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P83972

- LYSD_DROME

UniProt

P83972 - LYSD_DROME

Protein

Lysozyme D

Gene

LysD

Organism
Drosophila melanogaster (Fruit fly)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at transcript leveli
  1. Functioni

    Unlikely to play an active role in the humoral immune defense. May have a function in the digestion of bacteria in the food.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.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei50 – 501PROSITE-ProRule annotation
    Active sitei68 – 681PROSITE-ProRule annotation

    GO - Molecular functioni

    1. chitinase activity Source: FlyBase
    2. lysozyme activity Source: FlyBase

    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

    Enzyme and pathway databases

    ReactomeiREACT_180705. Amyloids.

    Protein family/group databases

    CAZyiGH22. Glycoside Hydrolase Family 22.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Lysozyme D (EC:3.2.1.17)
    Alternative name(s):
    1,4-beta-N-acetylmuramidase D
    Gene namesi
    Name:LysD
    ORF Names:CG9118
    OrganismiDrosophila melanogaster (Fruit fly)
    Taxonomic identifieri7227 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraEndopterygotaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
    ProteomesiUP000000803: Chromosome 3L

    Organism-specific databases

    FlyBaseiFBgn0004427. LysD.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 1818By similarityAdd
    BLAST
    Chaini19 – 140122Lysozyme DPRO_0000018512Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi24 ↔ 139PROSITE-ProRule annotation
    Disulfide bondi45 ↔ 129PROSITE-ProRule annotation
    Disulfide bondi80 ↔ 96PROSITE-ProRule annotation
    Disulfide bondi92 ↔ 110PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Proteomic databases

    PaxDbiP83972.
    PRIDEiP83972.

    Expressioni

    Tissue specificityi

    Found in the midgut.1 Publication

    Developmental stagei

    Maximal expression is found during the third larval instar, it drops to become undetectable in the late pupal stage. The expression in adults is similar to that of first and second larval instars.1 Publication

    Interactioni

    Protein-protein interaction databases

    BioGridi63673. 3 interactions.

    Structurei

    3D structure databases

    ProteinModelPortaliP83972.
    SMRiP83972. Positions 19-140.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    Phylogenomic databases

    eggNOGiNOG283382.
    GeneTreeiENSGT00550000074398.
    InParanoidiP83972.
    KOiK01185.
    OMAiSECELAK.
    OrthoDBiEOG7BW0M5.
    PhylomeDBiP83972.

    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.

    P83972-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKAFIVLVAL ACAAPAFGRT MDRCSLAREM SNLGVPRDQL ARWACIAEHE    50
    SSYRTGVVGP ENYNGSNDYG IFQINDYYWC APPSGRFSYN ECGLSCNALL 100
    TDDITHSVRC AQKVLSQQGW SAWSTWHYCS GWLPSIDDCF 140
    Length:140
    Mass (Da):15,636
    Last modified:June 7, 2004 - v1
    Checksum:i75C24CA6F85DF903
    GO

    Sequence cautioni

    The sequence ACX30015.1 differs from that shown. Reason: Erroneous initiation.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58382 Genomic DNA. Translation: CAA41272.1.
    AE014296 Genomic DNA. Translation: AAF47450.1.
    BT099853 mRNA. Translation: ACX30015.1. Different initiation.
    PIRiS20914.
    RefSeqiNP_476823.1. NM_057475.3.
    UniGeneiDm.12727.
    Dm.33497.

    Genome annotation databases

    EnsemblMetazoaiFBtr0072634; FBpp0072530; FBgn0004427.
    GeneIDi38127.
    KEGGidme:Dmel_CG9118.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X58382 Genomic DNA. Translation: CAA41272.1 .
    AE014296 Genomic DNA. Translation: AAF47450.1 .
    BT099853 mRNA. Translation: ACX30015.1 . Different initiation.
    PIRi S20914.
    RefSeqi NP_476823.1. NM_057475.3.
    UniGenei Dm.12727.
    Dm.33497.

    3D structure databases

    ProteinModelPortali P83972.
    SMRi P83972. Positions 19-140.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 63673. 3 interactions.

    Protein family/group databases

    CAZyi GH22. Glycoside Hydrolase Family 22.

    Proteomic databases

    PaxDbi P83972.
    PRIDEi P83972.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblMetazoai FBtr0072634 ; FBpp0072530 ; FBgn0004427 .
    GeneIDi 38127.
    KEGGi dme:Dmel_CG9118.

    Organism-specific databases

    CTDi 38127.
    FlyBasei FBgn0004427. LysD.

    Phylogenomic databases

    eggNOGi NOG283382.
    GeneTreei ENSGT00550000074398.
    InParanoidi P83972.
    KOi K01185.
    OMAi SECELAK.
    OrthoDBi EOG7BW0M5.
    PhylomeDBi P83972.

    Enzyme and pathway databases

    Reactomei REACT_180705. Amyloids.

    Miscellaneous databases

    GenomeRNAii 38127.
    NextBioi 807100.

    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. "The lysozyme locus in Drosophila melanogaster: different genes are expressed in midgut and salivary glands."
      Kylsten P., Kimbrell D.A., Daffre S., Samakovlis C., Hultmark D.
      Mol. Gen. Genet. 232:335-343(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, TISSUE SPECIFICITY, DEVELOPMENTAL STAGE.
      Strain: Canton-S.
    2. "The genome sequence of Drosophila melanogaster."
      Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D.
      , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C.
      Science 287:2185-2195(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: Berkeley.
    3. Cited for: GENOME REANNOTATION.
      Strain: Berkeley.
    4. Carlson J.W., Booth B., Frise E., Sandler J., Wan K.H., Yu C., Celniker S.E.
      Submitted (SEP-2009) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: Berkeley.

    Entry informationi

    Entry nameiLYSD_DROME
    AccessioniPrimary (citable) accession number: P83972
    Secondary accession number(s): C9QNX1
    , P29614, P37157, Q9W0J6, Q9W0J7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 87 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programDrosophila annotation project

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Drosophila
      Drosophila: entries, gene names and cross-references to FlyBase
    2. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3