ID   DPO1_THEFI              Reviewed;         833 AA.
AC   O52225;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1998, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=DNA polymerase I, thermostable;
DE            EC=2.7.7.7;
DE   AltName: Full=TFI polymerase 1;
GN   Name=polA; Synonyms=pol;
OS   Thermus filiformis.
OC   Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX   NCBI_TaxID=276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9509419;
RA   Jung S.E., Choi J.J., Kim H.K., Kwon S.-T.;
RT   "Cloning and analysis of the DNA polymerase-encoding gene from Thermus
RT   filiformis.";
RL   Mol. Cells 7:769-776(1997).
CC   -!- FUNCTION: Has 5'-3' exonuclease activity and no 3'-5' exonuclease
CC       activity.
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         Thermostable.;
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AF030320; AAC46079.1; -; Genomic_DNA.
DR   RefSeq; WP_038067428.1; NZ_JPSL02000039.1.
DR   AlphaFoldDB; O52225; -.
DR   SMR; O52225; -.
DR   STRING; 276.THFILI_06865; -.
DR   PRIDE; O52225; -.
DR   OrthoDB; 1220182at2; -.
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..833
FT                   /note="DNA polymerase I, thermostable"
FT                   /id="PRO_0000101260"
FT   DOMAIN          173..267
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000255"
FT   REGION          412..833
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   833 AA;  93891 MW;  51BF8B0417EEFC4D CRC64;
     MTPLFDLEEP PKRVLLVDGH HLAYRTFYAL SLTTSRGEPV QMVYGFARSL LKALKEDGQA
     VVVVFDAKAP SFRHEAYEAY KAGRAPTPED FPRQLALVKR LVDLLGLVRL EAPGYEADDV
     LGTLAKKAER EGMEVRILTG DRDFFQLLSE KVSVLLPDGT LVTPKDVQEK YGVPPERWVD
     FRALTGDRSD NIPGVAGIGE KTALRLLAEW GSVENLLKNL DRVKPDSLRR KIEAHLEDLH
     LSLDLARIRT DLPLEVDFKA LRRRTPDLEG LRAFLEELEF GSLLHEFGLL GGEKPREEAP
     WPPPEGAFVG FLLSRKEPMW AELLALAAAS EGRVHRATSP VEALADLKEA RGFLAKDLAV
     LALREGVALD PTDDPLLVAY LLDPANTHPE GVARRYGGEF TEDAAERALL SERLFQNLFP
     RLSEKLLWLY QEVERPLSRV LAHMEARGVR LDVPLLEALS FELEKEMERL EGEVFRLAGH
     PFNLNSRDQL ERVLFDELGL TPVGRTEKTG KRSTAQGALE ALRGAHPIVE LILQYRELSK
     LKSTYLDPLP RLVHPRTGRL HTRFNQTATA TGRLSSSDPN LQNIPVRTPL GQRIRKAFVA
     EEGWLLLAAD YSQIELRVLA HLSGDENLKR VFREGKDIHT ETAAWMFGLD PALVDPKMRR
     AAKTVNFGVL YGMSAHRLSQ ELGIDYKEAE AFIERYFQSF PKVRAWIERT LEEGRTRGYV
     ETLFGRRRYV PDLASRVRSV REAAERMAFN MPVQGTAADL MKIAMVKLFP RLKPLGAHLL
     LQVHDELVLE VPEDRAEEAK ALVKEVMENA YPLDVPLEVE VGVGRDWLEA KQD