ID K0CF40_ALCDB Unreviewed; 1167 AA.
AC K0CF40;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-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=dnaE {ECO:0000313|EMBL:AFT70211.1};
GN OrderedLocusNames=B5T_01936 {ECO:0000313|EMBL:AFT70211.1};
OS Alcanivorax dieselolei (strain DSM 16502 / CGMCC 1.3690 / MCCC 1A00001 /
OS B-5) (Alloalcanivorax dieselolei).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alloalcanivorax.
OX NCBI_TaxID=930169 {ECO:0000313|EMBL:AFT70211.1, ECO:0000313|Proteomes:UP000006286};
RN [1] {ECO:0000313|EMBL:AFT70211.1, ECO:0000313|Proteomes:UP000006286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16502 / CGMCC 1.3690 / B-5
RC {ECO:0000313|Proteomes:UP000006286};
RX PubMed=23144414; DOI=10.1128/JB.01813-12;
RA Lai Q., Li W., Shao Z.;
RT "Complete genome sequence of Alcanivorax dieselolei type strain B5.";
RL J. Bacteriol. 194:6674-6674(2012).
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; CP003466; AFT70211.1; -; Genomic_DNA.
DR RefSeq; WP_014994283.1; NC_018691.1.
DR AlphaFoldDB; K0CF40; -.
DR STRING; 930169.B5T_01936; -.
DR KEGG; adi:B5T_01936; -.
DR PATRIC; fig|930169.3.peg.1917; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000006286; 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; cd07433; PHP_PolIIIA_DnaE1; 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; IPR048472; DNA_pol_IIIA_C.
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 InterPro; IPR049821; PolIIIA_DnaE1_PHP.
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; PF20914; DNA_pol_IIIA_C; 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:UP000006286};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1167 AA; 131269 MW; 2BF56C2BCADEBCD3 CRC64;
MSEPRFVHLR LHTDYSLVDG VVRVKELIKT CTAQGMPAVA VTDENNLFAL IKFYSNAQNA
GIKPVMGADL WVQADDPEDE PSYITCLVQN EQGYRNLTLL ISRAWQTNQV RERALIRREW
LLELNEGLIV LSGARFGDVG KWLLAEKTDL ARERATEYKT VFGDRYYLEV QRTQRPGDED
CLHASVALAA ELDIPVVASN DVRFLKREDF EAHEARVCIH DGNTLDDPRR PRKYSEEQYL
KSAEEMAELF SDLPEALQNS VEIARRCTLD IRLGKNFLPD FPVPEGMTIE QYFEKVSRDG
LEERLVKILD PQAPDYAERR KIYDDRLKFE LDIINQMGFP GYFLIVADFI QWGKEHQVPV
GPGRGSGAGS LVAYALKITD LDPIAYDLLF ERFLNPERVS MPDFDVDFCM EKRDRVINYV
ADKYGRDAVS QIITFGTMAA KAVVRDVARV QGKPYGMADR LSKMIPGTPG MTLSKALEQE
ETLRDFLEDD GNPDKEAVNE IMEMAFKLEG LTRNVGKHAG GVVIAPGKLT DFAPLHCDEH
GENLVTQYDK DDVEQAGLVK FDFLGLKTLT IIDWAMKAVN VRRQREGDGP LEIERIPLDD
SPSFDLLKRG DTTAVFQLES QGMKELIKKL KPDVFEDIIA LVALYRPGPL ESGMVDNFIN
RKHGREPLAY PDPQYQHEWL ESILKPTYGV ILYQEQVMQI AQVLAGYTLG GADMLRRAMG
KKKPEEMAKQ REIFESGAKE KGVDPDLAMK IFDLVEKFAG YGFNKSHSAA YALVAYQTAW
LKAHYPAEFM AAVISADMQN TDKVVTFIDE CHSMGLKVLP PDVNSCGYRF TVNPEGDIIY
GLGAIKGLGE GPIEAIVSAR GDTDGFDDLF DFCRRIDLKK INRRSLEALV RAGALDKLGP
NRHFRDRATL LATLPDAIAA AEQDARNEEA GMTDLFGSMQ TAETPVVEWK PAREWNDELR
LNGERDTLGL FLTGHPIDQF EHEVRQFVSA RFNALQPTAK GEAATVAGLV VALRITRSKR
SGERMAFVTL DDKTGRLEVS VFGKTFAQFG ERIQKDILLV VRGGVRNDDY SGGFNLVADE
VMDMRQAREV FARRLCVSVP VEQQLPDTLD RLFAPYRGGA IPVTLRLAHK EADVAMPLGD
EWKISPHEAL VDELRNRFGE TSVQLEY
//
