ID   DPO3A_ALKHC             Reviewed;        1116 AA.
AC   Q9K838;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 128.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=BH3169;
OS   Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344
OS   / JCM 9153 / C-125) (Bacillus halodurans).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=272558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125;
RX   PubMed=11058132; DOI=10.1093/nar/28.21.4317;
RA   Takami H., Nakasone K., Takaki Y., Maeno G., Sasaki R., Masui N., Fuji F.,
RA   Hirama C., Nakamura Y., Ogasawara N., Kuhara S., Horikoshi K.;
RT   "Complete genome sequence of the alkaliphilic bacterium Bacillus halodurans
RT   and genomic sequence comparison with Bacillus subtilis.";
RL   Nucleic Acids Res. 28:4317-4331(2000).
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. This DNA
CC       polymerase also exhibits 3' to 5' exonuclease activity. The alpha chain
CC       is the DNA polymerase (By similarity). {ECO:0000250}.
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   -!- SUBUNIT: DNA polymerase III contains a core (composed of alpha, epsilon
CC       and theta chains) that associates with a tau subunit. This core
CC       dimerizes to form the PolIII' complex. PolIII' associates with the
CC       gamma complex (composed of gamma, delta, delta', psi and chi chains)
CC       and with the beta chain to form the complete DNA polymerase III complex
CC       (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC       subfamily. {ECO:0000305}.
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DR   EMBL; BA000004; BAB06888.1; -; Genomic_DNA.
DR   PIR; A84046; A84046.
DR   RefSeq; WP_010899312.1; NC_002570.2.
DR   AlphaFoldDB; Q9K838; -.
DR   SMR; Q9K838; -.
DR   STRING; 272558.10175791; -.
DR   EnsemblBacteria; BAB06888; BAB06888; BAB06888.
DR   KEGG; bha:BH3169; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_1_9; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000001258; 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   Gene3D; 1.10.10.1600; -; 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; 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; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 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; SSF89550; 1.
DR   TIGRFAMs; TIGR00594; polc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..1116
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103309"
SQ   SEQUENCE   1116 AA;  127532 MW;  97181EE0BFFD15F1 CRC64;
     MESVHIHVHS EYTLLSSMCR IPALVEKAKA AQFSALALTD RHVMYGAVPF YKACKESGLK
     PIIGMETTVR FAEDRESDLL LYARSNKGYE HLLKLSTIIQ CREEKEKYVT WEELLAYKDD
     LLYVIPYSGG FVRACLEDEA LERGERFIQF LKDHLGGESV YLEIQGTDRS KVEPINQLAA
     KLAIPLVCSQ HIQVLEREDL DAWKVIQAIR EGVLVEELRI EQEEDVCFFT LTEMEQTFRA
     YPEALQNTKK LADRCHVELT LGKPRLPKFQ TPNEQSAEDY LRKLCEQGAK ERYGEEWTKE
     KAQRLGEELA VIERMGFSDY FLIVWDFMRF AREASIVTGP GRGSVAGSLV AYVLFITDVD
     PLHYDLLFER FLNPERISLP DIDLDFPDHR REEVIVYVKK KYGANRVAQI LTFGTLAARA
     SVRDVGKALA IPPNVIEKIS KEISGRPGMT LVKAYNENER LRQLVHASDE AQKVMKLARK
     VEGLPRHTST HAAGVVISEQ PLTEVIALQH GQGEVPLTQG TMETVEDVGL IKMDFLGLRN
     LTLLEMVVKR VRETYGHSLN VKQLPLNDAK TFALLAKGET TGVFQLESGG MRKVLRELKP
     NTFADIVAVN ALYRPGPMEF IPDYIQGKEG TKEITYLHPD LEPILSSTYG VIVYQEQIMQ
     IAAKMAGFSL GEADLLRRAI SKKKGEALRQ QEEAFVTGAV RQGYEQETAK KIYELIVRFA
     NYGFNKSHAV AYSMLAYQLA YLKAHYPSSF YAALASTIWN QPEKLERLLQ EMKQQGIRVL
     PPSLSKSDIH FSEEEEGVRF PLLPLRYVSV RAIRELIKAR REAPVRSLFD LCSRVDGRIV
     TSRVMESLIK AGALDELGER ATLLANIEEA FQFAEQVKEF QENTGGLFQL SVEEPEYIKV
     EPLTDLEKLA YEKEAVGFYL SGHPLLAYTE SLRQYDRLTY LEGTERRFVK LAGMIHRIRR
     IRTKRGEVMG FLTMSDETGE WEAVVFPAVW AMYEWGLKEG ELYFVEGKMD RGRSEELQLL
     VDKVLPLKHM LKKEKEKLFL KITADVEKEV ERLNDIRRLL QVHHGPTPVV MYYEKQRKTI
     QLPEKYHVSL SFTLLHELEQ LVGKEHVVVS TYEDES