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Q0CFP1 (CBHC_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 32. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Probable 1,4-beta-D-glucan cellobiohydrolase C

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase C
Exocellobiohydrolase C
Exoglucanase C
Gene names
Name:cbhC
ORF Names:ATEG_07493
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length468 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

The biological conversion of cellulose to glucose generally requires three types of hydrolytic enzymes: (1) Endoglucanases which cut internal beta-1,4-glucosidic bonds; (2) Exocellobiohydrolases that cut the dissaccharide cellobiose from the non-reducing end of the cellulose polymer chain; (3) Beta-1,4-glucosidases which hydrolyze the cellobiose and other short cello-oligosaccharides to glucose By similarity.

Catalytic activity

Hydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose and cellotetraose, releasing cellobiose from the non-reducing ends of the chains.

Subcellular location

Secreted By similarity.

Domain

Has a modular structure: a carbohydrate-binding module (CBM) at the N-terminus, a linker rich in threonines, and a C-terminal exocellobiohydrolase catalytic module. The genes for catalytic modules and CBMs seem to have evolved separately and have been linked by gene fusion.

Sequence similarities

Belongs to the glycosyl hydrolase 6 (cellulase B) family.

Contains 1 CBM1 (fungal-type carbohydrate-binding) domain.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functioncellulose 1,4-beta-cellobiosidase activity

Inferred from electronic annotation. Source: UniProtKB-EC

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 468450Probable 1,4-beta-D-glucan cellobiohydrolase C
PRO_0000394052

Regions

Domain19 – 5436CBM1
Region57 – 10650Thr-rich linker
Region107 – 468362Catalytic

Sites

Active site1981 By similarity
Active site2441Proton donor By similarity
Active site4231Nucleophile By similarity

Amino acid modifications

Disulfide bond26 ↔ 43 By similarity
Disulfide bond37 ↔ 53 By similarity
Disulfide bond199 ↔ 258 By similarity
Disulfide bond390 ↔ 437 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CFP1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 8FA36060121BF2AB

FASTA46848,846
        10         20         30         40         50         60 
MGRVSSLALA LLLPAVQAQQ TLWGQCGGIG WTGPTNCVAG AACSTQNPYY AQCLPGTATT 

        70         80         90        100        110        120 
STTLTTTTRV TTTTTSTTSK SSSTGSTTTT KSTGTTTTSG SSTTITSAPS GNPFSGYQLY 

       130        140        150        160        170        180 
ANPYYSSEVH TLAMPSLASS LLPAASAAAK VPSFTWLDTA AKVPTMGTYL ADIKAKNAAG 

       190        200        210        220        230        240 
ANPPIAAQFV VYDLPDRDCA ALASNGEYSI ANGGVANYKK YIDAIRAQLL NYPDVHTILV 

       250        260        270        280        290        300 
IEPDSLANLV TNLNVAKCAN AQSAYLECVN YALIQLNLPN VAMYIDAGHA GWLGWPANIG 

       310        320        330        340        350        360 
PAAQLFAGVY KDAGAPAALR GLATNVANYN AFSISTCPSY TSGDANCDEN RYINAIAPLL 

       370        380        390        400        410        420 
KDQGWDAHFI VDTGRNGVQP TKQNAWGDWC NVIGTGFGVR PTTNTGNSLV DAFVWVKPGG 

       430        440        450        460 
ESDGTSDSSS ARYDAHCGYS DALQPAPEAG TWFQAYFEQL LKNANPAF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476604 Genomic DNA. Translation: EAU31755.1.
RefSeqXP_001216114.1. XM_001216114.1.

3D structure databases

ProteinModelPortalQ0CFP1.
SMRQ0CFP1. Positions 20-54, 106-468.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING33178.CADATEAP00001301.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00001301; CADATEAP00001301; CADATEAG00001301.
GeneID4322742.

Phylogenomic databases

eggNOGCOG5297.
HOGENOMHOG000178851.
OMAYTQGNSV.
OrthoDBEOG72C594.

Family and domain databases

Gene3D3.20.20.40. 1 hit.
InterProIPR016288. Beta_cellobiohydrolase.
IPR000254. Cellulose-bd_dom_fun.
IPR001524. Glyco_hydro_6_CS.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF01341. Glyco_hydro_6. 1 hit.
[Graphical view]
PIRSFPIRSF001100. Beta_cellobiohydrolase. 1 hit.
PRINTSPR00733. GLHYDRLASE6.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF51989. SSF51989. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
PS00655. GLYCOSYL_HYDROL_F6_1. 1 hit.
PS00656. GLYCOSYL_HYDROL_F6_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBHC_ASPTN
AccessionPrimary (citable) accession number: Q0CFP1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: October 17, 2006
Last modified: March 19, 2014
This is version 32 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries