catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Leviviridae of ...
210-445
2.88e-74
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Leviviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Leviviridae, order Levivirales. Leviviridae is a family of (+)ssRNA viruses which are highly antigenic and are abundantly present in sewage, waste water, animal and human feces. Within this family two genera can be distinguished, Levivirus and Allolevivirus. Members of the family Leviviridae that propagate in Escherichia coli infect by adsorption to the sides of F(ertility) pili. This event leads to cleavage of the A-protein and release of the RNA from the virion into the bacterium. The infecting RNA encodes a replicase, which assembles with three host proteins, ribosomal protein S1 and translation elongation factors EF-Tu and EF-Ts, to form the active RNA polymerase. Leviviruses not only infect enterobacteria, but also species of the genera Caulobacter, Pseudomonas, and Acinetobacter, and probably many other Gram-negative bacteria. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.
Pssm-ID: 438026 Cd Length: 396 Bit Score: 241.22 E-value: 2.88e-74
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Leviviridae of ...
210-445
2.88e-74
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Leviviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Leviviridae, order Levivirales. Leviviridae is a family of (+)ssRNA viruses which are highly antigenic and are abundantly present in sewage, waste water, animal and human feces. Within this family two genera can be distinguished, Levivirus and Allolevivirus. Members of the family Leviviridae that propagate in Escherichia coli infect by adsorption to the sides of F(ertility) pili. This event leads to cleavage of the A-protein and release of the RNA from the virion into the bacterium. The infecting RNA encodes a replicase, which assembles with three host proteins, ribosomal protein S1 and translation elongation factors EF-Tu and EF-Ts, to form the active RNA polymerase. Leviviruses not only infect enterobacteria, but also species of the genera Caulobacter, Pseudomonas, and Acinetobacter, and probably many other Gram-negative bacteria. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.
Pssm-ID: 438026 Cd Length: 396 Bit Score: 241.22 E-value: 2.88e-74
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Botourmiaviridae of ...
288-403
1.06e-03
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Botourmiaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Botourmiaviridae, order Ourlivirales. The family includes six genera: Ourmiavirus, Botoulivirus, Magoulivirus, Penoulivirus, Rhizoulivirus and Scleroulivirus. Family Botourmiaviridae genomes can be monopartite (Botoulivirus, Magoulivirus, Penoulivirus, Rhizoulivirus and Scleroulivirus) (2-3 kb) or tripartate (Ourmiavirus). Members of genus Ourmiavirus infect plants and the other genera infect fungi. Members of the genera Botoulivirus, Magoulivirus and Scleroulivirus infect fungi from the genera Botrytis, Magnaporthe or Sclerotinia, respectively. Members of the genus Ourmiavirus infect plants: Ourmia melon virus infects melon, producing chlorotic spots and irregular ringspots, Epirus cherry virus produces rasp-leaf symptoms in cherry, and cassava virus C induces severe stunting and a yellow mosaic pattern in cassava. Ourmiavirus replication is dependent on the virus RdRp. Synthesis of the ourmiavirus coat protein from actively replicating RNA3 is necessary for both virion assembly and systemic infection of the host. The ourmiavirus movement protein determines symptoms and forms tubular structures involved in cell-to-cell movement and may undergo post-translational modification. Botoulivirus, magoulivirus and scleroulivirus replication is strictly dependent on the virus RNA-dependent RNA polymerase. The RdRp domain displays a right hand with three functional subdomains, called fingers, palm, and thumb. All RdRps contain conserved polymerase motifs (A-G), located in the palm (A-E motifs) and finger (F-G) subdomains. All these motifs have been implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides.
Pssm-ID: 438033 Cd Length: 223 Bit Score: 40.74 E-value: 1.06e-03
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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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.
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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.
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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,
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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,
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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
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