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Database: UniProt
Entry: A0A1G0SWD2_9BACT
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ID   A0A1G0SWD2_9BACT        Unreviewed;      1152 AA.
AC   A0A1G0SWD2;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A3G43_03740 {ECO:0000313|EMBL:OGU76693.1};
OS   Ignavibacteria bacterium RIFCSPLOWO2_12_FULL_56_21.
OC   Bacteria; Ignavibacteriota; Ignavibacteria.
OX   NCBI_TaxID=1798438 {ECO:0000313|EMBL:OGU76693.1, ECO:0000313|Proteomes:UP000177278};
RN   [1] {ECO:0000313|EMBL:OGU76693.1, ECO:0000313|Proteomes:UP000177278}
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:OGU76693.1}.
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DR   EMBL; MHAK01000011; OGU76693.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0SWD2; -.
DR   Proteomes; UP000177278; 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          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1152 AA;  127832 MW;  45A68F2AE88BE4B8 CRC64;
     MPDFVHLHNH THYSLLDGAA TVEGLVKAAV ANKMPAVAIS DHGVMFGAIE FYKKATKAGI
     KPIIGCEAYI VTRGTRFDKS GTTERGGGGQ GRYHHILLLA KNEKGYRNLI KLCTLGHTEG
     YYYKPRIDVE LINRYHEGIV CTSACPGGIV GAHLKEGRYD DAREYASIYN DIFGEDFYIE
     IQNHGMEVEV PILRDAPRLA KELGIQLVAT NDCHYIAADH AIPHNIMLAI PEATSTFAPD
     INELRYGSDQ LYFKSAEEMH RLFKDQPEAL RSTMEIAEKC SLELDLKTNH MPAFPIPDES
     GVKNPDEYFE KLVREGMQRR YGTVAPEIED RLNLEISTIR RMGYSGYFLI VQDFIAKARS
     MGVHVGPGRG SAAGSIVSYA LGITSVDPLQ YGLLFERFLN PERISMPDID IDFADDKRDK
     VIEYVRAKYG ENSVSQIITF GTLSSRAVLK DVGRVLGIPL STIDSITKQI PVIQGKVTPI
     EEALETIPDL KWVKESPDEK IKLLIKTAKV LEGMNRNVST HAAGVVIAPS EISDYVPMYK
     TPQTDLMTQY NMKDLEDAGL LKMDFLGLRT LTVLDHAVEM VKTNFNVDLD LDRLPHPDQK
     TFELFGKGQT VAIFQFESSG MQDYLRKLKP TTIHDLVAMN ALYRPGPMEN IPDFIDRKHG
     RQQITYAHPK LEAILAETYG VIVYQEQVMR IASEIAGFSL AQADLLRRAM GKKDKKLMGD
     QKAKFVDSAV KHGTDTKTAG DIYDLIEKFA SYGFNKSHSV AYSVLAYQTA YLKAHYPAEY
     MAATMSSEMG NTDKIVLLID DCRKLGISVL PPDVNESGVH FVVTPKGIRF GMSAVKGVGV
     SAVEHIVRAR SEGGRFQDIF DFCARVDLRL NNKRTIEALV QSGAFDSLHE NRAQLFANVE
     GAIGYGQGRQ EQKGKGQSNL FDGGAMQVQA RPAMREVHPW GEQEQLHREK SVLGFYVSGH
     PLMKYADEIE GFASAMLGSP ESVRPNSTVR VFGIVTDVKK KIDKRGNTMA FITIEDFSGK
     AECIVFSDPF QKYGKLLEPG SIVMVIGRND GSDEAIKVIV NEVIAIDDVR KRFAKSVMVN
     LNLDTTSESS VHELAVLLER HTGSCPCYLN VVGGGSDKNS LYLARKFTIN PNPQFTSAVR
     QLLGPGSVRL QG
//
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