ID   DPO3A_PASMU             Reviewed;        1159 AA.
AC   Q9CPK3;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 128.
DE   RecName: Full=DNA polymerase III subunit alpha;
DE            EC=2.7.7.7;
GN   Name=dnaE; OrderedLocusNames=PM0034;
OS   Pasteurella multocida (strain Pm70).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Pasteurella.
OX   NCBI_TaxID=272843;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pm70;
RX   PubMed=11248100; DOI=10.1073/pnas.051634598;
RA   May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT   "Complete genomic sequence of Pasteurella multocida Pm70.";
RL   Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK02118.1; -; Genomic_DNA.
DR   RefSeq; WP_010906442.1; NC_002663.1.
DR   AlphaFoldDB; Q9CPK3; -.
DR   SMR; Q9CPK3; -.
DR   STRING; 747.DR93_2045; -.
DR   EnsemblBacteria; AAK02118; AAK02118; PM0034.
DR   KEGG; pmu:PM0034; -.
DR   PATRIC; fig|272843.6.peg.34; -.
DR   HOGENOM; CLU_001600_0_0_6; -.
DR   OMA; NECRRMG; -.
DR   Proteomes; UP000000809; 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: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; Reference proteome; Transferase.
FT   CHAIN           1..1159
FT                   /note="DNA polymerase III subunit alpha"
FT                   /id="PRO_0000103333"
SQ   SEQUENCE   1159 AA;  129281 MW;  56CC880303C73F82 CRC64;
     MSEPRFVHLR VHSDFSMING IAKVKPLIKA CVDNHMVAMG LTDFTNFCGL VRFYGEALSA
     GVKPIIGADV LVRSELCGDE PFELTLLAKN NIGYHNITLL LSKAYERGYQ DLPYLDQAWL
     AEHREGIIVL SGGHNGDVGK KLLKGHAAEI ESAVAFYQDF FPDHFYLSLS RTGRYEEERY
     VSLALTLAEE KGLPVVATND VLFLHEDDFE AHEIRVAIHD SYTLDDPKRP KLYTNQQYFR
     SEQEMCDLFA DVPSALENTL LIAQRCNVTI RLGEYFLPQF PTGDLSTEDF LVKKSKEGLE
     ERLKFLFPDE KVRQARRPEY DERLQVELDV INQMGFPGYF LIVMEFIQWS KDNDIPVGPG
     RGSGAGSLVA YALKITDLDP LEFDLLFERF LNPERVSMPD FDVDFCMDGR DRVIDHVAET
     YGRGAVSQII TFGTMAAKAV IRDVGRVLGH PYGFVDRISK LIPPDPGMTL AKAFAAEPQL
     QAVYDSDEEV KALIDMARKL EGVTRNAGKH AGGVVISPGL ITDFSPLYCD SEGKHPVTHF
     DKNDVEYAGL VKFDFLGLRT LTIIKWALDM INTRLAKEGK PPVDIATIPL DDPASFELLK
     RSETTAVFQL ESRGMKDLIK RLQPDCFEDI IALVALFRPG PLESGMVQNF IDRKHGNEVV
     AYPDPEYQHD SLKPILEPTY GVIVYQEQVM QIAQELAGYT LGGADLLRRA MGKKKPEEMA
     AQREIFEKGA IQKGVDGELA MKIFDLVEKF AGYGFNKSHS AAYALVSYQT LWLKTHYPAE
     FMAAVMTSEM DNTDKIVGLY DECLRMGLKV APPDINTGKH HFSVNEYGEI VYGIGAIKGV
     GEGPIEALIS AREQGGIFKD LFDLCARVDL KKINRRTFES LILSGAFDKL GPHRAALSKN
     LEDALKASDQ HAKDAAMGQA DMFGVLTESH EDVEKAYAST PRWSEKVILE GERETLGLYL
     SSHPISPYLK ELAHYSATRL KDLVPNSRGQ MSTVSGLLVS SRFAVTKKGN RLGIATLDDR
     SGRLDITLFG EALDKYADKL QKDTVIIVSG QVSFDEFSGG LKMSVRELMS LDEARSRYAK
     SLAICLSEEN MKPTFIRELK ALLTPYSGGT LPIYVYYAST AGQCRVKMGV QWSVNPTDQL
     FTELAEKLGE NAVELEFQS