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Q08880

- DPO3E_BUCAP

UniProt

Q08880 - DPO3E_BUCAP

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Protein

DNA polymerase III subunit epsilon

Gene

dnaQ

Organism
Buchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Status
Reviewed - Annotation score: 3 out of 5- Protein inferred from homologyi

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 (By similarity).By similarity

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 divalent metal cations. Magnesium or manganese.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi11 – 111Divalent metal cation 1; catalyticBy similarity
Metal bindingi11 – 111Divalent metal cation 2; catalyticBy similarity
Binding sitei11 – 111SubstrateBy similarity
Metal bindingi13 – 131Divalent metal cation 1; catalyticBy similarity
Binding sitei13 – 131SubstrateBy similarity
Binding sitei60 – 601SubstrateBy similarity
Binding sitei65 – 651SubstrateBy similarity
Active sitei161 – 1611Proton acceptorBy similarity
Metal bindingi166 – 1661Divalent metal cation 1; catalyticBy similarity
Binding sitei166 – 1661SubstrateBy similarity

GO - Molecular functioni

  1. DNA binding Source: InterPro
  2. DNA-directed DNA polymerase activity Source: UniProtKB-KW
  3. exonuclease activity Source: UniProtKB-KW
  4. metal ion binding Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

DNA-directed DNA polymerase, Exonuclease, Hydrolase, Nuclease, Nucleotidyltransferase, Transferase

Keywords - Biological processi

DNA replication

Keywords - Ligandi

Magnesium, Manganese, Metal-binding

Enzyme and pathway databases

BioCyciBAPH198804:GHMG-253-MONOMER.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA polymerase III subunit epsilon (EC:2.7.7.7)
Gene namesi
Name:dnaQ
Synonyms:mutD
Ordered Locus Names:BUsg_240
OrganismiBuchnera aphidicola subsp. Schizaphis graminum (strain Sg)
Taxonomic identifieri198804 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera
ProteomesiUP000000416: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 233233DNA polymerase III subunit epsilonPRO_0000105481Add
BLAST

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. The composition of the holoenzyme is, therefore: (alpha,epsilon,theta)[2]-(gamma/tau)[3]-delta,delta', psi,chi-beta[4] (By similarity).By similarity

Protein-protein interaction databases

STRINGi198804.BUsg240.

Structurei

3D structure databases

ProteinModelPortaliQ08880.
SMRiQ08880. Positions 6-178.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Phylogenomic databases

eggNOGiCOG0847.
KOiK02342.
OMAiGFMDHEF.
OrthoDBiEOG696BTR.

Family and domain databases

Gene3Di3.30.420.10. 1 hit.
InterProiIPR006054. DnaQ.
IPR006309. DnaQ_proteo.
IPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamiPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTiSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMiSSF53098. SSF53098. 1 hit.
TIGRFAMsiTIGR00573. dnaq. 1 hit.
TIGR01406. dnaQ_proteo. 1 hit.

Sequencei

Sequence statusi: Complete.

Q08880-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNNTQRIIVL DTETTGMNSV GPPYLNHRII EIGAIEIINR RFTGKKFHTY
60 70 80 90 100
IKPNRLIESD ASKIHGITDD FLSDKPSFKD IAKDFFNYIK NSELIIHNAS
110 120 130 140 150
FDVGFINQEF SMLTKKIQDI SNFCNIIDTL KIARKLFPGK KNTLDALCMR
160 170 180 190 200
YKIKNSHRVL HGAILDAFLL GKLYLLMTSG QESIIFNKNI QNERNFRYIK
210 220 230
KSITKKHRFL KIIKANKTEL KLHNEYLKFL KEK
Length:233
Mass (Da):27,170
Last modified:November 1, 1997 - v2
Checksum:iF722E4C65DB1E583
GO

Sequence cautioni

The sequence AAM67799.1 differs from that shown. Reason: Erroneous initiation. Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77464 Genomic DNA. Translation: AAC44791.1.
AE013218 Genomic DNA. Translation: AAM67799.1. Different initiation.
L18927 Genomic DNA. Translation: AAA17435.1.
PIRiI40594.
RefSeqiNP_660588.1. NC_004061.1.
WP_011053766.1. NC_004061.1.

Genome annotation databases

EnsemblBacteriaiAAM67799; AAM67799; BUsg_240.
GeneIDi1005441.
KEGGibas:BUsg240.
PATRICi21247281. VBIBucAph100086_0251.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U77464 Genomic DNA. Translation: AAC44791.1 .
AE013218 Genomic DNA. Translation: AAM67799.1 . Different initiation.
L18927 Genomic DNA. Translation: AAA17435.1 .
PIRi I40594.
RefSeqi NP_660588.1. NC_004061.1.
WP_011053766.1. NC_004061.1.

3D structure databases

ProteinModelPortali Q08880.
SMRi Q08880. Positions 6-178.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 198804.BUsg240.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAM67799 ; AAM67799 ; BUsg_240 .
GeneIDi 1005441.
KEGGi bas:BUsg240.
PATRICi 21247281. VBIBucAph100086_0251.

Phylogenomic databases

eggNOGi COG0847.
KOi K02342.
OMAi GFMDHEF.
OrthoDBi EOG696BTR.

Enzyme and pathway databases

BioCyci BAPH198804:GHMG-253-MONOMER.

Family and domain databases

Gene3Di 3.30.420.10. 1 hit.
InterProi IPR006054. DnaQ.
IPR006309. DnaQ_proteo.
IPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view ]
Pfami PF00929. RNase_T. 1 hit.
[Graphical view ]
SMARTi SM00479. EXOIII. 1 hit.
[Graphical view ]
SUPFAMi SSF53098. SSF53098. 1 hit.
TIGRFAMsi TIGR00573. dnaq. 1 hit.
TIGR01406. dnaQ_proteo. 1 hit.
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Evolution of dnaQ, the gene encoding the editing 3' to 5' exonuclease subunit of DNA polymerase III holoenzyme in Gram-negative bacteria."
    Huang Y., Braithwaite D.K., Ito J.
    FEBS Lett. 400:94-98(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sg.
  3. "Buchnera aphidicola (a prokaryotic endosymbiont of aphids) contains a putative 16S rRNA operon unlinked to the 23S rRNA-encoding gene: sequence determination, and promoter and terminator analysis."
    Munson M.A., Baumann L., Baumann P.
    Gene 137:171-178(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-179.

Entry informationi

Entry nameiDPO3E_BUCAP
AccessioniPrimary (citable) accession number: Q08880
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1994
Last sequence update: November 1, 1997
Last modified: November 26, 2014
This is version 101 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. Buchnera aphidicola (subsp. Schizaphis graminum)
    Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

External Data

Dasty 3