A0A2U8QP26 · A0A2U8QP26_9CAUD
- ProteinDNA-directed DNA polymerase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids903 (go to sequence)
- Protein existenceInferred from homology
- Annotation score3/5
Function
function
Replicates the viral genomic DNA. This polymerase possesses two enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic activity that degrades single-stranded DNA in the 3'- to 5'-direction for proofreading purpose.
Catalytic activity
- a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) = diphosphate + DNA(n+1)
Cofactor
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 114 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for 3'-5' exonuclease activity | ||||
Sequence: D | ||||||
Binding site | 116 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for 3'-5' exonuclease activity | ||||
Sequence: E | ||||||
Binding site | 222 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for 3'-5' exonuclease activity | ||||
Sequence: D | ||||||
Binding site | 327 | Mg2+ 1 (UniProtKB | ChEBI); catalytic; for 3'-5' exonuclease activity | ||||
Sequence: D | ||||||
Binding site | 327 | Mg2+ 2 (UniProtKB | ChEBI); catalytic; for 3'-5' exonuclease activity | ||||
Sequence: D | ||||||
Binding site | 411 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for polymerase activity | ||||
Sequence: D | ||||||
Binding site | 411 | Mg2+ 4 (UniProtKB | ChEBI); catalytic; for polymerase activity | ||||
Sequence: D | ||||||
Binding site | 412 | Mg2+ 4 (UniProtKB | ChEBI); catalytic; for polymerase activity | ||||
Sequence: L | ||||||
Binding site | 414-416 | substrate | ||||
Sequence: SLY | ||||||
Binding site | 482 | substrate | ||||
Sequence: R | ||||||
Binding site | 560 | substrate | ||||
Sequence: K | ||||||
Site | 621 | Optimization of metal coordination by the polymerase active site | ||||
Sequence: D | ||||||
Binding site | 623 | Mg2+ 4 (UniProtKB | ChEBI); catalytic; for polymerase activity | ||||
Sequence: D | ||||||
Binding site | 623 | Mg2+ 3 (UniProtKB | ChEBI); catalytic; for polymerase activity | ||||
Sequence: D | ||||||
Site | 706 | Optimization of metal coordination by the polymerase active site | ||||
Sequence: K | ||||||
Site | 714 | Essential for viral replication | ||||
Sequence: D |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | 3'-5' exonuclease activity | |
Molecular Function | DNA binding | |
Molecular Function | DNA-directed DNA polymerase activity | |
Molecular Function | metal ion binding | |
Molecular Function | nucleotide binding | |
Biological Process | bidirectional double-stranded viral DNA replication | |
Biological Process | DNA replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA-directed DNA polymerase
- EC number
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Straboviridae > Tevenvirinae > Mosigvirus > Mosigvirus mar005p1
Accessions
- Primary accessionA0A2U8QP26
Proteomes
Interaction
Subunit
Part of the replicase complex that includes the DNA polymerase, the polymerase clamp, the clamp loader complex, the single-stranded DNA binding protein, and the primase/helicase. Interacts with the polymerase clamp; this interaction constitutes the polymerase holoenzyme.
Structure
Family & Domains
Features
Showing features for domain, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 106-293 | DNA-directed DNA polymerase family B exonuclease | ||||
Sequence: TKIRVANFDIEVTSPDGFPEPSQAKHPIDAITHYDSIDDRFYVFDLLNSPYGNVEEWSIEIAAKLQEQGGDEVPSEIIDKIVYMPFDNEKELLMEYLNFWQQKTPVILTGWNVESFDIPYVYNRIKNIFGESTAKRLSPHRKTRVKVIENMYGSREIITLFGISVLDYIDLYKKFSFTNQPSYSLDYI | ||||||
Region | 248-264 | Beta hairpin | ||||
Sequence: TRVKVIENMYGSREIIT | ||||||
Domain | 368-494 | DNA-directed DNA polymerase family B multifunctional | ||||
Sequence: IIFNSLKEQNKVIPQGRSHPVQPYPGAFVKEPIPNRYKYVMSFDLTSLYPSIIRQVNISPETIAGTFKVAPLHDYINAIAERPSDVYSCSPNGMMYYKDRDGVVPTEITKVFNQRKEHKGYMLAAQR | ||||||
Region | 380-903 | Polymerase | ||||
Sequence: IPQGRSHPVQPYPGAFVKEPIPNRYKYVMSFDLTSLYPSIIRQVNISPETIAGTFKVAPLHDYINAIAERPSDVYSCSPNGMMYYKDRDGVVPTEITKVFNQRKEHKGYMLAAQRNCEIIKEALHNPNLSVDEPLDVDYRFDFSDEIKEKIKKLSAKSLNEMLFRAQRTEVAGMTAQINRKLLINSLYGALGNVWFRYYDLRNATAITTFGQMALQWIERKVNEYLNEVCGTEGEAFVLYGDTDSIYVSADKIIDKVGESKFRDTNHWVDFLDKFARERMEPAIDKGFREMCEYMNNKQHLMFMDREAIAGPPLGSKGIGGFWTGKKRYALNVWDMEGTRYAEPKLKIMGLETQKSSTPKAVQKALKECIRRMLQEGEESLQEYFKEFEKEFRQLNYISIASVSSANNIAKYDVGGFPGPKCPFHIRGILTYNRAIKGNIDAPQVVEGEKVYVLPLREGNPFGDKCIAWPSGTEITDLIKDDVLHWMDYTVLLEKTFIKPLEGFTSAAKLDYEKKASLFDMFDF | ||||||
Domain | 555-629 | DNA-directed DNA polymerase family B multifunctional | ||||
Sequence: AQINRKLLINSLYGALGNVWFRYYDLRNATAITTFGQMALQWIERKVNEYLNEVCGTEGEAFVLYGDTDSIYVSA | ||||||
Region | 705-708 | Binding of DNA in B-conformation | ||||
Sequence: KKRY | ||||||
Region | 897-903 | Interaction with the polymerase clamp | ||||
Sequence: LFDMFDF |
Domain
The N-terminus contains the 3'-5' exonuclease activity. The C-terminus contains the polymerase activity and is involved in binding to the polymerase clamp protein. A beta hairpin structure is necessary for the proofreading function of the polymerase.
Sequence similarities
Belongs to the DNA polymerase type-B family.
Family and domain databases
Sequence
- Sequence statusComplete
- Length903
- Mass (Da)104,631
- Last updated2018-09-12 v1
- Checksum3D9E479EB9FF47D2