ID A0A1Y6L3E9_9GAMM Unreviewed; 242 AA.
AC A0A1Y6L3E9;
DT 30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT 30-AUG-2017, sequence version 1.
DT 27-MAR-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 ECO:0000313|EMBL:SMY17138.1};
GN ORFNames=PAQU9191_02410 {ECO:0000313|EMBL:SMY17138.1};
OS Photobacterium aquimaris.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=512643 {ECO:0000313|EMBL:SMY17138.1, ECO:0000313|Proteomes:UP000196485};
RN [1] {ECO:0000313|Proteomes:UP000196485}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=type strain: CECT 9192 {ECO:0000313|Proteomes:UP000196485};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (JUN-2017) 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|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}.
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DR EMBL; FYAH01000003; SMY17138.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Y6L3E9; -.
DR Proteomes; UP000196485; 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: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|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 ECO:0000313|EMBL:SMY17138.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000196485};
KW Transferase {ECO:0000256|RuleBase:RU364087, ECO:0000313|EMBL:SMY17138.1}.
FT DOMAIN 9..186
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 242 AA; 26994 MW; 25235A9F4954519A CRC64;
MKATNTNQRI IVFDTETTGM NMTGPHYEGH GIVEIGAVEI INRKLTGNTF HVYIKPDRTI
DPEAIAVHGI TDEFLRDKPA YADIHQEFID FIDGAELVAH NASFDTGFMD YEFHKMGASI
AKIEDICQVT DTLEMAKRLF PGKRNNLDIL CSRYGIDNSH RTLHGALLDA EILADVYLMM
TGGQTSLRLS SGNDDSTTAT SIRRLATDRK VLKVINATAD ELTAHQDRLD LIGKKADVIW
RL
//
