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Database: UniProt
Entry: A0A1F8E289_9BACT
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ID   A0A1F8E289_9BACT        Unreviewed;       724 AA.
AC   A0A1F8E289;
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:OGM94943.1};
GN   ORFNames=A2610_02100 {ECO:0000313|EMBL:OGM94943.1};
OS   Candidatus Wolfebacteria bacterium RIFOXYD1_FULL_48_65.
OC   Bacteria; Candidatus Wolfebacteria.
OX   NCBI_TaxID=1802561 {ECO:0000313|EMBL:OGM94943.1, ECO:0000313|Proteomes:UP000179057};
RN   [1] {ECO:0000313|EMBL:OGM94943.1, ECO:0000313|Proteomes:UP000179057}
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:OGM94943.1}.
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DR   EMBL; MGIV01000010; OGM94943.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F8E289; -.
DR   Proteomes; UP000179057; 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          481..688
FT                   /note="DNA-directed DNA polymerase family A palm"
FT                   /evidence="ECO:0000259|SMART:SM00482"
SQ   SEQUENCE   724 AA;  81160 MW;  C912B2B3A146D65F CRC64;
     MKKLLLIDAN ALIHRAFHAI PNLTTPDGRP SGALYGLANV LIKIFREEHP EYAVAFFDRP
     EPTFRKKMYA EYKAHRPKAP DELVSQIIEA HNLFDIFGVK TYEVPGFEGD DLIGTAAEQF
     KGEKDVQVVI LTGDLDALQL VEGNKVVVET LKQGISETIT YDTTAVEARY GITPSQLADY
     KGLVGDTSDN IAGVRGVGPK TAAAIIQEFS SLENFFATVK ASDSTDKKML SYKKIAEHEE
     IAMLSKQLAT IRRDAPIGIT SINEIKYEQF PIEAIVPYLQ DLGFTSIIKR LAPEARETRG
     TRQEVRETQG QLSFLDAQPT LSKTLLDDVE RPLVPILEEM KQWGIMIDRV RLAEKEVILD
     RDIDALTKEL YREAGQVFNP NSPKQLLELL KTKYQLKIKS TNIDKIEQFR ATVPLVDLIL
     KYRELFKVKS TYLEPLKRMS DPSTSSGQMG DSRIHPTFVQ LKAATGRITC EQPNLQNIPP
     SVRDIFVAPA GSKLVSLDYS QIELRILASL TEDPEMLRAF KSNSDIHQIT ASKIYNVPLA
     DVTPTMRKVA KTLNFGVIYG MGARALAQQS GLSPKEAKAF IEEYFKDFAT IKHWQEGILA
     KVREQGFVEN INGRIRPLPE IVSFNKMLQS EAERMAINFP IQSVGADIIK SAMVKVKEHL
     SAEGLWGADV KMLLTVHDEL VFEIKDTERL PQTVNEIKDI LESVYTLKVP LTVNVEIGDN
     WGEL
//
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