ID A0A1I5W3T9_9FIRM Unreviewed; 1159 AA.
AC A0A1I5W3T9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=SAMN02910358_00848 {ECO:0000313|EMBL:SFQ14398.1};
OS Lachnospiraceae bacterium XBB1006.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=1520827 {ECO:0000313|EMBL:SFQ14398.1, ECO:0000313|Proteomes:UP000199554};
RN [1] {ECO:0000313|EMBL:SFQ14398.1, ECO:0000313|Proteomes:UP000199554}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=XBB1006 {ECO:0000313|EMBL:SFQ14398.1,
RC ECO:0000313|Proteomes:UP000199554};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOXT01000006; SFQ14398.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5W3T9; -.
DR STRING; 1520827.SAMN02910358_00848; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199554; 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; cd12113; PHP_PolIIIA_DnaE3; 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 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:UP000199554};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1159 AA; 131588 MW; BA8BB41EED2D8666 CRC64;
MAFAHLHVHT EFSLLDGSNK IKECVARVKE LGMDSVAITD HGVMYGVIDF YRAAREAGIR
PVIGCEVYVA PGSRFDREAG AGDDRYYHLV LLAENNEGYA NLMKIVSRGF TEGFYYKPRV
DYELLEEFHE GIICLSACLA GEVQKELARD HYEEAREAAL RYQKIFGKNN FFLELQDHGI
PEQRKVNQRL MRLSQETGIE LVATNDVHYT LAEDAEAHDI LLCIQTGKKL SDENRMRYEG
GQYYIKSEEE MKTLFPYALE ALENTEKIAK RCNVEIEFGV TKLPRYPVPE GYTSWEYLNE
LCLQGLQKRY PDKWEDVKAQ LDFELHTIKT MGYVDYFLIV WDFIHYARSK DIMVGPGRGS
AAGSIVAYTL GITNIDPLRY NLIFERFLNP ERVTMPDIDV DFCFERRQEV IDYVGEFYGE
GKVVQIVTFG TMAAKNAIRD VGRVMDLPYS FVDTISKAIP NELNMTITKA LAMNPDLKKM
YDGDEQVKKL IDMSLRLEGL PRHTSMHAAG VVISQLPVEE YVPLSKASDG SVTTQYTMTT
LEELGLLKMD FLGLRTLTVI QNAMKNAKAS CGVDIDIDNI DFNDKNVLNM IGAGKTMGVF
QLESPGMTGF FKELKPQTLE DIIAGISLYR PGPMDFIPAY LKGKNHPEDV TYECPQLEPI
LKPTYGCIVY QEQVMQIVRD LAGYSWGRSD LVRRAMSKKK AAVMEKERQN FVYGNEEEGV
KGCIANGIDE KVANHIYDEM IDFAKYAFNK SHAAGYAVVA YQTAWLKYYY PVEYMAALMT
SVLGNANKVS EYIMACRQMG IEVLPPDINA GEAVFSVQNG KIRYGLSAIK SIGRPVIDAI
IENRCQYGKF RSLSDFISRM NNGEINKRSV ENFIKAGAFD SLGINRHAAM LVYPMMMDAM
NKEKKTSLAG QMSLFDFAPE EEKENYEIKI PKVSEFPKAE SLAFEKEVLG VYISGHPLDE
YEEKWRKNIT NTTAEFLLDE ETMKPRVHDG ATTLVGGMVV DCNIKYTKNN KTMAFLTIED
LLGTVEVIVF PREFEKYRGC LNEDEKLFVR GRVSVEEDKN AKIICEAVVP FDEISKQVWL
RFPDKETYDA KSGELFTLLA ASDGKDEIII YLEKEKAKKK LPPSRNILAN EETLETLYDF
LDKESVRVVE KSMTNAYKS
//
