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Database: UniProt
Entry: A0A1F6RY51_9BACT
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ID   A0A1F6RY51_9BACT        Unreviewed;       891 AA.
AC   A0A1F6RY51;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-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=A3J76_05815 {ECO:0000313|EMBL:OGI25568.1};
OS   Candidatus Moranbacteria bacterium RBG_13_45_13.
OC   Bacteria; Candidatus Moranbacteria.
OX   NCBI_TaxID=1801635 {ECO:0000313|EMBL:OGI25568.1, ECO:0000313|Proteomes:UP000178026};
RN   [1] {ECO:0000313|EMBL:OGI25568.1, ECO:0000313|Proteomes:UP000178026}
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:OGI25568.1}.
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DR   EMBL; MFRT01000024; OGI25568.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F6RY51; -.
DR   Proteomes; UP000178026; 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; 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; 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.
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          7..267
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          297..471
FT                   /note="3'-5' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00474"
FT   DOMAIN          650..856
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   891 AA;  101791 MW;  9FBC8DDFE9887102 CRC64;
     MPSSHKKRLI LIDSNALIHR AYHALPPLTT KEGELVNAVY GYTSVLLNVL NKFKPEYIVA
     TFDLKEPTFR HKQFKDYKAT RVKAPDDLYA QIPRVKEIVK ALSIPIAEKE GYEADDLIAT
     FARKTEKLHP DVEVIVVTGD LDTLQLVDEK IKVFALRRGM SDSVLYDKKS IMERYGLNPE
     QMVDYKGLRG DPSDNLPGVK GVGEKTAADL LKKYKTLENV YKNLPEIKEG IRKKLERDKV
     QAYFSKRLAR LVDNVPSNFD LEKARAEDFS RVKIINLLRE LEFFSLLRRL PGYEEHLKDI
     EEKNELKEKK EKLTWEKISP HQMPEIKNRL SLVSDGEIGG GIRGVAVCQN QKSAFYISRI
     DEKVKNIFSD GKIGKIGYDL KKEWKILDEN KISLRGIKFD VQLAAYLLNS GVNLSWEDLV
     LRELGILVEK ENKKAGQTAL IFQEDEGAIE KICRRASYNL ALEEKLEEKL EEISREQIMA
     EKEKTLRNLF ENLEMPLIEA LARMEKEGIR INKTVLHGIS EKLDRRVEKL EKAIQKMAGE
     KFNVNSSVQL RDVLFEKLKI PTKNIKTGKT GYSTASPELQ KIKTLHPIVE KIEEYRELFK
     LKTTYLDPLP TLTDKNSRLH TSFNQAVTAT GRLSSSEPNL QNIPIRTDLG QLIRTAFEAE
     EGFRLVGVDY SQIELRIAAH LSGDVRMITT FINGEDIHTA TAARVNKLDL DKVTKKMRSA
     AKALNFGIIY GMSTFGFAQS AGVDQDASRE FIRKYFENYP QVAQFLENVK ISAREKGFVE
     TELGRRRYIP EINSTNIQLR NQAERMAVNM PIQGLAADII KLAMLAAEKM IRKKYPIAKM
     VLQIHDELLF EVPEQEAEKF ARDIKIAMEN VYKLSVPLIA DVKIGDNWGE I
//
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