ID A0A1H0ATB9_9FIRM Unreviewed; 1166 AA.
AC A0A1H0ATB9;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-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=SAMN05192585_11736 {ECO:0000313|EMBL:SDN36750.1};
OS Acetanaerobacterium elongatum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC Acetanaerobacterium.
OX NCBI_TaxID=258515 {ECO:0000313|EMBL:SDN36750.1, ECO:0000313|Proteomes:UP000199182};
RN [1] {ECO:0000313|EMBL:SDN36750.1, ECO:0000313|Proteomes:UP000199182}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.5012 {ECO:0000313|EMBL:SDN36750.1,
RC ECO:0000313|Proteomes:UP000199182};
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FNID01000017; SDN36750.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0ATB9; -.
DR STRING; 258515.SAMN05192585_11736; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000199182; 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:UP000199182};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 5..72
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1166 AA; 131505 MW; 7CA0E324DDEB3557 CRC64;
MNEFVHLHVH TEYSLLDGAC RIPQLIKRVK DLGQTSVAIT DHGVMYGVVD FYKEAKKNGI
KPIIGCEVYV APRTRFDKVH ALDSSPYHLV LLCQNNQGYQ NLIQLVSLGF IDGFYNRPRV
DMELLKRYSD GLICLSACLA GEIPRKLLNG EYDEAKRVAL EYEAIFGKGN YYLEIQDHGI
EEQKQIIPYI IRLSQETGIG LVATNDAHYL VREDAKMQHV MVCIQTGHTV DDDDTLEFPT
EEFYIKSGEE MKSLFSYAPQ AISNTLAIAE RCEVTFEFGV TKLPYFKAPE NKDNVEYFKE
KCYEGLKRNY GDNPAPTLYE RLDYELSVII KMGYVDYFLI VHDFIAYAKR NDIPVGPGRG
SGAGSLAAYC IGITGIDPIK YNLLFERFLN PERVSMPDFD IDFCYEKRQK VIDYVISKYG
SDHVAQIITF GTMAARAAIR DVGRALGLTF QAVDTVAKLI PTELHMTIEK ALSVMPELKT
LYENDVKIRE LIDMARKLEG MPRHASTHAA GVVITRDPVS SYVPLSKSDE SIITQFTMTT
LEELGLLKMD FLGLRNLTVI HDCEEMIRCT TPDFSMEHIP NGDQDVFKML SQGYTLGVFQ
FESAGMKRVL TDLKPDKIED LIAINSLYRP GPMESIPKYI ANRHRPELVT YKTPLLKPIL
DVTYGCIVYQ EQVMQICRQL AGYSYGRADL VRRAMSKKKA DVMEKERHNF IYGAKRDDGS
IECVGAVSNG VSEEVANDIF NEMSSFASYA FNKSHAAAYA FVAYQTAYLK YHYPKEYMAA
LLTSVLDNTD KVVEYIGECS RMNIKVLPPD INQSGEGFTV AGEGIRFGLV AIKNLGRNLI
RDLINERRNG PFTSFYSFCE RMQGSDLNKR GMESLIKAGA FDSLGYKRRQ LCLNSESILN
AIGSRSRSML EGQIDLFALN NPIKQSEPVM ADTEEFSLTE LLHYEKETIG LFISGHPLND
FRHAAERIGT VNLSDVIASQ KEETGRFKDR DIVKLLCIVT SKKLKTTKSN ETMAFIEIED
TTASVEAIVF PKLLADNTKL LTVGGTVVIT GRVSVREEEE PKIVCENIES VEQAVASSVA
AERINTAPEK KGRTGLFLKL ESRQDERLKK AQNILEYFNG TTAVYVYFNH EKELTQAPAS
LWITPYPNML LELKRILGAE NVVLRE
//
