DPOL_BPT3
ID DPOL_BPT3 Reviewed; 704 AA.
AC P20311;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1991, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000255|HAMAP-Rule:MF_04101};
DE EC=2.7.7.7 {ECO:0000250|UniProtKB:P00581, ECO:0000255|HAMAP-Rule:MF_04101};
DE EC=3.1.11.- {ECO:0000250|UniProtKB:P00581, ECO:0000255|HAMAP-Rule:MF_04101};
DE AltName: Full=Gene product 5;
DE Short=Gp5;
GN Name=5;
OS Enterobacteria phage T3 (Bacteriophage T3).
OC Viruses; Duplodnaviria; Heunggongvirae; Uroviricota; Caudoviricetes;
OC Caudovirales; Autographiviridae; Studiervirinae; Teetrevirus;
OC Escherichia virus T3.
OX NCBI_TaxID=10759;
OH NCBI_TaxID=562; Escherichia coli.
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Luria;
RX PubMed=2614843; DOI=10.1016/0022-2836(89)90102-2;
RA Beck P.J., Gonzalez S., Ward C.L., Molineux I.J.;
RT "Sequence of bacteriophage T3 DNA from gene 2.5 through gene 9.";
RL J. Mol. Biol. 210:687-701(1989).
CC -!- FUNCTION: Replicates viral genomic DNA. This polymerase possesses two
CC enzymatic activities: DNA synthesis (polymerase) and an exonucleolytic
CC activity that degrades single-stranded DNA in the 3'-5' direction.
CC {ECO:0000255|HAMAP-Rule:MF_04101}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC ChEBI:CHEBI:173112; EC=2.7.7.7; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_04101};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_04101};
CC -!- SUBUNIT: Composed of two subunits. One is encoded by the phage and the
CC other is encoded by the host thioredoxin.
CC {ECO:0000250|UniProtKB:P00581}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC {ECO:0000255|HAMAP-Rule:MF_04101}.
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DR EMBL; X17255; CAA35140.1; -; Genomic_DNA.
DR PIR; S07512; S07512.
DR RefSeq; NP_523320.1; NC_003298.1.
DR SMR; P20311; -.
DR PRIDE; P20311; -.
DR GeneID; 927419; -.
DR KEGG; vg:927419; -.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0039693; P:viral DNA genome replication; IEA:UniProtKB-KW.
DR Gene3D; 3.30.420.10; -; 1.
DR HAMAP; MF_04101; DPOL_T7; 1.
DR InterPro; IPR019760; DNA-dir_DNA_pol_A_CS.
DR InterPro; IPR001098; DNA-dir_DNA_pol_A_palm_dom.
DR InterPro; IPR043502; DNA/RNA_pol_sf.
DR InterPro; IPR002298; DNA_polymerase_A.
DR InterPro; IPR034699; DPOL_T7.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR PANTHER; PTHR10133; PTHR10133; 1.
DR Pfam; PF00476; DNA_pol_A; 1.
DR PRINTS; PR00868; DNAPOLI.
DR SMART; SM00482; POLAc; 1.
DR SUPFAM; SSF53098; SSF53098; 1.
DR SUPFAM; SSF56672; SSF56672; 1.
DR PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE 3: Inferred from homology;
KW DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW Hydrolase; Magnesium; Metal-binding; Multifunctional enzyme; Nuclease;
KW Nucleotidyltransferase; Transferase; Viral DNA replication.
FT CHAIN 1..704
FT /note="DNA-directed DNA polymerase"
FT /id="PRO_0000101268"
FT REGION 1..187
FT /note="3'-5'exonuclease"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT REGION 202..704
FT /note="Polymerase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 5
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 7
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 174
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /ligand_note="catalytic; for 3'-5' exonuclease activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 475
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 476
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 506
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 518
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 522
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 526
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="3"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
FT BINDING 654
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="4"
FT /ligand_note="catalytic; for polymerase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_04101"
SQ SEQUENCE 704 AA; 79985 MW; D65DFBD99AE31234 CRC64;
MLVSDIEANN LLEKVTKFHC GVIYDYRDGE YHSYRPGDFG AYLDALEAEV KRGGLIVFHN
GHKYDVPALT KLAKLQLNRE FHLPRENCID TLVLSRLIHS NLKDTDMGLL RSGKLPGKRF
GSHALEAWGY RLGEMKGEYK DDFKRMLEEQ GEEYVDGMEW WNFNEEMMDY NVQDVVVTKA
LLEKLLSDKH YFPPEIDFTD VGYTTFWSES LEAVDVEHRA AWLLAKQERN GFPFDTKAIE
ELYVELAARR SELLRNLTET FGSWYQPKGG TEMFCHPRTG KPLPKYPRIK IPKVGGIFKK
PKNKAQREGR EPCELDTREY VAGAPYTPVE HVVFNPSSRD HIQKKLQEAG WVPTKFTDKG
APVVDDEVLE GVRVDDPEKQ AAIDLIKEYL MIQKRIGQSA EGDKAWLRYV AEDGKIHGSV
NPNGAVTGRA THAFPNLAQI PGVRSPYGEQ CRAAFGAEHH LDGITGKPWV QAGIDASGLE
LRCLAHFMAR FDNGEYAHEI LNGDIHTKNQ MAAELPTRDN AKTFIYGFLY GAGDEKIGQI
VGAGKERGKE LKKKFLENTP AIAALRESIQ QTLVESSQWV AGEQQVKWKR RWIKGLDGRK
VHVRSPHAAL NTLLQSAGAL ICKLWIIKTE EMLVEKGLKH GWDGDFAYMA WIHDEIQVAC
RTEEIAKTVI EVAQEAMRWV GEHWNFRCLL DTEGKMGANW KECH
