ID   DPO3A_AQUAE             Reviewed;        1161 AA.
AC   O67125;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 126.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=aq_1008;
OS   Aquifex aeolicus (strain VF5).
OC   Bacteria; Aquificae; Aquificales; Aquificaceae; Aquifex.
OX   NCBI_TaxID=224324;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VF5;
RX   PubMed=9537320; DOI=10.1038/32831;
RA   Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L.,
RA   Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R.,
RA   Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.;
RT   "The complete genome of the hyperthermophilic bacterium Aquifex aeolicus.";
RL   Nature 392:353-358(1998).
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; AE000657; AAC07087.1; -; Genomic_DNA.
DR   PIR; B70387; B70387.
DR   RefSeq; NP_213688.1; NC_000918.1.
DR   RefSeq; WP_010880626.1; NC_000918.1.
DR   AlphaFoldDB; O67125; -.
DR   SMR; O67125; -.
DR   STRING; 224324.aq_1008; -.
DR   PRIDE; O67125; -.
DR   EnsemblBacteria; AAC07087; AAC07087; aq_1008.
DR   KEGG; aae:aq_1008; -.
DR   PATRIC; fig|224324.8.peg.788; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_0; -.
DR   InParanoid; O67125; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000798; 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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR   Gene3D; 1.10.10.1600; -; 1.
DR   Gene3D; 2.40.50.140; -; 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; IPR012340; NA-bd_OB-fold.
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   SMART; SM00481; POLIIIAc; 1.
DR   SUPFAM; SSF50249; SSF50249; 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..1161
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103308"
SQ   SEQUENCE   1161 AA;  133208 MW;  619F7436E1262BD4 CRC64;
     MSKDFVHLHL HTQFSLLDGA IKIDELVKKA KEYGYKAVGM SDHGNLFGSY KFYKALKAEG
     IKPIIGMEAY FTTGSRFDRK TKTSEDNITD KYNHHLILIA KDDKGLKNLM KLSTLAYKEG
     FYYKPRIDYE LLEKYGEGLI ALTACLKGVP TYYASINEVK KAEEWVKKFK DIFGDDLYLE
     LQANNIPEQE VANRNLIEIA KKYDVKLIAT QDAHYLNPED RYAHTVLMAL QMKKTIHELS
     SGNFKCSNED LHFAPPEYMW KKFEGKFEGW EKALLNTLEV MEKTADSFEI FENSTYLLPK
     YDVPPDKTLE EYLRELAYKG LRQRIERGQA KDTKEYWERL EYELEVINKM GFAGYFLIVQ
     DFINWAKKND IPVGPGRGSA GGSLVAYAIG ITDVDPIKHG FLFERFLNPE RVSMPDIDVD
     FCQDNREKVI EYVRNKYGHD NVAQIITYNV MKAKQTLRDV ARAMGLPYST ADKLAKLIPQ
     GDVQGTWLSL EEMYKTPVEE LLQKYGEHRT DIEDNVKKFR QICEESPEIK QLVETALKLE
     GLTRHTSLHA AGVVIAPKPL SELVPLYYDK EGEVATQYDM VQLEELGLLK MDFLGLKTLT
     ELKLMKELIK ERHGVDINFL ELPLDDPKVY KLLQEGKTTG VFQLESRGMK ELLKKLKPDS
     FDDIVAVLAL YRPGPLKSGL VDTYIKRKHG KEPVEYPFPE LEPVLKETYG VIVYQEQVMK
     MSQILSGFTP GEADTLRKAI GKKKADLMAQ MKDKFIQGAV ERGYPEEKIR KLWEDIEKFA
     SYSFNKSHSV AYGYISYWTA YVKAHYPAEF FAVKLTTEKN DNKFLNLIKD AKLFGFEILP
     PDINKSDVGF TIEGENRIRF GLARIKGVGE ETAKIIVEAR KKYKQFKGLA DFINKTKNRK
     INKKVVEALV KAGAFDFTKK KRKELLAKVA NSEKALMATQ NSLFGAPKEE VEELDPLKLE
     KEVLGFYISG HPLDNYEKLL KNRYTPIEDL EEWDKESEAV LTGVITELKV KKTKNGDYMA
     VFNLVDKTGL IECVVFPGVY EEAKELIEED RVVVVKGFLD EDLETENVKF VVKEVFSPEE
     FAKEMRNTLY IFLKREQALN GVAEKLKGII ENNRTEDGYN LVLTVDLGDY FVDLALPQDM
     KLKADRKVVE EIEKLGVKVI I