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G3XDT7

- LYSC_DRONO

UniProt

G3XDT7 - LYSC_DRONO

Protein

Lysozyme C

Gene
N/A
Organism
Dromaius novaehollandiae (Emu)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    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. Has bacteriolytic activity against M.luteus.1 PublicationPROSITE-ProRule annotation

    Catalytic activityi

    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.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei53 – 531By similarityPROSITE-ProRule annotation
    Active sitei70 – 701By similarityPROSITE-ProRule annotation
    Binding sitei119 – 1191SubstrateBy similarity

    GO - Molecular functioni

    1. lysozyme activity Source: UniProtKB-EC

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. cytolysis Source: UniProtKB-KW
    3. defense response to bacterium Source: UniProtKB-KW

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme CImported (EC:3.2.1.17By similarity)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase CBy similarity
    OrganismiDromaius novaehollandiae (Emu)
    Taxonomic identifieri8790 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesDromaiidaeDromaius

    Subcellular locationi

    Secreted By similarity

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818Sequence AnalysisAdd
    BLAST
    Chaini19 – 147129Lysozyme CSequence AnalysisPRO_5000795993Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 145By similarityPROSITE-ProRule annotation
    Disulfide bondi48 ↔ 133By similarityPROSITE-ProRule annotation
    Disulfide bondi82 ↔ 98By similarityPROSITE-ProRule annotation
    Disulfide bondi94 ↔ 112By similarityPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed in liver and ovary. Not expressed in bone marrow, lung, spleen, intestine or oviduct.1 Publication

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliG3XDT7.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 22 family.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00062. Lys. 1 hit.
    [Graphical view]
    PRINTSiPR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTiSM00263. LYZ1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    PROSITEiPS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    G3XDT7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKFFLILGFC LLPLIAQGKV FQRCELAAAM KKHGLSNYRG YSLGHWVCAA    50
    KYESNFNTAA INRNRDGSSD YGILQINSRW WCNDGRTSGA KNLCKISCSA 100
    LLSSDITASV NCAKRVVSDK NGMNAWVAWR NHCKGRDVSQ WIRGCRV 147
    Length:147
    Mass (Da):16,443
    Last modified:December 14, 2011 - v1
    Checksum:iF771E0B42235C110
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB513676 Genomic DNA. Translation: BAL03621.1.
    AB513854 mRNA. Translation: BAL03622.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB513676 Genomic DNA. Translation: BAL03621.1 .
    AB513854 mRNA. Translation: BAL03622.1 .

    3D structure databases

    ProteinModelPortali G3XDT7.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR001916. Glyco_hydro_22.
    IPR019799. Glyco_hydro_22_CS.
    IPR000974. Glyco_hydro_22_lys.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00062. Lys. 1 hit.
    [Graphical view ]
    PRINTSi PR00137. LYSOZYME.
    PR00135. LYZLACT.
    SMARTi SM00263. LYZ1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    PROSITEi PS00128. LACTALBUMIN_LYSOZYME_1. 1 hit.
    PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Molecular characterization of goose- and chicken-type lysozymes in emu (Dromaius novaehollandiae): evidence for extremely low lysozyme levels in emu egg white."
      Maehashi K., Matano M., Irisawa T., Uchino M., Kashiwagi Y., Watanabe T.
      Gene 492:244-249(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, TISSUE SPECIFICITY.
      Tissue: Muscle1 Publication and OviductImported.

    Entry informationi

    Entry nameiLYSC_DRONO
    AccessioniPrimary (citable) accession number: G3XDT7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 9 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    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.By similarity

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3