A0A1L3GV98 · A0A1L3GV98_9PAPI

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 site436-443ATP (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

  • Taxonomic identifier
  • Strain
    • GC2011
  • Taxonomic lineage
    Viruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Deltapapillomavirus > Deltapapillomavirus 7

Accessions

  • Primary accession
    A0A1L3GV98

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, cross-link.

Type
IDPosition(s)Description
Modified residue81Phosphoserine; by host
Modified residue84Phosphoserine; by host
Modified residue102Phosphoserine; by host
Cross-link517Glycyl 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.

Family & Domains

Features

Showing features for motif, domain, region.

Type
IDPosition(s)Description
Motif75-77Nuclear localization signal
Domain410-560SF3 helicase
Region583-609Disordered

Sequence similarities

Belongs to the papillomaviridae E1 protein family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    609
  • Mass (Da)
    67,992
  • Last updated
    2017-03-15 v1
  • Checksum
    CD8D54C88994BE10
MDNHQGRHGLGGGCVFLDDEAVCEDSQDPDSPAAGEADAADLDFVDNAALEQGNHLLLFQTQMKEAGDKQIAGIKRKLQLSPYSQVPACPTQPQISQNRNHSLVKRRLFDCDRPVAGSHEAPRTVETILQVHQGDNQQEKGQNRGCGEEDLHAQLCRAKNSAACMLKLFKTLFIASFAELTRVFKSSKTCNPQWVVAAFGVPEVLHEASFELLKKDCVYLQTTRKVHEAGSAALYLCVFHVAKSRETVENLVSKLLNVPTSCIMTQPPKIRGTCAPLFWVKSSMSPFSYCHGDMPQWILSQTLISENVAEVTKFDFGAMVQWAYDMGYTEESKIAYEYALSADTDSNAKAFLAACNQPKLVKDCATMVKLYQRAQVQKMTMSAYIHHRCERAGTGGNWNNIMSLLKFQGITPITFVNALKSWLKGIPKQNCLAFIGPPNSGKSMLCNSLMSFMGGKVLTFANHHSHFWLQPLTDARVALIDDATDACWKYFDTYLRNVLDGYEVCIDRKHKSAVQMKAPPLLITSNVDVCSVQKFFYLKSRIVPFYFPETVPTSENGEPLFFITDADWSVFFTRLWGRLDLSDQEEEGDEDGQSQGSFRCSARKADDAH

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KX954132
EMBL· GenBank· DDBJ
APG30981.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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