(data stored in ACNUC9543 zone)

SWISSPROT: A0A0E1NX72_YERPA

ID   A0A0E1NX72_YERPA        Unreviewed;       254 AA.
AC   A0A0E1NX72;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 21.
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=YPA_0560 {ECO:0000313|EMBL:ABG12528.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12528.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12528.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12528.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(2006).
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: The DNA polymerase holoenzyme is a complex that contains
CC       10 different types of subunits. These subunits are organized into
CC       3 functionally essential subassemblies: the pol III core, the beta
CC       sliding clamp processivity factor and the clamp-loading complex.
CC       The pol III core (subunits alpha,epsilon and theta) contains the
CC       polymerase and the 3'-5' exonuclease proofreading activities. The
CC       polymerase is tethered to the template via the sliding clamp
CC       processivity factor. The clamp-loading complex assembles the beta
CC       processivity factor onto the primer template and plays a central
CC       role in the organization and communication at the replication
CC       fork. This complex contains delta, delta', psi and chi, and copies
CC       of either or both of two different DnaX proteins, gamma and tau.
CC       {ECO:0000256|RuleBase:RU364087}.
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DR   EMBL; CP000308; ABG12528.1; -; Genomic_DNA.
DR   RefSeq; WP_002210700.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12528; ABG12528; YPA_0560.
DR   EnsemblBacteria; AJJ81574; AJJ81574; CH58_3416.
DR   KEGG; ypa:YPA_0560; -.
DR   PATRIC; fig|360102.15.peg.3581; -.
DR   KO; K02342; -.
DR   OMA; FHVYLNP; -.
DR   Proteomes; UP000001971; 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; A0A0E1NX72.
DR   SWISS-2DPAGE; A0A0E1NX72.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
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:ABG12528.1};
KW   Transferase {ECO:0000256|RuleBase:RU364087,
KW   ECO:0000313|EMBL:ABG12528.1}.
SQ   SEQUENCE   254 AA;  28762 MW;  1782D1FAEC10202D CRC64;
     MIITPTRQIV LDTETTGMNK LGVHYEGHRI IEIGAVEVIN RRLTGRNFHV YVKPDRLVDP
     EAYGVHGISD EFLADKPTFA DITPEFLDFI RGAELVIHNA AFDIGFMDYE FRMLQQDIPK
     TETFCTITDS LLMARRLFPG KRNNLDALCD RYQIDNTKRT LHGALLDAEI LAEVYLAMTG
     GQTSLTFSME GEVSQNNASE DIQRITRPAS ALKIIYATED ELANHESRLD FVMKKGGSCL
     WRMPLEAEEE TKAE
//

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