ID   DPO3A_STRPY             Reviewed;        1034 AA.
AC   P0C0F2; Q9FDF6;
DT   13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 74.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE;
OS   Streptococcus pyogenes.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1314;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10878011; DOI=10.1074/jbc.m003565200;
RA   Bruck I., O'Donnell M.;
RT   "The DNA replication machine of a Gram-positive organism.";
RL   J. Biol. Chem. 275:28971-28983(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; AF280766; AAF98350.1; -; Genomic_DNA.
DR   AlphaFoldDB; P0C0F2; -.
DR   SMR; P0C0F2; -.
DR   PRIDE; P0C0F2; -.
DR   eggNOG; COG0587; Bacteria.
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   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; 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; 2.
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; Transferase.
FT   CHAIN           1..1034
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103349"
SQ   SEQUENCE   1034 AA;  118964 MW;  8BCC969533A4ED53 CRC64;
     MFAQLDTKTV YSFMDSLIDL NHYFERAKQF GYHTIGIMDK DNLYGAYHFI KGCQKNGLQP
     VLGLEIEILY QERQVLLNLI AQNTQGYHQL LKISTAKMSG KLHMDYFCQH LEGIAVIIPS
     KGWSDTLVVP FDYYMGVDQY TDLSHMDSKR QLIPLRTVRY FAQDDMETLH MLHAIRDNLS
     LAETPVVESD QELADCQQLT AFYQTHCPQA LQNLEDLVSG IYYDFDTNLK LPHFNRDKSA
     KQELQDLTEA GLKEKGLWKE PYQSRLLHEL VIISDMGFDD YFLIVWDLLR FGRSKGYYMG
     MGRGSAAGSL VAYALNITGI DPVQHDLLFE RFLNKERYSM PDIDIDLPDI YRSEFLRYVR
     NRYGSDHSAQ IVTFSTFGQA IRDVFKRFGV PEYELTNLTK KIGFKDSLAT VYEKSISFRQ
     VINSRTEFQK AFAIAKRIEG NPRQTSIHAA GIVMSDDALT NHIPLKSGDD MMITQYDAHA
     VEANGLLKMD FLGLRNLTFV QKMQEKVAKD YGCQIDITAI DLEDPQTLAL FAKGDTKGIF
     QFEQNGAINL LKRIKPQRFE EIVATTSLNR PGASDYTTNF IKRREGQEKI DLIDPVIAPI
     LEPTYGIMLY QEQVMQIAQV YAGFTLGKAD LLRRAMSKKN LQEMQKMEED FIASAKHLGR
     AEETARGLFK RMEKFAGYGF NRSHAFAYSA LAFQLAYFKA HYPAVFYDIM MNYSSSDYIT
     DALESDFQVA QVTINSIPYT DKIEASKIYM GLKNIKGLPR DFAYWIIEQR PFNSVEDFLT
     RTPEKYQKKV FLEPLIKIGL FDCFEPNRKK ILDNLDGLLV FVNELGSLFS DSSFSWVDTK
     DYSVTEKYSL EQEIVGVGMS KHPLIDIAEK STQTFTPISQ LVKESEAVVL IQIDSIRIIR
     TKTSGQQMAF LSVNDTKKKL DVTLFPQEYA IYKDQLKEGE FYYLKGRIKE RDHRLQMVCQ
     QVQMAISQKY WLLVENHQFD SQISEILGAF PGTTPVVIHY QKNKETIALT KIQVHVTENL
     KEKLRPFVLK TVFR