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Protein

Replication-associated protein

Gene

C1

Organism
Tomato yellow leaf curl Sardinia virus (isolate Spain-2) (TYLCSV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Essential for the replication of viral ssDNA. The closed circular ssDNA genome is first converted to a superhelical dsDNA. Rep binds a specific region at the genome origin of replication. It introduces an endonucleolytic nick within the conserved sequence 5'-TAATATTAC-3' in the intergenic region of the genome present in all geminiviruses, 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 similarity

Cofactori

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi49Divalent metal cationSequence analysis1
Metal bindingi57Divalent metal cationSequence analysis1
Metal bindingi59Divalent metal cationSequence analysis1
Active sitei103For DNA cleavage activityBy similarity1
Metal bindingi107Divalent metal cationSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi221 – 228ATPSequence analysis8

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Helicase, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication, Host-virus interaction

Keywords - Ligandi

ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Replication-associated protein (EC:2.7.7.-, EC:3.1.21.-)
Short name:
Rep
Alternative name(s):
Protein C1
Gene namesi
ORF Names:C1
OrganismiTomato yellow leaf curl Sardinia virus (isolate Spain-2) (TYLCSV)
Taxonomic identifieri221538 [NCBI]
Taxonomic lineageiVirusesssDNA virusesGeminiviridaeBegomovirus
Virus hostiCynanchum acutum [TaxID: 185024]
Solanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]
Solanum nigrum (Black nightshade) [TaxID: 4112]
Proteomesi
  • UP000008266 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003201131 – 359Replication-associated proteinAdd BLAST359

Keywords - PTMi

Covalent protein-DNA linkage

Interactioni

Subunit structurei

Homooligomer. Interacts with the replication enhancer protein (REn). Interacts with host retinoblastoma-related protein 1 (RBR1), and may thereby induce the transcription of host replicative enzymes even if the cell is not dividing anymore. Interacts with host PCNA (By similarity). Interacts with host SCE1 protein.By similarity1 Publication

Structurei

3D structure databases

ProteinModelPortaliQ67620.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni143 – 153Binding to RBR1By similarityAdd BLAST11
Regioni156 – 176OligomerizationBy similarityAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi15 – 19RCR-15
Motifi57 – 62RCR-26
Motifi103 – 106RCR-34

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 (By similarity).By similarity

Sequence similaritiesi

Belongs to the geminiviridae Rep protein family.Curated

Family and domain databases

InterProiIPR001301. Gemini_AL1_CLV.
IPR001191. Gemini_AL1_REP.
IPR022690. Gemini_AL1_REP_cat-dom.
IPR022692. Gemini_AL1_REP_central.
[Graphical view]
PfamiPF00799. Gemini_AL1. 1 hit.
PF08283. Gemini_AL1_M. 1 hit.
[Graphical view]
PRINTSiPR00227. GEMCOATAL1.
PR00228. GEMCOATCLVL1.

Sequencei

Sequence statusi: Complete.

Q67620-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAQPKRFQIN AKHYFLTFPK CSLSKEEALE QLLQLQTPTN KKYIKICREL
60 70 80 90 100
HEDGQPHLHM LIQFEGKFNC KNNRFFDLVS PTRSAHFHPN IQGAKSSSDV
110 120 130 140 150
KSYIDKDGDV LEWGTFQIDG RSARGGQQTA NDAYAKAINA GRKSEALDVI
160 170 180 190 200
KELAPRDYIL HFHNINSNLN MVFQVPPAPY VSPFLSSSFD QVPDELEHWV
210 220 230 240 250
SENVMDVAAR PWRPVSIVIE GDSRTGKTMW ARSLGPHNYL CGHLDLSQKV
260 270 280 290 300
YSNNAWYNVI DDVDPHYLKH FKEFMGSQRD WQSNTKYGKP IQIKGGIPTI
310 320 330 340 350
FLCNPGPQSS FKEYLDEEKN QTLKNWAIKN AIFVTIHQPL FTNTNQDPTP

HRQEETSEA
Length:359
Mass (Da):41,150
Last modified:November 1, 1996 - v1
Checksum:i89B54621D40171F3
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27708 Genomic DNA. Translation: AAA47955.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L27708 Genomic DNA. Translation: AAA47955.1.

3D structure databases

ProteinModelPortaliQ67620.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

InterProiIPR001301. Gemini_AL1_CLV.
IPR001191. Gemini_AL1_REP.
IPR022690. Gemini_AL1_REP_cat-dom.
IPR022692. Gemini_AL1_REP_central.
[Graphical view]
PfamiPF00799. Gemini_AL1. 1 hit.
PF08283. Gemini_AL1_M. 1 hit.
[Graphical view]
PRINTSiPR00227. GEMCOATAL1.
PR00228. GEMCOATCLVL1.
ProtoNetiSearch...

Entry informationi

Entry nameiREP_TYCS2
AccessioniPrimary (citable) accession number: Q67620
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Multifunctional enzyme

Documents

  1. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.