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Database: UniProt
Entry: A0A1T4NK67_9ENTE
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Original site: A0A1T4NK67_9ENTE 
ID   A0A1T4NK67_9ENTE        Unreviewed;       879 AA.
AC   A0A1T4NK67;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   RecName: Full=DNA polymerase I {ECO:0000256|RuleBase:RU004460};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU004460};
GN   Name=polA {ECO:0000256|RuleBase:RU004460};
GN   ORFNames=SAMN02745116_01459 {ECO:0000313|EMBL:SJZ79660.1};
OS   Pilibacter termitis.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Pilibacter.
OX   NCBI_TaxID=263852 {ECO:0000313|EMBL:SJZ79660.1, ECO:0000313|Proteomes:UP000190328};
RN   [1] {ECO:0000313|EMBL:SJZ79660.1, ECO:0000313|Proteomes:UP000190328}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-1030 {ECO:0000313|EMBL:SJZ79660.1,
RC   ECO:0000313|Proteomes:UP000190328};
RA   Peterson S.W.;
RL   Submitted (FEB-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   -!- SUBUNIT: Single-chain monomer with multiple functions.
CC       {ECO:0000256|RuleBase:RU004460}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
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DR   EMBL; FUXI01000015; SJZ79660.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4NK67; -.
DR   STRING; 263852.SAMN02745116_01459; -.
DR   OrthoDB; 9806424at2; -.
DR   Proteomes; UP000190328; Unassembled WGS sequence.
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:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
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; cd06140; DNA_polA_I_Bacillus_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; 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   PRINTS; PR00868; DNAPOLI.
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   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW   ECO:0000256|RuleBase:RU004460};
KW   Reference proteome {ECO:0000313|Proteomes:UP000190328};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          4..264
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          635..843
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   879 AA;  99476 MW;  406D04DA64A1FD1D CRC64;
     MSQKRLLLID GNSIAFKAYF ALPKTFTNKA GLHTNAIYGF HTMLDSVLAR VEPTHILVAF
     DAGKTTFRTE MFQDYKGGRP TTDPELREQF LPLREMLAAR SIRYYELPNY EADDIIGTLA
     TRASEAGFLV TIVSGDRDMT QLATEKITVE ISKKGVSDIE EYTPAVVQEK MGITPKQIID
     LKGLMGDKSD NIPGVTKVGE KTALKLLWEY QTVEGVYEHI DELKASKMKE NLINEQEIAL
     LSKKLATINL TSPVEIELDE LAMKEPDAEK LIAFYQENNF NEFLSRMGSA VEEEVQEISY
     EVVENFSAEH LANAEVFHLE TFGENYHEAE VLAAVVGNKE KLFVTSNLDT LSSSEAKKWL
     DDRTKEKIVF DVKAISVFLS KMDLSIKGVK HDVLLSAYLL DKLDKTQEIA GVAKKLHTSP
     IKFNEDVYGK GAKYAVPMFF EEVESFAAQK AFATLNVSER LHEELEEKEM LHLLLEMEMP
     LAIVLSEMEE KGIAVKPEVL DELSVDLMSR IEELKTKIYA QAGVELNLNS PKQLGELLFE
     TLGFDYKLYS KKTKTGYSTN AEVLEKMSVV APIVDDILTY RELQKLQSTY IEGLKKSRRA
     DGKIHTRYQQ ALTQTGRLSS VDPNLQNIPI RTEDGRKIRQ AFVASKEDWV IYSSDYSQIE
     LRVLAHISQD EHLKSAFMEG QDIHTSTAMR VFGISSPDEV TPLDRRNAKA VNFGVVYGIS
     EWGLAKNLGI EPYKAKDFID KYFEKYPGIK QYMEEVVREA KEVGYVETMF HRRRNLPEIN
     ERNFARRSFA ERTAINSPIQ GSAADILKIA MNNLHTRLAK ENLQANLLLQ VHDELIFEVA
     KSDVEALDKI VRSEMEDAVK LSVPLVADSA WGESWYDAK
//
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