ID   DPO1_RICFE              Reviewed;         922 AA.
AC   Q9RAA9; Q4UK45;
DT   11-JUL-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-2000, sequence version 1.
DT   27-MAR-2024, entry version 137.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=RF_1239;
OS   Rickettsia felis (strain ATCC VR-1525 / URRWXCal2) (Rickettsia azadi).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=315456;
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   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-1525 / URRWXCal2;
RX   PubMed=15984913; DOI=10.1371/journal.pbio.0030248;
RA   Ogata H., Renesto P., Audic S., Robert C., Blanc G., Fournier P.-E.,
RA   Parinello H., Claverie J.-M., Raoult D.;
RT   "The genome sequence of Rickettsia felis identifies the first putative
RT   conjugative plasmid in an obligate intracellular parasite.";
RL   PLoS Biol. 3:1-12(2005).
RN   [3]
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}.
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DR   EMBL; AJ238763; CAB56067.1; -; Genomic_DNA.
DR   EMBL; CP000053; AAY62090.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9RAA9; -.
DR   SMR; Q9RAA9; -.
DR   STRING; 315456.RF_1239; -.
DR   KEGG; rfe:RF_1239; -.
DR   eggNOG; COG0258; Bacteria.
DR   eggNOG; COG0749; Bacteria.
DR   HOGENOM; CLU_004675_0_0_5; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000008548; 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; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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; IPR005728; RPE1.
DR   NCBIfam; TIGR00593; pola; 1.
DR   NCBIfam; TIGR01045; RPE1; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 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; SM00475; 53EXOc; 1.
DR   SMART; SM00279; HhH2; 1.
DR   SMART; SM00482; POLAc; 1.
DR   SUPFAM; SSF47807; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 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..922
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000101249"
FT   DOMAIN          1..283
FT                   /note="5'-3' exonuclease"
FT   DOMAIN          439..487
FT                   /note="RPE1 insert"
SQ   SEQUENCE   922 AA;  104006 MW;  EA47F799536948A0 CRC64;
     MTQKNTLLLI DGYGFVFRAY YAQQPLTSPK GEPVGALYGF ASMLLKLLSD FKPKHVAVVF
     DSGGKNFRHH IYPEYKANRP PPPEDLVVQL PLVRDVASNL NFPILEKNGY EADDIIATFA
     AKTAALGEDV VVISSDKDLL QLMGENIKIY DPLKGKYITE DDVVKKFGTT SDKLREVMAL
     IGDRSDNIPG VPSIGPKTAS SLITQFGSVE NIFNSLEQVS SLKQRETLQN SKEAALISWQ
     LIGLDSNVDL DFQLNNLEWS PPNSDKLTGF LQEYGFKSLY KRAENLFDIK INDHKEIVEN
     KVTEAKEISN ASELADFAKK AEKIGIFGIY LLQHKGDNVA LILSLQNQSY IIKISNTSHD
     LFSYNTKNNN DWFSDIIFNL LTDKSIRKIT YSLKPLLKFY AEQSHEITAI EDLELMQYAL
     SAGLSQKNLF EEALKEDNRH LSKPAYREEF KGDTEALATA AYKSVREDAS TGSTSKLPLE
     TKFGKMSNVI NESARIVAEF TSLYKQNILE LKDNKAFRLY SNIDLPICFI LDKMEKIGIK
     VDANYLNQLS AEFGAEILKL EEEIFALSGT KFNIGSPKQL GEILFEKMQL PFGKASAKAS
     SYSTGAEILE KLSEHGYNIA DLLLRWRQLT KLKNTYTDSL PKQIDNITHR VHTTFLQTST
     TTGRLSSQEP NLQNVPIRSS EGNKIRQAFI AEEGYKLISA DYSQIELRIL SHIANIDALK
     QAFINKDDIH TQTACQIFNL QKHELTSEHR RKAKAINFGI IYGISAFGLA KQLNVSNGEA
     SEYIKKYFAE YKGVQEYMEQ TKAFASSNGY VINFFGRKCF VPLIHDKKLK QFAERAAINA
     PIQGTNADII KIAMINLDQE IEKNNLKTRL VLQIHDELLF EVPEDEVELV TPIIKKIMEN
     STNMDVPIIT EIRVGNNWME IH
//