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Protein

Replication-associated protein

Gene

C1

Organism
Tomato pseudo-curly top virus (TPCTV)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein inferred from homologyi

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 bindingi50Divalent metal cationSequence analysis1
Metal bindingi58Divalent metal cationSequence analysis1
Metal bindingi60Divalent metal cationSequence analysis1
Active sitei104For DNA cleavage activityBy similarity1
Metal bindingi108Divalent metal cationSequence analysis1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi223 – 230ATPSequence 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 pseudo-curly top virus (TPCTV)
Taxonomic identifieri49267 [NCBI]
Taxonomic lineageiVirusesssDNA virusesGeminiviridaeTopocuvirus
Virus hostiSolanum lycopersicum (Tomato) (Lycopersicon esculentum) [TaxID: 4081]
Solanum nigrum (Black nightshade) [TaxID: 4112]
Proteomesi
  • UP000007068 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_00003237041 – 349Replication-associated proteinAdd BLAST349

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. Interacts with host SCE1 protein (By similarity).By similarity

Structurei

3D structure databases

ProteinModelPortaliQ88888.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni144 – 154Binding to RBR1By similarityAdd BLAST11
Regioni157 – 177OligomerizationBy similarityAdd BLAST21

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi16 – 20RCR-1By similarity5
Motifi58 – 63RCR-2By similarity6
Motifi104 – 107RCR-3By similarity4

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.

Q88888-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSNPKRFQI AAKNYFLTYP NCSLSKEEAL DQLQRLQTPT NKKYIKVARE
60 70 80 90 100
LHENGEPHLH VLIQFEGKFN CKNQRFFDLV SPTRSTHFHP NIQGAKSSSD
110 120 130 140 150
VNSYVDKDGD TIEWGEFQID ARSARGGQQT ANDECAEALN RSSKEEALQI
160 170 180 190 200
IKEKLPKDFL FCYHNLVSNL DRIFTPAPTP FVPPFQLSSF TNVPEDMQEW
210 220 230 240 250
ADDYFGVSAA ARPMRYKSII IEGESRTGKT MWARSLGPHN YLSGHLDFNS
260 270 280 290 300
RVYSNSALYN VIDDVTPHYL KLKHWKELIG AQRDWQSNCK YGKPVQIKGG
310 320 330 340
IPSIVLCNPG GDTSFQDFLD KEENEALKDW TLYNAVFIKL TEPLYDGTV
Length:349
Mass (Da):39,843
Last modified:November 1, 1996 - v1
Checksum:i79EB0D0870C70FE1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84735 Genomic DNA. Translation: CAA59223.1.
RefSeqiNP_620735.1. NC_003825.1.

Genome annotation databases

GeneIDi944407.
KEGGivg:944407.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X84735 Genomic DNA. Translation: CAA59223.1.
RefSeqiNP_620735.1. NC_003825.1.

3D structure databases

ProteinModelPortaliQ88888.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi944407.
KEGGivg:944407.

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_TPCTV
AccessioniPrimary (citable) accession number: Q88888
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 18, 2008
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 66 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, Reference proteome

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.