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Q0CEU4 (EGLD_ASPTN) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 24. 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:ATEG_07790
OrganismAspergillus terreus (strain NIH 2624 / FGSC A1156) [Complete proteome]
Taxonomic identifier341663 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length360 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 – 360341Probable endo-beta-1,4-glucanase D
PRO_0000394066

Regions

Domain322 – 35837CBM1
Region20 – 234215Catalytic
Region235 – 30369Ser/Thr-rich linker

Sites

Active site1641Proton donor By similarity
Active site2101Nucleophile By similarity

Amino acid modifications

Glycosylation3341N-linked (GlcNAc...) Potential
Disulfide bond330 ↔ 347 By similarity
Disulfide bond341 ↔ 357 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0CEU4 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 0BABA36D957D8F7D

FASTA36036,795
        10         20         30         40         50         60 
MKTSFGLLAL AAAAKLVNAH ATVFAVWIND EDQGLGNTAD GYIRSPPNNS PVTDVTSKDM 

        70         80         90        100        110        120 
TCNVNGATAA AKTLDVKAGD KITFEWHHNS RDASDDIIAS SHLGPVMVYM APTEKGSAGS 

       130        140        150        160        170        180 
GWVKIAEDGY SNGKWAVDTL IANRGKHSIT VPDVPAGEYL FRPEIIALHE GNREGGAQLY 

       190        200        210        220        230        240 
MECVQVKVTS DGSKTLPEGV SIPGTYTATD PGILFDIYNS FDSYPIPGPA VWDGSSSGSS 

       250        260        270        280        290        300 
SGSSKTTAAA PAATSAASAS STKAPATTAA PVQTESAKPA TSTTQAAAPT TLVTSAKPTA 

       310        320        330        340        350        360 
TATAGAGDSG SGSCSATAPA TGVVKMYAQC GGMNYSGSTT CESGLTCKQW NPYYHQCVKA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CH476604 Genomic DNA. Translation: EAU32052.1.
RefSeqXP_001216411.1. XM_001216411.1.

3D structure databases

ProteinModelPortalQ0CEU4.
SMRQ0CEU4. Positions 324-358.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADATEAT00003463; CADATEAP00003463; CADATEAG00003463.
GeneID4322940.

Phylogenomic databases

eggNOGNOG120437.
HOGENOMHOG000158937.
OMAGYIDSPP.
OrthoDBEOG7KM64H.

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_ASPTN
AccessionPrimary (citable) accession number: Q0CEU4
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: October 17, 2006
Last modified: November 13, 2013
This is version 24 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