DPO1_HELPY
ID DPO1_HELPY Reviewed; 891 AA.
AC P56105;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=DNA polymerase I;
DE Short=POL I;
DE EC=2.7.7.7;
GN Name=polA; OrderedLocusNames=HP_1470;
OS Helicobacter pylori (strain ATCC 700392 / 26695) (Campylobacter pylori).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=85962;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700392 / 26695;
RX PubMed=9252185; DOI=10.1038/41483;
RA Tomb J.-F., White O., Kerlavage A.R., Clayton R.A., Sutton G.G.,
RA Fleischmann R.D., Ketchum K.A., Klenk H.-P., Gill S.R., Dougherty B.A.,
RA Nelson K.E., Quackenbush J., Zhou L., Kirkness E.F., Peterson S.N.,
RA Loftus B.J., Richardson D.L., Dodson R.J., Khalak H.G., Glodek A.,
RA McKenney K., FitzGerald L.M., Lee N., Adams M.D., Hickey E.K., Berg D.E.,
RA Gocayne J.D., Utterback T.R., Peterson J.D., Kelley J.M., Cotton M.D.,
RA Weidman J.F., Fujii C., Bowman C., Watthey L., Wallin E., Hayes W.S.,
RA Borodovsky M., Karp P.D., Smith H.O., Fraser C.M., Venter J.C.;
RT "The complete genome sequence of the gastric pathogen Helicobacter
RT pylori.";
RL Nature 388:539-547(1997).
CC -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC exhibits 3'-5' and 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.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-A family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD08510.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE000511; AAD08510.1; ALT_INIT; Genomic_DNA.
DR PIR; F64703; F64703.
DR RefSeq; NP_208261.1; NC_000915.1.
DR RefSeq; WP_000437576.1; NC_000915.1.
DR AlphaFoldDB; P56105; -.
DR SMR; P56105; -.
DR DIP; DIP-3098N; -.
DR IntAct; P56105; 5.
DR MINT; P56105; -.
DR STRING; 85962.C694_07610; -.
DR PaxDb; P56105; -.
DR EnsemblBacteria; AAD08510; AAD08510; HP_1470.
DR KEGG; hpy:HP_1470; -.
DR PATRIC; fig|85962.47.peg.1581; -.
DR eggNOG; COG0258; Bacteria.
DR eggNOG; COG0749; Bacteria.
DR OMA; NRPPMPD; -.
DR PhylomeDB; P56105; -.
DR Proteomes; UP000000429; Chromosome.
DR GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
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: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; IPR002562; 3'-5'_exonuclease_dom.
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 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; SM00474; 35EXOc; 1.
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..891
FT /note="DNA polymerase I"
FT /id="PRO_0000101241"
FT DOMAIN 1..313
FT /note="5'-3' exonuclease"
FT DOMAIN 314..488
FT /note="3'-5' exonuclease"
FT REGION 492..890
FT /note="Polymerase"
SQ SEQUENCE 891 AA; 101975 MW; 3D6E7D8FF613EB88 CRC64;
MEQPVIKEGT LALIDTFAYL FRSYYMSAKN KPLTNDKGFP TGLLTGLVGM VKKFYKDRKN
MPFIVFALES QTKTKRAEKL GEYKQNRKDA PKEMLLQIPI ALEWLQKMGF VCVEVNGFEA
DDVIASLATL SPYKTRIYSK DKDFNQLLSD KIALFDGKTE FLAKDCVEKY GILPSQFTDY
QGIVGDSSDN YKGVKGIGSK NAKELLQRLG SLEKIYENLD LAKNLLSPKM YRALIHDKAS
AFLSKELATL ERGCIKEFDF LSCAFPSENP LLKIKDELKE YGFISTLRDL ENSPTPLILD
NAPLLDNTPA LDNTPKKSCM IVLESAAPLS AFLEKLEKTN ARVFARLVLD KEKKVLALAF
LYEDQGYFLP LEEALFSPFS LEFLQNAFFK MLQHAQIIGH DLKPLLSFLK AKYQVPLENI
RIQDTQILAF LKNPEKVGFD EVLKEYLKEE LIPHEKIKDF KTKAEKLELL SVELNALKRL
CEYFEKGGLE ENLLSLAREI ETPFMKVLMG MEFQGFKIDA PYFKRLEQEF KNELHVLERQ
ILELIGVDFN LNSPKQLSEV LYDKLGLPKN KSHSTDEKSL LKILDKHPSI ALILEYRELN
KLFNTYTTPL LRLKDKDDKI HTTFIQTGTA TGRLSSHSPN LQNIPVRSPK GLLIRKGFIA
SSKEYCLLGV DYSQIELRLL AHFSQDKDLM EAFLKGRDIH LETSKALFGE YLAKEKRSIA
KSINFGLVYG MGSKKLSETL NISLNEAKSY IEAYFKRFPS IKDYLNRMKE EILKTSKAFT
LLGRYRVFDF TGANDYVKGN YLREGVNAIF QGSASDLLKL GMLKVSERFK NNPSVRLLLQ
VHDELIFEIE EKNAPELQQE IQRILNDEVY PLRVPLETSA FIAKRWNELK G
