ID R7JRZ2_9FIRM Unreviewed; 1157 AA.
AC R7JRZ2;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BN630_01040 {ECO:0000313|EMBL:CDE65607.1};
OS Blautia sp. CAG:37.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX NCBI_TaxID=1262757 {ECO:0000313|EMBL:CDE65607.1, ECO:0000313|Proteomes:UP000018204};
RN [1] {ECO:0000313|EMBL:CDE65607.1, ECO:0000313|Proteomes:UP000018204}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:37 {ECO:0000313|Proteomes:UP000018204};
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:CDE65607.1}.
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DR EMBL; CBJJ010000063; CDE65607.1; -; Genomic_DNA.
DR AlphaFoldDB; R7JRZ2; -.
DR Proteomes; UP000018204; 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; SSF160975; AF1531-like; 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:UP000018204};
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; 130867 MW; 204613C1842B8FB5 CRC64;
MSFTHLHVHT EYSLLDGSNK IKEYVARVKE LGMNSAAITD HGVMFGCIDF YKEARAQGIK
PILGCEVYVA PGSRFDRETS RGEDRYYHLV LLAENNTGYS NLMKIVSAGF IDGFYYKPRV
DMEILEKYHE GIIALSACLA GEVARAMVRN QYEMGKEAAL RYEKIFGKGN FFLELQDHGI
SEQRMVNQQL MRLSAETGIE LVATNDIHYT YAEDADSHDI LLCLQTGKKI TDEDRMRYEG
GQYFVKSEAE MASLFPYAPQ AIENTQKIAD RCNVEIEFGV TKLPKFDVPE GYTSWEYLNK
LCYDGLEERY HPATDELKAR LKYELDTIKT MGYVDYFLIV WDFIKFARDH DIMVGPGRGS
AAGSIVSYTL GITQLDPMRY QLLFERFLNP ERVTMPDIDV DFCFERRPEV IDYVTRKYGK
DRVVQIVTFG TLAARGVIRD VGRVLDMPYA QVDSIAKMIP NELNITIDKA LQMNHELREL
YQGNEEVAHL IDMSRRLEGL PRHTSMHAAG VVIGSRPLVE FVPLSRGSDG TIVTQFTMTT
LEELGLLKMD FLGLRTLTVI QNATKLAERY SNKKIDLLHI DYNDPKVLGM IGASKTVGVF
QLESAGMKNF MKELKPQSLE DIIAGISLYR PGPMDFIPQY IKGKNNPESV TYDTPLLKPI
LEPTYGCIVY QEQVMQIVQA LAGYSLGRAD LVRRAMSKKK ASVMEKERQN FVYGNEAEGV
PGCIKNGIDE KTANKIYDEM IDFAKYAFNK SHAAAYAFVS YQTAWLKYYY PVEFMAALMT
SCIDNPGKVA EYILSSRQMG ISILPPDINR SEGKFTVDGQ AIRYGMAAVK GIGKPVMEAI
VEERSANGPF RSLKDFAERL SGKEVNKRTV ENFIKAGAFD CFGVTRKQLM FVYANVLDDV
AREKKDSLSG QMSLFDFVDE TTKRSYETVY PDVGEYEKSD LLALEKEVLG IYVSGHPLEE
QEECWRKNIS AVTTDFQPDE ETGFPSVTDG AKEIVGGIIT DKKIKYTKNN KTMAFLTLED
LVGSMEIVVF PRDYEKNAAM MQTDARVFIQ GRVSAEDDKP SKLICEKIFP FAGIPKELWI
QFPDKETYER EVADLYQMLH ESDGKDSVIL YIKSIKAMKK LPPSRNVQAD ARLVASLQAK
FGTGNVKVVE KSIEKRA
//
