Reviewed,
UniProtKB/Swiss-Prot Q6L6Q6 (LYS_CRAGI)
Last modified
June 16, 2009.
Version 21.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase | ||
| Gene names |
| ||
| Organism | Crassostrea gigas (Pacific oyster) (Crassostrea angulata) | ||
| Taxonomic identifier | 29159 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Mollusca › Bivalvia › Pteriomorphia › Ostreoida › Ostreoidea › Ostreidae › Crassostrea |
Protein attributes
| Sequence length | 137 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at transcript level. |
General annotation (Comments)
| Function | May play a role in digestion and in the host defense mechanisms against invading microbes. |
| Catalytic activity | Hydrolysis of (1->4)-beta-linkages between N-acetylmuramic acid and N-acetyl-D-glucosamine residues in a peptidoglycan and between N-acetyl-D-glucosamine residues in chitodextrins. |
| Subcellular location | |
| Tissue specificity | Expressed in the basophil cells of the oyster digestive gland. Ref.1 |
| Sequence similarities | Belongs to the lysozyme type I family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Domain | Signal |
| Molecular function | Antibiotic Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| Gene Ontology (GO) | |
| Biological process | cytolysis Inferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW metabolic processInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | extracellular region Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | lysozyme activity Inferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Cloning of cDNAs and hybridization analysis of lysozymes from two oyster species, Crassostrea gigas and Ostrea edulis." Matsumoto T., Nakamura A.M., Takahashi K.G. Comp. Biochem. Physiol. 145B:325-330(2006) [PubMed: 16996284] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY. |
Cross-references
Sequence databases | |
|---|---|
| AB179775 mRNA. Translation: BAD19059.1. | |
3D structure databases | |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Enzyme and pathway databases | |
| BRENDA | 3.2.1.17. 8516. |
Family and domain databases | |
| InterPro | IPR008597. Destabilase. [Graphical view] |
| PANTHER | PTHR11195. Destabilase. 1 hit. |
| Pfam | PF05497. Destabilase. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYS_CRAGI | ||||||||
| Accession | Primary (citable) accession number: Q6L6Q6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


