ID   GUNK_FUSOX              Reviewed;         376 AA.
AC   P45699;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-MAY-2023, entry version 91.
DE   RecName: Full=Putative endoglucanase type K;
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 45 (cellulase K) family.
CC       {ECO:0000305}.
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DR   EMBL; L29381; AAA65589.1; -; mRNA.
DR   AlphaFoldDB; P45699; -.
DR   SMR; P45699; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH45; Glycoside Hydrolase Family 45.
DR   VEuPathDB; FungiDB:FOC1_g10009944; -.
DR   VEuPathDB; FungiDB:FOC4_g10009030; -.
DR   VEuPathDB; FungiDB:FOIG_08964; -.
DR   VEuPathDB; FungiDB:FOMG_07426; -.
DR   VEuPathDB; FungiDB:FOXG_10638; -.
DR   VEuPathDB; FungiDB:FOZG_10130; -.
DR   VEuPathDB; FungiDB:HZS61_008825; -.
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:UniProtKB-KW.
DR   CDD; cd22278; DPBB_GH45_endoglucanase; 1.
DR   Gene3D; 2.40.40.10; RlpA-like domain; 1.
DR   InterPro; IPR035971; CBD_sf.
DR   InterPro; IPR000254; Cellulose-bd_dom_fun.
DR   InterPro; IPR000334; Glyco_hydro_45.
DR   InterPro; IPR036908; RlpA-like_sf.
DR   PANTHER; PTHR39730; ENDOGLUCANASE 1; 1.
DR   PANTHER; PTHR39730:SF1; ENDOGLUCANASE 1; 1.
DR   Pfam; PF00734; CBM_1; 1.
DR   Pfam; PF02015; Glyco_hydro_45; 1.
DR   SMART; SM00236; fCBD; 1.
DR   SUPFAM; SSF50685; Barwin-like endoglucanases; 1.
DR   SUPFAM; SSF57180; Cellulose-binding domain; 1.
DR   PROSITE; PS00562; CBM1_1; 1.
DR   PROSITE; PS51164; CBM1_2; 1.
DR   PROSITE; PS01140; GLYCOSYL_HYDROL_F45; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Cellulose degradation; Glycosidase; Hydrolase;
KW   Polysaccharide degradation; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..376
FT                   /note="Putative endoglucanase type K"
FT                   /id="PRO_0000008024"
FT   DOMAIN          335..374
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          19..308
FT                   /note="Catalytic"
FT   REGION          229..332
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          309..338
FT                   /note="Linker"
FT   COMPBIAS        230..277
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        305..319
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        29
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10069"
FT   ACT_SITE        140
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   376 AA;  39236 MW;  B430A5F962B9F882 CRC64;
     MRSYTLLALA GPLAVSAASG SGHSTRYWDC CKPSCSWSGK AAVNAPALTC DKNDNPISNT
     NAVNGCEGGG SAYACTNYSP WAVNDELAYG FAATKISGGS EASWCCACYA LTFTTGPVKG
     KKMIVQSTNT GGDLGDNHFD LMMPGGGVGI FDGCTSEFGK ALGGAQYGGI SSRSECDSYP
     ELLKDGCHWR FDWFENADNP DFTFEQVQCP KALLDISGCK RDDDSSFPAF KGDTSASKPQ
     PSSSAKKTTS AAAAAQPQKT KDSAPVVQKS STKPAAQPEP TKPADKPQTD KPVATKPAAT
     KPAQPVNKPK TTQKVRGTKT RGSCPAKTDA TAKASVVPAY YQCGGSKSAY PNGNLACATG
     SKCVKQNEYY SQCVPN
//