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Reviewed, UniProtKB/Swiss-Prot Q7Z9M7 (GUN7_TRIRE)

Last modified June 16, 2009. Version 21. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Endoglucanase-7
    EC=3.2.1.4
Alternative name(s):
    Endoglucanase VII
    Endo-1,4-beta-glucanase VII
      Short name=EGVII
    Endoglucanase-61B
    Cellulase-61B
      Short name=Cel61B
Gene names
Name: cel61b
Synonyms: egl7
OrganismTrichoderma reesei (Hypocrea jecorina)
Taxonomic identifier51453 [NCBI]
Taxonomic lineageEukaryotaFungiDikaryaAscomycotaPezizomycotinaSordariomycetesHypocreomycetidaeHypocrealesHypocreaceaeHypocrea

Protein attributes

Sequence length249 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Has low levels of endoglucanase activity. May be involved in the degradation of cellulose or lignocellulose, chitin, or other polysaccharides.

Catalytic activity

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

Cofactor

Calcium Probable.

Subunit structure

Monomer. Ref.2

Subcellular location

Secreted. Ref.2

Induction

By cellulose, lactose and sophorose. Ref.1

Sequence similarities

Belongs to the glycosyl hydrolase 61 family.

Ontologies

Keywords
   Biological processCarbohydrate metabolism
Cellulose degradation
Polysaccharide degradation
   Cellular componentSecreted
   DomainSignal
   LigandCalcium
Metal-binding
   Molecular functionGlycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
   Technical term3D-structure
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 functioncalcium ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

cellulase activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1919 Potential
Chain20 – 249230Endoglucanase-7
PRO_0000364090

Sites

Metal binding201Divalent metal cation
Metal binding1081Divalent metal cation
Metal binding1951Divalent metal cation

Amino acid modifications

Glycosylation251N-linked (GlcNAc...)
Disulfide bond78 ↔ 198
Disulfide bond120 ↔ 124

Sequences

Sequence LengthMass (Da)Tools
Q7Z9M7-1 [UniParc].

Last modified October 1, 2003. Version 1.
Checksum: 1BC7F179D657E0EF

FASTA24926,828
        10         20         30         40         50         60 
MKSCAILAAL GCLAGSVLGH GQVQNFTING QYNQGFILDY YYQKQNTGHF PNVAGWYAED 

        70         80         90        100        110        120 
LDLGFISPDQ YTTPDIVCHK NAAPGAISAT AAAGSNIVFQ WGPGVWPHPY GPIVTYVVEC 

       130        140        150        160        170        180 
SGSCTTVNKN NLRWVKIQEA GINYNTQVWA QQDLINQGNK WTVKIPSSLR PGNYVFRHEL 

       190        200        210        220        230        240 
LAAHGASSAN GMQNYPQCVN IAVTGSGTKA LPAGTPATQL YKPTDPGILF NPYTTITSYT 


IPGPALWQG 

« Hide

References

[1]"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: 12788920] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], INDUCTION.
Strain: QM6a.
[2]"The first structure of a glycoside hydrolase family 61 member, Cel61B from Hypocrea jecorina, at 1.6 A resolution."
Karkehabadi S., Hansson H., Kim S., Piens K., Mitchinson C., Sandgren M.
J. Mol. Biol. 383:144-154(2008) [PubMed: 18723026] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 20-249, SUBUNIT, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION.
Strain: QM6a.

Cross-references

Sequence databases

AY281372 mRNA. Translation: AAP57753.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
2VTCX-ray1.60A/B1-249[»]
ModBaseSearch...

Protein family/group databases

CAZyGH61. Glycoside Hydrolase Family 61.

Family and domain databases

InterProIPR003961. FN_III.
IPR005103. Glyco_hydro_61.
[Graphical view]
PfamPF03443. Glyco_hydro_61. 1 hit.
[Graphical view]
SMARTSM00060. FN3. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameGUN7_TRIRE
AccessionPrimary (citable) accession number: Q7Z9M7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: October 1, 2003
Last modified: June 16, 2009
This is version 21 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectFPAP (Fungal Proteome Annotation Project)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents