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Database: UniProt
Entry: A0A097R021_HAFAL
LinkDB: A0A097R021_HAFAL
Original site: A0A097R021_HAFAL 
ID   A0A097R021_HAFAL        Unreviewed;       344 AA.
AC   A0A097R021;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 37.
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:AIU72086.1};
GN   ORFNames=AT03_06540 {ECO:0000313|EMBL:AIU72086.1};
OS   Hafnia alvei FB1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Hafniaceae; Hafnia.
OX   NCBI_TaxID=1453496 {ECO:0000313|EMBL:AIU72086.1, ECO:0000313|Proteomes:UP000029986};
RN   [1] {ECO:0000313|EMBL:AIU72086.1, ECO:0000313|Proteomes:UP000029986}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB1 {ECO:0000313|EMBL:AIU72086.1,
RC   ECO:0000313|Proteomes:UP000029986};
RX   PubMed=25075225; DOI=10.1186/1757-4749-6-29;
RA   Tan J.Y., Yin W.F., Chan K.G.;
RT   "Gene clusters of Hafnia alvei strain FB1 important in survival and
RT   pathogenesis: a draft genome perspective.";
RL   Gut Pathog. 6:29-29(2014).
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; CP009706; AIU72086.1; -; Genomic_DNA.
DR   RefSeq; WP_025800652.1; NZ_CP009706.1.
DR   AlphaFoldDB; A0A097R021; -.
DR   KEGG; hav:AT03_06540; -.
DR   PATRIC; fig|1453496.5.peg.1312; -.
DR   eggNOG; COG1466; Bacteria.
DR   HOGENOM; CLU_044694_0_2_6; -.
DR   OrthoDB; 9770982at2; -.
DR   Proteomes; UP000029986; 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:UP000029986}.
FT   DOMAIN          21..190
FT                   /note="DNA polymerase III delta N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF06144"
FT   DOMAIN          214..337
FT                   /note="DNA polymerase III subunit delta C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14840"
SQ   SEQUENCE   344 AA;  39075 MW;  2A9197E3FE15B178 CRC64;
     MTRVYPEQLA AQLREGLRAC YLVMGNEPLL LQESLDLIRQ QAQEHGFTEY FTFALDAHTD
     WESIFSLSQA MSLFASRQII SLTLPENGAN AAIGEQLTKL STLLHPDLLL IIRGNKPTKA
     QENAGWFKTL SQNAVMISCQ TPEQAQLPRW VATRAKQMNL QLDEAANQLI CYCYEGNLLA
     LSQALERLSL LYPDGKLTLP RVEEAVSDAA HFSPFHWVDA ILAGRSKRAW HILQQLRQED
     MEPVILLRTV QREVLLLMTL KSQMSHTPLR NLFDQHKVWQ NRRPAMTQAL QLLSLQQLHQ
     SIALLSHIEV ILKQDYGQSV WSELESLTLL LCGKSLPESM LNAE
//
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