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G3XDD8

- LYG_DRONO

UniProt

G3XDD8 - LYG_DRONO

Protein

Lysozyme G

Gene
N/A
Organism
Dromaius novaehollandiae (Emu)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 10 (01 Oct 2014)
      Sequence version 1 (14 Dec 2011)
      Previous versions | rss
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    Functioni

    Has bacteriolytic activity against M.luteus.1 Publication

    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 sitei92 – 921By similarity
    Active sitei105 – 1051By 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
    4. peptidoglycan catabolic process Source: InterPro

    Keywords - Molecular functioni

    Antimicrobial, Bacteriolytic enzyme, Glycosidase, Hydrolase

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme GImported (EC:3.2.1.17By similarity)
    Alternative name(s):
    1,4-beta-N-acetylmuramidaseBy 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 – 1919Sequence AnalysisAdd
    BLAST
    Chaini20 – 204185Lysozyme GSequence AnalysisPRO_5000795990Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi23 ↔ 79By similarity
    Disulfide bondi37 ↔ 48By similarity

    Keywords - PTMi

    Disulfide bond

    Structurei

    3D structure databases

    ProteinModelPortaliG3XDD8.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 23 family.Sequence Analysis

    Keywords - Domaini

    Signal

    Family and domain databases

    InterProiIPR002152. Glyco_hydro_23.
    IPR023346. Lysozyme-like_dom.
    IPR008258. TGlycosylase-like_SLT.
    [Graphical view]
    PfamiPF01464. SLT. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001065. Lysozyme_g. 1 hit.
    PRINTSiPR00749. LYSOZYMEG.
    SUPFAMiSSF53955. SSF53955. 1 hit.

    Sequencei

    Sequence statusi: Complete.

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

    G3XDD8-1 [UniParc]FASTAAdd to Basket

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    MHLMLVLLGL AALLGTSQSQ TGCYGVVNRI DTTGASCETA KPEKLNYCGV    50
    AASRMIAERD LRSMDRYKTL IKKVGQKLCV DPAVIAGIIS RESHAGKALK 100
    NGWGDNGNGF GLMQVDKRSH TPVGEWNGER HLTQGTEILI SMIKKIQKKF 150
    PRWTKEQQLK GGISAYNAGS GNVRSYERMD IGTTHNDYAN DVVARAQYYK 200
    QHGY 204
    Length:204
    Mass (Da):22,493
    Last modified:December 14, 2011 - v1
    Checksum:i4061327BB92C820C
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB451700 mRNA. Translation: BAL03618.1.
    AB462632 Genomic DNA. Translation: BAL03619.1.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AB451700 mRNA. Translation: BAL03618.1 .
    AB462632 Genomic DNA. Translation: BAL03619.1 .

    3D structure databases

    ProteinModelPortali G3XDD8.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    InterProi IPR002152. Glyco_hydro_23.
    IPR023346. Lysozyme-like_dom.
    IPR008258. TGlycosylase-like_SLT.
    [Graphical view ]
    Pfami PF01464. SLT. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001065. Lysozyme_g. 1 hit.
    PRINTSi PR00749. LYSOZYMEG.
    SUPFAMi SSF53955. SSF53955. 1 hit.
    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: OvaryImported and OviductImported.

    Entry informationi

    Entry nameiLYG_DRONO
    AccessioniPrimary (citable) accession number: G3XDD8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 5, 2012
    Last sequence update: December 14, 2011
    Last modified: October 1, 2014
    This is version 10 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    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