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Database: UniProt
Entry: R6APN4_9FIRM
LinkDB: R6APN4_9FIRM
Original site: R6APN4_9FIRM 
ID   R6APN4_9FIRM            Unreviewed;      1140 AA.
AC   R6APN4;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=BN678_00509 {ECO:0000313|EMBL:CDA50674.1};
OS   Dialister sp. CAG:486.
OC   Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC   Dialister; environmental samples.
OX   NCBI_TaxID=1262870 {ECO:0000313|EMBL:CDA50674.1, ECO:0000313|Proteomes:UP000017985};
RN   [1] {ECO:0000313|EMBL:CDA50674.1, ECO:0000313|Proteomes:UP000017985}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:486 {ECO:0000313|Proteomes:UP000017985};
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:CDA50674.1}.
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DR   EMBL; CBBY010000276; CDA50674.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6APN4; -.
DR   STRING; 1262870.BN678_00509; -.
DR   Proteomes; UP000017985; 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:UP000017985};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1140 AA;  127450 MW;  403EE173336BA58D CRC64;
     MDPFVHLHVH TEYSLFDGTC RIKELVSYVK SLGQTAVAIT DHGVMYGAVY LYKECIAQGI
     KPIIGCEVYV TRKSRFERAK GEKEKLGHLI LLAETNEGYQ NLIKICSKAW TEGYFHKPRV
     DHELLSKYHK GLIALSACVA GELPQAILNR DMDEVRKVIR YYIDTFGKEN YFLELQNHGI
     PEEADVRPVL ASLAKEYGLG LVATNDFHYT KKEDAKSQEI KLCISTGKTL DDPYHFHFPN
     DEFYCKSGEE MQAILGEYPG AIENTAKIAE RCHVTFTFGN HKLPSFDVPE GETSKSYLRK
     LCEAAIPERY PESTGKEQER LDYELGVINQ MGFSDYFLIV MDFIRYAKTH GIPIGPGRGS
     AAGSIVAYLL HITEIDPLRF DLLFERFLNP ERVSMPDIDT DLCYRGRGQV IAYLAEKYGA
     EQVAQIITFG TLAARAVIRD VGRVMNLPLR EVDKIAKMVP SGPGVTLKKT LDGSKEFKDL
     YESNATVRTL IDHCLDLEGL SRNSGTHAAG VVICSKPVDE YVPIQLTADD FIQTQYEKDQ
     VEQLGLLKMD LLGLRNLTVI HDAVEMIRAN RGVTIDIDRI PSVDEKTCEM LCAGDTTGVF
     QSESSGFTNL LMKLHPDRFE DLIPMVALYR PGPLGSGMAE DFIKRKHGEI PIEYPHPSLA
     PILKETYGVI LYQEQVMQIA SVMGGFSLGQ SDMLRRAMGH KEPEILQKNR DTFVTGAVKN
     GVDEKTANYV FDLMVHFAGY GFNKSHSVCY GWIAWQTAYL KAHYRAEFMA AMMTCYNGDK
     NKVSRYISDT RRAGVEIAAP DVNLSEAYFS VSGNKILFGL DAIQNVGENA VEAIIKARKK
     GGPFTSMSDF LERVEGKGLN SRACESLIRC GAMDGFGYNR SQLLAALPQV MSDVAASKSD
     RESGQMSLFG GDEMKSSVVY PDLEDMDADE KIDWERKLLG FYVSGHPLEK YKKQMAACTP
     IYQLETEGSR YDGKTVTLGG TVTRVKGMVT KKGAPMGYVT IEDYESEIES VLFPSVWEAA
     RPFLTEDAPI CIRGRVQSNE REVKILADSI IPMAQFQKTV RMPVDEVHLY VDPRHETDKV
     SAALARVLAK YHGGTPVILH LISSRQEIRM VPKFYVDFSE EAEEALKGLL GNAAVEGRKN
//
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