HELIC_BPT7
ID HELIC_BPT7 Reviewed; 566 AA.
AC P03692;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=DNA helicase/primase {ECO:0000255|HAMAP-Rule:MF_04154};
DE EC=2.7.7.- {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:2829184};
DE EC=3.6.4.12 {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:2829184, ECO:0000269|PubMed:9185573};
DE AltName: Full=Gene product 4 {ECO:0000255|HAMAP-Rule:MF_04154};
DE Short=Gp4 {ECO:0000255|HAMAP-Rule:MF_04154};
GN OrderedLocusNames=4;
OS Escherichia phage T7 (Bacteriophage T7).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teseptimavirus.
OX NCBI_TaxID=10760;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=6864790; DOI=10.1016/s0022-2836(83)80282-4;
RA Dunn J.J., Studier F.W.;
RT "Complete nucleotide sequence of bacteriophage T7 DNA and the locations of
RT T7 genetic elements.";
RL J. Mol. Biol. 166:477-535(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179, AND ALTERNATIVE INITIATION.
RX PubMed=7310871; DOI=10.1016/0022-2836(81)90178-9;
RA Dunn J.J., Studier F.W.;
RT "Nucleotide sequence from the genetic left end of bacteriophage T7 DNA to
RT the beginning of gene 4.";
RL J. Mol. Biol. 148:303-330(1981).
RN [3]
RP FUNCTION.
RX PubMed=6454135; DOI=10.1073/pnas.78.1.205;
RA Tabor S., Richardson C.C.;
RT "Template recognition sequence for RNA primer synthesis by gene 4 protein
RT of bacteriophage T7.";
RL Proc. Natl. Acad. Sci. U.S.A. 78:205-209(1981).
RN [4]
RP DOMAIN, ALTERNATIVE INITIATION, AND CATALYTIC ACTIVITY.
RX PubMed=2829184; DOI=10.1073/pnas.85.2.396;
RA Bernstein J.A., Richardson C.C.;
RT "A 7-kDa region of the bacteriophage T7 gene 4 protein is required for
RT primase but not for helicase activity.";
RL Proc. Natl. Acad. Sci. U.S.A. 85:396-400(1988).
RN [5]
RP DOMAIN, AND CATALYTIC ACTIVITY.
RX PubMed=9185573; DOI=10.1093/nar/25.13.2620;
RA Bird L.E., Haekansson K., Pan H., Wigley D.B.;
RT "Characterization and crystallization of the helicase domain of
RT bacteriophage T7 gene 4 protein.";
RL Nucleic Acids Res. 25:2620-2626(1997).
RN [6]
RP INTERACTION WITH THE SINGLE-STRANDED DNA-BINDING PROTEIN.
RX PubMed=1634539; DOI=10.1016/s0021-9258(18)42142-4;
RA Kim Y.T., Tabor S., Churchich J.E., Richardson C.C.;
RT "Interactions of gene 2.5 protein and DNA polymerase of bacteriophage T7.";
RL J. Biol. Chem. 267:15032-15040(1992).
RN [7]
RP FUNCTION.
RX PubMed=8617248; DOI=10.1002/j.1460-2075.1996.tb00552.x;
RA Kong D., Richardson C.C.;
RT "Single-stranded DNA binding protein and DNA helicase of bacteriophage T7
RT mediate homologous DNA strand exchange.";
RL EMBO J. 15:2010-2019(1996).
RN [8]
RP FUNCTION.
RX PubMed=9096333; DOI=10.1073/pnas.94.7.2987;
RA Kong D., Griffith J.D., Richardson C.C.;
RT "Gene 4 helicase of bacteriophage T7 mediates strand transfer through
RT pyrimidine dimers, mismatches, and nonhomologous regions.";
RL Proc. Natl. Acad. Sci. U.S.A. 94:2987-2992(1997).
RN [9]
RP FUNCTION.
