ID   GUXC_FUSOX              Reviewed;         514 AA.
AC   P46238;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=Putative exoglucanase type C;
DE            EC=3.2.1.91;
DE   AltName: Full=1,4-beta-cellobiohydrolase;
DE   AltName: Full=Beta-glucancellobiohydrolase;
DE   AltName: Full=Exocellobiohydrolase I;
DE   Flags: Precursor;
OS   Fusarium oxysporum (Fusarium vascular wilt).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=5507;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RX   PubMed=7959045; DOI=10.1016/0378-1119(94)90878-8;
RA   Sheppard P.O., Grant F.J., Oort P.J., Sprecher C.A., Foster D.C.,
RA   Hagen F.S., Upshall A., McKnight G.L., O'Hara P.J.;
RT   "The use of conserved cellulase family-specific sequences to clone
RT   cellulase homologue cDNAs from Fusarium oxysporum.";
RL   Gene 150:163-167(1994).
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; L29379; AAA65587.1; -; mRNA.
DR   AlphaFoldDB; P46238; -.
DR   SMR; P46238; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH7; Glycoside Hydrolase Family 7.
DR   VEuPathDB; FungiDB:FOC1_g10015774; -.
DR   VEuPathDB; FungiDB:FOC4_g10015049; -.
DR   VEuPathDB; FungiDB:FOIG_00987; -.
DR   VEuPathDB; FungiDB:FOMG_01181; -.
DR   VEuPathDB; FungiDB:FOXG_00480; -.
DR   VEuPathDB; FungiDB:FOZG_01175; -.
DR   VEuPathDB; FungiDB:HZS61_000873; -.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   CDD; cd07999; GH7_CBH_EG; 1.
DR   Gene3D; 2.70.100.10; -; 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; PTHR33753; 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; SSF49899; SSF49899; 1.
DR   SUPFAM; SSF57180; SSF57180; 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; Signal.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000255"
FT   CHAIN           18..514
FT                   /note="Putative exoglucanase type C"
FT                   /id="PRO_0000007913"
FT   DOMAIN          478..514
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          18..439
FT                   /note="Catalytic"
FT   REGION          408..433
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          440..482
FT                   /note="Linker"
FT   REGION          448..485
FT                   /note="Disordered"
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        287
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        490
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        486..503
FT                   /evidence="ECO:0000250"
FT   DISULFID        497..513
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   514 AA;  54704 MW;  6A4617323A46E062 CRC64;
     MYRIVATASA LIAAARAQQV CSLNTETKPA LTWSKCTSSG CSDVKGSVVI DANWRWTHQT
     SGSTNCYTGN KWDTSICTDG KTCAEKCCLD GADYSGTYGI TSSGNQLSLG FVTNGPYSKN
     IGSRTYLMEN ENTYQMFQLL GNEFTFDVDV SGIGCGLNGA PHFVSMDEDG GKAKYSGNKA
     GAKYGTGYCD AQCPRDVKFI NGVANSEGWK PSDSDVNAGV GNLGTCCPEM DIWEANSIST
     AFTPHPCTKL TQHSCTGDSC GGTYSSDRYG GTCDADGCDF NAYRQGNKTF YGPGSNFNID
     TTKKMTVVTQ FHKGSNGRLS EITRLYVQNG KVIANSESKI AGNPGSSLTS DFCSKQKSVF
     GDIDDFSKKG GWNGMSDALS APMVLVMSLW HDHHSNMLWL DSTYPTDSTK VGSQRGSCAT
     TSGKPSDLER DVPNSKVSFS NIKFGPIGST YKSDGTTPNP PASSSTTGSS TPTNPPAGSV
     DQWGQCGGQN YSGPTTCKSP FTCKKINDFY SQCQ