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DNA polymerase (EC 2.7.7.7) (EC 3.1.11.-) (Gene product 2) (gp2) (Protein p2)

 DPOL_BPPH2              Reviewed;         575 AA.
P03680; B3VMN6; Q38545;
21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
21-JUL-1986, sequence version 1.
25-OCT-2017, entry version 117.
RecName: Full=DNA polymerase;
EC=2.7.7.7 {ECO:0000269|PubMed:3863101};
EC=3.1.11.- {ECO:0000269|PubMed:2790959};
AltName: Full=Gene product 2 {ECO:0000305};
Short=gp2 {ECO:0000305};
AltName: Full=Protein p2 {ECO:0000305};
Name=2;
Bacillus phage phi29 (Bacteriophage phi-29).
Viruses; dsDNA viruses, no RNA stage; Caudovirales; Podoviridae;
Picovirinae; Phi29virus.
NCBI_TaxID=10756;
NCBI_TaxID=1423; Bacillus subtilis.
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=6809534; DOI=10.1016/0378-1119(82)90149-4;
Yoshikawa H., Ito J.;
"Nucleotide sequence of the major early region of bacteriophage phi
29.";
Gene 17:323-335(1982).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Villegas A.P., Lingohr E.J., Ceyssens P.-J., Kropinski A.M.;
Submitted (MAY-2008) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-85.
PubMed=6292852; DOI=10.1093/nar/10.19.5785;
Escarmis C., Salas M.;
"Nucleotide sequence of the early genes 3 and 4 of bacteriophage phi
29.";
Nucleic Acids Res. 10:5785-5798(1982).
[4]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND MUTANT TEMPERATURE-SENSITIVE
TS2(24).
PubMed=2118623;
Blasco M.A., Blanco L., Pares E., Salas M., Bernad A.;
"Structural and functional analysis of temperature-sensitive mutants
of the phage phi 29 DNA polymerase.";
Nucleic Acids Res. 18:4763-4770(1990).
[5]
FUNCTION, AND CATALYTIC ACTIVITY.
PubMed=3863101; DOI=10.1073/pnas.82.19.6404;
Blanco L., Salas M.;
"Replication of phage phi 29 DNA with purified terminal protein and
DNA polymerase: synthesis of full-length phi 29 DNA.";
Proc. Natl. Acad. Sci. U.S.A. 82:6404-6408(1985).
[6]
FUNCTION.
PubMed=2498321;
Blanco L., Bernad A., Lazaro J.M., Martin G., Garmendia C., Salas M.;
"Highly efficient DNA synthesis by the phage phi 29 DNA polymerase.
Symmetrical mode of DNA replication.";
J. Biol. Chem. 264:8935-8940(1989).
[7]
FUNCTION, AND MUTAGENESIS OF ASP-12; GLU-14 AND ASP-66.
PubMed=2790959; DOI=10.1016/0092-8674(89)90883-0;
Bernad A., Blanco L., Lazaro J.M., Martin G., Salas M.;
"A conserved 3'->5' exonuclease active site in prokaryotic and
eukaryotic DNA polymerases.";
Cell 59:219-228(1989).
[8]
MUTAGENESIS OF TYR-454; CYS-455; ASP-456; THR-457 AND ASP-458.
PubMed=2191296; DOI=10.1073/pnas.87.12.4610;
Bernad A., Lazaro J.M., Salas M., Blanco L.;
"The highly conserved amino acid sequence motif Tyr-Gly-Asp-Thr-Asp-
Ser in alpha-like DNA polymerases is required by phage phi 29 DNA
polymerase for protein-primed initiation and polymerization.";
Proc. Natl. Acad. Sci. U.S.A. 87:4610-4614(1990).
[9]
DOMAIN.
PubMed=1850426;
Blasco M.A., Bernad A., Blanco L., Salas M.;
"Characterization and mapping of the pyrophosphorolytic activity of
the phage phi 29 DNA polymerase. Involvement of amino acid motifs
highly conserved in alpha-like DNA polymerases.";
J. Biol. Chem. 266:7904-7909(1991).
[10]
FUNCTION.
PubMed=1730646;
Blanco L., Bernad A., Esteban J.A., Salas M.;
"DNA-independent deoxynucleotidylation of the phi 29 terminal protein
by the phi 29 DNA polymerase.";
J. Biol. Chem. 267:1225-1230(1992).
[11]
MUTAGENESIS OF ASP-12; GLU-14; ASP-66 AND ASP-169, AND COFACTOR.
PubMed=1310035; DOI=10.1021/bi00117a006;
Esteban J.A., Bernad A., Salas M., Blanco L.;
"Metal activation of synthetic and degradative activities of phi 29
DNA polymerase, a model enzyme for protein-primed DNA replication.";
Biochemistry 31:350-359(1992).
[12]
FUNCTION.
PubMed=8428945;
Esteban J.A., Salas M., Blanco L.;
"Fidelity of phi 29 DNA polymerase. Comparison between protein-primed
initiation and DNA polymerization.";
J. Biol. Chem. 268:2719-2726(1993).
[13]
MUTAGENESIS OF ASN-387; SER-388; GLY-391 AND PHE-393.
PubMed=8344956;
Blasco M.A., Lazaro J.M., Blanco L., Salas M.;
"Phi 29 DNA polymerase active site. The conserved amino acid motif
'Kx3NSxYG' is involved in template-primer binding and dNTP
selection.";
J. Biol. Chem. 268:16763-16770(1993).
[14]
MUTAGENESIS OF ASP-249; SER-252; LEU-253 AND PRO-255.
PubMed=8226957;
Blasco M.A., Lazaro J.M., Blanco L., Salas M.;
"Phi 29 DNA polymerase active site. Residue ASP249 of conserved amino
acid motif 'Dx2SLYP' is critical for synthetic activities.";
J. Biol. Chem. 268:24106-24113(1993).
[15]
MUTAGENESIS OF THR-434; ALA-437 AND ARG-438.
PubMed=7962004;
Mendez J., Blanco L., Lazaro J.M., Salas M.;
"Primer-terminus stabilization at the phi 29 DNA polymerase active
site. Mutational analysis of conserved motif TX2GR.";
J. Biol. Chem. 269:30030-30038(1994).
[16]
MUTAGENESIS OF TYR-254 AND TYR-390.
PubMed=8537389; DOI=10.1074/jbc.270.52.31235;
Saturno J., Blanco L., Salas M., Esteban J.A.;
"A novel kinetic analysis to calculate nucleotide affinity of
proofreading DNA polymerases. Application to phi 29 DNA polymerase
fidelity mutants.";
J. Biol. Chem. 270:31235-31243(1995).
[17]
MUTAGENESIS OF LYS-498 AND TYR-500.
