Reviewed,
UniProtKB/Swiss-Prot B1NKR5 (VP3_ROTAD)
Last modified
June 16, 2009.
Version 8.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Protein VP3 Including the following 2 domains: 1- Recommended name: mRNA guanylyltransferase EC=2.7.7.50 2- Recommended name: mRNA (guanine-N(7)-)-methyltransferase EC=2.1.1.56 |
| Organism | Rotavirus A (strain Human/United States/D/1974 G1-P1A[8]-I1-R1-C1-M1-A1-N1-T1-E1-H1) (RV-A) [Complete proteome] |
| Taxonomic identifier | 578831 [NCBI] |
| Taxonomic lineage | Viruses › dsRNA viruses › Reoviridae › Rotavirus › Rotavirus A |
| Virus host | Homo sapiens (Human) [TaxID: 9606] |
Protein attributes
| Sequence length | 835 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Multifunctional enzyme involved in mRNA capping. Catalyzes the formation of the 5' cap structure on the viral plus-strand transcripts. Specifically binds to GTP and displays guanylyltransferase and methyltransferase activities. Has affinity for ssRNA but not for dsRNA. Capping activity is non-specific and caps RNAs that initiate with either a G or an A residue. Together with VP1 polymerase, forms an enzyme complex positioned near the channels situated at each of the five-fold vertices of the core. Following infection, the outermost layer of the virus is lost, leaving a double-layered particle (DLP) made up of the core and VP6 shell. VP1 then catalyzes the transcription of fully conservative plus-strand genomic RNAs that are capped by VP3 and extruded through the DLP's channels into the cytoplasm where they function as mRNAs for translation of viral proteins. DLPs probably have an RNA triphosphatase activity as well, whereas open cores don't By similarity. |
| Catalytic activity | GTP + (5')pp-Pur-mRNA = diphosphate + G(5')ppp-Pur-mRNA. S-adenosyl-L-methionine + G(5')pppR-RNA = S-adenosyl-L-homocysteine + m7G(5')pppR-RNA. |
| Subunit structure | Interacts with VP1 Potential. Interacts with VP2 By similarity. |
| Subcellular location | Virion Potential. Note: Attached inside the inner capsid as a minor component. Also found in spherical cytoplasmic structures, called virus factories, that appear early after infection and are the site of viral replication and packaging Potential. |
| Sequence similarities | Belongs to the rotavirus VP3 family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | mRNA capping mRNA processing |
| Cellular component | Core protein Virion |
| Ligand | GTP-binding Nucleotide-binding RNA-binding S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Nucleotidyltransferase Transferase |
| Technical term | Complete proteome Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | mRNA capping Inferred from electronic annotation. Source: UniProtKB-KW viral reproductionInferred from electronic annotation. Source: InterPro |
| Cellular component | viral nucleocapsid Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | GTP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA bindingInferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activityInferred from electronic annotation. Source: EC mRNA guanylyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Full genome-based classification of rotaviruses reveals a common origin between human Wa-Like and porcine rotavirus strains and human DS-1-like and bovine rotavirus strains." Matthijnssens J., Ciarlet M., Heiman E.M., Arijs I., Delbeke T., McDonald S.M., Palombo E.A., Iturriza-Gomara M., Maes P., Patton J.T., Rahman M., Van Ranst M. J. Virol. 82:3204-3219(2008) [PubMed: 18216098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
Cross-references
Sequence databases | |
|---|---|
| EF583023 Genomic RNA. Translation: ABU87832.1. | |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR011181. Pesterase_Rotav. IPR009697. Rotavirus_VP3. [Graphical view] |
| Pfam | PF06929. Rotavirus_VP3. 1 hit. [Graphical view] |
| PIRSF | PIRSF004015. LigT_rotavirus. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | VP3_ROTAD | ||||||||
| Accession | Primary (citable) accession number: B1NKR5 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||

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