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Database: UniProt
Entry: Q7VRA8_BLOFL
LinkDB: Q7VRA8_BLOFL
Original site: Q7VRA8_BLOFL 
ID   Q7VRA8_BLOFL            Unreviewed;       344 AA.
AC   Q7VRA8;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   RecName: Full=DNA polymerase III subunit delta {ECO:0000256|ARBA:ARBA00017703};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=holA {ECO:0000313|EMBL:CAD83381.1};
GN   OrderedLocusNames=Bfl311 {ECO:0000313|EMBL:CAD83381.1};
OS   Blochmannia floridanus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; ant endosymbionts; Blochmannia.
OX   NCBI_TaxID=203907 {ECO:0000313|EMBL:CAD83381.1, ECO:0000313|Proteomes:UP000002192};
RN   [1] {ECO:0000313|EMBL:CAD83381.1, ECO:0000313|Proteomes:UP000002192}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12886019; DOI=10.1073/pnas.1533499100;
RA   Gil R., Silva F.J., Zientz E., Delmotte F., Gonzalez-Candelas F.,
RA   Latorre A., Rausell C., Kramerbeek J., Gadau J., Hoelldobler B.,
RA   van Ham R.C.H.J., Gross R., Moya A.;
RT   "The genome sequence of Blochmannia floridanus: comparative analysis of
RT   reduced genomes.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:9388-9393(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2'-deoxyribonucleoside 5'-triphosphate + DNA(n) =
CC         diphosphate + DNA(n+1); Xref=Rhea:RHEA:22508, Rhea:RHEA-COMP:17339,
CC         Rhea:RHEA-COMP:17340, ChEBI:CHEBI:33019, ChEBI:CHEBI:61560,
CC         ChEBI:CHEBI:173112; EC=2.7.7.7;
CC         Evidence={ECO:0000256|ARBA:ARBA00024632};
CC   -!- SIMILARITY: Belongs to the DNA polymerase HolA subunit family.
CC       {ECO:0000256|ARBA:ARBA00034754}.
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DR   EMBL; BX248583; CAD83381.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7VRA8; -.
DR   STRING; 203907.Bfl311; -.
DR   KEGG; bfl:Bfl311; -.
DR   eggNOG; COG1466; Bacteria.
DR   HOGENOM; CLU_044694_0_2_6; -.
DR   OrthoDB; 9770982at2; -.
DR   Proteomes; UP000002192; Chromosome.
DR   GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
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:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd18138; HLD_clamp_pol_III_delta; 1.
DR   Gene3D; 1.10.8.60; -; 1.
DR   Gene3D; 1.20.272.10; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR008921; DNA_pol3_clamp-load_cplx_C.
DR   InterPro; IPR032780; DNA_pol3_delt_C.
DR   InterPro; IPR010372; DNA_pol3_delta_N.
DR   InterPro; IPR005790; DNA_polIII_delta.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   NCBIfam; TIGR01128; holA; 1.
DR   PANTHER; PTHR34388; DNA POLYMERASE III SUBUNIT DELTA; 1.
DR   PANTHER; PTHR34388:SF1; DNA POLYMERASE III SUBUNIT DELTA; 1.
DR   Pfam; PF14840; DNA_pol3_delt_C; 1.
DR   Pfam; PF06144; DNA_pol3_delta; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF48019; post-AAA+ oligomerization domain-like; 1.
PE   3: Inferred from homology;
KW   Nucleotidyltransferase {ECO:0000313|EMBL:CAD83381.1};
KW   Transferase {ECO:0000313|EMBL:CAD83381.1}.
FT   DOMAIN          21..192
FT                   /note="DNA polymerase III delta N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06144"
FT   DOMAIN          218..339
FT                   /note="DNA polymerase III subunit delta C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14840"
SQ   SEQUENCE   344 AA;  41251 MW;  144683C096298E1A CRC64;
     MNWIYPEQLI LELKKKTKFI YILFGNDFYL IQDCHINILN TIKEQSLSID HFRIGSSVCF
     DWDKVFQLCQ TTHLFSTQQI LSLQFPKNYP STYFDKNIPS LISTLTYNKL LFILLIHTSL
     PMTQYQTWIK LFDKTGILVN CNTLEYTRLE KWVKKQSQLM NLTLENLACQ LLCYYYEGNI
     ILLQQILQHL SLIYPDKKIS FDRLKNIITD SACFNVNHWI ESILLGKKKR ANRILEQLKY
     TNDNLQTLLY KIQREMLVII QIKYNIIFHG KMLYTLFKKY NVYTQYRRML LSQVIRRLNL
     TQLNKILELL VLMELQYHKN HVYLSSSNFE LLTEMLCCNC YDNK
//
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