A3F913 · A3F913_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 site471-478ATP (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
    • CN-SC1
    • C1
  • Taxonomic lineage
    Viruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Alphapapillomavirus > Alphapapillomavirus 4

Accessions

  • Primary accession
    A3F913

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue, cross-link.

TypeIDPosition(s)Description
Modified residue90Phosphoserine; by host
Modified residue103Phosphoserine; by host
Cross-link552Glycyl 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 region, motif, compositional bias, domain.

TypeIDPosition(s)Description
Region28-60Disordered
Motif84-86Nuclear localization signal
Motif102-111Nuclear export signal
Region119-138Disordered
Region143-185Disordered
Compositional bias148-170Basic and acidic residues
Region180-346DNA-binding region
Domain445-595SF3 helicase
Region617-643Disordered

Sequence similarities

Belongs to the papillomaviridae E1 protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    643
  • Mass (Da)
    72,433
  • Last updated
    2007-03-20 v1
  • Checksum
    A87C6637B379E70A
MEDSEGTDGTEEDGCRAGGWFHVEAIITHGQRQVSSDEDEDETETGEDLDFIDNRAPGDGQEIPLQLYAQQTAQDDEATVQALKRKFVASPLSACSCIENDLSPRLDAISLNRKSEKAKRRLFETEPPDSGYGNTQMVVGTPEEVTGDEESQGGRPVEDQEEERQGGDGEADLTVHTPQSGTDATGSVLNLLRSSNLKATLLSKFKDLFGVGFYELVRQFKSSKTACADWVVCAYGVYYAVAEGLKKLIQPHTQYAHIQVQTSSWGMVVFMLLRYNCAKNRDSVSKNMSMLLNIPEKHMLIEPPKLRSTPAALYWYKTAMGNGSEVYGETPEWIVRQTLVGHSMEDEQFRLSVMVQYAYDHDIVEESVLAFEYAQLADVDANAAAFLNSNCQAKYVKDAVTMCRHYKRAEREQMSMSQWITFRGNKVSEEGDWKPIVRFLRHQGVEFVSFLAAFKLFLKGVPKKNCIVFYGPADTGKSYFCMSLLQFLGGAVISYANSSSHFWLQPLSDSKIGLLDDATPQCWSYIDIYLRNLLDGHPVSIDRKHKTLLQLKCPPLMITTNTNPLEEDRWKYLRSRLTVFTFKNPFPFASPGEPLYPINNANWKCFFQRSWSRLDLNSPEEQDDNGNTGEPFRCVPGDVARTV

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias148-170Basic and acidic residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
EF362755
EMBL· GenBank· DDBJ
ABN49466.1
EMBL· GenBank· DDBJ
Genomic DNA
EF117890
EMBL· GenBank· DDBJ
ABO14915.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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