ID N1Z181_9CLOT Unreviewed; 1186 AA.
AC N1Z181;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 46.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:USF29872.1};
GN ORFNames=C820_001280 {ECO:0000313|EMBL:USF29872.1}, C820_02820
GN {ECO:0000313|EMBL:EMZ10847.1};
OS Clostridium sp. MD294.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=97138 {ECO:0000313|EMBL:EMZ10847.1};
RN [1] {ECO:0000313|EMBL:EMZ10847.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ASF356 {ECO:0000313|EMBL:EMZ10847.1};
RX PubMed=24723722;
RA Wannemuehler M.J., Overstreet A.M., Ward D.V., Phillips G.J.;
RT "Draft genome sequences of the altered schaedler flora, a defined bacterial
RT community from gnotobiotic mice.";
RL Genome Announc. 2:e00287-e00214(2014).
RN [2] {ECO:0000313|EMBL:USF29872.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ASF356 {ECO:0000313|EMBL:USF29872.1};
RA Proctor A., Parvinroo S., Richie T., Jia X., Lee S.T.M., Karp P.D.,
RA Paley S., Kostic A.D., Pierre J.F., Wannemuehler M.J., Phillips G.J.;
RT "Resources to Facilitate Use of the Altered Schaedler Flora (ASF) Mouse
RT Model to Study Microbiome Function.";
RL Submitted (MAY-2022) 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; AQFQ01000030; EMZ10847.1; -; Genomic_DNA.
DR EMBL; CP097810; USF29872.1; -; Genomic_DNA.
DR AlphaFoldDB; N1Z181; -.
DR STRING; 97138.C820_02820; -.
DR PATRIC; fig|97138.3.peg.2820; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_9; -.
DR Proteomes; UP000012445; 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 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; 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; PF14579; HHH_6; 1.
DR Pfam; PF02811; PHP; 1.
DR Pfam; PF01336; tRNA_anti-codon; 1.
DR SMART; SM00481; POLIIIAc; 1.
DR SUPFAM; SSF50249; Nucleic acid-binding proteins; 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:USF29872.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000012445};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:USF29872.1}.
FT DOMAIN 41..108
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1186 AA; 134797 MW; A19DA73C2E9D0660 CRC64;
MNYFELFYDT MLQKKNKKCV KVGEYMELEK QQYNIEKRPF THLHVHTEYS LLDGSAKIKE
LVERTKELGM NSIAITDHGA MYGAVEFYKA AKEKGIKPII GCEVYVANGS RLEKENKNGY
QYTHLVLLAE NNEGYQNLIK LVSYGFIDGF YYKPRVDKQL LKKYHKGIIA SSACLAGAVA
RDILTVSYEK AKQTALEYEQ IFGKGNYFLE LQDHGMREQK IVNEALRKIH NETGIPMICS
NDSHYIYKED NVSHDILLCI QTGKTVNDEN RMRYEGGQFY VKSVEEMYSL FTEDVEALEN
TQAIADRCNV EFVFHDLKLP RFDVPEGKTA KQYLRELCYT GFAQKYPNAS EQLKKRLDYE
LNTIETMGYV DYFLIVWDFI KFSKDNGIIV GPGRGSAAGS IVSYCLSITT IDPIAYDLIF
ERFLNPERIS MPDIDVDFCY ERRQEVIDYV IQKYGEDHVA QIITFGTMAA RAAIKDVGRA
LAMPYADVDR VSKMIPTELG ITIEKALKTN LELKRAYDTE ESTRYLIDMS MRLEGLPRHA
STHAAGVVIC RDAVMEYVPL NSNDGAITTQ YTMNTLEELG ILKMDFLGLR TLTVIQNAVK
EIERIHDIKI DIDHIDQKEP EVYQLIAQGK TEGIFQLESG GMKQFLRELQ PSNLEDLIAG
ISLYRPGPMD FIPKYIKGKR EKDNIQYTHI SLEPILKTTY GCIVYQEQVM QIVRDLAGYS
LGRSDLVRRA MSKKKADVMA QERKNFIYGI GEEVAGCIKN GIDEDTAAKI FDEMTDFAKY
AFNKSHAVCY AVVGYQTAWL KTHYPVEFMA ALMTSVMDNS DKLSGYIDEC KKMNIALLPP
DINEGFGHFS VSDGKIRFSL SAIKNVGKNT IKALVSEREK NGAYTSLTDF CNRMETGELN
RRSLESLVKA GAFDSLGGFR SQYMTIYKSI LDGIGQSRKN NLEGQMSLFD MEEQKQTYVI
EELPIKEEYP IKEKLALEKE VLGIYVSGHP LAEYEAVLKQ KINCVSKNFL PDEEQNTKIF
DGQRVIIGGM IIHKSVKHTR TGTKMAFLTL EDLSGTIEVV VFSNVYEKVS HKIQEDAVVI
VKGRASISAE GETKLIASQI DFLNTEGEQY SVLGLVLEKE SKINLQDIIK VLLKYHGSMP
VYIDNRKTGQ MLKADSRYWF EQSALAIQEL ELLLGNGNVI IKNKNI
//
