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Conserved domains on  [gi|1885452987|dbj|BCD41461|]
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RNA dependent RNA polymerase, partial [uncultured marine RNA virus]

Protein Classification

RNA-dependent RNA polymerase family protein( domain architecture ID 1750808)

RNA-dependent RNA polymerase (RdRp) family protein similar to the RdRp catalytic domain of alpha-, beta-, gamma-, delta-coronaviruses, including three highly pathogenic human coronaviruses (CoVs) such as Middle East respiratory syndrome (MERS)-related CoV, Severe acute respiratory syndrome (SARS) CoV, and SARS-CoV-2

EC:  2.7.7.48
Gene Ontology:  GO:0097747
PubMed:  29439438

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ps-ssRNAv_RdRp-like super family cl40470
conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense ...
1-155 2.00e-84

conserved catalytic core domain of RNA-dependent RNA polymerase (RdRp) from the positive-sense single-stranded RNA [(+)ssRNA] viruses and closely related viruses; This family contains the catalytic core domain of RdRp of RNA viruses which belong to Group IV of the Baltimore classification system, and are a group of related viruses that have positive-sense (+), single-stranded (ss) genomes made of ribonucleic acid (RNA). RdRp (also known as RNA replicase) catalyzes the replication of RNA from an RNA template; specifically, it catalyzes the synthesis of the RNA strand complementary to a given RNA template. The Baltimore Classification is divided into 7 classes, 3 of which include RNA viruses: Group IV (+) RNA viruses, Group III double-stranded (ds) RNA viruses, and Group V negative-sense (-) RNA viruses. Baltimore groups of viruses differ with respect to the nature of their genome (i.e., the nucleic acid form that is packaged into virions) and correspond to distinct strategies of genome replication and expression. (+) viral RNA is similar to mRNA and thus can be immediately translated by the host cell. (+)ssRNA viruses can also produce (+) copies of the genome from (-) strands of an intermediate dsRNA genome. This acts as both a transcription and a replication process since the replicated RNA is also mRNA. RdRps belong to the expansive class of polymerases containing so-called palm catalytic domains along with the accessory fingers and thumb domains. All RdRps also have six conserved structural motifs (A-F), located in its majority in the palm subdomain (A-E motifs) and the F motif is located on the finger subdomain. All these motifs have been shown to be implicated in RdRp fidelity such as processes of correct incorporation and reorganization of nucleotides. In addition to Group IV viruses, this model also includes Picobirnaviruses (PBVs), members of the family Picobirnaviridae of dsRNA viruses (Baltimore classification Group III), which are bi-segmented dsRNA viruses. The phylogenetic tree of the RdRps of RNA viruses (realm Riboviria) showed that picobirnaviruses are embedded in the branch of diverse (+)RNA viruses; sometimes they are collectively referred to as the picornavirus supergroup. RdRps of members of the family Permutatetraviridae, a distinct group of RNA viruses that encompass a circular permutation within the RdRp palm domain, are not included in this model.


The actual alignment was detected with superfamily member cd23195:

Pssm-ID: 477363  Cd Length: 310  Bit Score: 250.05  E-value: 2.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFID-IAKHCGYDARTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLR 79
Cdd:cd23195    87 YDKRMSAQLILAAFKILIDiAAKSGGYSEEDLKIMRGIATDIAYPLVDFNGDLIQFFGSNPSGHPLTVIINSIVNSLYMR 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  80 CSFYSIFSSE--IAFRSAVAAMTYGDDLKSSVSEKYPEFNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:cd23195   167 YAYYSLYPEKevPPFRDVVALMTYGDDNIMSVSPGYPWFNHTSIAEFLAKIGIKYTMADKEAESVPFIHISEADFLKR 244
 
Name Accession Description Interval E-value
Marnaviridae_RdRp cd23195
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of ...
1-155 2.00e-84

