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Protein

Lysozyme C

Gene

LYZ

Organism
Colobus angolensis (Angolan colobus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

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 sitei53PROSITE-ProRule annotation1
Active sitei71PROSITE-ProRule annotation1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme C (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase C
Gene namesi
Name:LYZ
Synonyms:LZM
OrganismiColobus angolensis (Angolan colobus)
Taxonomic identifieri54131 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeColobinaeColobus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Signal peptidei1 – 18By similarityAdd BLAST18
ChainiPRO_000001846219 – 148Lysozyme CAdd BLAST130

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Disulfide bondi24 ↔ 146PROSITE-ProRule annotation
Disulfide bondi48 ↔ 134PROSITE-ProRule annotation
Disulfide bondi83 ↔ 99PROSITE-ProRule annotation
Disulfide bondi95 ↔ 113PROSITE-ProRule annotation

Keywords - PTMi

Disulfide bond

Proteomic databases

PRIDEiP61631.

Interactioni

Subunit structurei

Monomer.

Structurei

3D structure databases

ProteinModelPortaliP61631.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

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

Keywords - Domaini

Signal

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P61631-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKALIILGLV LLSVTVQGKI FERCELARTL KKLGLDGYKG VSLANWVCLA
60 70 80 90 100
KWESGYNTDA TNYNPGDEST DYGIFQINSR YWCNNGKTPG AVNACHISCN
110 120 130 140
ALLQNNIADA VACAKRVVSD PQGIRAWVAW KKHCQNRDVS QYVEGCGV
Length:148
Mass (Da):16,258
Last modified:June 7, 2004 - v1
Checksum:i2402FC175CA271AA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76937
, U76934, U76935, U76936 Genomic DNA. Translation: AAB41215.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U76937
, U76934, U76935, U76936 Genomic DNA. Translation: AAB41215.1.

3D structure databases

ProteinModelPortaliP61631.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

CAZyiGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEiP61631.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG052297.

Family and domain databases

CDDicd00119. LYZ1. 1 hit.
InterProiIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
IPR023346. Lysozyme-like_dom.
[Graphical view]
PfamiPF00062. Lys. 1 hit.
[Graphical view]
PRINTSiPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTiSM00263. LYZ1. 1 hit.
[Graphical view]
SUPFAMiSSF53955. SSF53955. 1 hit.
PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiLYSC_COLAN
AccessioniPrimary (citable) accession number: P61631
Secondary accession number(s): P79151, P79698
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: October 5, 2016
This is version 48 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Lysozyme C is capable of both hydrolysis and transglycosylation; it shows also a slight esterase activity. It acts rapidly on both peptide-substituted and unsubstituted peptidoglycan, and slowly on chitin oligosaccharides.

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.