ID   DPO3A_BUCAP             Reviewed;        1161 AA.
AC   Q8K9S3;
DT   08-NOV-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=BUsg_233;
OS   Buchnera aphidicola subsp. Schizaphis graminum (strain Sg).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Buchnera.
OX   NCBI_TaxID=198804;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Sg;
RX   PubMed=12089438; DOI=10.1126/science.1071278;
RA   Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S.,
RA   Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.;
RT   "50 million years of genomic stasis in endosymbiotic bacteria.";
RL   Science 296:2376-2379(2002).
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; AE013218; AAM67792.1; -; Genomic_DNA.
DR   RefSeq; WP_011053759.1; NC_004061.1.
DR   AlphaFoldDB; Q8K9S3; -.
DR   SMR; Q8K9S3; -.
DR   STRING; 198804.BUsg_233; -.
DR   PRIDE; Q8K9S3; -.
DR   EnsemblBacteria; AAM67792; AAM67792; BUsg_233.
DR   KEGG; bas:BUsg_233; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OMA; NECRRMG; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000000416; 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   InterPro; IPR018856; Stn1_N.
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; PF10451; Stn1; 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..1161
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103313"
SQ   SEQUENCE   1161 AA;  133577 MW;  83FDB6DA65A85485 CRC64;
     MNLEEFVHLH VHSDYSIVDG LSKPEDLIKK SVNLGMKALS ITDFNNLYGA IKFYNAAHKW
     GLKPIIGVTV KFFSELIKNE LTELTLLATN QDGYKNLILL ISRAYKKGYF CEKYVTIEKK
     WLSELNNGLI LLSGGCQGEI GKTLLRGQTS LISDCLHFYE KYFSGFYYLE LIRTYRENEE
     KYLSLAVDLS YSQNIPVVAT NDVCFLNKED FKIHKIRIAI NEGVRLKESK IQNNYSKHQF
     LKTEKEMCFL FSDIPEAIIN SVEISKRCNV FIKSGQYFLP QFNTRKISIE NYLIQKSNKG
     LKKRLESNFK KVDKEIFLKY KNRLDTELGI INKMGFPSYF LIVMEFIQWA KDNNIPVGPG
     RGSGAGSLVA YVLNITEVDP LFFDLLFERF LNPERISLPD FDIDFCMEKR DRVIEHVVHT
     YGRESVAQII TFGTMTAKAV IRDVGRVLGY PYGFINNLSK LVPLDPGITL KDAFSKNSEL
     YTLYKSDEDI QNLIDVSKKL EGVNRNVGKH AGGVVISPSK ITDFCPVYCD EKGNNPVTQF
     DKNDIEYVGL LKFDFLGLRT LTIINCAVNM INKNLLLSNK KTININSIPL NESKCFLLLK
     KCETTGIFQL ESYGMKDLVK RLQPDCFEDI IALIALFRPG PLQSGMVDNF INRKHGYEEI
     SYPDHKWQHI LLKPVLESTY GIILYQEQVM QIAQILAGYT LGKADILRRA MSKKNIKDMA
     EQRSIFIEGA QKNGINRKLA IKIFDLLEKF AGYGFNKSHS VAYALVSYQT LWLKAHYPSE
     FMASAMTSDI DNTDKIVMLV NESIQMGIKI IPPNINLSKY EFYVDHTKNI VYGLGAVKGI
     GRNPILNLVQ EREKNGLFSD LFDLCMRTDP NKITRKVLEK LIMSGSCDCF NKNRNYLLSL
     IEDAIKASKE HFKIKKFQQE SLFGSFKEEL NILKKNNNLL NSFSDEEKKL ENEHKVLGLY
     LTGHPIDRYA EELKYYLNNS TFSKLKLFNH TKKKIMVAGI VVSIKTKVTK NKNRIVILIL
     DDSTGLLEVV IFKRLLNISE KLIQLNKILI VSGFLNTNFI SKNLKMTAYD IMNLNLAREK
     YLDKLTIVLT EKQRDKCFLK KIYQFFQNQT TGIVPVYIFC KKKDLDSEYK LIKKWLITIS
     NKLLVELDIF SKENKMQIKY F