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Database: UniProt
Entry: A0A0K1XFR7_9GAMM
LinkDB: A0A0K1XFR7_9GAMM
Original site: A0A0K1XFR7_9GAMM 
ID   A0A0K1XFR7_9GAMM        Unreviewed;       339 AA.
AC   A0A0K1XFR7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   RecName: Full=DNA polymerase III subunit delta {ECO:0000256|ARBA:ARBA00017703};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=AKN88_09735 {ECO:0000313|EMBL:AKX60176.1};
OS   Thiopseudomonas alkaliphila.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Thiopseudomonas.
OX   NCBI_TaxID=1697053 {ECO:0000313|EMBL:AKX60176.1, ECO:0000313|Proteomes:UP000063953};
RN   [1] {ECO:0000313|EMBL:AKX60176.1, ECO:0000313|Proteomes:UP000063953}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=E5571 {ECO:0000313|EMBL:AKX60176.1,
RC   ECO:0000313|Proteomes:UP000063953};
RX   PubMed=26679585;
RA   Lauer A.C., Nicholson A.C., Humrighouse B.W., Emery B., Drobish A.,
RA   Juieng P., Loparev V., McQuiston J.R.;
RT   "Genome Sequences of Oblitimonas alkaliphila gen. nov. sp. nov. (Proposed),
RT   a Novel Bacterium of the Pseudomonadaceae Family.";
RL   Genome Announc. 3:e01474-15(2015).
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; CP012365; AKX60176.1; -; Genomic_DNA.
DR   RefSeq; WP_053101478.1; NZ_CP012365.1.
DR   AlphaFoldDB; A0A0K1XFR7; -.
DR   STRING; 1697053.AKN87_00220; -.
DR   PATRIC; fig|1698449.3.peg.1955; -.
DR   Proteomes; UP000063953; 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   Reference proteome {ECO:0000313|Proteomes:UP000063953}.
FT   DOMAIN          20..191
FT                   /note="DNA polymerase III delta N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06144"
FT   DOMAIN          216..333
FT                   /note="DNA polymerase III subunit delta C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14840"
SQ   SEQUENCE   339 AA;  37558 MW;  D6C6B5EBE0B56E35 CRC64;
     MQLKTDKLSQ QLQQKLLPVY WVSGDELLLC QEACDKIRAT CRQQGFDERQ VLNADRSFDW
     GLLYEAGASL SLFAQKRLIE LRLSSSKPGD KGAKALQEYL ARPPVDTVLL INSPRFDSAT
     LKTKWAKALL DSQDCALLQV QPIARHGLSA WIQQRLSQQG FSADLDALEL IVTRVEGNLL
     AAVQEIEKLK LLTDETHLSL AVIQAAIADS SRYDVFSLTD AALAGDIART VRIINGLRHE
     GTEIPLLLWA VARDLRQLAQ ASQKAQQLGI DAALRHVWPT PRKTLFAQAL KRLTPKDLAP
     LFLLAQQIDE QGKGQAPGDA WSTLTEVLLK LAGQPIFTQ
//
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