PubMed=7852344; DOI=10.1074/jbc.270.6.2735;
Blasco M.A., Mendez J., Lazaro J.M., Blanco L., Salas M.;
"Primer terminus stabilization at the phi 29 DNA polymerase active
site. Mutational analysis of conserved motif KXY.";
J. Biol. Chem. 270:2735-2740(1995).
[18]
DOMAIN.
PubMed=8621470; DOI=10.1074/jbc.271.15.8509;
Blanco L., Salas M.;
"Relating structure to function in phi29 DNA polymerase.";
J. Biol. Chem. 271:8509-8512(1996).
[19]
MUTAGENESIS OF ARG-223; TYR-226; TYR-226; ARG-227; ARG-227; GLY-228;
GLY-228; GLY-229; GLY-229; PHE-230; PHE-230 AND PHE-230, AND DOMAIN.
PubMed=8670845;
Truniger V., Lazaro J.M., Salas M., Blanco L.;
"A DNA binding motif coordinating synthesis and degradation in
proofreading DNA polymerases.";
EMBO J. 15:3430-3441(1996).
[20]
MUTAGENESIS OF THR-15 AND ASN-62.
PubMed=8605889;
de Vega M., Lazaro J.M., Salas M., Blanco L.;
"Primer-terminus stabilization at the 3'-5' exonuclease active site of
phi29 DNA polymerase. Involvement of two amino acid residues highly
conserved in proofreading DNA polymerases.";
EMBO J. 15:1182-1192(1996).
[21]
FUNCTION.
PubMed=9171364; DOI=10.1093/emboj/16.9.2519;
Mendez J., Blanco L., Salas M.;
"Protein-primed DNA replication: a transition between two modes of
priming by a unique DNA polymerase.";
EMBO J. 16:2519-2527(1997).
[22]
MUTAGENESIS OF LYS-143.
PubMed=9231901; DOI=10.1006/jmbi.1997.1093;
de Vega M., Ilyina T., Lazaro J.M., Salas M., Blanco L.;
"An invariant lysine residue is involved in catalysis at the 3'-5'
exonuclease active site of eukaryotic-type DNA polymerases.";
J. Mol. Biol. 270:65-78(1997).
[23]
MUTAGENESIS OF LYS-383.
PubMed=9199402; DOI=10.1006/jmbi.1997.1053;
Saturno J., Lazaro J.M., Esteban F.J., Blanco L., Salas M.;
"Phi29 DNA polymerase residue Lys383, invariant at motif B of DNA-
dependent polymerases, is involved in dNTP binding.";
J. Mol. Biol. 269:313-325(1997).
[24]
MUTAGENESIS OF PHE-65; SER-122 AND LEU-123.
PubMed=9642062; DOI=10.1006/jmbi.1998.1805;
de Vega M., Lazaro J.M., Salas M., Blanco L.;
"Mutational analysis of phi29 DNA polymerase residues acting as ssDNA
ligands for 3'-5' exonucleolysis.";
J. Mol. Biol. 279:807-822(1998).
[25]
MUTAGENESIS OF PHE-65; SER-122 AND LEU-123.
PubMed=9786901; DOI=10.1074/jbc.273.44.28966;
de Vega M., Blanco L., Salas M.;
"phi29 DNA polymerase residue Ser122, a single-stranded DNA ligand for
3'-5' exonucleolysis, is required to interact with the terminal
protein.";
J. Biol. Chem. 273:28966-28977(1998).
[26]
MUTAGENESIS OF ASP-456, AND COFACTOR.
PubMed=9784372; DOI=10.1006/jmbi.1998.2121;
Saturno J., Lazaro J.M., Blanco L., Salas M.;
"Role of the first aspartate residue of the 'YxDTDS' motif of phi29
DNA polymerase as a metal ligand during both TP-primed and DNA-primed
DNA synthesis.";
J. Mol. Biol. 283:633-642(1998).
[27]
DOMAIN.
PubMed=9614939; DOI=10.1006/jmbi.1998.1724;
Truniger V., Lazaro J.M., Salas M., Blanco L.;
"Phi 29 DNA polymerase requires the N-terminal domain to bind terminal
protein and DNA primer substrates.";
J. Mol. Biol. 278:741-755(1998).
[28]
MUTAGENESIS OF ARG-223; TYR-226; ARG-227; GLY-228; GLY-229; PHE-230
AND PHE-230, DOMAIN, AND INTERACTION WITH THE PRIMER TERMINAL PROTEIN.
PubMed=9931249; DOI=10.1006/jmbi.1998.2477;
Truniger V., Blanco L., Salas M.;
"Role of the 'YxGG/A' motif of Phi29 DNA polymerase in protein-primed
replication.";
J. Mol. Biol. 286:57-69(1999).
[29]
MUTAGENESIS OF TYR-254.
PubMed=10388570; DOI=10.1006/jmbi.1999.2900;
Bonnin A., Lazaro J.M., Blanco L., Salas M.;
"A single tyrosine prevents insertion of ribonucleotides in the
eukaryotic-type phi29 DNA polymerase.";
J. Mol. Biol. 290:241-251(1999).
[30]
FUNCTION.
PubMed=10493855; DOI=10.1006/jmbi.1999.3052;
de Vega M., Blanco L., Salas M.;
"Processive proofreading and the spatial relationship between
polymerase and exonuclease active sites of bacteriophage phi29 DNA
polymerase.";
J. Mol. Biol. 292:39-51(1999).
[31]
MUTAGENESIS OF LYS-392.
PubMed=12054770; DOI=10.1016/S0022-2836(02)00022-0;
Truniger V., Lazaro J.M., Blanco L., Salas M.;
"A highly conserved lysine residue in phi29 DNA polymerase is
important for correct binding of the templating nucleotide during
initiation of phi29 DNA replication.";
J. Mol. Biol. 318:83-96(2002).
[32]
INTERACTION WITH THE PRIMER TERMINAL PROTEIN, AND MUTAGENESIS OF
TYR-59; HIS-61 AND PHE-69.
PubMed=11884636; DOI=10.1093/nar/30.6.1379;
Eisenbrandt R., Lazaro J.M., Salas M., de Vega M.;
"Phi29 DNA polymerase residues Tyr59, His61 and Phe69 of the highly
conserved ExoII motif are essential for interaction with the terminal
protein.";
Nucleic Acids Res. 30:1379-1386(2002).
