ID A0A1H9FVX8_9FIRM Unreviewed; 888 AA.
AC A0A1H9FVX8;
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=SAMN02910369_01741 {ECO:0000313|EMBL:SEQ41949.1};
OS Lachnospiraceae bacterium NE2001.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520823 {ECO:0000313|EMBL:SEQ41949.1, ECO:0000313|Proteomes:UP000199680};
RN [1] {ECO:0000313|EMBL:SEQ41949.1, ECO:0000313|Proteomes:UP000199680}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NE2001 {ECO:0000313|EMBL:SEQ41949.1,
RC ECO:0000313|Proteomes:UP000199680};
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; FOEK01000011; SEQ41949.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9FVX8; -.
DR STRING; 1520823.SAMN02910369_01741; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000199680; 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; 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:UP000199680};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 2..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 646..852
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 888 AA; 99613 MW; B4A0A14D5F242467 CRC64;
MSKLLLIDGN SIMNRGYYAL PKTLTDSKGL HTNAILGFLN IFYKIYSEEQ PTNIIVAFDM
HAPTFRHNIY KEYKGTRKGM EPELREQFPV IKDVLSIMKV LYVEKAGYEA DDIIGTYSRQ
AEKEGMEVSI LSGDRDLLQL ATDSILVRIP KTKGGQTTIE NYYAKDVVAE YGVTPLEFIE
MKGLMGDTSD NIPGVEGIGP KTASNIIQKY HSIEAALADI EHVKPDKART NLDANREMAL
FSRDLATIKL DCELEESVSE SQVGSGDIYS SDVYNVLLEL GFRTLLKRFE NVSAEEIKVE
TKIEINPVDI SYPELIEKIR SYADSSVDAV SDNAAEAEKF VGFGTTLTNG SIYGAAISFN
KEVYIVRGNE LKNLRRDIPS NIKLSFVGLK EYIDYFGLEE SDNLFDVSLG AYLIDPLVNG
YNYSYIASRF LGVEIEDEKL LIGKDEITPF SLDMDNYRKM ISYMAYTAAE SVKPIIDKLK
SMDEYSLYTD IEYPVIFVLN SMESYGVRVD SETLTEYGKQ LDEKLDTLTE SIYKLAGEEF
NINSPKQLGV ILFEKLGLKS GKKTKSGYST SVDVLSKLRD DHPIIPEILE YRSISKLRST
YVDGLLESIR SDGRIHSKFN QTVTATGRLS STEPNLQNIP TRTAEGREIR KSFVPAEGYT
FVDADYSQIE LRVMASISED ESLIEAFNSS KDIHAITASQ VFGVPIEEVD STLRRRAKAV
NFGIIYGISS FGLGEDLGIS RKEAKDYIDK YFATYVRVKD YLDSCVQGAK DTGVVRTMYG
RLRPIPELQS SNFMQRSFGE RVAMNSPIQG TAADIIKLAM IKVWHELKAR NLKSRLILQI
HDELLIETAP GEVEEVTELL RENMENAATL AVPLYVDVHT GSTLYDAK
//
