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P50717

- LYS_HYPCU

UniProt

P50717 - LYS_HYPCU

Protein

Lysozyme

Gene
N/A
Organism
Hyphantria cunea (Fall webworm moth)
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.

    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 sitei53 – 531PROSITE-ProRule annotation
    Active sitei71 – 711PROSITE-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 (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase
    OrganismiHyphantria cunea (Fall webworm moth)
    Taxonomic identifieri39466 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaLepidopteraGlossataDitrysiaNoctuoideaArctiidaeHyphantria

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2020Sequence AnalysisAdd
    BLAST
    Chaini21 – 142122LysozymePRO_0000018507Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi27 ↔ 142PROSITE-ProRule annotation
    Disulfide bondi48 ↔ 131PROSITE-ProRule annotation
    Disulfide bondi83 ↔ 97PROSITE-ProRule annotation
    Disulfide bondi93 ↔ 111PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliP50717.
    SMRiP50717. Positions 25-142.
    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.

    P50717-1 [UniParc]FASTAAdd to Basket

    « Hide

    MQKLAVFLFA IAAVCIHCEA KYYSTRCDLV RELRKQGFPE NQMGDWVCLV    50
    ENESGRKTDK VGPVNKNGSK DYGLFQINDK YWCSNTRTPG KDCNVTCADL 100
    LLDDITKAST CAKKIFKRHN FRAWYGWRNH CDGKTLPDTS NC 142
    Length:142
    Mass (Da):16,241
    Last modified:October 1, 1996 - v1
    Checksum:i7A565C7748D4C127
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23786 mRNA. Translation: AAA84747.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U23786 mRNA. Translation: AAA84747.1 .

    3D structure databases

    ProteinModelPortali P50717.
    SMRi P50717. Positions 25-142.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    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. Park S.-S., Shin S.W., Park D.S., Kim M.K., Oh H.W., Park H.Y.
      Submitted (MAR-1995) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].

    Entry informationi

    Entry nameiLYS_HYPCU
    AccessioniPrimary (citable) accession number: P50717
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 59 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)

    Miscellaneousi

    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