Reviewed,
UniProtKB/Swiss-Prot P83451 (ASPG_ASOTA)
Last modified
June 16, 2009.
Version 26.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: N(4)-(beta-N-acetylglucosaminyl)-L-asparaginase EC=3.5.1.26 Alternative name(s): Glycosylasparaginase Aspartylglucosaminidase Short name=AGA N4-(N-acetyl-beta-glucosaminyl)-L-asparagine amidase Cleaved into the following 2 chains: 1- Recommended name: Glycosylasparaginase alpha chain Short name=AGA subunit alpha Alternative name(s): p18 2- Recommended name: Glycosylasparaginase beta chain Short name=AGA subunit beta Alternative name(s): p30 |
| Organism | Asobara tabida (Parasitic wasp) |
| Taxonomic identifier | 58720 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Hymenoptera › Apocrita › Ichneumonoidea › Braconidae › Alysiinae › Asobara |
Protein attributes
| Sequence length | 40 AA. |
| Sequence status | Fragments. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Cleaves the GlcNAc-Asn bond which joins oligosaccharides to the peptide of asparagine-linked glycoproteins By similarity. UniProtKB P20933 |
| Catalytic activity | N(4)-(beta-N-acetyl-D-glucosaminyl)-L-asparagine + H2O = N-acetyl-beta-D-glucosaminylamine + L-aspartate. UniProtKB P20933 |
| Subunit structure | Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Ref.1 |
| Subcellular location | |
| Tissue specificity | Expressed by the venom gland. Ref.1 |
| Post-translational modification | May be N-glycosylated. Ref.1 |
| Sequence similarities | Belongs to the Ntn-hydrolase family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Hydrolase |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | N4-(beta-N-acetylglucosaminyl)-L-asparaginase 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 | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – ›20 | ›20 | Glycosylasparaginase alpha chain Ref.1 | PRO_0000002341 | |||||
| Chain | 21 – ›40 | ›20 | Glycosylasparaginase beta chain Ref.1 | PRO_0000002342 | |||||
Sites | |||||||||
| Active site | 21 | 1 | Nucleophile By similarity UniProtKB P20933 | ||||||
Experimental info | |||||||||
| Non-adjacent residues | 20 – 21 | 2 | |||||||
| Non-terminal residue | 40 | 1 | |||||||
Sequences
References
| [1] | "Identification of an aspartylglucosaminidase-like protein in the venom of the parasitic wasp Asobara tabida (Hymenoptera: Braconidae)." Moreau S.J.M., Cherqui A., Doury G., Dubois F., Fourdrain Y., Sabatier L., Bulet P., Saarela J., Prevost G., Giordanengo P. Insect Biochem. Mol. Biol. 34:485-492(2004) [PubMed: 15110870] [Abstract] Cited for: PROTEIN SEQUENCE, SUBUNIT, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, GLYCOSYLATION. Tissue: Venom. |
Cross-references
3D structure databases | |
|---|---|
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 3.5.1.26. 294119. |
Family and domain databases | |
| InterPro | IPR000246. Peptidase_T2. [Graphical view] |
| Pfam | PF01112. Asparaginase_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ASPG_ASOTA | ||||||||
| Accession | Primary (citable) accession number: P83451 Secondary accession number(s): P83452 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||

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