ID   DPO1_RICBR              Reviewed;         871 AA.
AC   Q1RH76;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   16-MAY-2006, sequence version 1.
DT   03-AUG-2022, entry version 102.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=RBE_1207;
OS   Rickettsia bellii (strain RML369-C).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; belli group.
OX   NCBI_TaxID=336407;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RML369-C;
RX   PubMed=16703114; DOI=10.1371/journal.pgen.0020076;
RA   Ogata H., La Scola B., Audic S., Renesto P., Blanc G., Robert C.,
RA   Fournier P.-E., Claverie J.-M., Raoult D.;
RT   "Genome sequence of Rickettsia bellii illuminates the role of amoebae in
RT   gene exchanges between intracellular pathogens.";
RL   PLoS Genet. 2:733-744(2006).
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 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. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR   EMBL; CP000087; ABE05288.1; -; Genomic_DNA.
DR   RefSeq; WP_011477866.1; NC_007940.1.
DR   AlphaFoldDB; Q1RH76; -.
DR   SMR; Q1RH76; -.
DR   STRING; 336407.RBE_1207; -.
DR   EnsemblBacteria; ABE05288; ABE05288; RBE_1207.
DR   KEGG; rbe:RBE_1207; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_5; -.
DR   OMA; NRPPMPD; -.
DR   OrthoDB; 1220182at2; -.
DR   Proteomes; UP000001951; 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:0004527; F:exonuclease 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; 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; IPR036397; RNaseH_sf.
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   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; 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..871
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000280949"
FT   DOMAIN          1..283
FT                   /note="5'-3' exonuclease"
SQ   SEQUENCE   871 AA;  98632 MW;  8A4332119D6BD4FB CRC64;
     MTKKNTLLLI DGYGFVFRAY YAQQPLTSPK GEPVGALYGF TSMLLKLLND FKPKHAAVVF
     DSGGKNFRHE IYPEYKANRP PPPEDLIAQL PLVRDVARNL NFPILEKNGF EADDIIATFA
     AKTASIGEEV VVISSDKDLL QLMNDNVKIY DPLKAKYITE DNVVEKFGVT SDKLREVMAL
     IGDKSDNIPG VPSIGPKTAS SLITQFGTVE NIFNSLEQVS SIKQRETLQN SKEAALISWQ
     LIGLDYNVDM DFKLDALEWS PPDHNKLTEF LHEYGFKSLY KRAENLFDIK ISEHKEVIEE
     KAVEIKDISN KAELEAFAEK AKKVGIFGIY ILQNKGANIA FILSLKNQAY IIKISNEANN
     LFTYNSKADN EWFTDIIFNL LTDQSIKKIT YSLKPLLKFY ASRAQQITAI EDLELMNYAL
     SAGLPQKNLF EAVEKEATIE EAAKIVVGFI DLYQQTILEL KDNKAFRIYK EIDLPVCFVI
     DKMEKAGIKV DANYLNQLSS EFGAEILKLE EEIFVLSGMK FNIGSPKQLG EILFEKMQLP
     FGKTSAKANS YSTGADILEK LSEQGYPIAD LLLRWRQLTK LKNTYTDSLP KQIDNITRRI
     HTTFLQTSTT TGRLSSQEPN LQNVPIRSGE GNKIRQAFVA EQGYKLISAD YSQIELRILS
     HIADIKALKQ AFINKDDIHT QTACQIFNLQ KEELTSEHRR KAKAINFGII YGISAFGLAK
     QLNVSNTEAA EYIKKYFAEY KGVQEYMEAT KSFAQANGYV TDFFGRKCFV PLINDKRLKQ
     FAERAAINAP IQGTNADIIK IAMTLLDREI EKRKLKTRLV LQIHDELLFE APIDEIETIM
     PIIKQIMENS TNMDVPIITE IRAGNNWMEI H