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Q7LZR3

- LYG_CASCA

UniProt

Q7LZR3 - LYG_CASCA

Protein

Lysozyme g

Gene
N/A
Organism
Casuarius casuarius (Australian cassowary) (Double-wattled cassowary)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
  1. Functioni

    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 sitei73 – 731By similarity
    Active sitei86 – 861By 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 g (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase
    Goose-type lysozyme
    OrganismiCasuarius casuarius (Australian cassowary) (Double-wattled cassowary)
    Taxonomic identifieri8787 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupArchosauriaDinosauriaSaurischiaTheropodaCoelurosauriaAvesPalaeognathaeCasuariiformesCasuariidaeCasuarius

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Secreted

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 185185Lysozyme gPRO_0000193514Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11Pyrrolidone carboxylic acid
    Disulfide bondi4 ↔ 60By similarity
    Disulfide bondi18 ↔ 29By similarity

    Keywords - PTMi

    Disulfide bond, Pyrrolidone carboxylic acid

    Structurei

    3D structure databases

    ProteinModelPortaliQ7LZR3.
    SMRiQ7LZR3. Positions 1-185.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 23 family.Curated

    Phylogenomic databases

    HOVERGENiHBG006299.

    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.

    Q7LZR3-1 [UniParc]FASTAAdd to Basket

    « Hide

    QTGCYGVVNR IDTTGASCET AKPEKLNYCG VAASRKIAEG DLQSMDRYKT    50
    LIKKVGQKLC VDPAVIAGII SRESHAGKAL KDGWGDNGNG FGLMQVDKRS 100
    HTPVGKWNGE RHLTQGTEIL ISMIKKIQKK FPRWTKEQQL KGGISAYNAG 150
    SGNVRTYERM DIGTTHNDYA NDVVARAQYY KQHGY 185
    Length:185
    Mass (Da):20,426
    Last modified:December 15, 2003 - v1
    Checksum:i0522F8187896F53A
    GO

    Sequence databases

    PIRiA59351.

    Cross-referencesi

    Sequence databases

    PIRi A59351.

    3D structure databases

    ProteinModelPortali Q7LZR3.
    SMRi Q7LZR3. Positions 1-185.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG006299.

    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. Thammasirirak S., Torikata T., Takami K., Murata K., Araki T.
      Submitted (OCT-2000) to the PIR data bank
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiLYG_CASCA
    AccessioniPrimary (citable) accession number: Q7LZR3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2004
    Last sequence update: December 15, 2003
    Last modified: October 1, 2014
    This is version 40 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Miscellaneous

    Shows preference for N-acetylmuramic acid residues that are substituted with a peptide moiety. It acts only as a glycanohydrolase By similarity.By similarity

    Keywords - Technical termi

    Direct protein sequencing

    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