[33]
MUTAGENESIS OF ILE-364 AND LYS-371.
PubMed=11917008; DOI=10.1093/nar/30.7.1483;
Truniger V., Lazaro J.M., Esteban F.J., Blanco L., Salas M.;
"A positively charged residue of phi29 DNA polymerase, highly
conserved in DNA polymerases from families A and B, is involved in
binding the incoming nucleotide.";
Nucleic Acids Res. 30:1483-1492(2002).
[34]
MUTAGENESIS OF LEU-384.
PubMed=12805385; DOI=10.1074/jbc.M303052200;
Truniger V., Lazaro J.M., de Vega M., Blanco L., Salas M.;
"phi 29 DNA polymerase residue Leu384, highly conserved in motif B of
eukaryotic type DNA replicases, is involved in nucleotide insertion
fidelity.";
J. Biol. Chem. 278:33482-33491(2003).
[35]
MUTAGENESIS OF PHE-128.
PubMed=12473453; DOI=10.1016/S0022-2836(02)01130-0;
Rodriguez I., Lazaro J.M., Salas M., de Vega M.;
"phi29 DNA polymerase residue Phe128 of the highly conserved
(S/T)Lx(2)h motif is required for a stable and functional interaction
with the terminal protein.";
J. Mol. Biol. 325:85-97(2003).
[36]
MUTAGENESIS OF LYS-366 AND LYS-379.
PubMed=14672657; DOI=10.1016/j.jmb.2003.10.024;
Truniger V., Lazaro J.M., Salas M.;
"Two positively charged residues of phi29 DNA polymerase, conserved in
protein-primed DNA polymerases, are involved in stabilisation of the
incoming nucleotide.";
J. Mol. Biol. 335:481-494(2004).
[37]
DOMAIN.
PubMed=14729920; DOI=10.1093/nar/gkh184;
Truniger V., Lazaro J.M., Salas M.;
"Function of the C-terminus of phi29 DNA polymerase in DNA and
terminal protein binding.";
Nucleic Acids Res. 32:361-370(2004).
[38]
DOMAIN, AND MUTAGENESIS OF ARG-187; THR-189; SER-192; LYS-196; PHE-198
AND LYS-206.
PubMed=15777661; DOI=10.1016/j.gene.2004.12.041;
Truniger V., Bonnin A., Lazaro J.M., de Vega M., Salas M.;
"Involvement of the 'linker' region between the exonuclease and
polymerization domains of phi29 DNA polymerase in DNA and TP
binding.";
Gene 348:89-99(2005).
[39]
DOMAIN.
PubMed=15845765; DOI=10.1073/pnas.0500597102;
Rodriguez I., Lazaro J.M., Blanco L., Kamtekar S., Berman A.J.,
Wang J., Steitz T.A., Salas M., de Vega M.;
"A specific subdomain in phi29 DNA polymerase confers both
processivity and strand-displacement capacity.";
Proc. Natl. Acad. Sci. U.S.A. 102:6407-6412(2005).
[40]
MUTAGENESIS OF TYR-390.
PubMed=17652324; DOI=10.1093/nar/gkm545;
de Vega M., Salas M.;
"A highly conserved Tyrosine residue of family B DNA polymerases
contributes to dictate translesion synthesis past 8-oxo-7,8-dihydro-
2'-deoxyguanosine.";
Nucleic Acids Res. 35:5096-5107(2007).
[41]
FUNCTION.
PubMed=19011105; DOI=10.1073/pnas.0809882105;
Longas E., Villar L., Lazaro J.M., de Vega M., Salas M.;
"Phage phi29 and Nf terminal protein-priming domain specifies the
internal template nucleotide to initiate DNA replication.";
Proc. Natl. Acad. Sci. U.S.A. 105:18290-18295(2008).
[42]
MUTAGENESIS OF TYR-148.
PubMed=19576228; DOI=10.1016/j.jmb.2009.06.068;
Perez-Arnaiz P., Lazaro J.M., Salas M., de Vega M.;
"Functional importance of bacteriophage phi29 DNA polymerase residue
Tyr148 in primer-terminus stabilisation at the 3'-5' exonuclease
active site.";
J. Mol. Biol. 391:797-807(2009).
[43]
DOMAIN.
PubMed=19033368; DOI=10.1093/nar/gkn928;
Rodriguez I., Lazaro J.M., Salas M., de Vega M.;
"Involvement of the TPR2 subdomain movement in the activities of phi29
DNA polymerase.";
Nucleic Acids Res. 37:193-203(2009).
[44]
MUTAGENESIS OF VAL-250.
PubMed=19883660; DOI=10.1016/j.jmb.2009.10.061;
Perez-Arnaiz P., Lazaro J.M., Salas M., de Vega M.;
"phi29 DNA polymerase active site: role of residue Val250 as metal-
dNTP complex ligand and in protein-primed initiation.";
J. Mol. Biol. 395:223-233(2010).
[45]
INTERACTION WITH THE PRIMER TERMINAL PROTEIN.
PubMed=22210885; DOI=10.1093/nar/gkr1283;
del Prado A., Villar L., de Vega M., Salas M.;
"Involvement of residues of the Phi29 terminal protein intermediate
and priming domains in the formation of a stable and functional
heterodimer with the replicative DNA polymerase.";
Nucleic Acids Res. 40:3886-3897(2012).
[46]
MUTAGENESIS OF LYS-529.
PubMed=24023769; DOI=10.1371/journal.pone.0072765;
del Prado A., Lazaro J.M., Villar L., Salas M., de Vega M.;
"Dual role of phi29 DNA polymerase Lys529 in stabilisation of the DNA
priming-terminus and the terminal protein-priming residue at the
polymerisation site.";
PLoS ONE 8:E72765-E72765(2013).
[47]
MUTAGENESIS OF TYR-226 AND TYR-390.
PubMed=24464581; DOI=10.1074/jbc.M113.535666;
Dahl J.M., Wang H., Lazaro J.M., Salas M., Lieberman K.R.;
"Dynamics of translocation and substrate binding in individual
complexes formed with active site mutants of {phi}29 DNA polymerase.";
J. Biol. Chem. 289:6350-6361(2014).
[48] {ECO:0000244|PDB:1XHX, ECO:0000244|PDB:1XHZ}
X-RAY CRYSTALLOGRAPHY (2.35 ANGSTROMS).
