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Q66862 (REP1_FBNY2) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 63. 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 C1

Short name=Rep1
EC=2.7.7.-
EC=3.1.21.-
EC=3.6.1.3
Alternative name(s):
ATP-dependent helicase C1
Replication-associated protein of non-essential DNA C1
Gene names
Name:C1
ORF Names:ORF1
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 length278 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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. Ref.2

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.

Ontologies

Keywords
   Biological processDNA replication
   Cellular componentHost nucleus
   LigandATP-binding
DNA-binding
Metal-binding
Nucleotide-binding
   Molecular functionEndonuclease
Helicase
Hydrolase
Nuclease
Nucleotidyltransferase
Transferase
   PTMCovalent protein-DNA linkage
   Technical termComplete proteome
Multifunctional enzyme
Gene Ontology (GO)
   Biological_processATP catabolic process

Inferred from direct assay Ref.2. Source: GOC

DNA replication

Inferred from electronic annotation. Source: UniProtKB-KW

protein-DNA covalent cross-linking

Inferred from electronic annotation. Source: InterPro

viral DNA cleavage involved in viral genome maturation

Inferred from direct assay Ref.2. Source: CACAO

   Cellular_componenthost cell nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionATP binding

Inferred from electronic annotation. Source: UniProtKB-KW

ATPase activity

Inferred from direct assay Ref.2. Source: CACAO

ATPase activity, uncoupled

Inferred from electronic annotation. Source: InterPro

DNA binding

Inferred from electronic annotation. Source: UniProtKB-KW

RNA binding

Inferred from electronic annotation. Source: InterPro

RNA helicase activity

Inferred from electronic annotation. Source: InterPro

endodeoxyribonuclease activity, producing 5'-phosphomonoesters

Inferred from electronic annotation. Source: InterPro

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

nucleotidyltransferase activity

Inferred from direct assay Ref.2. Source: CACAO

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 278278Para-Rep C1
PRO_0000222439

Regions

Nucleotide binding176 – 1783ATP Probable
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
Metal binding331Divalent metal cation Potential
Metal binding391Divalent metal cation Potential
Metal binding831Divalent metal cation Potential

Experimental info

Mutagenesis781Y → F: Complete loss of DNA cleavage and nucleotidyl transfer activity. Ref.2
Mutagenesis1771K → A: Complete loss of ATPase activity. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q66862 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 4D9F4451F4EA2DED

FASTA27832,382
        10         20         30         40         50         60 
MACSNWVFTR NFQGALPLLS FDERVQYAVW QHERGTHDHI QGVIQLKKKA RFSTVKEIIG 

        70         80         90        100        110        120 
GNPHVEKMKG TIEEASAYVQ KEETRVAGPW SYGDLLKRGS HRRKTMERYL EDPEEMQLKD 

       130        140        150        160        170        180 
PDTALRCNAK RLKEDFMKEK TKLQLRPWQK ELHDLILTEP DDRTIIWVYG PDGGEGKSMF 

       190        200        210        220        230        240 
AKELIKYGWF YTAGGKTQDI LYMYAQDPER NIAFDVPRCS SEMMNYQAME MMKNRCFAST 

       250        260        270 
KYRSVDLCCN KNVHLVVFAN VAYDPTKISE DRIVIINC 

« Hide

References

[1]"Sequence analysis of a faba bean necrotic yellows virus DNA component containing a putative replicase gene."
Katul L., Maiss E., Vetten V.J.
J. Gen. Virol. 76:475-479(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"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: FUNCTION, MUTAGENESIS OF TYR-78 AND LYS-177.
[3]"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
X80879 Genomic DNA. Translation: CAA56847.1.

3D structure databases

ProteinModelPortalQ66862.
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 nameREP1_FBNY2
AccessionPrimary (citable) accession number: Q66862
Entry history
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: November 1, 1996
Last modified: April 16, 2014
This is version 63 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