ID   DPO1_BACCA              Reviewed;         877 AA.
AC   Q04957;
DT   01-OCT-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1993, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA;
OS   Bacillus caldotenax.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus;
OC   Geobacillus thermoleovorans group.
OX   NCBI_TaxID=1395;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-15.
RX   PubMed=8486614; DOI=10.1093/oxfordjournals.jbchem.a124058;
RA   Uemori T., Ishino Y., Fujita K., Asada K., Kato I.;
RT   "Cloning of the DNA polymerase gene of Bacillus caldotenax and
RT   characterization of the gene product.";
RL   J. Biochem. 113:401-410(1993).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 5'-3' exonuclease 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   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; D12982; BAA02361.1; -; Genomic_DNA.
DR   PIR; JX0256; JX0256.
DR   PDB; 2HHX; X-ray; 2.26 A; A=298-877.
DR   PDBsum; 2HHX; -.
DR   AlphaFoldDB; Q04957; -.
DR   SMR; Q04957; -.
DR   EvolutionaryTrace; Q04957; -.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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: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; IPR002562; 3'-5'_exonuclease_dom.
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   PANTHER; PTHR10133; PTHR10133; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
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   3D-structure; Direct protein sequencing; DNA damage; DNA repair;
KW   DNA replication; DNA-binding; DNA-directed DNA polymerase; Exonuclease;
KW   Hydrolase; Nuclease; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..877
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101233"
FT   DOMAIN          1..310
FT                   /note="5'-3' exonuclease"
FT   DOMAIN          311..465
FT                   /note="3'-5' exonuclease"
FT   REGION          469..877
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   877 AA;  99475 MW;  DA5FC7F5B6DFA6F4 CRC64;
     MKKKLVLIDG SSVAYRAFFA LPLLHNDKGI HTNAVYGFTM MLNKILAEEE PTHMLVAFDA
     GKTTFRHEAF QEYKGGRQQT PPELSEQFPL LRELLRAYRI PAYELENYEA DDIIGTLAAR
     AEQEGFEVKV ISGDRDLTQL ASPHVTVDIT KKGITDIEPY TPEAVREKYG LTPEQIVDLK
     GLMGDKSDNI PGVPGIGEKT AVKLLRQFGT VENVLASIDE IKGEKLKETL RQHREMALLS
     KKLAAIRRDA PVELSLDDIA YQGEDREKVV ALFKELGFQS FLEKMESPSS EEEKPLAKMA
     FTLADRVTEE MLADKAALVV EVVEENYHDA PIVGIAVVNE HGRFFLRPET ALADPQFVAW
     LGDETKKKSM FDSKRAAVAL KWKGIELCGV SFDLLLAAYL LDPAQGVDDV AAAAKMKQYE
     AVRPDEAVYG KGAKRAVPDE PVLAEHLVRK AAAIWALERP FLDELRRNEQ DRLLVELEQP
     LSSILAEMEF AGVKVDTKRL EQMGEELAEQ LRTVEQRIYE LAGQEFNINS PKQLGVILFE
     KLQLPVLKKS KTGYSTSADV LEKLAPYHEI VENILQHYRQ LGKLQSTYIE GLLKVVRPDT
     KKVHTIFNQA LTQTGRLSST EPNLQNIPIR LEEGRKIRQA FVPSESDWLI FAADYSQIEL
     RVLAHIAEDD NLMEAFRRDL DIHTKTAMDI FQVSEDEVTP NMRRQAKAVN FGIVYGISDY
     GLAQNLNISR KEAAEFIERY FESFPGVKRY MENIVQEAKQ KGYVTTLLHR RRYLPDITSR
     NFNVRSFAER MAMNTPIQGS AADIIKKAMI DLNARLKEER LQARLLLQVH DELILEAPKE
     EMERLCRLVP EVMEQAVTLR VPLKVDYHYG STWYDAK