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A1DJQ7 (CBHC_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 35. 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:NFIA_002990
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length450 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
Glycoprotein
   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 – 450431Probable 1,4-beta-D-glucan cellobiohydrolase C
PRO_0000394054

Regions

Domain20 – 5536CBM1
Region59 – 9032Thr-rich linker
Region91 – 450360Catalytic

Sites

Active site1801 By similarity
Active site2261Proton donor By similarity
Active site4051Nucleophile By similarity

Amino acid modifications

Glycosylation4091N-linked (GlcNAc...) Potential
Disulfide bond27 ↔ 44 By similarity
Disulfide bond38 ↔ 54 By similarity
Disulfide bond181 ↔ 240 By similarity
Disulfide bond372 ↔ 419 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1DJQ7 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 591EB3C96C03AB8A

FASTA45047,383
        10         20         30         40         50         60 
MKHLASSIAL TLLLPAVQAQ QTVWGQCGGQ GWSGPTNCVA GAACSTLNPY YAQCIPGATA 

        70         80         90        100        110        120 
TSTTLSTTTT TQTTTKPTTT GPTTSAPTVT ASGNPFSGYQ LYANPYYSSE VHTLAMPSLP 

       130        140        150        160        170        180 
SSLQPKASAV AEVPSFVWLD VAAKVPTMGT YLADIQAKNK AGASPPIAGI FVVYDLPDRD 

       190        200        210        220        230        240 
CAALASNGEY SIANNGVANY KAYIDAIRAQ LVKYSDVHTI LVIEPDSLAN LVTNLNVAKC 

       250        260        270        280        290        300 
ANAQSAYLEC VDYALKQLNL PNVAMYLDAG HAGWLGWPAN LGPAATLFAK VYTDAGSPAA 

       310        320        330        340        350        360 
LRGLATNVAN YNAWSLSTCP SYTQGDPNCD EKKYINAMAP LLKNAGFDAH FIMDTSRNGV 

       370        380        390        400        410        420 
QPTKQSAWGD WCNVIGTGFG VRPSTNTGDP LQDAFVWIKP GGESDGTSNS SSARYDAHCG 

       430        440        450 
YSDALQPAPE AGTWFQAYFE QLLTNANPSF 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027697 Genomic DNA. Translation: EAW16946.1.
RefSeqXP_001258843.1. XM_001258842.1.

3D structure databases

ProteinModelPortalA1DJQ7.
SMRA1DJQ7. Positions 21-55, 88-450.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00000050; CADNFIAP00000041; CADNFIAG00000050.
GeneID4585216.
KEGGnfi:NFIA_002990.

Phylogenomic databases

eggNOGCOG5297.
HOGENOMHOG000178851.
OMAKCANAQS.
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_NEOFI
AccessionPrimary (citable) accession number: A1DJQ7
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 35 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