PubMed=15546620; DOI=10.1016/j.molcel.2004.10.019;
Kamtekar S., Berman A.J., Wang J., Lazaro J.M., de Vega M., Blanco L.,
Salas M., Steitz T.A.;
"Insights into strand displacement and processivity from the crystal
structure of the protein-primed DNA polymerase of bacteriophage
phi29.";
Mol. Cell 16:609-618(2004).
[49] {ECO:0000244|PDB:1XI1}
X-RAY CRYSTALLOGRAPHY (2.20 ANGSTROMS) IN COMPLEX WITH MAGNESIUM, AND
COFACTOR.
PubMed=15608377; DOI=10.1107/S0907444904026721;
Wang J., Kamtekar S., Berman A.J., Steitz T.A.;
"Correction of X-ray intensities from single crystals containing
lattice-translocation defects.";
Acta Crystallogr. D 61:67-74(2005).
[50] {ECO:0000244|PDB:2EX3}
X-RAY CRYSTALLOGRAPHY (3.00 ANGSTROMS).
PubMed=16511564; DOI=10.1038/sj.emboj.7601027;
Kamtekar S., Berman A.J., Wang J., Lazaro J.M., de Vega M., Blanco L.,
Salas M., Steitz T.A.;
"The phi29 DNA polymerase:protein-primer structure suggests a model
for the initiation to elongation transition.";
EMBO J. 25:1335-1343(2006).
[51] {ECO:0000244|PDB:2PY5, ECO:0000244|PDB:2PYJ, ECO:0000244|PDB:2PYL, ECO:0000244|PDB:2PZS}
X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) IN COMPLEX WITH MANGANESE AND
TTP, AND COFACTOR.
PubMed=17611604; DOI=10.1038/sj.emboj.7601780;
Berman A.J., Kamtekar S., Goodman J.L., Lazaro J.M., de Vega M.,
Blanco L., Salas M., Steitz T.A.;
"Structures of phi29 DNA polymerase complexed with substrate: the
mechanism of translocation in B-family polymerases.";
EMBO J. 26:3494-3505(2007).
-!- FUNCTION: Polymerase responsible for protein-primed viral DNA
replication by strand displacement with high processivity and
fidelity (PubMed:3863101) (PubMed:2498321). To start replication,
the DNA polymerase forms a heterodimer with a free primer terminal
protein (TP), recognizes the replication origins at both 5' ends
of the linear chromosome, and initiates replication using as
primer the OH-group of Ser-232 of the TP (PubMed:22210885). This
polymerase possesses three enzymatic activities: DNA synthesis
(polymerase), primer terminal protein (TP) deoxynucleotidylation,
which is the formation of a covalent linkage (phosphoester)
between the hydroxyl group of a specific serine residue in TP and
5'-dAMP, a reaction directed by the second T at the 3' end, and 3'
to 5' exonuclease activity (PubMed:2790959). Exonuclease activity
has a proofreading purpose (PubMed:2790959). DNA polymerase edits
the polymerization errors using an intramolecular pathway as the
primer terminus travels from one active site to the other without
dissociation from the DNA (PubMed:10493855). DNA polymerization
catalyzed by the DNA polymerase is a highly accurate process, but
the protein-primed initiation is a quite inaccurate reaction
(PubMed:8428945). Since the polymerase initiates the replication
on the second thymine, the TP-dAMP initiation product translocates
backwards to recover the template information of the first
nucleotide (sliding back-mechanism) (PubMed:19011105).
{ECO:0000269|PubMed:10493855, ECO:0000269|PubMed:1730646,
ECO:0000269|PubMed:19011105, ECO:0000269|PubMed:22210885,
ECO:0000269|PubMed:2498321, ECO:0000269|PubMed:2790959,
ECO:0000269|PubMed:3863101, ECO:0000269|PubMed:8428945,
ECO:0000269|PubMed:9171364}.
-!- CATALYTIC ACTIVITY: Deoxynucleoside triphosphate + DNA(n) =
diphosphate + DNA(n+1). {ECO:0000269|PubMed:3863101}.
-!- COFACTOR:
Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
Evidence={ECO:0000269|PubMed:1310035,
ECO:0000269|PubMed:15608377, ECO:0000269|PubMed:17611604,
ECO:0000269|PubMed:9784372};
-!- SUBUNIT: Interacts with the primer terminal protein; this
interaction allows the initiation of TP-primed DNA replication at
both viral DNA ends. Interacts with DNA.
{ECO:0000269|PubMed:11884636, ECO:0000269|PubMed:22210885,
ECO:0000269|PubMed:9931249}.
-!- DOMAIN: The N-terminus contains the 3'-5' exonuclease activity and
strand displacement ability (PubMed:8621470). The conserved motif
YxGG/A located between the 3'-5' exonuclease and polymerization
domains is important for DNA-binding, coordination between DNA
synthesis and degradation and for the formation of a stable
complex between TP and the DNA polymerase (PubMed:8670845,
PubMed:9931249, PubMed:15777661). The C-terminus is involved in
the protein-primed initiation, DNA polymerization and
pyrophosphorolytic activities (PubMed:8621470, PubMed:1850426).
The YCDTD motif is essential for the pyrophosphorolytic activity
(PubMed:1850426). The TPR2 region is necessary for the strand
displacement coupled to DNA synthesis and probably also for
allowing the TP priming domain to move out from the polymerase
during transition from initiation to elongation (PubMed:15845765,
PubMed:19033368). {ECO:0000269|PubMed:15845765,
ECO:0000269|PubMed:1850426, ECO:0000269|PubMed:19033368,
ECO:0000269|PubMed:8621470, ECO:0000269|PubMed:9614939,
ECO:0000269|PubMed:9931249}.
-!- MISCELLANEOUS: This DNA polymerase requires a protein as a primer.
{ECO:0000269|PubMed:16511564}.
-!- SIMILARITY: Belongs to the DNA polymerase type-B family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=ACE96023.1; Type=Erroneous initiation; Note=Translation N-terminally extended.;
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EMBL; V01155; CAA24480.1; -; Genomic_DNA.
EMBL; X53370; CAA37450.1; -; Genomic_DNA.
EMBL; EU771092; ACE96023.1; ALT_INIT; Genomic_DNA.
EMBL; X53371; CAA37451.1; -; Genomic_DNA.
PIR; A04282; ERBP29.
RefSeq; YP_002004529.1; NC_011048.1.
PDB; 1XHX; X-ray; 2.35 A; A/B/C/D=1-575.
PDB; 1XHZ; X-ray; 2.70 A; A/B/C/D=1-575.
PDB; 1XI1; X-ray; 2.20 A; A/B=1-575.
PDB; 2EX3; X-ray; 3.00 A; A/C/E/G/I/K=1-575.