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Marnaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. They are mono- or dicistronic, have a polyadenylate tail and have conserved motifs for RNA helicase, RdRp, and structural protein domains. The first RNA virus isolated and characterized that infects a marine protist was Heterosigma akashiwo RNA virus (HaRNAV) in the genus Marnavirus, that infects the toxic bloom-forming Raphidophyte alga, Heterosigma akashiwo. Recently, it has undergone a major taxonomic revision and now includes 20 species within 7 genera, which include Bacillarnavirus, Kusarnavirus, Labyrnavirus, Locarnavirus, Marnavirus, Salisharnavirus, and Sogarnavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438045  Cd Length: 310  Bit Score: 250.05  E-value: 2.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFID-IAKHCGYDARTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLR 79
Cdd:cd23195    87 YDKRMSAQLILAAFKILIDiAAKSGGYSEEDLKIMRGIATDIAYPLVDFNGDLIQFFGSNPSGHPLTVIINSIVNSLYMR 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  80 CSFYSIFSSE--IAFRSAVAAMTYGDDLKSSVSEKYPEFNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:cd23195   167 YAYYSLYPEKevPPFRDVVALMTYGDDNIMSVSPGYPWFNHTSIAEFLAKIGIKYTMADKEAESVPFIHISEADFLKR 244
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
14-155 5.01e-08

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 50.87  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  14 FRIFIDIAKH-CGYDARTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRCSFYS----IFSS 88
Cdd:pfam00680 245 IRFAFEILRElLGFPSNVKEWRAILELLIYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLKslenDGPR 324
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  89 EIAFRSAVAAMTYGDDLKSSVS-EKYPEFNHVTyANYlkgFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:pfam00680 325 VCNLDKYFDFFTYGDDSLVAVSpDFDPVLDRLS-PHL---KELGLTITPAKKTFPVSRELEEVSFLKR 388
 
Name Accession Description Interval E-value
Marnaviridae_RdRp cd23195
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of ...
1-155 2.00e-84

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Marnaviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Marnaviridae, order Picornavirales. Member viruses have a (+)ssRNA genome. They are mono- or dicistronic, have a polyadenylate tail and have conserved motifs for RNA helicase, RdRp, and structural protein domains. The first RNA virus isolated and characterized that infects a marine protist was Heterosigma akashiwo RNA virus (HaRNAV) in the genus Marnavirus, that infects the toxic bloom-forming Raphidophyte alga, Heterosigma akashiwo. Recently, it has undergone a major taxonomic revision and now includes 20 species within 7 genera, which include Bacillarnavirus, Kusarnavirus, Labyrnavirus, Locarnavirus, Marnavirus, Salisharnavirus, and Sogarnavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438045  Cd Length: 310  Bit Score: 250.05  E-value: 2.00e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFID-IAKHCGYDARTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLR 79
Cdd:cd23195    87 YDKRMSAQLILAAFKILIDiAAKSGGYSEEDLKIMRGIATDIAYPLVDFNGDLIQFFGSNPSGHPLTVIINSIVNSLYMR 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  80 CSFYSIFSSE--IAFRSAVAAMTYGDDLKSSVSEKYPEFNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:cd23195   167 YAYYSLYPEKevPPFRDVVALMTYGDDNIMSVSPGYPWFNHTSIAEFLAKIGIKYTMADKEAESVPFIHISEADFLKR 244
ps-ssRNAv-Picornavirales cd23169
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of ...
1-155 7.49e-29

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the order Picornavirales of positive-sense single-stranded RNA [(+)ssRNA] viruses; This family contains the catalytic core domain of RdRp of Picornavirales, an order of (+)ssRNA viruses. The order Picornavirales comprises viruses that historically are referred to as picorna-like viruses and which are classified into eight virus families: Caliciviridae, Dicistroviridae, Iflaviridae, Marnaviridae, Picornaviridae, Polycipiviridae, Secoviridae, and Solinviviridae. All known genomes of Picornavirales members encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. The picornavirus genome is replicated via a negative-sense (-) RNA intermediate by the viral RdRp, named 3Dpol, which uses VPg (the product of 3B) as a primer to initiate the replication process. 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: 438019  Cd Length: 309  Bit Score: 107.30  E-value: 7.49e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFIDIAKHCGYDARTVaIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRC 80
Cdd:cd23169    89 FDGSLPPDVMEAAFDIINDWYDEYVDDEDER-VRKVLFEELINTIHLVGNLVYQVHGGNPSGNPLTTIINSIVNLLYIRY 167
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  81 SFYSIF--SSEIAFRSAVAAMTYGDDLKSSVSEKYPE-FNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:cd23169   168 AWLRITglTSLSDFKKNVRLVTYGDDVIISVSDEVKDeFNFVTISEFLKELGITYTDADKSGDIVPYRPLEEVTFLKR 245
RNA_dep_RNAP cd01699
RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the ...
1-155 8.43e-16

RNA_dep_RNAP: RNA-dependent RNA polymerase (RdRp) is an essential protein encoded in the genomes of all RNA containing viruses with no DNA stage. RdRp catalyzes synthesis of the RNA strand complementary to a given RNA template. RdRps of many viruses are products of processing of polyproteins. Some RdRps consist of one polypeptide chain, and others are complexes of several subunits. The domain organization and the 3D structure of the catalytic center of a wide range of RdRps, including those with a low overall sequence homology, are conserved. The catalytic center is formed by several motifs containing a number of conserved amino acid residues. This subfamily represents the RNA-dependent RNA polymerases from all positive-strand RNA eukaryotic viruses with no DNA stage.


