P19894 · DPOL_BPM2
- ProteinDNA polymerase
- GeneG
- StatusUniProtKB reviewed (Swiss-Prot)
- Amino acids572 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
Polymerase responsible for protein-primed viral DNA replication by strand displacement with high processivity and fidelity. To start replication, the DNA polymerase forms a heterodimer with a free primer terminal protein (TP), recognizes the replication origins at both 5' ends of the linear chromosome, and initiates replication using as primer the OH-group of Ser-232 of the TP. This polymerase possesses three enzymatic activities: DNA synthesis (polymerase), primer terminal protein (TP) deoxynucleotidylation, which is the formation of a covalent linkage (phosphoester) between the hydroxyl group of a specific serine residue in TP and 5'-dAMP, a reaction directed by the second T at the 3' end, and 3' to 5' exonuclease activity. Exonuclease activity has a proofreading purpose.
Miscellaneous
This DNA polymerase requires a protein as a primer.
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
Features
Showing features for site, binding site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Site | 9 | Essential for 3'-5' exonucleolysis | ||||
Sequence: D | ||||||
Site | 11 | Essential for 3'-5' exonucleolysis | ||||
Sequence: E | ||||||
Site | 62 | Essential for 3'-5' exonucleolysis | ||||
Sequence: F | ||||||
Site | 90 | Involved in binding template-primer structures | ||||
Sequence: I | ||||||
Site | 119 | Critical for 3'-5' exonucleolysis | ||||
Sequence: S | ||||||
Site | 119 | Essential for 3'-5' exonucleolysis | ||||
Sequence: S | ||||||
Site | 120 | Essential for 3'-5' exonucleolysis | ||||
Sequence: L | ||||||
Binding site | 142 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 166 | Mg2+ 1 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 246 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 247 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: V | ||||||
Site | 249 | Probably involved in binding template-primer structures | ||||
Sequence: S | ||||||
Binding site | 251 | TTP (UniProtKB | ChEBI) | ||||
Sequence: Y | ||||||
Site | 251 | Probably involved in nucleotide binding selection | ||||
Sequence: Y | ||||||
Binding site | 368 | TTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 380 | TTP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Site | 380 | Probably involved in nucleotide binding selection | ||||
Sequence: K | ||||||
Site | 384 | Probably involved in binding template-primer structures | ||||
Sequence: N | ||||||
Site | 387 | Probably involved in nucleotide binding selection | ||||
Sequence: Y | ||||||
Site | 388 | Probably involved in binding template-primer structures | ||||
Sequence: G | ||||||
Site | 431 | Probably involved in binding template-primer structures | ||||
Sequence: T | ||||||
Site | 435 | Probably involved in binding template-primer structures | ||||
Sequence: R | ||||||
Binding site | 453 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 455 | Mg2+ 2 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 455 | TTP (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Site | 495 | Probably involved in binding template-primer structures | ||||
Sequence: K | ||||||
Site | 497 | Probably involved in binding template-primer structures | ||||
Sequence: Y | ||||||
Site | 526 | Stabilizes the primer-terminus at the polymerization active site and contributes to the coordination between the exonuclease and polymerazation activities | ||||
Sequence: K |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | DNA binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | exonuclease activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleoside binding | |
Molecular Function | nucleotide binding | |
Biological Process | DNA replication | |
Biological Process | viral DNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA polymerase
- EC number
- Alternative names
Gene names
Organism names
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Salasmaviridae > Picovirinae > Salasvirus
- Virus hosts
Accessions
- Primary accessionP19894
Phenotypes & Variants
Features
Showing features for natural variant.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Natural variant | 192 | in mutant APH2 | ||||
Sequence: L → F |
Variants
We now provide the "Disease & Variants" viewer in its own tab.
The viewer provides 1 variant from UniProt as well as other sources including ClinVar and dbSNP.
