P61631 (LYSC_COLAN)
Reviewed,
UniProtKB/Swiss-Prot
Last modified
August 10, 2010.
Version 36.
History...
Clusters with 
Names and origin
| Protein names | Recommended name: Lysozyme C EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase C | ||||
| Gene names |
| ||||
| Organism | Colobus angolensis (Angolan colobus) | ||||
| Taxonomic identifier | 54131 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Cercopithecidae › Colobinae › Colobus |
Protein attributes
| Sequence length | 148 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 | Lysozymes have primarily a bacteriolytic function; those in tissues and body fluids are associated with the monocyte-macrophage system and enhance the activity of immunoagents. |
| 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. |
| Subunit structure | Monomer. |
| Miscellaneous | Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides. |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond |
| 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 |
| 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 | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
| Signal peptide | 1 – 18 | 18 | By similarity | ||||||||
| Chain | 19 – 148 | 130 | Lysozyme C | PRO_0000018462 | |||||||
Sites | |||||||||||
| Active site | 53 | 1 | By similarity | ||||||||
| Active site | 71 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 24 ↔ 146 | By similarity | |||||||||
| Disulfide bond | 48 ↔ 134 | By similarity | |||||||||
| Disulfide bond | 83 ↔ 99 | By similarity | |||||||||
| Disulfide bond | 95 ↔ 113 | By similarity | |||||||||
Sequences
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References
| [1] | "Episodic adaptive evolution of primate lysozymes." Messier W., Stewart C.B. Nature 385:151-154(1997) [PubMed: 8990116] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Blood. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U76937  U76936 Genomic DNA. Translation: AAB41215.1. |
3D structure databases | |
| ProteinModelPortal | P61631. |
| SMR | P61631. Positions 19-148. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Phylogenomic databases | |
| HOVERGEN | HBG052297. |
Family and domain databases | |
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. [Graphical view] |
| Pfam | PF00062. Lys. 1 hit. [Graphical view] |
| PRINTS | PR00137. LYSOZYME. PR00135. LYZLACT. |
| SMART | SM00263. LYZ1. 1 hit. [Graphical view] |
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | LYSC_COLAN | ||||||||
| Accession | Primary (citable) accession number: P61631 Secondary accession number(s): P79151, P79698 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |
