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Q9DD65 (LYSC_PAROL) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 44. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Names and origin

Protein namesRecommended name:
Lysozyme C
EC=3.2.1.17
Alternative name(s):
1,4-beta-N-acetylmuramidase C
OrganismParalichthys olivaceus (Japanese flounder)
Taxonomic identifier8255 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Actinopterygii › Neopterygii › Teleostei › Euteleostei › Neoteleostei › Acanthomorpha › Acanthopterygii › Percomorpha › Pleuronectiformes › Pleuronectoidei › Paralichthyidae › Paralichthys

Protein attributes

Sequence length143 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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

Keywords
   Cellular componentSecreted
   DomainSignal
   Molecular functionAntimicrobial
Bacteriolytic enzyme
Glycosidase
Hydrolase
   PTMDisulfide bond
Glycoprotein
Gene Ontology (GO)
   Biological processcell wall macromolecule catabolic process

Inferred from electronic annotation. Source: InterPro

cytolysis

Inferred from electronic annotation. Source: UniProtKB-KW

defense response to bacterium

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentextracellular region

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular functionlysozyme activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 1515 Potential
Chain16 – 143128Lysozyme C
PRO_0000018502

Sites

Active site501 By similarity
Active site671 By similarity

Amino acid modifications

Glycosylation801N-linked (GlcNAc...) Potential
Disulfide bond21 ↔ 141 By similarity
Disulfide bond45 ↔ 129 By similarity
Disulfide bond79 ↔ 94 By similarity
Disulfide bond90 ↔ 108 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9DD65-1 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: 6335792BE5E6C736

FASTA14316,169
        10         20         30         40         50         60 
MRTLVVLLLV AVANARVYER CEWARLLRNQ GMDGYRGISL ANWVCLTEWE SHYNTRATNH 

        70         80         90        100        110        120 
NTDGSTDYGI FQINSRWWCN DSQTPTSNAC NIRCSELLTD DVIVAIKCAK RVVRDPNGIG 

       130        140 
AWVAWRQHCQ GQDLSSYLAG CGL

« Hide

References

[1]"Characterization and expression of c-type lysozyme cDNA from Japanese flounder (Paralichthys olivaceus)."
Hikima J., Hirono I., Aoki T.
Mol. Mar. Biol. Biotechnol. 6:339-344(1997) [PubMed: 9418289] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Moleculer cloning and novel repeated sequences of a c-type lysozyme gene in Japanese flounder (Paralichthys olivaceus)."
Hikima J., Hirono I., Aoki T.
Mar. Biotechnol. 2:241-247(2000) [PubMed: 10852802] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AB050469 mRNA. Translation: BAB17215.1.
AB050589 Genomic DNA. Translation: BAB18249.1.

3D structure databases

ProteinModelPortalQ9DD65.
SMRQ9DD65. Positions 16-143.
ModBaseSearch...

Protein family/group databases

CAZyGH22. Glycoside Hydrolase Family 22.

Phylogenomic databases

HOVERGENHBG052297.

Enzyme and pathway databases

BRENDA3.2.1.17. 74107.

Family and domain databases

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

Entry information

Entry nameLYSC_PAROL
AccessionPrimary (citable) accession number: Q9DD65
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: March 1, 2001
Last modified: August 10, 2010
This is version 44 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·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents