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Database: UniProt
Entry: A0A1F6QPW6_9BACT
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ID   A0A1F6QPW6_9BACT        Unreviewed;       926 AA.
AC   A0A1F6QPW6;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 34.
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=A3F80_09715 {ECO:0000313|EMBL:OGI10456.1};
OS   Candidatus Melainabacteria bacterium RIFCSPLOWO2_12_FULL_35_11.
OC   Bacteria; Candidatus Melainabacteria.
OX   NCBI_TaxID=1801609 {ECO:0000313|EMBL:OGI10456.1, ECO:0000313|Proteomes:UP000198261};
RN   [1] {ECO:0000313|EMBL:OGI10456.1, ECO:0000313|Proteomes:UP000198261}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705, ECO:0000256|RuleBase:RU004460}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OGI10456.1}.
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DR   EMBL; MFRO01000007; OGI10456.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6QPW6; -.
DR   STRING; 1801609.A3F80_09715; -.
DR   Proteomes; UP000198261; 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; cd06139; DNA_polA_I_Ecoli_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; 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; IPR013520; Exonuclease_RNaseT/DNA_pol3.
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; SM00479; EXOIII; 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.
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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU004460}.
FT   DOMAIN          2..247
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          321..515
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          341..516
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
FT   DOMAIN          685..890
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   926 AA;  105515 MW;  96EBDC1FE474E20A CRC64;
     MFFAMERTNM RTLGGIPTWA TYGFFKAIFD LLDRVKPKAI AAAYDCKEPT FRHKEYEDYK
     ANRPEEMPEE LSVQWPYIRE GLESFEIPIY ELPGYEADDV IGTLAKKATK DGFNVLILTG
     DRDAFQLIND KTKVLVPSKG ELKEYNRQAV FDYWGIWPEQ VIDFKSLSGD ASDNIPGIKG
     IGEKTAEKLL TEFGSLDNIF KNAKKIPQKG LQEKILTGEK SAYLSKRLAA IDTDVPIDIN
     LKDAHLNVPD MDKLVGFLQK FEFNSFIKRL PTILAMFNGE KAIVEKPAIV KRQGQMRLDL
     DNLNGKTDDP LDDLQTPDLK INIIDTEKEL EKIISVLKDK KFICIDLETT SVNSNICDIV
     GISLSYFKDE KSKLEKSDGI KAYYIPLGHE NGKQLNIEHV LQILKLILED NEKLKIAQNC
     KFEYKILKRH GINLGKNIYD TMLASYVMNP DEKHGLKDQA ARILGMRMQK IDELIGEGKK
     QLSMAQVEIK KAAPYAISDA TYTLQLSKYY KSTLEQPLEN VLETIENPLV PVLSEMELNG
     IRIDTKVLKD LSDIITKKAQ ELEEKIFKIA GEPFNINSSQ QLGKILFQKL GIEHEGKITK
     SGQLSTDART LETLARDDKT GIIENILEYR QLSKLISTYT DSLPEQIDKK TKNIHCDFNQ
     TITSTGRLSS SNPNLQNIPI RSEIGRKIRK AFIPSFDNGL ILSADYSQIE LRILAHMSED
     PVLIEAFKAG EDIHKRTAME IYGVKEITPE MRGHGKTLNF ALIYQQGAYA TARQLDISQK
     EAQKFIDKYF QTFKKVKPFF EKLLNHARDH GYAETIYGRR RYFKNLKSHI KTLQREDERA
     ACNAPLQGTA ADIMKLAMIK VAKDLKEKNY KSKLILQVHD ELVLDVHPHE KEKIKTLVQE
     GMELGQPLHV PLVVNLSWGK DWYECG
//
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