ID A0A1F6IM09_9BACT Unreviewed; 1075 AA.
AC A0A1F6IM09;
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=A2629_03670 {ECO:0000313|EMBL:OGH23744.1};
OS Candidatus Levybacteria bacterium RIFCSPHIGHO2_01_FULL_41_15.
OC Bacteria; Candidatus Levybacteria.
OX NCBI_TaxID=1798598 {ECO:0000313|EMBL:OGH23744.1, ECO:0000313|Proteomes:UP000176249};
RN [1] {ECO:0000313|EMBL:OGH23744.1, ECO:0000313|Proteomes:UP000176249}
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:OGH23744.1}.
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DR EMBL; MFNV01000002; OGH23744.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F6IM09; -.
DR STRING; 1798598.A2629_03670; -.
DR Proteomes; UP000176249; 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; SSF160975; AF1531-like; 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 1075 AA; 121695 MW; 055ABA3B1A1CDB48 CRC64;
MTDFVHLHNH SDYSLLDGLS KIEDMVKKAK ELGMKAIALT DHGNMYAAIK FYKECQLAGI
KPIIGCEIYI SKRSRHDKEA GIDADSNHLI LLVKNETGYK NLMKIISIAN LEGYYYKPRS
DLDLLREYHE GLICLTSCVN GYVSEPLVLN QDETGIERAK KLLEIFGEEN FYLELQKHIN
VESQDSLNEK LISLSKKLGI PLVATNDNHY INARDAQAQE VLLCIQTQTT LNDKERKLSM
ISSPDFYIKS KEEMVGLFLQ NPEAVENTVK IADMCNLEIK LGQWIMPFFD VPGNIPPSEY
IRKKVDEGLR KRYKTTIKEI KERAEYELSI IIKKGYETYI LIVSDFVNWA KSVGITVGPG
RGSNAGSIVS YALEISDVDP LFFKLPFERF LNPMRPSPPD IDLDFADNRR DEVIKYVTEK
YGRDKVAQII TFGTIEARGS VRDTGRVLGM PYSYPDRISK MIPPGWQGHA MTIDRALEQS
PDLRISYQTE PETKKLLDLA RKIEGVARHA SVHAAGVVIA DKPLTEYTPL QREPNGNKII
TQYDMYTVGE DGVGLLKIDF LGLRNLTIIQ ETLRFIKENK KTKIDLSVLP FDDEKTYELL
ASGETTGIFQ LESAGMRRYI KELRPTSIFD LQAMVALYRP GPMANIPEFI RRKHNPSLIT
YPDPRLKDIL KESYGIITFQ DDLLLTAIKV AGYSWAETDK LRKAVGKKIP SEMKKQHDKF
VEGCIDNGMQ KKNAENLWNL FEPFAGYGFG KAHAACYATI AFRTAYLKAH YPVEFMTAFL
TAESRGASGP SKNEKIAEGV AECRRLNIII FPPDINKSDS EFSIENGKSI RFGLSAIKNI
GEAAISTIIK NREKAPFKSF EDFLQRVDLG AVNKKTIESL IKAGAMDLFG KRTSLLINYP
QIIDKLNKRK KKENEGQGSL FEEDLEAKEF ETEIEDSNVE DFSSKEKLNF EKEFLGFYLT
SHPMLSELMS IKSKITHEMG LVIEEPEGVR VRIGGIVEHT RRIFTKKSGS EMAFVTIGDE
KGIVVECVIF PKVFEQYKSY IQKDTVIIVE GKVDTKNERP VIIAEKIVTV GNFAS
//