RX PubMed=9139692; DOI=10.1074/jbc.272.19.12446;
RA Kusakabe T., Richardson C.C.;
RT "Gene 4 DNA primase of bacteriophage T7 mediates the annealing and
RT extension of ribo-oligonucleotides at primase recognition sites.";
RL J. Biol. Chem. 272:12446-12453(1997).
RN [10]
RP DOMAIN.
RX PubMed=10200256; DOI=10.1073/pnas.96.8.4295;
RA Kusakabe T., Hine A.V., Hyberts S.G., Richardson C.C.;
RT "The Cys4 zinc finger of bacteriophage T7 primase in sequence-specific
RT single-stranded DNA recognition.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:4295-4300(1999).
RN [11]
RP SUBUNIT.
RX PubMed=10880454; DOI=10.1093/emboj/19.13.3418;
RA Ahnert P., Picha K.M., Patel S.S.;
RT "A ring-opening mechanism for DNA binding in the central channel of the T7
RT helicase-primase protein.";
RL EMBO J. 19:3418-3427(2000).
RN [12]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=15795374; DOI=10.1073/pnas.0501637102;
RA Hamdan S.M., Marintcheva B., Cook T., Lee S.J., Tabor S., Richardson C.C.;
RT "A unique loop in T7 DNA polymerase mediates the binding of helicase-
RT primase, DNA binding protein, and processivity factor.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:5096-5101(2005).
RN [13]
RP SUBUNIT.
RX PubMed=16777142; DOI=10.1016/j.jmb.2006.05.037;
RA Crampton D.J., Ohi M., Qimron U., Walz T., Richardson C.C.;
RT "Oligomeric states of bacteriophage T7 gene 4 primase/helicase.";
RL J. Mol. Biol. 360:667-677(2006).
RN [14]
RP FUNCTION.
RX PubMed=17604719; DOI=10.1016/j.cell.2007.04.038;
RA Johnson D.S., Bai L., Smith B.Y., Patel S.S., Wang M.D.;
RT "Single-molecule studies reveal dynamics of DNA unwinding by the ring-
RT shaped T7 helicase.";
RL Cell 129:1299-1309(2007).
RN [15]
RP FUNCTION.
RX PubMed=21606333; DOI=10.1073/pnas.1106678108;
RA Zhang H., Lee S.J., Zhu B., Tran N.Q., Tabor S., Richardson C.C.;
RT "Helicase-DNA polymerase interaction is critical to initiate leading-strand
RT DNA synthesis.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:9372-9377(2011).
RN [16]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE, IDENTIFICATION IN THE REPLICASE
RP COMPLEX, AND FUNCTION.
RX PubMed=22977246; DOI=10.1074/jbc.m112.410647;
RA Kulczyk A.W., Akabayov B., Lee S.J., Bostina M., Berkowitz S.A.,
RA Richardson C.C.;
RT "An interaction between DNA polymerase and helicase is essential for the
RT high processivity of the bacteriophage T7 replisome.";
RL J. Biol. Chem. 287:39050-39060(2012).
RN [17]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=23675753; DOI=10.1021/bi400284j;
RA Wallen J.R., Majka J., Ellenberger T.;
RT "Discrete interactions between bacteriophage T7 primase-helicase and DNA
RT polymerase drive the formation of a priming complex containing two copies
RT of DNA polymerase.";
RL Biochemistry 52:4026-4036(2013).
RN [18]
RP INTERACTION WITH THE VIRAL DNA POLYMERASE.
RX PubMed=26620561; DOI=10.1074/jbc.m115.698233;
RA Zhang H., Tang Y., Lee S.J., Wei Z., Cao J., Richardson C.C.;
RT "Binding Affinities among DNA Helicase-Primase, DNA Polymerase, and
RT Replication Intermediates in the Replisome of Bacteriophage T7.";
RL J. Biol. Chem. 291:1472-1480(2016).
RN [19]
RP FUNCTION.
