ID A0A1G2ER62_9BACT Unreviewed; 1053 AA.
AC A0A1G2ER62;
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=A2365_03915 {ECO:0000313|EMBL:OGZ27841.1};
OS Candidatus Nealsonbacteria bacterium RIFOXYB1_FULL_40_15.
OC Bacteria; Candidatus Nealsonbacteria.
OX NCBI_TaxID=1801677 {ECO:0000313|EMBL:OGZ27841.1, ECO:0000313|Proteomes:UP000177740};
RN [1] {ECO:0000313|EMBL:OGZ27841.1, ECO:0000313|Proteomes:UP000177740}
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:OGZ27841.1}.
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; MHMM01000004; OGZ27841.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G2ER62; -.
DR STRING; 1801677.A2365_03915; -.
DR Proteomes; UP000177740; 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 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1053 AA; 119468 MW; 97FD07CCB3269468 CRC64;
MKFTHLHVHS HYSLLDGLPK IDLLLERVKE LGMDSVAITD HGVMYGAIEF YQKAKKAGIK
PIIGCEVYMA QERMHQKRPK IDDKKYHLIL LAKNETGYKN LVKLVTKAHL EGFYYKPRID
DELLAKHSEG LIAMTACIAG RIPRLIASKK FDEAEKLALR YQEIFGPGNF YLEIQHHPNL
QDQKPVNEGL IAISKKYGIP LVATNDAHYL RLEDAEAQDI LMLINTGAKP DDPERATIKS
DDFSLKSSEE MADLFKETPE AIENTQKIKE MCNLELELGK TLLPHYEVPE AKEPDIYLKD
LCFKNLEKRY GSKPGKEVAE RLEYELSVIK QTGFASYFLI VQDFVNWAKS QRIVVGPGRG
SAAGSIVAYL TNITNVDPLK NNLLFERFLN PERISMPDID LDFTDRRRDE VINYVAEKYG
KDHVAQIITF GTMASRAVIR DVGRALGYEY SYCDKTAKMI PFGFSLKDAL EKVDEFREFY
EADEKATRLI DLGLKLEGVV RHASTHACGV VISAKPLTDL TPLQRPTQDD NSIVTQFEMH
SIESLGLLKM DFLGLKNLTI IEDTLARIYV LRNGLKIDID NIPPDDAKSF KLFQKAQTTS
VFQLESDGMK KYLKELKPTE FEDIVAMVAL YRPGPMQFIP EYIARKHKKK EIEYLHQKLK
PILEKTQGIC IYQEQLMQIA RDLAGFTLGE ADVLRKAIGK KIPELLKEQE KKFIQGMINN
GIDGKIAIKL WEWVLPFAQY GFNKSHSAAY ATIAYQTAYL KANFPVEFMA SVLTSEKGDI
ERVAFLIDEC RQMGIEVLAP SINESLRNFT VVEEGKKIRF GLIAIKNVGE NIVDVIVEER
KNGKFSSIAD FLQRVQSKDL NKKSMEALIK SGAFDEFEER NKLLQNLERL LEWSKESQKN
KAMGQKGLFE SSGFAVSVSL EEAPALSNLE RLRWEKELLG LYVSSHPLED FKEAMKGTTA
LKELKNCFMK QRVKVGGVIS SVKKIITKTG KPMLFVKLED VSEKAEVVVF PSTLEKYPQA
FEENKIVFIS GTVDHRDNSP KVIADSAEEI IVS
//
