ID A0A173KV47_9SPHN Unreviewed; 234 AA.
AC A0A173KV47;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=EP837_01464 {ECO:0000313|EMBL:ANI77886.1};
OS Sphingobium sp. EP60837.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=1855519 {ECO:0000313|EMBL:ANI77886.1, ECO:0000313|Proteomes:UP000078304};
RN [1] {ECO:0000313|EMBL:ANI77886.1, ECO:0000313|Proteomes:UP000078304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EP60837 {ECO:0000313|EMBL:ANI77886.1,
RC ECO:0000313|Proteomes:UP000078304};
RA Lee C.-M., Yoon S.-H., Kim B.-Y.;
RT "Complete genome sequence of a organophosphorus pesticides.";
RL Submitted (JUN-2016) 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|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}.
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DR EMBL; CP015986; ANI77886.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A173KV47; -.
DR STRING; 1855519.EP837_01464; -.
DR KEGG; sphb:EP837_01464; -.
DR PATRIC; fig|1855519.3.peg.1493; -.
DR Proteomes; UP000078304; Chromosome 1.
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 ECO:0000313|EMBL:ANI77886.1}; 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:ANI77886.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000078304};
KW Transferase {ECO:0000256|RuleBase:RU364087, ECO:0000313|EMBL:ANI77886.1}.
FT DOMAIN 6..176
FT /note="Exonuclease"
FT /evidence="ECO:0000259|SMART:SM00479"
SQ SEQUENCE 234 AA; 25896 MW; D0ADEE4DFE8FEE4C CRC64;
MKRAMREIIF DTETTGFDPA SGDRLVEIGC IELVNRVPTG RTFHAYYNPQ RAMPSAAEAI
HGLSDIFLKD KPFFSAGVAE LLDFLEDSHL VAHNARFDFG FLNHELKLCG LPEVTMARMI
DTVAIARQLH PGAKHSLDAL CTRYGIDRSH RIKHGALLDA ELLAQLYIEL TGGRQIGLGL
AQEEDNDAIR VELAGIAAVR PVRPARIFTV SAAELERHAA FVATLEKPLW LEEA
//
