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Reviewed, UniProtKB/Swiss-Prot P79806 (LYSC_MIOTA)

Last modified June 16, 2009. Version 53. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Lysozyme C
    EC=3.2.1.17
Alternative name(s):
    1,4-beta-N-acetylmuramidase C
Gene names
Name: LYZ
Synonyms: LZM
OrganismMiopithecus talapoin (Talapoin) (Cercopithecus talapoin)
Taxonomic identifier36231 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniCercopithecidaeCercopithecinaeMiopithecus

Protein attributes

Sequence length148 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceInferred from homology.

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.

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.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1818 By similarity
Chain19 – 148130Lysozyme C
PRO_0000018471

Sites

Active site531 By similarity
Active site711 By similarity

Amino acid modifications

Disulfide bond24 ↔ 146 By similarity
Disulfide bond48 ↔ 134 By similarity
Disulfide bond83 ↔ 99 By similarity
Disulfide bond95 ↔ 113 By similarity

Sequences

Sequence LengthMass (Da)Tools
P79806-1 [UniParc].

Last modified May 1, 1997. Version 1.
Checksum: 41AE0FB3432BC07E

FASTA14816,487
        10         20         30         40         50         60 
MKAVIILGLV LLSVTVQGKI FERCELARTL KRLGLDGYRG ISLANWVCLA KWESDYNTQA 

        70         80         90        100        110        120 
TNYNPGDQST DYGIFQINSH YWCNNGKTPG AVNACHISCN ALLQDNIADA VTCAKRVVRD 

       130        140 
PQGIRAWVAW RNHCHNRDVS QYVQGCGV 

« Hide

References

[1]"Episodic adaptive evolution of primate lysozymes."
Messier W., Stewart C.B.
Nature 385:151-154(1997) [PubMed: 8990116] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Blood.

Cross-references

Sequence databases

U76955 expand/collapse EMBL AC list , U76952, U76953, U76954 Genomic DNA. Translation: AAB41220.1.

3D structure databases

HSSPHSSP built from PDB template 1C46 based on UniProtKB P00695.
SMRP79806. Positions 19-148.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGENP79806.

Enzyme and pathway databases

BRENDA3.2.1.17. 295950.

Family and domain databases

InterProIPR001916. Glyco_hydro_22.
IPR019799. Glyco_hydro_22_CS.
IPR000974. Glyco_hydro_22_lys.
[Graphical view]
PfamPF00062. Lys. 1 hit.
[Graphical view]
PRINTSPR00137. LYSOZYME.
PR00135. LYZLACT.
SMARTSM00263. LYZ1. 1 hit.
[Graphical view]
PROSITEPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameLYSC_MIOTA
AccessionPrimary (citable) accession number: P79806
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: May 1, 1997
Last modified: June 16, 2009
This is version 53 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Glycosyl hydrolases

Classification of glycosyl hydrolase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents