ID A0A370K354_9GAMM Unreviewed; 240 AA.
AC A0A370K354;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=DVT68_18540 {ECO:0000313|EMBL:RDI97084.1};
OS Dyella solisilvae.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Dyella.
OX NCBI_TaxID=1920168 {ECO:0000313|EMBL:RDI97084.1, ECO:0000313|Proteomes:UP000254711};
RN [1] {ECO:0000313|EMBL:RDI97084.1, ECO:0000313|Proteomes:UP000254711}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DHG54 {ECO:0000313|EMBL:RDI97084.1,
RC ECO:0000313|Proteomes:UP000254711};
RA Gao Z., Qiu L.;
RT "Dyella solisilvae sp. nov., isolated from the pine and broad-leaved mixed
RT forest soil.";
RL Submitted (JUL-2018) to the EMBL/GenBank/DDBJ databases.
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|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|ARBA:ARBA00024632,
CC 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:RDI97084.1}.
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DR EMBL; QQSY01000007; RDI97084.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370K354; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000254711; Unassembled WGS sequence.
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:SF41; 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|ARBA:ARBA00022839, 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|ARBA:ARBA00022722, ECO:0000256|RuleBase:RU364087};
KW Nucleotidyltransferase {ECO:0000256|RuleBase:RU364087};
KW Transferase {ECO:0000256|RuleBase:RU364087}.
FT DOMAIN 2..175
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 240 AA; 26749 MW; 35C1F32999C876A8 CRC64;
MRQIVLDTET TGLEVRQGHR LIEIACVEMI ERRPSGRHYQ TYLNPDRAID EGARQVTGIE
DEFLLDKPRF GDVVEEFLAF IDGAELIIHN ATFDVGFLNA ELARLGASYG RIEDRCNVLD
TLVMARERYP GQRNSLDALC KRLGVDNSAR DLHGGLIDAQ LLAEVYLSMT SGQVVLDLGF
EGAQEQGATV KLAPVVLDRR PRVLRANEEE LVAHERRLDA LDKNAGGASV WRRDQAPAVN
//