A0A8X8M4V4 · A0A8X8M4V4_9CAUD
- ProteinDNA helicase/primase
- Gene4
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids566 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
Function
function
ATP-dependent DNA helicase and primase essential for viral DNA replication and recombination. The helicase moves 5' -> 3' on the lagging strand template, unwinding the DNA duplex ahead of the leading strand polymerase at the replication fork and generating ssDNA for both leading and lagging strand synthesis. ATP or dTTP hydrolysis propels each helicase domain to translocate 2 nt per step sequentially along DNA. Mediates strand transfer when a joint molecule is available and participates in recombinational DNA repair through its role in strand exchange. Primase activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the lagging strand that the polymerase elongates using dNTPs and providing the primase is still present.
Catalytic activity
- ATP + H2O = ADP + H+ + phosphate
Cofactor
Note: Binds 2 Mg2+, one of which is catalytic.
Features
Showing features for binding site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 15 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 18 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 34 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 37 | Zn2+ (UniProtKB | ChEBI) | ||||
Sequence: C | ||||||
Binding site | 157 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: E | ||||||
Binding site | 207 | Mg2+ 1 (UniProtKB | ChEBI); catalytic | ||||
Sequence: D | ||||||
Binding site | 237 | Mg2+ 2 (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 312-319 | ATP (UniProtKB | ChEBI) | ||||
Sequence: SGSGMGKS | ||||||
Site | 361 | dTTP/dATP binding | ||||
Sequence: R | ||||||
Site | 465 | dTTP/dATP binding | ||||
Sequence: H | ||||||
Site | 504 | dTTP/dATP binding | ||||
Sequence: R | ||||||
Site | 522 | dTTP/dATP binding | ||||
Sequence: R | ||||||
Site | 535 | dTTP/dATP binding | ||||
Sequence: Y |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | primosome complex | |
Molecular Function | 5'-3' DNA helicase activity | |
Molecular Function | ATP binding | |
Molecular Function | DNA primase activity | |
Molecular Function | hydrolase activity | |
Molecular Function | single-stranded DNA binding | |
Molecular Function | zinc ion binding | |
Biological Process | viral DNA genome replication |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended nameDNA helicase/primase
- EC number
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageViruses > Duplodnaviria > Heunggongvirae > Uroviricota > Caudoviricetes > Autographiviridae > Studiervirinae > Teseptimavirus
Accessions
- Primary accessionA0A8X8M4V4
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
Keywords
- Cellular component
Interaction
Subunit
Homohexamer. Assembles as a hexamer onto linear or circular ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with the viral DNA polymerase that is bound to DNA; this interaction is essential to initiate leading-strand DNA synthesis. The priming complex consists of 2 DNA polymerases and 1 helicase-primase hexamer that assemble on the DNA template. Interacts with the single-stranded DNA-binding protein. Part of the replicase complex that includes the DNA polymerase, thioredoxin, the primase/helicase and the single-stranded DNA binding protein.
Structure
Family & Domains
Features
Showing features for zinc finger, domain, region, compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Zinc finger | 15-37 | C4-like; zinc ribbon fold | ||||
Sequence: CENCGSSDGNSVYSDGHQFCFVC | ||||||
Domain | 151-238 | Toprim | ||||
Sequence: KKIVVTEGEIDMLTVMELQDCKYPVVSLGHGASAAKKTCAANYEYFDQFEQIILMFDMDEAGRKAVEEAAQVLPAGKVRVAVLPCKDA | ||||||
Domain | 281-548 | SF4 helicase | ||||
Sequence: SEESVGLLFSGCSGINDKTLGARGGEVIMVTSGSGMGKSTFVRQQALQWGTAMGKKVGLAMLEESVEETAEDLIGLHNRVRLRQSDSLKREIIENGKFDQWFDELFGNDTFHLYDSFAEAETDRLLAKLAYMRSGLGCDVIILDHISIVVSASGESDERKMIDNLMTKLKGFAKSTGVVLVVICHLKNPDKGKAHEEGRPVSITDLRGSGALRQLSDTIIALERNQQGDMPNLVLVRILKCRFTGDTGIAGYMEYNKETGWLEPSSYS | ||||||
Region | 543-566 | Disordered | ||||
Sequence: EPSSYSGEEESHSESTDWSKDTDF | ||||||
Compositional bias | 549-566 | Basic and acidic residues | ||||
Sequence: GEEESHSESTDWSKDTDF | ||||||
Region | 550-566 | Binding to viral DNA polymerase | ||||
Sequence: EEESHSESTDWSKDTDF |
Domain
The N-terminus zinc finger domain is essential for delivering the primed DNA template to the DNA polymerase. The central core domain contains the primase activity. The C-terminus region is responsible for the helicase activity and binds 1 Mg2+-dTTP.
Sequence similarities
Belongs to the Teseptimavirus DNA helicase/primase family.
Keywords
- Domain
Family and domain databases
Sequence
- Sequence statusComplete
- Length566
- Mass (Da)62,786
- Last updated2022-12-14 v1
- Checksum5A8372A019D639CD
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 549-566 | Basic and acidic residues | ||||
Sequence: GEEESHSESTDWSKDTDF |
Keywords
- Technical term