ID R4WFX7_9BURK Unreviewed; 1175 AA.
AC R4WFX7;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:BAN22678.1};
GN ORFNames=BRPE64_ACDS09240 {ECO:0000313|EMBL:BAN22678.1};
OS Caballeronia insecticola.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=758793 {ECO:0000313|EMBL:BAN22678.1, ECO:0000313|Proteomes:UP000013966};
RN [1] {ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=23833137; DOI=10.1128/genomeA.00441-13;
RA Shibata T.F., Maeda T., Nikoh N., Yamaguchi K., Oshima K., Hattori M.,
RA Nishiyama T., Hasebe M., Fukatsu T., Kikuchi Y., Shigenobu S.;
RT "Complete Genome Sequence of Burkholderia sp. Strain RPE64, Bacterial
RT Symbiont of the Bean Bug Riptortus pedestris.";
RL Genome Announc. 1:340-344(2013).
RN [2] {ECO:0000313|EMBL:BAN22678.1, ECO:0000313|Proteomes:UP000013966}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RPE64 {ECO:0000313|EMBL:BAN22678.1};
RX PubMed=29863457; DOI=10.1099/ijsem.0.002848;
RA Takeshita K., Tamaki H., Ohbayashi T., Meng X.-Y., Sone T., Mitani Y.,
RA Peeters C., Kikuchi Y., Vandamme P.;
RT "Burkholderia insecticola sp. nov., a gut symbiotic bacterium of the bean
RT bug Riptortus pedestris.";
RL Int. J. Syst. Evol. Microbiol. 68:2370-2374(2018).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; AP013058; BAN22678.1; -; Genomic_DNA.
DR RefSeq; WP_016344836.1; NC_021287.1.
DR AlphaFoldDB; R4WFX7; -.
DR STRING; 758793.BRPE64_ACDS09240; -.
DR KEGG; buo:BRPE64_ACDS09240; -.
DR PATRIC; fig|758793.3.peg.927; -.
DR HOGENOM; CLU_001600_0_0_4; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000013966; Chromosome 1.
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 Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR048472; DNA_pol_IIIA_C.
DR InterPro; IPR004805; DnaE2/DnaE/PolC.
DR InterPro; IPR029460; DNAPol_HHH.
DR InterPro; IPR012340; NA-bd_OB-fold.
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; PF20914; DNA_pol_IIIA_C; 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 4: Predicted;
KW Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Ligase {ECO:0000256|ARBA:ARBA00023146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 12..79
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1101..1125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1175 AA; 130389 MW; 1FFC6302896A6939 CRC64;
MYNVAMSDPR FVHLRVHSEF SIADGIVRLD DVVKAAAKDG QGALALTDLG NAFGLVRFYK
EARGAGVKPI AGCDVWITNP DDRDKPSRLL LLVRDKQGYL NLCELLSRAW LTNQYRGRAE
VLVEWLDEGL AEGLLALSGA QTGDIGMALA AGNAASAQRH AERWAKCFPD AFYIELQRAG
QPGEQAYITE AVALAAKLRL PVVATHPLQF MTADDYTAHE ARVCISEGDM LANPRRQKRF
TTDQYFRTQD EMCALFADLP SALANTVEIA KRCNLTLELG KPKLPLFPTP DGMSLDDYLV
HLSKEGLEVR LQQLYPVEAE REAQRQTYYE RLEFECGTII KMGFPGYFLI VADFIMWAKN
NGVPVGPGRG SGAGSLVAYA LGITDLDPLR YNLLFERFLN PERVSMPDFD IDFCQEGRDR
VIQYVKQKYG ADAVSQIATF GTMAAKAAVR DIGRVLDLGY MFTDGIAKLI PFKPGKHVTI
ADAMREEPTL QERFDSEDEV HQLLELAQRV EGLTRNVGMH AGGVLIAPGK LTDFCPLYTQ
GEDGGVVSQY DKDDVEAVGL VKFDFLGLTT LTILDWAERY IRRLDPSKKD WNLTQVPLDD
PASFSILKKA NTVAVFQLES RGMQGMLKDA QPDRFEDIIA LVALYRPGPM DLIPSFCARK
HGREIVEYPD PRVEPVLKET YGIMVYQEQV MQMAQIIGGY SLGGADLLRR AMGKKKPEEM
AKHRELFREG AAKNGLTAQK ADETFDLMEK FAGYGFNKSH AAAYALLAYH TAWLKAHHPA
EFMAANMSLA MDDTDKVKIL FEDCIANGMK VLPPDINQSA YRFEPVAEAD GKRSKTIRYG
LGAVKGSGQN AIEEILRARE DGPFTDLFDF CERIDRRVVN RRTVEALIRA GALDALHANR
AQLLASVPLA MEAADQAAAN AMQAGLFDMG DAPLQAHELV EEAMWSDKKR LQEEKTALGF
YLSGHLFDAY KGEVRRFVRQ KIGELKEGRD KLVAGVISAL RTQMTQRGKM MIVNLDDGSG
QCEVTVFNEQ FEANKALFKE DELLVVQGQA RNDAFTGGIR FTVDTAMDLE RARSRYAQSL
KVEMNGNADA LRLRRVLEAH AAGAQTEPPP APARENGRSR QSAPIPNGLN VSIVYRSEHA
EGEVRLGDAW RVKPTDELIT ALRGEFAGSA IEIVY
//
