ID   A0A1D9MKJ9_9ACTO        Unreviewed;      1194 AA.
AC   A0A1D9MKJ9;
DT   15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT   15-FEB-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=BK816_05615 {ECO:0000313|EMBL:AOZ72837.1};
OS   Boudabousia tangfeifanii.
OC   Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC   Boudabousia.
OX   NCBI_TaxID=1912795 {ECO:0000313|EMBL:AOZ72837.1, ECO:0000313|Proteomes:UP000176288};
RN   [1] {ECO:0000313|EMBL:AOZ72837.1, ECO:0000313|Proteomes:UP000176288}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=VUL4_3 {ECO:0000313|EMBL:AOZ72837.1,
RC   ECO:0000313|Proteomes:UP000176288};
RA   Wang Y.;
RT   "Actinomyces aegypiusis sp. nov., isolated from the Aegypius monachus in
RT   Qinghai Tibet Plateau China.";
RL   Submitted (OCT-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; CP017812; AOZ72837.1; -; Genomic_DNA.
DR   RefSeq; WP_071164302.1; NZ_CP017812.1.
DR   AlphaFoldDB; A0A1D9MKJ9; -.
DR   STRING; 1912795.BK816_05615; -.
DR   KEGG; avu:BK816_05615; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000176288; 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; 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; 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   Reference proteome {ECO:0000313|Proteomes:UP000176288};
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   1194 AA;  133590 MW;  ED17E440F2099DD9 CRC64;
     MATSDFVHLH CHTDFSMLDG AARIKPMVQR AKDIGQKAVA ITDHGYLFGA FEFYQACKDV
     GIKPIVGLEA YVTPGTSRHD RTRHTWGTTA QQEAGDDVSA RGSYTHMTLL ARTTAGMHNL
     FRLGSRASLE GQWGKWPRAD RQLIETYADG LIGTTGCPSG AVQTRLRLGQ IEEAYREAGE
     LQDIFGKDYF FVELMDHGLE IERRVQNELL ELSRKLGAPL LATNDSHYVN SDERDVQDAM
     LCISTGSRLS DPDRFRFDGS DYYIRTAEEM RETFRDLPEA CDNTLLVADM CEIEFKTVKE
     GANFMPRFPL PPGEDEHSWF VAEVERGLNY RFPNGIPDEV RKQAEYEVGI ITQMGFPGYF
     LVVADYIQWA KDQGIRVGPG RGSGAGSMVA YAMRITDLNP LEHGLLFERF LNPERVSMPD
     FDVDFDERRR GEVIDYVTKK YGADKVAQVV TYGKIKTKQA LKDSARVLGY EYQMGERLTK
     AMPPSVMGKD ITVKGIFDPT DKRYAEAEEF RKLHAQDPDA QQVVELAKGL EGLTRQWGVH
     ACAVIMSSET LTDIIPMMMR PQDEAVITQF EYPACETLGL LKMDFLGLRN LTVISDALQN
     IIDNGKDPVD LEHLTLDDKA TYELLSTGET LGVFQMDGGG MRDLLRLMRP DNFEDISAVG
     ALYRPGPMGA DSHTNYALRK NGVQQIEAIH PALAEPLKDI LGETYGLIVY QEQVMAIAQK
     LAGYSLGQAD LLRRAMGKKK KEILDKEYVP FHDGMIERGY PEDAIKTLWD ILVPFSNYAF
     NKAHSAAYGV VSYWTAFLKA NYPVEYMAAL LTSQKDNKDK LSVYLAECRR MQIKVLPPDV
     NESVGVFRAV GDDIRFGMAA IRNVGQHVVE GIIEAREEQG AFTSFQDFLS KVPLQVCSKR
     TIDSLIKSGA FDSISDSRRA LVACHEEAVD SVTSQKRNEA VGQFDLFADF GAEEEVGFTF
     TVPNLPEWER MVKLQFEREM LGLYVSDHPL NGMERRLSRE QDIQIANVKA EDGPAHQETV
     KIAGLITDVT RRTSRNGMLW ATVTLEDLTG AMEVTFFPRQ YETFNPFLKQ DTVVSVTGQV
     SREEGRLTLK VSSLTTIEGT DSDERPLTLE LRSTDCTRDK MEQLLGVLQN HPGAAPVRLK
     IRDGLKVTTL ELDQTTVDVS EALISDLKVL LGTRAIPQSA SATPPPARPP FRGR
//