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Database: UniProt
Entry: A0A1G2R3K9_9BACT
LinkDB: A0A1G2R3K9_9BACT
Original site: A0A1G2R3K9_9BACT 
ID   A0A1G2R3K9_9BACT        Unreviewed;       589 AA.
AC   A0A1G2R3K9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:OHA67416.1};
DE   Flags: Fragment;
GN   ORFNames=A3C82_02240 {ECO:0000313|EMBL:OHA67416.1};
OS   Candidatus Wildermuthbacteria bacterium RIFCSPHIGHO2_02_FULL_47_12.
OC   Bacteria; Candidatus Wildermuthbacteria.
OX   NCBI_TaxID=1802451 {ECO:0000313|EMBL:OHA67416.1, ECO:0000313|Proteomes:UP000176901};
RN   [1] {ECO:0000313|EMBL:OHA67416.1, ECO:0000313|Proteomes:UP000176901}
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   -!- 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   -!- SIMILARITY: Belongs to the DNA polymerase type-A family.
CC       {ECO:0000256|ARBA:ARBA00007705}.
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:OHA67416.1}.
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DR   EMBL; MHTW01000013; OHA67416.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G2R3K9; -.
DR   STRING; 1802451.A3C82_02240; -.
DR   Proteomes; UP000176901; Unassembled WGS sequence.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016788; F:hydrolase activity, acting on ester bonds; IEA:UniProt.
DR   GO; GO:0006261; P:DNA-templated DNA replication; IEA:InterPro.
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   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; IPR002298; DNA_polymerase_A.
DR   InterPro; IPR008918; HhH2.
DR   InterPro; IPR029060; PIN-like_dom_sf.
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.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          7..277
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          497..589
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
FT   NON_TER         589
FT                   /evidence="ECO:0000313|EMBL:OHA67416.1"
SQ   SEQUENCE   589 AA;  65672 MW;  C600F933720AFBF9 CRC64;
     MKTEKKKRLL LIDANSLIHR AFHALPPLSA STGEMVNAVY GFCLAFFKAV KEFQPDYIAA
     AFDVAGGSFR DKKFAAYKAK REKAPDELYG QMPLVKKVLA VFHVPVYEKG GFEADDIIGT
     ISLQAPRKQV KPPLETIILS GDADVFQLVD GHTKAYTLRK GIQDSVLYDE KAVEKRFGGL
     KPVQLVDYKA LRGDPSDNIP GVTGIGEKTA IALLLQFGSL DNIYKELEEN TEKAKSLRPR
     LKDMLVQYKE QAAISKELAQ IERHAPIDCK LSDLAWKEFD EKEAEQLLQS FGFRSLTLRL
     PELHGNGKKQ EKEQGEDDQL AVIEQLERDG VLSHEIAEVE RNLTPVLRAM EKTGIAVSKE
     YFAGLEKDMR RELAKAESKI FELAESVFNV GSPKQLSAVL FEKLMLSPKG MHKTPGGIVS
     TASPELEKIK SLHPIVQEVL NYRELAKLLH TYVAPLPLLA DKEGRIHTHF EQFGAETGRL
     SSANPNLQNI PLQGSWGKKV RGGFVAAPGY QLVSCDYSQM ELRLAAHIAK EEKMQKIFQE
     NKDIHRMTAS EVFGIPAQEV SDEMRYRAKA LNFGVLYGMG ARGFAQSAK
//
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