ID   DPO1F_THETH             Reviewed;         831 AA.
AC   P30313;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=DNA polymerase I, thermostable;
DE            EC=2.7.7.7;
DE   AltName: Full=Tfl polymerase 1;
GN   Name=polA; Synonyms=pol;
OS   Thermus thermophilus.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ACM B-1257;
RX   PubMed=1454544; DOI=10.1093/nar/20.21.5839;
RA   Akhmetzjanov A.A., Vakhitov V.A.;
RT   "Molecular cloning and nucleotide sequence of the DNA polymerase gene from
RT   Thermus flavus.";
RL   Nucleic Acids Res. 20:5839-5839(1992).
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   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Optimum temperature is above 70 degrees Celsius. Active up to 95
CC         degrees Celsius.;
CC   -!- BIOTECHNOLOGY: Used in the PCR method because of its high
CC       thermostability.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; X66105; CAA46900.1; -; Genomic_DNA.
DR   AlphaFoldDB; P30313; -.
DR   SMR; P30313; -.
DR   ChEMBL; CHEMBL3347254; -.
DR   PRIDE; P30313; -.
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   1: Evidence at protein level;
KW   DNA damage; DNA repair; DNA replication; DNA-binding;
KW   DNA-directed DNA polymerase; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..831
FT                   /note="DNA polymerase I, thermostable"
FT                   /id="PRO_0000101259"
FT   DOMAIN          174..258
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          409..831
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   831 AA;  93784 MW;  96F93CEFA3CA536D CRC64;
     MAMLPLFEPK GRVLLVDGHH LAYRTFFALK GLTTSRGEPV QAVYGFAKSL LKALKEDGDV
     VVVVFDAKAP SFRHEAYEAY KAGRAPTPED FPRQLALIKE LVDLLGLVRL EVPGFEADDV
     LATLAKRAEK EGYEVRILTA DRDLYQLLSE RIAILHPEGY LITPAWLYEK YGLRPEQWVD
     YRALAGDPSD NIPGVKGIGE KTAQRLIREW GSLENLFQHL DQVKPSLREK LQAGMEALAL
     SRKLSQVHTD LPLEVDFGRR RTPNLEGLRA FLERLEFGSL LHEFGLLEGP KAAEEAPWPP
     PEGAFLGFSF SRPEPMWAEL LALAGAWEGR LHRAQDPLRG LRDLKGVRGI LAKDLAVLAL
     REGLDLFPED DPMLLAYLLD PSNTTPEGVA RRYGGEWTED AGERALLAER LFQTLKERLK
     GEERLLWLYE EVEKPLSRVL ARMEATGVRL DVAYLQALSL EVEAEVRQLE EEVFRLAGHP
     FNLNSRDQLE RVLFDELGLP AIGKTEKTGK RSTSAAVLEA LREAHPIVDR ILQYRELTKL
     KNTYIDPLPA LVHPKTGRLH TRFNQTATAT GRLSSSDPNL QNIPVRTPLG QRIRRAFVAE
     EGWVLVVLDY SQIELRVLAH LSGDENLIRV FQEGRDIHTQ TASWMFGVSP EGVDPLMRRA
     AKTINFGVLY GMSAHRLSGE LSIPYEEAVA FIERYFQSYP KVRAWIEGTL EEGRRRGYVE
     TLFGRRRYVP DLNARVKSVR EAAERMAFNM PVQGTAADLM KLAMVRLFPR LQELGARMLL
     QVHDELVLEA PKDRAERVAA LAKEVMEGVW PLQVPLEVEV GLGEDWLSAK E