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UniProtKB/Swiss-Prot entry P61944


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name LYSC_FUGRU
Primary accession number P61944
Secondary accession numbers None
Integrated into Swiss-Prot on June 7, 2004
Sequence was last modified on June 7, 2004 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 33)
Name and origin of the protein
Protein name Lysozyme C [Precursor]
Synonyms EC 3.2.1.17
1,4-beta-N-acetylmuramidase C
Gene name None
From
Fugu rubripes (Japanese pufferfish) (Takifugu rubripes) [TaxID: 31033] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Actinopterygii; Neopterygii; Teleostei; Euteleostei; Neoteleostei; Acanthomorpha; Acanthopterygii; Percomorpha; Tetraodontiformes; Tetradontoidea; Tetraodontidae; Takifugu.
Protein existence 2: Evidence at transcript level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
TISSUE=Liver;
Miyadai T., Ootani M., Iwata K.;
"Molecular cloning, expression of chicken- and goose-type lysozyme gene of torafugu (Takifugu rubripes).";
Submitted (NOV-2003) to the EMBL/GenBank/DDBJ databases.
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: Monomer (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.
  • SIMILARITY: Belongs to the glycosyl hydrolase 22 family [view classification].
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB126243; BAD02933.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_001027914.1; -.
UniGene Tru.1982
3D structure databases
SMR P61944; 16-143.
ModBase P61944.
Ontologies
GO
GO:0005576; Cellular component: extracellular region (inferred from electronic annotation from InterPro).
GO:0003796; Molecular function: lysozyme activity (inferred from electronic annotation from InterPro).
GO:0016998; Biological process: cell wall catabolic process (inferred from electronic annotation from InterPro).
GO:0019835; Biological process: cytolysis (inferred from electronic annotation from UniProtKB-KW).
GO:0042742; Biological process: defense response to bacterium (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR001916; Glyco_hydro_22.
IPR000974; Glyco_hydro_22_lys.
Graphical view of domain structure.
Pfam PF00062; Lys; 1.
Pfam graphical view of domain structure.
PRINTS PR00137; LYSOZYME.
PR00135; LYZLACT.
SMART SM00263; LYZ1; 1.
SMART graphical view of domain structure.
PROSITE PS00128; LACTALBUMIN_LYSOZYME_1; FALSE_NEG.
PS51348; LACTALBUMIN_LYSOZYME_2; 1.
PROSITE graphical view of domain structure (profiles).
Genome annotation databases
Ensembl NEWSINFRUG00000147914; Fugu rubripes. [Contig view]
GeneID 445925; -.
Phylogenomic databases
HOVERGEN P61944; -.
Other
ProtoNet P61944.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Antimicrobial; Bacteriolytic enzyme; Glycosidase; Hydrolase; Signal.
Features
SEVIEWER logo Feature table viewer
KeyFrom  To Length Description FTId
SIGNAL   1    15  15     Potential. 
CHAIN   16   143  128     Lysozyme C. PRO_0000018500
ACT_SITE   50    50        By similarity. 
ACT_SITE   67    67        By similarity. 
DISULFID   21   141        By similarity. 
DISULFID   45   129        By similarity. 
DISULFID   79    94        By similarity. 
DISULFID   90   108        By similarity. 
Sequence information
Length: 143 AA [This is the length of the unprocessed precursor] Molecular weight: 16198 Da [This is the MW of the unprocessed precursor] CRC64: 72A5DC9C3F44C139 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MKIPVFLLLL ALANAKVFQR CEWARVLKAR GMDGYRGISL ADWVCLSKWE SQYNTNAINH 

        70         80         90        100        110        120 
NTDGSTDYGI FQINSRWWCN DDRIPTRNAC NIKCSALQTD DVTVAINCAK RVVSDPQGIR 

       130        140 
AWVAWNRHCQ NRDLSAYIAG CGL 

P61944 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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