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P85218 (GUN1_TRIVI) Reviewed, UniProtKB/Swiss-Prot

Last modified June 28, 2011. Version 14. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Endoglucanase 1

EC=3.2.1.4
Alternative name(s):
Endo-1,4-beta-D-glucanase 1
OrganismTrichoderma viride (Hypocrea rufa)
Taxonomic identifier5547 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeHypocrea

Protein attributes

Sequence length15 AA.
Sequence statusFragment.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Has endoglucanase activity on carboxymethylcellulose (CMC). Ref.1

Catalytic activity

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

Subcellular location

Secreted Ref.1.

Biophysicochemical properties

pH dependence:

Optimum pH is 5.0. Ref.1

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   Molecular functionGlycosidase
Hydrolase
   Technical termDirect protein sequencing
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: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›15›15Endoglucanase 1
PRO_0000315940

Experimental info

Non-terminal residue151

Sequences

Sequence LengthMass (Da)Tools
P85218 [UniParc].

Last modified January 15, 2008. Version 1.
Checksum: 0ED77433D6F953B4

FASTA151,759
        10 
SYPNKQPYGP SGFWM 

« Hide

References

[1]"Purification, characterization and N-terminal sequence analysis of novel endo-beta-1,4-D-glucanase from Trichoderma viride."
Chaudhary N., Sharma B.C.
Submitted (JUL-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE, FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Strain: MTCC 167.

Cross-references

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameGUN1_TRIVI
AccessionPrimary (citable) accession number: P85218
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 15, 2008
Last modified: June 28, 2011
This is version 14 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries