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Protein

Lysozyme

Gene
N/A
Organism
Hyalophora cecropia (Cecropia moth)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript 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.

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.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei51PROSITE-ProRule annotation1
Active sitei69PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionAntimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
OrganismiHyalophora cecropia (Cecropia moth)
Taxonomic identifieri7123 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaLepidopteraGlossataDitrysiaBombycoideaSaturniidaeSaturniinaeAttaciniHyalophora

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 19By similarityAdd BLAST19
ChainiPRO_000001850620 – 139LysozymeAdd BLAST120

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi25 ↔ 139PROSITE-ProRule annotation
Disulfide bondi46 ↔ 129PROSITE-ProRule annotation
Disulfide bondi81 ↔ 95PROSITE-ProRule annotation
Disulfide bondi91 ↔ 109PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Structurei

3D structure databases

ProteinModelPortaliP05105.
SMRiP05105.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiView protein in InterPro
IPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
PfamiView protein in Pfam
PF00062. Lys. 1 hit.
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiView protein in SMART
SM00263. LYZ1. 1 hit.
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiView protein in PROSITE
PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P05105-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTKYVILLAV LAFALHCDAK RFTRCGLVQE LRRLGFDETL MSNWVCLVEN
60 70 80 90 100
ESGRFTDKIG KVNKNGSRDY GLFQINDKYW CSKGTTPGKD CNVTCNQLLT
110 120 130
DDISVAATCA KKIYKRHKFD AWYGWKNHCQ HGLPDISDC
Length:139
Mass (Da):15,877
Last modified:May 1, 1992 - v2
Checksum:iE8AF5C2CE561F641
GO

Sequence cautioni

The sequence AAA29190 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAA26542 differs from that shown. Reason: Erroneous initiation.Curated

Polymorphismi

3 allelic variants of cecropia moth lysozyme have been found. The sequence shown is that of lysozyme 1.1 Publication

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural varianti34L → R in lysozyme-2. 1
Natural varianti85T → S in lysozyme-2 and lysozyme-3. 1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60914 Genomic DNA. Translation: AAA29189.1.
X02765 mRNA. Translation: CAA26542.1. Different initiation.
M34923 mRNA. Translation: AAA29190.1. Different initiation.
PIRiA24649. LZWK.
A38744.

Keywords - Coding sequence diversityi

Polymorphism

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.

Entry informationi

Entry nameiLYS_HYACE
AccessioniPrimary (citable) accession number: P05105
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 13, 1987
Last sequence update: May 1, 1992
Last modified: April 12, 2017
This is version 93 of the entry and version 2 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Documents

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