PDB; 2PY5; X-ray; 1.60 A; A/B=1-575.
PDB; 2PYJ; X-ray; 2.03 A; A/B=1-575.
PDB; 2PYL; X-ray; 2.20 A; A=1-575.
PDB; 2PZS; X-ray; 2.60 A; A/B/C/D=1-575.
PDBsum; 1XHX; -.
PDBsum; 1XHZ; -.
PDBsum; 1XI1; -.
PDBsum; 2EX3; -.
PDBsum; 2PY5; -.
PDBsum; 2PYJ; -.
PDBsum; 2PYL; -.
PDBsum; 2PZS; -.
ProteinModelPortal; P03680; -.
SMR; P03680; -.
GeneID; 6446511; -.
KEGG; vg:6446511; -.
KO; K21237; -.
OrthoDB; VOG0900004K; -.
EvolutionaryTrace; P03680; -.
Proteomes; UP000001207; Genome.
GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0039693; P:viral DNA genome replication; IDA:UniProtKB.
Gene3D; 3.30.420.10; -; 1.
InterPro; IPR006172; DNA-dir_DNA_pol_B.
InterPro; IPR017964; DNA-dir_DNA_pol_B_CS.
InterPro; IPR004868; DNA-dir_DNA_pol_B_mt/vir.
InterPro; IPR014416; DNA-dir_DNA_polB_phi29_vir.
InterPro; IPR012337; RNaseH-like_sf.
InterPro; IPR036397; RNaseH_sf.
Pfam; PF03175; DNA_pol_B_2; 1.
PIRSF; PIRSF004178; Dpol_Bac_phage; 1.
PRINTS; PR00106; DNAPOLB.
SMART; SM00486; POLBc; 1.
SUPFAM; SSF53098; SSF53098; 1.
PROSITE; PS00116; DNA_POLYMERASE_B; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; DNA replication; DNA-binding;
DNA-directed DNA polymerase; Early protein; Exonuclease; Hydrolase;
Magnesium; Metal-binding; Nuclease; Nucleotide-binding;
Nucleotidyltransferase; Reference proteome; Transferase;
Viral DNA replication.
CHAIN 1 575 DNA polymerase.
/FTId=PRO_0000046542.
REGION 1 191 3'-5' exonuclease and strand displacement
activities. {ECO:0000269|PubMed:8621470}.
REGION 192 229 Involved in DNA-binding, coordination
between DNA synthesis and degradation and
TP interaction.
{ECO:0000269|PubMed:15777661,
ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
REGION 230 562 Initiation, polymerization and
pyrophosphorolytic activities.
{ECO:0000269|PubMed:8621470}.
REGION 398 420 TPR2. {ECO:0000269|PubMed:15845765}.
REGION 563 575 Involved in DNA-binding and TP
interaction.
{ECO:0000269|PubMed:14729920}.
MOTIF 454 458 YCDTD. {ECO:0000269|PubMed:1850426}.
METAL 145 145 Magnesium 1. {ECO:0000244|PDB:1XI1}.
METAL 169 169 Magnesium 1. {ECO:0000244|PDB:1XI1}.
METAL 249 249 Magnesium 2; catalytic.
{ECO:0000244|PDB:2PYJ,
ECO:0000269|PubMed:8226957}.
METAL 250 250 Magnesium 2; via carbonyl oxygen;
catalytic. {ECO:0000244|PDB:2PYJ,
ECO:0000269|PubMed:19883660}.
METAL 456 456 Magnesium 2; catalytic.
{ECO:0000269|PubMed:9784372}.
METAL 458 458 Magnesium 2; catalytic.
{ECO:0000244|PDB:2PYJ}.
BINDING 254 254 TTP; via amide nitrogen.
{ECO:0000244|PDB:2PYL}.
BINDING 371 371 TTP. {ECO:0000244|PDB:2PYL}.
BINDING 383 383 TTP. {ECO:0000244|PDB:2PYL}.
BINDING 458 458 TTP. {ECO:0000244|PDB:2PYL}.
SITE 12 12 Essential for 3'-5' exonucleolysis.
{ECO:0000269|PubMed:2790959,
ECO:0000269|PubMed:8344956}.
SITE 14 14 Essential for 3'-5' exonucleolysis.
{ECO:0000269|PubMed:2790959,
ECO:0000269|PubMed:8344956}.
SITE 15 15 Involved in proofreading function by
stabilization of the frayed primer-
terminus at the 3'-5' exonuclease active
site. {ECO:0000269|PubMed:8605889}.
SITE 59 59 Interaction with the primer terminal
protein. {ECO:0000269|PubMed:11884636}.
SITE 61 61 Interaction with the primer terminal
protein. {ECO:0000269|PubMed:11884636}.
SITE 62 62 Involved in proofreading function by
stabilization of the frayed primer-
terminus at the 3'-5' exonuclease active
site. {ECO:0000269|PubMed:8605889}.
SITE 65 65 Binds ssDNA; Essential for 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:9786901}.
SITE 66 66 Essential for 3'-5' exonucleolysis.
{ECO:0000269|PubMed:2790959,
ECO:0000269|PubMed:8344956}.
SITE 69 69 Interaction with the primer terminal
protein. {ECO:0000269|PubMed:11884636}.
SITE 93 93 Involved in binding template-primer
structures. {ECO:0000269|PubMed:8344956}.
SITE 122 122 Binds ssDNA; Essential for 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:9786901}.
SITE 123 123 Binds ssDNA; Essential for 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:9786901}.
SITE 148 148 Involved in the stabilization of the
frayed 3' terminus at the exonuclease
active site.
{ECO:0000269|PubMed:19576228}.
SITE 252 252 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:8226957}.
SITE 254 254 Probably involved in nucleotide binding
selection. {ECO:0000269|PubMed:8537389}.
SITE 356 356 Binds ssDNA; Essential for 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:8605889}.
SITE 364 364 Involved in the binding of DNA and dNTP.
{ECO:0000269|PubMed:11917008}.
SITE 366 366 Stabilization of the incoming nucleotide.
{ECO:0000269|PubMed:14672657}.
SITE 371 371 Interacts with the phosphate groups of
the incoming nucleotide.
{ECO:0000269|PubMed:11917008}.
SITE 379 379 Stabilization of the incoming nucleotide.
{ECO:0000269|PubMed:14672657}.
SITE 383 383 Probably involved in nucleotide binding
selection. {ECO:0000269|PubMed:9199402}.
