ID A0A0Q5MFF7_9BURK Unreviewed; 1180 AA.
AC A0A0Q5MFF7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
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:KQR55705.1};
GN ORFNames=ASF94_04760 {ECO:0000313|EMBL:KQR55705.1};
OS Acidovorax sp. Leaf160.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Acidovorax.
OX NCBI_TaxID=1736280 {ECO:0000313|EMBL:KQR55705.1, ECO:0000313|Proteomes:UP000051403};
RN [1] {ECO:0000313|EMBL:KQR55705.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55705.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQR55705.1, ECO:0000313|Proteomes:UP000051403}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf160 {ECO:0000313|EMBL:KQR55705.1,
RC ECO:0000313|Proteomes:UP000051403};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KQR55705.1}.
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DR EMBL; LMOV01000012; KQR55705.1; -; Genomic_DNA.
DR RefSeq; WP_056664688.1; NZ_LMOV01000012.1.
DR AlphaFoldDB; A0A0Q5MFF7; -.
DR STRING; 1736280.ASF94_04760; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000051403; 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; 1.10.150.870; -; 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; 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; 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 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:KQR55705.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000051403};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KQR55705.1}.
FT DOMAIN 3..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1180 AA; 130617 MW; 56290B247E76BB29 CRC64;
MFVHLRLHTE FSVVDGTNRI DEVAKAAAKD GQPALAITDL NNLFGAIKFY KETRGKGVKP
LLGAEINVPS TTGGPCRMVV LVQNMQGYLN LSELLARAWT RNIVKNVPVC TLEWLRELNA
GLILLAGAQA GPVGQALMRG DGAGAADMAL ELASMFPHRF YLEIQRAGRA DDEAHVVAAV
QLAARLNLPV VATHPVQFAT AEDYEAHEAR ICIAEGEILA NQRRVRKFTR EQYFKSSAEM
EALFADVPTA IANTLEIAKR CNLTLVLGKP RLPDFPTPNG MPIDEYFRYA SYEGLEERLA
QIFPKEAERA KQRPRYVERL EFELGTILKM GFPGYFLIVG DFIQWAKQNG CPVGPGRGSG
AGSLVAYALK ITDLDPLQYN LLFERFLNPE RVSMPDFDID FCQSNRDRVI DYVKDKYGKN
AVSQIATFGT LAAKAAIRDV GRVMDMSYTF CDGISKLVPG KPGMSYTLAY PPEVKKEGDK
NNYALELEPM LYERVRKEED VKTVIEMAQK LEGMTRNIGM HAGGVLIAPG KLTDFCPLYQ
QPGSESAVSQ YDKDDVEAIG LVKFDFLGLA TLTILEIARE FIMKRHKGQE NFAFENIPLD
DSPTYRLFSD GKTEAVFQFE SRGMQGMLKE ARPSRLEDLI ALNALYRPGP MDLIPTFVNR
KHGKEPVEYP HPLVEPVLAE TYGIMVYQEQ VMQTAQVLGG YSLGGADMLR RAMGKKKAEE
MAEHREIFRK GAAEKGIDQN KADEVFDLME KFAGYGFNKS HAAAYSLLAY HTGWLKVHYT
AEFFCANMTV EMDDTDKLKV LYEDAVKNFG MTFEPPDVNR GMYRFEPVTD KVIRYGLGAI
KGTGQQAIEA IIAAREGRGE GPQGSTVGPF KSLFDFCVRV DRARINKRTV DALIKAGAFD
GLQMNRAALS ASLDRAFDFA SATHANANQG GLFDMMGDDA HGSSTQEPDL VEVTPWGIKE
RLTQEKTAIG YYLSGHLFDE VALEVRRFVR TRLDEMGDSR EPQILAGIVS DLRVINGQRG
RLALFKLDDK TATIEASADE GVLNAHRDVL KDDEFVVISG RVQLDHFSGG LRVKVQQAWD
LAGARAKYGR YLQVAVGDAV PDVNRLVREF PAKREETEHG DILVHGLRVR MGLRCKAEQG
AATAEIQLGE ASRFFPSDAA LAAWSAQAGS GTVSVVYDAG
//
