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Q9IR51 (MREP_MDV1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 41. 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:
Master replication protein

Short name=M-Rep
EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3
Gene names
Name:DNA-R
Synonyms:C11
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 length286 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Essential for the replication of all genomic viral ssDNA (trans-replication). 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 conserved sequence 5'-A[GT]TATTAC-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 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 By similarity.

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Master replication protein
PRO_0000378520

Regions

Nucleotide binding180 – 1889ATP By similarity
Motif10 – 134RCR-1 By similarity
Motif41 – 466RCR-2 By similarity
Motif50 – 7021Nuclear localization signal Potential
Motif79 – 824RCR-3 By similarity
Motif96 – 1027Nuclear localization signal Potential
Compositional bias144 – 1474Poly-Lys

Sites

Active site791For DNA cleavage activity By similarity
Metal binding331Divalent metal cation Potential
Metal binding411Divalent metal cation Potential
Metal binding841Divalent metal cation Potential

Sequences

Sequence LengthMass (Da)Tools
Q9IR51 [UniParc].

Last modified October 1, 2000. Version 1.
Checksum: FC8854716C7F6C6B

FASTA28633,334
        10         20         30         40         50         60 
MARQVICWCF TLNNPLSPLS LHELMKYLVY QREQGEAGNI HFQGYIEMKK RTSLAGMKKL 

        70         80         90        100        110        120 
IPGAHFEKRR GTQGEARAYA MKEDTRLEGP WEYGEFIPTI EDKLREVMND MKITGKRPIE 

       130        140        150        160        170        180 
YIEECCNTYD KSASTLREFR GELKKKKAII SWELQRKPWM DEVDTLLQER DGRRIIWVYG 

       190        200        210        220        230        240 
PQGGEGKTSY AKHLVKTRDA FYSTGGKTAD IAFAWDHQEL VLFDFPRSFE EYVNYGVIEQ 

       250        260        270        280 
LKNGIIQSGK YQSVIKYSDY VEVIVFANFT PRSGMFSDDR IVYVYA 

« 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
AB027511 Genomic DNA. Translation: BAA97561.1.
RefSeqNP_619769.1. NC_003648.1.

3D structure databases

ProteinModelPortalQ9IR51.
SMRQ9IR51. Positions 2-95.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID995288.

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 nameMREP_MDV1
AccessionPrimary (citable) accession number: Q9IR51
Entry history
Integrated into UniProtKB/Swiss-Prot: July 7, 2009
Last sequence update: October 1, 2000
Last modified: April 16, 2014
This is version 41 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