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O39828 (MREP_FBNY2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 59. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
Alternative name(s):
ATP-dependent helicase C2
Replication-associated protein 2
Short name=Rep2
Gene names
Name:DNA-R
Synonyms:C2
OrganismFaba bean necrotic yellows virus (isolate SV292-88) (FBNYV) [Complete proteome]
Taxonomic identifier291604 [NCBI]
Taxonomic lineageVirusesssDNA virusesNanoviridaeNanovirus
Virus hostCicer arietinum (Chickpea) (Garbanzo) [TaxID: 3827]
Lens culinaris (Lentil) (Cicer lens) [TaxID: 3864]
Phaseolus vulgaris (Kidney bean) (French bean) [TaxID: 3885]
Vicia faba (Broad bean) (Faba vulgaris) [TaxID: 3906]

Protein attributes

Sequence length286 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Catalytic activity

ATP + H2O = ADP + phosphate.

Cofactor

Divalent metal cations, possibly magnesium or manganese Probable. Ref.2

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 286286Master replication protein
PRO_0000318772

Regions

Nucleotide binding186 – 1883ATP 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

Secondary structure

.................... 286
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O39828 [UniParc].

Last modified January 1, 1998. Version 1.
Checksum: FE878BF9336D23CD

FASTA28633,141
        10         20         30         40         50         60 
MARQVICWCF TLNNPLSPLS LHDSMKYLVY QTEQGEAGNI HFQGYIEMKK RTSLAGMKKL 

        70         80         90        100        110        120 
IPGAHFEKRR GTQGEARAYS MKEDTRLEGP WEYGEFVPTI EDKLREVMND MKITGKRPIE 

       130        140        150        160        170        180 
YIEECCNTYD KSASTLREFR GELKKKKAIS SWELQRKPWM GEVDALLQER DGRRIIWVYG 

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

       250        260        270        280 
LKNGIIQSGK YQSVIKYSDY VEVIVFANFT PRSGMFSEDR IVYVYA 

« Hide

References

[1]"Analysis of six DNA components of the faba bean necrotic yellows virus genome and their structural affinity to related plant virus genomes."
Katul L., Maiss E., Morozov S.Y., Vetten H.J.
Virology 233:247-259(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Solution structure of the endonuclease domain from the master replication initiator protein of the nanovirus faba bean necrotic yellows virus and comparison with the corresponding geminivirus and circovirus structures."
Vega-Rocha S., Gronenborn B., Gronenborn A.M., Campos-Olivas R.
Biochemistry 46:6201-6212(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR OF 2-95, COFACTOR, CHARACTERIZATION.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
Y11405 Genomic DNA. Translation: CAA72209.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2HWTNMR-A2-95[»]
ProteinModelPortalO39828.
SMRO39828. Positions 2-95.
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...

Other

EvolutionaryTraceO39828.

Entry information

Entry nameMREP_FBNY2
AccessionPrimary (citable) accession number: O39828
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: January 1, 1998
Last modified: April 16, 2014
This is version 59 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references