ID Q872Q1_NEUCS Unreviewed; 293 AA. AC Q872Q1; DT 01-JUN-2003, integrated into UniProtKB/TrEMBL. DT 01-JUN-2003, sequence version 1. DT 27-MAR-2024, entry version 102. 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 Name=B19A17.010 {ECO:0000313|EMBL:CAD70529.1}; GN ORFNames=GE21DRAFT_9486 {ECO:0000313|EMBL:KHE87990.1}; OS Neurospora crassa. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Sordariomycetidae; Sordariales; Sordariaceae; Neurospora. OX NCBI_TaxID=5141 {ECO:0000313|EMBL:CAD70529.1}; RN [1] {ECO:0000313|EMBL:CAD70529.1} RP NUCLEOTIDE SEQUENCE. RA German Neurospora genome project; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [2] {ECO:0000313|EMBL:CAD70529.1} RP NUCLEOTIDE SEQUENCE. RA Schulte U., Aign V., Hoheisel J., Brandt P., Fartmann B., Holland R., RA Nyakatura G., Mewes H.W., Mannhaupt G.; RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases. RN [3] {ECO:0000313|EMBL:KHE87990.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=73 {ECO:0000313|EMBL:KHE87990.1}; RG DOE Joint Genome Institute; RA Baker S.E., Grigoriev I., Haridas S., LaButti K., McCluskey K.; RT "Draft genome sequence of Neurospora crassa strain FGSC 73."; RL Submitted (NOV-2014) to the EMBL/GenBank/DDBJ databases. 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}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; BX284763; CAD70529.1; -; Genomic_DNA. DR EMBL; KN389638; KHE87990.1; -; Genomic_DNA. DR SMR; Q872Q1; -. DR CAZy; CBM1; Carbohydrate-Binding Module Family 1. DR CAZy; GH45; Glycoside Hydrolase Family 45. DR VEuPathDB; FungiDB:NCU05121; -. DR eggNOG; ENOG502RXA6; Eukaryota. DR HOGENOM; CLU_045022_1_0_1; -. DR OrthoDB; 1349031at2759; -. DR Proteomes; UP000053122; 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 Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP}. FT SIGNAL 1..21 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 22..293 FT /note="Cellulase" FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5010846870" FT DOMAIN 257..293 FT /note="CBM1" FT /evidence="ECO:0000259|PROSITE:PS51164" FT REGION 221..255 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 221..254 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 33 FT /note="Nucleophile" FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10069" SQ SEQUENCE 293 AA; 30261 MW; E7D96407F349877A CRC64; MRSSTILQTG LVAALPFAVQ AASGSGQSTR YWDCCKPSCS WSGKAPVNRP VLACDANNNP LSDASVKSGC DGGSAYTCAN NSPWAVNDQL SYGFAATKLS GGTESSWCCA CYALTFTSGP VAGKTLVVQS TSTGGDLGSN HFDINMPGGG VGLFDGCKRQ FGGLPGAQYG GISSRSQCDS FPAALKPGCQ WRFDWFQNAD NPNFTFKQVQ CPSELTSRTG CKRNDDSQFP VFTPPSGGGS NPSTPTTPPS SGGGSGCTAD KYAQCGGSGW SGCTNCPSGS TCKTINDYYH QCA //