EC Number   |
General Information |
Reference |
|---|
   2.7.7.88 | evolution |
the putative RABV PRNTase domain (residues 1093-1349) shares five conserved motifs, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids) with those in L proteins of NNS RNA viruses belonging to the the order Mononegavirales. The structural model of the putative RABV PRNTase domain suggests that it possesses a large loop structure flanking the PRNTase motif B, which corresponds to a priming loop proposed for the VSV L protein |
-, 762507 |
| 2.7.7.88 | evolution |
the unconventional mRNA capping enzyme (GDP polyribonucleotidyltransferase, PRNTase) or block V domain in RNA polymerase L proteins of nonsegmented negative strand (NNS) RNA viruses (e.g. rabies, measles, Ebola) contains five collinear sequence elements, Rx(3)Wx(3-8)PhixGxdeltax(P/A) (motif A), (Y/W)PhiGSxT (motif B), W (motif C), HR (motif D), and deltaxxPhix(F/Y)QxxPhi (motif E) (Phi = hydrophobic, delta = hydrophilic amino acids). Identification of conserved motifs in putative PRNTase domains. Phylogenetic analysis of putative PRNTase domains in NNS RNA viral L proteins, overview |
-, 762033 |
| 2.7.7.88 | malfunction |
Cap-defective mutants produce uncapped abortive transcripts by aberrant stop-start transcription. Cap defective mutations in these residues induced termination of mRNA synthesis at position +40 followed by aberrant stop-start transcription, and abolished virus gene expression in host cells |
-, 762033 |
| 2.7.7.88 | metabolism |
molecular mechanisms of RABV RNA biogenesis, overview. In the second step, the PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA. Roles of RABV replication proteins in transcription and replication, and unique RABV machineries required for mRNA capping and transcription initiation. Comparison of Rabies virus mechanism of mRNA capping with that of eukaryotic cells |
-, 762507 |
| 2.7.7.88 | more |
residues G1112 in motif A, T1170 in motif B, W1201 in motif C, H1241 and R1242 in motif D, and F1285 and Q1286 in motif E are identified as essential for the PRNTase activity of the RABV L protein. The RABV counterpart (H1241) of the VSV H1227 residue can be predicted to serve as a covalent pRNA attachment site for the putative L-pRNA intermediate formation. Structure and structure-function analysis, overview |
-, 762507 |
| 2.7.7.88 | more |
signature motifs of GDP polyribonucleotidyltransferase, a non-segmented negative strand RNA viral mRNA capping enzyme, domain in the L protein are required for covalent enzyme-pRNA intermediate formation, overview. Similar to the catalytic residues in motif D, G1100 in motif A, T1157 in motif B, W1188 in motif C, and F1269 and Q1270 in motif E were found to be essential or important for the PRNTase activity in the step of the covalent LpRNA intermediate formation, but not for the GTPase activity that generates GDP (pRNA acceptor) |
-, 762033 |
| 2.7.7.88 | physiological function |
RNA polymerase L protein shows RNA:GDP polyribonucleotidyltransferase activity, which transfers the 5'-monophosphorylated viral mRNA start sequence to GDP to produce a capped RNA. The conserved HR motif in the L protein is essential for the this activity. L protein forms two distinct SDS-resistant complexes with the mRNA and leader RNA start sequences, mutations in the HR motif significantly reduce the formation of the former complex, but not the latter complex |
-, 734399 |
| 2.7.7.88 | physiological function |
the conserved motifs constitute the active site of the PRNTase domain and the L-pRNA intermediate formation followed by the cap formation is essential for successful synthesis of full-length mRNAs. The PRNTase motifs are required for VSV gene expression in host cells |
-, 762033 |
| 2.7.7.88 | physiological function |
the large (L) protein of the rabies virus (RABV) is a multifunctional RNA-dependent RNA-polymerase. Transcriptional control and mRNA capping are exerted by the GDP polyribonucleotidyltransferase domain of the rabies virus large protein. It catalyzes mRNA processing reactions, such as 5'-capping, cap methylation, and 3'-polyadenylation, in addition to RNA synthesis. The PRNTase domain in the VSV L protein transfers 5'-monophosphate-ended RNA (pRNA) from pppRNA (pRNA donor) to GDP (pRNA acceptor) through a covalent enzyme-(histidyl-N'')-pRNA (called L-pRNA) intermediate to generate GpppRNA, roles of the GDP polyribonucleotidyltransferase (PRNTase) domain of the rabies virus (RABV) large (L) protein in transcription initiation and pre-mRNA capping |
-, 762507 |
