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P57337 (DPO3E_BUCAI) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 81. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
DNA polymerase III subunit epsilon

EC=2.7.7.7
Gene names
Name:dnaQ
Ordered Locus Names:BU248
OrganismBuchnera aphidicola subsp. Acyrthosiphon pisum (strain APS) (Acyrthosiphon pisum symbiotic bacterium) [Reference proteome] [HAMAP]
Taxonomic identifier107806 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length237 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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.

Catalytic activity

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

Cofactor

Binds 2 divalent metal cations. Magnesium or manganese By similarity.

Subunit structure

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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 237237DNA polymerase III subunit epsilon
PRO_0000105480

Sites

Active site1591Proton acceptor By similarity
Metal binding101Divalent metal cation 1; catalytic By similarity
Metal binding101Divalent metal cation 2; catalytic By similarity
Metal binding121Divalent metal cation 1; catalytic By similarity
Metal binding1641Divalent metal cation 1; catalytic By similarity
Binding site101Substrate By similarity
Binding site121Substrate By similarity
Binding site641Substrate By similarity
Binding site1641Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
P57337 [UniParc].

Last modified December 1, 2000. Version 1.
Checksum: 3E4C4F102C50EBB7

FASTA23727,365
        10         20         30         40         50         60 
MNRKRTIILD TETTGINQTS LPHINHRIIE IGAVEIIDRC FTGNNFHVYI QPGRSIESGA 

        70         80         90        100        110        120 
LKVHGITNKF LLDKPIFKDI ADSFLNYIKN SILVIHNASF DVGFINQELE ILNKKIKINT 

       130        140        150        160        170        180 
FCSIIDTLKI ARELFPGKKN TLDALCTRYK INKSHRNLHS AIVDSYLLGK LYLLMTGGQD 

       190        200        210        220        230 
SLFSDNTINY KENFKKLKKN IQLKNNTLRI LHPTLKENDL HEKYLQYMKD KSTCLWN 

« Hide

References

[1]"Genome sequence of the endocellular bacterial symbiont of aphids Buchnera sp. APS."
Shigenobu S., Watanabe H., Hattori M., Sakaki Y., Ishikawa H.
Nature 407:81-86(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: APS.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000003 Genomic DNA. Translation: BAB12959.1.
RefSeqNP_240073.1. NC_002528.1.

3D structure databases

ProteinModelPortalP57337.
SMRP57337. Positions 5-177.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB12959; BAB12959; BAB12959.
GeneID1109688.
KEGGbuc:BU248.
PATRIC21244020. VBIBucAph127364_0259.

Phylogenomic databases

eggNOGCOG0847.
HOGENOMHOG000258616.
KOK02342.
OMAFHVYLNP.
OrthoDBEOG696BTR.
ProtClustDBCLSK315823.

Enzyme and pathway databases

BioCycBAPH107806:GBZJ-248-MONOMER.

Family and domain databases

Gene3D3.30.420.10. 1 hit.
InterProIPR006054. DnaQ.
IPR006309. DnaQ_proteo.
IPR006055. Exonuclease.
IPR013520. Exonuclease_RNaseT/DNA_pol3.
IPR012337. RNaseH-like_dom.
[Graphical view]
PfamPF00929. RNase_T. 1 hit.
[Graphical view]
SMARTSM00479. EXOIII. 1 hit.
[Graphical view]
SUPFAMSSF53098. SSF53098. 1 hit.
TIGRFAMsTIGR00573. dnaq. 1 hit.
TIGR01406. dnaQ_proteo. 1 hit.
ProtoNetSearch...

Entry information

Entry nameDPO3E_BUCAI
AccessionPrimary (citable) accession number: P57337
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: April 16, 2014
This is version 81 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Acyrthosiphon pisum)

Buchnera aphidicola (subsp. Acyrthosiphon pisum): entries and gene names