ID E1V9Q4_HALED Unreviewed; 329 AA.
AC E1V9Q4;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 54.
DE RecName: Full=DNA polymerase III subunit delta' {ECO:0000256|ARBA:ARBA00014363};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=holB {ECO:0000313|EMBL:CBV41888.1};
GN OrderedLocusNames=HELO_2004 {ECO:0000313|EMBL:CBV41888.1};
OS Halomonas elongata (strain ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198
OS / 1H9).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=768066 {ECO:0000313|EMBL:CBV41888.1, ECO:0000313|Proteomes:UP000008707};
RN [1] {ECO:0000313|Proteomes:UP000008707}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33173 / DSM 2581 / NBRC 15536 / NCIMB 2198 / 1H9
RC {ECO:0000313|Proteomes:UP000008707};
RX PubMed=20849449; DOI=10.1111/j.1462-2920.2010.02336.x;
RA Schwibbert K., Marin-Sanguino A., Bagyan I., Heidrich G., Lentzen G.,
RA Seitz H., Rampp M., Schuster S.C., Klenk H.P., Pfeiffer F., Oesterhelt D.,
RA Kunte H.J.;
RT "A blueprint of ectoine metabolism from the genome of the industrial
RT producer Halomonas elongata DSM 2581(T).";
RL Environ. Microbiol. 13:1973-1994(2011).
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};
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DR EMBL; FN869568; CBV41888.1; -; Genomic_DNA.
DR AlphaFoldDB; E1V9Q4; -.
DR STRING; 768066.HELO_2004; -.
DR KEGG; hel:HELO_2004; -.
DR eggNOG; COG0470; Bacteria.
DR HOGENOM; CLU_006229_4_3_6; -.
DR OrthoDB; 9811073at2; -.
DR Proteomes; UP000008707; Chromosome.
DR GO; GO:0009360; C:DNA polymerase III complex; IEA:InterPro.
DR GO; GO:0008408; F:3'-5' exonuclease activity; 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:UniProtKB-KW.
DR Gene3D; 1.20.272.10; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR InterPro; IPR004622; DNA_pol_HolB.
DR InterPro; IPR015199; DNA_pol_III_delta_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR NCBIfam; TIGR00678; holB; 1.
DR PANTHER; PTHR11669:SF8; DNA POLYMERASE III SUBUNIT DELTA; 1.
DR PANTHER; PTHR11669; REPLICATION FACTOR C / DNA POLYMERASE III GAMMA-TAU SUBUNIT; 1.
DR Pfam; PF13177; DNA_pol3_delta2; 1.
DR Pfam; PF09115; DNApol3-delta_C; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 4: Predicted;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:CBV41888.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CBV41888.1}.
FT DOMAIN 213..323
FT /note="DNA polymerase III delta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09115"
SQ SEQUENCE 329 AA; 36575 MW; 1E4D031D26757C49 CRC64;
MTDIVRPYPW LATRWQEITR LADAGRLPHA LLFAGPKGIG KQSLAEALIA RTLCAAPGEF
ACGQCHACQM LASGYHPDLM RVSPEEGKRQ IRIGPVRDVN AFVSQTAQQG GYRVIVIAPA
EAMNVAASNA LLKSLEEPGG KTLFVLLSDI PSHLLPTIRS RCQQWSLATA DEAQSLAWLG
ERLGGEEDAR FWWRASGGLP LRALELADPE SRALRQQLHE TFDALVRGAE PVAEAARLDR
QSIDAILWYG IAWLEDLIRL GLSGVSAELR NPDLLPLYRQ AVKNARVRDW FRLLDYAREQ
RRLLAEGNNP NPQLVLEAWL VRWAALLRS
//
