Q7SID7 (LYS_ANTMY) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 31, 2011.
Version 34.
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: Lysozyme EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase |
| Organism | Antheraea mylitta (Tasar silkworm) |
| Taxonomic identifier | 34739 [NCBI] |
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Lepidoptera › Glossata › Ditrysia › Bombycoidea › Saturniidae › Saturniinae › Saturniini › Antheraea |
Protein attributes
| Sequence length | 120 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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. Ref.1 |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | 3D-structure 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 |
| 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 – 120 | 120 | Lysozyme | PRO_0000235825 | ||||||||||||||||||||||||||||
Sites | ||||||||||||||||||||||||||||||||
| Active site | 32 | 1 | By similarity UniProtKB P00698 | |||||||||||||||||||||||||||||
| Active site | 50 | 1 | By similarity UniProtKB P00698 | |||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||
| Disulfide bond | 6 ↔ 120 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 27 ↔ 110 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 62 ↔ 76 | Ref.1 | ||||||||||||||||||||||||||||||
| Disulfide bond | 72 ↔ 90 | Ref.1 | ||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||
| Helix | 5 – 14 | 10 | ||||||||||||||||||||||||||||||
| Helix | 19 – 21 | 3 | ||||||||||||||||||||||||||||||
| Helix | 22 – 32 | 11 | ||||||||||||||||||||||||||||||
| Turn | 33 – 35 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 36 – 38 | 3 | ||||||||||||||||||||||||||||||
| Beta strand | 45 – 47 | 3 | ||||||||||||||||||||||||||||||
| Turn | 52 – 55 | 4 | ||||||||||||||||||||||||||||||
| Turn | 58 – 61 | 4 | ||||||||||||||||||||||||||||||
| Beta strand | 62 – 67 | 6 | ||||||||||||||||||||||||||||||
| Helix | 76 – 80 | 5 | ||||||||||||||||||||||||||||||
| Beta strand | 81 – 83 | 3 | ||||||||||||||||||||||||||||||
| Helix | 85 – 98 | 14 | ||||||||||||||||||||||||||||||
| Turn | 99 – 102 | 4 | ||||||||||||||||||||||||||||||
| Helix | 104 – 109 | 6 | ||||||||||||||||||||||||||||||
| Beta strand | 110 – 112 | 3 | ||||||||||||||||||||||||||||||
Sequences
| ||||||||||||||||||
References
| [1] | "Structure of the induced antibacterial protein from tasar silkworm, Antheraea mylitta. Implications to molecular evolution." Jain D., Nair D.T., Swaminathan G.J., Abraham E.G., Nagaraju J., Salunke D.M. J. Biol. Chem. 276:41377-41382(2001) [PubMed: 11522783] [Abstract] Cited for: PROTEIN SEQUENCE OF 1-32, X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS). |
| + | Additional computationally mapped references. |
Cross-references
3D structure databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| PDBe RCSB PDB PDBj |
| ||||||||||||
| ProteinModelPortal | Q7SID7. | ||||||||||||
| SMR | Q7SID7. Positions 1-120. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protein family/group databases | |||||||||||||
| CAZy | GH22. Glycoside Hydrolase Family 22. | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Family and domain databases | |||||||||||||
| InterPro | IPR001916. Glyco_hydro_22. IPR019799. Glyco_hydro_22_CS. IPR000974. Glyco_hydro_22_lys. IPR023346. Lysozyme-like_dom. [Graphical view] | ||||||||||||
| Pfam | PF00062. Lys. 1 hit. [Graphical view] | ||||||||||||
| PRINTS | PR00137. LYSOZYME. PR00135. LYZLACT. | ||||||||||||
| SMART | SM00263. LYZ1. 1 hit. [Graphical view] | ||||||||||||
| SUPFAM | SSF53955. SSF53955. 1 hit. | ||||||||||||
| PROSITE | PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit. PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit. [Graphical view] | ||||||||||||
| ProtoNet | Search... | ||||||||||||
Entry information
| Entry name | LYS_ANTMY | ||||||||
| Accession | Primary (citable) accession number: Q7SID7 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
Relevant documents
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with