ID A4IRQ9_GEOTN Unreviewed; 1095 AA.
AC A4IRQ9;
DT 01-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 102.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=GTNG_2668 {ECO:0000313|EMBL:ABO68013.1};
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246 {ECO:0000313|EMBL:ABO68013.1, ECO:0000313|Proteomes:UP000001578};
RN [1] {ECO:0000313|EMBL:ABO68013.1, ECO:0000313|Proteomes:UP000001578}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2 {ECO:0000313|EMBL:ABO68013.1,
RC ECO:0000313|Proteomes:UP000001578};
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
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; CP000557; ABO68013.1; -; Genomic_DNA.
DR AlphaFoldDB; A4IRQ9; -.
DR KEGG; gtn:GTNG_2668; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_1_9; -.
DR Proteomes; UP000001578; 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 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 InterPro; IPR011708; DNA_pol3_alpha_NTPase_dom.
DR InterPro; IPR041931; DNA_pol3_alpha_thumb_dom.
DR InterPro; IPR040982; DNA_pol3_finger.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
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; 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 Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 6..73
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1095 AA; 121299 MW; 1F11B5D01F5EBE87 CRC64;
MAMTFVHLHV LSGYSLFQST ATVEALVAKA KQLGYRALAL TDHQVLYGAI PFYRECQRHG
LRPIIGMMAD VVLDGDSGAF PLVLLAANEE GYRHLIEIST AVQMREEKHV HEAALRRLSG
GIIAITPGLN GRVESFLAAG EVAQAKETLL RYRQLFAGRL YIAIQRGERT RAPYESALLR
LAEETGVPVV ATNEVRYVER EDALAWRCLQ AIGDGVPLAH IPEEDERYLA ALDEMARRFA
DLPEALENSM NIANQCELHI EFGHWRLPKF PVPDGETADS YLRRLCEQGL ARRVPSADAR
YRERLEHELH IIQTMRFSDY FLIVADVLAY ARQRGILTGP GRGSAAGSLV AYALSITDVD
PIEYGLLFER FLNPERVSVP DIDLDFPDDR REEVIRYVVE TYGRDHVAQI ITFGTFGAKA
ALRETAKVLG VSGREAERVM ALLPNKQGVT ISQWHRESAA FRRALRALPD GERWLTIAKK
LEGLPRHTSI HAAGVIISPD PLMRHVPLQP SHGEWPLTQY AMGALEALGL LKIDFLGLRT
LTLLGQMVRL IERQTGKPFD VRALPLDDEK TYALLSAGDT SGVFQLESSG MKRVLAELRP
ATLEEIVAVN ALYRPGPMNM IPTYIRRKRG EEAISYLHPD LEPILAPTYG VLIYQEQIMQ
IAARIAGFSL GKADVLRRAV AKKEKALLAE HREAFVAGCV ANGYPAPMAE ELYRQIVRFA
DYGFNRSHAV SYTLLSYALA YIKAHYPLCF YAVMLSNASG DREKMVLYSY EAARKGIALL
PPSVNRSGYR FAVEGEAIRA GLATVKHVGS AAKLIIDERK ENGPFADFFD FAVRLLPKGL
ARSALEALIS AGAFDELGEE RGSLLASIEI AIEHVQLMRP YLEAGGLSLK PKYADAPPLS
PAERRQREKE LLGFAVTPHP AAVCRPLFQA VRAVPAAEVH GSPVVVGGCI AELRKTRTKF
GEEMAFITVS DESGELEAVA FPSVYARAAG ELEEGNFVLL AGTVDMRAGR RQLVLRRAER
LPTSALYIHA SLADRSRLSA LKLLLEQHRG STPVYLYDET KRSLLRLPER YGVALTAPLI
DELIALFGAR RLAVK
//
