ID CBHC_ASPFC Reviewed; 454 AA. AC B0XWL3; DT 18-MAY-2010, integrated into UniProtKB/Swiss-Prot. DT 08-APR-2008, sequence version 1. DT 03-MAY-2023, entry version 57. DE RecName: Full=Probable 1,4-beta-D-glucan cellobiohydrolase C; DE EC=3.2.1.91; DE AltName: Full=Beta-glucancellobiohydrolase C; DE AltName: Full=Exocellobiohydrolase C; DE AltName: Full=Exoglucanase C; DE Flags: Precursor; GN Name=cbhC; ORFNames=AFUB_046510; OS Aspergillus fumigatus (strain CBS 144.89 / FGSC A1163 / CEA10) (Neosartorya OS fumigata). OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Fumigati. OX NCBI_TaxID=451804; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=CBS 144.89 / FGSC A1163 / CEA10; RX PubMed=18404212; DOI=10.1371/journal.pgen.1000046; RA Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., RA Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., RA Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M., RA Haas B.J., Inman J.M., Kent R., Lemieux S., Malavazi I., Orvis J., RA Roemer T., Ronning C.M., Sundaram J.P., Sutton G., Turner G., Venter J.C., RA White O.R., Whitty B.R., Youngman P., Wolfe K.H., Goldman G.H., RA Wortman J.R., Jiang B., Denning D.W., Nierman W.C.; RT "Genomic islands in the pathogenic filamentous fungus Aspergillus RT fumigatus."; RL PLoS Genet. 4:E1000046-E1000046(2008). CC -!- FUNCTION: The biological conversion of cellulose to glucose generally CC requires three types of hydrolytic enzymes: (1) Endoglucanases which CC cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that CC cut the disaccharide cellobiose from the non-reducing end of the CC cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the CC cellobiose and other short cello-oligosaccharides to glucose. CC {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose CC and cellotetraose, releasing cellobiose from the non-reducing ends of CC the chains.; EC=3.2.1.91; CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250}. CC -!- DOMAIN: Has a modular structure: a carbohydrate-binding module (CBM) at CC the N-terminus, a linker rich in threonines, and a C-terminal CC exocellobiohydrolase catalytic module. The genes for catalytic modules CC and CBMs seem to have evolved separately and have been linked by gene CC fusion. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 6 (cellulase B) family. CC {ECO:0000305}. 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; DS499596; EDP53472.1; -; Genomic_DNA. DR AlphaFoldDB; B0XWL3; -. DR SMR; B0XWL3; -. DR GlyCosmos; B0XWL3; 1 site, No reported glycans. DR EnsemblFungi; EDP53472; EDP53472; AFUB_046510. DR VEuPathDB; FungiDB:AFUB_046510; -. DR HOGENOM; CLU_015488_0_0_1; -. DR PhylomeDB; B0XWL3; -. DR Proteomes; UP000001699; Unassembled WGS sequence. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016162; F:cellulose 1,4-beta-cellobiosidase 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; 3.20.20.40; 1, 4-beta cellobiohydrolase; 1. DR InterPro; IPR016288; Beta_cellobiohydrolase. DR InterPro; IPR036434; Beta_cellobiohydrolase_sf. DR InterPro; IPR035971; CBD_sf. DR InterPro; IPR000254; Cellulose-bd_dom_fun. DR InterPro; IPR001524; Glyco_hydro_6_CS. DR PANTHER; PTHR34876; -; 1. DR PANTHER; PTHR34876:SF4; 1,4-BETA-D-GLUCAN CELLOBIOHYDROLASE C-RELATED; 1. DR Pfam; PF00734; CBM_1; 1. DR Pfam; PF01341; Glyco_hydro_6; 1. DR PIRSF; PIRSF001100; Beta_cellobiohydrolase; 1. DR PRINTS; PR00733; GLHYDRLASE6. DR SMART; SM00236; fCBD; 1. DR SUPFAM; SSF57180; Cellulose-binding domain; 1. DR SUPFAM; SSF51989; Glycosyl hydrolases family 6, cellulases; 1. DR PROSITE; PS00562; CBM1_1; 1. DR PROSITE; PS51164; CBM1_2; 1. DR PROSITE; PS00655; GLYCOSYL_HYDROL_F6_1; 1. DR PROSITE; PS00656; GLYCOSYL_HYDROL_F6_2; 1. PE 3: Inferred from homology; KW Carbohydrate metabolism; Cellulose degradation; Disulfide bond; KW Glycoprotein; Glycosidase; Hydrolase; Polysaccharide degradation; Secreted; KW Signal. FT SIGNAL 1..19 FT /evidence="ECO:0000255" FT CHAIN 20..454 FT /note="Probable 1,4-beta-D-glucan cellobiohydrolase C" FT /id="PRO_0000394050" FT DOMAIN 20..55 FT /note="CBM1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00597" FT REGION 59..94 FT /note="Thr-rich linker" FT REGION 68..95 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 95..454 FT /note="Thr-rich linker" FT ACT_SITE 184 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056" FT ACT_SITE 230 FT /note="Proton donor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10057" FT ACT_SITE 409 FT /note="Nucleophile" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10056" FT CARBOHYD 413 FT /note="N-linked (GlcNAc...) asparagine" FT /evidence="ECO:0000255" FT DISULFID 27..44 FT /evidence="ECO:0000250" FT DISULFID 38..54 FT /evidence="ECO:0000250" FT DISULFID 185..244 FT /evidence="ECO:0000250" FT DISULFID 376..423 FT /evidence="ECO:0000250" SQ SEQUENCE 454 AA; 47796 MW; 9EFFB0212288A576 CRC64; MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTSCVA GAACSTLNPY YAQCIPGATA TSTTLTTTTA ATTTSQTTTK PTTTGPTTSA PTVTASGNPF SGYQLYANPY YSSEVHTLAM PSLPSSLQPK ASAVAEVPSF VWLDVAAKVP TMGTYLADIQ AKNKAGANPP IAGIFVVYDL PDRDCAALAS NGEYSIANNG VANYKAYIDA IRAQLVKYSD VHTILVIEPD SLANLVTNLN VAKCANAQSA YLECVDYALK QLNLPNVAMY LDAGHAGWLG WPANLGPAAT LFAKVYTDAG SPAAVRGLAT NVANYNAWSL STCPSYTQGD PNCDEKKYIN AMAPLLKEAG FDAHFIMDTS RNGVQPTKQN AWGDWCNVIG TGFGVRPSTN TGDPLQDAFV WIKPGGESDG TSNSTSPRYD AHCGYSDALQ PAPEAGTWFQ AYFEQLLTNA NPSF //