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Database: UniProt
Entry: A0A0G0N871_9BACT
LinkDB: A0A0G0N871_9BACT
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ID   A0A0G0N871_9BACT        Unreviewed;       716 AA.
AC   A0A0G0N871;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
DE   SubName: Full=Polymerase I protein {ECO:0000313|EMBL:KKR12369.1};
GN   ORFNames=UT41_C0002G0143 {ECO:0000313|EMBL:KKR12369.1};
OS   Candidatus Wolfebacteria bacterium GW2011_GWC2_39_22.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1619013 {ECO:0000313|EMBL:KKR12369.1, ECO:0000313|Proteomes:UP000034665};
RN   [1] {ECO:0000313|EMBL:KKR12369.1, ECO:0000313|Proteomes:UP000034665}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA   Wilkins M.J., Williams K.H., Banfield J.F.;
RT   "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT   radiation of phyla.";
RL   Nature 0:0-0(2015).
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:KKR12369.1}.
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DR   EMBL; LBWR01000002; KKR12369.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0G0N871; -.
DR   STRING; 1619013.UT41_C0002G0143; -.
DR   PATRIC; fig|1619013.3.peg.796; -.
DR   Proteomes; UP000034665; 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; 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; 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.
DR   PROSITE; PS00447; DNA_POLYMERASE_A; 1.
PE   3: Inferred from homology;
KW   DNA damage {ECO:0000256|ARBA:ARBA00022763};
KW   DNA repair {ECO:0000256|ARBA:ARBA00023204};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
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          2..268
FT                   /note="5'-3' exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00475"
FT   DOMAIN          473..680
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   716 AA;  80556 MW;  79BA6199B45ACF32 CRC64;
     MKKLLLIDAN ALIHRAFHAI PNLTTPDGRP SGALYGLTNV LIKIFKEEHP EYAVAFFDRP
     EPTFRKEMYA EYKAHRPKAP DELISQIIEA HHLFDVFGVK TYEIPGFEGD DLIGTAAEQF
     KGEKDVQVVV LTGDLDALQL VEGNKVVVET LKQGISETIT YDETAVVARY GISPSQLADY
     KGLVGDASDN ISGVRGVGPK TASGIIQEFG SLENFFATIK VSDDAGKKML SYKKLIEHEE
     IALLSKTLAT IRRDAPIGIQ SISEIAYTAF PTETVIPYLK DMGFTSILKR LVPAENEIRV
     ARQKAQENQG QLFSLTSQPT LSQQLLDDVE LPLVSILEEM NQYGIMIDRT RLAEKEVILD
     RDIDALVKEL YREAGHVFNP NSPKQLLEIL KTTYKLKIKS TNIDKIEQFR STVPFIDLIL
     KYRELFKLKS TYLEPIKRMS ELDTRIHPTF VQLKAATGRI TCEHPNLQNI PPSIREIFVA
     SSGYKLVSLD YSQIELRILA SLTEDPEMLR AFKSNADIHQ ITASKIYNVS LEEVTPVMRK
     VAKTLNFGVI YGMGARALAQ QSGLTPKEAK LFIDEYFSDF STIKQWQETI LATVRTQGFV
     ENINGRMRPL PEIMSFNKML QSEAERMAIN FPIQSVAADI IKSAMVKVKE HFSSKGIWGT
     DVKMLLTIHD ELVFEIKDTD RLLATVTEIK DIMESIYTLN VPLTVNLEIG DNWGEL
//
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