Q9YUD3 (REP_BFDV) Reviewed, UniProtKB/Swiss-Prot
Last modified April 3, 2013. Version 52. History...
Names and origin
|Protein names||Recommended name:|
ATP-dependent helicase Rep
|Organism||Beak and feather disease virus (BFDV) [Complete proteome]|
|Taxonomic identifier||77856 [NCBI]|
|Taxonomic lineage||Viruses › ssDNA viruses › Circoviridae › Circovirus|
|Virus host||Gracula [TaxID: 116991]|
Psittaciformes [TaxID: 9223]
|Sequence length||289 AA.|
|Protein existence||Evidence at protein level|
General annotation (Comments)
Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep and/or Rep' binds a specific hairpin at the genome origin of replication. Introduces an endonucleolytic nick within the conserved sequence 5'-AGTATTAC-3' in 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. ATPase activity is probably carried by the isoform Rep By similarity.
ATP + H2O = ADP + phosphate.
Divalent metal cations, possibly magnesium or manganese By similarity.
Interacts with the capsid protein; this interaction relocates Rep into the nucleus. Ref.2
Host nucleus Potential.
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.
Belongs to the nanoviruses/circoviruses replication-associated protein family.
Sequence annotation (Features)
|Feature key||Position(s)||Length||Description||Graphical view||Feature identifier|
|Chain||1 – 289||289||Replication-associated protein||PRO_0000319862|
|Nucleotide binding||165 – 172||8||ATP By similarity|
|Motif||4 – 13||10||Nuclear localization signal Potential|
|Motif||14 – 17||4||RCR-1 By similarity|
|Motif||51 – 56||6||RCR-2 By similarity|
|Motif||60 – 80||21||Nuclear localization signal Potential|
|Motif||89 – 92||4||RCR-3 By similarity|
|Active site||89||1||For DNA cleavage activity By similarity|
|Metal binding||43||1||Divalent metal cation Potential|
|Metal binding||51||1||Divalent metal cation Potential|
|Metal binding||93||1||Divalent metal cation Potential|
|||"Psittacine beak and feather disease virus nucleotide sequence analysis and its relationship to porcine circovirus, plant circoviruses, and chicken anaemia virus."|
Bassami M.R., Berryman D., Wilcox G.E., Raidal S.R.
Virology 249:453-459(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
|||"The capsid protein of beak and feather disease virus binds to the viral DNA and is responsible for transporting the replication-associated protein into the nucleus."|
Heath L., Williamson A.L., Rybicki E.P.
J. Virol. 80:7219-7225(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH CAPSID PROTEIN.
|AF080560 Genomic DNA. Translation: AAC69861.1.|
3D structure databases
Protocols and materials databases
Family and domain databases
|InterPro||IPR000605. Helicase_SF3_ssDNA/RNA_vir. |
|Pfam||PF00910. RNA_helicase. 1 hit. |
PF02407. Viral_Rep. 1 hit.
|Accession||Primary (citable) accession number: Q9YUD3|
|Entry status||Reviewed (UniProtKB/Swiss-Prot)|
|Annotation program||Viral Protein Annotation Program|
Index of protein domains and families