Birnavirus RNA dependent RNA polymerase (VP1), palm domain; Birnaviruses are dsRNA viruses. This entry corresponds to the "palm" domain of the RNA dependent RNA polymerase, also known as VP1. All of the birnavirus VP1 proteins contain conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases. However, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. The catalytic motifs are arranged in a permuted order in sequence.
The actual alignment was detected with superfamily member pfam04197:
Pssm-ID: 461223 Cd Length: 531 Bit Score: 360.44 E-value: 1.70e-113
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. ...
580-710
4.24e-10
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. The RNA dependent RNA polymerase, also known as VP1, contains the conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases but in a characteriztic permuted order, thus, it adopts a unique active site topology. Additionally, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. This entry covers the thumb domain of RdRP from Birnaviruses.
The actual alignment was detected with superfamily member pfam20488:
Pssm-ID: 466637 Cd Length: 167 Bit Score: 59.53 E-value: 4.24e-10
Birnavirus RNA dependent RNA polymerase (VP1), palm domain; Birnaviruses are dsRNA viruses. This entry corresponds to the "palm" domain of the RNA dependent RNA polymerase, also known as VP1. All of the birnavirus VP1 proteins contain conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases. However, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. The catalytic motifs are arranged in a permuted order in sequence.
Pssm-ID: 461223 Cd Length: 531 Bit Score: 360.44 E-value: 1.70e-113
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. ...
580-710
4.24e-10
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. The RNA dependent RNA polymerase, also known as VP1, contains the conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases but in a characteriztic permuted order, thus, it adopts a unique active site topology. Additionally, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. This entry covers the thumb domain of RdRP from Birnaviruses.
Pssm-ID: 466637 Cd Length: 167 Bit Score: 59.53 E-value: 4.24e-10
Birnavirus RNA dependent RNA polymerase (VP1), palm domain; Birnaviruses are dsRNA viruses. This entry corresponds to the "palm" domain of the RNA dependent RNA polymerase, also known as VP1. All of the birnavirus VP1 proteins contain conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases. However, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. The catalytic motifs are arranged in a permuted order in sequence.
Pssm-ID: 461223 Cd Length: 531 Bit Score: 360.44 E-value: 1.70e-113
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. ...
580-710
4.24e-10
Birnavirus RNA dependent RNA polymerase (VP1), thumb domain; Birnaviruses are dsRNA viruses. The RNA dependent RNA polymerase, also known as VP1, contains the conserved RdRp motifs that reside in the catalytic "palm" domain of all classes of polymerases but in a characteriztic permuted order, thus, it adopts a unique active site topology. Additionally, the birnavirus RdRps lack the highly conserved Gly-Asp-Asp (GDD) sequence, a component of the proposed catalytic site of this enzyme family that exists in the conserved motif VI of the palm domain of other RdRps. This entry covers the thumb domain of RdRP from Birnaviruses.
Pssm-ID: 466637 Cd Length: 167 Bit Score: 59.53 E-value: 4.24e-10
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 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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