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Database: UniProt
Entry: M4RBJ8_9BIFI
LinkDB: M4RBJ8_9BIFI
Original site: M4RBJ8_9BIFI 
ID   M4RBJ8_9BIFI            Unreviewed;      1190 AA.
AC   M4RBJ8;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 53.
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:AGH40851.1};
GN   ORFNames=D805_0584 {ECO:0000313|EMBL:AGH40851.1};
OS   Bifidobacterium thermophilum RBL67.
OC   Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC   Bifidobacteriaceae; Bifidobacterium.
OX   NCBI_TaxID=1254439 {ECO:0000313|EMBL:AGH40851.1, ECO:0000313|Proteomes:UP000011835};
RN   [1] {ECO:0000313|EMBL:AGH40851.1, ECO:0000313|Proteomes:UP000011835}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RBL67 {ECO:0000313|EMBL:AGH40851.1,
RC   ECO:0000313|Proteomes:UP000011835};
RX   PubMed=23640377;
RA   Jans C., Lacroix C., Follador R., Stevens M.J.;
RT   "Complete Genome Sequence of the Probiotic Bifidobacterium thermophilum
RT   Strain RBL67.";
RL   Genome Announc. 1:E00191-13(2013).
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; CP004346; AGH40851.1; -; Genomic_DNA.
DR   RefSeq; WP_015450112.1; NC_020546.1.
DR   AlphaFoldDB; M4RBJ8; -.
DR   KEGG; btp:D805_0584; -.
DR   PATRIC; fig|1254439.12.peg.586; -.
DR   eggNOG; COG0587; Bacteria.
DR   HOGENOM; CLU_001600_0_0_11; -.
DR   Proteomes; UP000011835; 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; 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:AGH40851.1};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AGH40851.1}.
FT   DOMAIN          8..75
FT                   /note="Polymerase/histidinol phosphatase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00481"
SQ   SEQUENCE   1190 AA;  132855 MW;  31BF981DDA66F042 CRC64;
     MTDSGNFVQL HNHTHYSLLD GASKIPDLVK RVKELGMPAV GITDHGNMHG AYELWRNAVD
     QGIKPIIGIE AYVTPETARQ DKTRVSWDTN WVPQPHHERN PDDVSGGGLI THLTLWAEND
     EGLVNLIKAS SVANLEGRVM RYPRMDKEVL QRYHKGVICS SGCPSGIIQT RLRLGQFDEA
     LRAAGEMQDI FGKDNFYIEL MDHGLEIERR VTKDLLTIAK KLNAPLLATN DSHYVHEEDR
     DAQDAMLCIN SGSRLDDPDR FKFDGSGYYI KSAQEMRDLF KELPEACDNT LAIADRCNVI
     FDDHEDGAFM PRFDCPEGWD ETSLFLKHVD EGLKRRYNGN PPIEVLKQAD YECGVICQMQ
     FCGYFLVVAD YINWAKSHGV MVGPGRGSAA GSMVAYAMGI TELDPLKHGL IFERFLNPER
     VSLPDIDVDF DPDGRMKVLD YVANKYGHDK VAQCVIYGTI KTKQALKDSA RIMGYEFSVG
     ERITKALPPS KNGKDASLHD IFDPTSKRYA EAREFRELYD ADPDAKRITE EAKGIEGLIR
     QTGVHACATI MGSEAITNTS PLLERTDGTI TTTFEYHTCE TLGLVKMDFL GLSNLTVIRD
     TLTNIRNNGK EPIDYTKIPL DDKPTYELLA RGDTLGVFQL DSDGMRSLLK TLKPDNFNDI
     SALIALYRPG PMDMDSHNNY AKRKNGLQKI TPIHPEVAEP LKEVLGETYG LIVYQEQVQS
     AARILAGYSL GKADVLRRAM GKKKPEVLAK EKVPFFQGMK EHGYSMEAAQ AVWDILVPFS
     GYAFNKAHSA AYGLISYWTA YLKTHYPVEF MAALLQNERT NKDKTALYLG EARRMGIKVL
     PPDVNESRLE YSAVGDVVRF GLGAIRNVGD KAVEDIIAER ETARGKYVNF MDFIRRVPVT
     ALNRRLVESL IKAGAFDSID PNRRALYEIH ETAIDSVIGL KRKQAEGQFD LFADDDDGGA
     DMMGDASVVV PDIEEWDKKT KLNFEREMLG LYVSDHPLSG MTAILANLRE MSIAHLIDRA
     KTMGDSQQVT IAGLVTNVDR RVSKKGNPWA IVTVEDMESS IQCMFFGKVY ENAAAQLAID
     EVVQVRGQVE VRDETVSLRA TEMQVPSLEA DDSRPVVITL PPVALDRDHA MQLGRVLMNH
     PGYCPVKLAI MGEKGDAQVL TFGDRFRVKR DTSLFAEIKI LFGPSCLPAA
//
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