O00529 · O00529_HPV16

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.

Caution

Lacks conserved residue(s) required for the propagation of feature annotation.

Catalytic activity

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site477-484ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenthost cell nucleus
Molecular FunctionATP binding
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
Molecular Functionhydrolase activity, acting on acid anhydrides
Biological ProcessDNA replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    Replication protein E1
  • EC number
  • Alternative names
    • ATP-dependent helicase E1

Gene names

    • Name
      E1

Organism names

  • Taxonomic identifier
  • Strains
    • R4000S3
    • R4000S4
    • K0133
    • K0604
    • K1227
  • Taxonomic lineage
    Viruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Alphapapillomavirus > Alphapapillomavirus 9

Accessions

  • Primary accession
    O00529
  • Secondary accessions
    • C6G875

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, cross-link.

TypeIDPosition(s)Description
Modified residue93Phosphoserine; by host
Modified residue107Phosphoserine; by host
Cross-link558Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

Post-translational modification

Phosphorylated.
Sumoylated.

Keywords

Expression

Keywords

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

3D structure databases

Family & Domains

Features

Showing features for motif, region, domain.

TypeIDPosition(s)Description
Motif87-89Nuclear localization signal
Motif106-115Nuclear export signal
Region186-352DNA-binding region
Domain451-601SF3 helicase
Region624-649Disordered

Sequence similarities

Belongs to the papillomaviridae E1 protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    649
  • Mass (Da)
    72,915
  • Last updated
    1997-07-01 v1
  • Checksum
    9267D32D04391FC6
MADPAGTNGEEGTGCNGWFYVEAVVEKKTGDAISDDENENDSDTGEDLVDFIVNDNDYLTQAETETAHALFTAQEAKQHRDAVQVLKRKYLGSPLSDISGCVDNNISPRLKAICIEKQSRAAKRRLFESEDSGYGNTEVETQQMLQVEGRHETETPCSQYSGGSGGGCSQYSSGSGGEGVSERHTICQTPLTNILNVLKTSNAKAAMLAKFKELYGVSFSELVRPFKSNKSTCCDWCIAAFGLTPSIADSIKTLLQQYCLYLHIQSLACSWGMVVLLLVRYKCGKNRETIEKLLSKLLCVSPMCMMIEPPKLRSTAAALYWYKTGMSNISEVYGDTPEWIQRQTVLQHSFNDCTFELSQMVQWAYDNDIVDDSEIAYKYAQLADTNSNASAFLKSNSQAKIVKDCATMCRHYKRAEKKQMSMSQWIKYRCDRVDDGGDWKQIVMFLRYQGVEFMSFLTALKRFLQGIPKKNCILLYGAANTGKSLFGMSLMKFLQGSVICFVNSKSHFWLQPLADAKIGMLDDATVPCWNYIDDNLRNALDGNLVSMDVKHRPLVQLKCPPLLITSNINAGTDSRWPYLHNRLVVFTFPNEFPFDENGNPVYELNDKNWKSFFSRTWSRLSLHEDEDKENDGDSLPTFKCVSGQNTNTL

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
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

Similar Proteins

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