SUPERFAMILY 1.75 HMM library and genome assignments server

Superfamily is undergoing a server migration - you are now browsing on the new server. Please contact us if you experience any problems.

Sialidases superfamily

SCOP classification
Root:   SCOP hierarchy in SUPERFAMILY [ 0] (11)
Class:   All beta proteins [ 48724] (174)
Fold:   6-bladed beta-propeller [ 50938] (11)
Superfamily:   Sialidases [ 50939] (2)
Families:   Sialidases (neuraminidases) [ 50940] (9)
  Endo-alpha-sialidase [ 117276]

Superfamily statistics
Genomes (1,244) Uniprot 2018_03 genome PDB chains (SCOP 1.75)
Domains 3,788 0 43
Proteins 3,369 0 43

Functional annotation
General category Metabolism
Detailed category Polysaccharide metabolism and transport

Function annotation of SCOP domain superfamilies

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEO levelAnnotation (direct or inherited)
Enzyme Commission (EC)Glycosidases, i.e. enzymes hydrolyzing O- and S-gl0Moderately InformativeDirect

Document: EC annotation of SCOP domains

Disease Ontology (DO)

(show details) Document: DO annotation of SCOP domains

Yeast Phenotype (YP)

(show details) Document: YP annotation of SCOP domains

Enzyme Commission (EC)

(show details)
EC termFDR (all)SDEC levelAnnotation (direct or inherited)
Enzyme Commission (EC)Hydrolases0Least InformativeDirect
Enzyme Commission (EC)Glycosylases0Moderately InformativeDirect

Document: EC annotation of SCOP domains

UniProtKB KeyWords (KW)

(show details)
KW termFDR (all)SDKW levelAnnotation (direct or inherited)
Biological processTransport0.8179Least InformativeInherited
Biological processHost-virus interaction0Moderately InformativeDirect
Biological processProtein transport0.000000000325Moderately InformativeDirect
Biological processCarbohydrate metabolism0.0000004696Moderately InformativeDirect
Biological processLipid metabolism0.001729Moderately InformativeInherited
Biological processVirus entry into host cell0InformativeDirect
Biological processLipid degradation0.0000000000001698InformativeDirect
Cellular componentMembrane0Least InformativeDirect
Cellular componentVirion0Moderately InformativeDirect
Cellular componentGolgi apparatus0.0000000002598Moderately InformativeDirect
Cellular componentHost membrane0InformativeDirect
Cellular componentLysosome0.0001743InformativeDirect
DomainTransmembrane0Least InformativeDirect
Molecular functionMetal-binding0Least InformativeDirect
Molecular functionCalcium0Moderately InformativeDirect
Post-translational modificationHydrolase0Least InformativeDirect
Post-translational modificationReceptor0.0000002144Moderately InformativeDirect
Post-translational modificationGlycosidase0InformativeDirect
Post-translational modificationHemagglutinin0Highly InformativeDirect
Post-translational modificationGlycoprotein0Least InformativeDirect
Post-translational modificationDisulfide bond0Least InformativeDirect

Document: KW annotation of SCOP domains

InterPro annotation
Cross references IPR011040 SSF50939 Protein matches

Neuraminidases (sialidases) hydrolyse the non-reducing, terminal sialic acid linkage in various natural substrates, such as glycoproteins, glycolipids, gangliosides, and polysaccharides [PubMed12374200]. In mammals, neuraminidases occur in the lysosome, the cytosol, and associated with the plasma membrane. Neuraminidases have also been implicated in the pathogenesis of many diseases. For example, in viruses neuraminidases enable the transport of the virus through mucin, the eruption of the virus from the infected host cell, and the prevention of self-aggregation of virus particles through the destruction of the host cell receptor recognised by the virus [PubMed14561719]. Eukaryotic, bacterial and viral neuraminidases share highly conserved regions of beta-sheet motifs. Bacterial neuraminidases often possess domains in addition to the catalytic neuraminidase domain, for instance the neuraminidase from Micromonospora viridifaciens contains three domains, of which the catalytic domain described here is the N-terminal domain [PubMed8591030]. Similarly, leech neuraminidase is a multidomain protein, where the catalytic domain is the C-terminal domain [PubMed9878409]. In several paramyxoviruses, neuraminidase forms part of the multi-functional haemagglutinin-neuraminidase glycoprotein found on the viral envelope [PubMed14729348].

InterPro database

PDBeMotif information about ligands, sequence and structure motifs
Cross references PDB entries
Ligand binding statistics
Nucleic-acid binding statistics
Occurrence of secondary structure elements
Occurrence of small 3D structural motifs

PDBeMotif resource

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Yeast Phenotype (YP) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) ]

Internal database links

Browse genome assignments for this superfamily. The SUPERFAMILY hidden Markov model library has been used to carry out SCOP domain assignments to all genomes at the superfamily level.

Alignments of sequences to 15 models in this superfamily are available by clicking on the 'Alignments' icon above. PDB sequences less than 40% identical are shown by default, but any other sequence(s) may be aligned. Select PDB sequences, genome sequences, or paste in or upload your own sequences.

Browse and view proteins in genomes which have different domain combinations including a Sialidases domain.

Examine the distribution of domain superfamilies, or families, across the major taxonomic kingdoms or genomes within a kingdom. This gives an immediate impression of how superfamilies, or families, are restricted to certain kingdoms of life.

Explore domain occurrence network where nodes represent genomes and edges are domain architectures (shared between genomes) containing the superfamily of interest.

There are 15 hidden Markov models representing the Sialidases superfamily. Information on how the models are built, and plots showing hydrophobicity, match emmission probabilities and insertion/deletion probabilities can be inspected.

Jump to [ Top of page · SCOP classification · InterPro annotation · PDBeMotif links · Functional annotation · Enzyme Commission (EC) · Disease Ontology (DO) · Yeast Phenotype (YP) · Enzyme Commission (EC) · UniProtKB KeyWords (KW) · Internal database links ]