ID A0A1G1P5C8_9BACT Unreviewed; 1146 AA.
AC A0A1G1P5C8;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A3D87_06045 {ECO:0000313|EMBL:OGX37088.1};
OS Omnitrophica WOR_2 bacterium RIFCSPHIGHO2_02_FULL_50_17.
OC Bacteria; Candidatus Omnitrophota.
OX NCBI_TaxID=1801857 {ECO:0000313|EMBL:OGX37088.1, ECO:0000313|Proteomes:UP000177986};
RN [1] {ECO:0000313|EMBL:OGX37088.1, ECO:0000313|Proteomes:UP000177986}
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:OGX37088.1}.
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DR EMBL; MHGQ01000063; OGX37088.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G1P5C8; -.
DR STRING; 1801857.A3D87_06045; -.
DR Proteomes; UP000177986; 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 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1146 AA; 128838 MW; CEA9E5834BA01CB4 CRC64;
MNPSDFVHLH VHTQYSLLDG ACRIKNLIQK AVDYKMPALG ITDHGNLFGA IDFYQTATAM
GVKPIIGCEA YVVTAGSRLD KQSREKGGVS HLVLFARDNE GYHNLMKLVS LAYLEGFYYY
PRMDKEILAQ YAKGLLGTSA CLKGELSWHL QQGNYNTALK TADDLHHIFG KGNFYLEIMD
HGLPEQKTVN EGLLKIAREL DLPIVVTNDV HYLEQSQSTA HEALLCIQTQ STLDDPKRMR
LKTDQFYFKD PDLMRREFSW IPQGLANTVE IADKCQLNLD FDRIHLPRFT PPEGKTKEAY
IRELCEEGLK RRYSHATQEI LDRLNHELKV IEKMGFASYF LIVSDFINFA RQKGIPVGPG
RGSAAGSLVS YLLGITDLDP LVYGLLFERF LNSDRKGMPD IDIDFCYERR GEVIDYVTQK
YGKEKVAQII TFGTMQARAA IRDVGRVKGV PYAQVDKIAK LIPAELGITI EDALVKEPQL
EKLCKEDKTA AEILETAKVL EGLNRHASTH AAGVVIADKP LDEYVPLFKT SEGQVTTGFA
MNAIAKIGLL KMDFLGLRTL TVISEAVQLI QRRHDIQMDI HTIPLGDRKT YELLGNANSF
GVFQLESAGM RELLKKIKPS EFEDIISVLA LYRPGPMGSG MLDDFIKRKR GDVQVKYDHP
KLEPILKETY GIIVYQEQVM KIAVALAGFS MTQADHLRQA MSKKIASVME KMRQDFIHGC
YKTSGIDEKK ANRLFDLIDY FSGYGFNRSH SAAYAVISYQ TAYLKANYPV EFMCALLNSE
KDNTDKIVEY VKECEAMGIG ILPPDINQSR KDFDVVDDHT IRFGLLALKN VGSTAINSIV
ENREKGMYAS LFDLCERVDL RLVNRKVMES LIKAGALDCF QAFRSQMMEV LERALGAGAR
SQKEKAVGQV SFFDLVGESG GFTSGAEKNL PNIKEWPKNK ILAFEKEILG FYISGHPLLH
YRAEIKEFSN YSIKNLKEAI DGEEVKLVGL LEEVKLTNTR KTNERMAILK LEDMDGEVEA
VVFPSAYTTL ASYLNGGEVV FLSGRVSRRD EEPKIVVTDI KRVHDVYGAI KTINVDLAVV
GQEKLKDLRE RLSRSPGSVP VYLRLDTKSH KSVQILVGED LFVTPNEHLM NEIKELVGEG
NFSLTL
//
