Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9Z0D4 (REP2_MDV1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 48. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Para-Rep C2

Short name=Rep2
EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3
Alternative name(s):
Replication-associated protein of non-essential DNA C2
Gene names
Name:C2
OrganismMilk vetch dwarf virus (isolate N) (MDV) [Complete proteome]
Taxonomic identifier291605 [NCBI]
Taxonomic lineageVirusesssDNA virusesNanoviridaeNanovirus
Virus hostAstragalus sinicus (Chinese milk vetch) [TaxID: 47065]
Glycine max (Soybean) (Glycine hispida) [TaxID: 3847]
Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885]
Pisum sativum (Garden pea) [TaxID: 3888]
Vicia faba (Broad bean) (Faba vulgaris) [TaxID: 3906]

Protein attributes

Sequence length282 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 282282Para-Rep C2
PRO_0000378522

Regions

Nucleotide binding174 – 1829ATP By similarity
Motif8 – 114RCR-1 By similarity
Motif47 – 526RCR-2 By similarity
Motif56 – 7722Nuclear localization signal Potential
Motif86 – 894RCR-3 By similarity
Motif99 – 1057Nuclear localization signal Potential

Sites

Active site861For DNA cleavage activity By similarity
Metal binding381Divalent metal cation Potential
Metal binding471Divalent metal cation Potential

Sequences

Sequence LengthMass (Da)Tools
Q9Z0D4 [UniParc].

Last modified May 1, 1999. Version 1.
Checksum: 6E8CE00C0BB7462E

FASTA28232,682
        10         20         30         40         50         60 
MASKRWCFTL NYKTALERET FISLFSRDEL NYFVCGDEIA PTTGQKHLQG YVSMKKLIRL 

        70         80         90        100        110        120 
GGLKKKFGSI AHWEIAKGDD FQNRDYCTKE TLIAEIGAPV KKGSNRRKIM EIYEEDPEEM 

       130        140        150        160        170        180 
KLRDPDTALR CKAKKLREEY CSEVSVFSLR PWQIELHRAL MEVPDDRTII WAYGPDGGEG 

       190        200        210        220        230        240 
KSTFAKELIK YGWFYTAGGK TQDILYMYAQ DPERNIAFDV PRCSSEMMNY QAMEMMKNRV 

       250        260        270        280 
FASTKYRPVD LCIRKKVHLI VFANVAPDPT KLSEDRIVII NC 

« Hide

References

[1]"Sequences of ten circular ssDNA components associated with the milk vetch dwarf virus genome."
Sano Y., Wada M., Hashimoto Y., Matsumoto T., Kojima M.
J. Gen. Virol. 79:3111-3118(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB000921 Genomic DNA. Translation: BAA33981.1.

3D structure databases

ProteinModelPortalQ9Z0D4.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000605. Helicase_SF3_ssDNA/RNA_vir.
IPR003365. Viral_rep_N.
[Graphical view]
PfamPF00910. RNA_helicase. 1 hit.
PF02407. Viral_Rep. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameREP2_MDV1
AccessionPrimary (citable) accession number: Q9Z0D4
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: May 1, 1999
Last modified: April 16, 2014
This is version 48 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