ID   DPO1_RICHE              Reviewed;         921 AA.
AC   Q9RLB6;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA;
OS   Rickettsia helvetica.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=35789;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10486973; DOI=10.1093/oxfordjournals.molbev.a026208;
RA   Andersson J.O., Andersson S.G.E.;
RT   "Genome degradation is an ongoing process in Rickettsia.";
RL   Mol. Biol. Evol. 16:1178-1191(1999).
RN   [2]
RP   DOMAIN RPE1.
RX   PubMed=11030655; DOI=10.1126/science.290.5490.347;
RA   Ogata H., Audic S., Barbe V., Artiguenave F., Fournier P.-E., Raoult D.,
RA   Claverie J.-M.;
RT   "Selfish DNA in protein-coding genes of Rickettsia.";
RL   Science 290:347-350(2000).
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}.
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; AJ238762; CAB56073.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RLB6; -.
DR   SMR; Q9RLB6; -.
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; IPR005728; Rickett_RPE.
DR   InterPro; IPR012337; RNaseH-like_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; SSF53098; SSF53098; 1.
DR   SUPFAM; SSF56672; SSF56672; 1.
DR   SUPFAM; SSF88723; SSF88723; 1.
DR   TIGRFAMs; TIGR00593; pola; 1.
DR   TIGRFAMs; TIGR01045; RPE1; 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..921
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101250"
FT   DOMAIN          1..283
FT                   /note="5'-3' exonuclease"
FT   DOMAIN          439..486
FT                   /note="RPE1 insert"
SQ   SEQUENCE   921 AA;  104450 MW;  B0201F5E8E651242 CRC64;
     MTQKNTLLLI DGYGFVFRAY YAQQPLTSPK GEPVGALYGF TSMLLKLLSD FKPKHVAVVF
     DSGGKNFRHY IYPEYKANRP PPPEDLIVQL PLVRDVASNL NFPILEKNGY EADDIIATFA
     TKTAALGENV VIISSDKDLL QLMSENIKIY DPLRGKYITE DDVVKKFGTT SDKLREVMAL
     IGDRSDNIPG VPSIGPKTAS SLITQFGSVE NIFNSLDQVS SVKQRETLQN SREAALISWQ
     LIGLDSNVDL DFQLNNLEWS PPNSDKLTGF LQEYGFRSLY KRAENLFDIK INDHKDIVDN
     KVTEIKEISN KLELENFAKD AEKIGIFGIY LLQHKGDNLA FILSLQNQSY IIKISNTSHD
     LFSYNAKNNN DWFSDIIFNL LADKSIKKIT YSLKPLLKFY ANQSHEITAI EDLELMQYAL
     SAGLSQKNLF EEALKEDNRP LSKLAYREEF KGDTERSTAA YKSVREDAST GSTSKLPLEV
     EFGKRPIVIN ESARIVANFI SLYKQNILEL KDNKAFRLYS DIDLPICFIL DKMEKVGIKV
     DANYLKQLST EFGAEILKLE EEIFALSGTK FNIGSLKQLG EILFEKMQLP FGKASAKASS
     YSTGAEILEK LSEHGYNIAD LLLRWRQLTK LKNTYTDSLP KQIDNITHRV HTTFLQTSTT
     TGRLSSQEPN LQNVPIRSSE GNKIRQAFIA EEGYKLISAD YSQIELRILS HIANIDALKQ
     AFINKDDIHT QTACQIFNLQ KHELTNEHRR KAKAINFGII YGISAFGLAK QLNVTNGEAS
     EYIKKYFAEY KGVQEYMEQT KAFASSNGYV TNFFGRKCFV PLIHDKKLKQ FAERAAINAP
     IQGTNADIIK IAMINLDQEI EKRKLKTRLV LQIHDELLFE APIDEVEIII PIIKKIMEYS
     TNMDVPIITE IRTGNNWMEI H