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A1C4H2 (EGLD_ASPCL) Reviewed, UniProtKB/Swiss-Prot

Last modified November 13, 2013. Version 25. 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:ACLA_059790
OrganismAspergillus clavatus (strain ATCC 1007 / CBS 513.65 / DSM 816 / NCTC 3887 / NRRL 1) [Complete proteome]
Taxonomic identifier344612 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaEurotiomycetesEurotiomycetidaeEurotialesAspergillaceaeAspergillus

Protein attributes

Sequence length353 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 – 353334Probable endo-beta-1,4-glucanase D
PRO_0000394060

Regions

Domain315 – 35137CBM1
Region20 – 234215Catalytic
Region235 – 31177Ser/Thr-rich linker

Sites

Active site1641Proton donor By similarity
Active site2101Nucleophile By similarity

Amino acid modifications

Glycosylation3271N-linked (GlcNAc...) Potential
Disulfide bond323 ↔ 340 By similarity
Disulfide bond334 ↔ 350 By similarity

Sequences

Sequence LengthMass (Da)Tools
A1C4H2 [UniParc].

Last modified January 23, 2007. Version 1.
Checksum: CA30252C3CAB5C4C

FASTA35336,822
        10         20         30         40         50         60 
MKSTFGLLAL AAAAKMAHAH ATVQAIWING VDQGAGNSAS GYIRSPPNNS PLVDVTSADM 

        70         80         90        100        110        120 
TCNVNGKNPV AKTLPVKAGD KITFEWHHTD RSPSDDIIAS SHRGPIMVYM APTAKGAAGN 

       130        140        150        160        170        180 
GWVKIAEEGY SNGKWAVDNL IANRGKHSIV VPDVPAGDYL FRPEIIALHE GNRLGGAQFY 

       190        200        210        220        230        240 
MECVQVKVTS NGANALPAGV SIPGAYKATD PGVHFDIYNS FSSYPMPGPA VWNGASAAGS 

       250        260        270        280        290        300 
APAPTAAPTQ KPVVTAAPTT LATLVKPTTT TAAAPAETDS CDGDDDDYET ETPAPQASAT 

       310        320        330        340        350 
QAPAPQRPAP QTPSGSVKEW YQCGGINYTG AKNCESGLVC KEWNPYYHQC IKA 

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DS026990 Genomic DNA. Translation: EAW15312.1.
RefSeqXP_001276738.1. XM_001276737.1.

3D structure databases

ProteinModelPortalA1C4H2.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblFungiCADACLAT00005694; CADACLAP00005569; CADACLAG00005694.
GeneID4708945.
KEGGact:ACLA_059790.

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_ASPCL
AccessionPrimary (citable) accession number: A1C4H2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 18, 2010
Last sequence update: January 23, 2007
Last modified: November 13, 2013
This is version 25 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