ID G0S9D9_CHATD Unreviewed; 314 AA.
AC G0S9D9;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 40.
DE RecName: Full=Cellulase {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
DE EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601, ECO:0000256|PROSITE-ProRule:PRU10069};
GN ORFNames=CTHT_0045500 {ECO:0000313|EMBL:EGS20050.1};
OS Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
OS (Thermochaetoides thermophila).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Sordariales; Chaetomiaceae; Thermochaetoides.
OX NCBI_TaxID=759272 {ECO:0000313|Proteomes:UP000008066};
RN [1] {ECO:0000313|EMBL:EGS20050.1, ECO:0000313|Proteomes:UP000008066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1495 / CBS 144.50 / IMI 039719
RC {ECO:0000313|Proteomes:UP000008066};
RX PubMed=21784248; DOI=10.1016/j.cell.2011.06.039;
RA Amlacher S., Sarges P., Flemming D., van Noort V., Kunze R., Devos D.P.,
RA Arumugam M., Bork P., Hurt E.;
RT "Insight into structure and assembly of the nuclear pore complex by
RT utilizing the genome of a eukaryotic thermophile.";
RL Cell 146:277-289(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00000966, ECO:0000256|PROSITE-
CC ProRule:PRU10069};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 45 (cellulase K) family.
CC {ECO:0000256|ARBA:ARBA00007793}.
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DR EMBL; GL988043; EGS20050.1; -; Genomic_DNA.
DR RefSeq; XP_006694935.1; XM_006694872.1.
DR AlphaFoldDB; G0S9D9; -.
DR STRING; 759272.G0S9D9; -.
DR GeneID; 18258588; -.
DR KEGG; cthr:CTHT_0045500; -.
DR eggNOG; ENOG502RXA6; Eukaryota.
DR HOGENOM; CLU_045022_1_0_1; -.
DR OMA; NYSPWAV; -.
DR OrthoDB; 1349031at2759; -.
DR Proteomes; UP000008066; Unassembled WGS sequence.
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 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Cellulose degradation {ECO:0000256|ARBA:ARBA00023001};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000008066};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..314
FT /note="Cellulase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003409385"
FT DOMAIN 274..310
FT /note="CBM1"
FT /evidence="ECO:0000259|PROSITE:PS51164"
FT REGION 224..270
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..270
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 31
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069"
SQ SEQUENCE 314 AA; 33125 MW; 571BC253DE2D9498 CRC64;
MRSTPVLRTA LAAALPFTVL AADGKSTRYW DCCKPSCSWP GKAAVSQPVF ACDRNFNRIY
DFGAKSGCEG GPAYSCADQT PWAVNDQFSY GFAATNIAGG NEASWCCACY KLTFTSGPVA
GKVMVVQSTS TGGDLGNNHF DLNIPGGGVG IFDGCTPQFG GLPGERYGGI SSRSQCDSFP
DALKPGCYWR FDWFLNADNP NFTFERVQCP SELVARTGCK RNDDGNYPVF TPPSGDSPSS
SSAAPTSTST SQQPQQPTSS SSQASVPTSN PGGCTSQKWA QCGGIGFTGC TTCVSGTTCT
KLNDWYSQCT MINL
//
