ID   DPO1_RHILE              Reviewed;        1016 AA.
AC   Q9S1G2;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 109.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA;
OS   Rhizobium leguminosarum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=384;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10341077; DOI=10.1007/pl00006816;
RA   Huang Y.-P., Downie J.A., Ito J.;
RT   "Primary structure of the DNA polymerase I gene of an alpha-
RT   Proteobacterium, Rhizobium leguminosarum, and comparison with other family
RT   A DNA polymerases.";
RL   Curr. Microbiol. 38:355-359(1999).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 3'-5' and 5'-3' exonuclease activity. {ECO:0000250}.
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; U86403; AAD45559.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9S1G2; -.
DR   SMR; Q9S1G2; -.
DR   STRING; 936136.ARRT01000006_gene5879; -.
DR   PRIDE; Q9S1G2; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
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   Pfam; PF01612; DNA_pol_A_exo1; 1.
DR   PRINTS; PR00868; DNAPOLI.
DR   SMART; SM00474; 35EXOc; 1.
DR   SMART; SM00475; 53EXOc; 1.
DR   SMART; SM00479; EXOIII; 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; Exonuclease; Hydrolase; Nuclease;
KW   Nucleotidyltransferase; Transferase.
FT   CHAIN           1..1016
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101248"
FT   DOMAIN          1..308
FT                   /note="5'-3' exonuclease"
FT   DOMAIN          394..630
FT                   /note="3'-5' exonuclease"
FT   REGION          334..361
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          768..1016
FT                   /note="Polymerase"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   1016 AA;  111493 MW;  35738F85B8C70514 CRC64;
     MPNSIWTSSD ARAIHARMKK GDHLFLVDGS GFIFRAFHAL PPLTRKTDGL PIGAVSGFCN
     MLWKLLRDAR NTDVGVTPTH LAVIFDYSAK TFRKDLYDAY KANRSAPPEE LIPQFGLIRE
     ATRAFNLPCI ETEGFEADDI IATYARQAEA TGADVTIVSS DKDLMQLVSP NVHMYDSMKD
     KQIGIPDVIE KWGVPPEKMI DLQAMTGDSV DNVPGIPGIG PKTAAQLLEE YGDLDTLLER
     ATEIKQVKRR ETILANIDMA RLSRDLVRLR TDVPLDLDLD ALVLEPQNGP KLIGFLKTME
     FTTLTRRVAE ACDCDASAIE PAIVRIEWGE TARGPDLDAA EPEPVAGGIP EVSGESVPMP
     PRAKAKSAVE GAFSPADLAK ARAEAFATLP FDHSAYVTIR DLVTLDRWIA DARATGLVAF
     DTETTSLDAM QAELVGFSLA IADNTADPTG TKIRAAYVPL VHKNGVGDLL GGGLADNQIP
     MRDALPRLKA LLEDESVLKV AQNLKYDYLL LKRYGIETRS FDDTMLISYV LDAGTGAHGM
     DPLSEKFLGH TPIPYKDVAG SGKANVTFDL VDIDRATHYA AEDADVTLRL WLVLKPRLAA
     AGLTSVYERL ERPLLPVLAR MEARGITVDR QILSRLSGEL AQGAARLEDE IYVLAGERFN
     IGSPKQLGDI LFGKMGLSGG SKTKTGQWST SAQVLEDLAA AGFELPRKIV DWRQVTKLKS
     TYTDALPGYV HPETKRVHTS YSLASTTTGR LSSSEPNLQN IPVRTAEGRK IRTAFISTPG
     HKLISADYSQ IELRVLAHVA EIPQLTKAFE DGVDIHAMTA SEMFGVPVEG MPGEVRRRAK
     AINFGIIYGI SAFGLANQLS IERSEAGDYI KKYFERFPGI RDYMESRKAM ARDKGYVETI
     FGRRINYPEI RSSNPSVRAF NERAAINAPI QGSAADVIRR AMIKIEPALV EVGLADRVRM
     LLQVHDELIF EVEDQDVEKA MPVIVSVMEN ATMPALEMRV PLRVDARAAT NWDEAH