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G3XDT7 (LYSC_DRONO) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 8. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismDromaius novaehollandiae (Emu)
Taxonomic identifier8790 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesDromaiidaeDromaius

Protein attributes

Sequence length147 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Has bacteriolytic activity against M.luteus. Ref.1

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. UniProtKB P00698

Subunit structure

Monomer By similarity. UniProtKB P00698

Subcellular location

Secreted By similarity UniProtKB P00698.

Tissue specificity

Expressed in liver and ovary. Not expressed in bone marrow, lung, spleen, intestine or oviduct. Ref.1

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 By similarity. UniProtKB P00698

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
Gene Ontology (GO)
   Biological_processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

cytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 Potential
Chain19 – 147129Lysozyme C
PRO_5000795993

Sites

Active site531 By similarity UniProtKB P00698
Active site701 By similarity UniProtKB P00698
Binding site1191Substrate By similarity UniProtKB P00698

Amino acid modifications

Disulfide bond24 ↔ 145 By similarity UniProtKB P00698
Disulfide bond48 ↔ 133 By similarity UniProtKB P00698
Disulfide bond82 ↔ 98 By similarity UniProtKB P00698
Disulfide bond94 ↔ 112 By similarity UniProtKB P00698

Sequences

Sequence LengthMass (Da)Tools
G3XDT7 [UniParc].

Last modified December 14, 2011. Version 1.
Checksum: F771E0B42235C110

FASTA14716,443
        10         20         30         40         50         60 
MKFFLILGFC LLPLIAQGKV FQRCELAAAM KKHGLSNYRG YSLGHWVCAA KYESNFNTAA 

        70         80         90        100        110        120 
INRNRDGSSD YGILQINSRW WCNDGRTSGA KNLCKISCSA LLSSDITASV NCAKRVVSDK 

       130        140 
NGMNAWVAWR NHCKGRDVSQ WIRGCRV 

« Hide

References

[1]"Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white."
Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.
Gene 492:244-249(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Muscle and Oviduct.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB513676 Genomic DNA. Translation: BAL03621.1.
AB513854 mRNA. Translation: BAL03622.1.

3D structure databases

ProteinModelPortalG3XDT7.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMSSF53955. SSF53955. 1 hit.
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_DRONO
AccessionPrimary (citable) accession number: G3XDT7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 5, 2012
Last sequence update: December 14, 2011
Last modified: July 9, 2014
This is version 8 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries