ID W4EPT4_9BACL Unreviewed; 1030 AA.
AC W4EPT4;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:ETT82603.1};
GN ORFNames=C176_16482 {ECO:0000313|EMBL:ETT82603.1};
OS Viridibacillus arenosi FSL R5-213.
OC Bacteria; Bacillota; Bacilli; Bacillales; Planococcaceae; Viridibacillus.
OX NCBI_TaxID=1227360 {ECO:0000313|EMBL:ETT82603.1, ECO:0000313|Proteomes:UP000019062};
RN [1] {ECO:0000313|EMBL:ETT82603.1, ECO:0000313|Proteomes:UP000019062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FSL R5-213 {ECO:0000313|EMBL:ETT82603.1,
RC ECO:0000313|Proteomes:UP000019062};
RX PubMed=24422886; DOI=10.1186/1471-2164-15-26;
RA Moreno Switt A.I., Andrus A.D., Ranieri M.L., Orsi R.H., Ivy R.,
RA den Bakker H.C., Martin N.H., Wiedmann M., Boor K.J.;
RT "Genomic comparison of sporeforming bacilli isolated from milk.";
RL BMC Genomics 15:26-26(2014).
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 -!- 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:ETT82603.1}.
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DR EMBL; ASQA01000034; ETT82603.1; -; Genomic_DNA.
DR AlphaFoldDB; W4EPT4; -.
DR PATRIC; fig|1227360.4.peg.3357; -.
DR eggNOG; COG0587; Bacteria.
DR Proteomes; UP000019062; 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 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; 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 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.
PE 4: Predicted;
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:ETT82603.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019062};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ETT82603.1}.
FT DOMAIN 13..123
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 276..531
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 534..696
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 770..860
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 950..1023
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
SQ SEQUENCE 1030 AA; 116812 MW; 744AD339AA323555 CRC64;
MQNVYPQIVT AADMLKSTIR IEELISFLQQ EHAKAAAIVN SKLYGLLPFW RALKKAEIHP
VIGLTVRVQF REHQVRSVVL YAATQQGYQH LLKVTSAMSI REGEVLPLRW LEGYQEGCIL
MVPMTSPDWI AEGSFEDVQA LQGIFGKGRL YVGIDRPGGL KSDIEQDIIS YCHEQELPIC
ATHLCTFMRE EHAFSFEVAK AIEQGMKMNI SDQLTARERQ QFVPFNRQWQ DWFADYPEWL
LSAEEMLLSC QVDLAFDKFL MPKFPTPNNE TAFSLLEANS LRGLQERVPN ASADYIERLH
YELGIIQEMG YADYFLIVSD YIQYAKSKQI LTGPGRGSSA SSLVAYTLRI TDVDPLQYGL
LFERFLNPER ITMPDIDVDF ADHRRQEVIQ YVSDKYGKTY TSQIITFGTL SAKAVARDVA
RVFGFTSEEL SKISSLIPNK VGITLREALA ESISLRDWIA ASDIRQKWIE VALNLEGLPR
NASTHAAGVV LSPEPLVNIV PIEPGNDGLY ITQWPMQEVE SIGLLKMDFL GLRNLTILER
IRSMIYYDTR KFLDFEKIPL HDPSTFKLLQ QGDTTGVFQL ESDGMRQALR DITPTAFQDI
VAIIALYRPG PMDFIPVYSK RKHGGEAVIM PHPVLEPILR ETYGVIVYQE QIMQIASVMA
GFTMGEADIL RRAVSKKKKE ILDAEQQHFV KNSVAKGFTE QVAVEVYDLI VRFANYGFPK
SHAVAYSVIT YHMAYLKANF PTYFYAALLT STIGNQDRLM RLLQEVKQKG ITVLPPSVHH
SGRTFRVENG AIRFALSAIK GVPQSFLTKL LSLRKNGHSN WADLFDFALD MTGVHFTRKA
LEPLIKAGAL DDFGRNRGQL LASIEAVVKH ANLYRPNDEE SLLSDGDFLF GKPKYADASL
MPEKLLLQYE KEVLGFYMSE HPILKLKKEL QIDSMSAANI LEIQGRKYVK MLGIVSGIKQ
IRTKKGEQMA FIDLEDESGM LSITIFPREY IHIQEWLQEE QIVLAEGFVE PRNGKAQMIV
KKLITELTEK
//