Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Basket 0
(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Q9DD65

- LYSC_PAROL

UniProt

Q9DD65 - LYSC_PAROL

Protein

Lysozyme C

Gene
N/A
Organism
Paralichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
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.PROSITE-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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501PROSITE-ProRule annotation
    Active sitei67 – 671PROSITE-ProRule annotation

    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

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    OrganismiParalichthys olivaceus (Bastard halibut) (Hippoglossus olivaceus)
    Taxonomic identifieri8255 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiActinopterygiiNeopterygiiTeleosteiNeoteleosteiAcanthomorphataCarangimorphariaePleuronectiformesPleuronectoideiParalichthyidaeParalichthys

    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 – 1515Sequence AnalysisAdd
    BLAST
    Chaini16 – 143128Lysozyme CPRO_0000018502Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi21 ↔ 141PROSITE-ProRule annotation
    Disulfide bondi45 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi79 ↔ 94PROSITE-ProRule annotation
    Glycosylationi80 – 801N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi90 ↔ 108PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliQ9DD65.
    SMRiQ9DD65. Positions 16-143.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOVERGENiHBG052297.

    Family and domain databases

    InterProiIPR001916. Glyco_hydro_22.
    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.
    PROSITEiPS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9DD65-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRTLVVLLLV AVANARVYER CEWARLLRNQ GMDGYRGISL ANWVCLTEWE    50
    SHYNTRATNH NTDGSTDYGI FQINSRWWCN DSQTPTSNAC NIRCSELLTD 100
    DVIVAIKCAK RVVRDPNGIG AWVAWRQHCQ GQDLSSYLAG CGL 143
    Length:143
    Mass (Da):16,169
    Last modified:March 1, 2001 - v1
    Checksum:i6335792BE5E6C736
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050469 mRNA. Translation: BAB17215.1.
    AB050589 Genomic DNA. Translation: BAB18249.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB050469 mRNA. Translation: BAB17215.1 .
    AB050589 Genomic DNA. Translation: BAB18249.1 .

    3D structure databases

    ProteinModelPortali Q9DD65.
    SMRi Q9DD65. Positions 16-143.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    Family and domain databases

    InterProi IPR001916. Glyco_hydro_22.
    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 PS51348. LACTALBUMIN_LYSOZYME_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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] [Europe PMC] [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] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

    Entry informationi

    Entry nameiLYSC_PAROL
    AccessioniPrimary (citable) accession number: Q9DD65
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 54 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.

    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