SITE 384 384 Probably involved in positioning the
templating nucleotide at the
polymerization active site and in
controlling nucleotide insertion
fidelity. {ECO:0000269|PubMed:12805385}.
SITE 387 387 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:8344956}.
SITE 390 390 Probably involved in nucleotide binding
selection. {ECO:0000269|PubMed:8537389}.
SITE 391 391 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:8344956}.
SITE 420 420 Binds ssDNA; Essential for 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:8605889}.
SITE 434 434 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:7962004}.
SITE 438 438 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:7962004}.
SITE 498 498 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:7852344}.
SITE 500 500 Probably involved in binding template-
primer structures.
{ECO:0000269|PubMed:7852344}.
SITE 529 529 Stabilizes the primer-terminus at the
polymerization active site and
contributes to the coordination between
the exonuclease and polymerazation
activities.
{ECO:0000269|PubMed:24023769}.
VARIANT 176 176 A -> R (in mutant TS2(24)).
VARIANT 355 355 A -> V (in mutant TS2(24)).
MUTAGEN 12 12 D->A: Strong loss of 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:1310035,
ECO:0000269|PubMed:2790959}.
MUTAGEN 14 14 E->A: Strong loss of 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:1310035,
ECO:0000269|PubMed:2790959}.
MUTAGEN 15 15 T->I: 95% loss of ssDNA-binding.
Decreased in fidelity of DNA replication.
{ECO:0000269|PubMed:8605889}.
MUTAGEN 59 59 Y->F: Almost no effect on replication
activity. About 20% loss of TP-DNA
initiation, 20% loss of TP-DNA
replication and 10% loss of TP-DNA
amplification. Complete loss of
interaction with TP.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 59 59 Y->L: 3 fold decrease in replication
activity. About 80% loss of TP-DNA
initiation, 70% loss of TP-DNA
replication and 97% loss of TP-DNA
amplification. Complete loss of
interaction with TP.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 59 59 Y->R: 3 fold decrease in replication
activity. About 75% loss of TP-DNA
initiation, complete loss of TP-DNA
replication and complete loss of TP-DNA
amplification.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 61 61 H->L: 5 fold decrease in replication
activity. About 85% loss of TP-DNA
initiation, 80% loss of TP-DNA
replication and complete loss of TP-DNA
amplification. Complete loss of
interaction with TP.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 61 61 H->R: 100 fold decrease in replication
activity. Complete loss of interaction
with TP. {ECO:0000269|PubMed:11884636}.
MUTAGEN 62 62 N->D,H: 88% loss of ssDNA-binding.
Decreased in fidelity of DNA replication.
{ECO:0000269|PubMed:8605889}.
MUTAGEN 65 65 F->S: Loss of capacity to interact with a
DNA primer/template structure.
{ECO:0000269|PubMed:9786901}.
MUTAGEN 66 66 D->A: Strong loss of 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:1310035,
ECO:0000269|PubMed:2790959}.
MUTAGEN 69 69 F->S: 2 fold decrease in replication
activity. About 50% loss of TP-DNA
initiation, 40% loss of TP-DNA
replication and 60% loss of TP-DNA
amplification. Complete loss of
interaction with TP.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 69 69 F->Y: 2 fold decrease in replication
activity. About 80% loss of TP-DNA
initiation, 50% loss of TP-DNA
replication and almost 95% loss of TP-
DNA. Complete loss of interaction with TP
amplification.
{ECO:0000269|PubMed:11884636}.
MUTAGEN 122 122 S->T: Loss of capacity to interact with a
DNA primer/template structure.
{ECO:0000269|PubMed:9786901}.
MUTAGEN 123 123 L->N: Loss of capacity to interact with a
DNA primer/template structure.
{ECO:0000269|PubMed:9786901}.
MUTAGEN 128 128 F->A: Slight loss of interaction with TP.
{ECO:0000269|PubMed:12473453}.
MUTAGEN 128 128 F->Y: Almost complete loss of interaction
with TP. {ECO:0000269|PubMed:12473453}.
MUTAGEN 143 143 K->I,R: Strong loss of 3'-5' exonuclease,
proofreading and strand-displacement
activities. {ECO:0000269|PubMed:9231901}.
MUTAGEN 148 148 Y->A: Reduced capacity to stabilize the
binding of the primer terminus at the 3'-
5' exonuclease active site.
{ECO:0000269|PubMed:19576228}.
MUTAGEN 169 169 D->A: Strong loss of 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:1310035}.
MUTAGEN 187 187 R->K: No effect on DNA-binding, TP
binding and replication/amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 189 189 T->A: No effect on DNA-binding, TP
binding and replication/amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 192 192 S->I: Loss of DNA-binding. Reduced TP
binding. 25% loss of replication and
almost complete loss of amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 192 192 S->N: Loss of DNA-binding. No effect on
TP binding. 50% loss of
replication/amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 196 196 K->I: Loss of DNA-binding. Reduced TP
binding. 25% loss of replication and
almost complete loss of amplification. 6-
fold reduced 3'-5' exonucleolysis.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 196 196 K->R: Slight loss of DNA-binding. No loss
of replication and amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 198 198 F->V: Loss of DNA-binding. Reduced TP
binding. 25% loss of replication and
almost complete loss of amplification. 6-
fold reduced 3'-5' exonucleolysis.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 206 206 K->I: No effect on DNA-binding. Reduced
TP binding. 70% loss of replication and
20% loss of amplification.
{ECO:0000269|PubMed:15777661}.
MUTAGEN 223 223 R->I: Favored exonucleolysis (low pol/exo
ratio). {ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 226 226 Y->F: Favored polymerization (high
pol/exo ratio). decrease in forward and
reverse rates of translocation. Increased
affinity for dNTP and for pyrophosphate
in the pre-translocation state.
{ECO:0000269|PubMed:24464581,
ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 226 226 Y->S: Favored exonucleolysis. Complete
loss of polymerization.
{ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 227 227 R->I: Favored exonucleolysis (low pol/exo
ratio). {ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 227 227 R->K: No effect on the pol/exo ratio.
{ECO:0000269|PubMed:9931249}.
MUTAGEN 228 228 G->A: Favored polymerization (high
pol/exo ratio).
{ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 229 229 G->A: Favored exonucleolysis (low pol/exo
ratio). {ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 229 229 G->D: Favored exonucleolysis. Complete
loss of polymerization.
{ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 230 230 F->A: Favored polymerization (high
pol/exo ratio).
{ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 230 230 F->S: Favored exonucleolysis (low pol/exo
ratio). {ECO:0000269|PubMed:8670845,
ECO:0000269|PubMed:9931249}.
