A0A6B9PT99 · A0A6B9PT99_9GEMI
- ProteinReplication-associated protein
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids195 (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 | 51 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 59 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 61 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 105 | For DNA cleavage activity | ||||
Sequence: Y | ||||||
Binding site | 109 | a divalent metal cation (UniProtKB | ChEBI) | ||||
Sequence: E |
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
Organism names
- Organism
- Strain
- Taxonomic lineageViruses > Monodnaviria > Shotokuvirae > Cressdnaviricota > Repensiviricetes > Geplafuvirales > Geminiviridae > Begomovirus
Accessions
- Primary accessionA0A6B9PT99
Subcellular Location
PTM/Processing
Keywords
- PTM
Interaction
Subunit
Homooligomer.
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 9-118 | CRESS-DNA virus Rep endonuclease | ||||
Sequence: RLTAKNIFLTYPRCDIPKDEVLQLLRDLPWAVVKPTYIRVARELHADGFPHLHCLIQLSGKSNIKDARFFNLTHPRRSAEFHPNAQSAKDANAVKNYITKEGDYCESGQY |
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 statusFragment
- Length195
- Mass (Da)21,999
- Last updated2020-06-17 v1
- Checksum335315B68A8FD7F5
Features
Showing features for non-terminal residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Non-terminal residue | 195 | |||||
Sequence: Q |