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Entry: Q6WYJ7_BPT7
LinkDB: Q6WYJ7_BPT7
Original site: Q6WYJ7_BPT7 
ID   Q6WYJ7_BPT7             Unreviewed;       566 AA.
AC   Q6WYJ7;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   24-JAN-2024, entry version 76.
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};
DE   AltName: Full=Gene product 4 {ECO:0000256|HAMAP-Rule:MF_04154};
DE            Short=Gp4 {ECO:0000256|HAMAP-Rule:MF_04154};
GN   Name=4 {ECO:0000256|HAMAP-Rule:MF_04154};
OS   Escherichia phage T7 (Bacteriophage T7).
OC   Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC   Autographiviridae; Studiervirinae; Teseptimavirus; Teseptimavirus T7.
OX   NCBI_TaxID=10760 {ECO:0000313|Proteomes:UP000007959};
OH   NCBI_TaxID=562; Escherichia coli.
RN   [1] {ECO:0000313|EMBL:AAP33984.1, ECO:0000313|Proteomes:UP000007959}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=K {ECO:0000313|EMBL:AAP33984.1};
RX   PubMed=14629033; DOI=10.1007/s00239-003-2470-1;
RA   Bull J.J., Badgett M.R., Rokyta D., Molineux I.J.;
RT   "Experimental evolution yields hundreds of mutations in a functional viral
RT   genome.";
RL   J. Mol. Evol. 57:241-248(2003).
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 2 nt per step sequentially along
CC       DNA. Mediates strand transfer when a joint molecule is available and
CC       participates in recombinational DNA repair through its role in strand
CC       exchange. Primase activity synthesizes short RNA primers at the
CC       sequence 5'-GTC-3' on the lagging strand that the polymerase elongates
CC       using dNTPs and providing the primase is still present.
CC       {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, thioredoxin, the primase/helicase and the single-stranded
CC       DNA binding 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}.
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DR   EMBL; AY264775; AAP33984.1; -; Genomic_DNA.
DR   Proteomes; UP000007959; 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; PF08273; Prim_Zn_Ribbon; 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};
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   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          151..238
FT                   /note="Toprim"
FT                   /evidence="ECO:0000259|PROSITE:PS50880"
FT   DOMAIN          281..548
FT                   /note="SF4 helicase"
FT                   /evidence="ECO:0000259|PROSITE:PS51199"
FT   ZN_FING         17..39
FT                   /note="C4-like; zinc ribbon fold"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
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:0000256|HAMAP-Rule:MF_04154"
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:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         20
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         36
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         39
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         157
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         207
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         237
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   BINDING         312..319
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            361
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            465
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            504
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            522
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
FT   SITE            535
FT                   /note="dTTP/dATP binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_04154"
SQ   SEQUENCE   566 AA;  62752 MW;  909865CFA8A9C13A CRC64;
     MDNSHDSDSV FLYHIPCDNC GSSDGNSLFS DEHTFCYVCE KWTAGNEDTK ERASKRKSSG
     GKPMTYNVWN FGEFNGRYSA LTARGISKET CQKAGYWIAK VDGVMYQVAD YRDQNGNIVS
     QKVRDKDKNF KTTGSHKSDA LFGKHLWNGG KKIVVTEGEI DMLTVMELQD CKYPVVSLGH
     GASAAKKTCV ANYEYFDQFE QIILMFDMDE AGRKAVEEAA QVLPAGKVRV AVLPCKDANE
     CHLNGHDREI MEQVWNAGPW IPDGVVSALS LRERIREHLS SEESVGLLFS GCTGINDKTL
     GARGGEVIMV TSGSGMGKST FVRQQALQWG TAMGKKVGLA MLEESVEETA EDLIGLHNRV
     RLRQSDSLKR KIIENGKFDQ WFDELFGNDT FHLYDSFAEA ETDRLLAKLA YMCSGLGCDV
     IILDHISIVV SASGESDERK MIDNLMTKLK GFAKSTGVVL VVICHLKNPD KGKAHEEGRP
     VSITDLRGSG ALRQLSDTII ALERNQQGDM PNLVLVRILK CRFTGDTGIA GYMEYNKETG
     WLEPSSYSGE EESHSESTDW SNDTDF
//
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