ID A0A1I5Z2Y0_9RHOB Unreviewed; 1165 AA.
AC A0A1I5Z2Y0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN05421853_107206 {ECO:0000313|EMBL:SFQ50834.1};
OS Roseivivax halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseivivax.
OX NCBI_TaxID=93684 {ECO:0000313|EMBL:SFQ50834.1, ECO:0000313|Proteomes:UP000243106};
RN [1] {ECO:0000313|Proteomes:UP000243106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10271 {ECO:0000313|Proteomes:UP000243106};
RA Varghese N., Submissions S.;
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; FOXV01000007; SFQ50834.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5Z2Y0; -.
DR STRING; 93684.SAMN05421853_107206; -.
DR Proteomes; UP000243106; 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 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; 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 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 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:UP000243106};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1165 AA; 128936 MW; A3FC9357B97CA4BA CRC64;
MADPRFIHLR VHTEYSLLEG AVRLKKLPGL CEKMGMPAVA VTDTNNLFAA LEFSVTAAGA
GVQPIVGCQV DLRFSDPQPG ERPRDPAPVV LLAQSEAGYE NLMKLNSCLY LRGDGELAHV
TLDELERHSE GVICLSGGPD GPVGMLLRQG SRGAAEALMV RLHAMFGDRL YVELQRHPGE
DGQPEAERLT ERGFVEMAYE MGLPLVATND VYFPKSDMYE AHDALICIAD GAYVDQQEPR
RRLTPQHYFK SPEEMVTLFA DLPEAVENTV EIARRCAFMT YKRDPILPRF ADDEVEELRR
QANEGLQARL AVIPHAASVE DYQARLDFEL GIIEGMGFPG YFLIVADFIK WGKEHDIPVG
PGRGSGAGSL VAYALTITDL DPLRYKLLFE RFLNPERVSM PDFDIDFCMD RREEVIHYVQ
EKYGRDKVAQ IITFGALLSK AAVRDVGRVL QMPYGQVDRL SKMIPVEGVK PVSIEKALAD
EPRLREEARN EEVVDRLLTY GQQVEGLLRN ASTHAAGVVI GDRPLDELVP LYQDPRSDMP
ATQFNMKWVE QAGLVKFDFL GLKTLTVIQN AVDLIHKSGR DLHVGADGAT LYEPFDGAEN
DIGQIPLDDE KTYDLYSRAK TVAVFQVESS GMMDALKRMK PTCIEDIVAL VALYRPGPME
NIPVYCEVKN GLRERAGIHP SIDHILDETQ GIIVYQEQVM QIAQEMAGYS LGGADLLRRA
MGKKIQEAMD AERPKFIEGA KKNGVDDDKA LEVWNLLDKF ANYGFNKSHA AAYAVVSYQT
AWLKTNHPVE FMAGVMNCDI HLTDKLAIYF EEVKKGLELP WVPPCVNRSQ AMFDVQNGEL
VYALGALKNV GVEAMRLVVE GRGAQPFATL YDLARRVDLK RVGKRPLEMM ARAGAFDQLD
PNRRRVFDSL DALVAYSAAV QEQKTSNQVS LFGDAGEDLP EPRLAPVNDW LPAERLAEEF
KAIGFYLSGH PLDDYLAALK RKGVMTLDEV MRKAEGGPFL AKLAGTVAGR QERKSAKGNR
FAFCQLSDPT GAYEVTLFSE TLEKSREHLE TGAKVVVTVE ATLESDQLKL LGRSVAPVDV
AVADAGASGL RIYLEEEAAI PQIASVLSRA AQQMPKAGRG PVHLCLSHRD LPGEVEIGLE
EEFPVTPEIK GAIKSLAGIM DVVEF
//
