ID   A0A157ZV83_9BURK        Unreviewed;      1178 AA.
AC   A0A157ZV83;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=AWB79_01423 {ECO:0000313|EMBL:SAK49432.1};
OS   Caballeronia hypogeia.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Caballeronia.
OX   NCBI_TaxID=1777140 {ECO:0000313|EMBL:SAK49432.1, ECO:0000313|Proteomes:UP000054851};
RN   [1] {ECO:0000313|Proteomes:UP000054851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Oliw E.H.;
RL   Submitted (JAN-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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; FCOA02000003; SAK49432.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A157ZV83; -.
DR   STRING; 1777140.AWB79_01423; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000054851; Unassembled WGS sequence.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048472; DNA_pol_IIIA_C.
DR   InterPro; IPR004805; DnaE2/DnaE/PolC.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR012340; NA-bd_OB-fold.
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; PF20914; DNA_pol_IIIA_C; 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   Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Ligase {ECO:0000256|ARBA:ARBA00023146};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          12..79
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          1101..1128
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1178 AA;  130782 MW;  5BA94677E8A3430D CRC64;
     MYNTAMSDPR FVHLRVHSEF SIADGIVRLD DVVAAAAKDG QGALALTDLG NAFGLVRFYK
     EARGKGVKPI AGCDVWITNP DDRDKPSRLL LLVRDKRGYL NLCELLSRAW LTNQYRGRAE
     VLVEWLEEGL AEGLLALSGA QTGDIGMAFA AGNTASAQRN AERWAKLFPN AFYIELQRAG
     QPGEQAYIQE AVKLAAKLKL PVVATHPMQF MTPDDFTAHE ARVCISEGDI LANPRRQKRF
     TQDQFFRTQD EMCALFTDIP SALANTVEIA RRCNLTLELG KPKLPLFPTP DGMSLDDYLV
     QLSKEGLEVR LQQLYPDETE RDAQRETYYA RLDFECGTII KMGFPGYFLI VADFIMWAKN
     NGVPVGPGRG SGAGSLVAYA LGITDLDPLR YNLLFERFLN PERVSMPDFD IDFCQEGRDR
     VIQYVKGKYG ADAVSQIATF GTMAAKAAVR DIGRVLDLGY MFTDGIAKLI PFKPGKHVTI
     ADAMKEEPAL QERFDSEDEV HQLLELAQRV EGLTRNVGMH AGGVLIAPGK LTDFCPLYTQ
     GEDGGVVSQY DKDDVEAVGL VKFDFLGLTT LTILDWAERY IRRLDPSKKD WNLAQVPLDD
     PASFSILKKA NTVAVFQLES RGMQGMLKDA QPDRFEDIIA LVALYRPGPM DLIPSFCARK
     HGREIVEFPD PRVEPVLKET YGIMVYQEQV MQMAQIIGGY SLGGADLLRR AMGKKKPEEM
     AQHRELFADG AAKNGLTREK SDEIFDLMEK FAGYGFNKSH AAAYALLAYY TAWLKAHHPA
     EFMAANMSLA MDDTDKVKIL FEDCATNGLA VLPPDINQSA YRFEPVAEAD GSRSKTIRYG
     LGAVKGSGQN AIEEILRARE DGKFTDLFDF CERIDRRVVN RRTVEALIRS GAFDTIHANR
     AQLLASVPMA MEAADQAAAN AMQAGLFDMG DAPLAKHEYV DEPEWSDKKR LQEEKTALGF
     YLSGHLFDAY KGEVRRFVRQ KIGELKEGRD KLVAGVISAM RTQMTQRGKM LIVNLDDGSG
     QCEVTVFNEQ FEANKALFKE DELLVVQGQA RNDAFTGGIR FTVDTAMDLE RARSRYAQSV
     KVEMNGNADA GRLRRVLEAH AAGAQSEPPP APVRDNGRNG RERQSAPIPN GLNVSIVYRS
     EHAEGEVRLG DAWRVKPTDD LITALRGEFA GSAIEIVY
//