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P81711 (LYSC_SYRSO) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 56. 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 C
CPL
Gene names
Name:LYZ
OrganismSyrmaticus soemmerringii (Copper pheasant) (Phasianus soemmerringii)
Taxonomic identifier9067 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesNeognathaeGalliformesPhasianidaePhasianinaeSyrmaticus

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 By similarity.

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_0000208872

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
P81711 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: F0EC776CEFAC7611

FASTA12914,286
        10         20         30         40         50         60 
KVYGRCELAA AMKRLGLDNF RGYSLGNWVC AAKFESNFNT HATNRNTDGS TDYGILQINS 

        70         80         90        100        110        120 
RWWCNDGRTP GSRNLCNIPC SALLSSDTIA SVNCAKKIVS DGNGMNAWVA WRKRCKGTDV 


NAWTRGCRL 

« Hide

References

[1]"The amino acid sequence of copper pheasant lysozyme."
Araki T., Kuramoto M., Torikata T.
Biosci. Biotechnol. Biochem. 58:794-795(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE.
Tissue: Egg white.

Cross-references

Sequence databases

PIRJC2144.

3D structure databases

ProteinModelPortalP81711.
SMRP81711. Positions 1-129.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Proteomic databases

PRIDEP81711.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG052297.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
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. False negative.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_SYRSO
AccessionPrimary (citable) accession number: P81711
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 3, 2013
This is version 56 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