DPO1_RICTY
ID DPO1_RICTY Reviewed; 872 AA.
AC Q9RLA0;
DT 20-MAR-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=RT0763;
OS Rickettsia typhi (strain ATCC VR-144 / Wilmington).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC Rickettsiaceae; Rickettsieae; Rickettsia; typhus group.
OX NCBI_TaxID=257363;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC VR-144 / Wilmington;
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-144 / Wilmington;
RX PubMed=15317790; DOI=10.1128/jb.186.17.5842-5855.2004;
RA McLeod M.P., Qin X., Karpathy S.E., Gioia J., Highlander S.K., Fox G.E.,
RA McNeill T.Z., Jiang H., Muzny D., Jacob L.S., Hawes A.C., Sodergren E.,
RA Gill R., Hume J., Morgan M., Fan G., Amin A.G., Gibbs R.A., Hong C.,
RA Yu X.-J., Walker D.H., Weinstock G.M.;
RT "Complete genome sequence of Rickettsia typhi and comparison with sequences
RT of other Rickettsiae.";
RL J. Bacteriol. 186:5842-5855(2004).
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; AJ238757; CAB56108.1; -; Genomic_DNA.
DR EMBL; AE017197; AAU04219.1; -; Genomic_DNA.
DR RefSeq; WP_011191194.1; NC_006142.1.
DR AlphaFoldDB; Q9RLA0; -.
DR SMR; Q9RLA0; -.
DR STRING; 257363.RT0763; -.
DR EnsemblBacteria; AAU04219; AAU04219; RT0763.
DR KEGG; rty:RT0763; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_5; -.
DR OMA; NRPPMPD; -.
DR OrthoDB; 1220182at2; -.
DR Proteomes; UP000000604; 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; 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; 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..872
FT /note="DNA polymerase I"
FT /id="PRO_0000280951"
FT DOMAIN 1..283
FT /note="5'-3' exonuclease"
SQ SEQUENCE 872 AA; 99310 MW; BC2EBE3490879A08 CRC64;
MTKKNTLLLI DGYGFVFRAY YAQQSLSSAK GEPVGALYGF TSMLLKLLSD FKPQYGAIVF
DSGGKNFRHK IYQNYKANRP TPPEDLIGQL PLIRDVASHL NFAILEKNGY EADDIIATFA
TKTITLGKEV IIISSDKDLL QLMSKNIKIY DPIKCKYITE DDVIIKFGTT PDKLREVMAL
IGDRSDNIPG VPSIGPKTAS SLITQFGSVE NIFNSLDQIS SIKQRKTLQN SREAALISWR
LIGLDSNVDL DFNLNNLEWS HPNSEKLIGF LQKYGFKSLY KRVENLFYIK INDHEEIVDN
KVTEAKEISN ASELENFAKE AEKIGIFGIY LLQQKGNNCA LILSLQNQSY IIKITNNNLF
PYNDNIKNNN DWFSYIILNL LTNKSIKKIT YSLKHLLKFY ANQSHKITAI EDLELMQYTL
SAGLVQKNLF AETLTKDNII NESAKIVINF ISLYKQTLLA LQKNKAFRLY REIDLPTCFI
LDKMEKIGIK VDANYLHQLS DEFGTEILKI EEEIFALSGT KFNIASQKQL SEILFKKMQL
PSGNTLAKTS SYSTKAGILK KLSEDGYHIA TLLLRWRQLT KLKNTYTDSL PKQINNITKR
IHTTFLQTST TTGRLSSQEP NLQNIPTRSS DGNKIRQAFI AEDGYKLISA DYSQIELRIL
SHIANVDVLK QAFINKEDIH TQTACQIFNL QKHELTSEHR RKAKAINFGI IYGISAFGLA
KQLNVSNGTA AEYIKQYFAE YKGMQEYMVQ TKAYANRNGY VTNFFGRKCF IPLIHDKKLK
QFAERAAINA PIQGTSADII KIAMIKLAQE IEKRKLKTRL ILQIHDELLF EVPEIELELV
IPIIKKIMEY STNIDVPIIT EIRAGNNWKE IH