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P0CK60 (REP9_FBNY1) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 8. 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 C9

Short name=Rep9
EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3
Alternative name(s):
ATP-dependent helicase C9
Replication-associated protein of non-essential DNA C9
Gene names
Name:C9
OrganismFaba bean necrotic yellows virus (isolate Egyptian EV1-93) (FBNYV) [Complete proteome]
Taxonomic identifier291603 [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 length281 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. Ref.1

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 – 281281Para-Rep C9
PRO_0000222442

Regions

Nucleotide binding178 – 1803ATP By similarity
Motif8 – 114RCR-1 By similarity
Motif39 – 446RCR-2 By similarity
Motif48 – 6922Nuclear localization signal Potential
Motif78 – 814RCR-3 By similarity
Motif95 – 1017Nuclear localization signal Potential

Sites

Active site781For DNA cleavage activity By similarity
Metal binding331Divalent metal cation Potential
Metal binding391Divalent metal cation Potential
Metal binding831Divalent metal cation Potential

Sequences

Sequence LengthMass (Da)Tools
P0CK60 [UniParc].

Last modified March 21, 2012. Version 1.
Checksum: F50CF0C3CFC6E3B2

FASTA28132,568
        10         20         30         40         50         60 
MSAVNWVFTL NFAGEVPVLS FDERVQYAVW QHERVNHDHI QGVIQLKKKA KMNTVKNIIG 

        70         80         90        100        110        120 
GNPHLEKMKG SIEEASAYAQ KEESRVAGPW SYGELLKKGS HKRKIMELIK DPENELEEPQ 

       130        140        150        160        170        180 
KYRRAMAWSA MDESRKLAEE GGFPYTLYSW QETVLGLLEE EPNDRIIIWV YGPNGNEGKS 

       190        200        210        220        230        240 
QFGKFLGLKK DYLYLPGGKT QDMTYMLMKN PKANVVMDIP RCNSEYLNYQ FMELIKNRTI 

       250        260        270        280 
FSYKYEPVGC IINNKIHVIV LANVLPDYEK ISQDRIKIIY C 

« Hide

References

[1]"A single Rep protein initiates replication of multiple genome components of faba bean necrotic yellows virus, a single-stranded DNA virus of plants."
Timchenko T., de Kouchkovsky F., Katul L., David C., Vetten H.J., Gronenborn B.
J. Virol. 73:10173-10182(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION.
[2]"Nanoviruses: genome organisation and protein function."
Gronenborn B.
Vet. Microbiol. 98:103-109(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: REVIEW.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ132187 Genomic DNA. Translation: CAB44027.1.
RefSeqNP_619574.1. NC_003567.1.

3D structure databases

ProteinModelPortalP0CK60.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID993380.

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 nameREP9_FBNY1
AccessionPrimary (citable) accession number: P0CK60
Secondary accession number(s): O91252, Q9WIK2
Entry history
Integrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: March 21, 2012
Last modified: April 16, 2014
This is version 8 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