RX PubMed=32009150; DOI=10.1093/nar/gkaa057;
RA Ma J.B., Chen Z., Xu C.H., Huang X.Y., Jia Q., Zou Z.Y., Mi C.Y., Ma D.F.,
RA Lu Y., Zhang H.D., Li M.;
RT "Dynamic structural insights into the molecular mechanism of DNA unwinding
RT by the bacteriophage T7 helicase.";
RL Nucleic Acids Res. 48:3156-3164(2020).
RN [20] {ECO:0007744|PDB:1CR0, ECO:0007744|PDB:1CR1, ECO:0007744|PDB:1CR2, ECO:0007744|PDB:1CR4}
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 271-566 IN COMPLEX WITH TTP, AND
RP SUBUNIT.
RX PubMed=10535735; DOI=10.1016/s0092-8674(00)81648-7;
RA Sawaya M.R., Guo S., Tabor S., Richardson C.C., Ellenberger T.;
RT "Crystal structure of the helicase domain from the replicative helicase-
RT primase of bacteriophage T7.";
RL Cell 99:167-177(1999).
RN [21] {ECO:0007744|PDB:1E0J, ECO:0007744|PDB:1E0K}
RP X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS) OF 261-549 IN COMPLEX WITH ATP
RP ANALOG, SUBUNIT, AND DNA-BINDING.
RX PubMed=10892646; DOI=10.1016/s0092-8674(00)80871-5;
RA Singleton M.R., Sawaya M.R., Ellenberger T., Wigley D.B.;
RT "Crystal structure of T7 gene 4 ring helicase indicates a mechanism for
RT sequential hydrolysis of nucleotides.";
RL Cell 101:589-600(2000).
RN [22] {ECO:0007744|PDB:1NUI}
RP X-RAY CRYSTALLOGRAPHY (2.90 ANGSTROMS) OF 1-255 IN COMPLEX WITH MAGNESIUM
RP AND ZINC, COFACTOR, AND DOMAIN.
RX PubMed=12769857; DOI=10.1016/s1097-2765(03)00195-3;
RA Kato M., Ito T., Wagner G., Richardson C.C., Ellenberger T.;
RT "Modular architecture of the bacteriophage T7 primase couples RNA primer
RT synthesis to DNA synthesis.";
RL Mol. Cell 11:1349-1360(2003).
RN [23] {ECO:0007744|PDB:1Q57}
RP X-RAY CRYSTALLOGRAPHY (3.45 ANGSTROMS) OF 64-566, AND SUBUNIT.
RX PubMed=14636571; DOI=10.1016/s1097-2765(03)00442-8;
RA Toth E.A., Li Y., Sawaya M.R., Cheng Y., Ellenberger T.;
RT "The crystal structure of the bifunctional primase-helicase of
RT bacteriophage T7.";
RL Mol. Cell 12:1113-1123(2003).
RN [24] {ECO:0007744|PDB:5IKN}
RP X-RAY CRYSTALLOGRAPHY (4.80 ANGSTROMS) OF 64-549.
RX PubMed=28052235; DOI=10.1016/j.str.2016.11.019;
RA Wallen J.R., Zhang H., Weis C., Cui W., Foster B.M., Ho C.M.W., Hammel M.,
RA Tainer J.A., Gross M.L., Ellenberger T.;
RT "Hybrid Methods Reveal Multiple Flexibly Linked DNA Polymerases within the
RT Bacteriophage T7 Replisome.";
RL Structure 25:157-166(2017).
RN [25] {ECO:0007744|PDB:6N7I, ECO:0007744|PDB:6N7N, ECO:0007744|PDB:6N7S, ECO:0007744|PDB:6N7T, ECO:0007744|PDB:6N7V, ECO:0007744|PDB:6N9U, ECO:0007744|PDB:6N9V, ECO:0007744|PDB:6N9W, ECO:0007744|PDB:6N9X}
RP STRUCTURE BY ELECTRON MICROSCOPY (3.20 ANGSTROMS) IN COMPLEX WITH TTP AND
RP MAGNESIUM, COFACTOR, AND SUBUNIT.
