P22669 (GUN_ASPAC) Reviewed, UniProtKB/Swiss-Prot
Last modified
April 3, 2013.
Version 76.
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): Cellulase Endo-1,4-beta-glucanase Endoglucanase I FI-CMCase |
| Organism | Aspergillus aculeatus |
| Taxonomic identifier | 5053 [NCBI] |
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Aspergillus![]() |
Protein attributes
| Sequence length | 237 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)
| Catalytic activity | Endohydrolysis of (1->4)-beta-D-glucosidic linkages in cellulose, lichenin and cereal beta-D-glucans. |
| Subcellular location | |
| Induction | By cellulosic materials and hemicelluloses. |
| Miscellaneous | Will also hydrolyze 1,4-linkages in beta-D-glucans also containing 1,3-linkages. |
| Sequence similarities | Belongs to the glycosyl hydrolase 12 (cellulase H) family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cellulose degradation Polysaccharide degradation |
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Glycosidase Hydrolase |
| PTM | Pyrrolidone carboxylic acid |
| Technical term | Direct protein sequencing |
| 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 | cellulase activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Complete nucleotide sequence of a gene coding for Aspergillus aculeatus cellulase (FI-CMCase)." Ooi T., Shinmyo A., Okada H., Murao S., Kawaguchi T., Arai M. Nucleic Acids Res. 18:5884-5884(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: F-50. |
| [2] | "Cloning and sequence analysis of a cDNA for cellulase (FI-CMCase) from Aspergillus aculeatus." Ooi T., Shinmyo A., Okada H., Hara S., Ikenaka T., Murao S., Arai M. Curr. Genet. 18:217-222(1990) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE. Strain: F-50. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | D00546 Genomic DNA. Translation: BAA00435.1. X52525 mRNA. Translation: CAA36757.1. |
| PIR | S12610. |
3D structure databases | |
| ProteinModelPortal | P22669. |
| SMR | P22669. Positions 21-236. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH12. Glycoside Hydrolase Family 12. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| Gene3D | 2.60.120.180. 1 hit. |
| InterPro | IPR008985. ConA-like_lec_gl_sf. IPR013319. Glyco_hydro_11/12. IPR002594. Glyco_hydro_12. [Graphical view] |
| Pfam | PF01670. Glyco_hydro_12. 1 hit. [Graphical view] |
| SUPFAM | SSF49899. ConA_like_lec_gl. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | GUN_ASPAC | ||||||||
| Accession | Primary (citable) accession number: P22669 | ||||||||
| 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 |
| SIMILARITY comments Index of protein domains and families |

Clusters with
