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B8NW70 (CELB_ASPFN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 27. 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:AFLA_118170
OrganismAspergillus flavus (strain ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167) [Complete proteome]
Taxonomic identifier332952 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length416 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 – 1717 Potential
Chain18 – 416399Probable endo-beta-1,4-glucanase celB
PRO_0000395155

Sites

Active site2141Nucleophile By similarity
Active site2191Proton donor By similarity

Amino acid modifications

Glycosylation451N-linked (GlcNAc...) Potential
Glycosylation1041N-linked (GlcNAc...) Potential
Glycosylation1171N-linked (GlcNAc...) Potential
Glycosylation1351N-linked (GlcNAc...) Potential
Glycosylation2331N-linked (GlcNAc...) Potential
Glycosylation2781N-linked (GlcNAc...) Potential
Glycosylation2921N-linked (GlcNAc...) Potential
Glycosylation3821N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
B8NW70 [UniParc].

Last modified March 3, 2009. Version 1.
Checksum: 437ADE03BF84AB53

FASTA41644,448
        10         20         30         40         50         60 
MIWTLAPFVA LLPLVTAQQV GTTADAHPRL TTYKCTSQNG CTRQNTSVVL DAATHFIHKK 

        70         80         90        100        110        120 
GTQTSCTNSN GLDTAICPDK QTCADNCVVD GITDYASYGV QTKNDTLTLQ QYLQTGNATK 

       130        140        150        160        170        180 
SLSPRVYLLA EDGENYSMLK LLNQEFTFDV DASTLVCGMN GALYLSEMEA SGGKSSLNQA 

       190        200        210        220        230        240 
GAKYGTGYCD AQCYTTPWIN GEGNTESVGS CCQEMDIWEA NARATGLTPH PCNTTGLYEC 

       250        260        270        280        290        300 
SGSGCGDSGV CDKAGCGFNP YGLGAKDYYG YGLKVNTNET FTVVTQFLTN DNTTSGQLSE 

       310        320        330        340        350        360 
IRRLYIQNGQ VIQNAAVTSG GKTVDSITKD FCSGEGSAFN RLGGLEEMGH ALGRGMVLAL 

       370        380        390        400        410 
SIWNDAGSFM QWLDGGSAGP CNATEGNPAL IEKLYPDTHV KFSKIRWGDI GSTYRH 

« Hide

References

[1]"Genome sequence of Aspergillus flavus strain NRRL 3357."
Payne W.G.A., Dean R.A., Nierman W.C., Amedeo P., Caler E.G.A., Fedorova N.D., Maiti R., Joardar V., Inman J., Galinsky K.J., Yu J., Bhatnagar D., Cleveland T.E.
Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 200026 / FGSC A1120 / NRRL 3357 / JCM 12722 / SRRC 167.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
EQ963485 Genomic DNA. Translation: EED45588.1.
RefSeqXP_002384524.1. XM_002384483.1.

3D structure databases

ProteinModelPortalB8NW70.
SMRB8NW70. Positions 18-413.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING5059.CADAFLAP00012389.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFLAT00012389; CADAFLAP00012389; CADAFLAG00012389.
GeneID7917417.
KEGGafv:AFLA_118170.

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_ASPFN
AccessionPrimary (citable) accession number: B8NW70
Entry history
Integrated into UniProtKB/Swiss-Prot: June 15, 2010
Last sequence update: March 3, 2009
Last modified: March 19, 2014
This is version 27 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