ID   GUNF_FUSOX              Reviewed;         385 AA.
AC   P46239;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Putative endoglucanase type F;
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 10 (cellulase F) family.
CC       {ECO:0000305}.
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DR   EMBL; L29380; AAA65588.1; -; mRNA.
DR   AlphaFoldDB; P46239; -.
DR   SMR; P46239; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH10; Glycoside Hydrolase Family 10.
DR   VEuPathDB; FungiDB:FOC1_g10005625; -.
DR   VEuPathDB; FungiDB:FOC4_g10005497; -.
DR   VEuPathDB; FungiDB:FOIG_11547; -.
DR   VEuPathDB; FungiDB:FOMG_09444; -.
DR   VEuPathDB; FungiDB:FOXG_13415; -.
DR   VEuPathDB; FungiDB:FOZG_15322; -.
DR   VEuPathDB; FungiDB:HZS61_010952; -.
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:0031176; F:endo-1,4-beta-xylanase activity; IEA:UniProt.
DR   GO; GO:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR044846; GH10.
DR   InterPro; IPR031158; GH10_AS.
DR   InterPro; IPR001000; GH10_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31490; PTHR31490; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF00331; Glyco_hydro_10; 1.
DR   PRINTS; PR00134; GLHYDRLASE10.
DR   SMART; SM00236; fCBD; 1.
DR   SMART; SM00633; Glyco_10; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
DR   SUPFAM; SSF57180; SSF57180; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS00591; GH10_1; 1.
DR   PROSITE; PS51760; GH10_2; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..385
FT                   /note="Putative endoglucanase type F"
FT                   /id="PRO_0000007961"
FT   DOMAIN          23..53
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   DOMAIN          105..384
FT                   /note="GH10"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01096"
FT   REGION          53..84
FT                   /note="Linker"
FT   REGION          56..84
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        57..80
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        210
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        321
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10061"
SQ   SEQUENCE   385 AA;  41225 MW;  B3C3807C07D3C0EC CRC64;
     MHTLSVLLAL APVSALAQAP IWGQCGGNGW TGATTCASGL KCEKINDWYY QCVPGSGGSE
     PQPSSTQGGG TPQPTGGNSG GTGLDAKFKA KGKQYFGTEI DHYHLNNNPL INIVKAQFGQ
     VTCENSMKWD AIEPSRNSFT FSNADKVVDF ATQNGKLIRG HTLLWHSQLP QWVQNINDRS
     TLTAVIENHV KTMVTRYKGK ILQWDVVNNE IFAEDGNLRD SVFSRVLGED FVGIAFRAAR
     AADPAAKLYI NDYNLDKSDY AKVTRGMVAH VNKWIAAGIP IDGIGSQGHL AAPSGWNPAS
     GVPAALRALA ASDAKEIAIT ELDIAGASAN DYLTVMNACL AVPKCVGITV WGVSDKDSWR
     PGDNPLLYDS NYQPKAAFNA LANAL