ID A0A1I0XSI0_9FIRM Unreviewed; 877 AA.
AC A0A1I0XSI0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=SAMN05216249_10790 {ECO:0000313|EMBL:SFB03396.1};
OS Acetitomaculum ruminis DSM 5522.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Acetitomaculum.
OX NCBI_TaxID=1120918 {ECO:0000313|EMBL:SFB03396.1, ECO:0000313|Proteomes:UP000198838};
RN [1] {ECO:0000313|EMBL:SFB03396.1, ECO:0000313|Proteomes:UP000198838}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5522 {ECO:0000313|EMBL:SFB03396.1,
RC ECO:0000313|Proteomes:UP000198838};
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; FOJY01000007; SFB03396.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I0XSI0; -.
DR STRING; 1120918.SAMN05216249_10790; -.
DR OrthoDB; 9806424at2; -.
DR Proteomes; UP000198838; 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:SF27; DNA POLYMERASE NU; 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|RuleBase:RU004460};
KW DNA repair {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:UP000198838};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT DOMAIN 1..264
FT /note="5'-3' exonuclease"
FT /evidence="ECO:0000259|SMART:SM00475"
FT DOMAIN 635..841
FT /note="DNA-directed DNA polymerase family A palm"
FT /evidence="ECO:0000259|SMART:SM00482"
SQ SEQUENCE 877 AA; 99365 MW; 0755EB2A32445356 CRC64;
MKEKIVLIDG HSILNRAFYG IPALTNSKGI YTNGVYGFLN IMFKLIDEEN PQYLAVAFDT
SKPTFRHEMF KEYKGTRKPT PKELSSQVPL IKEVLSAMNI FIISKAGLEA DDLIGTMAEY
SRNKGLDVVI ISGDRDLLQL VKDDVKLRIP KTTRNGTTVE NYYPDDVIEK YQLKPAQIID
LKSLMGDSAD NIPGIPGVGE KTATKILLEY ETLEKAYENV DNLKPPKASK SLKENYDLAV
LSKKLATINT KADIEFDIEN AKLGSMFNEN SKEKFVELEF KNLLSRFSFE DEKEKIERKF
EHIVTLKALD EFLNEAKKAK EIGTGMAYEK KLYGFSIAFD ERNAFIEVND EIKEDELCEK
IKELIIASKS ASFMDLKGIL KVINLEKFEN KYLDLSIGAY LINPIGGSYS YEDLAGIYLN
ESLESPKELL LKNSIEKTFK EDKKRVLTLT CYQAMTALLA KNIIFEKLKE MEMSDLYFNM
EGPLIFVLDA MEKEGMLVKR EALKEYGDSL VGRINQLEKS IYEKAGEEFN INSPKQLGVI
LFEKLQMPNA KKTKTGYSTS ADILEKLAGE YPIVNEILEY RTLAKLKSTY ADGLANYIGK
DERIHSNFNQ TITATGRISS TEPNLQNIPI KLELGRLIRK VFVPKDGFIF LDADYSQIEL
RVLAHMSGDE TLIDAYRNSK DIHKATAASV FNIPIEEVTP LQRRNAKAVN FGIIYGMSAF
GLGQDLGISN KEAADYIEKY YNAYPKIKMF LDGLVASARE KGYSITMFNR RRPMPELKAS
NFMQRSFGER TAKNSPIQGS AADIIKIAMI EVYEELKKRN LKSKLILSVH DELLVETALE
EVEEVKKILT EKMMGAAKLQ VPLEIELETG TNWYEAK
//