Pssm-ID: 238843 [Multi-domain]  Cd Length: 278  Bit Score: 71.93  E-value: 8.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFIDIAKHCGYDARTVAIMEGIASDISYplmaYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRC 80
Cdd:cd01699   106 FDSSLSPQLLEAEHSIYNALYDDDDELERRNLLRSLTNNSLHI----GFNEVYKVRGGRPSGDPLTSIGNSIINCILVRY 181
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1885452987  81 SFYSIFSSEiaFRSAVAAMTYGDDLKSSVSEKYPEFNHVTYANYLKGFDivFTMPDKESKATEYMHGLDADFLKR 155
Cdd:cd01699   182 AFRKLGGKS--FFKNVRLLNYGDDCLLSVEKADDKFNLETLAEWLKEYG--LTMTDEDKVESPFRPLEEVEFLKR 252
Dicistroviridae_RdRp cd23194
RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense ...
1-155 2.76e-13

RNA-dependent RNA polymerase (RdRp) in the family Dicistroviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the RdRp of RNA viruses belonging to the family Dicistroviridae, order Picornavirales. Dicistroviridae is a family of small non-enveloped viruses with a (+)ssRNA genome of approximately 8-10 kilobases. The family contains 3 genera: Aparavirus, Cripavirus, and Triatovirus. All members infect arthropod hosts with some having devastating economic consequences, such as acute bee paralysis virus, Kashmir bee virus, and Israeli acute paralysis virus in domesticated honeybees, and taura syndrome virus and mud crab virus in the seafood industry. On the contrary, host specificity and other desirable traits make several members of this group amenable to development as biopesticides for insect control, such as Solenopsis invicta virus 1 against fire ants, and triatoma virus against triatomine bugs that vector Chagas disease. Members in the family Dicistroviridae have similarity to viruses in the Picornavirales members (Iflaviridae, Picornaviridae, Marnaviridae and Secoviridae). The genomes of viruses of these taxa encode proteins with helicase, 3C-like protease, and RdRp domains, as well as capsid proteins with related structures, although the genome organizations can differ among viruses. 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: 438044 [Multi-domain]  Cd Length: 315  Bit Score: 65.60  E-value: 2.76e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFIDIakhcgYD-----ARtvaIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNS 75
Cdd:cd23194    94 FDGSLNPQILWAILDIINEW-----YDdgeenAL---IRRVLWEDIVNSVHICGGYVYQWTHSQPSGNPLTAIINSIYNS 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  76 LLLRCSFYSIFSSEIA-----FRSAVAAMTYGDDLKSSVSEKYPE-FNHVTYANYLKGFDIVFTMPDKESKATEYMHGLD 149
Cdd:cd23194   166 IIMRYVYLLLTKEAGLmtmsdFNKHVSMVSYGDDNVINVSDEVSEwFNQLTITEAMAEIGMTYTDETKTGEIVPYRSLEE 245

                  ....*.
gi 1885452987 150 ADFLKR 155
Cdd:cd23194   246 VSFLKR 251
RdRP_1 pfam00680
Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase ...
14-155 5.01e-08

Viral RNA-dependent RNA polymerase; This family represents the RNA-directed RNA polymerase found in many positive strand RNA eukaryotic viruses. Structural studies indicate that these proteins form the "right hand" structure found in all oligonucleotide polymerases, containing thumb, finger and palm domains, and also the additional bridging finger and thumb domains unique to RNA-directed RNA polymerases.


