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P37715 (LYS_ASTRU) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 44. 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

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismAsterias rubens (Common European starfish) (Asterias vulgaris)
Taxonomic identifier7604 [NCBI]
Taxonomic lineageEukaryotaMetazoaEchinodermataEleutherozoaAsterozoaAsteroideaForcipulataceaForcipulatidaAsteriidaeAsterias

Protein attributes

Sequence length25 AA.
Sequence statusFragment.
Protein existenceEvidence 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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Keywords
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological_processcytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular_functionlysozyme activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – ›25›25Lysozyme
PRO_0000208877

Experimental info

Non-terminal residue251

Sequences

Sequence LengthMass (Da)Tools
P37715 [UniParc].

Last modified October 1, 1994. Version 1.
Checksum: 6FA1D6BE87C5BE18

FASTA252,569
        10         20 
SGPVPSGCLR CICVVESGXR MPNPV 

« Hide

References

[1]"The losozyme from Asterias rubens."
Jolles J., Jolles P.
Eur. J. Biochem. 54:19-23(1975) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRA11762.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

ProtoNetSearch...

Entry information

Entry nameLYS_ASTRU
AccessionPrimary (citable) accession number: P37715
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: October 1, 1994
Last modified: February 19, 2014
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries