P23044 (GUN_ROBSP) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 71.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Endoglucanase 1 EC=3.2.1.4 Alternative name(s): Carboxymethyl-cellulase I Short name=CMCase I Endo-1,4-beta-glucanase Endoglucanase I | ||
| Gene names |
| ||
| Organism | Robillarda sp. (strain Y-20) | ||
| Taxonomic identifier | 72589 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › mitosporic Ascomycota › Robillarda![]() |
Protein attributes
| Sequence length | 385 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 | Active towards carboxymethyl cellulose. |
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Pathway | |
| Sequence similarities | Belongs to the glycosyl hydrolase 5 (cellulase A) family. |
| Sequence caution | The sequence described in Ref.2 differs from that shown. Reason: Frameshift at several positions. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological_process | cellulose catabolic process Inferred from electronic annotation. Source: UniProtKB-UniPathway |
| Molecular_function | cellulase activity Inferred 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 – 17 | 17 | Ref.2 | ||||||
| Chain | 18 – 385 | 368 | Endoglucanase 1 | PRO_0000184049 | |||||
Sites | |||||||||
| Active site | 176 | 1 | Proton donor By similarity | ||||||
| Active site | 284 | 1 | Nucleophile By similarity | ||||||
Amino acid modifications | |||||||||
| Glycosylation | 93 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 140 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 200 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 237 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 289 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 331 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 27 – 28 | 2 | SS → GN AA sequence Ref.2 | ||||||
Sequences
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References
| [1] | "Endoglucanase gene from cellulolytic fungi, Robillarda sp. Y-20." Kashiwagi Y. Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "Cloning and sequencing of the endo-cellulase cDNA from Robillarda sp. Y-20." Yoshigi N., Taniguchi H., Sasaki T. J. Biochem. 108:388-392(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 33-385, PROTEIN SEQUENCE OF 18-35. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | AB030819 Genomic DNA. Translation: BAA90480.1. |
3D structure databases | |
| ProteinModelPortal | P23044. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH5. Glycoside Hydrolase Family 5. |
| mycoCLAP | EGL5A_ROBSP. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Enzyme and pathway databases | |
| UniPathway | UPA00696. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR001547. Glyco_hydro_5. IPR018087. Glyco_hydro_5_CS. IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| Pfam | PF00150. Cellulase. 1 hit. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00659. GLYCOSYL_HYDROL_F5. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | GUN_ROBSP | ||||||||
| Accession | Primary (citable) accession number: P23044 Secondary accession number(s): Q9P981 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with
