ID A0A1G5JE52_9RHOB Unreviewed; 1156 AA.
AC A0A1G5JE52;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN05660710_03167 {ECO:0000313|EMBL:SCY86663.1};
OS Paracoccus tibetensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Paracoccus.
OX NCBI_TaxID=336292 {ECO:0000313|EMBL:SCY86663.1, ECO:0000313|Proteomes:UP000199502};
RN [1] {ECO:0000313|EMBL:SCY86663.1, ECO:0000313|Proteomes:UP000199502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8925 {ECO:0000313|EMBL:SCY86663.1,
RC ECO:0000313|Proteomes:UP000199502};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FMVT01000012; SCY86663.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G5JE52; -.
DR STRING; 336292.SAMN05660710_03167; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199502; 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 Reference proteome {ECO:0000313|Proteomes:UP000199502};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..76
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1156 AA; 126328 MW; 41875B1DA594CC21 CRC64;
MAADSPRFIH LRTHSEHSLL EGAIPVGKLP GLAADAGMPA VALTDTNNMF AALEFSVKAK
DKGVQPIIGC TLTLAAEATG PVVLLVQDKA GWMNLMKLSS CLYLREGGAL PHVTLDELCA
HAEGLICLTG GATGPVGQLV AAAQTEKAAA LVDRLAAAFP TRLYIELQRH LGEDGRLMLA
EAASEGGLID LAYAKDLPLV ATNDVYFPKA QMYEAHDALI CIAEKAYVDQ PQPRRRLTPQ
HYFKTAEEMA VLFADLPEAT QNTVEIARRC AFAVAKHAPI LPRFADDEVA ELRRQAREGL
EARLAVIPHA VSVEEYHQRL DFELGIIEQM GFPGYFLIVA DFIHWAKSQG IPVGPGRGSG
AGSLVAYALT ITDLDPLRYS LLFERFLNPE RVSMPDFDID FCMDRREEVI RYVQEKYGKD
RVGQIITFGA LLSKAAVRDV GRVLQLPFGQ VDRLSKMIPV EGVKPVSIAK ARADEPRLRE
AAREEVVKRL LDYAEQLEGL YRNASTHAAG VVIGDRPLDQ LVPLYRDPGS DMPATQFNMK
WVEQAGLVKF DFLGLKTLTV IQNAVDLING QGRPLHVAAD GRQLYQPTPG TENEINLIPL
DDKASYDLFA SARTVAVFQV ESSGMMDALR RMRPTCIEDI VALVALYRPG PMENIPTYCE
VKNGLRELES IHPSIDHILA ETQGIIVYQE QVMQIAQVMA GYSLGGADLL RRAMGKKIAA
EMAKERPKFV KGSVANGVPE KKAGEVFDLL EKFANYGFNK SHAAAYAVVS YQTAWLKANH
PVEFMAAVMN CDIHLTDKLA VYKRECDRMG IEIVPPCVNR SAPTFTVGQG RIHYALGALK
GVGIEAMKLI HDARGDRPFK DIHDFARRVD MKRVGKRPLE MLARAGAFDV LDDNRARVMK
SLDALCAWSA AVQEQAASSQ TSLFGGGEDL PPPRAPLAQV WLPTEKLGEE HKAIGFYLSG
HPLDDYQTAL RRKKVQTLAD ITRDAEGGPM VAQIAGTVAA RMERKSAKGT AYAFVSLSDP
TGLYEVTCFS DLLTACRDKL EPGQNVVLQV KVEPSGEQVK MLANSVALLE DFVADAGAGC
LAVEIQGADT IPRLAEVLTR VTAEISAPSR ARGPIRLRLR HEDEIIEIEV ANDAPLTTPA
RQALRAVPGV LDVIEE
//
