O89344 (L_HENDH) Reviewed, UniProtKB/Swiss-Prot
Last modified
December 14, 2011.
Version 59.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: RNA-directed RNA polymerase L Short name=Protein L Alternative name(s): Large structural protein Replicase Transcriptase Including the following 3 domains:
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| Gene names |
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| Organism | Hendra virus (isolate Horse/Autralia/Hendra/1994) | ||
| Taxonomic identifier | 928303 [NCBI] | ||
| Taxonomic lineage | Viruses › ssRNA negative-strand viruses › Mononegavirales › Paramyxoviridae › Paramyxovirinae › Henipavirus | ||
| Virus host | Pteropus alecto (Black flying fox) [TaxID: 9402] Pteropus poliocephalus (Grey-headed flying fox) [TaxID: 9403] Homo sapiens (Human) [TaxID: 9606] Equus caballus (Horse) [TaxID: 9796] Pteropus scapulatus (Little red flying fox) [TaxID: 94117] |
Protein attributes
| Sequence length | 2244 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 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 paramyxovirus 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 – 2244 | 2244 | RNA-directed RNA polymerase L | PRO_0000236010 | |||||
Regions | |||||||||
| Domain | 715 – 899 | 185 | RdRp catalytic | ||||||
| Nucleotide binding | 1840 – 1849 | 10 | ATP Potential | ||||||
Sequences
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References
| [1] | "The exceptionally large genome of Hendra virus: support for creation of a new genus within the family Paramyxoviridae." Wang L.-F., Yu M., Hansson E., Pritchard L.I., Shiell B., Michalski W.P., Eaton B.T. J. Virol. 74:9972-9979(2000) [PubMed: 11024125] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
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| EMBL GenBank DDBJ | AF017149 Genomic RNA. Translation: AAC83194.2. |
| PIR | T08212. |
| RefSeq | NP_047113.2. NC_001906.2. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1446468. |
Family and domain databases | |
| InterPro | IPR014023. RNA-dir_pol_cat. IPR016269. RNA-dir_pol_paramyxovirus. IPR024352. RNA_pol_cap_MeTfrase. [Graphical view] |
| Pfam | PF12803. G-7-MTase. 1 hit. 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_HENDH | ||||||||
| Accession | Primary (citable) accession number: O89344 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Viral Protein Annotation Program | ||||||||
Relevant documents
| SIMILARITY comments Index of protein domains and families |

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