MUTAGEN 230 230 F->Y: No effect on the pol/exo ratio.
{ECO:0000269|PubMed:9931249}.
MUTAGEN 249 249 D->E: Complete loss of DNA polymerase
activity. Slight decrease in template-
primer binding. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:8226957}.
MUTAGEN 250 250 V->A: No effect on TP-DNA replication.
{ECO:0000269|PubMed:19883660}.
MUTAGEN 250 250 V->F: Complete loss of TP-DNA
replication.
{ECO:0000269|PubMed:19883660}.
MUTAGEN 251 251 N->D: No effect on TP-DNA replication.
{ECO:0000269|PubMed:19883660}.
MUTAGEN 252 252 S->G: 40% loss of DNA polymerase
activity. No effect on translocation or
stabilization of the incorporated
nucIeotide. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:8226957}.
MUTAGEN 252 252 S->R: Complete loss of DNA polymerase
activity. Drastic loss of template-primer
binding. No effect on 3' to 5'
exonucleolysis and interaction with the
TP primer. {ECO:0000269|PubMed:8226957}.
MUTAGEN 253 253 L->V: 30% loss of DNA polymerase
activity. No effect on translocation or
stabilization of the incorporated
nucIeotide. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:8226957}.
MUTAGEN 254 254 Y->F: Decreased dNTP binding affinity.
10-fold reduced affinity for the correct
nucleotide. {ECO:0000269|PubMed:8537389}.
MUTAGEN 254 254 Y->V: Loss of discrimination for rNTPs
over dNTPs.
{ECO:0000269|PubMed:10388570}.
MUTAGEN 255 255 P->S: 30% loss of DNA polymerase
activity. No effect on translocation or
stabilization of the incorporated
nucIeotide. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:8226957}.
MUTAGEN 364 364 I->Q: Partial loss of hability to stably
bind the DNA substrate.
{ECO:0000269|PubMed:11917008}.
MUTAGEN 364 364 I->R: Complete loss of hability to stably
bind the DNA substrate.
{ECO:0000269|PubMed:11917008}.
MUTAGEN 366 366 K->T: Slight decrease in DNA-binding
capacity. No effect on polymerisation
activity, except that it is reduced in
the absence of a DNA template. Reduced
affinity for the initiating nucleotide. 3
fold reduction of the initiation activity
in the presence of p6.
{ECO:0000269|PubMed:14672657}.
MUTAGEN 371 371 K->T: Strong decrease in the affinity for
dNTPs and pyrophosphorolytic activity. No
effect on exonucleolysis.
{ECO:0000269|PubMed:11917008}.
MUTAGEN 379 379 K->T: Slight increase in DNA-binding
capacity. Reduced affinity for the
initiating nucleotide.
{ECO:0000269|PubMed:14672657}.
MUTAGEN 383 383 K->P: Complete loss of incorporation of
dNTP substrates using either DNA or TP as
primer. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:9199402}.
MUTAGEN 383 383 K->R: Strong loss of ability to use dNTPs
in both processive and non-processive DNA
synthesis. Impaired progression from
protein-primed initiation to DNA
elongation. No effect on 3' to 5'
exonucleolysis.
{ECO:0000269|PubMed:9199402}.
MUTAGEN 384 384 L->R: Reduced nucleotide insertion
fidelity during DNA-primed polymerization
and protein-primed initiation. No effect
on the affinity for the different dNTPs.
{ECO:0000269|PubMed:12805385}.
MUTAGEN 387 387 N->Y: 3-fold higher Km value for dATP and
more than 11-fold lower Vmax value than
the wild-type enzyme in the initiation
reaction. Impaired in enzyme-DNA
translocation.
{ECO:0000269|PubMed:8344956}.
MUTAGEN 388 388 S->G: No effect on initiation and
polymerization activities. Increased
efficiency of dNTP incorporation in non-
templated reactions.
{ECO:0000269|PubMed:8344956}.
MUTAGEN 390 390 Y->F: Decreased dNTP binding affinity in
the post-translocation state. 4.6-fold
reduced affinity for the correct
nucleotide. {ECO:0000269|PubMed:24464581,
ECO:0000269|PubMed:8537389}.
MUTAGEN 390 390 Y->S: Decreased dNTP binding affinity.
14-fold reduced affinity for the correct
nucleotide. Loss of discrimination
against dA insertion opposite 8oxodG.
{ECO:0000269|PubMed:17652324,
ECO:0000269|PubMed:8537389}.
MUTAGEN 391 391 G->D: Complete loss of template-primer
binding. {ECO:0000269|PubMed:8344956}.
MUTAGEN 392 392 K->Q: 50% loss of exonuclease activity.
80% loss of processivity. No effect on
DNA polymerase/DNA complex formation.
{ECO:0000269|PubMed:12054770}.
MUTAGEN 392 392 K->R: 90% loss of exonuclease activity.
80% loss of processivity. No effect on
DNA polymerase/DNA complex formation.
{ECO:0000269|PubMed:12054770}.
MUTAGEN 393 393 F->Y: Severe decrease in initial binding
to template-primer DNA molecules.
{ECO:0000269|PubMed:8344956}.
MUTAGEN 434 434 T->N: Complete loss of TP-dAMP formation.
Almost complete loss of DNA
polymerization.
{ECO:0000269|PubMed:7962004}.
MUTAGEN 437 437 A->G: No effect on TP-dAMP formation. 20%
loss of DNA polymerization.
{ECO:0000269|PubMed:7962004}.
MUTAGEN 438 438 R->I: Complete loss of TP-dAMP formation.
Almost complete loss of DNA
polymerization.
{ECO:0000269|PubMed:7962004}.
MUTAGEN 438 438 R->K: Complete loss of TP-dAMP formation.
30% loss of DNA polymerization.
{ECO:0000269|PubMed:7962004}.
MUTAGEN 454 454 Y->F: No effect on the formation of the
covalent complex between the TP and 5'-
dAMP. Loss of replication of a p3-DNA
complex or a primed M13 DNA. Increased
3'-5' exonucleolysis.
{ECO:0000269|PubMed:2191296}.
MUTAGEN 455 455 C->G: 65% loss of formation of the
covalent complex between the TP and 5'-
dAMP. Increased 3'-5' exonucleolysis.
{ECO:0000269|PubMed:2191296}.
MUTAGEN 456 456 D->G: 50% loss of synthetic activities,
TP-primed initiation and DNA-primed
polymerization. When polymerization
requires an efficient translocation along
the template, catalytic efficiency is
strongly reduced. 90% loss of formation
of the covalent complex between the TP
and 5'-dAMP. Increased 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:2191296,
ECO:0000269|PubMed:9784372}.