RX PubMed=30679383; DOI=10.1126/science.aav7003;
RA Gao Y., Cui Y., Fox T., Lin S., Wang H., de Val N., Zhou Z.H., Yang W.;
RT "Structures and operating principles of the replisome.";
RL Science 363:0-0(2019).
CC -!- FUNCTION: ATP-dependent DNA helicase and primase essential for viral
CC DNA replication and recombination (PubMed:21606333, PubMed:22977246,
CC PubMed:32009150). The helicase moves 5' -> 3' on the lagging strand
CC template, unwinding the DNA duplex ahead of the leading strand
CC polymerase at the replication fork and generating ssDNA for both
CC leading and lagging strand synthesis (PubMed:21606333, PubMed:22977246,
CC PubMed:32009150). ATP or dTTP hydrolysis propels each helicase domain
CC to translocate 2 nt per step sequentially along DNA (PubMed:30679383,
CC PubMed:17604719). Mediates strand transfer when a joint molecule is
CC available and participates in recombinational DNA repair through its
CC role in strand exchange (PubMed:9096333, PubMed:8617248). 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 (PubMed:6454135, PubMed:9139692).
CC {ECO:0000255|HAMAP-Rule:MF_04154, ECO:0000269|PubMed:17604719,
CC ECO:0000269|PubMed:21606333, ECO:0000269|PubMed:22977246,
CC ECO:0000269|PubMed:30679383, ECO:0000269|PubMed:32009150,
CC ECO:0000269|PubMed:6454135, ECO:0000269|PubMed:8617248,
CC ECO:0000269|PubMed:9096333, ECO:0000269|PubMed:9139692}.
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:0000255|HAMAP-Rule:MF_04154,
CC ECO:0000269|PubMed:2829184, ECO:0000269|PubMed:9185573};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04154,
CC ECO:0000269|PubMed:12769857};
CC Note=Binds 2 Mg(2+), one of which is catalytic. {ECO:0000255|HAMAP-
CC Rule:MF_04154, ECO:0000269|PubMed:12769857,
CC ECO:0000269|PubMed:30679383};
CC -!- SUBUNIT: Homohexamer (PubMed:16777142, PubMed:10880454,
CC PubMed:30679383, PubMed:10535735, PubMed:10892646, PubMed:14636571).
CC Assembles as a hexamer onto linear or circular ssDNA in the presence of
CC ATP or dTTP (PubMed:10880454). Present in a mixture of heptamers and
CC hexamers in the absence of DNA (PubMed:16777142, PubMed:14636571).
CC Interacts (via C-terminus) with the viral DNA polymerase that is bound
CC to DNA; this interaction is essential to initiate leading-strand DNA
CC synthesis (PubMed:15795374, PubMed:22977246, PubMed:23675753,
CC PubMed:26620561). The priming complex consists of 2 DNA polymerases and
CC 1 helicase-primase hexamer that assemble on the DNA template
CC (PubMed:23675753). Interacts with the single-stranded DNA-binding
CC protein (PubMed:1634539). Part of the replicase complex that includes
CC the DNA polymerase, thioredoxin, the primase/helicase and the single-
CC stranded DNA binding protein (PubMed:22977246). {ECO:0000255|HAMAP-
CC Rule:MF_04154, ECO:0000269|PubMed:10535735,
CC ECO:0000269|PubMed:10880454, ECO:0000269|PubMed:10892646,
CC ECO:0000269|PubMed:14636571, ECO:0000269|PubMed:15795374,
CC ECO:0000269|PubMed:1634539, ECO:0000269|PubMed:16777142,
CC ECO:0000269|PubMed:22977246, ECO:0000269|PubMed:23675753,
CC ECO:0000269|PubMed:26620561, ECO:0000269|PubMed:30679383}.
