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Protein

Replication-associated protein

Gene

AC1

Organism
Cabbage leaf curl virus (isolate Jamaica) (CaLCuV)
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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi51 – 511Divalent metal cationSequence analysis
Metal bindingi59 – 591Divalent metal cationSequence analysis
Metal bindingi61 – 611Divalent metal cationSequence analysis
Active sitei105 – 1051For DNA cleavage activityBy similarity
Metal bindingi109 – 1091Divalent metal cationSequence analysis

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi220 – 2278ATPSequence analysis

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):
40.2 kDa protein
Protein AC1
Protein AL1
Gene namesi
ORF Names:AC1, AL1
OrganismiCabbage leaf curl virus (isolate Jamaica) (CaLCuV)
Taxonomic identifieri345184 [NCBI]
Taxonomic lineageiVirusesssDNA virusesGeminiviridaeBegomovirus
Virus hostiBrassica oleracea (Wild cabbage) [TaxID: 3712]
Proteomesi
  • UP000007622 Componenti: Genome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Host nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 349349Replication-associated proteinPRO_0000320110Add
BLAST

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

ProteinModelPortaliQ96704.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni141 – 15111Binding to RBR1By similarityAdd
BLAST
Regioni154 – 17421OligomerizationBy similarityAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi16 – 205RCR-1
Motifi59 – 646RCR-2
Motifi105 – 1084RCR-3

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.

Q96704-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPRNPKSFRL AARNIFLTYP QCDIPKDEAL QMLQTLSWSV VKPTYIRVAR
60 70 80 90 100
EEHSDGFPHL HCLIQLSGKS NIKDARFFDI THPRRSANFH PNIQAAKDTN
110 120 130 140 150
AVKNYITKDG DYCESGQYKV SGGTKANKDD VYHNAVNAGC VEEALAIIRA
160 170 180 190 200
GDPKTFIVSY HNVRANIERL FTKAPEPWAP PFQLSSFTNV PDEMSSWADD
210 220 230 240 250
YFGRSAAARA ERPISIIVEG DSRTGKTMWA RALGPHNYLS GHLDFNSKVF
260 270 280 290 300
SNNAEYNVID DIAPHYLKLK HWKELIGAQR DWQSNCKYGK PVQIKGGIPS
310 320 330 340
IVLCNPGEGS SYISFLNKEE NASLRAWTTK NAKFITLEAP LYQSTAQDC
Length:349
Mass (Da):39,231
Last modified:October 1, 2001 - v2
Checksum:i1DF5B398B2FA7880
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65529 Genomic DNA. Translation: AAB17963.2.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U65529 Genomic DNA. Translation: AAB17963.2.

3D structure databases

ProteinModelPortaliQ96704.
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...

Publicationsi

  1. "Cloning, identification and partial sequencing of a new geminivirus infecting Brassicaceae."
    Abouzid A.M., Hiebert E., Strandberg J.O.
    Phytopathology 82:1070-1070(1992)
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Abouzid A.M., Hiebert E., Strandberg J.O.
    Submitted (AUG-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.

Entry informationi

Entry nameiREP_CALCV
AccessioniPrimary (citable) accession number: Q96704
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 1, 2001
Last modified: November 11, 2015
This is version 65 of the entry and version 2 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.