ID A0A2Z2K6C1_9BACL Unreviewed; 1231 AA.
AC A0A2Z2K6C1;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=B9T62_05480 {ECO:0000313|EMBL:ASA20297.1};
OS Paenibacillus donghaensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=414771 {ECO:0000313|EMBL:ASA20297.1, ECO:0000313|Proteomes:UP000249890};
RN [1] {ECO:0000313|EMBL:ASA20297.1, ECO:0000313|Proteomes:UP000249890}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 13049 {ECO:0000313|EMBL:ASA20297.1,
RC ECO:0000313|Proteomes:UP000249890};
RA Jung B.K., Hong S.-J., Shin J.-H.;
RT "Complete genome sequence of Paenibacillus donghaensis KCTC 13049T isolated
RT from East Sea sediment, South Korea.";
RL Submitted (JUN-2017) 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; CP021780; ASA20297.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2Z2K6C1; -.
DR KEGG; pdh:B9T62_05480; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000249890; 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 CDD; cd12113; PHP_PolIIIA_DnaE3; 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 Reference proteome {ECO:0000313|Proteomes:UP000249890};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1080..1154
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1126..1140
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1231 AA; 135214 MW; D393575ABA16FB88 CRC64;
MSPFVHLHVH SEYSLLDGAA RITDLVRRAG EYGMKSLALT DHGVMYGAIP FYKACQAQGI
KPIIGCEAYM TSGSRRERGS RKDQPIYHLI LLVKNETGYK NLMKLVSIGH LEGQHYKPRI
DMEVLAEYAE GIVCLSACLG GEVPQHLLHG REAEARKAAL RYKEIFGPDF YLELQDHGMA
EQKRVNPQLI ALAAELDIPL VATNDVHYLQ RQDAEVQDVL ICIGTGKTVD DEDRLKMASE
QLFFKSGAEM AALFPHVPEA LENTVRIAEK CNLELTFGNH ILPAYSPLPE QQSSAAYLRQ
LCHAGLEQRY AGTPRWESPE QREAAQQRLE YELGVIETMG FCDYFLIVWD FIAYAHRMDI
AVGPGRGSSA GSLTAYSLRI TDVDPLRYNL LFERFLNPER ITMPDIDIDF SDERREEVIQ
YVVDKYGKEH VAQIITFGTM AARAAVRDVG RALNLPYNEV DKAAKLIPAQ LGISIAKALE
ATPELKSLYE TSPKIKGLLD MAMKVEGMPR HASTHAAGIV ISKGPLTDAV PLQAGNESTV
LTQYSMEHLE SVGLLKMDFL GLRTLSIIER CLQSIREMNG TVPDFRLIPD NDELTYRMLS
AGETAGVFQM ESSGVRRVLK DLRPTGFEDI VSVVALYRPG PMEFIPKYIG GKHGQFEVVY
PHPDLEPILA DTYGIIVYQE QIMQIASLMA GFSLGESDLL RRAVSKKKRE TLDKERSHFV
EGSLQQGYSE QDANAVYDMI VRFADYGFPR AHAAAYGVLA FQTAYLKAHY PVQFTAAMLT
AVMGNHRKVA EYVLECRRTG IGVLPPDVNE SGVLFTPVPG EGSAGHIRFG LAAVKNVGTL
AVENIIAERK ARPFDSLLDF CRRVDLRVCN KRVVESLLQA GAFDGLPGHR AQLLAMLDET
VEAALKWRKE RDELQIQLFD DLVETPNWEI RYPDIPRFTV GQQLELEREL LGLYLSGHPL
DDSAELLEEP GMQRLMDLGE ALDESQTVTA GMVVSVKEIT TKAGKAMAFV QWEDQIERCE
VVLFPEVWKR SRTLIEKGAL LALRAKVQHE DEGFKLLAEE VAPLAADTLR SLLQRRSAAA
ARPQGAGRAA PGAGAPQGAA PAARAAGAGA RGPARAAGGA NAPAAGTPKP PAPPAASGPG
SPAPAGAGPD RSAAGTAQRL FIKITPASEN PALLSRLQEL LQAEPGPVPV LLFYERGQRL
LALSDSYRIK PSETLLADIE AMLGAGTARI K
//
