ID   DPO3A_PSEFL             Reviewed;        1173 AA.
AC   Q9XDH6;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   25-MAY-2022, entry version 91.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10229580; DOI=10.1007/pl00006520;
RA   Huang Y.P., Ito J.;
RT   "DNA polymerase C of the thermophilic bacterium Thermus aquaticus:
RT   classification and phylogenetic analysis of the family C DNA polymerases.";
RL   J. Mol. Evol. 48:756-769(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; AF062919; AAD44402.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9XDH6; -.
DR   SMR; Q9XDH6; -.
DR   STRING; 690597.JH730961_gene4523; -.
DR   PRIDE; Q9XDH6; -.
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; 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; 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..1173
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103335"
SQ   SEQUENCE   1173 AA;  131217 MW;  E0BF3158F3876E55 CRC64;
     MPASFVHLRL HTEYSLVDGL VRIKPLVKAL TGMGMPAVAV TDQNNMCSLV KFYKNAMGAG
     IKPICGADLW LSNKDPDGPL SRISLLVMNA QGYRNLTELI SRGFIDGQRN GMVIIEREWV
     AEANEGLIML SAAKEGEIGM AMIGGNPAEA EALAREWMAV FPDRFYLEIQ RTNRPNDEEQ
     LHGAVALADK LGAPLVATND VRFIKQEDFA AHETRVCIGE GRALDDPRRS KNYSDQQYLK
     SAEEMAELFS DLPDAIENTV EIAKRCNIDV KLGKHFLPDY PIPDGMTIDE YFRKVSFDGL
     EERLSVLLPK DTTEDYEAKR QVYVDRLNFE LDIIIQMGFP GYFLIVMDFI QWAKNNGVPV
     GPGRGSGAGS LVAYVQKITD LDPLEYDLLF ERFLNPERVS MPDFDVDFCM DGRDRVIDYV
     AEKYGRNAVS QIITFGSMAA KAVVRDVARA QGKSFGLADR LSKMVPFEVG MTLEKAYEQE
     EILRDFIKVD EEAAEIWEMA RKLEGVVRNV GKHAGGVVIA PTKLTDFSPI YCDEAGDGLV
     TQFDKDDVEA AGLVKFDFLG LRTLTIIDWA LKTINRDRAK VNEPPLDIAF IPLDDKPTYQ
     LLQKAETTAV FQLESRGMKE LIKKLKLDCL EDLIALVALF RPGPLQSGMV DDFINRKHGR
     AELAYPHPDY QYEGLQPVLA PTYGIILYQE QVMQIAQVMA GYTLGGADML RRAMGKKKPE
     EMAKQRGGFI EGCASNNIDA DLAGNIFDLV EKFAGYGFNK SHSAAYGLVS YQTAWLKAHY
     PAPFMAAVLS ADMHNTDKVV TLIEEVRTMK LRLDAPDVNT SEFKFTVNDE GRIVYGLGAI
     KGVGEGPVEA ITEARQAGPF KDLFDFCARV DLKRINKRTL DGLIRSGALD RLGPYFHDEQ
     KAYQANIDRN RAVLLAAMEE AIKSAEQTAR TRDSGHADLF GGLFVEEDAD VYAIHRKAKE
     LTLKERLKGE KDTLGLYLTG HPIDEYEGEI RRFARQRIID LKPARDTQTV AGMIIALRVM
     KNKKGDKMGF ITLDDRSGRI EASLFADAFH SAQSLLQTDA MVVVEGEVSN DDFSGGLRLR
     VKRVMSMEDA RTNLAESLRL KLQTQDLKGD QLRWLGDLLK RHRGACPITM EYTSPDAKTL
     LQFGETWRID PADALIQALR DQFGRDNVFL QYR