A1DJ47 (EGLC_NEOFI) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 35.
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: Probable glucan endo-1,3-beta-glucosidase eglC EC=3.2.1.39 Alternative name(s): Endo-1,3-beta-glucanase eglC Laminarinase eglC | ||||
| Gene names |
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| Organism | Neosartorya fischeri (strain ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181) (Aspergillus fischerianus) [Complete proteome] | ||||
| Taxonomic identifier | 331117 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Neosartorya › ![]() |
Protein attributes
| Sequence length | 450 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Glucanases play a role in cell expansion during growth, in cell-cell fusion during mating, and in spore release during sporulation. This enzyme may be involved in beta-glucan degradation and also function biosynthetically as a transglycosylase By similarity. |
| Catalytic activity | Hydrolysis of (1->3)-beta-D-glucosidic linkages in (1->3)-beta-D-glucans. |
| Subcellular location | Cell membrane; Lipid-anchor › GPI-anchor By similarity. Secreted › cell wall By similarity. Note: Covalently-linked GPI-modified cell wall protein By similarity. |
| Post-translational modification | The GPI-anchor is attached to the protein in the endoplasmic reticulum and serves to target the protein to the cell surface. There, the glucosamine-inositol phospholipid moiety is cleaved off and the GPI-modified mannoprotein is covalently attached via its lipidless GPI glycan remnant to the 1,6-beta-glucan of the outer cell wall layer By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 17 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Carbohydrate metabolism Cell wall biogenesis/degradation Polysaccharide degradation |
| Cellular component | Cell membrane Cell wall Membrane Secreted |
| Domain | Signal |
| Molecular function | Hydrolase |
| PTM | GPI-anchor Glycoprotein Lipoprotein |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological_process | polysaccharide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Cellular_component | anchored to membrane Inferred from electronic annotation. Source: UniProtKB-KW cell wallInferred from electronic annotation. Source: UniProtKB-SubCell extracellular regionInferred from electronic annotation. Source: UniProtKB-KW plasma membraneInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | glucan endo-1,3-beta-D-glucosidase 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 – 18 | 18 | Potential | ||||||
| Chain | 19 – 427 | 409 | Probable glucan endo-1,3-beta-glucosidase eglC | PRO_0000395151 | |||||
| Propeptide | 428 – 450 | 23 | Removed in mature form Potential | PRO_0000395152 | |||||
Regions | |||||||||
| Compositional bias | 309 – 435 | 127 | Ser-rich | ||||||
Sites | |||||||||
| Active site | 128 | 1 | Nucleophile By similarity | ||||||
| Active site | 239 | 1 | Proton donor By similarity | ||||||
Amino acid modifications | |||||||||
| Lipidation | 427 | 1 | GPI-anchor amidated asparagine Potential | ||||||
| Glycosylation | 183 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 365 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 371 | 1 | N-linked (GlcNAc...) Potential | ||||||
Sequences
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References
| [1] | "Genomic islands in the pathogenic filamentous fungus Aspergillus fumigatus." Fedorova N.D., Khaldi N., Joardar V.S., Maiti R., Amedeo P., Anderson M.J., Crabtree J., Silva J.C., Badger J.H., Albarraq A., Angiuoli S., Bussey H., Bowyer P., Cotty P.J., Dyer P.S., Egan A., Galens K., Fraser-Liggett C.M. Nierman W.C.PLoS Genet. 4:E1000046-E1000046(2008) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 1020 / DSM 3700 / FGSC A1164 / NRRL 181. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | DS027697 Genomic DNA. Translation: EAW16736.1. |
| RefSeq | XP_001258633.1. XM_001258632.1. |
3D structure databases | |
| ProteinModelPortal | A1DJ47. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| EnsemblFungi | CADNFIAT00000381; CADNFIAP00000372; CADNFIAG00000381. |
| GeneID | 4585162. |
| KEGG | nfi:NFIA_000800. |
Phylogenomic databases | |
| eggNOG | COG5309. |
| HOGENOM | HOG000179527. |
Family and domain databases | |
| Gene3D | 3.20.20.80. 1 hit. |
| InterPro | IPR013781. Glyco_hydro_catalytic_dom. IPR017853. Glycoside_hydrolase_SF. [Graphical view] |
| SUPFAM | SSF51445. Glyco_hydro_cat. 1 hit. |
| PROSITE | PS00587. GLYCOSYL_HYDROL_F17. False negative. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | EGLC_NEOFI | ||||||||
| Accession | Primary (citable) accession number: A1DJ47 | ||||||||
| 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
