ID L0H0F0_9GAMM Unreviewed; 350 AA.
AC L0H0F0;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=DNA polymerase III subunit delta' {ECO:0000256|ARBA:ARBA00014363};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=Thimo_2374 {ECO:0000313|EMBL:AGA91110.1};
OS Thioflavicoccus mobilis 8321.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Thioflavicoccus.
OX NCBI_TaxID=765912 {ECO:0000313|EMBL:AGA91110.1, ECO:0000313|Proteomes:UP000010816};
RN [1] {ECO:0000313|EMBL:AGA91110.1, ECO:0000313|Proteomes:UP000010816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=8321 {ECO:0000313|EMBL:AGA91110.1,
RC ECO:0000313|Proteomes:UP000010816};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Lu M., Detter J.C., Han C., Tapia R., Land M.,
RA Hauser L., Kyrpides N., Ivanova N., Pagani I., Vogl K., Liu Z., Imhoff J.,
RA Thiel V., Frigaard N.-U., Bryant D., Woyke T.;
RT "Complete sequence of chromosome of Thioflavicoccus mobilis 8321.";
RL Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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; CP003051; AGA91110.1; -; Genomic_DNA.
DR RefSeq; WP_015281243.1; NC_019940.1.
DR AlphaFoldDB; L0H0F0; -.
DR STRING; 765912.Thimo_2374; -.
DR KEGG; tmb:Thimo_2374; -.
DR PATRIC; fig|765912.4.peg.2324; -.
DR eggNOG; COG0470; Bacteria.
DR HOGENOM; CLU_006229_4_3_6; -.
DR OrthoDB; 9811073at2; -.
DR Proteomes; UP000010816; 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 Reference proteome {ECO:0000313|Proteomes:UP000010816};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 231..341
FT /note="DNA polymerase III delta subunit C-terminal"
FT /evidence="ECO:0000259|Pfam:PF09115"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 350 AA; 37789 MW; BD3B4D7973A88372 CRC64;
MTEARRATAA DPSPGDERCP PPWLQPVWAV LTQARVAGRL PHALLISGPT GIGKRRLATA
FVDALLCSAP GSDQGVNGGA CGRCADCHLL AVGNHPDRLA AGPDPEAKSN EIRVDAIREL
IDREGLTPHR GRRKVVVIDP AHQLNRAAAN SLLKTLEEPA PTTLLVLIAE EPNRLPATIR
SRCQRLALSP PSESAALEWL AGRVGDRDPR RLLHLAHGAP LRALDYLADG RLERHETLFE
GFHGVLAGRR DPVTEARGWI ELDPALSCEW LAGWVSDLLR LTADPACDCL IDLERHAVLK
GLAQGLEPAP AHRYLQRVFE ARGQVDSTIN KQLLFESLLI GLAGLRGSGA
//
