ID A0A365U3V8_9RHOB Unreviewed; 1189 AA.
AC A0A365U3V8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=DQW77_01605 {ECO:0000313|EMBL:RBI77158.1};
OS Roseovarius sp. TE539.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=2249812 {ECO:0000313|EMBL:RBI77158.1, ECO:0000313|Proteomes:UP000252940};
RN [1] {ECO:0000313|EMBL:RBI77158.1, ECO:0000313|Proteomes:UP000252940}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TE539 {ECO:0000313|EMBL:RBI77158.1,
RC ECO:0000313|Proteomes:UP000252940};
RA Liu B.-T., Du Z.-J.;
RT "Roseovarius sp. strain TE539.";
RL Submitted (JUL-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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RBI77158.1}.
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DR EMBL; QNGB01000002; RBI77158.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A365U3V8; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000252940; 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; 1.10.10.1600; 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; 2.
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:UP000252940};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 8..75
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 867..887
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1189 AA; 130728 MW; AC94D65E04734FA7 CRC64;
MTSTPRFIHL RVHSEYSLLE GAVRLKKLPG LCRDARMPAV AVTDTNNMFA ALEFSVAAQS
EGIQPIMGCQ IDLSYASAAP GDRQTPPAPV VLLAQNEQGY RNLMKLNSRF YLRGDGQAGH
VTMDELAQLG DGLICLTGGP DGPVGRLLRA GQRAAAETLL SQLSGAFGDR LYVELQRHPG
EEGPPEAERL SERGHVEMAY AMDLPLVATN DVYFPESGMF EAHDAMLCVA DGAYVDQNEP
RRRLTPQHYF KTQQEMVPLF ADLPEALENT VEIARRCAFG AYRRDPILPR FAEDEVEELR
RQAKEGLQAR LAVIPHAAPV EDYQTRLEFE LGVIESMGFP GYFLIVADFI KWAKGRDIPV
GPGRGSGAGS LVAYALTITD LDPLRYSLLF ERFLNPDRVS MPDFDIDFCM DRREEVIQYV
QEKYGRDRVG QIITFGALLS KAAVRDIGRV LQMPYGQVDR LSKMIPVEGV KPVSIEKALA
EEPRLREEAR NEEVVDRLLT YGQQVEGLLR NASTHAAGVV IADRPIDELV PVYQDPRSEM
PATQFNMKWV EQAGLVKFDF LGLKTLTVIQ NAIEQIHGAG RDLHVAQDGA LIYTPNPGAE
NDIGQIPLDD PKTYELYARA RTAAVFQVES EGMRDALKRM KPTCIEDIVA LVALYRPGPM
ENIPKYCEVK NALSEREYLH PSVDHILDET QGIIVYQEQV MQIAQEMAGY SLGGADLLRR
AMGKKIQAAM DAERPKFIAG AKANGVDDAK ALEVWNLLDK FANYGFNKSH AAAYAVVSYQ
TAWLKANHPV EFMAGVMNCD IHLTDKLSLY FEEVRKGLGL PWAPPCVNRS EATFAVRDGV
LHYALGGLKN VGVEAMKLIT RARREACQPS PAAAPGKGAP GPATGPDERP FATLHDFARR
VDLKRIGKRS LEMLARAGAF DALDPNRRRV FESLEALLNY STAIQEQKNS SQVSLFGEAG
EDLPEPRLAA VEDWLPAERL TEEFRAVGFY LSGHPLDDYM AALRRKDVKT LDEVTAMAAT
APVVVKMAGV VAGRQERKSA RGNRFAFAQL SDTTGGYEVT IFSDTLETAR EHLETGAQVV
ITVEASMESE QLKLLARSVQ PADGVVADAG MAGLRVFVEK QEVIASVASI LENAARTVKR
GGAGPVSFCL LDPDLPGEVE VATGREFPVS PQVKGAIKSL NGVVTVEEY
//
