ID A0A1I3NTC3_HALDA Unreviewed; 1118 AA.
AC A0A1I3NTC3;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN04487936_10169 {ECO:0000313|EMBL:SFJ12377.1};
OS Halobacillus dabanensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Halobacillus.
OX NCBI_TaxID=240302 {ECO:0000313|EMBL:SFJ12377.1, ECO:0000313|Proteomes:UP000183557};
RN [1] {ECO:0000313|EMBL:SFJ12377.1, ECO:0000313|Proteomes:UP000183557}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3704 {ECO:0000313|EMBL:SFJ12377.1,
RC ECO:0000313|Proteomes:UP000183557};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOSB01000001; SFJ12377.1; -; Genomic_DNA.
DR RefSeq; WP_075034580.1; NZ_FOSB01000001.1.
DR AlphaFoldDB; A0A1I3NTC3; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000183557; Unassembled WGS sequence.
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; SSF160975; AF1531-like; 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 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1118 AA; 127947 MW; 1BF82E58E8313A7C CRC64;
MTFTHLNVQS GYSLMNSTIK IPSLVETAKQ SGFKAIALTD EGSLSGTILF YQECKRSGIK
PIIGLKTTIV DRSLPFPVIL IAKSNVGYEN LIKISTFTQK NGENMTLEMM KEHKEGLIFI
LLTSSSPWAD SIANRMFDKI EDTRKRWLEA LGEEDFYLSI QDQDLHSERQ LHTPMKDWVQ
HNKMKVVAVG DVRYLHREDE VAYQCLRAID EGTRYHSERN KGHYYLKTMK EMESFFSEWW
PEVLTATETI VDACHVEMKL DRQLLPSYPT PNHEKPDGYL RELCEASLYR KYRQEERNKA
SERLEHELSV ITRMGFSDYF LIVWDFISYA RGKGIHAGPG RGSAAGSIVA FLLDITQVDP
LEYDLLFERF LNPERINMPD IDIDFPDHRR DEVIAYVVEK YGSDHVAQIC TFGTFAARSV
LRELFKVLGI EDSDASFILN QVPKVTTSSL VNIVKQSTEL KDYVRNSERL KMLFRVAAKL
EGLPRHVSTH AAGVVLSEEP LIQYTALMKG QGEVPLTQLA MGDLEKVGLL KIDFLGLRNL
SFIERMESKV KRYRDEEFSV NQIPLNDPLT FELLKRGKTN GVFQLESQGM KSVLMRLKPN
HFEDVVAVNA LYRPGPMEYI PTYIERKNGG KDVPFPHPDL KPILAPTFGV LVYQEQIMQV
AQLVAGYSLG EADILRRAVS KKQADVLENE RMKFITGCEK RGYEESVAHQ LFDWIVKFSN
YGFNRSHAVA YSLISYQLAY MKAHFPSYFI AELMNAHLGD REKLTVYIRE ARDMEVEVRA
PSINRSQSLT QDENGEIRLG LTAVKGVGYQ AAQAIIQERM NGAFRNLNDF CLRVDGKIVS
RKVIESLVLA GCFDALHQNR ASVLASIDQA LEQGELFKEF QDQPGFFGSE LEMEMVHVDP
FPPLKRLLME KEVLGTYLSQ HPLGQQRRSL REKGIIPLQQ ANGLDSKRKV KVASSIENLR
EIRTKRGDPM AFVTLSDETS EMDAVLFPET YRDVKVWLKE QMLVLLEGRL EERSNRKQLI
IDRVAAFNPE NLKASPEQRL FIKVTEKNEY QSIEKLKEVA EYFPGNTPVF IFRSEDRVTY
RLDESYCLTV SRESLNNLND FFGETSVALR SVNKETGD
//
