Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

A1CG87 (CELB_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 29. 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 endo-beta-1,4-glucanase celB

Short name=Endoglucanase celB
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase celB
Cellulase B
Gene names
Name:celB
ORF Names:ACLA_066030
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology

General annotation (Comments)

Function

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. Involved in the degradation of complex natural cellulosic substrates By similarity.

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans.

Subcellular location

Secreted By similarity.

Sequence similarities

Belongs to the glycosyl hydrolase 7 (cellulase C) family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   Molecular functionGlycosidase
Hydrolase
   PTMGlycoprotein
   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_functioncellulase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 418400Probable endo-beta-1,4-glucanase celB
PRO_0000395153

Sites

Active site2151Nucleophile By similarity
Active site2201Proton donor By similarity

Amino acid modifications

Glycosylation461N-linked (GlcNAc...) Potential
Glycosylation1181N-linked (GlcNAc...) Potential
Glycosylation1361N-linked (GlcNAc...) Potential
Glycosylation2341N-linked (GlcNAc...) Potential
Glycosylation2911N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A1CG87 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: C9607BB9C58EC80B

FASTA41844,827
        10         20         30         40         50         60 
MVRTFAVTAL ALLPLVAAQQ IGSTKEVHPQ LTTYKCTSQG GCVKQNTSIV LDSGSHWIHA 

        70         80         90        100        110        120 
KGGEVSCTTS SGLDPALCPD KETCAENCVV EGITDYSQYG VQTRGDAMLL REYIKQNNQT 

       130        140        150        160        170        180 
KAPSPRVYLL DEDGENYSML RLLNQEFTFD VDVSKLPCGM NGALYFSEMS ASGGRSALNP 

       190        200        210        220        230        240 
AGAAYGTGYC DAQCYTNAWI NGEANTAKAG LCCQEMDIWE ANARANAFTP HPCNSTGLLG 

       250        260        270        280        290        300 
CAGDECNSVC DKAGCGFNPY ALGARDYYGT AMTVDTTKPF TVVTQFLTAD NSTTGALREI 

       310        320        330        340        350        360 
RRLYVQAGQV IQNAVVKVDG RTVNSITEPY CASQGVFEGL GGLRRMGEAL GRGMVLSMSI 

       370        380        390        400        410 
WNDAGGFMHW LDSGNSGPCS STEGDPSLIE NKYPDTAVTF SKIRWGDLGT TFATRRLH 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027053 Genomic DNA. Translation: EAW10967.1.
RefSeqXP_001272393.1. XM_001272392.1.

3D structure databases

ProteinModelPortalA1CG87.
SMRA1CG87. Positions 19-414.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00006346; CADACLAP00006191; CADACLAG00006346.
GeneID4704573.
KEGGact:ACLA_066030.

Phylogenomic databases

eggNOGNOG138370.
HOGENOMHOG000182210.
OMAEGHADDI.
OrthoDBEOG7Q8CXJ.

Family and domain databases

Gene3D2.70.100.10. 1 hit.
InterProIPR008985. ConA-like_lec_gl_sf.
IPR001722. Glyco_hydro_7.
[Graphical view]
PfamPF00840. Glyco_hydro_7. 1 hit.
[Graphical view]
PRINTSPR00734. GLHYDRLASE7.
SUPFAMSSF49899. SSF49899. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCELB_ASPCL
AccessionPrimary (citable) accession number: A1CG87
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 29 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