A0A8X8M4V4 · A0A8X8M4V4_9CAUD

  • Protein
    DNA helicase/primase
  • Gene
    4
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

Function

function

ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis. ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA. Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange. Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present.

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 2 Mg2+, one of which is catalytic.

Features

Showing features for binding site, site.

TypeIDPosition(s)Description
Binding site15Zn2+ (UniProtKB | ChEBI)
Binding site18Zn2+ (UniProtKB | ChEBI)
Binding site34Zn2+ (UniProtKB | ChEBI)
Binding site37Zn2+ (UniProtKB | ChEBI)
Binding site157Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site207Mg2+ 1 (UniProtKB | ChEBI); catalytic
Binding site237Mg2+ 2 (UniProtKB | ChEBI)
Binding site312-319ATP (UniProtKB | ChEBI)
Site361dTTP/dATP binding
Site465dTTP/dATP binding
Site504dTTP/dATP binding
Site522dTTP/dATP binding
Site535dTTP/dATP binding

GO annotations

AspectTerm
Cellular Componentprimosome complex
Molecular Function5'-3' DNA helicase activity
Molecular FunctionATP binding
Molecular FunctionDNA primase activity
Molecular Functionhydrolase activity
Molecular Functionsingle-stranded DNA binding
Molecular Functionzinc ion binding
Biological Processviral DNA genome replication

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA helicase/primase
  • EC number
  • Alternative names
    • Gene product 4
      (Gp4
      )

Gene names

    • Name
      4

Organism names

  • Taxonomic identifier
  • Organism
  • Taxonomic lineage
    Viruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Autographiviridae > Studiervirinae > Teseptimavirus

Accessions

  • Primary accession
    A0A8X8M4V4

Proteomes

Subcellular Location

Keywords

Interaction

Subunit

Homohexamer. Assembles as a hexamer onto linear or circular ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with the viral DNA polymerase that is bound to DNA; this interaction is essential to initiate leading-strand DNA synthesis. The priming complex consists of 2 DNA polymerases and 1 helicase-primase hexamer that assemble on the DNA template. Interacts with the single-stranded DNA-binding protein. Part of the replicase complex that includes the DNA polymerase, thioredoxin, the primase/helicase and the single-stranded DNA binding protein.

Family & Domains

Features

Showing features for zinc finger, domain, region, compositional bias.

TypeIDPosition(s)Description
Zinc finger15-37C4-like; zinc ribbon fold
Domain151-238Toprim
Domain281-548SF4 helicase
Region543-566Disordered
Compositional bias549-566Basic and acidic residues
Region550-566Binding to viral DNA polymerase

Domain

The N-terminus zinc finger domain is essential for delivering the primed DNA template to the DNA polymerase. The central core domain contains the primase activity. The C-terminus region is responsible for the helicase activity and binds 1 Mg2+-dTTP.

Sequence similarities

Belongs to the Teseptimavirus DNA helicase/primase family.

Keywords

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    566
  • Mass (Da)
    62,786
  • Last updated
    2022-12-14 v1
  • Checksum
    5A8372A019D639CD
MELEQDSIFLYHAPCENCGSSDGNSVYSDGHQFCFVCEHRVPASEERKQELSSRRRIVGGGKPMSYNVWNFGESNGRYSALTARGISKETCQKAGYWIAKVDGVMYQVADYRDQNGNIVSQKVRDKDKNFKTTGSHKSDALFGKHLWNGGKKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDANECHLNGHDREIMEQVWNAGPWIPDGVVSALSLRERIREHLSSEESVGLLFSGCSGINDKTLGARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRVRLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDVIILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRPVSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETGWLEPSSYSGEEESHSESTDWSKDTDF

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias549-566Basic and acidic residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
ON528715
EMBL· GenBank· DDBJ
URY10667.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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