ID R5DGK4_9FIRM Unreviewed; 1157 AA.
AC R5DGK4;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BN457_00187 {ECO:0000313|EMBL:CCX75016.1};
OS Dorea sp. CAG:105.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Dorea.
OX NCBI_TaxID=1262872 {ECO:0000313|EMBL:CCX75016.1, ECO:0000313|Proteomes:UP000017921};
RN [1] {ECO:0000313|EMBL:CCX75016.1, ECO:0000313|Proteomes:UP000017921}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:105 {ECO:0000313|Proteomes:UP000017921};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) 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:CCX75016.1}.
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DR EMBL; CAWY010000087; CCX75016.1; -; Genomic_DNA.
DR AlphaFoldDB; R5DGK4; -.
DR STRING; 1262872.BN457_00187; -.
DR Proteomes; UP000017921; 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:UP000017921};
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 1157 AA; 131403 MW; 9DCF5BFCD86E06FA CRC64;
MSFAHLHVHT EFSLLDGSNK IKECVSRVKE LGMNSVAITD HGVMFGVIDF YRAAKAAGIK
PILGCEVYVA PGSRFDKEAV GNNDDRYYHL VLLAENETGY YNLMKIVSRG FTEGYYYKPR
VDMELLEQYH EGIIALSACL AGEVQKNILR GMYGEAKAAA CRYKDIFGEG NFFLELQDHG
MEEQKLVNQS LLRMSQETGI ELVATNDIHY TYADDVKPHD ILLCIQTGKK LADEDRMRYE
GGQYYIKSEE EMRKLFPYAQ EAIDNTQKIA DRCNVEIVFG EKKLPKYDVP DGFTSWEYLN
KLCYEGLERR YPGDDPTIRE RLEYELSVIK RMGYVDYFLI VWDFIKYARD HGISVGPGRG
SAAGSIVSYC LGITSIDPLR YQLLFERFLN PERVSMPDID VDFCFERRQE VIDYVVRKYG
TDRVVQIVTF GTMAARGVIR DVGRVMDLPY AFVDGIAKMI PKELNITLGK ALQSSPDFKK
AYDNDPQVKE LIDMSMRLEG LPRHTSMHAA GVVISQKAVE EYVPLSVGSD GSVVTQFTMT
TLEELGLLKM DFLGLRTLTV IQDAVRLAEK SSSKEIDINA IDYNDKKVLD YIGSGETDGI
FQLESGGMKG FMKELKPQNL EDIIAGISLY RPGPMDFIPQ YIKGKNHPEA ITYDCPQLEP
ILAPTYGCIV YQEQVMQIVR DLAGFTLGRS DLLRRAMSKK KGDVMQKERQ AFVYGDEEGG
VPGCIANGID EKTANKIYDE MIDFAKYAFN KSHAAAYAVV SYQTAWLKYY YPVEFMAALM
TSMIDNPPKV AEYIYSCRQM GIDILPPDIN EGVGNFSVQD GKIRYGLAAI KSIGRPVIES
IVRERNERGK FKTLKDFIER LSGKEVNKRT IESFIKSGAF DGLGGTRKQF MIIYVQIVDQ
VNQERKYSMA GQLSLFDMVD DDQKAEFDIP LPKVGEYEKE TRLAFEKEVL GVYLTGHPME
EYEEKWRKSI SKTTLDFQLD KETGAAKVHD GAKEIIGGII ATLAIKYTKT NKTMAILTLE
DLLGTVEVVV FPRDYEKYKE YLQEENKVFI RGRVSEEDDA PSKLICESVV PFSQTRKELW
LQYADKDTFL AQEQMLYDLI GNSDGRDEVV IYCKKERVVK RLGRNRNVQV ETGLLSRLMN
YLGDSCVKVI EKNIENI
//