CC -!- INTERACTION:
CC P03692; P03692: 4; NbExp=2; IntAct=EBI-8664802, EBI-8664802;
CC P03692; P00581: 5; NbExp=2; IntAct=EBI-8664802, EBI-8664634;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative initiation; Named isoforms=2;
CC Comment=Isoform 4A contains the primase/helicase region, whereas
CC isoform 4B contains only the helicase region (PubMed:7310871).
CC Isoform 4A and 4B are present in a molar ratio of 1:8
CC (PubMed:2829184). {ECO:0000269|PubMed:2829184,
CC ECO:0000269|PubMed:7310871};
CC Name=4A; Synonyms=63-kDa protein;
CC IsoId=P03692-1; Sequence=Displayed;
CC Name=4B; Synonyms=56-kDa protein;
CC IsoId=P03692-2; Sequence=VSP_018683;
CC -!- DOMAIN: The N-terminus zinc finger domain is essential for delivering
CC the primed DNA template to the DNA polymerase (PubMed:12769857,
CC PubMed:10200256). The central core domain contains the primase activity
CC (PubMed:2829184). The C-terminus region is responsible for the helicase
CC activity and binds 1 Mg(2+)-dTTP (PubMed:2829184, PubMed:9185573,
CC PubMed:30679383). {ECO:0000255|HAMAP-Rule:MF_04154,
CC ECO:0000269|PubMed:10200256, ECO:0000269|PubMed:12769857,
CC ECO:0000269|PubMed:2829184, ECO:0000269|PubMed:30679383,
CC ECO:0000269|PubMed:9185573}.
CC -!- SIMILARITY: Belongs to the Teseptimavirus DNA helicase/primase family.
CC {ECO:0000255|HAMAP-Rule:MF_04154}.
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DR EMBL; V01127; CAA24348.1; -; Genomic_DNA.
DR EMBL; V01146; CAA24405.1; -; Genomic_DNA.
DR EMBL; V01146; CAA24407.1; -; Genomic_DNA.
DR PIR; A04314; YDBPA7.
DR RefSeq; NP_041975.1; NC_001604.1. [P03692-1]
DR RefSeq; NP_041977.1; NC_001604.1. [P03692-2]
DR PDB; 1CR0; X-ray; 2.30 A; A=271-566.
DR PDB; 1CR1; X-ray; 2.30 A; A=271-566.
DR PDB; 1CR2; X-ray; 2.30 A; A=271-566.
DR PDB; 1CR4; X-ray; 2.50 A; A=271-566.
DR PDB; 1E0J; X-ray; 3.00 A; A/B/C/D/E/F=261-549.
DR PDB; 1E0K; X-ray; 3.30 A; A/B/C/D/E/F=261-549.
DR PDB; 1NUI; X-ray; 2.90 A; A/B=1-255.
DR PDB; 1Q57; X-ray; 3.45 A; A/B/C/D/E/F/G=64-566.
DR PDB; 5IKN; X-ray; 4.80 A; D/E/F/G/H/I/J=64-549.
DR PDB; 6N7I; EM; 3.20 A; A/B/C/D/E/F=1-566.
DR PDB; 6N7N; EM; 3.50 A; A/B/C/D/E/F=1-566.
DR PDB; 6N7S; EM; 4.60 A; A/B/C/D/E/F=1-566.
DR PDB; 6N7T; EM; 3.90 A; A/B/C/D/E/F=1-566.
DR PDB; 6N7V; EM; 3.80 A; A/B/C/D/E/F=1-566.
DR PDB; 6N9U; EM; 3.70 A; E/F=1-566.
DR PDB; 6N9V; EM; 4.00 A; A/B/C/D/E/F=1-566.
DR PDB; 6N9W; EM; 4.00 A; A/B/C/D/E/F=1-566.
