                   /note="Linker"
FT   REGION          458..508
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        458..505
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        235
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        240
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   CARBOHYD        136
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        414
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        456
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        509..526
FT                   /evidence="ECO:0000250"
FT   DISULFID        520..536
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   537 AA;  56845 MW;  A6B9C6EB73F17FE4 CRC64;
     MKGSISYQIY KGALLLSALL NSVSAQQVGT LTAETHPALT WSKCTAGXCS QVSGSVVIDA
     NWPXVHSTSG STNCYTGNTW DATLCPDDVT CAANCAVDGA RRQHLRVTTS GNSLRINFVT
     TASQKNIGSR LYLLENDTTY QKFNLLNQEF TFDVDVSNLP CGLNGALYFV DMDADGGMAK
     YPTNKAGAKY GTGYCDSQCP RDLKFINGQA NVDGWTPSKN DVNSGIGNHG SCCAEMDIWE
     ANSISNAVTP HPCDTPSQTM CTGQRCGGTY STDRYGGTCD PDGCDFNPYR MGVTNFYGPG
     ETIDTKSPFT VVTQFLTNDG TSTGTLSEIK RFYVQGGKVI GNPQSTIVGV SGNSITDSWC
     NAQKSAFGDT NEFSKHGGMA GMGAGLADGM VLVMSLWDDH ASDMLWLDST YPTNATSTTP
     GAKRGTCDIS RRPNTVESTY PNAYVIYSNI KTGPLNSTFT GGTTSSSSTT TTTSKSTSTS
     SSSKTTTTVT TTTTSSGSSG TGARDWAQCG GNGWTGPTTC VSPYTCTKQN DWYSQCL
//