Pssm-ID: 425815  Cd Length: 450  Bit Score: 50.87  E-value: 5.01e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  14 FRIFIDIAKH-CGYDARTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRCSFYS----IFSS 88
Cdd:pfam00680 245 IRFAFEILRElLGFPSNVKEWRAILELLIYTPIALPNGTVFKKTGGLPSGSPFTSIINSIVNYLLILYALLKslenDGPR 324
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1885452987  89 EIAFRSAVAAMTYGDDLKSSVS-EKYPEFNHVTyANYlkgFDIVFTMPDKESKATEYMHGLDADFLKR 155
Cdd:pfam00680 325 VCNLDKYFDFFTYGDDSLVAVSpDFDPVLDRLS-PHL---KELGLTITPAKKTFPVSRELEEVSFLKR 388
Secoviridae_RdRp cd23196
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Secoviridae of ...
60-155 7.36e-06

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Secoviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Secoviridae, order Picornavirales. Members of the family Secoviridae are non-enveloped viruses with mono- or bipartite (RNA-1 and RNA-2) linear (+)ssRNA genomes of 9 to 13.7 kilobases in total. Secoviruses are related to picornaviruses and are classified in the order Picornavirales. The majority of known members infect dicotyledonous plants and many are important plant pathogens (e.g., grapevine fanleaf virus and rice tungro spherical virus). The Secoviridae includes 8 genera (Comovirus, Fabavirus, Nepovirus, Cheravirus, Sadwavirus, Torradovirus, Sequivirus, and Waikavirus) as well as unassigned species (strawberry latent ringspot virus-MEN 454, strawberry mottle virus-Thompson, black raspberry necrosis virus- 1, chocolate lily virus A-KP2, and Dioscorea mosaic associated virus-goiana). RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438046  Cd Length: 309  Bit Score: 44.30  E-value: 7.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  60 PSGQNLTVYLNGVVNSLLLRCSFYSIFSSEIA--FRSAVAAMTYGDDLKSSVSEK-YPEFNHVTYANYLKGFDIVFT-MP 135
Cdd:cd23196   145 PSGCALTVIINSIFNEILIRYVYRKVVPRPARnnFNKYVRLVVYGDDNLISVKEEiIPYFDGPVIKKEMAKVGVTITdGT 224
                          90       100
                  ....*....|....*....|
gi 1885452987 136 DKESKATEYMHGLDADFLKR 155
Cdd:cd23196   225 DKTSPTLERKPLESLDFLKR 244
Cosavirus_RdRp cd23226
RNA-dependent RNA polymerase (RdRp) in the genus Cosavirus of positive-sense single-stranded ...
25-155 3.85e-05

RNA-dependent RNA polymerase (RdRp) in the genus Cosavirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Cosavirus genus within the family Picornaviridae, order Picornavirales. The Cosavirus contains viruses with (+)ssRNA genomes that produce nonenveloped virions. This genus consists of five species Cosavirus A, Cosavirus B, Cosavirus D, Cosavirus E and Cosavirus F. The candidate species, Cosavirus C, remains unclassified due to a lack of full genome sequence data. Cosaviruses (formerly called Dekaviruses) have been identified in the stools of south Asian children. Cosaviruses are most closely related to members of the Cardiovirus and Senecavirus genera, but they lack a leader polypeptide. The name Cosavirus stands for common stool-associated picornavirus. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438076  Cd Length: 461  Bit Score: 42.31  E-value: 3.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  25 GYDARTVAIMEGIASDISyplmAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRCSFYSIFSSeiaFR-SAVAAMTYGD 103
Cdd:cd23226   263 GFDHRCSLMIDSLVTSTH----CYEDQRMTIRGGLPSGTSGTSVINTIINNIIFKAALYHTYSN---FEwDDVQMLAYGD 335
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1885452987 104 DLKSSvSEKYPEFNHVTYANYLKGFDIvfTMPDKESKAT-EYMHGLdaDFLKR 155
Cdd:cd23226   336 DIVAA-SDCLLDLDRVKYFMALIGYKI--TPADKGEKFIpKDMQNI--QFLKR 383
Nora-virus_RdRp cd23200
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like ...
1-155 3.25e-04

