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O14405 (GUN4_HYPJE) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 70. 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:
Endoglucanase-4

EC=3.2.1.4
Alternative name(s):
Cellulase IV
Cellulase-61A
Short name=Cel61A
Endo-1,4-beta-glucanase IV
Short name=EGIV
Endoglucanase IV
Endoglucanase-61A
Gene names
Name:cel61a
Synonyms:egl4
OrganismHypocrea jecorina (Trichoderma reesei)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeTrichoderma

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has endoglucanase activity on substrates containing beta-1,4 glycosidic bonds, like in carboxymethylcellulose (CMC), hydroxyethylcellulose (HEC) and beta-glucan. May be involved in the degradation of complex natural cellulosic substrates. Ref.2

Catalytic activity

Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. Ref.1 Ref.2

Subcellular location

Secreted.

Induction

By cellulose, cellobiose, lactose and sophorose. Ref.1 Ref.3

Post-translational modification

May also be O-glycosylated.

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
Gene Ontology (GO)
   Biological_processcellulose catabolic process

Inferred from direct assay Ref.1. Source: UniProtKB

   Cellular_componentextracellular region

Inferred from direct assay Ref.1. Source: UniProtKB

   Molecular_functioncellulase activity

Inferred from direct assay Ref.1. Source: UniProtKB

cellulose binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2121 Potential
Chain22 – 344323Endoglucanase-4
PRO_0000008032

Regions

Domain307 – 34337CBM1
Region22 – 256235Catalytic Potential
Region257 – 30751Linker Potential

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Glycosylation1581N-linked (GlcNAc...) Potential
Disulfide bond315 ↔ 332 By similarity
Disulfide bond326 ↔ 342 By similarity

Sequences

Sequence LengthMass (Da)Tools
O14405 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: 7FBF1C4AB705350C

FASTA34435,511
        10         20         30         40         50         60 
MIQKLSNLLV TALAVATGVV GHGHINDIVI NGVWYQAYDP TTFPYESNPP IVVGWTAADL 

        70         80         90        100        110        120 
DNGFVSPDAY QNPDIICHKN ATNAKGHASV KAGDTILFQW VPVPWPHPGP IVDYLANCNG 

       130        140        150        160        170        180 
DCETVDKTTL EFFKIDGVGL LSGGDPGTWA SDVLISNNNT WVVKIPDNLA PGNYVLRHEI 

       190        200        210        220        230        240 
IALHSAGQAN GAQNYPQCFN IAVSGSGSLQ PSGVLGTDLY HATDPGVLIN IYTSPLNYII 

       250        260        270        280        290        300 
PGPTVVSGLP TSVAQGSSAA TATASATVPG GGSGPTSRTT TTARTTQASS RPSSTPPATT 

       310        320        330        340 
SAPAGGPTQT LYGQCGGSGY SGPTRCAPPA TCSTLNPYYA QCLN 

« Hide

References

[1]"cDNA cloning of a Trichoderma reesei cellulase and demonstration of endoglucanase activity by expression in yeast."
Saloheimo M., Nakari-Setaelae T., Tenkanen M., Penttilae M.
Eur. J. Biochem. 249:584-591(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], CATALYTIC ACTIVITY, INDUCTION.
Strain: ATCC 56765 / Rut C-30.
[2]"Homologous expression and characterization of Cel61A (EG IV) of Trichoderma reesei."
Karlsson J., Saloheimo M., Siika-aho M., Tenkanen M., Penttilae M., Tjerneld F.
Eur. J. Biochem. 268:6498-6507(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
[3]"Transcriptional regulation of biomass-degrading enzymes in the filamentous fungus Trichoderma reesei."
Foreman P.K., Brown D., Dankmeyer L., Dean R., Diener S., Dunn-Coleman N.S., Goedegebuur F., Houfek T.D., England G.J., Kelley A.S., Meerman H.J., Mitchell T., Mitchinson C., Olivares H.A., Teunissen P.J.M., Yao J., Ward M.
J. Biol. Chem. 278:31988-31997(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11113 mRNA. Translation: CAA71999.1.

3D structure databases

ProteinModelPortalO14405.
SMRO14405. Positions 308-343.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING51453.JGI73643.

Protein family/group databases

CAZyCBM1. Carbohydrate-Binding Module Family 1.
GH61. Glycoside Hydrolase Family 61.
mycoCLAPPMO9A_TRIRE.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

eggNOGNOG126663.
OMAFFKIDGA.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16504.

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 nameGUN4_HYPJE
AccessionPrimary (citable) accession number: O14405
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: January 1, 1998
Last modified: October 16, 2013
This is version 70 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