ID   A0A3G6ZMF9_9MICO        Unreviewed;      1170 AA.
AC   A0A3G6ZMF9;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 18.
DE   RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE            EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN   ORFNames=DT073_08650 {ECO:0000313|EMBL:AZC13772.1};
OS   Microbacterium sp. ABRD28.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Microbacterium.
OX   NCBI_TaxID=2268461 {ECO:0000313|EMBL:AZC13772.1, ECO:0000313|Proteomes:UP000280903};
RN   [1] {ECO:0000313|EMBL:AZC13772.1, ECO:0000313|Proteomes:UP000280903}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ABRD_28 {ECO:0000313|EMBL:AZC13772.1};
RA   Jin H.M.;
RT   "Genome sequence of Microbacterium sp. ABRD28.";
RL   Submitted (JUL-2018) 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; CP031015; AZC13772.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3G6ZMF9; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000280903; 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   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   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:AZC13772.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000280903};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AZC13772.1}.
FT   DOMAIN          7..74
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
FT   REGION          78..99
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1170 AA;  129544 MW;  B078C8B11769BE67 CRC64;
     MASDSFVHLH VHSEYSMLDG AAKIGAMTQA AADYGMPAIA VTDHGNTFAA FEFYNAAKAA
     GIKPIIGLEA YVTPGTHRSD KSRVQWGTPE QRSDDVSGSG AYTHMTMWSQ STEGMHNLFR
     LSSLSSMEGY YFKPRMDREL LETYGKGLIA TTGCPSGEVQ TRLRLGQYDA ARAAAAEFQD
     IFGRENYFAE IMDHGLSIER RVMTDLIRIS KDLGIPLVAT NDSHYTHQHE ADAHAALLCV
     QSGSTLDDPN RFKFDGDGYY VKTAQEMRQI FREHPEACDN TLLIAERCEV EFNTSANYMP
     RFPVPDGETE DSWLVKEVEK GLHYRYPNGI PDNVRKQAEY ETGIILQMGF PGYFLVVADF
     INWAKDNGIR VGPGRGSGAG SMVAYAMRIT DLDPLEHGLI FERFLNPDRV SMPDFDVDFD
     DRRRGEVIDY VTEKYGSERV AQIVTYGTIK SKQALKDAGR VLGFPFSMGE RLTKAMPPAV
     MGKDMPLSGM YDAQHPRFKE ASEFRALIDT DPEAKTVFDR ALGLEGLKRQ WGVHAAGVIM
     SSEPLLDIIP IMRREQDGQI VTQFDYPSCE ALGLIKMDFL GLRNLTIISD ALDNIRMNRG
     EELDLEHLAL DDTAAYELLT RGDTLGVFQL DGGPMRSLLR LLKPDNFEDV SAVIALYRPG
     PMGANSHINY ALRKNGQQEV TPIHPELEEP LKDILDISYG LIIYQEQVMA IAQKVAGFSL
     GQADILRRAM GKKKKSELDK QYEGFSGGMK ERGYGESAIK ALWDILLPFS DYAFNKAHSA
     AYGLVSYWTA YLKAHYPAEY MAALLTSVGD SKDKMAVYLN ECRRMGIKVL PPDVGESIRY
     FAAVGEDIRF GLGAVRNVGA NVVDAIVAAR QEARFTSFHD FLSKVPVPVA NKRTVESLIK
     AGAFDSLGAT RRALMEIHED ATEQAVLDKR REANGEVGFD FDSLWDEPQQ VQKVPDRPEW
     TKKDKLAFER EMLGLYVSDH PLAGLEIPLA KHASLSIHDL LASEDIADGE QVTVAGLVTS
     VQHRVAKSSG NPYGMITVED FDGEVTVMFM GKTYTEFQSM LQADSILVVR GRVSRRDDGM
     NLHAVSAFVP DLGAVDAAGP LVLLVPEHRA TETVVTELAQ VLTRHRGDTE VTLRLHKGGV
     AKVFEVPLPV TVTADLYGEL KGLLGPQCLG
//