DPO1_DEIRA
ID DPO1_DEIRA Reviewed; 956 AA.
AC P52027;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=DR_1707;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / LMG
OS 4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC Bacteria; Deinococcus-Thermus; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 36-956.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=8501062; DOI=10.1128/jb.175.11.3581-3590.1993;
RA Gutman P.D., Fuchs P., Ouyang L., Minton K.W.;
RT "Identification, sequencing, and targeted mutagenesis of a DNA polymerase
RT gene required for the extreme radioresistance of Deinococcus radiodurans.";
RL J. Bacteriol. 175:3581-3590(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / LMG 4051 / NBRC 15346 / NCIMB
RC 9279 / R1 / VKM B-1422;
RX PubMed=19303848; DOI=10.1016/j.cell.2009.01.018;
RA Slade D., Lindner A.B., Paul G., Radman M.;
RT "Recombination and replication in DNA repair of heavily irradiated
RT Deinococcus radiodurans.";
RL Cell 136:1044-1055(2009).
CC -!- FUNCTION: A DNA polymerase, required for DNA repair after DNA damage
CC induced by ionizing radiation (IR); this is not the major DNA
CC polymerase (PubMed:19303848). Following severe irradiation (7 kGy of
CC gamma irradiation) genomic DNA is fragmented. DNA is progressively
CC degraded for the first 1.5 hours after IR, in a step promoted by RecA
CC and counterbalanced by DNA Pol I and Pol III, followed by massive DNA
CC synthesis and genome reassembly in the next hour. Optimal priming of
CC DNA synthesis requires both RecA and RadA, Pol III initiates DNA
CC synthesis while both Pol I and Pol III are required for its contination
CC (PubMed:19303848). May also have 5'-3' exonuclease activity (By
CC similarity). {ECO:0000250|UniProtKB:P00582,
CC ECO:0000269|PubMed:19303848}.
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.
CC -!- DISRUPTION PHENOTYPE: Increased sensitivity to ionizing radiation (IR),
CC lag time before DNA synthesis/repair commences increases considerably,
CC decreased rates of both DNA synthesis and DNA repair following IR. If
CC combined with a temperature-senstitive mutation in dnaE (catalytic
CC subunit of Pol III) viability at 37 degrees is dramatically reduced
CC (PubMed:19303848). {ECO:0000269|PubMed:19303848}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
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DR EMBL; L14581; AAC36974.1; -; Unassigned_DNA.
DR EMBL; AE000513; AAF11264.1; -; Genomic_DNA.
DR PIR; A40597; A40597.
DR RefSeq; NP_295430.1; NC_001263.1.
DR RefSeq; WP_010888342.1; NZ_CP015081.1.
DR AlphaFoldDB; P52027; -.
DR SMR; P52027; -.
DR STRING; 243230.DR_1707; -.
DR EnsemblBacteria; AAF11264; AAF11264; DR_1707.
DR KEGG; dra:DR_1707; -.
DR PATRIC; fig|243230.17.peg.1918; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR HOGENOM; CLU_004675_0_0_0; -.
DR InParanoid; P52027; -.
DR OMA; NRPPMPD; -.
DR OrthoDB; 1220182at2; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0003887; F:DNA-directed DNA polymerase activity; IBA:GO_Central.
DR GO; GO:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0001882; F:nucleoside binding; IEA:InterPro.
DR GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
DR GO; GO:0006302; P:double-strand break repair; IBA:GO_Central.
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; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR InterPro; IPR015361; Taq_pol_thermo_exonuc.
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 Pfam; PF09281; Taq-exonuc; 2.
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 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; Reference proteome; Transferase.
FT CHAIN 1..956
FT /note="DNA polymerase I"
FT /id="PRO_0000101238"
FT DOMAIN 209..296
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000255"
FT CONFLICT 48
FT /note="T -> A (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
FT CONFLICT 77
FT /note="H -> D (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
FT CONFLICT 108
FT /note="F -> L (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
FT CONFLICT 128
FT /note="P -> R (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="P -> R (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
FT CONFLICT 540
FT /note="L -> V (in Ref. 1; AAC36974)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 956 AA; 105660 MW; 6ABBF117D75AB84A CRC64;
MVFCGDGGLS CESIDFALCC LRGRSGNYVQ SRILPMADAS PDPSKPDTLV LIDGHALAFR
SYFALPPLNN SKGEMTHAIV GFMKLLLRLA RQKSNQVIVV FDPPVKTFRH EQYEGYKSGR
AQTPEDLPGQ INRIRALVDA LGFPRLEEPG YEADDVIASL TRMAEGKGYE VRIVTSDRDA
YQLLDEHVKV IANDFSLIGP AQVEEKYGVT VRQWVDYRAL TGDASDNIPG AKGIGPKTAA
KLLQEYGTLE KVYEAAHAGT LKPDGTRKKL LDSEENVKFS HDLSCMVTDL PLDIEFGVRR
LPDNPLVTED LLTELELHSL RPMILGLNGP EQDGHAPDDL LEREHAQTPE EDEAAALPAF
SAPELAEWQT PAEGAVWGYV LSREDDLTAA LLAAATFEDG VARPAPVSEP DEWAQAEAPE
NLFGELLPSD KPLTKKEQKA LEKAQKDAEK ARAKLREQFP ATVDEAEFVG QRTVTAAAAK
ALAAHLSVRG TVVEPGDDPL LYAYLLDPAN TNMPVVAKRY LDREWPADAP TRAAITGHLL
RELPPLLDDA RRKMYDEMEK PLSGVLGRME VRGVQVDSDF LQTLSIQAGV RLADLESQIH
EYAGEEFHIR SPKQLETVLY DKLELASSKK TKLTGQRSTA VSALEPLRDA HPIIPLVLEF
RELDKLRGTY LDPIPNLVNP HTGRLHTTFA QTAVATGRLS SLNPNLQNIP IRSELGREIR
KGFIAEDGFT LIAADYSQIE LRLLAHIADD PLMQQAFVEG ADIHRRTAAQ VLGLDEATVD
ANQRRAAKTV NFGVLYGMSA HRLSNDLGIP YAEAATFIEI YFATYPGIRR YINHTLDFGR
THGYVETLYG RRRYVPGLSS RNRVQREAEE RLAYNMPIQG TAADIMKLAM VQLDPQLDAI
GARMLLQVHD ELLIEAPLDK AEQVAALTKK VMENVVQLKV PLAVEVGTGP NWFDTK
