ID   GUX1_PHACH     STANDARD;      PRT;   516 AA.
AC   P13860;
DT   01-JAN-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1990, sequence version 1.
DT   21-MAR-2006, entry version 57.
DE   Exoglucanase 1 precursor (EC 3.2.1.91) (Exoglucanase I)
DE   (Exocellobiohydrolase I) (1,4-beta-cellobiohydrolase).
GN   Name=CBH1;
OS   Phanerochaete chrysosporium (White-rot fungus).
OC   Eukaryota; Fungi; Basidiomycota; Hymenomycetes; Homobasidiomycetes;
OC   Aphyllophorales; Corticiaceae; Phanerochaete.
OX   NCBI_TaxID=5306;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 34541 / ME446;
RX   MEDLINE=89232732; PubMed=3246351; DOI=10.1016/0378-1119(88)90174-6;
RA   Sims P.F.G., James C., Broda P.;
RT   "The identification, molecular cloning and characterisation of a gene
RT   from Phanerochaete chrysosporium that shows strong homology to the
RT   exo-cellobiohydrolase I gene from Trichoderma reesei.";
RL   Gene 74:411-422(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=ATCC 34541 / ME446;
RX   MEDLINE=94335641; PubMed=8057846;
RA   Sims P.F.G., Soares-Felipe M.S., Wang Q., Gent M.E., Tempelaars C.,
RA   Broda P.;
RT   "Differential expression of multiple exo-cellobiohydrolase I-like
RT   genes in the lignin-degrading fungus Phanerochaete chrysosporium.";
RL   Mol. Microbiol. 12:209-216(1994).
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   -!- SUBCELLULAR LOCATION: Secreted protein.
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; M22220; AAB46373.1; -; Genomic_DNA.
DR   EMBL; Z22528; CAA80253.1; -; mRNA.
DR   PIR; JS0083; JS0083.
DR   HSSP; Q09431; 1GPI.
DR   SMR; P13860; 19-448.
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     18       Potential.
FT   CHAIN        19    516       Exoglucanase 1.
FT                                /FTId=PRO_0000007924.
FT   DOMAIN      480    516       CBM1.
FT   REGION        ?    449       Catalytic.
FT   REGION      450    480       Linker.
FT   ACT_SITE    225    225       Nucleophile (By similarity).
FT   ACT_SITE    230    230       Proton donor (By similarity).
FT   CARBOHYD    208    208       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    326    326       N-linked (GlcNAc...) (Potential).
FT   CARBOHYD    442    442       N-linked (GlcNAc...) (Potential).
FT   DISULFID    488    505       By similarity.
FT   DISULFID    499    515       By similarity.
FT   CONFLICT     27     28       RS -> EN (in Ref. 1).
FT   CONFLICT     30     31       PA -> RT (in Ref. 1).
SQ   SEQUENCE   516 AA;  54858 MW;  1C7C3D338ECE1B72 CRC64;
     MFRTATLLAF TMAAMVFGQQ VGTNTARSHP ALTSQKCTKS GGCSNLNTKI VLDANWRWLH
     STSGYTNCYT GNQWDATLCP DGKTCAANCA LDGADYTGTY GITASGSSLK LQFVTGSNVG
     SRVYLMADDT HYQMFQLLNQ EFTFDVDMSN LPCGLNGALY LSAMDADGGM AKYPTNKAGA
     KYGTGYCDSQ CPRDIKFING EANVEGWNAT SANAGTGNYG TCCTEMDIWE ANNDAAAYTP
     HPCTTNAQTR CSGSDCTRDT GLCDADGCDF NSFRMGDQTF LGKGLTVDTS KPFTVVTQFI
     TNDGTSAGTL TEIRRLYVQN GKVIQNSSVK IPGIDPVNSI TDNFCSQQKT AFGDTNYFAQ
     HGGLKQVGEA LRTGMVLALS IWDDYAANML WLDSNYPTNK DPSTPGVARG TCATTSGVPA
     QIEAQSPNAY VVFSNIKFGD LNTTYTGTVS SSSVSSSHSS TSTSSSHSSS STPPTQPTGV
     TVPQWGQCGG IGYTGSTTCA SPYTCHVLNP YYSQCY
//