A0A1L3GV98 · A0A1L3GV98_9PAPI
- ProteinReplication protein E1
- GeneE1
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids609 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
ATP-dependent DNA helicase required for initiation of viral DNA replication. It forms a complex with the viral E2 protein. The E1-E2 complex binds to the replication origin which contains binding sites for both proteins. During the initial step, a dimer of E1 interacts with a dimer of protein E2 leading to a complex that binds the viral origin of replication with high specificity. Then, a second dimer of E1 displaces the E2 dimer in an ATP-dependent manner to form the E1 tetramer. Following this, two E1 monomers are added to each half of the site, which results in the formation of two E1 trimers on the viral ori. Subsequently, two hexamers will be created. The double hexamer acts as a bi-directional helicase machinery and unwinds the viral DNA and then recruits the host DNA polymerase to start replication.
Catalytic activity
- ATP + H2O = ADP + phosphate + H+
Features
Showing features for binding site.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Binding site | 436-443 | ATP (UniProtKB | ChEBI) | |||
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleus | |
Molecular Function | ATP binding | |
Molecular Function | ATP hydrolysis activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA helicase activity | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameReplication protein E1
- EC number
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageViruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Deltapapillomavirus > Deltapapillomavirus 7
Accessions
- Primary accessionA0A1L3GV98
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, cross-link.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Modified residue | 81 | Phosphoserine; by host | |||
Modified residue | 84 | Phosphoserine; by host | |||
Modified residue | 102 | Phosphoserine; by host | |||
Cross-link | 517 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | |||
Post-translational modification
Phosphorylated.
Sumoylated.
Keywords
- PTM
Expression
Keywords
- Developmental stage
Interaction
Subunit
Can form hexamers. Interacts with E2 protein; this interaction increases E1 DNA binding specificity. Interacts with host DNA polymerase subunit POLA2. Interacts with host single stranded DNA-binding protein RPA1. Interacts with host TOP1; this interaction stimulates the enzymatic activity of TOP1.
Structure
Family & Domains
Features
Showing features for motif, domain, region.
Type | ID | Position(s) | Description | ||
---|---|---|---|---|---|
Motif | 75-77 | Nuclear localization signal | |||
Domain | 410-560 | SF3 helicase | |||
Region | 583-609 | Disordered | |||
Sequence similarities
Belongs to the papillomaviridae E1 protein family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length609
- Mass (Da)67,992
- Last updated2017-03-15 v1
- ChecksumCD8D54C88994BE10
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
KX954132 EMBL· GenBank· DDBJ | APG30981.1 EMBL· GenBank· DDBJ | Genomic DNA |