ID   DPO1_RICCN              Reviewed;         875 AA.
AC   Q92GB7;
DT   20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=DNA polymerase I;
DE            Short=POL I;
DE            EC=2.7.7.7;
GN   Name=polA; OrderedLocusNames=RC1206;
OS   Rickettsia conorii (strain ATCC VR-613 / Malish 7).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Rickettsiaceae; Rickettsieae; Rickettsia; spotted fever group.
OX   NCBI_TaxID=272944;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-613 / Malish 7;
RX   PubMed=11557893; DOI=10.1126/science.1061471;
RA   Ogata H., Audic S., Renesto-Audiffren P., Fournier P.-E., Barbe V.,
RA   Samson D., Roux V., Cossart P., Weissenbach J., Claverie J.-M., Raoult D.;
RT   "Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
RL   Science 293:2093-2098(2001).
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; AE006914; AAL03744.1; -; Genomic_DNA.
DR   PIR; F97850; F97850.
DR   RefSeq; WP_010977771.1; NC_003103.1.
DR   AlphaFoldDB; Q92GB7; -.
DR   SMR; Q92GB7; -.
DR   EnsemblBacteria; AAL03744; AAL03744; RC1206.
DR   KEGG; rco:RC1206; -.
DR   PATRIC; fig|272944.4.peg.1381; -.
DR   HOGENOM; CLU_004675_0_0_5; -.
DR   OMA; NRPPMPD; -.
DR   Proteomes; UP000000816; 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..875
FT                   /note="DNA polymerase I"
FT                   /id="PRO_0000280950"
FT   DOMAIN          1..283
FT                   /note="5'-3' exonuclease"
SQ   SEQUENCE   875 AA;  99030 MW;  B0FC913759E5A7AF CRC64;
     MTQKNTLLLI DGYGFVFRAY YAQQPLTSPK GEPVGALYGF TSMLLKLLSD FKPKHVAVVF
     DSGGKNFRHQ IYPDYKANRP PPPEDLIIQL PLVRDVASNL NFPILEKNGY EADDIIATFA
     TKTAALGAHV VIISSDKDLL QLMTENIKIY DPLKGKYITE DDVVKKFGTT SDKLREVMAL
     IGDRSDNIPG VPSIGPKTAS SLITQFGSVE NIFNSLDQVS SVKQRETLQN SREAALISWQ
     LIGLNSNVDL DFQLNNLEWS PPNSDKLTGF LQEYGFRSLY KRVENLLDIK INDHKEIADS
     KVTEIKELNN ANELADFAKE ATKIGIFGIY LLQHKGANLA FILSLQNQSY IIKISNTSHD
     LFSYNTKSNN NWFSDIIFNL LTDKSIKKIT YSLKPLLKFY ANQSHDITAI EDLELMQYAL
     SAGLSQKNLF KEVLKETWIE NIIIESAKIV INFIALYKQT IWELKDNKTF RLYSNIDLPI
     CFILDKMEKV GITVDANYLK QLSAEFGTEI LKLEEEIFAL SGTKFNIGSP KQLGEILFEK
     MQLPFGKASA KASSYSTGAE ILEKLSEHGY NIADLLLRWR QLTKLKNTYT DSLPKQIDNI
     THRVHTTFLQ TSTTTGRLSS QEPNLQNVPI RSSEGNQIRK AFIAEEGYKL ISADYSQIEL
     RILSHIANID ALKQAFINKD DIHTQTACQI FNLQKHELTS EHRRKAKAIN FGIIYGISAF
     GLAKQLNVTN GEASEYIKKY FAEYKGVQEY MEQTKAFASS NGYVTNCFGR KCFVPLIHDK
     KLKQFAERAA INAPIQGTNT DIIKIAMINL DQEIEKRKLK TRLVLQIHDE LLFEAPIDEV
     EIITPIIKKI MENSTNMAVP IITEIRAGNN WMEIH