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Q7LZT2 (LYSC_TRATE) Reviewed, UniProtKB/Swiss-Prot

Last modified November 28, 2012. Version 43. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Lysozyme C

EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase
Gene names
Name:LYZ
OrganismTragopan temminckii (Temminck's tragopan) (Satyra temminckii)
Taxonomic identifier9071 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeTragopan

Protein attributes

Sequence length129 AA.
Sequence statusComplete.
Protein existenceEvidence at protein 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 By similarity.

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.

Subunit structure

Monomer By similarity.

Subcellular location

Secreted.

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.

Sequence similarities

Belongs to the glycosyl hydrolase 22 family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 129129Lysozyme C
PRO_0000208875

Sites

Active site351 By similarity
Active site521 By similarity

Amino acid modifications

Disulfide bond6 ↔ 127 By similarity
Disulfide bond30 ↔ 115 By similarity
Disulfide bond64 ↔ 80 By similarity
Disulfide bond76 ↔ 94 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7LZT2 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 70F5D3312444848E

FASTA12914,238
        10         20         30         40         50         60 
KVYGRCELAA AMKRLGLDNY RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS 

        70         80         90        100        110        120 
RWWCNDGRTP GSRNLCNIPC SALLSSDITA SVNCAKKIVS GGNGMSAWVA WRNRCKGTDV 


HAWIRGCRL 

« Hide

References

[1]"The amino acid sequence of Temminck's tragopan lysozyme and evaluation of the influence of amino acid substitution for enzymatic activity against chitin oligomer."
Araki T., Seki S., Torikata T.
Kichin Kitosan Kenkyu 6:217-225(2000)
Cited for: PROTEIN SEQUENCE.

Cross-references

Sequence databases

PIRJC5544.

3D structure databases

ProteinModelPortalQ7LZT2.
SMRQ7LZT2. Positions 1-129.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEQ7LZT2.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

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 nameLYSC_TRATE
AccessionPrimary (citable) accession number: Q7LZT2
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2004
Last sequence update: December 15, 2003
Last modified: November 28, 2012
This is version 43 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families