P11298 · VE1_BPV2

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.
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

Features

Showing features for binding site.

TypeIDPosition(s)Description
Binding site432-439ATP (UniProtKB | ChEBI)

GO annotations

AspectTerm
Cellular Componenthost cell nucleus
Molecular FunctionATP binding
Molecular FunctionATP hydrolysis activity
Molecular FunctionDNA binding
Molecular FunctionDNA helicase activity
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

Accessions

  • Primary accession
    P11298

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for chain, modified residue, cross-link.

TypeIDPosition(s)Description
ChainPRO_00001330911-604Replication protein E1
Modified residue90Phosphoserine; by host
Modified residue94Phosphoserine; by host
Cross-link513Glycyl 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.

Protein-protein interaction databases

Structure

3D structure databases

Family & Domains

Features

Showing features for region, motif, domain, compositional bias.

TypeIDPosition(s)Description
Region24-48Disordered
Motif84-86Nuclear localization signal
Region90-112Disordered
Region141-307DNA-binding region
Domain406-556SF3 helicase
Region581-604Disordered
Compositional bias590-604Polar residues

Sequence similarities

Belongs to the papillomaviridae E1 protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    604
  • Mass (Da)
    68,077
  • Last updated
    1989-07-01 v1
  • Checksum
    D2D7036ADE88A9DD
MANDKGSNWDSALGCSYLLTEAECESDKENEEPGAGVELSVESDRYDSQDEDFLDNASVFQGNHLEVFQALEKKAGEEQLLNLKRKVLGSSENSSGSEASETPAKRQKAGAKRRLFSENEANRVLTPLQVQGGEWRQGFNEDQAISHRLLQLVKSKNATVFKLGLFKSLFLCSFHDLTRLFKNDKTTNQQWVLAVFGIAEVFFEASLELLKKQCSFVQMQKRSHEGGTCAVYLLCFNTAKSRETVRNLMANMLNVREECLLMQPPKIRGLSAALFWFKSSLSPATLKHGALPEWIRAQTTLHDSLATEKFDFGTMVQWAYDHKYAEESKIAYEYALAAGSDSNARAFLATNSQAKHVKDCATMVRHYLRAETQALSMPAYIKTRCKLATGEGSWKSILTFFNYQNIELITFINALKLWLNGIPKKNCLAFIGPPKTGKSMLCNSLIHFLGGSVLSFANHKSHFWLASLADARAALVDDATHACWRYFDTYLRNALDGYPVSIDRKHKAAVQIKAPPLLVTSNIDVQAEERYLYLHSRVQTFRFEQPCTDESGEQPFTITDADWKSFFVRLWGRLDLVDEEEDSEEDGDSMRTFTCSARNTNAVD

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias590-604Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
M20219
EMBL· GenBank· DDBJ
AAA66833.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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