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Database: UniProt
Entry: A0A2A2GTG4_9HELI
LinkDB: A0A2A2GTG4_9HELI
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ID   A0A2A2GTG4_9HELI        Unreviewed;       905 AA.
AC   A0A2A2GTG4;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   RecName: Full=DNA polymerase I {ECO:0000256|ARBA:ARBA00020311, ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=B9T66_02210 {ECO:0000313|EMBL:PAV00482.1};
OS   Helicobacter sp. TUL.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=1848928 {ECO:0000313|EMBL:PAV00482.1, ECO:0000313|Proteomes:UP000218502};
RN   [1] {ECO:0000313|EMBL:PAV00482.1, ECO:0000313|Proteomes:UP000218502}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TUL {ECO:0000313|EMBL:PAV00482.1,
RC   ECO:0000313|Proteomes:UP000218502};
RA   Van Der Mee-Marquet N., Benejat L., Diene S.M., Gaia N., Cherkaoui A.,
RA   Lemaignen A., Ducournau A., Lacomme S., Gontier E., Bernard L., Megraud F.,
RA   Goudeau A., Lehours P., Francois P.;
RT   "Helicobacter caesarodunum: a novel human pathogen identified in a
RT   bloodstream infection.";
RL   Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: In addition to polymerase activity, this DNA polymerase
CC       exhibits 5'-3' exonuclease activity. {ECO:0000256|RuleBase:RU004460}.
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         Evidence={ECO:0000256|ARBA:ARBA00024632,
CC         ECO:0000256|RuleBase:RU004460};
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PAV00482.1}.
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DR   EMBL; NESU01000003; PAV00482.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2A2GTG4; -.
DR   Proteomes; UP000218502; Unassembled WGS sequence.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:UniProtKB-UniRule.
DR   CDD; cd08637; DNA_pol_A_pol_I_C; 1.
DR   CDD; cd06139; DNA_polA_I_Ecoli_like_exo; 1.
DR   CDD; cd09898; H3TH_53EXO; 1.
DR   CDD; cd09859; PIN_53EXO; 1.
DR   Gene3D; 3.30.70.370; -; 1.
DR   Gene3D; 1.10.150.20; 5' to 3' exonuclease, C-terminal subdomain; 2.
DR   Gene3D; 3.40.50.1010; 5'-nuclease; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 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   NCBIfam; TIGR00593; pola; 1.
DR   PANTHER; PTHR10133; DNA POLYMERASE I; 1.
DR   PANTHER; PTHR10133:SF62; DNA POLYMERASE THETA; 1.
DR   Pfam; PF01367; 5_3_exonuc; 1.
DR   Pfam; PF02739; 5_3_exonuc_N; 1.
DR   Pfam; PF00476; DNA_pol_A; 1.
DR   Pfam; PF01612; DNA_pol_A_exo1; 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; 5' to 3' exonuclease, C-terminal subdomain; 1.
DR   SUPFAM; SSF56672; DNA/RNA polymerases; 1.
DR   SUPFAM; SSF88723; PIN domain-like; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004460};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU004460};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705,
KW   ECO:0000256|RuleBase:RU004460};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004460};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932,
KW   ECO:0000256|RuleBase:RU004460}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000218502};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          1..260
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          317..498
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          669..869
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   905 AA;  103374 MW;  A495BC92EEF2A6AB CRC64;
     MKTLTIIDTF GFFFRSFYAL PPLKNKEGFP TGLLLGFCNL LNNLYKDKNC DYILFALEGQ
     GKNRRKILDP RYKQNRQEVP KELLLQLPIA IEWIQKMGFV NLSVDGYEAD DVIASVSVLA
     HKKGLNVRII SHDKDLYQLI DSQTYIYDPI KKIEIHEEQC QEKFGVLPCE FIDYQSLVGD
     SSDNVAGVKG IGAKSAQKLI KHFQNLESLY QRSDEIAQVL TPRLQKIILD SKDEAFLAKS
     LVTLVKDIPL EIDFAQCAMP SQNPLLTIVD ALHKYEFNGI LTKIQGPKYN SLSTAPSFKN
     ATLSQQISQS STFTYEYEMI DSQSTLFALI QSIPKDALIA FDTESDGLDT KEANIVGFSF
     SIDGHKGYYV PLGHTYLGVQ TQIDKQSAKV ALESIFSHTL IGHNLKFDIA LVYHNFGIKP
     QNTIIDTMVL AWLLDSAKPV GLDKQMLQWF GYKMISFEEI VDKKQTFANV DINLASQYAA
     EDAVATYCLY KRLKQEFEQR GLEPILELAR ELEFPFINVL VQMEMEGIKI DTTLFESYNK
     DFTKILHSLT QQIYECAGEN FNINSPQQLS QILFTKLGLQ SGRSVKGGLS TDEHTLSNIA
     HSHPIIPLVL DYREMNKLKN TYIEPLLKYA NKNAEHKIYT SFLQTGTVTG RLSSKSPNLQ
     NIPVRSEYGR KIRKGFIAKE GHKLISVDYS QIELRLLAHF SQDSHLIEAF KQQKDIHYET
     ALRLFGEDQA HNKRFIAKTI NFGLIYGMGA RKLSETLKIT HKEAKEYIES YFKLFPTVKD
     YLHNQKEFLL ENGYTQTLLG RRRYFDFSDA TEFMKANYIR EGINCIFQGS AADLIKLCMY
     KIYQHYQNTE LQMLLQVHDE LIFQAPESKV GEFLPHIESL MNSIYTLLVP LKCSVSVGDN
     WADLK
//
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