P58965 · DPO4_CALS4
- ProteinDNA polymerase IV
- GenedinB
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids384 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
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).
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
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
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.
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | double-stranded DNA binding | |
Molecular Function | magnesium ion binding | |
Molecular Function | oxidized DNA binding | |
Biological Process | DNA synthesis involved in DNA repair | |
Biological Process | DNA-templated DNA replication | |
Biological Process | error-prone translesion synthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA polymerase IV
- EC number
- Short namesPol IV
- Alternative names
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Bacillota > Clostridia > Thermoanaerobacterales > Thermoanaerobacteraceae > Caldanaerobacter
Accessions
- Primary accessionP58965
- Secondary accessions
Proteomes
Subcellular Location
Phenotypes & Variants
Features
Showing features for mutagenesis.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 9 | Nearly 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. | ||||
Sequence: D → A | ||||||
Mutagenesis | 10 | Increased 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. | ||||
Sequence: M → A | ||||||
Mutagenesis | 12 | Decreased 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. | ||||
Sequence: A → E | ||||||
Mutagenesis | 13 | Increased 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. | ||||
Sequence: F → A | ||||||
Mutagenesis | 14 | Decreased 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. | ||||
Sequence: F → A | ||||||
Mutagenesis | 38 | 20-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. | ||||
Sequence: R → A | ||||||
Mutagenesis | 42 | Decreased 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. | ||||
Sequence: S → A | ||||||
Mutagenesis | 43 | Decreased 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. | ||||
Sequence: T → A | ||||||
Mutagenesis | 46 | Decreased 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. | ||||
Sequence: Y → A | ||||||
Mutagenesis | 49 | Decreased 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. | ||||
Sequence: R → A | ||||||
Mutagenesis | 56 | 20-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. | ||||
Sequence: A → E | ||||||
Mutagenesis | 103 | Decreased 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. | ||||
Sequence: D → A | ||||||
Mutagenesis | 147 | 20-fold lower dsDNA-binding compared to wild-type. | ||||
Sequence: K → A | ||||||
Mutagenesis | 154 | Significantly 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. | ||||
Sequence: K → A | ||||||
Mutagenesis | 180 | 20-fold lower dsDNA-binding compared to wild-type. | ||||
Sequence: G → V | ||||||
Mutagenesis | 182 | Significantly decreased dsDNA-binding compared to wild-type. | ||||
Sequence: G → E | ||||||
Mutagenesis | 185 | Significantly decreased dsDNA-binding compared to wild-type. | ||||
Sequence: S → A | ||||||
Mutagenesis | 240 | 20-fold lower dsDNA-binding compared to wild-type; when associated with E-241. | ||||
Sequence: I → A | ||||||
Mutagenesis | 241 | 20-fold lower dsDNA-binding compared to wild-type; when associated with A-240. | ||||
Sequence: G → E | ||||||
Mutagenesis | 245 | Significantly decreased dsDNA-binding compared to wild-type. | ||||
Sequence: T → A | ||||||
Mutagenesis | 290 | Significantly 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. | ||||
Sequence: F → A | ||||||
Mutagenesis | 297 | 20-fold lower dsDNA-binding compared to wild-type; when associated with A-298. | ||||
Sequence: K → A | ||||||
Mutagenesis | 298 | 20-fold lower dsDNA-binding compared to wild-type; when associated with A-297. | ||||
Sequence: T → A | ||||||
Mutagenesis | 327 | Significantly 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. | ||||
Sequence: R → A |
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000173960 | 1-384 | DNA polymerase IV | |||
Sequence: MKRKIIHVDMDAFFASIEQQDNPEYRGKPVIVGGLSGRGVVSTCSYEARKYGIHSAMPMYMAKKLCPQGIFLPVRRKRYEEVSEQIFRILYDITPFVEPVSIDEAYLDVTHVDKNPEDIALEIKKRVKDATGLTVSVGISYNKFLAKLASDWNKPDGLMVITEDMVPEILKPLPVTKVHGIGEKSAEKLRSIGIETVEDLLKLPQENLIELFGKTGVEIYNRIRGIDERPVETMREIKSIGKEKTLEKDTKNKELLIQHLKEFSEIVSEELIKERLYCRTVTVKIKTADFAVHTKSKTVDKYIRFSEDIYEVAKGILEEWKLEQYVRLIGLSVSNLSPVKYEQLSFLDKRLVKVIKAGNLAEEINKRIGKKIIKKGSELLKDNK |
Interaction
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-182 | UmuC | ||||
Sequence: IIHVDMDAFFASIEQQDNPEYRGKPVIVGGLSGRGVVSTCSYEARKYGIHSAMPMYMAKKLCPQGIFLPVRRKRYEEVSEQIFRILYDITPFVEPVSIDEAYLDVTHVDKNPEDIALEIKKRVKDATGLTVSVGISYNKFLAKLASDWNKPDGLMVITEDMVPEILKPLPVTKVHGIG |
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 statusComplete
- Length384
- Mass (Da)43,916
- Last updated2002-08-02 v1
- Checksum01C214516AD9AABB
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AE008691 EMBL· GenBank· DDBJ | AAM23550.1 EMBL· GenBank· DDBJ | Genomic DNA |