Reviewed,
UniProtKB/Swiss-Prot Q7Z9M7 (GUN7_TRIRE)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended 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 |
| ||||
| Organism | Trichoderma reesei (Hypocrea jecorina) | ||||
| Taxonomic identifier | 51453 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Sordariomycetes › Hypocreomycetidae › Hypocreales › Hypocreaceae › Hypocrea |
Protein attributes
| Sequence length | 249 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence 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 | |
| Induction | By cellulose, lactose and sophorose. Ref.1 |
| Sequence similarities | Belongs to the glycosyl hydrolase 61 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Ligand | Calcium Metal-binding |
| Molecular function | Glycosidase Hydrolase |
| PTM | Disulfide bond Glycoprotein |
| Technical term | 3D-structure |
| Gene Ontology (GO) | |
| Biological process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | calcium ion binding Inferred from electronic annotation. Source: UniProtKB-KW cellulase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 19 | 19 | Potential | ||||||||
| Chain | 20 – 249 | 230 | Endoglucanase-7 | PRO_0000364090 | |||||||
Sites | |||||||||||
| Metal binding | 20 | 1 | Divalent metal cation | ||||||||
| Metal binding | 108 | 1 | Divalent metal cation | ||||||||
| Metal binding | 195 | 1 | Divalent metal cation | ||||||||
Amino acid modifications | |||||||||||
| Glycosylation | 25 | 1 | N-linked (GlcNAc...) | ||||||||
| Disulfide bond | 78 ↔ 198 | ||||||||||
| Disulfide bond | 120 ↔ 124 | ||||||||||
Sequences
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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 | |||||||||||||
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| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH61. Glycoside Hydrolase Family 61. | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR003961. FN_III. IPR005103. Glyco_hydro_61. [Graphical view] | ||||||||||||
| Pfam | PF03443. Glyco_hydro_61. 1 hit. [Graphical view] | ||||||||||||
| SMART | SM00060. FN3. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | GUN7_TRIRE | ||||||||
| Accession | Primary (citable) accession number: Q7Z9M7 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (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 |

Clusters with