PTM/Processing
Features
Showing features for chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_0000046544 | 1-572 | DNA polymerase | |||
Sequence: MSRKMFSCDFETTTKLDDCRVWAYGYMEIGNLDNYKIGNSLDEFMQWVMEIQADLYFHNLKFDGAFIVNWLEQHGFKWSNEGLPNTYNTIISKMGQWYMIDICFGYKGKRKLHTVIYDSLKKLPFPVKKIAKDFQLPLLKGDIDYHTERPVGHEITPEEYEYIKNDIEIIARALDIQFKQGLDRMTAGSDSLKGFKDILSTKKFNKVFPKLSLPMDKEIRKAYRGGFTWLNDKYKEKEIGEGMVFDVNSLYPSQMYSRPLPYGAPIVFQGKYEKDEQYPLYIQRIRFEFELKEGYIPTIQIKKNPFFKGNEYLKNSGVEPVELYLTNVDLELIQEHYELYNVEYIDGFKFREKTGLFKDFIDKWTYVKTHEEGAKKQLAKLMLNSLYGKFASNPDVTGKVPYLKDDGSLGFRVGDEEYKDPVYTPMGVFITAWARFTTITAAQACYDRIIYCDTDSIHLTGTEVPEIIKDIVDPKKLGYWAHESTFKRAKYLRQKTYIQDIYVKEVDGKLKECSPDEATTTKFSVKCAGMTDTIKKKVTFDNFAVGFSSMGKPKPVQVNGGVVLVDSVFTIK |
Expression
Keywords
- Developmental stage
Interaction
Subunit
Interacts with the primer terminal protein; this interaction allows the initiation of TP-primed DNA replication at both viral DNA ends. Interacts with DNA.
Family & Domains
Features
Showing features for region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-222 | 3'-5' exonuclease and strand displacement activities | ||||
Sequence: MSRKMFSCDFETTTKLDDCRVWAYGYMEIGNLDNYKIGNSLDEFMQWVMEIQADLYFHNLKFDGAFIVNWLEQHGFKWSNEGLPNTYNTIISKMGQWYMIDICFGYKGKRKLHTVIYDSLKKLPFPVKKIAKDFQLPLLKGDIDYHTERPVGHEITPEEYEYIKNDIEIIARALDIQFKQGLDRMTAGSDSLKGFKDILSTKKFNKVFPKLSLPMDKEIRKA | ||||||
Region | 56-66 | Interaction with the primer terminal protein | ||||
Sequence: YFHNLKFDGAF | ||||||
Region | 223-226 | DNA-binding; Involved in the formation of a stable complex between TP and phi29 DNA polymerase | ||||
Sequence: YRGG | ||||||
Region | 227-572 | Initiation, polymerization and pyrophosphorolytic activities | ||||
Sequence: FTWLNDKYKEKEIGEGMVFDVNSLYPSQMYSRPLPYGAPIVFQGKYEKDEQYPLYIQRIRFEFELKEGYIPTIQIKKNPFFKGNEYLKNSGVEPVELYLTNVDLELIQEHYELYNVEYIDGFKFREKTGLFKDFIDKWTYVKTHEEGAKKQLAKLMLNSLYGKFASNPDVTGKVPYLKDDGSLGFRVGDEEYKDPVYTPMGVFITAWARFTTITAAQACYDRIIYCDTDSIHLTGTEVPEIIKDIVDPKKLGYWAHESTFKRAKYLRQKTYIQDIYVKEVDGKLKECSPDEATTTKFSVKCAGMTDTIKKKVTFDNFAVGFSSMGKPKPVQVNGGVVLVDSVFTIK |
Domain
The N-terminus contains the 3'-5' exonuclease activity and strand displacement ability. The C-terminus contains the protein-primed initiation, DNA polymerization and pyrophosphorolytic activities.
Sequence similarities
Belongs to the DNA polymerase type-B family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length572
- Mass (Da)66,423
- Last updated1991-02-01 v1
- Checksum1E69F27C1632CAC9