Q32PL8 · PRIPO_DANRE
- ProteinDNA-directed primase/polymerase protein
- Geneprimpol
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids523 (go to sequence)
- Protein existenceEvidence at transcript level
- Annotation score4/5
Function
function
DNA primase and DNA polymerase required to tolerate replication-stalling lesions by bypassing them. Required to facilitate mitochondrial and nuclear replication fork progression by initiating de novo DNA synthesis using dNTPs and acting as an error-prone DNA polymerase able to bypass certain DNA lesions (By similarity).
Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity).
Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as UV lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (By similarity).
Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion. Repriming avoids fork degradation while leading to accumulation of internal ssDNA gaps behind the forks. Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase. Also required for reinitiating stalled forks after ultraviolet (UV) damage during nuclear DNA replication. Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides. In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity).
Shows a high capacity to tolerate DNA damage lesions such as 8oxoG and abasic sites in DNA (By similarity).
Provides different translesion synthesis alternatives when DNA replication is stalled: able to synthesize DNA primers downstream of lesions, such as UV lesions, R-loops and G-quadruplexes, to allow DNA replication to continue (By similarity).
Can also realign primers ahead of 'unreadable lesions' such as abasic sites and 6-4 photoproduct (6-4 pyrimidine-pyrimidinone), thereby skipping the lesion. Repriming avoids fork degradation while leading to accumulation of internal ssDNA gaps behind the forks. Also able to incorporate nucleotides opposite DNA lesions such as 8oxoG, like a regular translesion synthesis DNA polymerase. Also required for reinitiating stalled forks after ultraviolet (UV) damage during nuclear DNA replication. Required for mitochondrial DNA (mtDNA) synthesis and replication, by reinitiating synthesis after UV damage or in the presence of chain-terminating nucleotides. In addition to its role in DNA damage response, also required to maintain efficient nuclear and mitochondrial DNA replication in unperturbed cells (By similarity).
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)This reaction proceeds in the forward direction.
Cofactor
Note: Can act both with Mn2+ and Mg2+ as cofactor in vitro, but Mn2+ is the preferred cofactor in vivo.
Features
Showing features for binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 78 | substrate | ||||
Sequence: R | ||||||
Binding site | 117 | Mn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 117-119 | substrate | ||||
Sequence: DLE | ||||||
Binding site | 119 | Mn2+ (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 168-172 | substrate | ||||
Sequence: KFSHH | ||||||
Binding site | 258-261 | substrate | ||||
Sequence: RNFR | ||||||
Binding site | 267 | substrate | ||||
Sequence: K | ||||||
Binding site | 390 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 397 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 417 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 422 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | DNA-directed RNA polymerase complex | |
Cellular Component | mitochondrial matrix | |
Cellular Component | nucleus | |
Cellular Component | replication fork | |
Molecular Function | chromatin binding | |
Molecular Function | DNA primase activity | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | manganese ion binding | |
Molecular Function | zinc ion binding | |
Biological Process | error-prone translesion synthesis | |
Biological Process | mitochondrial DNA repair | |
Biological Process | mitochondrial DNA replication | |
Biological Process | R-loop processing | |
Biological Process | replication fork processing | |
Biological Process | response to UV | |
Biological Process | translesion synthesis |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed primase/polymerase protein
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Actinopterygii > Neopterygii > Teleostei > Ostariophysi > Cypriniformes > Danionidae > Danioninae > Danio
Accessions
- Primary accessionQ32PL8
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000279397 | 1-523 | DNA-directed primase/polymerase protein | |||
Sequence: MTGGKWQDRVKSVEQRASSFQSSPLSCPYKPRLSQPWQPSSIWRLFPRQNAAIAFAQHIKQDVHIFSLEKEGSDAGQRIFLVTSYSELWHYYSTHRHSLMHCYEVILEGAVCKLYFDLEFHKASNKNLDGKMMVAKLIQYVCEKLEEVYGLHCSAKDVLDLDSSTSDKFSHHLIFMLPNAAFKDNSHVGRFIHDILHPALTNLKKSNPEAPGENRDDVEGTQAKRRKTEENDLGFLTVKNEKGQEQLFVDLGVYTKNRNFRLYKSSKLGKNAAFIVAEDNKFVPNPSKQITKDERIFLASLITNVSFTGQRILTYDMTQKSTAGSECPTLERESHSSDLLGDQKTSPFKEVDEFVLTLVCKDGIQGSIRRWNYFACEQLLVYDIEKFRWCHNVKRFHKSNNIIIVVDLKEEVWYQKCHDPECRRQNYRSSSFPLPQEVCMSHLLMEDEEDQAYLTDELGNIELAVTAPAESTSTTPSEDTEGWGDWPDDPAYLRALQEVEEEEEDEDEEVPDELLLQAVNECE |
Proteomic databases
Expression
Gene expression databases
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for region, compositional bias, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 203-230 | Disordered | ||||
Sequence: LKKSNPEAPGENRDDVEGTQAKRRKTEE | ||||||
Compositional bias | 209-230 | Basic and acidic residues | ||||
Sequence: EAPGENRDDVEGTQAKRRKTEE | ||||||
Motif | 390-423 | Zinc knuckle motif | ||||
Sequence: CHNVKRFHKSNNIIIVVDLKEEVWYQKCHDPECR | ||||||
Region | 467-523 | Disordered | ||||
Sequence: APAESTSTTPSEDTEGWGDWPDDPAYLRALQEVEEEEEDEDEEVPDELLLQAVNECE | ||||||
Compositional bias | 498-514 | Acidic residues | ||||
Sequence: EVEEEEEDEDEEVPDEL |
Domain
The zinc knuckle motif binds zinc and is required for the DNA primase activity. It facilitates the binding and selection of the 5'-nucleotide of the newly synthesized primer and the recognition of preferred initiation sites.
The presence of an Asp-Aaa-Glu (DxE) motif in the metal-binding active site favors the use of Mn2+ ions to achieve optimal incoming nucleotide stabilization, especially required during primer synthesis. Glu-119 is required to stabilize the incoming nucleotide at the 3'-site.
Sequence similarities
Belongs to the eukaryotic-type primase small subunit family.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length523
- Mass (Da)60,194
- Last updated2014-01-22 v2
- Checksum5BDF30811D95773D
Features
Showing features for sequence conflict, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Sequence conflict | 193 | in Ref. 2; AAI08067 | ||||
Sequence: H → N | ||||||
Compositional bias | 209-230 | Basic and acidic residues | ||||
Sequence: EAPGENRDDVEGTQAKRRKTEE | ||||||
Sequence conflict | 331 | in Ref. 2; AAI08067 | ||||
Sequence: E → Q | ||||||
Sequence conflict | 340 | in Ref. 2; AAI08067 | ||||
Sequence: L → Q | ||||||
Sequence conflict | 475 | in Ref. 2; AAI08067 | ||||
Sequence: T → A | ||||||
Sequence conflict | 497 | in Ref. 2; AAI08067 | ||||
Sequence: Q → H | ||||||
Compositional bias | 498-514 | Acidic residues | ||||
Sequence: EVEEEEEDEDEEVPDEL |
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
BX284619 EMBL· GenBank· DDBJ | - | Genomic DNA | No translation available. | |
BC108066 EMBL· GenBank· DDBJ | AAI08067.1 EMBL· GenBank· DDBJ | mRNA |