O00529 · O00529_HPV16
- ProteinReplication protein E1
- GeneE1
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids649 (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 9
- Virus hosts
Accessions
- Primary accessionO00529
- Secondary accessions
Subcellular Location
PTM/Processing
Features
Showing features for modified residue, cross-link.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 93 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Modified residue | 107 | Phosphoserine; by host | ||||
Sequence: S | ||||||
Cross-link | 558 | 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.
Family & Domains
Features
Showing features for motif, region, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Motif | 87-89 | Nuclear localization signal | ||||
Sequence: KRK | ||||||
Motif | 106-115 | Nuclear export signal | ||||
Sequence: ISPRLKAICI | ||||||
Region | 186-352 | DNA-binding region | ||||
Sequence: ICQTPLTNILNVLKTSNAKAAMLAKFKELYGVSFSELVRPFKSNKSTCCDWCIAAFGLTPSIADSIKTLLQQYCLYLHIQSLACSWGMVVLLLVRYKCGKNRETIEKLLSKLLCVSPMCMMIEPPKLRSTAAALYWYKTGMSNISEVYGDTPEWIQRQTVLQHSFND | ||||||
Domain | 451-601 | SF3 helicase | ||||
Sequence: VEFMSFLTALKRFLQGIPKKNCILLYGAANTGKSLFGMSLMKFLQGSVICFVNSKSHFWLQPLADAKIGMLDDATVPCWNYIDDNLRNALDGNLVSMDVKHRPLVQLKCPPLLITSNINAGTDSRWPYLHNRLVVFTFPNEFPFDENGNPV | ||||||
Region | 624-649 | Disordered | ||||
Sequence: EDEDKENDGDSLPTFKCVSGQNTNTL |
Sequence similarities
Belongs to the papillomaviridae E1 protein family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length649
- Mass (Da)72,915
- Last updated1997-07-01 v1
- Checksum9267D32D04391FC6
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AF001599 EMBL· GenBank· DDBJ | AAC27658.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
MG850069 EMBL· GenBank· DDBJ | AVN81326.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC027223 EMBL· GenBank· DDBJ | BAQ53888.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC027929 EMBL· GenBank· DDBJ | BAQ53894.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368954 EMBL· GenBank· DDBJ | BBC83374.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368958 EMBL· GenBank· DDBJ | BBC83406.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368965 EMBL· GenBank· DDBJ | BBC83462.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368974 EMBL· GenBank· DDBJ | BBC83534.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368985 EMBL· GenBank· DDBJ | BBC83622.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC368987 EMBL· GenBank· DDBJ | BBC83638.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456180 EMBL· GenBank· DDBJ | BBI15999.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456183 EMBL· GenBank· DDBJ | BBI16023.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456186 EMBL· GenBank· DDBJ | BBI16047.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456188 EMBL· GenBank· DDBJ | BBI16063.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456193 EMBL· GenBank· DDBJ | BBI16103.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456195 EMBL· GenBank· DDBJ | BBI16119.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456619 EMBL· GenBank· DDBJ | BBI18825.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456625 EMBL· GenBank· DDBJ | BBI18873.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC456634 EMBL· GenBank· DDBJ | BBI18945.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC511105 EMBL· GenBank· DDBJ | BBP42193.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC644182 EMBL· GenBank· DDBJ | BCZ98942.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC644184 EMBL· GenBank· DDBJ | BCZ98958.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC644185 EMBL· GenBank· DDBJ | BCZ98966.1 EMBL· GenBank· DDBJ | Genomic DNA | ||
LC644186 EMBL· GenBank· DDBJ | BCZ98974.1 EMBL· GenBank· DDBJ | Genomic DNA |