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Database: UniProt
Entry: A0A1F7J6P0_9BACT
LinkDB: A0A1F7J6P0_9BACT
Original site: A0A1F7J6P0_9BACT 
ID   A0A1F7J6P0_9BACT        Unreviewed;      1071 AA.
AC   A0A1F7J6P0;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   13-SEP-2023, entry version 17.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A3B50_04780 {ECO:0000313|EMBL:OGK51277.1};
OS   Candidatus Roizmanbacteria bacterium RIFCSPLOWO2_01_FULL_40_42.
OC   Bacteria; Candidatus Roizmanbacteria.
OX   NCBI_TaxID=1802066 {ECO:0000313|EMBL:OGK51277.1, ECO:0000313|Proteomes:UP000178558};
RN   [1] {ECO:0000313|EMBL:OGK51277.1, ECO:0000313|Proteomes:UP000178558}
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:OGK51277.1}.
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DR   EMBL; MGAQ01000002; OGK51277.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1F7J6P0; -.
DR   Proteomes; UP000178558; 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   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;  121549 MW;  86CE3D97E776AFB9 CRC64;
     MSFVHLHNHT EFSLLDGMAR VEESIQKAKE LGMPALAITD HGALYGAFKF FLKAKEYGVK
     PIIGVEAYKA KNSRFDKQIS IDRDQNHLIL LAKNLNGYQN LMKLVTQAHL EGFYYKPRID
     FDLLEKYGEG LIALSGCLKG ELPQLIMENQ TTEADKVLKK YLQIFGKNFY IEIQRHPKMP
     ELDSVNEQLI KLSRKHAVPL VATNDVHYIN KDDAYAQEIL LCIQTQRTIL ENNRPLSMYN
     NPDFYFKSAS EMKGQFLDLP EAIDNTVKIA EECNLEIPYG NWILPRFETP KGETAAQYLK
     ELVEKKAHRL KDSKGKEVQD RTKYELDIIT SKGYSTYFLI VQDFVNWAKE NHIMVGPGRG
     SVAGSLVAYI LGITDINPLL YNVPFERFLN PERPTPPDID IDFADIRRDD VLHYVRQKYG
     EDRVAQIITF GTMEARLVVR DVARALGWSY SQADRLAKMI PPGRQGFSMS IAQALEESSV
     LKFAYQTEPE TKKLLDIAQK LEGLPRHAST HAAGIVISDK PLTEYVPLQK ENKEGKIITQ
     YDMYCLDLNA VSSNQAIGLL KVDLLGLRNL TILEETLKYV EKTTGKKINI HEVPLDDKKA
     YELVSEGKTI GVFQLESTGM RRLAKDLKPN KLSDIIAMVA LFRPGPMELI PIFLEGKSNP
     QGVRYLHQDL KPILEETYGV LVYQEQVMEL ANKLAGYSMS EADNFRLAVG KKKKGLMKIE
     KEKFIKGAIK NKYSKSLADK IFNFIEKFAA YGFNKPHSTS YALIAYWTAY MKANYPAEFM
     TALLTAELQG IAGPMREIKM AQALEECRRM KIKVLPPDIN RSYESFRIEG NGVRFGLSAI
     KNVGHAAIES IVEARNKGDF RGFKDFLLRV DLRKVNKRTV ESLIKTSAFS KFGNRATLLS
     VYPKLVKEIG ELKVDKEKGQ SGLFDVAGRD EVLKDNFEEI KEFTEDEIFA MEKEVIGFLI
     NKNPLEKFKE IVEKKATKKI GEISRDDLNQ KLVLVGIISG KKVIKTKKNN DEMAFVTLFD
     ETGSVETVVF PSLYKKLLSV LAINQVLIFK GSITEKDDRI SMIMDVAMKL S
//
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