ID A0A0J0YRI0_9NEIS Unreviewed; 240 AA.
AC A0A0J0YRI0;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PL75_06495 {ECO:0000313|EMBL:KLT72725.1};
OS Neisseria arctica.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=1470200 {ECO:0000313|EMBL:KLT72725.1, ECO:0000313|Proteomes:UP000036027};
RN [1] {ECO:0000313|EMBL:KLT72725.1, ECO:0000313|Proteomes:UP000036027}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KH1503 {ECO:0000313|EMBL:KLT72725.1,
RC ECO:0000313|Proteomes:UP000036027};
RA Hansen C.M., Hueffer K., Choi S.C.;
RT "Genome of a novel goose pathogen.";
RL Submitted (NOV-2014) 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}.
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:KLT72725.1}.
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DR EMBL; JTDO01000009; KLT72725.1; -; Genomic_DNA.
DR RefSeq; WP_047761111.1; NZ_JTDO01000009.1.
DR AlphaFoldDB; A0A0J0YRI0; -.
DR STRING; 1470200.PL75_06495; -.
DR PATRIC; fig|1470200.3.peg.2517; -.
DR OrthoDB; 9804290at2; -.
DR Proteomes; UP000036027; 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|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 Reference proteome {ECO:0000313|Proteomes:UP000036027};
KW Transferase {ECO:0000256|RuleBase:RU364087}.
FT DOMAIN 4..178
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 240 AA; 26740 MW; 8997B933F4212788 CRC64;
MSQRQIILDT ETTGLYPQSG DRMVEFAGLE MVNRQFTGSN LHLYIHPERD MPEEAAAVHG
LTIEVLEEKN APIFAKVGQE IADFLRGAEL IIHNAKFDVG FLDMEFSRMG LPSIEELGCR
VTDTLSMARE MFPGQKASLD ALCTRFDVDR SKRVYHGALI DCELLGEVYL AMTRGQFSLV
DGLAETAAQE EVRQVARPVH LKVLKADEAE LAEHKAYLDI LDKASGGNCI WRPKEAEAEA
//
