ID W8FTA2_9CAUD Unreviewed; 575 AA.
AC W8FTA2;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 30.
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};
GN ORFNames=CHOED_042 {ECO:0000313|EMBL:AHK11902.1};
OS Vibrio phage CHOED.
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes.
OX NCBI_TaxID=1458716 {ECO:0000313|EMBL:AHK11902.1, ECO:0000313|Proteomes:UP000019496};
RN [1] {ECO:0000313|EMBL:AHK11902.1, ECO:0000313|Proteomes:UP000019496}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Romero J., Gajardo F., Higuera G., Castillo D., Middleboe M., Garcia K.,
RA Ramirez C., Espejo R.;
RT "Complete genome sequence of Vibrio anguillarum bacteriophage CHOED of the
RT family Podoviridae, successfully used for phage therapy in aquaculture.";
RL Submitted (JUN-2014) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KJ192399; AHK11902.1; -; Genomic_DNA.
DR RefSeq; YP_009021708.1; NC_023863.2.
DR GeneID; 18938578; -.
DR KEGG; vg:18938578; -.
DR OrthoDB; 615at10239; -.
DR Proteomes; UP000019496; 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: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 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; 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 Primosome {ECO:0000256|HAMAP-Rule:MF_04154};
KW Reference proteome {ECO:0000313|Proteomes:UP000019496};
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 295..563
FT /note="SF4 helicase"
FT /evidence="ECO:0000259|PROSITE:PS51199"
FT BINDING 173
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 223
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 255
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT BINDING 326..333
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 477
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 516
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 537
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT SITE 550
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ SEQUENCE 575 AA; 64548 MW; 59F0740E7E561BE5 CRC64;
MSEPIILRKQ PHWDDPRVHN PESCCSSDAV SVYADGSACC YSCGAQLFPH PSKFNYFDLM
DGKEMPQYQS RESTMNNSAS SFDIELRMYE KALFKGFPDR NISIQTAQKF GVKTDTNGNV
YFPYYNRDNH LCGFKIRTPA KDFRVVGKVV GDDVMLFGQQ LFKGGGKYAT IHEGEFDALA
GYQMMGSKFP HMSIPTGSKG AKKACQFNLD YLETYERKVL SLDGDKPGRE AADAVAPLFT
PGTCQVITHP EDRKDACEYS KANMGAVYYN MFWDSKIYTP SGIVNLGDNF EALFDRKARM
SHPYPWEGLN KKTRGFRKKE LVTLCSGSGM GKSAITRELS YHLLKTTEDN IGVLYLEEDQ
ERTKLGIMGM HAKKLLHLDD VFEGCSRDEI KEAFDATVGT GRFYAFDHFG SCGVEEILNR
VRYLIKGLEC EWIILDHLSI IVSGLDGEDE RKNIDIAMTK LRTLVEETGA GMFLVSHLKR
VGGDKGHEDG AQISLSHLRG SQSIAQLSDI VIGLERNQQH SNPLVANTTK LRVLKNRYTG
EVGEAGFLLY DRDTGRMSEV TESDLEFGDD DEDEF
//
