ID C5D666_GEOSW Unreviewed; 1104 AA.
AC C5D666;
DT 28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT 28-JUL-2009, sequence version 1.
DT 27-MAR-2024, entry version 87.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=GWCH70_2690 {ECO:0000313|EMBL:ACS25382.1};
OS Geobacillus sp. (strain WCH70).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=471223 {ECO:0000313|EMBL:ACS25382.1};
RN [1] {ECO:0000313|EMBL:ACS25382.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCH70 {ECO:0000313|EMBL:ACS25382.1};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Chertkov O., Brettin T., Detter J.C.,
RA Han C., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA Brumm P., Mead D.A., Richardson P.;
RT "Complete sequence of chromosome of Geopacillus sp. WCH70.";
RL Submitted (JUN-2009) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|ARBA:ARBA00025611}.
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 Evidence={ECO:0000256|ARBA:ARBA00024632};
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
CC complex. {ECO:0000256|ARBA:ARBA00026073}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
CC -!- SIMILARITY: Belongs to the DNA polymerase type-C family. DnaE
CC subfamily. {ECO:0000256|ARBA:ARBA00009496}.
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DR EMBL; CP001638; ACS25382.1; -; Genomic_DNA.
DR AlphaFoldDB; C5D666; -.
DR STRING; 471223.GWCH70_2690; -.
DR KEGG; gwc:GWCH70_2690; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_1_9; -.
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 CDD; cd04485; DnaE_OBF; 1.
DR Gene3D; 1.10.150.870; -; 1.
DR Gene3D; 1.10.10.1600; Bacterial DNA polymerase III alpha subunit, thumb domain; 1.
DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1.
DR Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048472; DNA_pol_IIIA_C.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
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 NCBIfam; TIGR00594; polc; 1.
DR PANTHER; PTHR32294; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR PANTHER; PTHR32294:SF0; DNA POLYMERASE III SUBUNIT ALPHA; 1.
DR Pfam; PF07733; DNA_pol3_alpha; 1.
DR Pfam; PF17657; DNA_pol3_finger; 1.
DR Pfam; PF20914; DNA_pol_IIIA_C; 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; PHP domain-like; 1.
PE 3: Inferred from homology;
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:ACS25382.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ACS25382.1}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1104 AA; 125608 MW; 785A98C044093C5D CRC64;
MLSFVHLHVR SCYSLLTSPA KISDLVKKAK DLQFSALALT DENVLYGAIP FYMECKRYGI
RPIIGMITDI VLEGESTYPL VLLAKNETGY QHLIKISSTI QTKTQEGIPE KWLWHYRGGL
IALTPGKSGQ IETLLAHNEI TKAKQLLERY KQIFGDDFYL SVQRGENKQQ EPYEQQLIHL
SNETNTPLVA TNDVQYIEKE DAFVQHCLLA IKQGAVIKTG MATDGERYLT SPEEMKKRFS
DLPEAVENSR KIADQCHLHI SLDTLKLPKY PVPEKENADH YLRRLCLKGL YERVSSPSDA
YIKRLEYELD VIQQMDFSDY FLIVWDFMNF ARKKGIVTGP GRGSAAGSLV AYTLYITDID
PIQYGLLFER FLNPERVSMP DIDIDFPDDR REEVIQYVAN KYGQQYVAQI ITFGTFGAKA
ALRDIGKVLQ IDSKEMENII KYVPNKHGIT IQEVYHQSFA FRQAVQASSL LKQWIAIAMK
VEGLPRHTST HAAGVIISSE PLSQIVPLQQ GHGELYLTQY PMDVLERLGL LKMDFLGLRT
LTLLEHICRL IQQQTGKTID VRSIPLDDRK TYELVSKGDT NGIFQLESDG MKHVLKQLKP
SQFEDIVAVN ALYRPGPIDY IPSYIKRKHG EENVSYLHPD LAPILAPTYG VLIYQEQIMQ
IAANIAGFSL GKADLLRRAV AKKKKEILDQ QRNEFVQGCI DQGYDEGFAN DVYDMIVRFA
NYGFNRSHAV AYSMLSYQLA YLKAHYPLYF YTALLTSVIG DEEKVSLYIY EARRKQIEIL
PPSINQSRYS FSVEHEKIRY SLAAIKHVGI AAVKAIVQER KKGPFADFFD FCVRLFGKGI
NRKTIESLIL SGCFDEFGIE RASLLASIDV ALEHAQLVGP YVEEGLFSDI SLKPKYVEAP
SLSLEEKLMY EKELLGVYVS PHPTSAYRKV FRLDGVRSVM SVIREKTDFP VKVGVYIVEE
RKTRTKTGKE MAFFTVSDES GEMDVVAFPD VYRRYSSVLK KGTVRLLEGK VEVRKGKAQL
VIRKADVPAM EALYVKIRPE HIASGKLFTL KELLKKYHGK TPVFLYYEQE QKMVKLTEEY
DVALTDECIA SLKALLGDEH IVVK
//
