ID F7JKH9_9FIRM Unreviewed; 1168 AA.
AC F7JKH9;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=HMPREF0988_00937 {ECO:0000313|EMBL:EGN31236.1};
OS Lachnospiraceae bacterium 1_4_56FAA.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=658655 {ECO:0000313|EMBL:EGN31236.1, ECO:0000313|Proteomes:UP000004289};
RN [1] {ECO:0000313|EMBL:EGN31236.1, ECO:0000313|Proteomes:UP000004289}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1_4_56FAA {ECO:0000313|EMBL:EGN31236.1,
RC ECO:0000313|Proteomes:UP000004289};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Daigneault M., Strauss J.,
RA Allen-Vercoe E., Young S.K., Zeng Q., Gargeya S., Fitzgerald M., Haas B.,
RA Abouelleil A., Alvarado L., Arachchi H.M., Berlin A., Brown A.,
RA Chapman S.B., Chen Z., Dunbar C., Freedman E., Gearin G., Gellesch M.,
RA Goldberg J., Griggs A., Gujja S., Heiman D., Howarth C., Larson L., Lui A.,
RA MacDonald P.J.P., Mehta T., Montmayeur A., Murphy C., Neiman D.,
RA Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N., Sisk P.,
RA Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Lachnospiraceae bacterium 1_4_56FAA.";
RL Submitted (MAY-2011) 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:EGN31236.1}.
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; ACTN01000008; EGN31236.1; -; Genomic_DNA.
DR AlphaFoldDB; F7JKH9; -.
DR STRING; 658655.HMPREF0988_00937; -.
DR PATRIC; fig|658655.3.peg.945; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_9; -.
DR Proteomes; UP000004289; 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:UP000004289};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 15..82
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1168 AA; 133412 MW; B45733A41880C3FF CRC64;
MGTALFFRRH SMNFAHLHVH TEYSLLDGSN KIKEYVGRVK ELGMNSAAIT DHGVMYGVID
FYRAAKAAGI KPILGCEVYV APNSRFDREL AGGEDRYYHL VLLAENNTGY ANLMKIVSKG
FVEGYYYKPR VDKEVLRTYS EGIIALSACL AGEVQRYISK GLYDEAKNKA LEYEEIFGKG
NYFLELQDHG IPEQAFVNQK LMQMSEELGI ELVATNDVHY TYAEDEKPHD ILLCIQTGKK
LADENRMRYE GGQYYVKSPE QMAELFPYAL QALENTQKIA DRCNVEIEFG VTKLPKYEVP
DGMTSWEYLN KLCFEGLERR YGNPGEELKE RLTYELDTIH NMGYVDYFLI VWDFINYAKT
HGIAVGPGRG SAAGSIVSYC LEITDIDPIR YQLLFERFLN PERVTMPDID VDFCYERRQE
VIDYVVRKYG KDRVVQIVTF GTLAARGVIR DVGRVMDLPY AFVDSIAKMI PQELNITIDK
ALKMNPELRK SYESDEQVKY LIDMSRRLEG LPRHSSMHAA GVVISQKSVD EYVPLSRASD
GSITTQFTMT TLEELGLLKM DFLGLRTLTV IQNAVKMAKK RMPDLDIDKI DYNDQDVLDY
IGTGKTDGIF QIESAGMKSF MKELKPHSLE DIIAGISLYR PGPMDFIPQY IKGKNDANSI
TYDCPQLEPI LAPTYGCIVY QEQVMQIVRD LAGYTLGRSD LLRRAMSKKK ADVMQKERQI
FVYGDEENGV PGCIKNGIDE KTANKIYDEM IDFAKYAFNK SHAAAYAVVA YQTAFLKYYY
PVEFMAALMT SVIENPPKVA EYIYACRHMD IKILPPDINR GVADFSVDEG CIRYGLMAIK
GVGRPVIDVI VKDREEFGPF KNLEDFITRI SMKDTMNKRV IESFIKAGAL DCLGGTRKQF
MSIYIRIVEH VSQEKKYAMT GQMTLFDLVE DDQKSEFEIK LPDVGEYAKE TSLAFEKEVL
GIYISGHPLE AYEETWKRNI SATTADFQPD EETGRAKVRD GAKEIVGGMI TEKTVKATKT
NQMMAFLTVE DLLGTVEIVV FPRDYEKNRE YLEVDQKVFV KGRVSEEEEK ASKLICEKII
PFERTKKELW IQFPDKAAYM EQEPIVFGYL ADSEGDDEVV IYCQQERAVK RLPRNRNIRI
DPQILGRLMN HFGEKRVKVV EKTIENKI
//
