ID F7QHA9_9BRAD Unreviewed; 231 AA.
AC F7QHA9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE RecName: Full=DNA polymerase III subunit epsilon {ECO:0000256|ARBA:ARBA00020352, ECO:0000256|RuleBase:RU364087};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417, ECO:0000256|RuleBase:RU364087};
GN Name=dnaQ {ECO:0000256|RuleBase:RU364087};
GN ORFNames=CSIRO_0936 {ECO:0000313|EMBL:EGP09398.1};
OS Bradyrhizobiaceae bacterium SG-6C.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae.
OX NCBI_TaxID=709797 {ECO:0000313|EMBL:EGP09398.1, ECO:0000313|Proteomes:UP000003148};
RN [1] {ECO:0000313|EMBL:EGP09398.1, ECO:0000313|Proteomes:UP000003148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SG-6C {ECO:0000313|EMBL:EGP09398.1,
RC ECO:0000313|Proteomes:UP000003148};
RX PubMed=21742875; DOI=10.1128/JB.05647-11;
RA Pearce S.L., Pandey R., Dorrian S.J., Russell R.J., Oakeshott J.G.,
RA Pandey G.;
RT "Genome Sequence of the Newly Isolated Chemolithoautotrophic
RT Bradyrhizobiaceae Strain SG-6C.";
RL J. Bacteriol. 193:5057-5057(2011).
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. {ECO:0000256|ARBA:ARBA00025483,
CC ECO:0000256|RuleBase:RU364087}.
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|RuleBase:RU364087};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000256|ARBA:ARBA00001946,
CC ECO:0000256|RuleBase:RU364087};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936,
CC ECO:0000256|RuleBase:RU364087};
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
CC complex. {ECO:0000256|RuleBase:RU364087}.
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:EGP09398.1}.
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DR EMBL; AFOF01000013; EGP09398.1; -; Genomic_DNA.
DR AlphaFoldDB; F7QHA9; -.
DR STRING; 709797.CSIRO_0936; -.
DR eggNOG; COG0847; Bacteria.
DR HOGENOM; CLU_047806_2_1_5; -.
DR Proteomes; UP000003148; Chromosome.
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:0004527; F:exonuclease activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd06131; DNA_pol_III_epsilon_Ecoli_like; 1.
DR Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR InterPro; IPR006054; DnaQ.
DR InterPro; IPR006309; DnaQ_proteo.
DR InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR InterPro; IPR012337; RNaseH-like_sf.
DR InterPro; IPR036397; RNaseH_sf.
DR NCBIfam; TIGR00573; dnaq; 1.
DR NCBIfam; TIGR01406; dnaQ_proteo; 1.
DR PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR PANTHER; PTHR30231:SF43; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR Pfam; PF00929; RNase_T; 1.
DR SMART; SM00479; EXOIII; 1.
DR SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|RuleBase:RU364087};
KW DNA-directed DNA polymerase {ECO:0000256|RuleBase:RU364087};
KW Exonuclease {ECO:0000256|RuleBase:RU364087};
KW Hydrolase {ECO:0000256|RuleBase:RU364087};
KW Magnesium {ECO:0000256|RuleBase:RU364087};
KW Manganese {ECO:0000256|RuleBase:RU364087};
KW Metal-binding {ECO:0000256|RuleBase:RU364087};
KW Nuclease {ECO:0000256|RuleBase:RU364087};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364087,
KW ECO:0000313|EMBL:EGP09398.1};
KW Transferase {ECO:0000256|RuleBase:RU364087, ECO:0000313|EMBL:EGP09398.1}.
FT DOMAIN 2..172
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 231 AA; 25821 MW; 08351215AD9DDE35 CRC64;
MREIVLDTET TGLDPLRGDR LVEIGCVEMV NRMPTGQTYH VYLNPERDMP QEAFNVHGLS
SEFLSDKPLF ASVVEDFLAF IGEAPLVIHN AMFDIGFINA ELDRVARAAI PRDRLVDTLT
LARRKHPGVS NRLDDLCSRY SIDNSRRTKH GALLDAELLA EVYIDLIGAR QSQLILSETR
QSFSSGPADT PRRQREVPLA PRVTEADIAA HAAFVATLGG TPYWNEYTKE N
//
