ID A0A0Q7DJ91_9CAUL Unreviewed; 1149 AA.
AC A0A0Q7DJ91;
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 ORFNames=ASC73_05420 {ECO:0000313|EMBL:KQW71543.1};
OS Phenylobacterium sp. Root1277.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=1736442 {ECO:0000313|EMBL:KQW71543.1, ECO:0000313|Proteomes:UP000051150};
RN [1] {ECO:0000313|EMBL:KQW71543.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71543.1,
RC ECO:0000313|Proteomes:UP000051150};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW71543.1, ECO:0000313|Proteomes:UP000051150}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root1277 {ECO:0000313|EMBL:KQW71543.1,
RC ECO:0000313|Proteomes:UP000051150};
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 -!- 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:KQW71543.1}.
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DR EMBL; LMDZ01000004; KQW71543.1; -; Genomic_DNA.
DR RefSeq; WP_056018686.1; NZ_LMDZ01000004.1.
DR AlphaFoldDB; A0A0Q7DJ91; -.
DR Proteomes; UP000051150; 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 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:UP000051150};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 10..77
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1149 AA; 125741 MW; D2DEB4B26D27D374 CRC64;
MSEAVNEGFV HLRVRSAYSL LEGAIKADKV SSLAKAAEMP AVALTDRANL YGALEFSVTS
KDAGVQPIVG VALPVTGIGG AQPERWAKIP TIVLLAQSEQ GYLNLSELSS LCYLESDGSE
DVSAPWSKVV EHSEGLILLS GGVDGPVDPL LAAGKIPEGK AALAEMARVF GDRFYIELQR
HGLPAQAAAE GELVAFAYDN DIPLVATNDV YFAKQTMYEA HEALLCIADG AFISQDERRR
VTPEHWFKPA ADMRALFSDL PEACDNTLDI ARRCAFMVKK RDPILPRFDT AGGRSEAEEL
AFQAREGLKA RIASGQASAL PVEDYEARLE REIGVIAQMG FPGYFLIVSD FIKWAKTHDI
PVGPGRGSGA GSLVAYALTI TDLDPLRYGL LFERFLNPER VSMPDFDIDF CQERREEVIS
YVQKHYGRDR VAQIITFGTL QARAVLRDVG RVLQLPLGLV DRLAKMVPAN PANPVTLAKA
IEIEPRLRQA KDDDEAVKQL LETALQLEGL YRNASTHAAG VVISDRPLTQ LTPLYRDPRS
ELPATQFNMK WVESAGLVKF DFLGLKTLTV IDRALKFLRK RGVDVDFATL GVDDAPAYEV
MSNGGTVGVF QLEGQGMRDT LRQLRPGSLE DVTAVVSLYR PGPMDNIPAF IDCKFGRKPI
DYMHPSLGPV LKETYGIIVY QEQVMQIAQI LAGYSLGEAD LLRRAMGKKK KEEMDLQRAR
FVSGAEAKGV PAEQAGSIFD LVDKFAGYGF NKSHAAAYAY VSYQTAWLKA NTPVEFFAAS
MSLDISNTDK LAVFYQDAKR FGVKVRSPDV NRSSADFEVE DGEVLYALGG IRNVGQQAME
HVVAVRKAGG PFKDIFDFAS RVDPKQVNKR TFETLARAGA FESIHADRAQ LLAAAELLVG
LGQSVASQES SEQGALFSDG TNHLVDQVRK KMPKAEPWTP VQRLDEELAA VGFYLSGHPL
DDMVTALRRR RTDLLADVIP KAEAGAEAFR MAGVVRRKQE RASQSSGEKF AFVTFSDPTG
EYEVLFPPES LRKCRDLLEP GKAVALKVRA KARDGEVRFF GDDAEPVDKA VENAVAGLRV
HVAPRSAEIE ALKKRLENVA NPRGGEIILV ANIERGREVE LKLPGRFSLD ASVRGALKTA
PGVVFVEDI
//
