ID A0A238L8Q7_9RHOB Unreviewed; 1171 AA.
AC A0A238L8Q7;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE1 {ECO:0000313|EMBL:SMX50762.1};
GN ORFNames=MAA8898_04973 {ECO:0000313|EMBL:SMX50762.1};
OS Maliponia aquimaris.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Maliponia.
OX NCBI_TaxID=1673631 {ECO:0000313|EMBL:SMX50762.1, ECO:0000313|Proteomes:UP000207598};
RN [1] {ECO:0000313|EMBL:SMX50762.1, ECO:0000313|Proteomes:UP000207598}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8898 {ECO:0000313|EMBL:SMX50762.1,
RC ECO:0000313|Proteomes:UP000207598};
RA Song R., Chenine A.L., Ruprecht R.M.;
RL Submitted (MAY-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; FXYF01000027; SMX50762.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A238L8Q7; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000207598; Unassembled WGS sequence.
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:0006260; P:DNA replication; IEA:UniProtKB-KW.
DR CDD; cd04485; DnaE_OBF; 1.
DR CDD; cd07433; PHP_PolIIIA_DnaE1; 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; IPR004013; PHP_dom.
DR InterPro; IPR003141; Pol/His_phosphatase_N.
DR InterPro; IPR016195; Pol/histidinol_Pase-like.
DR InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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 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 ECO:0000313|EMBL:SMX50762.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000207598};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SMX50762.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1171 AA; 128874 MW; 12AAEA712D9761FF CRC64;
MADPRFIHLR VHTEYSLLEG AVRLKKLPGL CAAMGMPAVA VTDTNNLFAA LEFSATASGA
GIQPIVGCQV SLRYIEPQPG ERPKPPAPVV LLAQTERGYE HLMKLNSCIY MRRDTELPHV
TLAELEAHSE DVICLTGGPD GPVGRLLRNG SRAAAEALMT RLTQVFGDRL YVELQRHPGE
DGALPEAERL SERGFVEMAY AMDLPLVATN DVYFPKPEMY EAHDALICIA EGAYVDQQQP
RRRLTPQHYL KTPQEMAVLF ADLPEALENT VEIARRCAFM AYKRAPILPK FADDEVAELR
RMANDGLQER LKVIPHAVTP AEYQERLDFE LGIIEGMGFP GYFLIVADFI QWAKDNNIPV
GPGRGSGAGS LVAYALTITD LDPLRYSLLF ERFLNPERVS MPDFDIDFCM DRREEVIRYV
QDKYGHDKVA QIITFGALLS KAAVRDMGRV LQMPYGQVDR LSKMIPVEGV KPVSIEQALR
DEPRLAEEAK NEEVVDRLLK YGMQVEGLLR SAGTHAAGVV IADRPTDELV PLYRDPRSDM
PATQFNMKWV EAAGLVKFDF LGLKTLTVIQ NAVDLILKSG RPLHVAADGT ELYQPAPGAE
NQMNLIPLDD AATYKLYAAA KTVAVFQVES SGMMDALKRM KPTCIEDIVA LVALYRPGPM
ENIPTYCEVK NGLREITSVH PSIDHILAET QGIIVYQEQV MQIAQVMAGY SLGGADLLRR
AMGKKIKEAM DAERPKFEKG AAENGVDKKK ATEVFDLLEK FANYGFNKSH AAAYAVVSYQ
TAWLKANHPV EFMAGVMNCD IHLTDKLAIY FEEVRKGLSL PYVPPCVNRS QATFDVAGGK
LVYALGALKN VGVEAMRLVV AGRGDKPFVS LFDFARRVDL KKIGKRPLEM MARAGAFDVL
DGNRRRVFDA LDALVAYSSA IHEQKASAQV SLFGEAGEDL PEPRLSPVSD WLPAERLAEE
FKAIGFYLSG HPLDDYMAQL RRVERSGSFM TLDELTHKVQ QNGAMVAKLA GVVAGRQERK
SARGNRFAFC QMSDPTGAYE VTLFSEALEK SREYLESGSK VVVTVEATME SDQLKLLGRS
VGPIDAAVAG AGVNGLRIYV EDAGALPQIA SVLSRAAEQM PKAARGPIHF CLNDPALPGE
VEMDSGRAYP VTPEIKGAVK SLDGVLAVED F
//
