ID   DPO3A_THEMA             Reviewed;         842 AA.
AC   Q9ZHG4;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 2.
DT   25-MAY-2022, entry version 129.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=TM_0461;
OS   Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS   / MSB8).
OC   Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX   NCBI_TaxID=243274;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9826752; DOI=10.1093/nar/26.23.5300;
RA   Huang Y.P., Ito J.;
RT   "The hyperthermophilic bacterium Thermotoga maritima has two different
RT   classes of family C DNA polymerases: evolutionary implications.";
RL   Nucleic Acids Res. 26:5300-5309(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX   PubMed=10360571; DOI=10.1038/20601;
RA   Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA   Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA   Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA   Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA   Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA   Smith H.O., Venter J.C., Fraser C.M.;
RT   "Evidence for lateral gene transfer between Archaea and Bacteria from
RT   genome sequence of Thermotoga maritima.";
RL   Nature 399:323-329(1999).
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; AF063188; AAC80434.1; -; Genomic_DNA.
DR   EMBL; AE000512; AAD35546.1; -; Genomic_DNA.
DR   PIR; E72373; E72373.
DR   RefSeq; NP_228271.1; NC_000853.1.
DR   RefSeq; WP_004081505.1; NZ_CP011107.1.
DR   AlphaFoldDB; Q9ZHG4; -.
DR   SMR; Q9ZHG4; -.
DR   STRING; 243274.THEMA_02385; -.
DR   PRIDE; Q9ZHG4; -.
DR   EnsemblBacteria; AAD35546; AAD35546; TM_0461.
DR   KEGG; tma:TM0461; -.
DR   eggNOG; COG0587; Bacteria.
DR   InParanoid; Q9ZHG4; -.
DR   OMA; AYAHITY; -.
DR   OrthoDB; 561611at2; -.
DR   Proteomes; UP000008183; 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   InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR   InterPro; IPR040982; DNA_pol3_finger.
DR   InterPro; IPR029460; DNAPol_HHH.
DR   InterPro; IPR003141; Pol/His_phosphatase_N.
DR   InterPro; IPR004805; PolC_alpha.
DR   PANTHER; PTHR32294; PTHR32294; 2.
DR   Pfam; PF07733; DNA_pol3_alpha; 2.
DR   Pfam; PF17657; DNA_pol3_finger; 1.
DR   Pfam; PF14579; HHH_6; 1.
DR   SMART; SM00481; POLIIIAc; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; DNA replication; DNA-directed DNA polymerase;
KW   Nucleotidyltransferase; Reference proteome; Transferase.
FT   CHAIN           1..842
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103355"
FT   CONFLICT        377
FT                   /note="I -> M (in Ref. 1; AAC80434)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   842 AA;  96500 MW;  19BB813C8085C277 CRC64;
     MIPWVISPYS FDGSVVRFEK LALLLKRKGL KSVILADRNF HAAVKFNTIM RKHGLIPVHG
     LWKDGRIFVA RNREEFDSLV RYYNGETHEI EDIPVFQESE LTPVRYLDAS EKKASIFMRK
     IFGLDEDVQG FPEKCEDVAD ILNAEAYDLR VNHRFPTPPK NWNELLIKKA EPLGEEYISR
     LKRELEVIKR KGFTPYIYTV EKVVEIAKKM GIKVGPGRGS AVGSLVAYLC GITEVDPIKY
     DLLFERFLNE ERQEPPDIDV DVEDRRRKDL IKELSKSFQV YQVSTFGNLT EKSLKNLINS
     VLPDASLEEK NEIYKTVYGL PHHPSVHAAG VVISENPLPL PTRTEEDIPI TDYDMYDLQE
     IGVVKIDILG LKTLSFIKDF KKEIFDYSDE KTYHLISKGK TLGVFQLEGL QARKLCRRIS
     PRNMDELSIL LALNRPGPLR SGLDVMFSNS KNVPAFFRKM FPETRGVLIY QEQIMRLAMF
     AGLSGTEADI LRRAIAKKER EKMEPLLEKM KKGLLEKGME NAEQILEILL NFSSYAFNKS
     HSVAYAHITY QTAYLKAHHL EEFFKLYFAY NSSDAGKIFL AVQELRNEGY RVHPPDINIS
     GKDLVFHGKD VYLPLTVVKG VGVTLVEQIE KIRPVSSVRE LQERVTGVPR NVVESLITAG
     AFDKLYENRK LALEELNKRV EKDILEIRSL FGEKVEQESS NIKIGDITEL EEKSMGFPLT
     PVHEVPTGLF ARIDDVFTYG RILPVLVKRV SRNIVTDGLS VCRVRTDVPD GVHLVLLSPL
     QKIIKIWPFN ENTRFVYRVD FTATLEKAGQ NEITEVLKNG AVVRYEGYRP LTDEYRYRVV
     PR