MUTAGEN 457 457 T->P: Complete loss of initiation and
polymerization activities. Severe loss of
protein-priming activity. Increased 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:2191296}.
MUTAGEN 458 458 D->G: Complete loss of initiation and
polymerization activities. Severe loss of
protein-priming activity. Increased 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:2191296}.
MUTAGEN 498 498 K->R: Strong decrease in DNA
polymerization activity. Loss of binding
to a primer-template DNA. Increased 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:7852344}.
MUTAGEN 498 498 K->T: Strong decrease in initiation and
DNA polymerization activities. Loss of
binding to a primer-template DNA.
Increased 3'-5' exonucleolysis.
{ECO:0000269|PubMed:7852344}.
MUTAGEN 500 500 Y->S: Strong decrease in DNA
polymerization activity and interaction
with primer-template DNA. Increased 3'-5'
exonucleolysis.
{ECO:0000269|PubMed:7852344}.
MUTAGEN 529 529 K->A: Increased exonuclease activity and
loss of primer elongation. Deficient in
nucleotide incorporation.
{ECO:0000269|PubMed:24023769}.
MUTAGEN 529 529 K->E: Increased exonuclease activity and
complete loss of primer elongation.
{ECO:0000269|PubMed:24023769}.
CONFLICT 492 492 A -> V (in Ref. 4; CAA37450).
{ECO:0000305}.
STRAND 8 15 {ECO:0000244|PDB:2PY5}.
STRAND 19 21 {ECO:0000244|PDB:2PYL}.
STRAND 24 33 {ECO:0000244|PDB:2PY5}.
STRAND 38 42 {ECO:0000244|PDB:2PY5}.
HELIX 44 54 {ECO:0000244|PDB:2PY5}.
STRAND 57 62 {ECO:0000244|PDB:2PY5}.
HELIX 63 76 {ECO:0000244|PDB:2PY5}.
STRAND 89 95 {ECO:0000244|PDB:2PY5}.
STRAND 100 110 {ECO:0000244|PDB:2PY5}.
STRAND 113 121 {ECO:0000244|PDB:2PY5}.
HELIX 122 125 {ECO:0000244|PDB:2PY5}.
HELIX 130 136 {ECO:0000244|PDB:2PY5}.
STRAND 148 150 {ECO:0000244|PDB:2PYL}.
HELIX 160 182 {ECO:0000244|PDB:2PY5}.
STRAND 187 189 {ECO:0000244|PDB:2PY5}.
HELIX 190 202 {ECO:0000244|PDB:2PY5}.
HELIX 204 210 {ECO:0000244|PDB:2PY5}.
HELIX 216 223 {ECO:0000244|PDB:2PY5}.
STRAND 231 233 {ECO:0000244|PDB:2PY5}.
HELIX 235 237 {ECO:0000244|PDB:2PY5}.
STRAND 238 242 {ECO:0000244|PDB:1XI1}.
STRAND 244 250 {ECO:0000244|PDB:2PY5}.
HELIX 253 260 {ECO:0000244|PDB:2PY5}.
STRAND 263 274 {ECO:0000244|PDB:2PY5}.
STRAND 283 294 {ECO:0000244|PDB:2PY5}.
STRAND 308 310 {ECO:0000244|PDB:2PYL}.
STRAND 324 329 {ECO:0000244|PDB:2PY5}.
HELIX 330 339 {ECO:0000244|PDB:2PY5}.
STRAND 340 357 {ECO:0000244|PDB:2PY5}.
HELIX 361 373 {ECO:0000244|PDB:2PY5}.
HELIX 376 387 {ECO:0000244|PDB:2PY5}.
HELIX 390 393 {ECO:0000244|PDB:2PY5}.
STRAND 401 406 {ECO:0000244|PDB:2PY5}.
STRAND 410 416 {ECO:0000244|PDB:2PY5}.
HELIX 427 447 {ECO:0000244|PDB:2PY5}.
TURN 448 451 {ECO:0000244|PDB:2PY5}.
STRAND 452 456 {ECO:0000244|PDB:2PY5}.
STRAND 459 466 {ECO:0000244|PDB:2PY5}.
HELIX 469 474 {ECO:0000244|PDB:2PY5}.
STRAND 477 479 {ECO:0000244|PDB:2PY5}.
STRAND 482 496 {ECO:0000244|PDB:2PY5}.
STRAND 499 509 {ECO:0000244|PDB:2PY5}.
STRAND 512 515 {ECO:0000244|PDB:2PY5}.
STRAND 518 520 {ECO:0000244|PDB:2PYJ}.
STRAND 522 530 {ECO:0000244|PDB:2PY5}.
HELIX 535 538 {ECO:0000244|PDB:2PY5}.
TURN 543 545 {ECO:0000244|PDB:2PY5}.
STRAND 551 561 {ECO:0000244|PDB:2PY5}.
STRAND 564 573 {ECO:0000244|PDB:2PY5}.
SEQUENCE 575 AA; 66714 MW; 856EEB6B04A7E268 CRC64;
MKHMPRKMYS CDFETTTKVE DCRVWAYGYM NIEDHSEYKI GNSLDEFMAW VLKVQADLYF
HNLKFDGAFI INWLERNGFK WSADGLPNTY NTIISRMGQW YMIDICLGYK GKRKIHTVIY
DSLKKLPFPV KKIAKDFKLT VLKGDIDYHK ERPVGYKITP EEYAYIKNDI QIIAEALLIQ
FKQGLDRMTA GSDSLKGFKD IITTKKFKKV FPTLSLGLDK EVRYAYRGGF TWLNDRFKEK
EIGEGMVFDV NSLYPAQMYS RLLPYGEPIV FEGKYVWDED YPLHIQHIRC EFELKEGYIP
TIQIKRSRFY KGNEYLKSSG GEIADLWLSN VDLELMKEHY DLYNVEYISG LKFKATTGLF
KDFIDKWTYI KTTSEGAIKQ LAKLMLNSLY GKFASNPDVT GKVPYLKENG ALGFRLGEEE
TKDPVYTPMG VFITAWARYT TITAAQACYD RIIYCDTDSI HLTGTEIPDV IKDIVDPKKL
GYWAHESTFK RAKYLRQKTY IQDIYMKEVD GKLVEGSPDD YTDIKFSVKC AGMTDKIKKE
VTFENFKVGF SRKMKPKPVQ VPGGVVLVDD TFTIK


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