DPO1_RICFE
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 03-AUG-2022, entry version 130.
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; Proteobacteria; 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 RefSeq; WP_011271539.1; NC_007109.1.
DR AlphaFoldDB; Q9RAA9; -.
DR SMR; Q9RAA9; -.
DR STRING; 315456.RF_1239; -.
DR EnsemblBacteria; AAY62090; AAY62090; RF_1239.
DR KEGG; rfe:RF_1239; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_5; -.
DR OMA; NRPPMPD; -.
DR OrthoDB; 1220182at2; -.
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; 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; 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; 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..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