(data stored in ACNUC7421 zone)

SWISSPROT: Q13E28_RHOPS

ID   Q13E28_RHOPS            Unreviewed;       231 AA.
AC   Q13E28;
DT   31-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2006, sequence version 1.
DT   08-MAY-2019, entry version 79.
DE   RecName: Full=DNA polymerase III subunit epsilon {ECO:0000256|RuleBase:RU364087};
DE            EC=2.7.7.7 {ECO:0000256|RuleBase:RU364087};
GN   Name=dnaQ {ECO:0000256|RuleBase:RU364087};
GN   OrderedLocusNames=RPD_0423 {ECO:0000313|EMBL:ABE37661.1};
OS   Rhodopseudomonas palustris (strain BisB5).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Bradyrhizobiaceae; Rhodopseudomonas.
OX   NCBI_TaxID=316057 {ECO:0000313|EMBL:ABE37661.1, ECO:0000313|Proteomes:UP000001818};
RN   [1] {ECO:0000313|EMBL:ABE37661.1, ECO:0000313|Proteomes:UP000001818}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BisB5 {ECO:0000313|EMBL:ABE37661.1,
RC   ECO:0000313|Proteomes:UP000001818};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H.,
RA   Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Pelletier D.A., Kyrpides N.,
RA   Lykidis A., Oda Y., Harwood C.S., Richardson P.;
RT   "Complete sequence of Rhodopseudomonas palustris BisB5.";
RL   Submitted (MAR-2006) 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
CC       3'-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-
CC         COMP:11130, Rhea:RHEA-COMP:11131, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61560, ChEBI:CHEBI:83828; 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|RuleBase:RU364087};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000256|RuleBase:RU364087};
CC   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha,
CC       epsilon and theta chains) that associates with a tau subunit. This
CC       core dimerizes to form the POLIII' complex. PolIII' associates
CC       with the gamma complex (composed of gamma, delta, delta', psi and
CC       chi chains) and with the beta chain to form the complete DNA
CC       polymerase III complex. {ECO:0000256|RuleBase:RU364087}.
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DR   EMBL; CP000283; ABE37661.1; -; Genomic_DNA.
DR   RefSeq; WP_011500849.1; NC_007958.1.
DR   STRING; 316057.RPD_0423; -.
DR   EnsemblBacteria; ABE37661; ABE37661; RPD_0423.
DR   KEGG; rpd:RPD_0423; -.
DR   eggNOG; ENOG4108JDX; Bacteria.
DR   eggNOG; COG0847; LUCA.
DR   HOGENOM; HOG000258616; -.
DR   KO; K02342; -.
DR   OMA; FHVYLNP; -.
DR   OrthoDB; 1985371at2; -.
DR   BioCyc; RPAL316057:RPD_RS02175-MONOMER; -.
DR   Proteomes; UP000001818; Chromosome.
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; -; 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   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
DR   TIGRFAMs; TIGR01406; dnaQ_proteo; 1.
PE   4: Predicted;
DR   PRODOM; Q13E28.
DR   SWISS-2DPAGE; Q13E28.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001818};
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   ECO:0000313|EMBL:ABE37661.1};
KW   Transferase {ECO:0000256|RuleBase:RU364087,
KW   ECO:0000313|EMBL:ABE37661.1}.
FT   DOMAIN        2    172       Exonuclease. {ECO:0000259|SMART:SM00479}.
SQ   SEQUENCE   231 AA;  25642 MW;  AF88363F6F476FA5 CRC64;
     MREIVLDTET TGLDPLRGDR LVEIGCVEIY NRMPTGQAFH RYINPERDMP AEAFAVHGLS
     AEFLADKPLF AQVVDEFLDF IGDAPLVIHN ASFDAGFLNA ELARLSRAAI PRERLVDTLL
     LARRKHPGVS NRLDDLCSRY AIDNSRRTKH GALLDAELLA EVYIDLIGAR QSQLILAEVP
     SERAGQGGDK PRRQRSTPLA ARVTELDLDA HRAFIATMGD KAIWKEYPAG A
//

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