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Database: UniProt
Entry: F8R4R3_9CAUD
LinkDB: F8R4R3_9CAUD
Original site: F8R4R3_9CAUD 
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
//
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