ID   CBHC_ASPNC              Reviewed;         459 AA.
AC   A2QYR9;
DT   18-MAY-2010, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   27-MAR-2024, entry version 76.
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=An12g02220;
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4892 / CBS 513.88 / FGSC A1513;
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA   Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA   van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA   Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA   Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA   Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA   Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA   Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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}.
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DR   EMBL; AM270264; CAK41068.1; -; Genomic_DNA.
DR   RefSeq; XP_001395308.1; XM_001395271.2.
DR   AlphaFoldDB; A2QYR9; -.
DR   SMR; A2QYR9; -.
DR   CAZy; CBM1; Carbohydrate-Binding Module Family 1.
DR   CAZy; GH6; Glycoside Hydrolase Family 6.
DR   GlyCosmos; A2QYR9; 1 site, No reported glycans.
DR   EnsemblFungi; CAK41068; CAK41068; An12g02220.
DR   GeneID; 4985573; -.
DR   KEGG; ang:An12g02220; -.
DR   VEuPathDB; FungiDB:An12g02220; -.
DR   HOGENOM; CLU_015488_0_0_1; -.
DR   OrthoDB; 275141at2759; -.
DR   Proteomes; UP000006706; Chromosome 3L.
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;
KW   Reference proteome; Secreted; Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..459
FT                   /note="Probable 1,4-beta-D-glucan cellobiohydrolase C"
FT                   /id="PRO_5000220698"
FT   DOMAIN          19..54
FT                   /note="CBM1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00597"
FT   REGION          54..94
FT                   /note="Thr-rich linker"
FT   REGION          76..97
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          95..459
FT                   /note="Catalytic"
FT   ACT_SITE        189
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   ACT_SITE        235
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10057"
FT   ACT_SITE        414
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10056"
FT   CARBOHYD        303
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        26..43
FT                   /evidence="ECO:0000250"
FT   DISULFID        37..53
FT                   /evidence="ECO:0000250"
FT   DISULFID        190..249
FT                   /evidence="ECO:0000250"
FT   DISULFID        381..428
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   459 AA;  48126 MW;  A584E983E58DCE87 CRC64;
     MHYPLSLALA FLPFGIQAQQ TLWGQCGGQG YSGATSCVAG ATCATVNEYY AQCTPAAGTS
     SATTLKTTTS STTAAVTTTT TTQSPTGSAS PTTTASASGN PFSGYQLYVN PYYSSEVASL
     AIPSLTGSLS SLQAAATAAA KVPSFVWLDT AAKVPTMGDY LADIQSQNAA GANPPIAGQF
     VVYDLPDRDC AALASNGEYS IADNGVEHYK SYIDSIREIL VQYSDVHTLL VIEPDSLANL
     VTNLNVAKCA NAESAYLECT NYALTQLNLP NVAMYLDAGH AGWLGWPANQ QPAADLFASV
     YKNASSPAAV RGLATNVANY NAWTISSCPS YTQGNSVCDE QQYINAIAPL LQAQGFDAHF
     IVDTGRNGKQ PTGQQAWGDW CNVINTGFGE RPTTDTGDAL VDAFVWVKPG GESDGTSDSS
     ATRYDAHCGY SDALQPAPEA GTWFQAYFVQ LLTNANPAF
//