AC MF_04154; DC Protein; auto TR HAMAP; MF_04154; -; 1; level=0 XX Names: Helic_Prim_T7 XX ID HELIC DE RecName: Full=DNA helicase/primase; DE EC=2.7.7.-; DE EC=3.6.4.12; case DE AltName: Full=Gene product 4; DE Short=Gp4; GN Name=4; end case XX case CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral CC DNA replication and recombination. The helicase moves 5' -> 3' on the CC lagging strand template, unwinding the DNA duplex ahead of the leading CC strand polymerase at the replication fork and generating ssDNA for both CC leading and lagging strand synthesis. ATP or dTTP hydrolysis propels CC each helicase domain to translocate 2 nt per step sequentially along CC DNA. Mediates strand transfer when a joint molecule is available and CC participates in recombinational DNA repair through its role in strand CC exchange. Primase activity synthesizes short RNA primers at the CC sequence 5'-GTC-3' on the lagging strand that the polymerase elongates CC using dNTPs and providing the primase is still present. else CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral CC DNA replication and recombination. The helicase moves 5' -> 3' on the CC lagging strand template, unwinding the DNA duplex ahead of the leading CC strand polymerase at the replication fork and generating ssDNA for both CC leading and lagging strand synthesis. ATP or dTTP hydrolysis propels CC each helicase domain to translocate sequentially along DNA. Mediates CC strand transfer when a joint molecule is available and participates in CC recombinational DNA repair through its role in strand exchange. Primase CC activity synthesizes short RNA primers at the sequence 5'-GTC-3' on the CC lagging strand that the polymerase elongates using dNTPs and providing CC the primase is still present. end case CC -!- CATALYTIC ACTIVITY: CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Note=Binds 2 Mg(2+), one of which is catalytic.; case CC -!- SUBUNIT: Homohexamer. Assembles as a hexamer onto linear or circular CC ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with CC the viral DNA polymerase that is bound to DNA; this interaction is CC essential to initiate leading-strand DNA synthesis. The priming complex CC consists of 2 DNA polymerases and 1 helicase-primase hexamer that CC assemble on the DNA template. Interacts with the single-stranded DNA- CC binding protein. Part of the replicase complex that includes the DNA CC polymerase, thioredoxin, the primase/helicase and the single-stranded CC DNA binding protein. else CC -!- SUBUNIT: Homohexamer. Assembles as a hexamer onto linear or circular CC ssDNA in the presence of ATP or dTTP. Interacts (via C-terminus) with CC the viral DNA polymerase that is bound to DNA; this interaction is CC essential to initiate leading-strand DNA synthesis. The priming complex CC consists of 2 DNA polymerases and 1 helicase-primase hexamer that CC assemble on the DNA template. Interacts with the single-stranded DNA- CC binding protein. Part of the replicase complex that includes the DNA CC polymerase, the primase/helicase and the single-stranded DNA binding CC protein. end case case and CC -!- DOMAIN: The N-terminus zinc finger domain is essential for delivering CC the primed DNA template to the DNA polymerase. The central core domain CC contains the primase activity. The C-terminus region is responsible for CC the helicase activity and binds 1 Mg(2+)-dTTP. else case and not CC -!- DOMAIN: The central core domain contains the primase activity. The C- CC terminus is responsible for the helicase activity. end case CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family. XX DR PROSITE; PS50880; TOPRIM; 1; trigger=no DR PROSITE; PS51199; SF4_HELICASE; 1; trigger=yes DR Pfam; PF03796; DnaB_C; 1; trigger=no DR Pfam; PF08273; Prim_Zn_Ribbon; 0-1; trigger=no XX KW ATP-binding KW Viral DNA replication KW Helicase KW Hydrolase KW Nucleotidyltransferase KW Primosome KW Metal-binding KW Multifunctional enzyme KW Transferase KW Zinc-finger KW Zinc case KW Magnesium end case XX GO GO:0003896; F:DNA primase activity case GO GO:0008270; F:zinc ion binding end case GO GO:0005524; F:ATP binding GO GO:0003678; F:DNA helicase activity GO GO:0039693; P:viral DNA genome replication GO GO:0016740; F:transferase activity XX FT From: HELIC_BPT7 (P03692) FT ZN_FING 17..39 FT /note="C4-like; zinc ribbon fold" FT Condition: C-x(2,4)-C-x(15,21)-C-x(2)-C FT BINDING 312..319 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT Condition: [AS]-G-[ST]-G-x-G-K-[ST] FT REGION 550..566 FT /note="Binding to viral DNA polymerase" FT BINDING 17 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 20 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 36 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 39 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT Group: 1; Condition: C FT BINDING 157 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT Group: 2; Condition: E FT BINDING 207 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="1" FT /ligand_note="catalytic" FT Group: 2; Condition: D FT BINDING 237 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /ligand_label="2" FT Condition: D FT SITE 361 FT /note="dTTP/dATP binding" FT Condition: R FT SITE 465 FT /note="dTTP/dATP binding" FT Condition: H FT SITE 504 FT /note="dTTP/dATP binding" FT Condition: R FT SITE 522 FT /note="dTTP/dATP binding" FT Condition: R FT SITE 535 FT /note="dTTP/dATP binding" FT Condition: Y XX Size: 460-650; Related: None; Template: P03692; Scope: Viruses Fusion: Nter: None Cter: None Duplicate: None Plasmid: None Comments: None XX # Revision 1.6 2022/11/19 //