P52639 (L_BDVV) Reviewed, UniProtKB/Swiss-Prot
Last modified
May 1, 2013.
Version 77.
History...
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
Protein attributes
| Sequence length | 1711 AA. |
| Sequence status | Complete. |
| Protein existence | Evidence at protein level |
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 three subgenomic RNAs, assuring their capping and polyadenylation by a stuttering mechanism. In replicase 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. Ref.3 |
| Subcellular location | Virion Potential. Host nucleus Ref.4. |
| Sequence similarities | Contains 1 RdRp catalytic domain. |
| Sequence caution | The sequence AAA20228.1 differs from that shown. Reason: Erroneous initiation. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Viral RNA replication mRNA capping mRNA processing |
| Cellular component | Host nucleus Virion |
| Coding sequence diversity | Alternative splicing |
| Ligand | ATP-binding Nucleotide-binding S-adenosyl-L-methionine |
| Molecular function | Methyltransferase Nucleotidyltransferase RNA-directed RNA polymerase Transferase |
| Technical term | Complete proteome Multifunctional enzyme Reference proteome |
| Gene Ontology (GO) | |
| Biological_process | RNA (guanine-N7)-methylation Inferred from electronic annotation. Source: GOC |
| Cellular_component | host cell cytoplasm Inferred from electronic annotation. Source: InterPro host cell nucleusInferred from electronic annotation. Source: UniProtKB-SubCell virionInferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular_function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW RNA-directed RNA polymerase activityInferred from electronic annotation. Source: UniProtKB-KW mRNA (guanine-N7-)-methyltransferase activityInferred from electronic annotation. Source: EC |
| Complete GO annotation... | |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform Large structural protein (identifier: P52639-1) This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry. | ||||||
| Isoform Matrix protein (identifier: P0C795-1) The sequence of this isoform can be found in the external entry P0C795. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. | ||||||
| Isoform Envelope glycoprotein p57 precursor (identifier: P52638-1) The sequence of this isoform can be found in the external entry P52638. Isoforms of the same protein are often annotated in two different entries if their sequences differ significantly. |
Sequence annotation (Features)
Sequences
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References
| [1] | "Genomic organization of Borna disease virus." Briese T., Schneemann A., Lewis A.J., Park Y.-S., Kim S., Ludwig H., Lipkin W.I. Proc. Natl. Acad. Sci. U.S.A. 91:4362-4366(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. |
| [2] | "Conservation of coding potential and terminal sequences in four different isolates of Borna disease virus." Pleschka S., Staeheli P., Kolodziejek J., Richt J.A., Nowotny N., Schwemmle M. J. Gen. Virol. 82:2681-2690(2001) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC RNA]. Strain: V/FR. |
| [3] | "Expression and characterization of the Borna disease virus polymerase." Walker M.P., Jordan I., Briese T., Fischer N., Lipkin W.I. J. Virol. 74:4425-4428(2000) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH P PROTEIN. |
| [4] | "Characterization of the nuclear localization signal of the borna disease virus polymerase." Walker M.P., Lipkin W.I. J. Virol. 76:8460-8467(2002) [PubMed] [Europe PMC] [Abstract] Cited for: SUBCELLULAR LOCATION. |
| [5] | "Borna disease virus and infection in humans." Ikuta K., Ibrahim M.S., Kobayashi T., Tomonaga K. Front. Biosci. 7:470-495(2002) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | U04608 Genomic RNA. Translation: AAA20228.1. Different initiation. AJ311521 Genomic RNA. Translation: CAC70639.1. |
| RefSeq | NP_042024.2. NC_001607.1. |
3D structure databases | |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1494405. |
Family and domain databases | |
| InterPro | IPR026890. Mononeg_mRNAcap. IPR014023. Mononeg_RNA_pol_cat. IPR025786. RNA-direct_RNA_pol_L. [Graphical view] |
| Pfam | PF14318. Mononeg_mRNAcap. 1 hit. PF00946. Mononeg_RNA_pol. 1 hit. [Graphical view] |
| PROSITE | PS50526. RDRP_SSRNA_NEG_NONSEG. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | L_BDVV | ||||||||
| Accession | Primary (citable) accession number: P52639 Secondary accession number(s): Q912Z6 | ||||||||
| 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 |

Clusters with
