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Conserved domains on  [gi|1013288201|dbj|BAU70606|]
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RNA dependent RNA polymerase, partial [Magnaporthe oryzae chrysovirus 1]

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 ...
179-445 1.87e-21

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 pfam02123:

Pssm-ID: 477363  Cd Length: 465  Bit Score: 96.38  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 179 FEFAEFPAIV----KRVLADYVPNS--FTRYFIKNEIGK----PAGRPLYPSHLAHYVVGQFALYALMKAQPIPKVRLTA 248
Cdd:pfam02123 199 LRLLSSVSLVdqlvRRMLFEPQNNNeiAWWGSVPSKPSMklehGKSRAIYACDTRSYLAFEYLLAPVEKAWANKSVILNP 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 249 ERdvaMDEHWMWMQAREFT---VGVMLDYDNFNEKHEFADMQLIMRELKglyrtaGVLSPDLKVMIDWVAEAYDRTVLEY 325
Cdd:pfam02123 279 GE---GDISGFDWSVQDWKrggVSLMLDYDDFNSQHSTESMRAVFERLR------RRLPDEPAEAADWLVCSMDSMYQLS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 326 DGE-LHSFKHG-MLSGQAPTSAINNIINgankRLLIrqveELTGRVIFQKRTS--GGDDV-AGETySLYDAYLAVKCGQL 400
Cdd:pfam02123 350 DGTlLAQRVPGtLKSGHRATTFINSVLN----CAYA----ELAGAPWADVPTSihMGDDVlEGLR-TPADATSLLDKYAR 420
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1013288201 401 MGLAFKDIKQLLSADYYEFFRLFVSVQGVHGSLPRALGSICSGQW 445
Cdd:pfam02123 421 LGFKVNPSKQSVGHTIAEFLRVAFCSHEVRGYLARAIASLVSGNW 465
 
Name Accession Description Interval E-value
RdRP_4 pfam02123
Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins ...
179-445 1.87e-21

Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins (RdRPs) from Luteovirus, Totivirus and Rotavirus.


Pssm-ID: 280316  Cd Length: 465  Bit Score: 96.38  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 179 FEFAEFPAIV----KRVLADYVPNS--FTRYFIKNEIGK----PAGRPLYPSHLAHYVVGQFALYALMKAQPIPKVRLTA 248
Cdd:pfam02123 199 LRLLSSVSLVdqlvRRMLFEPQNNNeiAWWGSVPSKPSMklehGKSRAIYACDTRSYLAFEYLLAPVEKAWANKSVILNP 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 249 ERdvaMDEHWMWMQAREFT---VGVMLDYDNFNEKHEFADMQLIMRELKglyrtaGVLSPDLKVMIDWVAEAYDRTVLEY 325
Cdd:pfam02123 279 GE---GDISGFDWSVQDWKrggVSLMLDYDDFNSQHSTESMRAVFERLR------RRLPDEPAEAADWLVCSMDSMYQLS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 326 DGE-LHSFKHG-MLSGQAPTSAINNIINgankRLLIrqveELTGRVIFQKRTS--GGDDV-AGETySLYDAYLAVKCGQL 400
Cdd:pfam02123 350 DGTlLAQRVPGtLKSGHRATTFINSVLN----CAYA----ELAGAPWADVPTSihMGDDVlEGLR-TPADATSLLDKYAR 420
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1013288201 401 MGLAFKDIKQLLSADYYEFFRLFVSVQGVHGSLPRALGSICSGQW 445
Cdd:pfam02123 421 LGFKVNPSKQSVGHTIAEFLRVAFCSHEVRGYLARAIASLVSGNW 465
Iflaviridae_RdRp cd23197
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae of ...
270-381 1.43e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae 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 Iflaviridae, order Picornavirales. Iflaviridae is a family of small non-enveloped viruses with (+)ssRNA genomes of approximately 9-11 kilobases in length encoding a single polyprotein. All members infect arthropod hosts with the majority infecting insects. Beneficial and pest insects serve as hosts and infections can be symptomless (Nilaparvata lugens honeydew virus 1), cause developmental abnormalities (deformed wing virus, Varroa destructor virus 1, sacbrood virus), behavioral changes (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, sacbrood virus) and premature mortality (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, infectious flacherie virus, sacbrood virus). 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: 438047  Cd Length: 319  Bit Score: 40.62  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 270 VMLDYDNFNEKHEFADMQLIMRELKGLYRTAGVLSPDLKVMIDWVA-EAYDRTVLEYdGELHSFKHGMLSGQAPTSAINN 348
Cdd:cd23197    88 LQMDYKNYSDAIPKECVAKAFHIIVDYYRKWHCLTVEIENALKTLFlDTADAELLVY-GDVFKVNNGVLAGHPMTSVVNS 166
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1013288201 349 IINGANKRLLIRQVEELTGRVIFqkRTSG----GDDV 381
Cdd:cd23197   167 VVNLILMNYMWIKITRRRASEFF--KLTYiivmGDDV 201
 
