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Entry: A0A2T5HN19_9PSED
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ID   A0A2T5HN19_9PSED        Unreviewed;       986 AA.
AC   A0A2T5HN19;
DT   18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT   18-JUL-2018, 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=C8K61_102158 {ECO:0000313|EMBL:PTQ72949.1};
OS   Pseudomonas sp. GV071.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=2135754 {ECO:0000313|EMBL:PTQ72949.1, ECO:0000313|Proteomes:UP000244119};
RN   [1] {ECO:0000313|EMBL:PTQ72949.1, ECO:0000313|Proteomes:UP000244119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GV071 {ECO:0000313|EMBL:PTQ72949.1,
RC   ECO:0000313|Proteomes:UP000244119};
RA   Pelletier D.;
RT   "Populus root and rhizosphere microbial communities from Tennessee, USA.";
RL   Submitted (APR-2018) 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   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC       {ECO:0000256|ARBA:ARBA00011541}.
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:PTQ72949.1}.
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DR   EMBL; QAOJ01000002; PTQ72949.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2T5HN19; -.
DR   Proteomes; UP000244119; 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};
KW   Exonuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Nuclease {ECO:0000256|ARBA:ARBA00022839};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000244119};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          52..314
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          379..574
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          744..950
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   986 AA;  107906 MW;  D7822391264E694B CRC64;
     MKLLTRHSGA FDLLASDYKS QSLRRPPVAR YIFPLSVHHG PSNRLILRMS QTPLVLVDGS
     SYLYRAFHAL PPLTTSKGLP TGAVKGVLNM LKSLRKQYPQ SPFAVVFDAK GGTFRDELFA
     DYKANRPSMP DELRVQIEPL HASVRALGYP LLCVDGVEAD DVIGTLARQC AAAGRDVVIS
     TGDKDMAQLV CPHVTLVNTM SGSVYDIDGV KEKFGVGPEL IIDYLALMGD KVDNIPGVPG
     VGEKTAVGLL VGVGGGLEVL YANLDKVPEL PIRGAKNLPA KLLEHKDMAF LSYQLATIKL
     DVPLNIEIDS LHPGEQDREA LAELYALLEF KTGLDELARD VKAAGIAAIR SGGLFDAPAA
     EPPATEENVA AVESAANQYE TVLDAERFAV WLEKLNKAEL FAFDTETTGL DAQQAQLVGI
     SIAVQVNEAA YIPLTHSYMG VPAQLDRDTV LKALKPILED PNKAKVGQHA KYDINILANC
     AIDGESNNGI TLRGVRFDSM LESYVLDSVA TRHNMDALAL KYLDHTTIAF EDIAGKGAKQ
     LTFDQIALEQ AGPYAAEDAD ITLRLHQVLW QKLQAVPSLA KVLSDIEMPL VPVLARIERN
     GALVDANLLG LQSNELGEKM VQLEREAFAI AGEEFNLSSP KQLGVILYEK LGMPVLSKTA
     KGQASTAEAV LAELAEQDFP LPKVLMQYRS MSKLKSTYTD RLPEQINPRT GRIHTSYHQA
     VAATGRLSST DPNLQNIPIR TAEGRRIRQA FIAPPGYKLL AADYSQIELR IMAHLAKDES
     LLHAFRDNLD VHRATAAEVF GVELEQVTTD MRRKAKAINF GLIYGMSAFG LAKQIGVDRK
     ESQAYIDRYF ARYPGVLSYM ERTREQASEQ GYVETLFGRR LYLPEIHSKN AGLRKGAERT
     AINAPMQGTA ADIIKRAMVK VDDWLSESGL DAKVILQVHD ELVLEVREDL LETVSAEIRQ
     RMSAAAELDV PLLVEVGVGA NWDEAH
//
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