ID A0A1I1Y4U3_9FIRM Unreviewed; 882 AA.
AC A0A1I1Y4U3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 28.
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=SAMN02910278_00021 {ECO:0000313|EMBL:SFE14627.1};
OS Peptostreptococcus sp. D1.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Peptostreptococcus.
OX NCBI_TaxID=72304 {ECO:0000313|EMBL:SFE14627.1, ECO:0000313|Proteomes:UP000199190};
RN [1] {ECO:0000313|EMBL:SFE14627.1, ECO:0000313|Proteomes:UP000199190}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D1 {ECO:0000313|EMBL:SFE14627.1,
RC ECO:0000313|Proteomes:UP000199190};
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; FONP01000001; SFE14627.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1Y4U3; -.
DR STRING; 72304.SAMN02910278_00021; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000199190; 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; 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; 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:UP000199190};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 5..263
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 299..473
FT /note="3'-5' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00474"
FT DOMAIN 640..846
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 882 AA; 99182 MW; 44B3E45471BCB935 CRC64;
MDNKKKILLI DGNSIINRAF FALPPMDNAD GLHTNAVYGF LTMMFKMIKN IQPTHISVAF
DLKAPTFRHK AFAEYKAGRK GMPSELAMQL EPLKNILDSM NIDRKEIAGY EADDILGTIS
RIGEENDFSV YVVTGDKDAI QLASDKTLVM ITKKGVAEVE EYNTEGVIER YGLTPAQFID
LKGLMGDKSD NIPGIPGIGE KTGIKLLQEF GSVEGVIENV DKLKGSQKKK VEENTETAIM
SKALATIDRN IPLDLSFEDM EFGSFDVHAV IEEFQKLKFN SLISKLSEFT SCEEKEVEKK
EINKLEDIEA FIKKIDEEGV LSIKTICKEG NILDKNIIKT FLSIDGKEYY YLDGEEIISL
KEVLESEDIE KIGYELKQDF VALRPYGIYL GNIKFDISIA EYVIESKSSS SYDIDSIANK
YLYKKVMTKD ELLGKGSKSL SFEEVDCEKL NDYIIGVFDT VFGVIEAMEK SIIDDCMEML
FYDVEMPLIA VLGDMEYSGI RVDKAVLNEL DLEIKELISD AEKKIFSLAG EEFNINSPKQ
LGIILFEKLG LPVVKKTKTG YSTNAEVLEK LMDEHEIIKL ISDYRTVVKL KSTYIDGLNS
VINEKDGRIH STFNQTIAST GRISSTDPNL QNIPVRTNIG RNIRKIFISE NGKKLVDADY
SQVELRVLAH MSGDKNMIEA FSSGEDIHRK TASQVFNVSF DDVTPELRSA AKAVNFGIIY
GKSDFGLAKD LNISLAKAKD YINSYFAKYD RIKGFMDEIV GKAEKTGYST TIFNRRRYIP
EIKSNNFIDK NRGKRAAMNA PIQGSAADII KIAMVNVHNR LFEEGLKSKL ILQVHDELIV
EAAEDELEII KALLKEEMEN AVYLDVDLDV DLNVGNSWYE TK
//
