ID A0A1F5CD00_9BACT Unreviewed; 987 AA.
AC A0A1F5CD00;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
DE Flags: Fragment;
GN ORFNames=A3I30_00080 {ECO:0000313|EMBL:OGD40725.1};
OS Candidatus Azambacteria bacterium RIFCSPLOWO2_02_FULL_44_14.
OC Bacteria; Candidatus Azambacteria.
OX NCBI_TaxID=1797306 {ECO:0000313|EMBL:OGD40725.1, ECO:0000313|Proteomes:UP000177197};
RN [1] {ECO:0000313|EMBL:OGD40725.1, ECO:0000313|Proteomes:UP000177197}
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:OGD40725.1}.
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DR EMBL; MEYV01000002; OGD40725.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F5CD00; -.
DR Proteomes; UP000177197; 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 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; 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 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 2..94
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 214..483
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 486..649
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 722..812
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 905..981
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:OGD40725.1"
SQ SEQUENCE 987 AA; 111575 MW; 57472518B6BA4643 CRC64;
KRFHLTLLIK NKTGYGNLVQ LITKAHLEGF YYKPRVDKDC LKEHAEGLIC LSGCSNSEIS
HLIYSNQPEA AKNAALEYRD IFGKENFYIE LQPHFELDRS KKIYPKLLEL AREVEAPIVA
TNDAHYLAKE DDDYQDVLLA IGTGNKVSDP NRLTMKGVNL SLRSAQDMEE LFKDLPEAIE
NTQKIADACN FEFEFGTMQL PHFELPEGKT IEGYLKELAH EGLKKLFGYT LEEAPEAIRE
RFLFELSVIK RTGFPSYILI VQDFVNWAKE RGIVVGPGRG SAAGSLISYL IGITNIDPIK
YNLLFERFLN PDRIAPPDID LDFADHRRDE VIEYVAQKYG RDHVAQIITF GTMAARAAVR
DAGRALGFSY TFCDRVAKMI PFAVGMTFAK ALEISDELKQ VMDTDPQARQ LIQTAQKLEG
VARHASTHAC GVVITKNPIT HYMPIQWAAQ SNARAKGQGQ ALVTQYDMKA VEALGLLKMD
FLGLRNLTII EKALELIEKN YGQRIDIYNI PLDDKDTFGL LARADTTGVF QFESKGMRRY
LKELRPNALE DLIVMVAAFR PGPMEFIPTY IARKHGKEKV NYLHPKLAPI LESTYGVAIY
QEQVLKIANQ LAGFTIGEAD ILRKAVGKKI KKLLDEQREK MIIGMINNGI DKITAEKIWD
FIEPFARYGF NRSHAACYAL IAYQTAYLKT RYPGEFMTAL LNTESFDIDR VAELIEETKR
MGIDVSPPDI NESARYFTLI QDEFGKRIRF GLGAIKNLGE NAVSAIMKEL EVGRFTELQS
FLERVPAKDL NKKSLESLIK CGALDAYGDR KTLYDNIEEL LRYSKDWSRS KESPQGGLFG
ANISVAPLRI KPTESATKKE KLGWEKELLG LYISDHPLKE YQQLLEKNAV LINNIKPALD
GKRINVGGVI SSVQKFVTKA HQLMLFVKIE DWLANIEVIV FPSVLEKTAN LWQENSMVMI
QGRVSNRDGN LKIICDTVQE LKAESRI
//
