ID   A0A1B3PLN3_9BURK        Unreviewed;      1177 AA.
AC   A0A1B3PLN3;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=dnaE {ECO:0000313|EMBL:AOG23657.1};
GN   ORFNames=BSY15_3332 {ECO:0000313|EMBL:AOG23657.1};
OS   Acidovorax sp. RAC01.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Acidovorax.
OX   NCBI_TaxID=1842533 {ECO:0000313|EMBL:AOG23657.1, ECO:0000313|Proteomes:UP000094760};
RN   [1] {ECO:0000313|Proteomes:UP000094760}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RAC01 {ECO:0000313|Proteomes:UP000094760};
RA   Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL   Submitted (JUL-2016) 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};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR   EMBL; CP016447; AOG23657.1; -; Genomic_DNA.
DR   RefSeq; WP_069105710.1; NZ_CP016447.1.
DR   AlphaFoldDB; A0A1B3PLN3; -.
DR   STRING; 1842533.BSY15_3332; -.
DR   KEGG; acra:BSY15_3332; -.
DR   PATRIC; fig|1842533.3.peg.3453; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000094760; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0003676; F:nucleic acid binding; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   CDD; cd04485; DnaE_OBF; 1.
DR   CDD; cd07433; PHP_PolIIIA_DnaE1; 1.
DR   Gene3D; 1.10.150.870; -; 1.
DR   Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR   Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR004365; NA-bd_OB_tRNA.
DR   InterPro; IPR004013; PHP_dom.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR016195; Pol/histidinol_Pase-like.
DR   InterPro; IPR049821; PolIIIA_DnaE1_PHP.
DR   NCBIfam; TIGR00594; polc; 1.
DR   PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR   Pfam; PF07733; DNA_pol3_alpha; 1.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   Pfam; PF02811; PHP; 1.
DR   Pfam; PF01336; tRNA_anti-codon; 1.
DR   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF89550; PHP domain-like; 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:AOG23657.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000094760};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AOG23657.1}.
FT   DOMAIN          3..70
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1177 AA;  130042 MW;  E9D8A773A1885DFF CRC64;
     MFVHLRLHTE FSVVDGTNRI DEVAKAAARD GQPALAITDL NNLFGAIKFY KETRGKGVKP
     ILGAEIFVEG EAGAAPARFI VLVQSRQGYL NLSELLARAW TRNIVKNVAV CTWAWIEELG
     EGLIALAGAQ AGPVGQALLK GDDQGAADVA LRMAGIFPHR FYIELQRAGR VDDESHVIAA
     AQLAARLNLP VVATHPVQFA TADDYEAHEA RVCIAEGEIL ANPRRVRKFT RDQYFKSASE
     MEALFADVPS AIANTVEIAQ RCNLTLVLGK PQLPDFPTPN GMPIDEYFRV ASFEGLEERL
     ALLFPKPAER DAQRPRYVER LEFEIGTILK MGFPGYFLIV GDFIQWAKNN GCPVGPGRGS
     GAGSLVAYAL KITDLDPLQY NLLFERFLNP ERVSMPDFDI DFCQSNRDRV IDYVKDKYGK
     NAVSQIATFG TMAAKAAIRD VGRVMDMSYT FCDGISKLVP GKPGMSYTLA YPPAVKKDGD
     KNNYALELEP LLAERVQKEE DVKTIIEMAQ KLEGMTRNIG MHAGGVLIAP GKLTDFCPLY
     QQPGSESAVS QYDKDDVEAI GLVKFDFLGL ATLTILEIAR EFIMKRHKGQ ENFTFEAIPL
     DDGPTYRLFS EGKTEAVFQF ESRGMQGMLK EARPSRLEDL IALNALYRPG PMDLIPSFVN
     RKHGKEVVEY PHPLVEKVLS ETYGIMVYQE QVMQTAQVLG GYSLGGADML RRAMGKKKAE
     EMAEHREIFR AGAAKQGISQ EKADEVFDLM EKFAGYGFNK SHAAAYSLLA YHTGWLKVHF
     TAEFFCANMT VEMDDTDKLK VLFEDAHKMG LSFEPPDVNR GFYRFEPVTD KIIRYGLGAV
     KGTGQQAIEA IVAAREGRGD GPQGSTKGPF KSLFDFCLRV DRARLNKRTV EALIKAGAFD
     SLNMNRASMV ASIDRAFDFA AATLANVNQG GLFDMMGDDA HGSSTQEPDL VEAVPWGIKE
     RLTQEKTAVG FYLSGHLFDE VATEVRRFVR TSIDELLDSR EPQILAGIVS DFRVINGQRG
     KLALFKLDDK SGVIEASADE ALLNTYRNQL KEDEFVVMLG RLQLDHFSGG LRLKVQQVWD
     LAGARCRFGK YLHVVVGDRG PDLQRLVREF PPRREEIAEG ELLHGLKVRM GVRCKADGGA
     ATAELQLGDS AKFYPTDAAL AAWTAQAGTG SATVVYE
//