A3F913 · A3F913_9PAPI
- ProteinReplication protein E1
- GeneE1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids643 (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 + H+ + phosphate
Features
Showing features for binding site.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | host cell nucleus | |
Molecular Function | ATP binding | |
Molecular Function | DNA binding | |
Molecular Function | DNA helicase activity | |
Molecular Function | hydrolase activity, acting on acid anhydrides | |
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
- Organism
- Strains
- Taxonomic lineageViruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Alphapapillomavirus > Alphapapillomavirus 4
Accessions
- Primary accessionA3F913
Proteomes
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 90 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 103 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Cross-link | 552 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) | ||||
Sequence: K |
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 region, motif, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 28-60 | Disordered | ||||
Sequence: THGQRQVSSDEDEDETETGEDLDFIDNRAPGDG | ||||||
Motif | 84-86 | Nuclear localization signal | ||||
Sequence: KRK | ||||||
Motif | 102-111 | Nuclear export signal | ||||
Sequence: LSPRLDAISL | ||||||
Region | 119-138 | Disordered | ||||
Sequence: KRRLFETEPPDSGYGNTQMV | ||||||
Region | 143-185 | Disordered | ||||
Sequence: EEVTGDEESQGGRPVEDQEEERQGGDGEADLTVHTPQSGTDAT | ||||||
Compositional bias | 148-170 | Basic and acidic residues | ||||
Sequence: DEESQGGRPVEDQEEERQGGDGE | ||||||
Region | 180-346 | DNA-binding region | ||||
Sequence: SGTDATGSVLNLLRSSNLKATLLSKFKDLFGVGFYELVRQFKSSKTACADWVVCAYGVYYAVAEGLKKLIQPHTQYAHIQVQTSSWGMVVFMLLRYNCAKNRDSVSKNMSMLLNIPEKHMLIEPPKLRSTPAALYWYKTAMGNGSEVYGETPEWIVRQTLVGHSMED | ||||||
Domain | 445-595 | SF3 helicase | ||||
Sequence: VEFVSFLAAFKLFLKGVPKKNCIVFYGPADTGKSYFCMSLLQFLGGAVISYANSSSHFWLQPLSDSKIGLLDDATPQCWSYIDIYLRNLLDGHPVSIDRKHKTLLQLKCPPLMITTNTNPLEEDRWKYLRSRLTVFTFKNPFPFASPGEPL | ||||||
Region | 617-643 | Disordered | ||||
Sequence: NSPEEQDDNGNTGEPFRCVPGDVARTV |
Sequence similarities
Belongs to the papillomaviridae E1 protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length643
- Mass (Da)72,433
- Last updated2007-03-20 v1
- ChecksumA87C6637B379E70A
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 148-170 | Basic and acidic residues | ||||
Sequence: DEESQGGRPVEDQEEERQGGDGE |