ID   DPO3A_BUCBP             Reviewed;        1077 AA.
AC   Q89AN8;
DT   13-APR-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 111.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=bbp_220;
OS   Buchnera aphidicola subsp. Baizongia pistaciae (strain Bp).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=224915;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bp;
RX   PubMed=12522265; DOI=10.1073/pnas.0235981100;
RA   van Ham R.C.H.J., Kamerbeek J., Palacios C., Rausell C., Abascal F.,
RA   Bastolla U., Fernandez J.M., Jimenez L., Postigo M., Silva F.J.,
RA   Tamames J., Viguera E., Latorre A., Valencia A., Moran F., Moya A.;
RT   "Reductive genome evolution in Buchnera aphidicola.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:581-586(2003).
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; AE016826; AAO26951.1; -; Genomic_DNA.
DR   RefSeq; WP_011091352.1; NC_004545.1.
DR   AlphaFoldDB; Q89AN8; -.
DR   SMR; Q89AN8; -.
DR   STRING; 224915.bbp_220; -.
DR   EnsemblBacteria; AAO26951; AAO26951; bbp_220.
DR   GeneID; 56470762; -.
DR   KEGG; bab:bbp_220; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000601; 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   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; 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; 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..1077
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103314"
SQ   SEQUENCE   1077 AA;  124313 MW;  6230F4BD1A858DED CRC64;
     MFNFKFVHLR VHSDFSMIDG LVKPNILAQH AKKLNMPAIA ITDSSNLHGM IKFYRATFSQ
     GIKPIIGVDF KVFPDDKYVS SNMFTKITLL AVNNSGYRNL LLLLSRAYKI GYNNKVGVFI
     TKEWLVEHRK GIILLSGGCY GDIGVNLLNN NKSLVLNCLS FYNRFFENFY YLEIMRIGRS
     NEEQYISRIK DISAREGIPV VATNEVCFLN KQDFEVHKIR VFINLGCTIK SNSAHYNYTP
     QQFMRTSNEM EELFLDFPDA ISNTIEISKR CNVILKFNKY FLPKFQTGNM NTTDFLVMKA
     KKGMQKRLIQ LFPNKQDRIN NVNRYYTRLL SELNVINKMG FPGYFLIVME FINWAKKNDI
     PVGPGRGSGA GSLVSYVLNI TELDPLSFDL LFERFLNPER VFMPDLDVDF CMDKRDKVIE
     HVSKIYGEES VSQIISFGTL TAKSVIRDVG RVFGFPYGFL NRLSKLIPLD LGMTLEKAIS
     QKVELLELYK FDKDVRELIN IAKRLEGITR NVSKHAGGVV ISPKKITDFV PLYYDENGNN
     PVTQFDKNDI GYTGLVKFDF LGLKTLTVIH GTVKMINTKF SNNQKKLINI NTISLKDKNC
     FKFLQTAQTI AVFQLESNGM KDLIRRLKPD SFEDLVALVA LFRPGPLQSG MVDNFINRKH
     GKEKILYPNK ECQHALLKPI LKSTYGIILY QEQVMKIVQV FANYTLGHAD LLRRTMEKKD
     QVEMNKHREM FKNGAKENNI NTKLSTKIFN LLEQFAGYAF NKSHSVSYAL VSYQTLWLKL
     YYPEEFMASA MNADIDNIKK IVVLINECKV MKLKIIPPNV NQSDYYFKVD DDKNIIYGLG
     AIKGIGKSVI LDIVNARKNR KRFSELFDLC VSVNSKRITH KVIEKLIMSG GCDCFGLNRS
     ILMHSCEYII KSANQYLKSI ILKKRDLFGL LLDDFNVIKK KYYSIKKLYS MKQILDWEKD
     SLGLYLTGHP VDEHVHLQMR YNNVIRLKDL FNNKITTEQI SILGMISFLK FKVTKTKKNM
     VFMILEDSFV QIEVIIFDNI LRRYRHLLEK EVIIIVTGRI QKSMFSKKYI VLAEKLI