Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q7Z9M7 (GUN7_HYPJQ) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 31. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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-7

EC=3.2.1.4
Alternative name(s):
Cellulase-61B
Short name=Cel61B
Endo-1,4-beta-glucanase VII
Short name=EGVII
Endoglucanase VII
Endoglucanase-61B
Gene names
Name:cel61b
Synonyms:egl7
ORF Names:TRIREDRAFT_120961
OrganismHypocrea jecorina (strain QM6a) (Trichoderma reesei) [Complete proteome]
Taxonomic identifier431241 [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.3

Cofactor

Calcium Probable.

Subunit structure

Monomer. Ref.3

Subcellular location

Secreted Ref.3.

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
Complete 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: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

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

Experimental info

Sequence conflict1181A → V in AAP57753. Ref.1

Secondary structure

................................... 249
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q7Z9M7 [UniParc].

Last modified November 16, 2011. Version 2.
Checksum: 1BD57A744D48F0EF

FASTA24926,800
        10         20         30         40         50         60 
MKSCAILAAL GCLAGSVLGH GQVQNFTING QYNQGFILDY YYQKQNTGHF PNVAGWYAED 

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

       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

« Hide 'large scale' 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]"Genome sequencing and analysis of the biomass-degrading fungus Trichoderma reesei (syn. Hypocrea jecorina)."
Martinez D., Berka R.M., Henrissat B., Saloheimo M., Arvas M., Baker S.E., Chapman J., Chertkov O., Coutinho P.M., Cullen D., Danchin E.G., Grigoriev I.V., Harris P., Jackson M., Kubicek C.P., Han C.S., Ho I., Larrondo L.F. expand/collapse author list , de Leon A.L., Magnuson J.K., Merino S., Misra M., Nelson B., Putnam N., Robbertse B., Salamov A.A., Schmoll M., Terry A., Thayer N., Westerholm-Parvinen A., Schoch C.L., Yao J., Barabote R., Nelson M.A., Detter C., Bruce D., Kuske C.R., Xie G., Richardson P., Rokhsar D.S., Lucas S.M., Rubin E.M., Dunn-Coleman N., Ward M., Brettin T.S.
Nat. Biotechnol. 26:553-560(2008) [PubMed: 18454138] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: QM6a.
[3]"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

EMBL
GenBank
DDBJ
AY281372 mRNA. Translation: AAP57753.1.
GL985060 Genomic DNA. Translation: EGR50392.1.

3D structure databases

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

Protein family/group databases

CAZyGH61. Glycoside Hydrolase Family 61.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16506.

Family and domain databases

InterProIPR003961. Fibronectin_type3.
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_HYPJQ
AccessionPrimary (citable) accession number: Q7Z9M7
Secondary accession number(s): G0RER9
Entry history
Integrated into UniProtKB/Swiss-Prot: February 10, 2009
Last sequence update: November 16, 2011
Last modified: January 25, 2012
This is version 31 of the entry and version 2 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families