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Q9YUD3 (REP_BFDV) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Replication-associated protein

EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3
Alternative name(s):
ATP-dependent helicase Rep
RepP
Gene names
Name:Rep
ORF Names:ORF1
OrganismBeak and feather disease virus (BFDV) [Complete proteome]
Taxonomic identifier77856 [NCBI]
Taxonomic lineageVirusesssDNA virusesCircoviridaeCircovirus
Virus hostGracula [TaxID: 116991]
Psittaciformes [TaxID: 9223]

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Divalent metal cations, possibly magnesium or manganese By similarity.

Subunit structure

Interacts with the capsid protein; this interaction relocates Rep into the nucleus. Ref.2

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.

Sequence similarities

Belongs to the nanoviruses/circoviruses replication-associated protein family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 289289Replication-associated protein
PRO_0000319862

Regions

Nucleotide binding165 – 1728ATP By similarity
Motif4 – 1310Nuclear localization signal Potential
Motif14 – 174RCR-1 By similarity
Motif51 – 566RCR-2 By similarity
Motif60 – 8021Nuclear localization signal Potential
Motif89 – 924RCR-3 By similarity

Sites

Active site891For DNA cleavage activity By similarity
Metal binding431Divalent metal cation Potential
Metal binding511Divalent metal cation Potential
Metal binding931Divalent metal cation Potential

Sequences

Sequence LengthMass (Da)Tools
Q9YUD3 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: A52614012B831791

FASTA28933,446
        10         20         30         40         50         60 
MPSKEGSGCR RWCFTLNNPT DGEIEFVRSL GPDEFYYAIV GREKGEQGTP HLQGYFHFKN 

        70         80         90        100        110        120 
KKRLSALKKL LPRAHFERAK GSDADNEKYC SKEGDVILTL GIVARDGHRA FDGAVAAVMS 

       130        140        150        160        170        180 
GRKMKEVARE FPEVYVRHGR GLHNLSLLVG SSPRDFKTEV DVIYGPPGCG KSRWANEQPG 

       190        200        210        220        230        240 
TKYYKMRGEW WDGYDGEDVV VLDDFYGWLP YCEMLRLCDR YPHKVPVKGA FVEFTSKRII 

       250        260        270        280 
ITSNKPPETW YKEDCDPKPL FRRFTRVWWY NVDKLEQVRP DFLAHPINY 

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References

[1]"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].
[2]"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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF080560 Genomic DNA. Translation: AAC69861.1.

3D structure databases

ProteinModelPortalQ9YUD3.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D3.40.50.300. 1 hit.
InterProIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR027417. P-loop_NTPase.
IPR003365. Viral_rep_N.
[Graphical view]
PfamPF00910. RNA_helicase. 1 hit.
PF02407. Viral_Rep. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Entry information

Entry nameREP_BFDV
AccessionPrimary (citable) accession number: Q9YUD3
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families