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Protein

Para-Rep C9

Gene

C9

Organism
Faba bean necrotic yellows virus (isolate Egyptian EV1-93) (FBNYV)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

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).By similarity1 Publication

Miscellaneous

The genome of nanoviruses is composed of six to eight segments. In addition, some isolates contain subviral DNAs.

Caution

This protein is encoded by a subviral DNA that is not present in all isolates of the virus.Curated

Catalytic activityi

ATP + H2O = ADP + phosphate.

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Divalent metal cations, possibly Mg2+ or Mn2+.By similarity

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi33Divalent metal cationSequence analysis1
Metal bindingi39Divalent metal cationSequence analysis1
Active sitei78For DNA cleavage activityBy similarity1
Metal bindingi83Divalent metal cationSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi178 – 180ATPBy similarity3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-binding, Endonuclease, Helicase, Hydrolase, Multifunctional enzyme, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA replication
LigandATP-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Para-Rep C9 (EC:2.7.7.-, EC:3.1.21.-, EC:3.6.1.3)
Short name:
Rep9
Alternative name(s):
ATP-dependent helicase C9
Replication-associated protein of non-essential DNA C9
Gene namesi
Name:C9
OrganismiFaba bean necrotic yellows virus (isolate Egyptian EV1-93) (FBNYV)
Taxonomic identifieri291603 [NCBI]
Taxonomic lineageiVirusesssDNA virusesNanoviridaeNanovirus
Virus hostiCicer 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]
Proteomesi
  • UP000008665 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00002224421 – 281Para-Rep C9Add BLAST281

Keywords - PTMi

Covalent protein-DNA linkage

Interactioni

Subunit structurei

Homooligomer (Potential). Rep binds to repeated DNA motifs (iterons) (By similarity).By similarityCurated

Structurei

3D structure databases

ProteinModelPortaliP0CK60
SMRiP0CK60
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi8 – 11RCR-1By similarity4
Motifi39 – 44RCR-2By similarity6
Motifi48 – 69Nuclear localization signalSequence analysisAdd BLAST22
Motifi78 – 81RCR-3By similarity4
Motifi95 – 101Nuclear localization signalSequence analysis7

Domaini

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.

Sequence similaritiesi

Phylogenomic databases

OrthoDBiVOG090002CZ

Family and domain databases

InterProiView protein in InterPro
IPR000605 Helicase_SF3_ssDNA/RNA_vir
IPR003365 Viral_rep_N
PfamiView protein in Pfam
PF00910 RNA_helicase, 1 hit
PF02407 Viral_Rep, 1 hit

Sequencei

Sequence statusi: Complete.

P0CK60-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSAVNWVFTL NFAGEVPVLS FDERVQYAVW QHERVNHDHI QGVIQLKKKA
60 70 80 90 100
KMNTVKNIIG GNPHLEKMKG SIEEASAYAQ KEESRVAGPW SYGELLKKGS
110 120 130 140 150
HKRKIMELIK DPENELEEPQ KYRRAMAWSA MDESRKLAEE GGFPYTLYSW
160 170 180 190 200
QETVLGLLEE EPNDRIIIWV YGPNGNEGKS QFGKFLGLKK DYLYLPGGKT
210 220 230 240 250
QDMTYMLMKN PKANVVMDIP RCNSEYLNYQ FMELIKNRTI FSYKYEPVGC
260 270 280
IINNKIHVIV LANVLPDYEK ISQDRIKIIY C
Length:281
Mass (Da):32,568
Last modified:March 21, 2012 - v1
Checksum:iF50CF0C3CFC6E3B2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ132187 Genomic DNA Translation: CAB44027.1

Similar proteinsi

Entry informationi

Entry nameiREP9_FBNY1
AccessioniPrimary (citable) accession number: P0CK60
Secondary accession number(s): O91252, Q9WIK2
Entry historyiIntegrated into UniProtKB/Swiss-Prot: March 21, 2012
Last sequence update: March 21, 2012
Last modified: June 20, 2018
This is version 28 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

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