Name Accession Description Interval E-value
RdRP_4 pfam02123
Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins ...
179-445 1.87e-21

Viral RNA-directed RNA-polymerase; This family includes RNA-dependent RNA polymerase proteins (RdRPs) from Luteovirus, Totivirus and Rotavirus.


Pssm-ID: 280316  Cd Length: 465  Bit Score: 96.38  E-value: 1.87e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 179 FEFAEFPAIV----KRVLADYVPNS--FTRYFIKNEIGK----PAGRPLYPSHLAHYVVGQFALYALMKAQPIPKVRLTA 248
Cdd:pfam02123 199 LRLLSSVSLVdqlvRRMLFEPQNNNeiAWWGSVPSKPSMklehGKSRAIYACDTRSYLAFEYLLAPVEKAWANKSVILNP 278
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 249 ERdvaMDEHWMWMQAREFT---VGVMLDYDNFNEKHEFADMQLIMRELKglyrtaGVLSPDLKVMIDWVAEAYDRTVLEY 325
Cdd:pfam02123 279 GE---GDISGFDWSVQDWKrggVSLMLDYDDFNSQHSTESMRAVFERLR------RRLPDEPAEAADWLVCSMDSMYQLS 349
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 326 DGE-LHSFKHG-MLSGQAPTSAINNIINgankRLLIrqveELTGRVIFQKRTS--GGDDV-AGETySLYDAYLAVKCGQL 400
Cdd:pfam02123 350 DGTlLAQRVPGtLKSGHRATTFINSVLN----CAYA----ELAGAPWADVPTSihMGDDVlEGLR-TPADATSLLDKYAR 420
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1013288201 401 MGLAFKDIKQLLSADYYEFFRLFVSVQGVHGSLPRALGSICSGQW 445
Cdd:pfam02123 421 LGFKVNPSKQSVGHTIAEFLRVAFCSHEVRGYLARAIASLVSGNW 465
Iflaviridae_RdRp cd23197
catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae of ...
270-381 1.43e-03

catalytic core domain of RNA-dependent RNA polymerase (RdRp) in the family Iflaviridae 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 Iflaviridae, order Picornavirales. Iflaviridae is a family of small non-enveloped viruses with (+)ssRNA genomes of approximately 9-11 kilobases in length encoding a single polyprotein. All members infect arthropod hosts with the majority infecting insects. Beneficial and pest insects serve as hosts and infections can be symptomless (Nilaparvata lugens honeydew virus 1), cause developmental abnormalities (deformed wing virus, Varroa destructor virus 1, sacbrood virus), behavioral changes (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, sacbrood virus) and premature mortality (deformed wing virus, Varroa destructor virus 1, slow bee paralysis virus, infectious flacherie virus, sacbrood virus). 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: 438047  Cd Length: 319  Bit Score: 40.62  E-value: 1.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1013288201 270 VMLDYDNFNEKHEFADMQLIMRELKGLYRTAGVLSPDLKVMIDWVA-EAYDRTVLEYdGELHSFKHGMLSGQAPTSAINN 348
Cdd:cd23197    88 LQMDYKNYSDAIPKECVAKAFHIIVDYYRKWHCLTVEIENALKTLFlDTADAELLVY-GDVFKVNNGVLAGHPMTSVVNS 166
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1013288201 349 IINGANKRLLIRQVEELTGRVIFqkRTSG----GDDV 381
Cdd:cd23197   167 VVNLILMNYMWIKITRRRASEFF--KLTYiivmGDDV 201
 
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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