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Protein

DNA polymerase III subunit epsilon

Gene

dnaQ

Organism
Buchnera aphidicola str. Ak (Acyrthosiphon kondoi)
Status
Unreviewed-Annotation score: -Protein predictedi

Functioni

DNA polymerase III is a complex, multichain enzyme responsible for most of the replicative synthesis in bacteria. The epsilon subunit contain the editing function and is a proofreading 3'-5' exonuclease.UniRule annotation

Catalytic activityi

Deoxynucleoside triphosphate + DNA(n) = diphosphate + DNA(n+1).UniRule annotation

Cofactori

Protein has several cofactor binding sites:
  • Mg2+UniRule annotation
  • Mn2+UniRule annotation

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionDNA-directed DNA polymeraseUniRule annotation, ExonucleaseUniRule annotation, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase
Biological processDNA replicationUniRule annotation
LigandMagnesiumUniRule annotation, ManganeseUniRule annotation, Metal-bindingUniRule annotation

Enzyme and pathway databases

BioCyciBAPH1005090:G1H03-253-MONOMER

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit epsilonUniRule annotation (EC:2.7.7.7UniRule annotation)
Gene namesi
Name:dnaQUniRule annotationImported
ORF Names:BAKON_250Imported
OrganismiBuchnera aphidicola str. Ak (Acyrthosiphon kondoi)Imported
Taxonomic identifieri1005090 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesErwiniaceaeBuchnera
Proteomesi
  • UP000001269 Componenti: Chromosome

Interactioni

Subunit structurei

The DNA polymerase holoenzyme is a complex that contains 10 different types of subunits. These subunits are organized into 3 functionally essential subassemblies: the pol III core, the beta sliding clamp processivity factor and the clamp-loading complex. The pol III core (subunits alpha,epsilon and theta) contains the polymerase and the 3'-5' exonuclease proofreading activities. The polymerase is tethered to the template via the sliding clamp processivity factor. The clamp-loading complex assembles the beta processivity factor onto the primer template and plays a central role in the organization and communication at the replication fork. This complex contains delta, delta', psi and chi, and copies of either or both of two different DnaX proteins, gamma and tau.UniRule annotation

Protein-protein interaction databases

STRINGi1005090.BAKON_250

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini5 – 182ExonucleaseInterPro annotationAdd BLAST178

Phylogenomic databases

eggNOGiENOG4107RZZ Bacteria
COG0847 LUCA
KOiK02342
OrthoDBiPOG091H0294

Family and domain databases

CDDicd06131 DNA_pol_III_epsilon_Ecoli_like, 1 hit
Gene3Di3.30.420.10, 1 hit
InterProiView protein in InterPro
IPR006054 DnaQ
IPR006309 DnaQ_proteo
IPR013520 Exonuclease_RNaseT/DNA_pol3
IPR012337 RNaseH-like_sf
IPR036397 RNaseH_sf
PfamiView protein in Pfam
PF00929 RNase_T, 1 hit
SMARTiView protein in SMART
SM00479 EXOIII, 1 hit
SUPFAMiSSF53098 SSF53098, 1 hit
TIGRFAMsiTIGR00573 dnaq, 1 hit
TIGR01406 dnaQ_proteo, 1 hit

Sequencei

Sequence statusi: Complete.

G2LMW4-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNKKRTIILD TETTGINKIS LPHINHRVIE IGAVEIINRR FTGNNFHVYI
60 70 80 90 100
QPNRLIESGA LKIHGITNSF LSDKPFFKDI SDQFLNYVKN SELVIHNASF
110 120 130 140 150
DLGFINQELE ILNHKIKNIN TFCSIIDTLK IARMLFPGKK NTLDALCKRY
160 170 180 190 200
KINKSHRKVH SAIVDAYLLG KLYLLMTGGQ ESMFSFNTID HKKNPQNLKK
210 220 230
NIKRKNSSLR ILYPTLKEMD LHKKYLQSMI DDNSICLWY
Length:239
Mass (Da):27,749
Last modified:November 16, 2011 - v1
Checksum:i78D19E3FED118391
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP002645 Genomic DNA Translation: AEO08602.1
RefSeqiWP_014499402.1, NC_017256.1

Genome annotation databases

EnsemblBacteriaiAEO08602; AEO08602; BAKON_250
KEGGibak:BAKON_250
PATRICifig|1005090.4.peg.244

Similar proteinsi

Entry informationi

Entry nameiG2LMW4_9GAMM
AccessioniPrimary (citable) accession number: G2LMW4
Entry historyiIntegrated into UniProtKB/TrEMBL: November 16, 2011
Last sequence update: November 16, 2011
Last modified: February 28, 2018
This is version 38 of the entry and version 1 of the sequence. See complete history.
Entry statusiUnreviewed (UniProtKB/TrEMBL)

Miscellaneousi

Keywords - Technical termi

Complete proteomeImported

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