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Q7LZR3 (LYG_CASCA) Reviewed, UniProtKB/Swiss-Prot

Last modified October 16, 2013. Version 39. 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 g

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
Goose-type lysozyme
OrganismCasuarius casuarius (Australian cassowary) (Double-wattled cassowary)
Taxonomic identifier8787 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesCasuariidaeCasuarius

Protein attributes

Sequence length185 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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.

Subcellular location

Secreted.

Miscellaneous

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

Sequence similarities

Belongs to the glycosyl hydrolase 23 family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 185185Lysozyme g
PRO_0000193514

Sites

Active site731 By similarity
Active site861 By similarity

Amino acid modifications

Modified residue11Pyrrolidone carboxylic acid
Disulfide bond4 ↔ 60 By similarity
Disulfide bond18 ↔ 29 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7LZR3 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 0522F8187896F53A

FASTA18520,426
        10         20         30         40         50         60 
QTGCYGVVNR IDTTGASCET AKPEKLNYCG VAASRKIAEG DLQSMDRYKT LIKKVGQKLC 

        70         80         90        100        110        120 
VDPAVIAGII SRESHAGKAL KDGWGDNGNG FGLMQVDKRS HTPVGKWNGE RHLTQGTEIL 

       130        140        150        160        170        180 
ISMIKKIQKK FPRWTKEQQL KGGISAYNAG SGNVRTYERM DIGTTHNDYA NDVVARAQYY 


KQHGY 

« Hide

References

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

Cross-references

Sequence databases

PIRA59351.

3D structure databases

ProteinModelPortalQ7LZR3.
SMRQ7LZR3. Positions 1-185.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG006299.

Family and domain databases

InterProIPR002152. Glyco_hydro_23.
IPR023346. Lysozyme-like_dom.
IPR008258. TGlycosylase-like_SLT.
[Graphical view]
PfamPF01464. SLT. 1 hit.
[Graphical view]
PIRSFPIRSF001065. Lysozyme_g. 1 hit.
PRINTSPR00749. LYSOZYMEG.
SUPFAMSSF53955. SSF53955. 1 hit.
ProtoNetSearch...

Entry information

Entry nameLYG_CASCA
AccessionPrimary (citable) accession number: Q7LZR3
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: October 16, 2013
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries