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Database: UniProt
Entry: A0A1I0XSI0_9FIRM
LinkDB: A0A1I0XSI0_9FIRM
Original site: A0A1I0XSI0_9FIRM 
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
//
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