ID A0A482IF05_9CAUD Unreviewed; 476 AA.
AC A0A482IF05;
DT 05-JUN-2019, integrated into UniProtKB/TrEMBL.
DT 05-JUN-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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 Synechococcus phage S-B28.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Autographiviridae; Qadamvirus; Qadamvirus SB28.
OX NCBI_TaxID=2545435 {ECO:0000313|EMBL:QBP05834.1, ECO:0000313|Proteomes:UP000295590};
RN [1] {ECO:0000313|EMBL:QBP05834.1, ECO:0000313|Proteomes:UP000295590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Liu X.;
RT "Isolation and Genetic Analysis of a Novel Cyanophage S-LB68 from the Huang
RT Bohai.";
RL Submitted (OCT-2018) 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 central core domain contains the primase activity. The C-
CC terminus is responsible for the helicase activity. {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; MK016662; QBP05834.1; -; Genomic_DNA.
DR Proteomes; UP000295590; 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:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003896; F:DNA primase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
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; 2.20.25.180; -; 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; IPR046394; Helic_Prim_T7.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; T7-LIKE MITOCHONDRIAL DNA HELICASE; 1.
DR PANTHER; PTHR12873:SF0; TWINKLE MTDNA HELICASE; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF13155; Toprim_2; 1.
DR SUPFAM; SSF56731; DNA primase core; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR PROSITE; PS51199; SF4_HELICASE; 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};
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 Nucleotidyltransferase {ECO:0000256|HAMAP-Rule:MF_04154,
KW ECO:0000313|EMBL:QBP05834.1}; Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Reference proteome {ECO:0000313|Proteomes:UP000295590};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_04154, ECO:0000313|EMBL:QBP05834.1};
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 207..467
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT BINDING 86
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 135
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 167
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 238..245
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 383
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 422
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 441
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 454
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 476 AA; 52845 MW; 5F9E8B5BDA65B1DB CRC64;
MKSNAQLKGS AVRLQKRNLS ESTLEKYKIY RDGNVLRFHY FSNEGVLLGA KIKTKDKNFS
FEGNNDGSFF GQHLFPTTGK RVVITEGELD AASCYEAMPG WPMVSLPSGA AAARKAIQRN
LQWLQGYEEI VLFFDNDEAG RKATEEACQV LPPGKVHIAL LQGDYKDASD ALSANDPEAI
RRAIWDARPY RPDGIVEGKS LLELVTTPTP PSNYDYPYQG LQQLLHGIRY GELVTITAGS
GIGKSSFCRE LATSLLQNGA RVGYLALEES NRRTALGLMS VAVGKSLHIG EHTHKELIEA
FDNSISKWNL YLFDGFGSFD PDVIYNRIEY LASGLDCKII FLDHLSILLS GLDGDERRMI
DTTMTKLRSL VERTGISLFL VSHLRRTTSD QNHEEGARVT LGQLRGSAAI AQLSDAVIGL
ERNQQANTDG NSTTVRVLKN RYSGEVGIAC KLQYDLDTCK FKEHEPEQEF NPSTDF
//
