ID   DPO1T_THET8             Reviewed;         834 AA.
AC   P52028; Q5SJF4;
DT   01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT   29-MAR-2005, sequence version 2.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=DNA polymerase I, thermostable;
DE            EC=2.7.7.7;
DE   AltName: Full=Tth polymerase 1;
GN   Name=polA; OrderedLocusNames=TTHA1054;
OS   Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8).
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=300852;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Asakura K., Komatsubara H., Soga S., Yomo T., Oka M., Emi S., Urabe I.;
RT   "Cloning, nucleotide sequence, and expression in Escherichia coli of DNA
RT   polymerase gene (polA) from Thermus thermophilus HB8.";
RL   J. Ferment. Bioeng. 76:265-269(1993).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 27634 / DSM 579 / HB8;
RA   Masui R., Kurokawa K., Nakagawa N., Tokunaga F., Koyama Y., Shibata T.,
RA   Oshima T., Yokoyama S., Yasunaga T., Kuramitsu S.;
RT   "Complete genome sequence of Thermus thermophilus HB8.";
RL   Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
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;
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; D28878; BAA06033.1; -; Genomic_DNA.
DR   EMBL; AP008226; BAD70877.1; -; Genomic_DNA.
DR   RefSeq; WP_011228405.1; NC_006461.1.
DR   RefSeq; YP_144320.1; NC_006461.1.
DR   AlphaFoldDB; P52028; -.
DR   SMR; P52028; -.
DR   STRING; 300852.55772436; -.
DR   EnsemblBacteria; BAD70877; BAD70877; BAD70877.
DR   GeneID; 3169068; -.
DR   KEGG; ttj:TTHA1054; -.
DR   PATRIC; fig|300852.9.peg.1034; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_0; -.
DR   OMA; NRPPMPD; -.
DR   PhylomeDB; P52028; -.
DR   Proteomes; UP000000532; Chromosome.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProt.
DR   GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR020046; 5-3_exonucl_a-hlix_arch_N.
DR   InterPro; IPR002421; 5-3_exonuclease.
DR   InterPro; IPR036279; 5-3_exonuclease_C_sf.
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; IPR020045; DNA_polI_H3TH.
DR   InterPro; IPR018320; DNA_polymerase_1.
DR   InterPro; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   InterPro; IPR015361; Taq_pol_thermo_exonuc.
DR   PANTHER; PTHR10133; PTHR10133; 2.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF09281; Taq-exonuc; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; SSF47807; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..834
FT                   /note="DNA polymerase I, thermostable"
FT                   /id="PRO_0000101258"
FT   DOMAIN          176..262
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          412..834
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        453
FT                   /note="L -> R (in Ref. 1; BAA06033)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   834 AA;  94006 MW;  2C9C83F390B92504 CRC64;
     MEAMLPLFEP KGRVLLVDGH HLAYRTFFAL KGLTTSRGEP VQAVYGFAKS LLKALKEDGY
     KAVFVVFDAK APSFRHEAYE AYKAGRAPTP EDFPRQLALI KELVDLLGFT RLEVPGYEAD
     DVLATLAKKA EKEGYEVRIL TADRDLYQLV SDRVAVLHPE GHLITPEWLW EKYGLRPEQW
     VDFRALVGDP SDNLPGVKGI GEKTALKLLK EWGSLENLLK NLDRVKPENV REKIKAHLED
     LRLSLELSRV RTDLPLEVDL AQGREPDREG LRAFLERLEF GSLLHEFGLL EAPAPLEEAP
     WPPPEGAFVG FVLSRPEPMW AELKALAACR DGRVHRAADP LAGLKDLKEV RGLLAKDLAV
     LASREGLDLV PGDDPMLLAY LLDPSNTTPE GVARRYGGEW TEDAAHRALL SERLHRNLLK
     RLEGEEKLLW LYHEVEKPLS RVLAHMEATG VRLDVAYLQA LSLELAEEIR RLEEEVFRLA
     GHPFNLNSRD QLERVLFDEL RLPALGKTQK TGKRSTSAAV LEALREAHPI VEKILQHREL
     TKLKNTYVDP LPSLVHPRTG RLHTRFNQTA TATGRLSSSD PNLQNIPVRT PLGQRIRRAF
     VAEAGWALVA LDYSQIELRV LAHLSGDENL IRVFQEGKDI HTQTASWMFG VPPEAVDPLM
     RRAAKTVNFG VLYGMSAHRL SQELAIPYEE AVAFIERYFQ SFPKVRAWIE KTLEEGRKRG
     YVETLFGRRR YVPDLNARVK SVREAAERMA FNMPVQGTAA DLMKLAMVKL FPRLREMGAR
     MLLQVHDELL LEAPQARAEE VAALAKEAME KAYPLAVPLE VEVGMGEDWL SAKG