GUNK_FUSOX
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-AUG-2022, entry version 88.
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 Gene3D; 2.40.40.10; -; 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 Pfam; PF00734; CBM_1; 1.
DR Pfam; PF02015; Glyco_hydro_45; 1.
DR SMART; SM00236; fCBD; 1.
DR SUPFAM; SSF50685; SSF50685; 1.
DR SUPFAM; SSF57180; SSF57180; 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
