ID R6CWB2_9FIRM Unreviewed; 1162 AA.
AC R6CWB2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BN516_00978 {ECO:0000313|EMBL:CDA80948.1};
OS Firmicutes bacterium CAG:176.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263007 {ECO:0000313|EMBL:CDA80948.1, ECO:0000313|Proteomes:UP000017932};
RN [1] {ECO:0000313|EMBL:CDA80948.1, ECO:0000313|Proteomes:UP000017932}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:176 {ECO:0000313|Proteomes:UP000017932};
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:CDA80948.1}.
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DR EMBL; CBCO010000003; CDA80948.1; -; Genomic_DNA.
DR AlphaFoldDB; R6CWB2; -.
DR Proteomes; UP000017932; 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:UP000017932};
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 1162 AA; 130040 MW; 450A639A9FDC51B0 CRC64;
MGFVHLHVHT EYSLLDGACR IRDLPKLVKE LGQTACAITD HGVMYGAVDF YRACKAEGIH
PIIGCEVYVA RRTRFDKQHE FDAESRHLVL LCKNETGYRN LSYMVSQAYI EGFYIKPRID
MELLRAHSDG LIALSACLAG EIPKRLMNGD YNGAKAYALE MRGIFGEDFY LELQDHGIAE
QTEVNRGLLR LHNETGIPLV CTNDAHYLRK EDAENHDVLL CIQTGKTVDD ENRMRYEPRN
FYIRSTEEME TLFAGYPDAV ANTEKIAEKC QLEFTFGKYH LPEFKLPEGY DSPTYLRKLC
DEGFAQRYGQ AKPEYRKQLD YELDMIEKMG FTDYFLIVSD FVRYAKSRGI PVGPGRGSAA
GSMVSYCLEI TDIDPMKYDL YFERFLNPER VSMPDIDMDF GDTRRGEVVE YVRKKYGDDH
VAQIVTFGTM AARAAIRDVG RALNMTYAEV DVVAKLVPAG PGALHITLQE ALKLSKQLAD
MYRENPKVKK LIDTAMALEG MPRHASTHAA GVVITKLPVY EYVPLARNDD AVVCQYVMTT
LEELGLLKMD FLGLRNLTVL DDAVKMVQQR EPEFALSKIP DDDAETYDMI SRGQTAGVFQ
IESTGMTGVC VGLKPQSIED ITAVIALYRP GPMESIPRFI ACKHDPKLVT YKHPRLVPIL
SVTYGCIVYQ EQVIRIFQEL GGFSLGQADM VRRAISKKKA KEIEKERQAF VYGDAERGIK
GCIANGIDEK TAQAIYDEIY DFANYAFNKA HAVSYAVVAY QTAYFKCHYT KEYMAALLTS
VLDNSDKVAG YIGECRDCGI ALLPPDVNRS SDRFTVEPDG IRFGLVAIKN IGRGFIQSVV
REREQGGSFT SLQDFCDRMY DCGDMNKRAV ENLIRSGAFD SMGARRSQLL AVYEKVLDGI
GNVRRRNVEG QIDFFGMSAA NSTVETVVMP DIPEFTATER MHMEKETTGL YLSGHPMVGY
RAAARSSGAV TLNEILEDVS SEEGPTRFAD GMPVTVAGIV ASSKTRPTKN GTLMAYVVLE
DETASMELLC FSRVLDKCGS YLAVNSPVLI KGRLSLRDEK PPQIMPDVVF PMNGSELPEG
QKAPENGAAA VYLRVKSIDD PAFSHLLLVA TMFEGKVPLK IRIADTGKLW GGFCLDHPAF
LKECREWLGP ENVVVRRKEK SE
//
