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B0Y9G4 (EGLD_ASPFC) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 21. 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 D

Short name=Endoglucanase D
EC=3.2.1.4
Alternative name(s):
Carboxymethylcellulase D
Cellulase D
Gene names
Name:eglD
ORF Names:AFUB_080950
OrganismNeosartorya fumigata (strain CEA10 / CBS 144.89 / FGSC A1163) (Aspergillus fumigatus) [Complete proteome]
Taxonomic identifier451804 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length349 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.

Domain

Has a modular structure: an endo-beta-1,4-glucanase catalytic module at the N-terminus, a linker rich in serines and threonines, and a C-terminal carbohydrate-binding module (CBM). 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 61 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_functioncellulase 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 – 349330Probable endo-beta-1,4-glucanase D
PRO_0000394061

Regions

Domain311 – 34737CBM1
Region20 – 235216Catalytic
Region236 – 30772Ser/Thr-rich linker

Sites

Active site1641Proton donor By similarity
Active site2101Nucleophile By similarity

Amino acid modifications

Glycosylation3231N-linked (GlcNAc...) Potential
Disulfide bond319 ↔ 336 By similarity
Disulfide bond330 ↔ 346 By similarity

Sequences

Sequence LengthMass (Da)Tools
B0Y9G4 [UniParc].

Last modified April 8, 2008. Version 1.
Checksum: 19610E8678EA60AE

FASTA34935,763
        10         20         30         40         50         60 
MKSTFGLLAL AAAAKLVSAH ATVHAVWIND VDQGAGNSAD GYIRSPPNNS PITDVTSTDM 

        70         80         90        100        110        120 
TCNVNGKNPV AKTLSVKAGD KVTFEWHHDT RSDSDDIIAS SHMGPVMVYM APTEKGTAGN 

       130        140        150        160        170        180 
GWVKIAEEGY SNGKWAVANL IANRGKHSIT VPDVPAGEYL LRPEIIALHE GNRQGGAQFY 

       190        200        210        220        230        240 
MECVQVKVTS AGTKTLPAGV SIPGAYKATD PGVLFDMYNS FTSYPIPGPA VWDGSSSGSS 

       250        260        270        280        290        300 
GSSGSSPATT TAPAVSVTAV PTKEAPVDTS ATPTTFVTAT KPATTAAPAA PSASSGSNSG 

       310        320        330        340 
SDSCNSGSAS GSVKIYGQCG GQNYSGPTSC EAGLICKEWN PYYHQCVSA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS499600 Genomic DNA. Translation: EDP48657.1.

3D structure databases

ProteinModelPortalB0Y9G4.
SMRB0Y9G4. Positions 313-347.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAFUBT00008022; CADAFUBP00007883; CADAFUBG00008022.

Phylogenomic databases

HOGENOMHOG000158937.
OrthoDBEOG7KM64H.
PhylomeDBB0Y9G4.

Family and domain databases

InterProIPR000254. Cellulose-bd_dom_fun.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamPF00734. CBM_1. 1 hit.
PF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
ProDomPD001821. CBD_fun. 1 hit.
[Graphical view] [Entries sharing at least one domain]
SMARTSM00236. fCBD. 1 hit.
[Graphical view]
SUPFAMSSF57180. SSF57180. 1 hit.
PROSITEPS00562. CBM1_1. 1 hit.
PS51164. CBM1_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameEGLD_ASPFC
AccessionPrimary (citable) accession number: B0Y9G4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 21 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