ID R5E138_9CLOT Unreviewed; 1159 AA.
AC R5E138;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 24-JAN-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=BN724_01257 {ECO:0000313|EMBL:CCX86188.1};
OS Clostridium sp. CAG:590.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1262825 {ECO:0000313|EMBL:CCX86188.1, ECO:0000313|Proteomes:UP000017939};
RN [1] {ECO:0000313|EMBL:CCX86188.1, ECO:0000313|Proteomes:UP000017939}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:590 {ECO:0000313|Proteomes:UP000017939};
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:CCX86188.1}.
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DR EMBL; CAXF010000053; CCX86188.1; -; Genomic_DNA.
DR AlphaFoldDB; R5E138; -.
DR STRING; 1262825.BN724_01257; -.
DR Proteomes; UP000017939; 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:UP000017939};
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 1159 AA; 131682 MW; EDE293EC2B6C0CBC CRC64;
MSFTHLHVHT EYSLLDGASK IPELVHQAKE LGMDSIAITD HGVMYGVIDF YRAAKKEGIK
PIIGCEVYVA PGSRFDKEAG KNENRYYHLV LLAENDTGYH NLMKIVSRGF TEGYYYKPRV
DREVLQEFHE GIIALSACLA GEVATYLRQG FYEEAKKAAL EHVEIFGGNN YFLELQDHGI
DDQQTVNQGL LRMSQETGIP LVATNDIHYV KKEDAEAHDI LLCIQTGKKV ADEDRMRYEG
GQYYLKSPEE METLFPYAKQ ALENTGKIAE RCNVEIVFGE QKVPKYEVPE GFTSYSYLKA
LCQEGLERRY DPVTPQLQER LDYELSTIET MGYVDYFLIV WDFIKYAKDH GIAVGPGRGS
AAGSIVSYCL EITNIDPIRF NLLFERFLNP ERVTMPDIDV DFCYERRQEV IDYVVRKYGK
EKVVQIVTFG TMAARMVIRD VGRVLDMPYA AVDRIAKMIP MGQNGHNPTI KEALTISSDL
KKAYDEEEDV RYLLDMSQRL EGLPRHASMH AAGVVIGQKA IDEFVPLSRG SEDAITTQFT
MTTIEELGLL KMDFLGLRTL TVIQDAVRNI KQSKGIDIDI DHLNMEDPEV YDLLCTGQTD
GIFQLESNGM KSFMKELKPR NIEDIIAGIS LYRPGPMDFI PLYIKGKEHP ETITYDCPQL
EKILSPTYGC IVYQEQVMQI VMELAGYTLG RSDLVRRAMS KKKGDVMQRE RQNFVYGNEE
EHVPGCINRG IDEKTANKIF DEMIDFAKYA FNKSHAAAYA VVAYQTAYLK CHYPAEFMAA
LITSVLDRTD KVSEYIAHCR KLDIPILPPD INEGYSQFSV SGNAIRYGLS ALKSVGRPVI
DAIVAEREAH GRYRDLKDFI SRLSNKEVNK RTIESFIKSG ALDSFPANRR QMMMIYVQLI
DQVNQEKKSA MTGQMSLMDL LGEEEKKAFD IRYPDVAEYE KEEKLSFEKE VLGIYVSGHP
LEDYQNLMDT NINATTHDFI ADAETGETVA KDQIYYTIGG MIAAKTVKMT KSNQNMAFIT
LEDLLGSLEV VVFPKKYEQY RSILEPDSKI LVYGRASISE DEGKLLLERA VSFDEIPKHV
YVQCLNKEAY TQQENAIYDI IDKYPGSSPV TVCLKEEHQS KDLGRQFYLK AGEEAIGELK
QLLGEGKVLC RQEKWNPGR
//
