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Q2US83 (EGLD_ASPOR) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 39. 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:AO090005000531
OrganismAspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold) [Complete proteome]
Taxonomic identifier510516 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length367 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 – 2020 Potential
Chain21 – 367347Probable endo-beta-1,4-glucanase D
PRO_0000394065

Regions

Domain329 – 36537CBM1
Region21 – 235215Catalytic
Region236 – 32590Ser/Thr-rich linker

Sites

Active site1641Proton donor By similarity
Active site2101Nucleophile By similarity

Amino acid modifications

Glycosylation2821N-linked (GlcNAc...) Potential
Disulfide bond337 ↔ 354 By similarity
Disulfide bond348 ↔ 364 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2US83 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: 0C038474B7C681F3

FASTA36738,033
        10         20         30         40         50         60 
MKSSTFGMLA LAAAAKLVSA HATVHAVWIN DVDQGEGNSE SGYIRSPPSN SPITDVTSKD 

        70         80         90        100        110        120 
MTCNVNNKAT AKTLEVKAGD KITFEWHHDS RSDSDDIIAS SHKGPIMVYM APTEKGTAGN 

       130        140        150        160        170        180 
GWVKIAEDGY TDGTWAVDTL IKNRGKHSVT VPDVAAGEYL FRPEIIALHE GNRQGGAQFY 

       190        200        210        220        230        240 
MECVQVKVTS SGSKTLPEGV SIPGAYTATD KGILFDIYNS FDSYPFPGPA VWDGASGSSS 

       250        260        270        280        290        300 
SPSASASASA PAATSAAPAP SSFTTIAKQP ATSSTEAPST ENTSTTSTIV STTAAASATA 

       310        320        330        340        350        360 
PATPSSTSAI ASSAASTNSV PQPSSNAGGA VKEWYQCGGL NYKGSTQCEE GLTCKKWNPY 


YYQCISA 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP007151 Genomic DNA. Translation: BAE55582.1.

3D structure databases

ProteinModelPortalQ2US83.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADAORAT00002518; CADAORAP00002480; CADAORAG00002518.

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]
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_ASPOR
AccessionPrimary (citable) accession number: Q2US83
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 24, 2006
Last modified: November 13, 2013
This is version 39 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