Reviewed,
UniProtKB/Swiss-Prot P41357 (L_RINDR)
Last modified
November 25, 2008.
Version 46.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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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 | Rinderpest virus (strain RBOK) (RDV) | ||
| Taxonomic identifier | 36409 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Morbillivirus | ||
| Virus host | Suidae (pigs) [TaxID: 9821] Hippopotamus [TaxID: 9832] Giraffa camelopardalis (Giraffe) [TaxID: 9894] Bos taurus (Bovine) [TaxID: 9913] Bos indicus (Zebu) [TaxID: 9915] Capra hircus (Goat) [TaxID: 9925] Gazella (gazelles) [TaxID: 9933] Ovis aries (Sheep) [TaxID: 9940] Bubalus bubalis (Domestic water buffalo) [TaxID: 89462] |
Protein attributes
| Sequence length | 2183 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| 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 the subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. The transcriptase stutters on a specific sequence, resulting on a cotranscriptional editing of the phosphoprotein (P) mRNA. 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 + m(7)G(5')pppR-RNA. |
| Subunit structure | Interacts with the P protein By similarity. |
| Subcellular location | |
| Sequence similarities | Belongs to the paramyxoviruses L protein family. Contains 1 RdRp catalytic domain. |
Ontologies
Keywords | |
|---|---|
| Biological process | RNA replication mRNA capping mRNA processing |
| Cellular component | Cytoplasm Virion |
| Ligand | ATP-binding Nucleotide-binding S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Nucleotidyltransferase RNA-directed RNA polymerase Transferase |
| Technical term | Multifunctional enzyme |
Gene Ontology (GO) | |
| Biological process | mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW transcription, RNA-dependentInferred from electronic annotation. Source: UniProtKB-KW |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW virionInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA bindingInferred from electronic annotation. Source: InterPro RNA-directed RNA polymerase activityInferred from electronic annotation. Source: InterPro mRNA (guanine-N7-)-methyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2183 | 2183 | Large structural protein | PRO_0000142735 | |||||
Regions | |||||||||
| Domain | 656 – 840 | 185 | RdRp catalytic | ||||||
| Nucleotide binding | 1785 – 1794 | 10 | ATP Potential | ||||||
Sequences
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References
| [1] | "Sequencing and analysis of the nucleocapsid (N) and polymerase (L) genes and the terminal extragenic domains of the vaccine strain of rinderpest virus." Baron M.D., Barrett T. J. Gen. Virol. 76:593-602(1995) [PubMed: 7897350] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
|---|---|
| Z30698 Genomic RNA. Translation: CAA83184.1. Z30697 Genomic RNA. Translation: CAA83183.1. | |
| PIR | S47307. |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR016269. RNA-dir_RNA_pol_paramyxovir. IPR014023. RNA_pol_cat. IPR001016. RNA_pol_L_viral. [Graphical view] |
| Pfam | PF00946. Paramyx_RNA_pol. 1 hit. [Graphical view] |
| PIRSF | PIRSF000830. RNA_pol_ParamyxoV. 1 hit. |
| PROSITE | PS50526. RDRP_SSRNA_NEG_NONSEG. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | L_RINDR | ||||||||
| Accession | Primary (citable) accession number: P41357 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

Clusters with


