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A1DME8 (EGLB_NEOFI) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 43. 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 B

Short name=Endoglucanase B
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase B
Cellulase B
Gene names
Name:eglB
ORF Names:NFIA_053150
OrganismNeosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome]
Taxonomic identifier331117 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeNeosartorya

Protein attributes

Sequence length329 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 5 (cellulase A) 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 – 329311Probable endo-beta-1,4-glucanase B
PRO_0000394059

Sites

Active site1561Proton donor By similarity
Active site2631Nucleophile By similarity

Amino acid modifications

Glycosylation331N-linked (GlcNAc...) Potential
Glycosylation961N-linked (GlcNAc...) Potential

Sequences

Sequence LengthMass (Da)Tools
A1DME8 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: DFA67E1E6BFA5E3F

FASTA32935,875
        10         20         30         40         50         60 
MKFGSIVLIA AAAGSAVAAP AKRASVFQWF GSNESGAEFG QNTIPGSYGK EFIFPDPSTI 

        70         80         90        100        110        120 
STLIGKGMNI FRVQFLMERL VPSSMTGSYN EEYLANLTSV VDAVTKAGSY AILDPHNFGR 

       130        140        150        160        170        180 
YNGQIISSTD DFKTFWQNLA GKFKSNNLVI FDTNNEYHDM DQALVLNLNQ AAINGIRAAG 

       190        200        210        220        230        240 
ATSQYIFVEG NSWSGAWTWV DVNDNLKALT DPQDKIVYEM HQYLDSDGSG TSESCVSTTI 

       250        260        270        280        290        300 
GKERVTAATK WLKDNGKVGI IGEFAGGVND QCRTAISGML EYLAQNTDVW KGALWWAAGP 

       310        320 
WWGNYMFNME PPSGAAYVGM LDILEPYLG 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS027698 Genomic DNA. Translation: EAW15969.1.
RefSeqXP_001257866.1. XM_001257865.1.

3D structure databases

ProteinModelPortalA1DME8.
SMRA1DME8. Positions 26-328.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING36630.CADNFIAP00005314.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADNFIAT00005442; CADNFIAP00005314; CADNFIAG00005442.
GeneID4584381.
KEGGnfi:NFIA_053150.

Phylogenomic databases

eggNOGCOG2730.
HOGENOMHOG000111120.
KOK01179.
OMAGKGMNIF.
OrthoDBEOG776T0S.

Family and domain databases

Gene3D3.20.20.80. 1 hit.
InterProIPR001547. Glyco_hydro_5.
IPR013781. Glyco_hydro_catalytic_dom.
IPR017853. Glycoside_hydrolase_SF.
[Graphical view]
PfamPF00150. Cellulase. 1 hit.
[Graphical view]
SUPFAMSSF51445. SSF51445. 1 hit.
ProtoNetSearch...

Entry information

Entry nameEGLB_NEOFI
AccessionPrimary (citable) accession number: A1DME8
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 43 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