ID A0A1I3ZX12_9FIRM Unreviewed; 843 AA.
AC A0A1I3ZX12;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=SAMN05216390_101300 {ECO:0000313|EMBL:SFK48437.1};
OS Lachnospiraceae bacterium KH1T2.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1855374 {ECO:0000313|EMBL:SFK48437.1, ECO:0000313|Proteomes:UP000198626};
RN [1] {ECO:0000313|EMBL:SFK48437.1, ECO:0000313|Proteomes:UP000198626}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1T2 {ECO:0000313|EMBL:SFK48437.1,
RC ECO:0000313|Proteomes:UP000198626};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOSY01000001; SFK48437.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I3ZX12; -.
DR STRING; 1855374.SAMN05216390_101300; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000198626; 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; 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; 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 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:UP000198626};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 3..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 601..807
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 843 AA; 93666 MW; 500FF77C29B47C5E CRC64;
MSEKILLIDG HSMMNRAFYG VPDLTNSAGV HTGAIYGFFN IILKILENER PQYFAVAFDE
HAPTFRHKIY AEYKGTRKPM PEELRQQIPL VKEILSAMGV PVVSKPGLEA DDILGTIAFR
AEKKGMDATI VSGDRDLLQL VTDKIALLLP RTVKGQTNVE RFTPEAVKEE YGVEPRGIID
LKALMGDSSD NIPGVPKVGP KTATELLTKY GDLKGVKEHI AEVTKKSIRE SLEEHFDLAE
LSQTLATINT ESDIEFDFDK AECESLGTAE AVKMLTDLEL KKLVERLGGV ETVVEEKTEF
REITELSDAE ALFNELAAKA TVGFAVDISE ENEISGIAFV ADGAWYIEPA GFITSAYLAD
HLVKLINKSN GMFYTAHLKQ VLKVADLPSR SNLVDYELEF YLLDPLRNDY AVPEKAQEAA
VEAFENGPKY MERIEAEGMK ELLENIEMPL CYVLSGMETE GIAIRKDMLT DFSAQLKEKI
DKLEKSIHEA AGEDFNINSP KQLGVILFEK MGLKGGKKTK TGYSTAAGVL EKLAPEVPFV
RDVLEYRTLS KLKATYADGL EPYIDKTGRI HSTFNQTITA TGRISSADPN LQNIPVRTEL
GRTLRKAFVP REGWSFIDAD YSQIELRILA SMSEDQKLIA AYKGGKDIHA ITASEVFHVP
FEEVTSDLRR KAKAVNFGIV YGISAFGLSQ GLSVSKSEAN EYIEKYFETY PGVKKFLDDL
VERAKDKGYA ETFFSRKRPM PELRSSNFMQ RSFGERVAMN APIQGTAADV IKIAMINVSK
RLKADGLQSK LILQIHDELL IETAPGEEEK VKEILREEMM GAASLAVPLE IDVNGGSNWD
EAH
//
