ID H6RTU6_BLASD Unreviewed; 1178 AA.
AC H6RTU6;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=DNA polymerase III subunit alpha {ECO:0000256|ARBA:ARBA00019114};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE2 {ECO:0000313|EMBL:CCG03156.1};
GN OrderedLocusNames=BLASA_2250 {ECO:0000313|EMBL:CCG03156.1};
OS Blastococcus saxobsidens (strain DD2).
OC Bacteria; Actinomycetota; Actinomycetes; Geodermatophilales;
OC Geodermatophilaceae; Blastococcus.
OX NCBI_TaxID=1146883 {ECO:0000313|EMBL:CCG03156.1, ECO:0000313|Proteomes:UP000007517};
RN [1] {ECO:0000313|EMBL:CCG03156.1, ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|EMBL:CCG03156.1,
RC ECO:0000313|Proteomes:UP000007517};
RX PubMed=22535935; DOI=10.1128/JB.00320-12;
RA Chouaia B., Crotti E., Brusetti L., Daffonchio D., Essoussi I., Nouioui I.,
RA Sbissi I., Ghodhbane-Gtari F., Gtari M., Vacherie B., Barbe V., Medigue C.,
RA Gury J., Pujic P., Normand P.;
RT "Genome Sequence of Blastococcus saxobsidens DD2, a Stone-Inhabiting
RT Bacterium.";
RL J. Bacteriol. 194:2752-2753(2012).
RN [2] {ECO:0000313|Proteomes:UP000007517}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DD2 {ECO:0000313|Proteomes:UP000007517};
RA Genoscope.;
RT "Complete genome sequence of Blastococcus saxobsidens strain DD2.";
RL Submitted (FEB-2012) 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; FO117623; CCG03156.1; -; Genomic_DNA.
DR AlphaFoldDB; H6RTU6; -.
DR STRING; 1146883.BLASA_2250; -.
DR KEGG; bsd:BLASA_2250; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_11; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000007517; 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:CCG03156.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007517};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:CCG03156.1}.
FT DOMAIN 1..68
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1178 AA; 128855 MW; 9F4C507C0712049F CRC64;
MHLHVHTEYS MLDGAAKLPE VTAAAAEQGM PALAMTDHGN VFGAYDFYKK ATAAGVKPII
GMEGYYTPGS RFDRAPFDFG DKLLDEEGDG GSNRGKAAYT HMTLLARTTE GMHNLFRISS
LASLEGQYRK PRFDRDLLEK YGTGLIATTG CPSGEVNMWL RAGKEDKARQ AAADFQDIFG
KENFYAELMD HGLSIEKKTR PALLAIAKDL GIPLLATNDL HYTHKEDADA HDALLCIQTG
SRLNEPNRFK FNGNGYYLKS AAEMRALFTG DLAEACDNTL LVAEQCEVTF TEGADLMPRF
PLPPGEDETS WFVKEVERGL HKRYPGGIPD HVRKQADYEV GIISQMGFPG YFLVVADFIN
WAKDNGIRVG PGRGSAAGSL AAFAMGITDL DPLAHGLIFE RFLNPERVSM PDVDIDFDDR
RRGEVIQYVS QKYGEERVSQ IVTYGTIKAK AAIKDAARVL DRPYSVGDEL TKLMPPGVMG
KDIPLSGIFD PKHERYKEAA EFRARYESDP GAAEVVDQAR KLEGLKRQWG VHAAGVIIGR
YPLIDSIPIM RREADGAVIT QFDYPTCETL GLLKMDFLGL RNLTVIDDAL RNIVLNGKEP
IDLDELSKDL TDKATYELLG RGDTLGVFQF DGGPMRSLLR LMRPDNFEDI SAVGALYRPG
PMGANSHTNY ALRKNGQQEI TPIHPELAEP LAEILGQTYG LIVYQEQVMA IAQKVAGYSL
GKADLLRRAM GKKKKSVLDA EYVGFEAGMT ANGFSAAAVK TLWDILVPFA DYAFNKAHSA
AYGLVSYWTA YLKANYPAEY MAGLLTSVGD DKDRRPIYLA ECRRMGIKVL PPDVNESSWD
FTAVGTDIRF GLASVRNVGT NVVESIVRAR EEKGAFKDFA DFMRKIDTVA CNKKVIESLA
KAGAFDSLGH SRQGIVAVHA QAVESAMGLK RKEAEGQFDL FGSFGDEGGA EDPFAGALDL
TIPTADWSKS ERLMFERDML GLYVSDHPLH GVEHVLAANA DTPIVEINAG GVEDGANVTI
AGILTAVSPR TNKQGAPWAI ATVEDLESGI EVLFFPKTWA EVSEKVVRDQ IVVVKGRISR
RDDQPSLFGS EVVIPELTDG PRGPVLVSMA AARCTPPVVE RLREVLGSHP GTTEVQLKLV
NGSRETVLRL DQGLRVRPST ALMGDIKALL GPTSVALL
//
