A0A7D6BY77 · A0A7D6BY77_9GEMI
- ProteinReplication-associated protein
- GeneC1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids373 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
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.
Cofactor
Protein has several cofactor binding sites:
Mn2+ (UniProtKB | Rhea| CHEBI:29035 )
Note: Divalent metal cations, possibly Mg2+ or Mn2+.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 50 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 58 | a divalent metal cation (UniProtKB | ChEBI) | |||
Binding site | 60 | a divalent metal cation (UniProtKB | ChEBI) | |||
Active site | 104 | For DNA cleavage activity | |||
Binding site | 108 | a divalent metal cation (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleus | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | endodeoxyribonuclease activity, producing 5'-phosphomonoesters | |
Molecular Function | helicase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotidyltransferase activity | |
Molecular Function | structural molecule activity | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReplication-associated protein
- EC number
- Short namesRep
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Monodnaviria > Shotokuvirae > Cressdnaviricota > Repensiviricetes > Geplafuvirales > Geminiviridae > Turncurtovirus
Accessions
- Primary accessionA0A7D6BY77
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homooligomer. Rep binds to repeated DNA motifs (iterons). Forms the O-complex, which is a Rep-DNA complex involved in the initiation of RCR. Part of the C- and V-complexes which are RepA-Rep-DNA complexes involved in the c-sense and v-sense transcription.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Domain | 9-117 | CRESS-DNA virus Rep endonuclease | |||
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.
Sequence similarities
Belongs to the geminiviridae Rep protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length373
- Mass (Da)42,750
- Last updated2020-12-02 v1
- Checksum1D850545255596E5
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
MT041691 EMBL· GenBank· DDBJ | QLJ85078.1 EMBL· GenBank· DDBJ | Genomic DNA |