ID   A0A127AYQ1_9BACT        Unreviewed;      1211 AA.
AC   A0A127AYQ1;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-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   ORFNames=TH61_02590 {ECO:0000313|EMBL:AMM50290.1};
OS   Rufibacter sp. DG15C.
OC   Bacteria; Bacteroidota; Cytophagia; Cytophagales; Hymenobacteraceae;
OC   Rufibacter.
OX   NCBI_TaxID=1379909 {ECO:0000313|EMBL:AMM50290.1, ECO:0000313|Proteomes:UP000070672};
RN   [1] {ECO:0000313|EMBL:AMM50290.1, ECO:0000313|Proteomes:UP000070672}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DG15C {ECO:0000313|EMBL:AMM50290.1,
RC   ECO:0000313|Proteomes:UP000070672};
RA   Kim M.K., Srinivasan S., Lee J.-J.;
RT   "Rufibacter sp. DG15C whole genome sequencing.";
RL   Submitted (JAN-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; CP010776; AMM50290.1; -; Genomic_DNA.
DR   RefSeq; WP_066505495.1; NZ_CP010776.1.
DR   AlphaFoldDB; A0A127AYQ1; -.
DR   STRING; 1379909.TH61_02590; -.
DR   KEGG; rud:TH61_02590; -.
DR   PATRIC; fig|1379909.4.peg.562; -.
DR   OrthoDB; 9803237at2; -.
DR   Proteomes; UP000070672; 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   Reference proteome {ECO:0000313|Proteomes:UP000070672};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          5..72
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1211 AA;  136975 MW;  62E31A9BF62478DB CRC64;
     MPDFSHLHTH TQYSLLDGAA SISGLMKKAQ ADGMKAVAMT DHGNMFGAFN FVAEANKYNV
     KPIVGCEFYL VNDRHQKTFT KEQKDVRHHQ LLLAKDQEGY QNLAKLCSYS YIDGLYSKWP
     RIDKELLVKY HKGLIATSCC IGAELPQAIL WKGEEEAEKL LKWWLDLFGD DYYIEIQRHG
     LMNIDNTGLS QEDVNQVLLK FAIKYNVKVI CTNDSHYVEQ TDWNAHDILL CVNTGEQESV
     PVGDFQTQYF RMMSGSGEVI YDTLTNIRNS YGHDENVRRM LYRIEEEQQK PRPQDRFGFP
     NDQFFFKSQA EMNQLFADVP FAVDNTNEIV DKITPPKLQR DILLPNFPLP PEHPTADLFL
     RHLTFEGAKK RYHEITAEVK ERLNYELGII ETMGFAGYFL ITQDFINKGR SMGVAVGPGR
     GSAAGSAVAY CVGITNIDPI KYALLFERFL NPERVSMPDI DIDFDDVNRQ RVIDYVVDKY
     GKTQVAQIIT FGTMAAKSSI KDVARAMDLP LSEANELAKM VPEVPGTTLA KAFIESPELA
     SIRDGNDLRA KVLKLAEKLE GSVRNTGIHA AGVIIAPDDI TNYIPVSTSK DSDLLVTQFD
     GKVIESAGML KMDFLGLKTL SILKDAMALI KRNHGVEIDI DNIPLDDEKT YALYQRGDTI
     GTFQFESEGM RMYLKDLKPT NIEDLIAMNA LYRPGPMQFI PNFINRKQGR EEVEYPHILL
     EPLLKNTYGI MVYQEQIMQT AQVLAGYSLG GADLLRRAMG KKDMKKMAQE REKFVAGAKE
     IHGIPAKQAS EVFDVMEKFA QYGFNRSHSA AYSVVAYQTG YLKAHYPAEY MAAVLTHNMN
     DIKKVTFFIE EARKQQIQVL GPDVNESIHQ FNVNQQGQIR FGMGAVKGTG EAAVEAIIEE
     REKTGPYTDV FDFAKRVNLR AVNKKTFESL AQAGAFDSFE RYHRAQYIET PPGETINLLE
     KAVRFGNQFQ AEKSAAQQSL FGGGGAVDMP LPKVPDVQPW SLTEMLRREK EVIGFYLSGH
     PLDQFKLEID SYCTCSLDRI EEFKGRDVNV AGIISNVVMR TGKNGNPFLL FSLEDYDNTM
     GLALFGEDFV KFSSYVKEGM YLFIRAKVTL RYKSEDQWEL KPLSMQLLSD VAEKMSKGVR
     MDIDIRNINA MLIDRLEEAA VNSPGQKKLE LVLTEPGERL AVELFSRKYR IDPKVFLQNV
     KDLEVATCQL I
//