DR PDB; 6N9X; EM; 4.10 A; A/B/C/D/E/F=1-566.
DR PDBsum; 1CR0; -.
DR PDBsum; 1CR1; -.
DR PDBsum; 1CR2; -.
DR PDBsum; 1CR4; -.
DR PDBsum; 1E0J; -.
DR PDBsum; 1E0K; -.
DR PDBsum; 1NUI; -.
DR PDBsum; 1Q57; -.
DR PDBsum; 5IKN; -.
DR PDBsum; 6N7I; -.
DR PDBsum; 6N7N; -.
DR PDBsum; 6N7S; -.
DR PDBsum; 6N7T; -.
DR PDBsum; 6N7V; -.
DR PDBsum; 6N9U; -.
DR PDBsum; 6N9V; -.
DR PDBsum; 6N9W; -.
DR PDBsum; 6N9X; -.
DR SMR; P03692; -.
DR IntAct; P03692; 1.
DR MINT; P03692; -.
DR DrugBank; DB03222; dATP.
DR DrugBank; DB02452; Thymidine 5'-triphosphate.
DR GeneID; 1261046; -.
DR GeneID; 1261048; -.
DR KEGG; vg:1261046; -.
DR KEGG; vg:1261048; -.
DR EvolutionaryTrace; P03692; -.
DR Proteomes; UP000000840; Genome.
DR GO; GO:0043139; F:5'-3' DNA helicase activity; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003678; F:DNA helicase activity; IDA:UniProtKB.
DR GO; GO:0003896; F:DNA primase activity; IDA:CACAO.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR CDD; cd01029; TOPRIM_primases; 1.
DR Gene3D; 3.40.50.300; -; 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; IPR013237; Phage_T7_Gp4_N.
DR InterPro; IPR034154; TOPRIM_DnaG/twinkle.
DR InterPro; IPR006171; TOPRIM_domain.
DR InterPro; IPR027032; Twinkle-like.
DR PANTHER; PTHR12873; PTHR12873; 1.
DR Pfam; PF03796; DnaB_C; 1.
DR Pfam; PF08273; Prim_Zn_Ribbon; 1.
DR SMART; SM00778; Prim_Zn_Ribbon; 1.
DR SMART; SM00493; TOPRIM; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR PROSITE; PS51199; SF4_HELICASE; 1.
DR PROSITE; PS50880; TOPRIM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative initiation; ATP-binding; DNA replication;
KW DNA-binding; Helicase; Hydrolase; Magnesium; Metal-binding;
KW Multifunctional enzyme; Nucleotide-binding; Nucleotidyltransferase;
KW Primosome; Reference proteome; Transferase; Viral DNA replication; Zinc;
KW Zinc-finger.
FT CHAIN 1..566
FT /note="DNA helicase/primase"
FT /id="PRO_0000003355"
FT DOMAIN 151..238
FT /note="Toprim"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00995"
FT DOMAIN 281..548
FT /note="SF4 helicase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT ZN_FING 17..39
FT /note="C4-like; zinc ribbon fold"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:10200256, ECO:0000269|PubMed:12769857,
FT ECO:0000305|PubMed:2829184"
FT REGION 543..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 550..566
FT /note="Binding to viral DNA polymerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:26620561"
FT COMPBIAS 549..566
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 17
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:12769857"
FT BINDING 20
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:12769857"
FT BINDING 36
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:12769857"
FT BINDING 39
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:12769857"
FT BINDING 157
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:12769857"
FT BINDING 207
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:12769857"
FT BINDING 237
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000269|PubMed:12769857"
FT BINDING 312..319
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154"
FT SITE 361
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:10892646"
FT SITE 465
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:10535735"
FT SITE 504
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:10535735, ECO:0000305|PubMed:10892646"
FT SITE 522
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:10535735, ECO:0000305|PubMed:10892646"
FT SITE 535
FT /note="dTTP/dATP binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04154,
FT ECO:0000305|PubMed:10535735, ECO:0000305|PubMed:10892646"
FT VAR_SEQ 1..63
FT /note="Missing (in isoform 4B)"
FT /evidence="ECO:0000305"
