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A1CU44 (CBHB_ASPCL) 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 B

EC=3.2.1.91
Alternative name(s):
Beta-glucancellobiohydrolase B
Exocellobiohydrolase B
Exoglucanase B
Gene names
Name:cbhB
ORF Names:ACLA_085260
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length539 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 Probable.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) 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 – 2626 Potential
Chain27 – 539513Probable 1,4-beta-D-glucan cellobiohydrolase B
PRO_0000393546

Regions

Domain503 – 53937CBM1
Region27 – 461435Catalytic
Region462 – 50342Thr-rich linker

Sites

Active site2381Nucleophile By similarity
Active site2431Proton donor By similarity

Amino acid modifications

Glycosylation901N-linked (GlcNAc...) Potential
Glycosylation2961N-linked (GlcNAc...) Potential
Glycosylation4951N-linked (GlcNAc...) Potential
Disulfide bond511 ↔ 528 By similarity
Disulfide bond522 ↔ 538 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1CU44 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: 27D7BD8E58C17687

FASTA53957,042
        10         20         30         40         50         60 
MLPSTISYRI YKNALFFAAL FGAVQAQKVG TSKAEVHPSM AWQTCAADGT CTTKNGKVVI 

        70         80         90        100        110        120 
DANWRWVHDV KGYTNCYTGN TWNAELCPDN ESCAENCALE GADYAATYGA TTSGNALSLK 

       130        140        150        160        170        180 
FVTQSQQKNI GSRLYMMKDD NTYETFKLLN QEFTFDVDVS NLPCGLNGAL YFVSMDADGG 

       190        200        210        220        230        240 
LSRYTGNEAG AKYGTGYCDS QCPRDLKFIN GLANVEGWTP SSSDANAGNG GHGSCCAEMD 

       250        260        270        280        290        300 
IWEANSISTA YTPHPCDTPG QAMCNGDSCG GTYSSDRYGG TCDPDGCDFN SYRQGNKSFY 

       310        320        330        340        350        360 
GPGMTVDTKK KMTVVTQFLT NDGTATGTLS EIKRFYVQDG KVIANSESTW PNLGGNSLTN 

       370        380        390        400        410        420 
DFCKAQKTVF GDMDTFSKHG GMEGMGAALA EGMVLVMSLW DDHNSNMLWL DSNSPTTGTS 

       430        440        450        460        470        480 
TTPGVARGSC DISSGDPKDL EANHPDASVV YSNIKVGPIG STFNSGGSNP GGSTTTTKPA 

       490        500        510        520        530 
TSTTTTKATT TATTNTTGPT GTGVAQPWAQ CGGIGYSGPT QCAAPYTCTK QNDYYSQCL 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027060 Genomic DNA. Translation: EAW06831.1.
RefSeqXP_001268257.1. XM_001268256.1.

3D structure databases

ProteinModelPortalA1CU44.
SMRA1CU44. Positions 27-463, 505-539.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5057.CADACLAP00007326.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00007517; CADACLAP00007326; CADACLAG00007517.
GeneID4699868.
KEGGact:ACLA_085260.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000182210.
OMAHPCDTPG.
OrthoDBEOG7ZGXCF.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR000254. Cellulose-bd_dom_fun.
IPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF49899. SSF49899. 1 hit.
SSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCBHB_ASPCL
AccessionPrimary (citable) accession number: A1CU44
Entry history
Integrated into UniProtKB/Swiss-Prot: April 20, 2010
Last sequence update: January 23, 2007
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