Reviewed,
UniProtKB/Swiss-Prot Q98776 (L_VSIVM)
Last modified
January 19, 2010.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
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Names and origin
| Protein names | Recommended name: Large structural protein Short name=Protein L Alternative name(s): Transcriptase Replicase Including the following 3 domains: 1- Recommended name: RNA-directed RNA polymerase EC=2.7.7.48 2- Recommended name: mRNA (guanine-N(7)-)-methyltransferase EC=2.1.1.56 3- Recommended name: mRNA guanylyltransferase EC=2.7.7.- | ||
| Gene names |
| ||
| Organism | Vesicular stomatitis Indiana virus (strain Mudd-Summers) (VSIV) | ||
| Taxonomic identifier | 11279 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Rhabdoviridae › Dimarhabdovirus supergroup › Vesiculovirus | ||
| Virus host | Aedes [TaxID: 7158] Simuliidae (black flies) [TaxID: 7190] Musca domestica (House fly) [TaxID: 7370] Homo sapiens (Human) [TaxID: 9606] Equus asinus (Donkey) [TaxID: 9793] Equus caballus (Horse) [TaxID: 9796] Sus scrofa (Pig) [TaxID: 9823] Bos taurus (Bovine) [TaxID: 9913] Culicoides [TaxID: 58271] Lutzomyia [TaxID: 252607] |
Protein attributes
| Sequence length | 2109 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Displays RNA-directed RNA polymerase, mRNA guanylyl transferase, mRNA (guanine-N(7)-)-methyltransferase and poly(A) synthetase activities. The viral mRNA guanylyl transferase displays a different biochemical reaction than the cellular enzyme. The template is composed of the viral RNA tightly encapsidated by the nucleoprotein (N). Functions either as transcriptase or as replicase. The transcriptase synthesizes subsequently five subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. The replicase mode is dependent on intracellular N protein concentration. In this mode, the polymerase replicates the whole viral genome without recognizing the transcriptional signals By similarity. |
| Catalytic activity | Nucleoside triphosphate + RNA(n) = diphosphate + RNA(n+1). S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA. |
| Subunit structure | Interacts with the P protein to form the functional polymerase By similarity. |
| Subcellular location | Virion. Host cytoplasm By similarity. |
| Sequence similarities | Belongs to the rhabdoviridae protein L family. Contains 1 RdRp catalytic domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2109 | 2109 | Large structural protein | PRO_0000287265 | |||||
Regions | |||||||||
| Domain | 598 – 784 | 187 | RdRp catalytic | ||||||
| Nucleotide binding | 1667 – 1676 | 10 | ATP Potential | ||||||
Sequences
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References
| [1] | "Primary structure of the vesicular stomatitis virus polymerase (L) gene: evidence for a high frequency of mutations." Schubert M., Harmison G.G., Meier E. J. Virol. 51:505-514(1984) [PubMed: 6086959] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | K02378 Genomic RNA. Translation: AAA48441.1. |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR014023. RNA-dir_pol_cat. IPR017234. RNA-dir_pol_rhabdovirus. IPR001016. RNA_pol_L_viral. IPR002877. rRNA_MeTrfase_RrmJ/FtsJ. [Graphical view] |
| Pfam | PF01728. FtsJ. 1 hit. PF00946. Paramyx_RNA_pol. 1 hit. [Graphical view] |
| PIRSF | PIRSF037546. RNA_pol_RhabdoV_sub. 1 hit. |
| PROSITE | PS50526. RDRP_SSRNA_NEG_NONSEG. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | L_VSIVM | ||||||||
| Accession | Primary (citable) accession number: Q98776 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

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