Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Lysozyme

Gene
N/A
Organism
Meretrix lusoria (Hard clam) (Common Orient clam)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Has antibacterial activity.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.By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cytolysis Source: UniProtKB-KW
  2. defense response to bacterium Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Antibiotic, Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme1 Publication (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidaseBy similarity
OrganismiMeretrix lusoria (Hard clam) (Common Orient clam)
Taxonomic identifieri74491 [NCBI]
Taxonomic lineageiEukaryotaMetazoaLophotrochozoaMolluscaBivalviaHeteroconchiaEuheterodontaVeneroidaVeneroideaVeneridaeMeretrix

Subcellular locationi

Secreted By similarity

GO - Cellular componenti

  1. extracellular region Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Secreted

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 122122LysozymePRO_0000389530Add
BLAST

Structurei

Secondary structure

1
122
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi4 – 63Combined sources
Helixi8 – 1912Combined sources
Beta strandi20 – 223Combined sources
Beta strandi26 – 294Combined sources
Beta strandi32 – 354Combined sources
Turni36 – 394Combined sources
Helixi42 – 476Combined sources
Beta strandi52 – 543Combined sources
Helixi55 – 595Combined sources
Helixi62 – 8019Combined sources
Helixi86 – 9510Combined sources
Helixi99 – 1013Combined sources
Helixi104 – 1129Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AB6X-ray1.78A1-122[»]
3AYQX-ray1.77A1-122[»]
ProteinModelPortaliP86383.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the lysozyme type I family.Sequence Analysis

Family and domain databases

InterProiIPR008597. Destabilase.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PANTHERiPTHR11195. PTHR11195. 1 hit.
PfamiPF05497. Destabilase. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

P86383-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
FAGGIVSQRC LSCICKMESG CRNVGCKMDM GSLSCGYFQI KEAYWIDCGR
60 70 80 90 100
PGSSWKSCAA SSYCASLCVQ NYMKRYAKWA GCPLRCEGFA REHNGGPRGC
110 120
KKGSTIGYWN RLQKISGCHG VQ
Length:122
Mass (Da):13,377
Last modified:November 24, 2009 - v1
Checksum:i92366099E8AD7881
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti5 – 51I → T in isozyme B. 1 Publication

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AB6X-ray1.78A1-122[»]
3AYQX-ray1.77A1-122[»]
ProteinModelPortaliP86383.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR008597. Destabilase.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PANTHERiPTHR11195. PTHR11195. 1 hit.
PfamiPF05497. Destabilase. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "The complete amino acid sequence of invertebrate lysozyme from common orient clam."
    Araki T., Kuwano Y.
    Submitted (OCT-2009) to UniProtKB
    Cited for: PROTEIN SEQUENCE (ISOZYMES A AND B).

Entry informationi

Entry nameiLYS_MERLU
AccessioniPrimary (citable) accession number: P86383
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 24, 2009
Last sequence update: November 24, 2009
Last modified: January 7, 2015
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

3D-structure, Direct protein sequencing

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.