Reviewed,
UniProtKB/Swiss-Prot P29615 (LYSP_DROME)
Last modified
June 16, 2009.
Version 79.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Lysozyme P EC=3.2.1.17 Alternative name(s): 1,4-beta-N-acetylmuramidase P | ||||
| Gene names |
| ||||
| Organism | Drosophila melanogaster (Fruit fly) [Complete proteome] | ||||
| Taxonomic identifier | 7227 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora |
Protein attributes
| Sequence length | 141 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 | Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food. Ref.1 Ref.2 |
| 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. |
| Tissue specificity | |
| Developmental stage | |
| Sequence similarities | Belongs to the glycosyl hydrolase 22 family. |
Ontologies
| Keywords | |
|---|---|
| Domain | Signal |
| Molecular function | Antimicrobial Bacteriolytic enzyme Glycosidase Hydrolase |
| PTM | Disulfide bond |
| Technical term | Complete proteome |
| 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 | Potential | ||||||||
| Chain | 19 – 141 | 123 | Lysozyme P | PRO_0000018514 | |||||||
Sites | |||||||||||
| Active site | 51 | 1 | By similarity | ||||||||
| Active site | 69 | 1 | By similarity | ||||||||
Amino acid modifications | |||||||||||
| Disulfide bond | 25 ↔ 140 | By similarity | |||||||||
| Disulfide bond | 46 ↔ 130 | By similarity | |||||||||
| Disulfide bond | 81 ↔ 97 | By similarity | |||||||||
| Disulfide bond | 93 ↔ 111 | By similarity | |||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands." Kylsten P., Kimbrell D.A., Daffre S., Samakovlis C., Hultmark D. Mol. Gen. Genet. 232:335-343(1992) [PubMed: 1588905] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S. |
| [2] | "The lysozyme locus in Drosophila melanogaster: an expanded gene family adapted for expression in the digestive tract." Daffre S., Kylsten P., Samakovlis C., Hultmark D. Mol. Gen. Genet. 242:152-162(1994) [PubMed: 8159165] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE. Strain: Canton-S. |
| [3] | "The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. Venter J.C.Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley. |
| [4] | "Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. Lewis S.E.Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION. |
| [5] | Stapleton M., Carlson J.W., Chavez C., Frise E., George R.A., Pacleb J.M., Park S., Wan K.H., Yu C., Celniker S.E. Submitted (MAY-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. |
Cross-references
Sequence databases | |
|---|---|
| X58383 Genomic DNA. Translation: CAA41273.1. AE014296 Genomic DNA. Translation: AAF47452.1. BT023249 mRNA. Translation: AAY55665.1. | |
| PIR | S20915. |
| RefSeq | NP_476828.1. |
| UniGene | Dm.24595 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1GD6 based on UniProtKB P48816. |
| SMR | P29615. Positions 20-141. |
| ModBase | Search... |
Protein family/group databases | |
| CAZy | GH22. Glycoside Hydrolase Family 22. |
Proteomic databases | |
| PRIDE | P29615. |
Genome annotation databases | |
| Ensembl | FBgn0004429. Drosophila melanogaster. [Contig view] |
| GeneID | 38129. |
| KEGG | dme:Dmel_CG9116. |
| NMPDR | fig|7227.3.peg.7492. |
Organism-specific databases | |
| FlyBase | FBgn0004429. LysP. |
Phylogenomic databases | |
| HOGENOM | P29615. |
| OMA | P29615. KRCELAK. |
Enzyme and pathway databases | |
| BioCyc | DMEL-XXX-02:DMEL-XXX-02-014582-MON. |
| BRENDA | 3.2.1.17. 48. |
Gene expression databases | |
| ArrayExpress | P29615. |
| GermOnline | CG9116. Drosophila melanogaster. |
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... |
Other Resources | |
| NextBio | 807110. |
Entry information
| Entry name | LYSP_DROME | ||||||||
| Accession | Primary (citable) accession number: P29615 Secondary accession number(s): Q4V3V7, Q9W0J4 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Drosophila annotation project | ||||||||
Relevant documents
| Drosophila Drosophila: entries, gene names and cross-references to FlyBase |
| Glycosyl hydrolases Classification of glycosyl hydrolase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

Clusters with


