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Database: UniProt
Entry: A0A1G0YT46_9BACT
LinkDB: A0A1G0YT46_9BACT
Original site: A0A1G0YT46_9BACT 
ID   A0A1G0YT46_9BACT        Unreviewed;      1198 AA.
AC   A0A1G0YT46;
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-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=A2017_08075 {ECO:0000313|EMBL:OGV49133.1};
OS   Lentisphaerae bacterium GWF2_44_16.
OC   Bacteria; Lentisphaerota.
OX   NCBI_TaxID=1798571 {ECO:0000313|EMBL:OGV49133.1, ECO:0000313|Proteomes:UP000176916};
RN   [1] {ECO:0000313|EMBL:OGV49133.1, ECO:0000313|Proteomes:UP000176916}
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   -!- 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:OGV49133.1}.
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DR   EMBL; MHBF01000126; OGV49133.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G0YT46; -.
DR   STRING; 1798571.A2017_08075; -.
DR   Proteomes; UP000176916; Unassembled WGS sequence.
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: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; 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   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          6..73
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1198 AA;  135305 MW;  11B7024C0EF45A73 CRC64;
     MPSEFVHLHL HSDYSLLDGA CSVSGIVKMA EAYKMRAVAM TDHGFMGGLI DFYQQMNAAK
     IKPIIGCEAY ISPTTRFDRD PNNPNIRGFH VVLLAKNEAG YKNLCKLIAE ANLNGMYYKP
     RIDREILAKH HDGLIALSAC IKGEIPSAIL DGKIKDAKRI LREYLDMMGK ENFYLEIMDH
     GLEEQKKINR ELILLSKEFD VPLVATNDVH YLKEEHAKAH ELMLCIQTRS TINDPKHFKF
     SSDQFYFKNG VEMRELFKEV PEAVKNTLEV AEKCNVVFTF APAANHYPVY QIEGNTDRKK
     YLRDICLQGI RERYGFEPLD AGLDAEKKKT LERMDYELNI IDNSHYTSYF LVVWDFLRYA
     KQSGIPVGPG RGSGAGSIVA YLTRITDVDP LRYKLLFERF LNPERISPPD FDIDFCERRR
     TEVIEYVRKK YGAENVAQIG TYGTLKAKAV IKDIARVTGH SIAESDLITK LIPNDPKMTL
     KKAIEASSEM RELINKEAWV KEIFDYAEAL EGLNRNMTIH AAGVIIGDQK LNGLVPLAKG
     SAGEIITQYS AKPCENLGLL KMDFLGLKTL TIIQDAIDNI KKFRGQEIII DNLPLDDQPT
     FNLLNRGDTV AVFQLESDGM QNLCRQFGVE TIEHIIALIA IYRPGPMEFI PDFVSRKMGQ
     STFEYEHPAM EPILKETYGI MLYQEQVMQI VQALAGFTPG QADTLRAAIS KKKVKDIELL
     KAKFLKDAPP FTKISEKTAN IIWEKIAKFA GYGFNKSHSA AYAFLAYRTA YLKANYPVEF
     MTAVLASEID NAEKIAFFIN ECREMEISIL PPDVNSSDIN FTVNGSSIRF GLGAIKGVGS
     NAANAIISSR EKEGPFKSML DFCERAGSSV NTRMLEHLIR SGAFDTFKVK RSQLIEITGA
     VLSMAQSTIK DKESGQGSLF DMLPEAERED TFAIPLPDIP EFDENEMLKD EKALLGFYVT
     GHPLAKYAEL IKTFSTVNLL KAKTLEHDTG IKIGGIIKSV QKRRSKKDDK PYAIVQLEDL
     EGSMECMVYN KLFEKELDED LRENDSTIFV KDLLEDEKPI FVEAFVNQRD ENEVKKLIAE
     KIVPMSAVSK KYTRELHLHV FEVSTKHKDL EDIKELCGKH PGESRVIFCV KCANGDIAYL
     ESSDKTKVSV DETLLHKIQE VLGERRYKLK ADKAVPIQKN RFYRNGANGK NGQEAPSQ
//
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