P58965 · DPO4_CALS4

Function

function

Poorly processive, error-prone DNA polymerase involved in translesion repair and untargeted mutagenesis. Copies undamaged DNA at stalled replication forks, which arise in vivo from mismatched or misaligned primer ends. These misaligned primers can be extended by PolIV. Exhibits no 3'-5' exonuclease (proofreading) activity (By similarity).
Involved in translesional synthesis. Primer extension fidelity in vitro is temperature-dependent. Inserts a correct base opposite templating bases at 70 degrees Celsius, but at 37 degrees Celsius in addition to correct base pairing, base transitions, transversions and frameshifts can occur. Preferably forms erroneous base pairs C:T. Bypasses 8-oxo-dG oxidative damage by incorporating dATP or dCTP opposite of the damaged DNA template site at both temperatures in vitro (PubMed:37683741).

Catalytic activity

Cofactor

Mg2+ (UniProtKB | Rhea| CHEBI:18420 )

Note: Binds 1 magnesium ion per subunit.

Temperature Dependence

Optimum temperature is around 70 degrees Celsius for the DNA polymerase activity. Active also at 25 degrees Celsius, but polymerase activity increases with increasing temperature. Activity decreases with temperatures higher than 70 degrees Celsius.

Features

Showing features for binding site, site, active site.

TypeIDPosition(s)Description
Binding site9Mg2+ (UniProtKB | ChEBI)
Binding site10Mg2+ (UniProtKB | ChEBI)
Site14Substrate discrimination
Binding site103Mg2+ (UniProtKB | ChEBI)
Active site104

GO annotations

AspectTerm
Cellular Componentcytoplasm
Molecular FunctionDNA-directed DNA polymerase activity
Molecular Functiondouble-stranded DNA binding
Molecular Functionmagnesium ion binding
Molecular Functionoxidized DNA binding
Biological ProcessDNA synthesis involved in DNA repair
Biological ProcessDNA-templated DNA replication
Biological Processerror-prone translesion synthesis

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

  • Recommended name
    DNA polymerase IV
  • EC number
  • Short names
    Pol IV
  • Alternative names
    • Translesion synthesis DNA polymerase TTEDbh
      (TLS DNA polymerase TTEDbh
      )

Gene names

    • Name
      dinB
    • Ordered locus names
      TTE0254

Organism names

Accessions

  • Primary accession
    P58965
  • Secondary accessions
    • Q8RD00

Proteomes

Subcellular Location

Keywords

Phenotypes & Variants

Features

Showing features for mutagenesis.

