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 g

Gene
N/A
Organism
Casuarius casuarius (Southern cassowary) (Struthio casuarius)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

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)LengthDescriptionGraphical viewFeature identifierActions
Active sitei73 – 731By similarity
Active sitei86 – 861By similarity

GO - Molecular functioni

  1. lysozyme activity Source: UniProtKB-EC

GO - Biological processi

  1. cell wall macromolecule catabolic process Source: InterPro
  2. cytolysis Source: UniProtKB-KW
  3. defense response to bacterium Source: UniProtKB-KW
  4. peptidoglycan catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

Names & Taxonomyi

Protein namesi
Recommended name:
Lysozyme g (EC:3.2.1.17)
Alternative name(s):
1,4-beta-N-acetylmuramidase
Goose-type lysozyme
OrganismiCasuarius casuarius (Southern cassowary) (Struthio casuarius)
Taxonomic identifieri8787 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchelosauriaArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesCasuariidaeCasuarius

Subcellular locationi

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 – 185185Lysozyme gPRO_0000193514Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11Pyrrolidone carboxylic acid
Disulfide bondi4 ↔ 60By similarity
Disulfide bondi18 ↔ 29By similarity

Keywords - PTMi

Disulfide bond, Pyrrolidone carboxylic acid

Structurei

3D structure databases

ProteinModelPortaliQ7LZR3.
SMRiQ7LZR3. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the glycosyl hydrolase 23 family.Curated

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.

Sequencei

Sequence statusi: Complete.

Q7LZR3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
QTGCYGVVNR IDTTGASCET AKPEKLNYCG VAASRKIAEG DLQSMDRYKT
60 70 80 90 100
LIKKVGQKLC VDPAVIAGII SRESHAGKAL KDGWGDNGNG FGLMQVDKRS
110 120 130 140 150
HTPVGKWNGE RHLTQGTEIL ISMIKKIQKK FPRWTKEQQL KGGISAYNAG
160 170 180
SGNVRTYERM DIGTTHNDYA NDVVARAQYY KQHGY
Length:185
Mass (Da):20,426
Last modified:December 15, 2003 - v1
Checksum:i0522F8187896F53A
GO

Sequence databases

PIRiA59351.

Cross-referencesi

Sequence databases

PIRiA59351.

3D structure databases

ProteinModelPortaliQ7LZR3.
SMRiQ7LZR3. Positions 1-185.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Phylogenomic databases

HOVERGENiHBG006299.

Family and domain databases

InterProiIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamiPF01464. SLT. 1 hit.
[Graphical view]
PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
PRINTSiPR00749. LYSOZYMEG.
SUPFAMiSSF53955. SSF53955. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. Thammasirirak S., Torikata T., Takami K., Murata K., Araki T.
    Submitted (OCT-2000) to the PIR data bank
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiLYG_CASCA
AccessioniPrimary (citable) accession number: Q7LZR3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: March 4, 2015
This is version 44 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase (By similarity).By similarity

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

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.