Reviewed,
UniProtKB/Swiss-Prot Q7LZR3 (LYG_CASCA)
Last modified
June 16, 2009.
Version 33.
History...
Clusters with 100%,
90%,
50% identity |
Documents (2) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme g EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase Goose-type lysozyme |
| Organism | Casuarius casuarius (Australian cassowary) (Double-wattled cassowary) |
| Taxonomic identifier | 8787 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Archosauria › Dinosauria › Saurischia › Theropoda › Coelurosauria › Aves › Palaeognathae › Casuariiformes › Casuariidae › Casuarius |
Protein attributes
| Sequence length | 185 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| 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 | |
| Miscellaneous | Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase By similarity. |
| Sequence similarities | Belongs to the glycosyl hydrolase 23 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Secreted |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond Pyrrolidone carboxylic acid |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | cell wall macromolecule catabolic process Inferred from electronic annotation. Source: InterPro cytolysisInferred from electronic annotation. Source: UniProtKB-KW defense response to bacteriumInferred from electronic annotation. Source: UniProtKB-KW peptidoglycan catabolic processInferred from electronic annotation. Source: InterPro |
| 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)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||||
Molecule processing | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 185 | 185 | Lysozyme g | PRO_0000193514 | |||||||
Sites | |||||||||||
| Active site | 73 | 1 | By similarity | ||||||||
| Active site | 86 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Modified residue | 1 | 1 | Pyrrolidone carboxylic acid | ||||||||
| Disulfide bond | 4 ↔ 60 | By similarity | |||||||||
| Disulfide bond | 18 ↔ 29 | By similarity | |||||||||
Sequences
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References
| [1] | Thammasirirak S., Torikata T., Takami K., Murata K., Araki T. Submitted (OCT-2000) to the PIR data bank Cited for: PROTEIN SEQUENCE. |
Cross-references
Sequence databases | |
|---|---|
| PIR | A59351. |
3D structure databases | |
| SMR | Q7LZR3. Positions 1-185. |
| ModBase | Search... |
Phylogenomic databases | |
| HOVERGEN | Q7LZR3. |
Family and domain databases | |
| InterPro | IPR002152. Glyco_hydro_23. IPR008258. Lytic_TGlycosylase-like_cat. [Graphical view] |
| Pfam | PF01464. SLT. 1 hit. [Graphical view] |
| PIRSF | PIRSF001065. Lysozyme_g. 1 hit. |
| PRINTS | PR00749. LYSOZYMEG. |
| ProtoNet | Search... |
Entry information
| Entry name | LYG_CASCA | ||||||||
| Accession | Primary (citable) accession number: Q7LZR3 | ||||||||
| 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