FT /id="VSP_018683"
FT STRAND 11..15
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 18..20
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 26..29
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1NUI"
FT TURN 37..39
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 50..54
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 71..73
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 82..84
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 88..94
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 96..101
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 104..112
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 118..124
FT /evidence="ECO:0007829|PDB:1NUI"
FT TURN 126..128
FT /evidence="ECO:0007829|PDB:1Q57"
FT STRAND 131..134
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 154..158
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 159..169
FT /evidence="ECO:0007829|PDB:1NUI"
FT TURN 179..184
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 185..191
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 193..196
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 202..205
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 210..222
FT /evidence="ECO:0007829|PDB:1NUI"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 238..242
FT /evidence="ECO:0007829|PDB:1NUI"
FT TURN 243..246
FT /evidence="ECO:0007829|PDB:1NUI"
FT HELIX 247..254
FT /evidence="ECO:0007829|PDB:1NUI"
FT STRAND 263..267
FT /evidence="ECO:0007829|PDB:1Q57"
FT HELIX 268..271
FT /evidence="ECO:0007829|PDB:1E0J"
FT HELIX 272..281
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 295..299
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 307..313
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 318..331
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 337..344
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 346..357
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 362..364
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 377..386
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 387..389
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 391..394
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 402..414
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 419..426
FT /evidence="ECO:0007829|PDB:1CR0"
FT HELIX 440..456
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 459..465
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 471..473
FT /evidence="ECO:0007829|PDB:1E0J"
FT TURN 475..478
FT /evidence="ECO:0007829|PDB:6N7I"
FT HELIX 483..485
FT /evidence="ECO:0007829|PDB:1E0J"
FT STRAND 486..491
FT /evidence="ECO:0007829|PDB:1E0J"
FT HELIX 492..495
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 497..504
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 506..509
FT /evidence="ECO:0007829|PDB:1Q57"
FT STRAND 514..521
FT /evidence="ECO:0007829|PDB:1CR0"
FT TURN 522..524
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 528..535
FT /evidence="ECO:0007829|PDB:1CR0"
FT TURN 537..539
FT /evidence="ECO:0007829|PDB:1CR0"
FT STRAND 542..544
FT /evidence="ECO:0007829|PDB:1CR0"
SQ SEQUENCE 566 AA; 62655 MW; C808C3663FEBE5AA CRC64;
MDNSHDSDSV FLYHIPCDNC GSSDGNSLFS DGHTFCYVCE KWTAGNEDTK ERASKRKPSG
GKPMTYNVWN FGESNGRYSA LTARGISKET CQKAGYWIAK VDGVMYQVAD YRDQNGNIVS
QKVRDKDKNF KTTGSHKSDA LFGKHLWNGG KKIVVTEGEI DMLTVMELQD CKYPVVSLGH
GASAAKKTCA ANYEYFDQFE QIILMFDMDE AGRKAVEEAA QVLPAGKVRV AVLPCKDANE
CHLNGHDREI MEQVWNAGPW IPDGVVSALS LRERIREHLS SEESVGLLFS GCTGINDKTL
GARGGEVIMV TSGSGMGKST FVRQQALQWG TAMGKKVGLA MLEESVEETA EDLIGLHNRV
RLRQSDSLKR EIIENGKFDQ WFDELFGNDT FHLYDSFAEA ETDRLLAKLA YMRSGLGCDV
IILDHISIVV SASGESDERK MIDNLMTKLK GFAKSTGVVL VVICHLKNPD KGKAHEEGRP
VSITDLRGSG ALRQLSDTII ALERNQQGDM PNLVLVRILK CRFTGDTGIA GYMEYNKETG
WLEPSSYSGE EESHSESTDW SNDTDF
