ID A0A1G0YYD5_9BACT Unreviewed; 1224 AA.
AC A0A1G0YYD5;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 13-SEP-2023, entry version 19.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=A2X49_05665 {ECO:0000313|EMBL:OGV50902.1};
OS Lentisphaerae bacterium GWF2_52_8.
OC Bacteria; Lentisphaerota.
OX NCBI_TaxID=1798575 {ECO:0000313|EMBL:OGV50902.1, ECO:0000313|Proteomes:UP000179262};
RN [1] {ECO:0000313|EMBL:OGV50902.1, ECO:0000313|Proteomes:UP000179262}
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:OGV50902.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MHBJ01000129; OGV50902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G0YYD5; -.
DR Proteomes; UP000179262; 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; 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 42..109
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
FT REGION 1201..1224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1224 AA; 136276 MW; DDF1770EEFA46568 CRC64;
MIFFEENAAA GLILHLGGRI IGELAGRVPE KREKEKMSAE FVHLHVHTDY SLLDGACATS
GLVELAQNFK MPAIAITDHG FMGGAIEFYQ ELCKGKLKPI IGCEMYVSPT TRFDKNPEQA
NIRGFHLVLL ARDNEGYKNL CKLISEAHIN GRYYSPRIDK ELLSRHSAGL IGLSACLKGE
VAQAVLDGRK KDAGRILNEY LDILGRENFY LEIMDHGMEE QKKIVREFQV LSREFDVPLV
ATNDVHYLKR EHATAHELML CIQTHSTMAD EKRLKMTGSE FYFKSPQEMG EIFREVPSAL
KSTLAIAERC NVNFKFAPEA NHYPVYEIPT PGVTQKEYLR KVCLENIQKR YDFDPLSASL
TEEQKAVLKR MDFELDVIDQ SKYCSYFLVV WDFIHHAKKE GVPVGPGRGS GAGSLVAYLT
GITDIDPLRY KLLFERFLNP ERVSPPDFDI DFCERRRVAV IDYVRQRYGA DNVAQIGTYG
TLKAKAVIKD VARAMGRSFA DGDMITKLIA NDPKMNLKKA REDSKELREL IANEAWVAEV
FRHAEPLEGL NRNMSIHAAG VIIGDQRLDN LVPLAMGAGG EIITQYPAAP CENLGLLKMD
FLGLRTLTVL QDAVDNIRKH RGIAIEMDRI PLDDKATFDL LNKGDTVSVF QLESSGMQAL
CRQFGVETIE HIIALIAIYR PGPMEFIPDF VARKMGSTKI EYDHPAMKPI LEETYGIMLY
QEQIMQAVQV LAGFSLGQAD ILRRAIGKKK VKELEEQRDK FIKGCASANN IPQAQAEQIW
DKIAKFAGYG FNKSHSAAYA FLAYRTAYLK ANYPVEFMTA VLASEINDAD KIAFLINECR
EMGIKILPPD VNTSDMNFSV DGPSIRFGLG AVKGVGESAA SAIIAARSEK PFESFLDFCE
RAGSLNSRML EHLIRAGAFD TFGGKRSQLV ATIDATIALA QDRVQDQASG QGSLFDMLDA
SEQSAVQTVS LPDIPEFEEG EMLRDEKALI GFYVTGHPLG EYADLLSTYT TTSLARAAEL
PTDTGVKVGG IIKSVKKMVS RKNDSTFAVL LLEDLEGSTE CMVYGRLYEK EIELPGTGKV
FVKDILQEGA PVFIEALVSR RDPNEKGKLS AESVLPLQNI TEKYTSELHI HLYQGSNKHA
DIEDLQKLCS ANRGRTKLVI CVTCTGGEIA FVEAGENHSV SVTGKFLDRI HDILGERRVR
LKADKSVPSP RPKFQNGERP SRGE
//
