ID   GUNB_FUSOX              Reviewed;         462 AA.
AC   P46236;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   02-SEP-2026, entry version 102.
DE   RecName: Full=Putative endoglucanase type B;
DE            EC=3.2.1.4;
DE   AltName: Full=Cellulase;
DE   AltName: Full=Endo-1,4-beta-glucanase;
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=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family.
CC       {ECO:0000305}.
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DR   EMBL; L29377; AAA65585.1; -; mRNA.
DR   AlphaFoldDB; P46236; -.
DR   SMR; P46236; -.
DR   VEuPathDB; FungiDB:FOC1_g10002687; -.
DR   VEuPathDB; FungiDB:FOC4_g10009603; -.
DR   VEuPathDB; FungiDB:FOIG_13447; -.
DR   VEuPathDB; FungiDB:FOMG_14546; -.
DR   VEuPathDB; FungiDB:FOXG_09643; -.
DR   VEuPathDB; FungiDB:FOZG_13867; -.
DR   VEuPathDB; FungiDB:HZS61_005819; -.
DR   GO; GO:0005576; C:extracellular region; IEA:InterPro.
DR   GO; GO:0008810; F:cellulase activity; IEA:UniProtKB-EC.
DR   GO; GO:0030248; F:cellulose binding; IEA:InterPro.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:InterPro.
DR   FunFam; 3.20.20.40:FF:000001; Glucanase; 1.
DR   Gene3D; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1.
DR   InterPro; IPR016288; Beta_cellobiohydrolase.
DR   InterPro; IPR036434; Beta_cellobiohydrolase_sf.
DR   InterPro; IPR000254; CBD.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR001524; Glyco_hydro_6_CS.
DR   PANTHER; PTHR34876; -; 1.
DR   PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF01341; Glyco_hydro_6; 1.
DR   PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1.
DR   PRINTS; PR00733; GLHYDRLASE6.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1.
DR   PROSITE; PS00656; GLYCOSYL_HYDROL_F6_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..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..462
FT                   /note="Putative endoglucanase type B"
FT                   /id="PRO_0000007910"
FT   DOMAIN          25..61
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          64..102
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          66..99
FT                   /note="Linker"
FT   REGION          100..462
FT                   /note="Catalytic"
FT   COMPBIAS        64..100
FT                   /note="Low complexity"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        190
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   ACT_SITE        236
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        416
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   CARBOHYD        37
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        223
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        272
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   CARBOHYD        317
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        33..50
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..60
FT                   /evidence="ECO:0000250"
FT   DISULFID        191..250
FT                   /evidence="ECO:0000250"
FT   DISULFID        383..430
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   462 AA;  49208 MW;  E25B2F5B828B637F CRC64;
     MAYKLILAAF AATALAAPVE ERQSCSNGVW AQCGGQNWSG TPCCTSGNKC VKLNDFYSQC
     QPGSAEPSST AAGPSSTTAT KTTATGGSST TAGGSVTSAP PAASDNPYAG VDLWANNYYR
     SEVMNLAVPK LSGAKATAAA KVADVPSFQW MDTYDHISLM EDTLADIRKA NKAGGKYAGQ
     FVVYDLPNRD CAAAASNGEY SLDKDGANKY KAYIAKIKGI LQNYSDTKVI LVIEPDSLAN
     LVTNLNVDKC AKAESAYKEL TVYAIKELNL PNVSMYLDAG HGGWLGWPAN IGPAAKLYAQ
     IYKDAGKPSR VRGLVTNVSN YNGWKLSTKP DYTESNPNYD EQRYINAFAP LLAQEGWSNV
     KFIVDQGRSG KQPTGQKAQG DWCNAKGTGF GLRPSTNTGD ALADAFVWVK PGGESDGTSD
     TSAARYDYHC GLDDALKPAP EAGTWFQAYF EQLLDNANPS FL
//