ID F8R4R3_9CAUD Unreviewed; 576 AA.
AC F8R4R3;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 24-JAN-2024, entry version 47.
DE RecName: Full=DNA helicase/primase {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000256|HAMAP-Rule:MF_04154};
DE EC=3.6.4.12 {ECO:0000256|HAMAP-Rule:MF_04154};
OS Escherichia phage K30.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Studiervirinae; Przondovirus; Przondovirus K30.
OX NCBI_TaxID=1041524 {ECO:0000313|EMBL:AEH41032.1, ECO:0000313|Proteomes:UP000000489};
RN [1] {ECO:0000313|EMBL:AEH41032.1, ECO:0000313|Proteomes:UP000000489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Bouwman C.W., Kropinski A.M., Whitfield C.;
RL Submitted (JUN-2010) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|HAMAP-Rule:MF_04154}.
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 Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_04154};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000256|HAMAP-
CC Rule:MF_04154};
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. {ECO:0000256|HAMAP-Rule:MF_04154}.
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. {ECO:0000256|HAMAP-
CC Rule:MF_04154}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000256|HAMAP-Rule:MF_04154}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_04154}.
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DR EMBL; HM480846; AEH41032.1; -; Genomic_DNA.
DR RefSeq; YP_004678739.1; NC_015719.1.
DR GeneID; 10894505; -.
DR KEGG; vg:10894505; -.
DR OrthoDB; 615at10239; -.
DR Proteomes; UP000000489; Genome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-UniRule.
DR CDD; cd19483; RecA-like_Gp4D_helicase; 1.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 2.20.25.10; -; 1.
DR Gene3D; 2.20.25.180; -; 1.
DR Gene3D; 3.40.1360.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_04154; Helic_Prim_T7; 1.
DR InterPro; IPR007694; DNA_helicase_DnaB-like_C.
DR InterPro; IPR048774; Helic-prim_T7_N.
DR InterPro; IPR046394; Helic_Prim_T7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; T7-LIKE MITOCHONDRIAL DNA HELICASE; 1.
DR PANTHER; PTHR12873:SF0; TWINKLE PROTEIN, MITOCHONDRIAL; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF21268; Helic-prim_T7_N; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF57783; Zinc beta-ribbon; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Helicase {ECO:0000256|HAMAP-Rule:MF_04154, ECO:0000313|EMBL:AEH41032.1};
KW Hydrolase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Magnesium {ECO:0000256|HAMAP-Rule:MF_04154};
KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_04154};
KW Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_04154};
KW Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_04154,
KW ECO:0000313|EMBL:AEH41032.1};
KW Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Reference proteome {ECO:0000313|Proteomes:UP000000489};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04154};
KW Viral DNA replication {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc {ECO:0000256|HAMAP-Rule:MF_04154};
KW Zinc-finger {ECO:0000256|HAMAP-Rule:MF_04154}.
FT DOMAIN 159..246
FT /note="Toprim"
FT /evidence="ECO:0000259|PROSITE:PS50880"
FT DOMAIN 289..558
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT ZN_FING 21..43
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT REGION 553..576
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 21
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 24
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 40
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 43
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 165
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 215
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 245
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 320..327
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 369
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 474
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 513
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 531
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 545
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 576 AA; 63362 MW; 2874B1F9DA5CC113 CRC64;
MSYGDSQEDG QESIFLFHAP CENCGSSDGN SVYSDAHEYC FVCQHRVPGS EERTEKLSAR
RPKGGNYGMN TQGSGLLVFG ESDGRYTDLT ARGISKATCQ KAGYWVAKVS GTAYQVADYR
DQNGSIVSQK LRDKEKNFST RGSHKGDALF GKHLWNGGKK IVITEGEIDM LTVMQLQDCK
WPVVSLGHGA SAAKKTCSAN YEYFDSFDQI ILMFDMDEPG RAAVEEAAQV LPPGKVHVAV
LTEKDANECL LKGKGKEVLD QIWNAAPWVP DGVIGAMSMK DRVREAMTSE QSVGYLFSGC
PGLNDRTLGA RGGEVIMVTS GSGMGKSTFV RQQALGFARG QGLKVGMAML EESVEETMED
VLGIANGIRL RQQPREFKQK LIEDGTYDKW FDELYGTDQF HLYDSFAEAE VDRLLAKLHY
MRTGLNCDVI ILDHISIVVS ASEESDERKM IDRLMTKLKG FAKSTGVVLI VICHLKNPEK
GKAHEEGRAV SITDLRGSGS LRQLSDTIIA LERNQQGDMP NLVLLRILKC RFNGIGVGIA
GYMEYNEKTG LLEPSNYTGG EGEGDTGWEG HEEDDY
//