Reviewed,
UniProtKB/Swiss-Prot Q66862 (REP1_FBNY2)
Last modified
July 7, 2009.
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: Para-Rep C1 Short name=Rep1 EC=2.7.7.- EC=3.1.21.- EC=3.6.1.3 Alternative name(s): Replication-associated protein of non-essential DNA C1 ATP-dependent helicase C1 | ||||
| Gene names |
| ||||
| Organism | Faba bean necrotic yellows virus (isolate SV292-88) (FBNYV) | ||||
| Taxonomic identifier | 291604 [NCBI] | ||||
| Taxonomic lineage | Viruses › ssDNA viruses › Nanoviridae › Nanovirus | ||||
| Virus host | Cicer arietinum (Chickpea) (Garbanzo) [TaxID: 3827] Lens culinaris (Lentil) (Cicer lens) [TaxID: 3864] Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885] Vicia faba (Broad bean) [TaxID: 3906] |
Protein attributes
| Sequence length | 278 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Initiates and terminates the replication only of its own subviral DNA molecule. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the intergenic region of the genome, thereby initiating the rolling circle replication (RCR). Following cleavage, binds covalently to the 5'-phosphate of DNA as a tyrosyl ester. The cleavage gives rise to a free 3'-OH that serves as a primer for the cellular DNA polymerase. The polymerase synthesizes the (+) strand DNA by rolling circle mechanism. After one round of replication, a Rep-catalyzed nucleotidyl transfer reaction releases a circular single-stranded virus genome, thereby terminating the replication. Displays origin-specific DNA cleavage, nucleotidyl transferase, ATPase and helicase activities. Ref.2 |
| Catalytic activity | ATP + H2O = ADP + phosphate. |
| Cofactor | Divalent metal cations, possibly magnesium or manganese By similarity. |
| Subunit structure | Homooligomer Potential. Rep binds to repeated DNA motifs (iterons) By similarity. |
| Subcellular location | Host nucleus Potential. |
| Domain | There are 3 rolling circle replication (RCR) motifs. RCR-2 is probably involved in metal coordination. RCR-3 is required for phosphodiester bond cleavage for initiation of RCR. |
| Miscellaneous | The genome of nanoviruses is composed of six to eight segments. In addition, some isolates contain subviral DNAs. |
| Sequence similarities | Belongs to the nanoviridea/circoviridae replication-associated protein family. |
| Caution | This protein is encoded by a subviral DNA that is not present in all isolates of the virus. |
Ontologies
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 278 | 278 | Para-Rep C1 | PRO_0000222439 | |||||
Regions | |||||||||
| Nucleotide binding | 176 – 178 | 3 | ATP Probable | ||||||
| Motif | 8 – 11 | 4 | RCR-1 By similarity | ||||||
| Motif | 39 – 44 | 6 | RCR-2 By similarity | ||||||
| Motif | 48 – 69 | 22 | Nuclear localization signal Potential | ||||||
| Motif | 78 – 81 | 4 | RCR-3 By similarity | ||||||
| Motif | 95 – 101 | 7 | Nuclear localization signal Potential | ||||||
Sites | |||||||||
| Active site | 78 | 1 | For DNA cleavage activity | ||||||
| Metal binding | 33 | 1 | Divalent metal cation Potential | ||||||
| Metal binding | 39 | 1 | Divalent metal cation Potential | ||||||
| Metal binding | 83 | 1 | Divalent metal cation Potential | ||||||
Experimental info | |||||||||
| Mutagenesis | 78 | 1 | Y → F: Complete loss of DNA cleavage and nucleotidyl transfer activity. Ref.2 | ||||||
| Mutagenesis | 177 | 1 | K → A: Complete loss of ATPase activity. Ref.2 | ||||||
Sequences
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References
| [1] | "Sequence analysis of a faba bean necrotic yellows virus DNA component containing a putative replicase gene." Katul L., Maiss E., Vetten V.J. J. Gen. Virol. 76:475-479(1995) [PubMed: 7844570] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. |
| [2] | "A single Rep protein initiates replication of multiple genome components of faba bean necrotic yellows virus, a single-stranded DNA virus of plants." Timchenko T., de Kouchkovsky F., Katul L., David C., Vetten H.J., Gronenborn B. J. Virol. 73:10173-10182(1999) [PubMed: 10559333] [Abstract] Cited for: FUNCTION, MUTAGENESIS OF TYR-78 AND LYS-177. |
| [3] | "Nanoviruses: genome organisation and protein function." Gronenborn B. Vet. Microbiol. 98:103-109(2004) [PubMed: 14741122] [Abstract] Cited for: REVIEW. |
Cross-references
Sequence databases | |
|---|---|
| X80879 Genomic DNA. Translation: CAA56847.1. | |
3D structure databases | |
| ModBase | Search... |
Family and domain databases | |
| InterPro | IPR000605. Helicase_SF3_ssDNA/RNA_vir. IPR013628. Viral_Rep_C. IPR003365. Viral_rep_N. [Graphical view] |
| Pfam | PF00910. RNA_helicase. 1 hit. PF02407. Viral_Rep. 1 hit. PF08419. Viral_Rep_C. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | REP1_FBNY2 | ||||||||
| Accession | Primary (citable) accession number: Q66862 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | Virus (Virus annotation project) | ||||||||
