Reviewed,
UniProtKB/Swiss-Prot P26676 (L_PI2HT)
Last modified
June 16, 2009.
Version 56.
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 | Human parainfluenza 2 virus (strain Toshiba) (HPIV-2) | ||
| Taxonomic identifier | 11214 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Rubulavirus | ||
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 2262 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 + m7G(5')pppR-RNA. |
| Subunit structure | Interacts with the P protein By similarity. |
| Subcellular location | Virion Potential. Host cytoplasm By similarity. |
| Sequence similarities | Belongs to the paramyxoviruses L protein family. Contains 1 RdRp catalytic domain. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 2262 | 2262 | Large structural protein | PRO_0000142734 | |||||
Regions | |||||||||
| Domain | 661 – 844 | 184 | RdRp catalytic | ||||||
| Nucleotide binding | 1810 – 1819 | 10 | ATP Potential | ||||||
Sequences
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References
| [1] | "Characterizations of the human parainfluenza type 2 virus gene encoding the L protein and the intergenic sequences." Kawano M., Okamoto K., Bando H., Kondo K., Tsurudome M., Komada H., Nishio M., Ito Y. Nucleic Acids Res. 19:2739-2746(1991) [PubMed: 1645865] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
|---|---|
| X57559 Genomic RNA. Translation: CAA40788.1. | |
| PIR | S16664. |
| RefSeq | NP_598406.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 935189. |
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... |
Other Resources | |
| DrugBank | DB00811. Ribavirin. |
Entry information
| Entry name | L_PI2HT | ||||||||
| Accession | Primary (citable) accession number: P26676 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

Clusters with


