A0A0P0E4M9 · A0A0P0E4M9_HPV51

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 site463-470ATP (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
  • Organism
  • Strains
    • BF63
    • Qv00885
    • Qv23639
    • Qv34180
    • RW20
  • Taxonomic lineage
    Viruses > Monodnaviria > Shotokuvirae > Cossaviricota > Papovaviricetes > Zurhausenvirales > Papillomaviridae > Firstpapillomavirinae > Alphapapillomavirus > Alphapapillomavirus 5

Accessions

  • Primary accession
    A0A0P0E4M9

Proteomes

Subcellular Location

Keywords

PTM/Processing

Features

Showing features for modified residue.

TypeIDPosition(s)Description
Modified residue91Phosphoserine; by host
Modified residue95Phosphoserine; by host

Post-translational modification

Phosphorylated.

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, compositional bias, domain.

TypeIDPosition(s)Description
Motif85-87Nuclear localization signal
Region92-117Disordered
Compositional bias95-117Polar residues
Region172-338DNA-binding region
Domain437-587SF3 helicase

Sequence similarities

Belongs to the papillomaviridae E1 protein family.

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    634
  • Mass (Da)
    71,685
  • Last updated
    2016-01-20 v1
  • Checksum
    C429CCBFA515CEE1
MDCEGTEDEGAGCNGWFFVEAIVEKKTGDNVSDDEDENADDTGSDLINFIDSETSICSQAEQETARALFQAQELQANKEAVHQLKRKFLVSPRSSPLGDITNQNNTHSHSQANESQVKRRLLDSYPDSGYGNTQVETVEATLQVDGQHGGSQNSVCSSGGGSVMDVETTESCANVELNSICEVLKSSNAKATLMAKFKELYGISYNELVRVFKSDKTCCIDWVCALFGVSPMVAENLKTLIKPFCMYYHIQCLSCDWGTIVLMLIRFSCAKNRTTIAKCLSTLVNIPQSQMFIEPPKLRSTPVALYFYRTGISNISNTYGETPEWITRQTQLQHSFEDSTFELSQMVQWAFDHEVLDDSEIAFHYAQLADIDSNAAAFLKSNCQAKYVKDCGTMARHYKRAQRKSLSMSAWIRYRCDRAKDGGNWREIAKFLRYQGVNFMSFIQMFKQFLKGTPKHNCIVIYGPPNTGKSLFAMSLMKFMQGSIISYVNSGSHFWLQPLEDAKIALLDDATYGCWTYIDQYLRNFLDGNPCSIDRKHRSLIQLVCPPLLITSNINPQEDANLMYLHTRVTVLKFLNTFPFDNNGNAVYTLNDENWKNFFSTTWSRLDLEEEEDKENGDPMPPFKCVPGENTRLL

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias95-117Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
KF436866
EMBL· GenBank· DDBJ
ALJ32863.1
EMBL· GenBank· DDBJ
Genomic DNA
KF436867
EMBL· GenBank· DDBJ
ALJ32870.1
EMBL· GenBank· DDBJ
Genomic DNA
KF436868
EMBL· GenBank· DDBJ
ALJ32877.1
EMBL· GenBank· DDBJ
Genomic DNA
KF436871
EMBL· GenBank· DDBJ
ALJ32898.1
EMBL· GenBank· DDBJ
Genomic DNA
KF436872
EMBL· GenBank· DDBJ
ALJ32905.1
EMBL· GenBank· DDBJ
Genomic DNA
KU298902
EMBL· GenBank· DDBJ
ALT54764.1
EMBL· GenBank· DDBJ
Genomic DNA
KU298903
EMBL· GenBank· DDBJ
ALT54771.1
EMBL· GenBank· DDBJ
Genomic DNA
KU298904
EMBL· GenBank· DDBJ
ALT54778.1
EMBL· GenBank· DDBJ
Genomic DNA
KU298905
EMBL· GenBank· DDBJ
ALT54785.1
EMBL· GenBank· DDBJ
Genomic DNA
KX514432
EMBL· GenBank· DDBJ
ARQ82732.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861810
EMBL· GenBank· DDBJ
CAD1799156.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861846
EMBL· GenBank· DDBJ
CAD1807082.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861863
EMBL· GenBank· DDBJ
CAD1807199.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861869
EMBL· GenBank· DDBJ
CAD1807244.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861887
EMBL· GenBank· DDBJ
CAD1807377.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861893
EMBL· GenBank· DDBJ
CAD1807420.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861896
EMBL· GenBank· DDBJ
CAD1807442.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861911
EMBL· GenBank· DDBJ
CAD1807549.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861920
EMBL· GenBank· DDBJ
CAD1807613.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861929
EMBL· GenBank· DDBJ
CAD1807676.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861939
EMBL· GenBank· DDBJ
CAD1807742.1
EMBL· GenBank· DDBJ
Genomic DNA
LR861977
EMBL· GenBank· DDBJ
CAD1813874.1
EMBL· GenBank· DDBJ
Genomic DNA
LR862023
EMBL· GenBank· DDBJ
CAD1814142.1
EMBL· GenBank· DDBJ
Genomic DNA
LR862037
EMBL· GenBank· DDBJ
CAD1814248.1
EMBL· GenBank· DDBJ
Genomic DNA
LR862069
EMBL· GenBank· DDBJ
CAD1814481.1
EMBL· GenBank· DDBJ
Genomic DNA
LR862072
EMBL· GenBank· DDBJ
CAD1814509.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care. Our staff consists of biologists and biochemists that are not trained to give medical advice.
We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.
FeedbackHelp