Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the ...
10-1089
0e+00
Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the Paramyxoviridae, like other non-segmented negative strand RNA viruses, have an RNA-dependent RNA polymerase composed of two subunits, a large protein L and a phosphoprotein P. This is a protein family of the L protein. The L protein confers the RNA polymerase activity on the complex. The P protein acts as a transcription factor.
:
Pssm-ID: 395756 Cd Length: 1042 Bit Score: 1176.74 E-value: 0e+00
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, ...
1105-1357
4.34e-94
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, GxxTx(n)HR, that is essential for mRNA cap formation. Nonsegmented negative-sense (NNS) RNA viruses, Mononegavirales, cap their mRNA by an unconventional mechanism. Specifically, 5'-monophosphate mRNA is transferred to GDP derived from GTP through a reaction that involves a covalent intermediate between the large polymerase protein L and mRNA. The V region is essential for this process.
:
Pssm-ID: 405070 Cd Length: 241 Bit Score: 304.69 E-value: 4.34e-94
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region ...
1215-2204
1.84e-89
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region shared by paramyxovirus-like RNA-dependent RNA polymerases (see pfam00946). Polymerase proteins described by these two models are often called L protein (large polymerase protein). Capping of mRNA requires RNA triphosphatase and guanylyl transferase activities, demonstrated for the rinderpest virus L protein and at least partially localized to the region of this model.
:
Pssm-ID: 275046 [Multi-domain] Cd Length: 893 Bit Score: 313.66 E-value: 1.84e-89
Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the ...
10-1089
0e+00
Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the Paramyxoviridae, like other non-segmented negative strand RNA viruses, have an RNA-dependent RNA polymerase composed of two subunits, a large protein L and a phosphoprotein P. This is a protein family of the L protein. The L protein confers the RNA polymerase activity on the complex. The P protein acts as a transcription factor.
Pssm-ID: 395756 Cd Length: 1042 Bit Score: 1176.74 E-value: 0e+00
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, ...
1105-1357
4.34e-94
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, GxxTx(n)HR, that is essential for mRNA cap formation. Nonsegmented negative-sense (NNS) RNA viruses, Mononegavirales, cap their mRNA by an unconventional mechanism. Specifically, 5'-monophosphate mRNA is transferred to GDP derived from GTP through a reaction that involves a covalent intermediate between the large polymerase protein L and mRNA. The V region is essential for this process.
Pssm-ID: 405070 Cd Length: 241 Bit Score: 304.69 E-value: 4.34e-94
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region ...
1215-2204
1.84e-89
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region shared by paramyxovirus-like RNA-dependent RNA polymerases (see pfam00946). Polymerase proteins described by these two models are often called L protein (large polymerase protein). Capping of mRNA requires RNA triphosphatase and guanylyl transferase activities, demonstrated for the rinderpest virus L protein and at least partially localized to the region of this model.
Pssm-ID: 275046 [Multi-domain] Cd Length: 893 Bit Score: 313.66 E-value: 1.84e-89
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
1902-2002
8.66e-03
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 39.49 E-value: 8.66e-03
Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the ...
10-1089
0e+00
Mononegavirales RNA dependent RNA polymerase; Members of the Mononegavirales including the Paramyxoviridae, like other non-segmented negative strand RNA viruses, have an RNA-dependent RNA polymerase composed of two subunits, a large protein L and a phosphoprotein P. This is a protein family of the L protein. The L protein confers the RNA polymerase activity on the complex. The P protein acts as a transcription factor.
Pssm-ID: 395756 Cd Length: 1042 Bit Score: 1176.74 E-value: 0e+00
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, ...
1105-1357
4.34e-94
Mononegavirales mRNA-capping region V; This V domain of L RNA-polymerase carries a new motif, GxxTx(n)HR, that is essential for mRNA cap formation. Nonsegmented negative-sense (NNS) RNA viruses, Mononegavirales, cap their mRNA by an unconventional mechanism. Specifically, 5'-monophosphate mRNA is transferred to GDP derived from GTP through a reaction that involves a covalent intermediate between the large polymerase protein L and mRNA. The V region is essential for this process.
Pssm-ID: 405070 Cd Length: 241 Bit Score: 304.69 E-value: 4.34e-94
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region ...
1215-2204
1.84e-89
mRNA capping enzyme, paramyxovirus family; This model represents a common C-terminal region shared by paramyxovirus-like RNA-dependent RNA polymerases (see pfam00946). Polymerase proteins described by these two models are often called L protein (large polymerase protein). Capping of mRNA requires RNA triphosphatase and guanylyl transferase activities, demonstrated for the rinderpest virus L protein and at least partially localized to the region of this model.
Pssm-ID: 275046 [Multi-domain] Cd Length: 893 Bit Score: 313.66 E-value: 1.84e-89
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal ...
1902-2002
8.66e-03
FtsJ-like methyltransferase; This family consists of FtsJ from various bacterial and archaeal sources FtsJ is a methyltransferase, but actually has no effect on cell division. FtsJ's substrate is the 23S rRNA. The 1.5 A crystal structure of FtsJ in complex with its cofactor S-adenosylmethionine revealed that FtsJ has a methyltransferase fold. This family also includes the N terminus of flaviviral NS5 protein. It has been hypothesized that the N-terminal domain of NS5 is a methyltransferase involved in viral RNA capping.
Pssm-ID: 426399 Cd Length: 179 Bit Score: 39.49 E-value: 8.66e-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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The thumbnail image, if present, provides an approximate view of the feature's location in 3 dimensions.
Click on the triangle for interactive 3D structure viewing options.
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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Domains are color coded according to superfamilies
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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,
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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
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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