Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and ...
161-571
0e+00
Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and related paramyxoviridiae; The hemagglutinin-neuraminidase (HN) found in this family of viruses has a variety of functions during viral infection; it participates in virus attachment to host cells, cleaves sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This model characterizes the global ectodomain of HN. Hemagglutinin-neuraminidase ectodomains of these viruses attaches the virion to sialic acid receptors on host cells; the neuraminidase cleaves sialic acid moieties from host cell molecules as well as virus particles, this removal may happen in the trans Golgi network.
:
Pssm-ID: 271233 Cd Length: 408 Bit Score: 520.31 E-value: 0e+00
Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and ...
161-571
0e+00
Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and related paramyxoviridiae; The hemagglutinin-neuraminidase (HN) found in this family of viruses has a variety of functions during viral infection; it participates in virus attachment to host cells, cleaves sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This model characterizes the global ectodomain of HN. Hemagglutinin-neuraminidase ectodomains of these viruses attaches the virion to sialic acid receptors on host cells; the neuraminidase cleaves sialic acid moieties from host cell molecules as well as virus particles, this removal may happen in the trans Golgi network.
Pssm-ID: 271233 Cd Length: 408 Bit Score: 520.31 E-value: 0e+00
Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and ...
161-571
0e+00
Hemagglutinin-neuraminidase (HN) of parainfluenza virus 5, Newcastle disease virus, and related paramyxoviridiae; The hemagglutinin-neuraminidase (HN) found in this family of viruses has a variety of functions during viral infection; it participates in virus attachment to host cells, cleaves sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This model characterizes the global ectodomain of HN. Hemagglutinin-neuraminidase ectodomains of these viruses attaches the virion to sialic acid receptors on host cells; the neuraminidase cleaves sialic acid moieties from host cell molecules as well as virus particles, this removal may happen in the trans Golgi network.
Pssm-ID: 271233 Cd Length: 408 Bit Score: 520.31 E-value: 0e+00
Haemagglutinin-neuraminidase (HN) of paramyxoviridae and similar proteins; Most ...
161-571
3.55e-37
Haemagglutinin-neuraminidase (HN) of paramyxoviridae and similar proteins; Most paramyxoviridae have two membrane-anchored glycoproteins that mediate entry of the virus into the host cell. The protein characterized by this model is called hemagglutinin-neuraminidase (HN), hemagglutinin glycoprotein (H), or glycoprotein (G). Typically it has a variety of functions during viral infection; it participates in virus attachment to host cells, may cleave sialic acid off host oligosaccharides, and has a stimulating effect on membrane fusion during the entry of the virus into the host cell.
Pssm-ID: 271230 Cd Length: 391 Bit Score: 142.20 E-value: 3.55e-37
sialidases/neuraminidases; Sialidases or neuraminidases function to bind and hydrolyze ...
162-557
1.02e-24
sialidases/neuraminidases; Sialidases or neuraminidases function to bind and hydrolyze terminal sialic acid residues from various glycoconjugates as well as playing roles in pathogenesis, bacterial nutrition and cellular interactions. They have a six-bladed beta-propeller fold. This hierarchy includes eubacterial, eukaryotic, and viral sialidases.
Pssm-ID: 271229 Cd Length: 361 Bit Score: 105.85 E-value: 1.02e-24
Glycoprotein G, or hemagglutinin-neuraminidase of Hendravirus and Nipah virus; The ...
161-533
1.69e-09
Glycoprotein G, or hemagglutinin-neuraminidase of Hendravirus and Nipah virus; The glycoprotein (G) of Nendravirus and Nipah virus has a variety of functions during viral infection; it participates in virus attachment to host cells and has a stimulating effect on membrane fusion during the entry of the virus into the host cell. This models characterizes the globular ectodomain of glycoprotein G. The receptors for Hendravirus and Nipah virus have been identified as ephrin B2 (EFNB2) and ephrin B3 (EFNB3).
Pssm-ID: 271232 Cd Length: 413 Bit Score: 59.86 E-value: 1.69e-09
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
The Show Concise/Full Display button at the top of the page can be used to select the desired level of detail: only top scoring hits
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
Click on the domain model's accession number to view the multiple sequence alignment of the proteins used to develop the corresponding domain model.
To view your query sequence embedded in that multiple sequence alignment, click on the colored bars in the Graphical Summary portion of the search results page,
or click on the triangles, if present, that represent functional sites (conserved features)
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
(labeled illustration) Full Display shows all domain models, in each hit category below, that meet or exceed the RPS-BLAST threshold for statistical significance.
(labeled illustration) Four types of hits can be shown, as available,
for each region on the query sequence:
specific hits meet or exceed a domain-specific e-value threshold
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and represent a very high confidence that the query sequence belongs to the same protein family as the sequences use to create the domain model
non-specific hits
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the domain superfamily to which the specific and non-specific hits belong
multi-domain models that were computationally detected and are likely to contain multiple single domains
Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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