ID Q24XZ1_DESHY Unreviewed; 1190 AA.
AC Q24XZ1;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 27-MAR-2024, entry version 110.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN OrderedLocusNames=DSY1312 {ECO:0000313|EMBL:BAE83101.1};
OS Desulfitobacterium hafniense (strain Y51).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=138119 {ECO:0000313|EMBL:BAE83101.1, ECO:0000313|Proteomes:UP000001946};
RN [1] {ECO:0000313|EMBL:BAE83101.1, ECO:0000313|Proteomes:UP000001946}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y51 {ECO:0000313|EMBL:BAE83101.1,
RC ECO:0000313|Proteomes:UP000001946};
RX PubMed=16513756; DOI=10.1128/JB.188.6.2262-2274.2006;
RA Nonaka H., Keresztes G., Shinoda Y., Ikenaga Y., Abe M., Naito K.,
RA Inatomi K., Furukawa K., Inui M., Yukawa H.;
RT "Complete genome sequence of the dehalorespiring bacterium
RT Desulfitobacterium hafniense Y51 and comparison with Dehalococcoides
RT ethenogenes 195.";
RL J. Bacteriol. 188:2262-2274(2006).
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; AP008230; BAE83101.1; -; Genomic_DNA.
DR RefSeq; WP_005814652.1; NC_007907.1.
DR AlphaFoldDB; Q24XZ1; -.
DR STRING; 138119.DSY1312; -.
DR KEGG; dsy:DSY1312; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_9; -.
DR Proteomes; UP000001946; 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; 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 Reference proteome {ECO:0000313|Proteomes:UP000001946};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1064..1108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1064..1082
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1190 AA; 133474 MW; 519453AF888FF7AE CRC64;
MGFVHLHVHT EYSLLDGAAR IEKLVKKAVE LGMPSVAITD HGVMYGIIDF YKACKKAGIK
PIIGCEVYVA PHRRTEKVPG RDDNNRHLVL LAENEEGYKN LIKLVSMAHI EGFYYKPRVD
KDILRKHSRG LIALSACLAG EVSEYLLNNQ LETAVESALE YEEIFGKGNF FLEVQDHGLE
EQQRVNTGMF EVQRRTGIPM VATNDVHYVN KEDAFIQDVL ICIQTGKNLT DASRMSFSSE
EFFLKSEAEM NLLFGEHPEI LENTARIAER CQVDFKFGDN YLPVFEVPEG YTLDTYLRKK
CYEAFPLFYP NQRTEEKERL DYELGVIAQT GFSGYFLIVA DFCQYARQNG IAVGPGRGSA
AASMVAYLMG ITTVEPMQHD LLFERFLNPE RISMPDIDID FDPDGRERVI NYVMEKYGAD
KVCQIITFGT MGAKAAIRDV GRVLGIPLAR VDKVAKAIPS DLGMTLEKAL AVSPDLVKLL
EEDGEIKKLY EIARSLEGMP RHASTHAAGV VIAKDALDTY IPLQRTSDGG FTMTQFPMKT
VEEVGLLKMD FLGLRNLTII QETLKQIEGN RGEVLDLQSL PLDDKATFDM LSLGNSTGVF
QLESGGMRNV LKELKPSCFE DIIAVVALFR PGPMEQIPEF IRRKHGGNVS YLHPLLEPIL
RSTYGVIVYQ EQVMQIARDL AGYSLGRADL LRRAMGKKKK EIMEEERQSF IYGLQSPSGE
EIIPGALKLG LTEKEAAEIF DLMAKFAEYG FNKGHATAYA VISYQTAYLK ANYPLEFNAA
LISTVMSSAD KVSFYIHEAR QSGIEILPPD VQYSQVGFSI EGRGIRFGLG AIRNVGVNVV
EKIIEARQEG LFESLYDFCI RVDAKVLNKR VLESLLKAGA FSLLCKRAQG LLALDSILEV
AQQRQRDKES GQISLFDFGD NLDEGIELPD VEEYSPRELL TMEKEYLGLY LSGHPLESVL
PKLKNAVSED ILTCLEGDEE KKVILGGIVT GYRTTVTKRG EMMASFVLED LTGTIDVLVF
PRIFAQSARL TEDQVVVVEG RYNIRDDERK IFAERITDLE NGAERNKPIG YKDYERTQSR
EKAQTRTQTP TQPPTQSPPK LSAVPSAKPG AVPARKLYLR FPCEGTPLLE ETLPILRHYS
GTHPVLFYFE QDKKLIQGNR ELWVNDLEEL VQALSNILGE SNVVWKVNAM
//
