ID   A0A3D8N2T1_9DELT        Unreviewed;      1188 AA.
AC   A0A3D8N2T1;
DT   16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT   16-JAN-2019, sequence version 1.
DT   24-JAN-2024, 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=DV096_05690 {ECO:0000313|EMBL:RDV40049.1};
OS   Bradymonadaceae bacterium TMQ3.
OC   Bacteria; Deltaproteobacteria; Bradymonadales; Bradymonadaceae.
OX   NCBI_TaxID=2283320 {ECO:0000313|EMBL:RDV40049.1, ECO:0000313|Proteomes:UP000256871};
RN   [1] {ECO:0000313|EMBL:RDV40049.1, ECO:0000313|Proteomes:UP000256871}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TMQ3 {ECO:0000313|EMBL:RDV40049.1,
RC   ECO:0000313|Proteomes:UP000256871};
RA   Wang S.;
RT   "Lujinxingia celare sp. nov., isolated from a marine island.";
RL   Submitted (AUG-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}.
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:RDV40049.1}.
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DR   EMBL; QRGZ01000001; RDV40049.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3D8N2T1; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000256871; 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   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; 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   ECO:0000313|EMBL:RDV40049.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:RDV40049.1}.
FT   DOMAIN          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1188 AA;  132969 MW;  351C85669AA69D33 CRC64;
     MSDFVHLHVH TQYSLLDGAI RIPKLMSRVA EQGMSAVAMT DHGNMYGAVD FQKAAKKAGV
     KSIIGVEMYM TSHPYEESKE PKSYHLTLLA QNLTGYQNLM YLNSMGWLHG QHPRTGLPRI
     DFELLAERNE GIICLSGDLG GEVNQHILRG DMDAAREAAA RYREVFGKER YYLEVMDNAL
     PEQRKCTQAM VEIGRELDIE LVATNDCHYL DREDARAHAV LMCIQLGKTV DIDRIMEHGV
     DQLYVRSAEE MYEAFADIPR ACENTVRIAE MCDLEIPLGE VFLPQYDVPQ SFRDEHEGAD
     SKTIIHEYFR HVARQGLGER YAEFDALGVS YDRQEYDERL EVEIGIICQM DFPGYFLIVW
     DFIAWSHEHD IPVGPGRGSG AGSLVAYAMR ITDIDPMPYD LLFERFLNPE RVSMPDFDID
     FCMNRRGEVI DYVTEKYGYH NVGQIVTYGQ LKARAAIKDV GRALNFSYGE TDRLAKLVPD
     VLGISLQESL DQEKRLRDMC EEDERVDTLF DIALSLENLN RQAGMHAAGI VISETPLWDF
     VPICRGANGE LVTQYAKNEV EEAGLVKFDF LGLKTLTVLQ DAIKLINQQR EARGEERFDL
     NAIPLDDPEV FRLISAGNTT GVFQLESSGF QELLKKLKPN CFEDIIAAVA LYRPGPLGSG
     MVDDFIDRKH GRKQVEYPHA WLEDVLKPTY GVMVYQEQVM KTAQVMAGYS LGGADLLRRA
     MGKKKPEVMA QQKEIFVAGA LEKEVDEQKA SDIFDLMAYF AGYGFNKSHS AAYGLITYQT
     AYLKTHFQVE FMAALMTSDR DNTDKIVRFI NEAKGLGIEV MPPDVNESLL DFSVVDQKIR
     FGLAAIKGVG AGVIEVILDE RAANGPFENL YDFCSRVDLK KINKRTIEAL VKCGAFDSIG
     PAITEQYIGE ICATRASIFA AIDTAVERGQ KAQHDKAVGQ SSLFGMMAQD VREEVLDDSY
     PECLAWNDRE LLENEKTLLG FYVTGHPLDR FESEFGLYGA STTHELMTNG SLRNRANVAV
     AGVVSAMREV PLKSGDGRMG FITIEDKTGE IEAIAFSSAY AEAEEVIKSG EPLLIKGQIQ
     EEGDPENRTR RIRLESASTL ESERESKVRQ VIVEIGVAQV TNGQLKELQK VLAANSGHCR
     TTLVFKKQTA QGVGEAQVVL PVDFATRPTD GLLMAIERLF GRKSVRLS
//