ID   A0A1F7L0J8_9BACT        Unreviewed;      1071 AA.
AC   A0A1F7L0J8;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 16.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A3K52_02160 {ECO:0000313|EMBL:OGK73574.1};
OS   Candidatus Roizmanbacteria bacterium RIFOXYD1_FULL_38_12.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802093 {ECO:0000313|EMBL:OGK73574.1, ECO:0000313|Proteomes:UP000177050};
RN   [1] {ECO:0000313|EMBL:OGK73574.1, ECO:0000313|Proteomes:UP000177050}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=27774985; DOI=10.1038/ncomms13219;
RA   Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA   Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA   Williams K.H., Hubbard S.S., Banfield J.F.;
RT   "Thousands of microbial genomes shed light on interconnected biogeochemical
RT   processes in an aquifer system.";
RL   Nat. Commun. 7:13219-13219(2016).
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   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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:OGK73574.1}.
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DR   EMBL; MGBR01000001; OGK73574.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7L0J8; -.
DR   Proteomes; UP000177050; 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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 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; IPR012340; NA-bd_OB-fold.
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   4: Predicted;
KW   DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW   DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW   Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695};
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   1071 AA;  121444 MW;  A2E596B8D39D6C43 CRC64;
     MSFVHLHLHT EYSLLDGMCR VGDILQKAKD QGMSALAITD HGAMYGAFKY YVKAKEIGVK
     PIIGVELYKA KKSRFDKQAN VDRDRYHLVL LAKDFEGYRN LLKLVSIAHL EGFYYKPRVD
     FEILKKFSKG IIAMSACLAG EIPQALLQNQ TKEAERLLET YLDIYKDNFY IELQRHPNVD
     DLEKVNKDLI SLAKRYAVPL VATNDVHYPN KEDAYAQEVL LCIQTQRTML EKNRAMSMLD
     VPDYYFKTEG EMRNSFSDLP DAIENTNKIA DLCNLEIPNG KWVLPYYETP NNMSPEEHLK
     VLVNERKSRT AIYDKKVTEK RLDYELDIIT KKGYATYFLI VQDFVNWAKN KGIAVGPGRG
     SVAGSLVAYV LRITDINPLE HNLPFERFLN PERPTPPDID IDFADIRRDE VLAYVTKKYG
     KEKVAQIITF GAMEARLAVR DVARALGQSY SQGDRIAKMI PQGKQGFQMK LAQALIEAPA
     LKFAYQSEPD VKKVVDIAMR LESLPRHSSV HAAGVIISKD DLTEYVPIQT ESKENRVITQ
     YDMYSLDLNS APNGKAVGLL KIDFLGLRNL TILEEALGFV KKSLGKTVDI HDVSLTDKKT
     YDLISKGETI GVFQLESGGM RRLAKDLKPS RMSDIIAMVA LYRPGPMDLI PMFLEGKRNP
     KSIKYLHRDL MTILEETYGI LVYQEQVMEI AHSLAGYSMS EADNLRMAMG KKKKALMDKE
     RVKFINGCVK RKYTKHLAES IFNFMEKFAA YGFNKPHSAS YALIAYWTAY MKANYPVEYM
     TALLTAELQG VAGPMREIKM AQAIEECRRM EIKVLPPDIN KSIHDFEIEN GEIRFGLSAI
     KNVGAAAIES ILEARKTGPF AGFKDFLFRV DLRKVNKKTV ESLAKTGAFN GMANPATLLF
     YYPQIVKELS DAKQESSKGQ FSLFFQTSSK ETLKDNFEPI QNFSEDELIT MEKEVIGFLI
     SKNPLIKFKN IIAQKSTKRI GEITKEDINK THVLVGVISN RKIIKTKKDN HEMAFITIYD
     ETGSIEAIVF PKLYAKISLS ISLNQAIILK GKVTEKEDQL SVIVENAMKL T
//