ID A0A1P8FNX9_9PROT Unreviewed; 1139 AA.
AC A0A1P8FNX9;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN ORFNames=BWI17_20000 {ECO:0000313|EMBL:APV51765.1};
OS Betaproteobacteria bacterium GR16-43.
OC Bacteria; Pseudomonadota; Betaproteobacteria.
OX NCBI_TaxID=1904640 {ECO:0000313|EMBL:APV51765.1, ECO:0000313|Proteomes:UP000185830};
RN [1] {ECO:0000313|EMBL:APV51765.1, ECO:0000313|Proteomes:UP000185830}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GR16-43 {ECO:0000313|EMBL:APV51765.1,
RC ECO:0000313|Proteomes:UP000185830};
RA Choi A.;
RT "Complete genome sequence of betaproteobacterium GR16-43, isolated from a
RT freshwater pond in South Korea.";
RL Submitted (DEC-2016) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP019169; APV51765.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1P8FNX9; -.
DR STRING; 1904640.BWI17_20000; -.
DR KEGG; beba:BWI17_20000; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000185830; Chromosome.
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; cd07433; PHP_PolIIIA_DnaE1; 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 InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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; SSF50249; Nucleic acid-binding proteins; 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 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1139 AA; 125241 MW; 6FBBB76A8302514D CRC64;
MAAPRFVHLR LHSEYSIIDG MARVDDAVDA AAADGMPALA ITDLANLFGA IKFFQAARGV
GVQPIVGCDL WLSNERSRDH PYRLAVLCRN REGYLALCAL LTRAHVENHW RGRAEVKREW
LRGLPGLVVL SGARLGDVGQ ALGAGNLVQA EALARAWEAD FPGAFYLELQ RADPDRDEPY
VRAAVALAGR LDLPVVATHP IQFVKREDYR AHEARVCIAQ GYVLGDQRRP REFRPSQYFK
TQDEMAEIFS DLPEALANSV EIARRCTFEF ELGKSRLPDF PTPNGETIED YLRKTSHDGL
ELRLAELYPE PAARDEARPR YAERLEFELK TIIQMGFAGY FLIVADFINW AQNHGVPVGP
GRGSGAGSLV AYVQGITGLD PLRYELLFER FLNPERVSMP DFDIDFCQDG RDRVIDYVKQ
KYGAECVSQI ATFGTMAAKA VVRDVGRVLG MPYGEVDRIA KLVPFELGIT LTRALEVEPQ
LKALAKEQEG VGELMELALA LEGLSRNVGM HAGGVLIAPG KLTDFTPLYS AEGSTALVSQ
FDKDDVEKAG LVKFDFLGLT TLTIIAEAER NIRALGHADF DIEKIPLDDP AAYKVFSSGN
TVSIFQFESR GMRDLIMKAR PDRLEDLIAL NALYRPGPMD LIPEFIDRKH GRQRWEYLDP
RLKEILEPTY GVMTYQEHVM TIAQVIGGYT LGGADLLRRA MGKKKPEEMA KQRAIFMKGA
TGGGLAEAKA NILFDQMEKF AGYGFNKSHS AAYALVAYQT AYLKSHHAAA FMAANLSAVM
DDTDKVQSFY DDAVKNGLKI AAPDVNTGGH RFAALDEKNI RFGLGAVKGT GAGAIENIVA
ARASGGAFRD LADFCRRVDR RVVNRRAMEA LIRAGAFDAV EPNRASLAAS LGAAIEVAEK
GEQYANQTSL FGGGDEASPE AFTLVPMPPW GERERLLNEK QSLGFYLSGH PFNAYRAELR
RVAATPLAKV APTNYGETVM LAGVIYGVQM RNTRRGRMAI LTLDDGTAKV EVVVFGELFN
EKRSVIQEDA VVALAGKVQN DEFSGGLRVT AEKLMDLAEV RSAHAKVLRL SINGQADAAK
LKQVLAPYAG GACAIAIRYR NAQGECDIRL PDAYRVKVSE PLLASLSEWL REENVEVVY
//
