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A1CCN4 (CBHC_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 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:ACLA_062560
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length464 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 – 1919 Potential
Chain20 – 464445Probable 1,4-beta-D-glucan cellobiohydrolase C
PRO_0000394049

Regions

Domain20 – 5536CBM1
Region59 – 10244Thr-rich linker
Region103 – 464362Catalytic

Sites

Active site1941 By similarity
Active site2401Proton donor By similarity
Active site4191Nucleophile By similarity

Amino acid modifications

Disulfide bond27 ↔ 44 By similarity
Disulfide bond38 ↔ 54 By similarity
Disulfide bond195 ↔ 254 By similarity
Disulfide bond386 ↔ 433 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CCN4 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: DDE4E7406F0F96B6

FASTA46448,841
        10         20         30         40         50         60 
MKNFAPSLAL SLLLPTVQAQ QTMWGQCGGA GWSGATDCVA GGVCSTQNAY YAQCLPGATT 

        70         80         90        100        110        120 
ATTLSTTSKG TTTTTTSSTT STGGGSSSTT TKTSTSAGPT VTGSPSGNPF SGYQQYANPY 

       130        140        150        160        170        180 
YSSEVHTLAI PSMTGALAVK ASAVADVPSF VWLDVAAKVP TMGTYLENIR AKNKAGANPP 

       190        200        210        220        230        240 
VAGIFVVYDL PDRDCAALAS NGEYAIADGG IAKYKAYIDA IRAQLLKYPD VHTILVIEPD 

       250        260        270        280        290        300 
SLANLITNIN VAKCSGAKDA YLECINYALK QLNLPNVAMY IDAGHGGWLG WDANIGPAAE 

       310        320        330        340        350        360 
MYAKVYKDAD APAALRGLAV NVANYNAWTI DTCPSYTQGN KNCDEKRYIH ALYPLLKAAG 

       370        380        390        400        410        420 
WDARFIMDTG RNGVQPTKQQ AQGDWCNVIG TGFGIRPSSE TGDDLLDAFV WVKPGAESDG 

       430        440        450        460 
TSDTTAARYD AHCGYTDALK PAPEAGQWFQ AYFEQLLTNA NPAF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027050 Genomic DNA. Translation: EAW12291.1.
RefSeqXP_001273717.1. XM_001273716.1.

3D structure databases

ProteinModelPortalA1CCN4.
SMRA1CCN4. Positions 21-55, 102-464.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00005938; CADACLAP00005801; CADACLAG00005938.
GeneID4706008.
KEGGact:ACLA_062560.

Phylogenomic databases

eggNOGCOG5297.
HOGENOMHOG000178851.
OMAANLMGTF.
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_ASPCL
AccessionPrimary (citable) accession number: A1CCN4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: May 14, 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