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P84492

- LYSC_CHEMY

UniProt

P84492 - LYSC_CHEMY

Protein

Lysozyme C

Gene

LYZ

Organism
Chelonia mydas (Green sea-turtle) (Chelonia agassizi)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein 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 sitei35 – 351PROSITE-ProRule annotation
    Active sitei53 – 531PROSITE-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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme C (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase C
    Gene namesi
    Name:LYZ
    OrganismiChelonia mydas (Green sea-turtle) (Chelonia agassizi)
    Taxonomic identifieri8469 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiTestudines + Archosauria groupTestudinesCryptodiraChelonioideaCheloniidaeChelonia

    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 – 130130Lysozyme CPRO_0000247815Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi6 ↔ 128PROSITE-ProRule annotation
    Disulfide bondi30 ↔ 116PROSITE-ProRule annotation
    Disulfide bondi65 ↔ 81PROSITE-ProRule annotation
    Disulfide bondi77 ↔ 95PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Interactioni

    Subunit structurei

    Monomer.By similarity

    Structurei

    3D structure databases

    ProteinModelPortaliP84492.
    SMRiP84492. Positions 1-130.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Phylogenomic databases

    HOVERGENiHBG052297.

    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.

    P84492-1 [UniParc]FASTAAdd to Basket

    « Hide

    KTYERCELAR AMKRLGLDGY WGYSLGHWVC AAKYESNFNT GATNYNPGDQ    50
    STDYGILQIN SRWWCNDGKT PRTKNACKIQ CRELLTADIT ASVNCAKRVV 100
    RDPNGMGAWV AWTKNCKGRD VSPWIRDCGL 130
    Length:130
    Mass (Da):14,704
    Last modified:March 29, 2005 - v1
    Checksum:i4CBB271A77565168
    GO

    Sequence databases

    PIRiJC7918.

    Cross-referencesi

    Sequence databases

    PIRi JC7918.

    3D structure databases

    ProteinModelPortali P84492.
    SMRi P84492. Positions 1-130.
    ModBasei Search...
    MobiDBi Search...

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Phylogenomic databases

    HOVERGENi HBG052297.

    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. Araki T., Chijiiwa Y., Okabayashi K., Kawase M., Kamesaki M., Torikata T.
      Submitted (MAR-2003) to the PIR data bank
      Cited for: PROTEIN SEQUENCE.

    Entry informationi

    Entry nameiLYSC_CHEMY
    AccessioniPrimary (citable) accession number: P84492
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 25, 2006
    Last sequence update: March 29, 2005
    Last modified: October 1, 2014
    This is version 29 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.

    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