HAMAP rule MF_04154
General rule information
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Accession | MF_04154 |
Dates | 8-FEB-2021 (Created)
19-NOV-2022 (Last updated, Version 6) |
Name | Helic_Prim_T7 |
Scope(s) |
Viruses |
Template(s) | P03692 (HELIC_BPT7); [ Recover all ] |
Triggered by |
HAMAP; MF_04154 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | HELIC |
RecName: Full=DNA helicase/primase;<br /> EC=<a href="https://enzyme.expasy.org/EC/2.7.7.-">2.7.7.-</a>;<br /> EC=<a href="https://enzyme.expasy.org/EC/3.6.4.12">3.6.4.12</a>; | |
case <OC:Teseptimavirus> | |
Protein name | AltName: Full=Gene product 4; Short=Gp4; |
Gene name | Name=4; |
end case |
Comments
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case <OC:Teseptimavirus> | |
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. |
else | |
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 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. |
end case | |
CATALYTIC ACTIVITY | Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; |
COFACTOR | Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Note=Binds 2 Mg(2+), one of which is catalytic.; |
case <OC:Teseptimavirus> | |
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. |
else | |
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, the primase/helicase and the single-stranded DNA binding protein. |
end case | |
case <FTGroup:1> and <FTGroup:2> | |
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 Mg(2+)-dTTP. |
else case <FTGroup:2> and not <FTGroup:1> | |
DOMAIN | The central core domain contains the primase activity. The C- terminus is responsible for the helicase activity. |
end case | |
SIMILARITY | Belongs to the Teseptimavirus DNA helicase/primase family. |
Keywords
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ATP-binding | |
Viral DNA replication | |
<a href="https://www.uniprot.org/keywords/KW-0347">Helicase</a> | |
Hydrolase | |
Nucleotidyltransferase | |
Primosome | |
Metal-binding | |
Multifunctional enzyme | |
Transferase | |
Zinc-finger | |
Zinc | |
case <FTGroup:2> | |
Magnesium | |
end case |
Gene Ontology
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GO:0003896; Molecular function:DNA primase activity | |
case <FTGroup:1> | |
GO:0008270; Molecular function:zinc ion binding | |
end case | |
GO:0005524; Molecular function:ATP binding | |
GO:0003678; Molecular function:DNA helicase activity | |
GO:0039693; Biological process:viral DNA genome replication | |
GO:0016740; Molecular function:transferase activity |
Cross-references
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PROSITE | PS50880; TOPRIM; 1; |
PROSITE | PS51199; SF4_HELICASE; 1; |
Pfam | PF03796; DnaB_C; 1; |
Pfam | PF08273; Prim_Zn_Ribbon; 0-1; |
Features
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From: HELIC_BPT7 (P03692) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
ZN_FING | 17 | 39 | /note="C4-like; zinc ribbon fold" | C-x(2,4)-C-x(15,21)-C-x(2)-C | ||||||||
BINDING | 312 | 319 | /ligand="ATP" /ligand_id="ChEBI:CHEBI:30616" |
[AS]-G-[ST]-G-x-G-K-[ST] | ||||||||
REGION | 550 | 566 | /note="Binding to viral DNA polymerase" | |||||||||
BINDING | 17 | 17 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 20 | 20 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 36 | 36 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 39 | 39 | /ligand="Zn(2+)" /ligand_id="ChEBI:CHEBI:29105" |
C | 1 | |||||||
BINDING | 157 | 157 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
E | 2 | |||||||
BINDING | 207 | 207 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="1" /ligand_note="catalytic" |
D | 2 | |||||||
BINDING | 237 | 237 | /ligand="Mg(2+)" /ligand_id="ChEBI:CHEBI:18420" /ligand_label="2" |
D | ||||||||
SITE | 361 | 361 | /note="dTTP/dATP binding" | R | ||||||||
SITE | 465 | 465 | /note="dTTP/dATP binding" | H | ||||||||
SITE | 504 | 504 | /note="dTTP/dATP binding" | R | ||||||||
SITE | 522 | 522 | /note="dTTP/dATP binding" | R | ||||||||
SITE | 535 | 535 | /note="dTTP/dATP binding" | Y |
Additional information
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Size range | 460-650 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |