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HAMAP rule MF_04154

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General rule information [?]

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 [?]

Identifier, protein and gene names [?]

Identifier HELIC
RecName: Full=DNA helicase/primase;<br /> &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;EC=<a href="https://enzyme.expasy.org/EC/2.7.7.-">2.7.7.-</a>;<br /> &nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;&nbsp;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 [?]

case <OC:Teseptimavirus>
FUNCTIONATP-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
FUNCTIONATP-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>
SUBUNITHomohexamer. 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
SUBUNITHomohexamer. 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>
DOMAINThe 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>
DOMAINThe central core domain contains the primase activity. The C- terminus is responsible for the helicase activity.
end case
SIMILARITYBelongs to the Teseptimavirus DNA helicase/primase family.

Keywords [?]

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 [?]

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 [?]

PROSITE PS50880; TOPRIM; 1;
PROSITE PS51199; SF4_HELICASE; 1;
Pfam PF03796; DnaB_C; 1;
Pfam PF08273; Prim_Zn_Ribbon; 0-1;

Features [?]

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 [?]

Size range 460-650 amino acids
Related rules None
Fusion Nter: None Cter: None



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