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in a novel picorna-like Drosophila virus, Nora virus; This group contains the catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the unclassified Nora virus, a new picorna-like virus family. Nora virus has a (+)ssRNA genome followed by a poly(A) tail. Unlike other picorna-like viruses, the genome has four open reading frames (ORFs). One ORF encodes a picornavirus-like cassette of proteins for virus replication, including an iflavirus-like RdRp and a helicase that is related to those of mammalian picornaviruses. The three other ORFs are not closely related to any previously described viruses. Nora virus is present as a persistent infection in several tested laboratory stocks and wild-caught flies. 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: 438050  Cd Length: 306  Bit Score: 39.52  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFIDIAKHCGYD----ARTVAIMEGIASdisypLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSL 76
Cdd:cd23200    88 YDKYLHRQVFKAVRKIQRSVIQQVCPDkwdkARAVEELDAIDT-----YVVDYQTVYKTNRGNKSGSYTTTIDNCLANDI 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  77 LLRCSFYSIFS--SEIAFRSAVAAMTYGDDLKSSVSEKYPE-FNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFL 153
Cdd:cd23200   163 YGLYAWVKTTGlrSLWDYRQNVSSVAFGDDIIKSVSDEYKDkYNYCTYRDVLNATGHIMTPGSKDGEEKPFTSFENLQFL 242

                  ..
gi 1885452987 154 KR 155
Cdd:cd23200   243 KR 244
Hepatovirus_RdRp cd23215
RNA-dependent RNA polymerase (RdRp) in the genus Hepatovirus of positive-sense single-stranded ...
35-105 1.86e-03

RNA-dependent RNA polymerase (RdRp) in the genus Hepatovirus of positive-sense single-stranded RNA [(+)ssRNA] viruses, within the family Picornaviridae; This group contains the RdRp of RNA viruses belonging to the Hepatovirus genus within the family Picornaviridae, order Picornavirales. Hepatoviruses are 27- to 32-nm, nonenveloped, icosahedral viruses with a (+)ssRNA linear genome of approximately 7.5-kb. The Hepatovirus genus has nine species, Hepatovirus A-I, of which Hepatovirus A is responsible for a self-limiting viral hepatitis in human beings and may be transmitted by the fecal-oral route during acute infection or by the ingestion of uncooked contaminated shellfish. RdRps are multi-domain proteins that play a pivotal role in enterovirus replication. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of hepatoviruses. 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: 438065  Cd Length: 464  Bit Score: 37.52  E-value: 1.86e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1885452987  35 EGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRCSFYSIF-SSEIAFRSAVAAMTYGDDL 105
Cdd:cd23215   251 QALINTIIYSKHLLYNLCYHVCGSMPSGSPCTSLLNSIVNNVNLYYVFSKIFkKSPVFFYDAVKFLCYGDDV 322
Polycipiviridae_RdRp cd23198
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of ...
1-154 3.49e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Polycipiviridae of positive-sense single-stranded RNA [(+)ssRNA] viruses, in the order Picornavirales; This group contains the catalytic core domain of RdRp of RNA viruses belonging to the family Polycipiviridae (polycistronic picorna-like viruses), order Picornavirales. Polycipiviridae is a family of picorna-like viruses with non-segmented, linear, (+)ssRNA genomes of approximately 10-12 kb. Their genomes are polycistronic, with four (or more) consecutive 5'-proximal open reading frames (ORFs) encoding structural (and possibly other) proteins and a long 3' ORF encoding the replication polyprotein. Members of species within the family are typically found in ants, with Apple picorna-like virus 1 and the unnamed Polycipiviridae virus in fruit bat stool as exceptions. RdRps catalyze RNA template-dependent formation of phosphodiester bonds between ribonucleotides in the presence of divalent metal ions. The initiation of synthesis occurs at the 3'-end of the template in a VPg-dependent manner, and proceeds in the direction of 5'-3'. The active sites of RdRps are highly conserved in different species of picornaviruses. 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: 438048  Cd Length: 317  Bit Score: 36.62  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987   1 YDLRMPAQLMMASFRIFIDIAKHCGYDaRTVAIMEGIASDISYPLMAYNGDLLQLFGSNPSGQNLTVYLNGVVNSLLLRC 80
Cdd:cd23198    94 WDGHLPAELFYAVLDIIKTVLGLKPNS-PNAKVIYSILTEVMNCHIQFEDIIYQKLRGLISGFPGTAEVNTLAHWLLIYY 172
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1885452987  81 SFYSIFSSEI------AFRSAVAAMTYGDDLKSSVS-EKYPEFNHVTYANYLKGFDIVFTMPDKESKATEYMHGLDADFL 153
Cdd:cd23198   173 IYLYLAQNTIydmtitAFLRNVSAIFYGDDIIITISdEILHWFNGKTIQRMYEEHGYPVTSAAKDTEIPESKPLSDCQFL 252

                  .
gi 1885452987 154 K 154
Cdd:cd23198   253 K 253
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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