ID A0A2R8AVG6_9RHOB Unreviewed; 1170 AA.
AC A0A2R8AVG6;
DT 20-JUN-2018, integrated into UniProtKB/TrEMBL.
DT 20-JUN-2018, 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:SPF80021.1};
GN ORFNames=PRI8871_01823 {ECO:0000313|EMBL:SPF80021.1};
OS Pseudoprimorskyibacter insulae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudoprimorskyibacter.
OX NCBI_TaxID=1695997 {ECO:0000313|EMBL:SPF80021.1, ECO:0000313|Proteomes:UP000244904};
RN [1] {ECO:0000313|Proteomes:UP000244904}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8871 {ECO:0000313|Proteomes:UP000244904};
RA Rodrigo-Torres L., Arahal R. D., Lucena T.;
RL Submitted (MAR-2018) 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; OMOJ01000002; SPF80021.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2R8AVG6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000244904; 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; 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:SPF80021.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000244904};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:SPF80021.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1170 AA; 130050 MW; 162CB4582B6F4BE1 CRC64;
MSTQRFVHLR VHTEYSLLEG AVRLKKLAGM CEAAEMPAVA VTDTNNLFSA LEFSVSASGA
GIQPIIGCQV DLRYADPAPG ERPRDPAPVV LLAQSETGYE HLMKLNSCLY MRTDGSVPHV
TLAELEAHSE GLICLTGGPD GPVGQLLQQH QRSHAETLMR ELHRVFGDRL YVELQRHPGE
DGQPEAERLT ERGFVEMAYA MNIPLVATND VYFPKTDMYE AHDALICIAE GAYVDQQEPR
RRLTAQHYFK SQQEMVTLFA DLPEAIDNTI EIAQRCAFMA YRRDPILPKF ADDEVTELRR
QANEGLQARL AVIPHAVTPE EYQERLDFEL GIIEGMGFPG YFLIVADFIQ WAKDHNIPVG
PGRGSGAGSL VAYALTITDL DPLRYSLLFE RFLNPERVSM PDFDIDFCMD RREEVIRYVQ
EKYGHDRVGQ IITFGALLSK AAVRDMGRVL QMPYGQVDRL SKMIPVEGVK PVSIEQALRD
EPRLAEEARN EEVVDRLLKY GMQVEGLLRS AGTHAAGVVI ADRPTDELVP LYRDPRSEMP
ATQFNMKWVE QAGLVKFDFL GLKTLTVVQN AVDLIHKSGR DLHFGPDGTQ LYEPAEGAAN
QINAIPLDDE KSYKLYAEAK TVAVFQVESS GMMTALRQMK PTCIEDVVAL VALYRPGPME
NIPTYCDVKH GRKPLESIHP TIDHILEETQ GIIVYQEQVM QIAQVMAGYT LGGADLLRRA
MGKKIKEAMD AERPKFVEGS KKNGVDQKKA MEVFDLLEKF ANYGFNKSHA AAYAVVSYYT
AWLKANHPVE FMAGVMNCDI HLTDKLAIYA EEVRRGMDIE IVPPCVNRSL ATFDVVDQKL
VYALGALKNV GGDAMNLIVE GRGDKPFATL FDLARRVDLK RVGKRPLEML ARAGAFDQLD
SNRRRVFESL DALVNYSAAI HEQKNSNQVS LFGEAGDDLP EPRLSPIGDW MASERLMEEQ
KAIGFFLSGH PLDDYAAALK RKNIGTIEDA RQKAEQEGAA VVRVGVMVSG LREMKSSKGT
RYFRMNISDS TGQVAGIAMF AREEKDLNAA RMVFENTDKV VAVLEARFND GQFDPMVRSV
SPVDAVVADA AAAGLRIHVD QPDAIPNIAS VLERAAEQMP KSRKGPVHLC LNHSSLPGEV
EMDLQKEFPM TPEIRGAIKS LPGILAVEEL
//
