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P50717 (LYS_HYPCU) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 58. 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
OrganismHyphantria cunea (Fall webworm moth)
Taxonomic identifier39466 [NCBI]
Taxonomic lineageEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaArctiidaeHyphantria

Protein attributes

Sequence length142 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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2020 Potential
Chain21 – 142122Lysozyme
PRO_0000018507

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond27 ↔ 142 By similarity
Disulfide bond48 ↔ 131 By similarity
Disulfide bond83 ↔ 97 By similarity
Disulfide bond93 ↔ 111 By similarity

Sequences

Sequence LengthMass (Da)Tools
P50717 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 7A565C7748D4C127

FASTA14216,241
        10         20         30         40         50         60 
MQKLAVFLFA IAAVCIHCEA KYYSTRCDLV RELRKQGFPE NQMGDWVCLV ENESGRKTDK 

        70         80         90        100        110        120 
VGPVNKNGSK DYGLFQINDK YWCSNTRTPG KDCNVTCADL LLDDITKAST CAKKIFKRHN 

       130        140 
FRAWYGWRNH CDGKTLPDTS NC 

« Hide

References

[1]Park S.-S., Shin S.W., Park D.S., Kim M.K., Oh H.W., Park H.Y.
Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U23786 mRNA. Translation: AAA84747.1.

3D structure databases

ProteinModelPortalP50717.
SMRP50717. Positions 25-142.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

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 nameLYS_HYPCU
AccessionPrimary (citable) accession number: P50717
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: October 16, 2013
This is version 58 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