ID   A0A0P0M9B7_9BURK        Unreviewed;      1175 AA.
AC   A0A0P0M9B7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 30.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   Name=dnaE {ECO:0000313|EMBL:ALK88781.1};
GN   ORFNames=L63ED372_01574 {ECO:0000313|EMBL:ALK88781.1};
OS   Limnohabitans sp. 63ED37-2.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Limnohabitans.
OX   NCBI_TaxID=1678128 {ECO:0000313|EMBL:ALK88781.1, ECO:0000313|Proteomes:UP000059510};
RN   [1] {ECO:0000313|EMBL:ALK88781.1, ECO:0000313|Proteomes:UP000059510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=63ED37-2 {ECO:0000313|EMBL:ALK88781.1,
RC   ECO:0000313|Proteomes:UP000059510};
RA   Ahn J.-H., Kim S.B.;
RT   "Limnohabitans sp. 2 strains.";
RL   Submitted (JUN-2015) 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; CP011774; ALK88781.1; -; Genomic_DNA.
DR   RefSeq; WP_062405057.1; NZ_CP011774.1.
DR   AlphaFoldDB; A0A0P0M9B7; -.
DR   STRING; 1678128.L63ED372_01574; -.
DR   KEGG; lih:L63ED372_01574; -.
DR   PATRIC; fig|1678128.3.peg.1562; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000059510; 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   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; 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; 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   ECO:0000313|EMBL:ALK88781.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000059510};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:ALK88781.1}.
FT   DOMAIN          3..70
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1175 AA;  130035 MW;  CE81BEEE1A8B7296 CRC64;
     MFVHLRLHTE FSVVDATCRI DDVVKIAAKD AQPALAITDL SNLFGTVKFY KEGRGKGVKP
     IIGAEIHLEG LGGDVGVTSR VVLLVQNHTG YLNLCELLAR AWTQNIVKGV AVVKLAWLKE
     LSDGLILLSG AQAGPVGQAI VQGDTDKAAD VALQLGSIFP HRFYLELQRA GRPEDEPQVA
     GAVALAARLG LPVVATHPVQ FHSPEDYEAH EARVCVSEGE ILANPRRVRR FTREQYFKSA
     AQMSALFADV PSAIANTLEI AKRCNLTLVL GKPQLPNFPI PPVAGVVMSV DEYFRHVSHE
     GLKERLVHLY PDAAKREAER QRYVDRLEFE LNTILKMGFP GYFLIVGDFI QWAKNNGCPV
     GPGRGSGAGS LVAYALKITD LDPLQYNLLF ERFLNPERVS MPDFDIDFCQ TNRDRVIEYV
     KQKYGREAVS QIVTFGTMAA RAAIRDVGRV LDMSYTFCDG ISKLIPNKPG MSVTLQYPPA
     TPKEGDKNNY AIAMEPILAE RIEREEDVKT LIELAQKLEG MTRNVGMHAG GVLIAPGKLT
     DFCPLYQQPG SESAVSQYDK DDVEAAGLVK FDFLGLATLT ILEIAREFII KRHKGQENFA
     FENIPLDDAP TYKLFSDGKT EAVFQFESRG MQGMLRDARP SRLEDLIALN ALYRPGPMDL
     IPSFVARKHG REPVEYPHPA VAQMLSETYG IMVYQEQVMQ TAQILGGYSL GGADLLRRAM
     GKKKAEEMAE HREKFRAGAL ATHNIPQDKA DEVFDLMEKF AGYGFNKSHA AAYSLLAYHT
     GWLKVHYTAE FFCANMTVEM DDTDKLKVLH EDALKFGIRF DPPDVNRGTH RFEPVTDKII
     RYGLGAIKGT GQQAIDAIVA AREQGGPFTS LFDFAVRVDR TRINKRTVDA LIKAGAFDSL
     HMNRAALSAS IDRAFEFSAA TTANVNQGGL FDMLGDDSHG SSTQEPELVE VMPWGIKERL
     LLEKTAVGFF LSGHLFDAVE REVRQFARRK IDDLIDSRES MVLAGIVSDL RIINGQRGKV
     AIFKLDDKSG MLEATADEAL INSAKHLLKD DELIIVTAKM QADRFSGGFR LKIEQIMDLA
     AARCRFGKYL RVAVNGRAPD IARIVKEFPA QREQTEHGDL VRGLPVRLVL ERSKDQLAAR
     AELALGDTAK FFPTDAALAS WMAQADQGLA QIVYD
//