TypeIDPosition(s)Description
Mutagenesis9Nearly complete loss of primer extension activity. No formation of correct or incorrect base pairs with the DNA template at 37 degrees Celsius. No incorporation of dATP, dGTP, dCTP, dTTP or dNTP mixes opposite 8-oxo-dG to bypass oxidative damage of the DNA template at neither 37 nor 70 degrees Celsius.
Mutagenesis10Increased primer extension activity compared to wild-type. Increased formation of incorrect base pairs with the DNA template at 37 degrees Celsius. Increased incorporation of dNTPs, especially dTTP, opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but shows no difference from wild-type at 70 degrees Celsius.
Mutagenesis12Decreased primer extension activity compared to wild-type. Forms correct, but not incorrect base pairs with the DNA template at 37 degrees Celsius. Can only incorporate dATP opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.
Mutagenesis13Increased primer extension activity compared to wild-type. Increased formation of incorrect base pairs with the DNA template at 37 degrees Celsius. No difference from wild-type on the incorporation of dNTPs opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but partial loss of the bypass ability at 70 degrees Celsius.
Mutagenesis14Decreased primer extension activity compared to wild-type. Forms correct, but not incorrect base pairs with the DNA template at 37 degrees Celsius. Can only incorporate dATP opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.
Mutagenesis3820-fold lower dsDNA-binding compared to wild-type. Bypasses 8-oxo-dG oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.
Mutagenesis42Decreased primer extension activity compared to wild-type. Loss of dCTP incorporation opposite adenine, but retained ability to form other incorrect base pairs with the DNA template at 37 degrees Celsius. No difference from wild-type on the incorporation of dNTPs opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but partial loss of the bypass ability at 70 degrees Celsius.
Mutagenesis43Decreased primer extension activity compared to wild-type. Partially retained formation of incorrect base pairs with the DNA template at 37 degrees Celsius. No difference from wild-type on the incorporation of dNTPs opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but partial loss of the bypass ability at 70 degrees Celsius.
Mutagenesis46Decreased primer extension activity compared to wild-type. Forms correct, but not incorrect base pairs with the DNA template at 37 degrees Celsius. No difference from wild-type on the incorporation of dNTPs opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.
Mutagenesis49Decreased primer extension activity compared to wild-type. Forms correct, but not incorrect base pairs with the DNA template at 37 degrees Celsius. Can only incorporate dATP opposite 8-oxo-dG to bypass oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.
Mutagenesis5620-fold lower dsDNA-binding compared to wild-type. Bypasses 8-oxo-dG oxidative damage of the DNA template at 37 degrees Celsius, but partial loss of the bypass ability at 70 degrees Celsius.
Mutagenesis103Decreased primer extension activity compared to wild-type. Forms correct base pairs to an extent with adenine, cytosine and thymine of the DNA template at 37 degrees Celsius. No incorporation of dATP, dGTP, dCTP, dTTP or dNTP mixes opposite 8-oxo-dG to bypass oxidative damage of the DNA template at neither 37 nor 70 degrees Celsius.
Mutagenesis14720-fold lower dsDNA-binding compared to wild-type.
Mutagenesis154Significantly decreased primer extension activity compared to wild-type. Forms correct, but not incorrect base pairs with the DNA template at 37 degrees Celsius. No incorporation of dATP, dGTP, dCTP, dTTP or dNTP mixes opposite 8-oxo-dG to bypass oxidative damage of the DNA template at neither 37 nor 70 degrees Celsius.
Mutagenesis18020-fold lower dsDNA-binding compared to wild-type.
Mutagenesis182Significantly decreased dsDNA-binding compared to wild-type.
Mutagenesis185Significantly decreased dsDNA-binding compared to wild-type.
Mutagenesis24020-fold lower dsDNA-binding compared to wild-type; when associated with E-241.
Mutagenesis24120-fold lower dsDNA-binding compared to wild-type; when associated with A-240.
Mutagenesis245Significantly decreased dsDNA-binding compared to wild-type.
Mutagenesis290Significantly decreased dsDNA-binding compared to wild-type. Bypasses 8-oxo-dG oxidative damage of the DNA template at 37 degrees Celsius, but partial loss of the bypass ability at 70 degrees Celsius.
Mutagenesis29720-fold lower dsDNA-binding compared to wild-type; when associated with A-298.
Mutagenesis29820-fold lower dsDNA-binding compared to wild-type; when associated with A-297.
Mutagenesis327Significantly decreased dsDNA-binding compared to wild-type. Bypasses 8-oxo-dG oxidative damage of the DNA template at 37 degrees Celsius, but complete loss of the bypass ability at 70 degrees Celsius.

PTM/Processing

Features

Showing features for chain.

TypeIDPosition(s)Description
ChainPRO_00001739601-384DNA polymerase IV

Interaction

Subunit

Monomer.

Protein-protein interaction databases

Family & Domains

Features

Showing features for domain.

TypeIDPosition(s)Description
Domain5-182UmuC

Domain

The catalytic core consists of residues from subdomains of the finger (11-75), palm (77-161), thumb (163-224) and little finger (240-335).

Sequence similarities

Belongs to the DNA polymerase type-Y family.

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    384
  • Mass (Da)
    43,916
  • Last updated
    2002-08-02 v1
  • Checksum
    01C214516AD9AABB
MKRKIIHVDMDAFFASIEQQDNPEYRGKPVIVGGLSGRGVVSTCSYEARKYGIHSAMPMYMAKKLCPQGIFLPVRRKRYEEVSEQIFRILYDITPFVEPVSIDEAYLDVTHVDKNPEDIALEIKKRVKDATGLTVSVGISYNKFLAKLASDWNKPDGLMVITEDMVPEILKPLPVTKVHGIGEKSAEKLRSIGIETVEDLLKLPQENLIELFGKTGVEIYNRIRGIDERPVETMREIKSIGKEKTLEKDTKNKELLIQHLKEFSEIVSEELIKERLYCRTVTVKIKTADFAVHTKSKTVDKYIRFSEDIYEVAKGILEEWKLEQYVRLIGLSVSNLSPVKYEQLSFLDKRLVKVIKAGNLAEEINKRIGKKIIKKGSELLKDNK

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AE008691
EMBL· GenBank· DDBJ
AAM23550.1
EMBL· GenBank· DDBJ
Genomic DNA

Genome annotation databases

Similar Proteins

Disclaimer

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