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Protein

Lysozyme

Gene
N/A
Organism
Estigmene acrea (Salt marsh moth) (Phalaena acrea)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

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.By similarity

Catalytic activityi

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.

Enzyme regulationi

By lipopolysaccharide (LPS).1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiEstigmene acrea (Salt marsh moth) (Phalaena acrea)
Taxonomic identifieri56594 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaErebidaeArctiinaeEstigmene

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – ›18›18LysozymePRO_0000208878Add
BLAST

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.Curated

Sequencei

Sequence statusi: Fragment.

P82175-1 [UniParc]FASTAAdd to basket

« Hide

        10 
KYFATRCDLV RELRKXGF
Length:18
Mass (Da):2,214
Last modified:May 1, 2000 - v1
Checksum:iB229D8F5ECDD7F57
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Non-terminal residuei18 – 181

Cross-referencesi

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

ProtoNetiSearch...

Publicationsi

  1. "LPS (lipopolysaccharide)-activated immune responses in a hemocyte cell line from Estigmene acraea (Lepidoptera)."
    Wittwer D., Weise C., Goetz P., Wiesner A.
    Dev. Comp. Immunol. 21:323-336(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE, ENZYME REGULATION.
    Tissue: Hemocyte.

Entry informationi

Entry nameiLYS_ESTAC
AccessioniPrimary (citable) accession number: P82175
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: May 1, 2000
Last modified: March 4, 2015
This is version 49 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.