ID   DPO3E_AQUAE             Reviewed;         202 AA.
AC   O67074;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 122.
DE   RecName: Full=DNA polymerase III subunit epsilon;
DE            EC=2.7.7.7;
GN   Name=dnaQ; OrderedLocusNames=aq_932;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. The
CC       epsilon subunit contain the editing function and is a proofreading 3'-
CC       5' exonuclease (By similarity). {ECO:0000250}.
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   -!- COFACTOR:
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations. Magnesium or manganese.
CC       {ECO:0000250};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the POLIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
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DR   EMBL; AE000657; AAC07031.1; -; Genomic_DNA.
DR   PIR; G70380; G70380.
DR   RefSeq; NP_213636.1; NC_000918.1.
DR   RefSeq; WP_010880574.1; NC_000918.1.
DR   AlphaFoldDB; O67074; -.
DR   SMR; O67074; -.
DR   STRING; 224324.aq_932; -.
DR   EnsemblBacteria; AAC07031; AAC07031; aq_932.
DR   KEGG; aae:aq_932; -.
DR   eggNOG; COG0847; Bacteria.
DR   HOGENOM; CLU_047806_7_1_0; -.
DR   InParanoid; O67074; -.
DR   OMA; FHVYLNP; -.
DR   OrthoDB; 1985371at2; -.
DR   Proteomes; UP000000798; Chromosome.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IBA:GO_Central.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0045004; P:DNA replication proofreading; IBA:GO_Central.
DR   Gene3D; 3.30.420.10; -; 1.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
PE   3: Inferred from homology;
KW   DNA replication; DNA-directed DNA polymerase; Exonuclease; Hydrolase;
KW   Magnesium; Manganese; Metal-binding; Nuclease; Nucleotidyltransferase;
KW   Reference proteome; Transferase.
FT   CHAIN           1..202
FT                   /note="DNA polymerase III subunit epsilon"
FT                   /id="PRO_0000105479"
FT   ACT_SITE        162
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         23
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         25
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /ligand_note="catalytic"
FT                   /evidence="ECO:0000250"
FT   BINDING         167
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   202 AA;  23045 MW;  7BB8144354FE0A6B CRC64;
     MKSSPKSLKM RDNLLDGTFV VIDLEATGFD VEKSEVIDLA AVRVEGGIIT EKFSTLVYPG
     YFIPERIKKL TGITNAMLVG QPTIEEVLPE FLEFVGDNIV VGHFVEQDIK FINKYTKQYR
     GKKFRNPSLC TLKLARKVFP GLKKYSLKEI AENFGFETNG VHRALKDATL TAEIFIKILE
     ELWFKYGIGD YYSLKRLEKG KF