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P15698

- NANH_CLOSO

UniProt

P15698 - NANH_CLOSO

Protein

Sialidase

Gene
N/A
Organism
Clostridium sordellii
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 88 (01 Oct 2014)
      Sequence version 1 (01 Apr 1990)
      Previous versions | rss
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    Functioni

    Sialidases have been suggested to be pathogenic factors in microbial infections.

    Catalytic activityi

    Hydrolysis of alpha-(2->3)-, alpha-(2->6)-, alpha-(2->8)- glycosidic linkages of terminal sialic acid residues in oligosaccharides, glycoproteins, glycolipids, colominic acid and synthetic substrates.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei55 – 551SubstrateBy similarity
    Active sitei80 – 801Proton acceptorBy similarity
    Binding sitei263 – 2631SubstrateSequence Analysis
    Active sitei365 – 3651NucleophileBy similarity

    GO - Molecular functioni

    1. exo-alpha-(2->3)-sialidase activity Source: UniProtKB-EC
    2. exo-alpha-(2->6)-sialidase activity Source: UniProtKB-EC
    3. exo-alpha-(2->8)-sialidase activity Source: UniProtKB-EC

    GO - Biological processi

    1. pathogenesis Source: InterPro

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Protein family/group databases

    CAZyiGH33. Glycoside Hydrolase Family 33.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Sialidase (EC:3.2.1.18)
    Alternative name(s):
    Neuraminidase
    OrganismiClostridium sordellii
    Taxonomic identifieri1505 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesClostridiaClostridialesPeptostreptococcaceaePeptoclostridium

    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
    Signal peptidei1 – 27271 PublicationPROSITE-ProRule annotationAdd
    BLAST
    Chaini28 – 404377SialidasePRO_0000012030Add
    BLAST

    Post-translational modificationi

    It is possible that the sialidase is cleaved in front of a cysteine within the leader peptide, forming a glyceride thioether bond which links the protein to the membrane. A second proteolytic cleavage releases the mature extracellular protein.

    Structurei

    3D structure databases

    ProteinModelPortaliP15698.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati89 – 10012BNR 1Add
    BLAST
    Repeati158 – 16912BNR 2Add
    BLAST
    Repeati226 – 23712BNR 3Add
    BLAST
    Repeati273 – 28412BNR 4Add
    BLAST

    Sequence similaritiesi

    Belongs to the glycosyl hydrolase 33 family.Curated
    Contains 4 BNR repeats.Curated

    Keywords - Domaini

    Repeat, Signal

    Family and domain databases

    Gene3Di2.120.10.10. 1 hit.
    InterProiIPR002860. BNR_rpt.
    IPR026856. Sialidase_fam.
    IPR008377. Sialidase_trypan.
    IPR011040. Sialidases.
    [Graphical view]
    PANTHERiPTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF5. PTHR10628:SF5. 1 hit.
    PfamiPF02012. BNR. 3 hits.
    [Graphical view]
    PRINTSiPR01803. TCSIALIDASE.
    SUPFAMiSSF50939. SSF50939. 1 hit.
    PROSITEiPS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P15698-1 [UniParc]FASTAAdd to Basket

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    MKKFIKILKV LSMAIVLSAC NINGIFASNL NTTNEPQKTT VFNKNDNTWN    50
    AQYFRIPSLQ TLADGTMLAF SDIRYNGAED HAYIDIGAAK STDNGQTWDY 100
    KTVMENDRID STFSRVMDST TVVTDTGRII LIAGSWNKNG NWASSTTSLR 150
    SDWSVQMVYS DDNGETWSDK VDLTTNKARI KNQPSNTIGW LAGVGSGIVM 200
    SDGTIVMPIQ IALRENNANN YYSSVIYSKD NGETWTMGNK VPDPKTSENM 250
    VIELDGALIM SSRNDGKNYR ASYISYDMGS TWEVYDPLHN KISTGNGSGC 300
    QGSFIKVTAK DGHRLGFISA PKNTKGGYVR DNITVYMIDF DDLSKGIREL 350
    CSPYPEDGNS SGGGYSCLSF NDGKLSILYE ANGNIEYKDL TDYYLSIENN 400
    KKLK 404
    Length:404
    Mass (Da):44,729
    Last modified:April 1, 1990 - v1
    Checksum:i525B9DA90083AA6A
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31584 Genomic DNA. Translation: AAA23280.1.
    PIRiA37234.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M31584 Genomic DNA. Translation: AAA23280.1 .
    PIRi A37234.

    3D structure databases

    ProteinModelPortali P15698.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    CAZyi GH33. Glycoside Hydrolase Family 33.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Family and domain databases

    Gene3Di 2.120.10.10. 1 hit.
    InterProi IPR002860. BNR_rpt.
    IPR026856. Sialidase_fam.
    IPR008377. Sialidase_trypan.
    IPR011040. Sialidases.
    [Graphical view ]
    PANTHERi PTHR10628. PTHR10628. 1 hit.
    PTHR10628:SF5. PTHR10628:SF5. 1 hit.
    Pfami PF02012. BNR. 3 hits.
    [Graphical view ]
    PRINTSi PR01803. TCSIALIDASE.
    SUPFAMi SSF50939. SSF50939. 1 hit.
    PROSITEi PS51257. PROKAR_LIPOPROTEIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Cloning, sequencing and expression of a sialidase gene from Clostridium sordellii G12."
      Rothe B., Roggentin P., Frank R., Bloecker H., Schauer R.
      J. Gen. Microbiol. 135:3087-3096(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 28-45.
      Strain: ATCC 9714 / DSM 2141 / JCM 3814 / LMG 15708 / NCIB 10717.

    Entry informationi

    Entry nameiNANH_CLOSO
    AccessioniPrimary (citable) accession number: P15698
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1990
    Last sequence update: April 1, 1990
    Last modified: October 1, 2014
    This is version 88 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    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