ID I0HNX2_RUBGI Unreviewed; 1169 AA.
AC I0HNX2;
DT 13-JUN-2012, integrated into UniProtKB/TrEMBL.
DT 13-JUN-2012, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:BAL94709.1};
GN OrderedLocusNames=RGE_13680 {ECO:0000313|EMBL:BAL94709.1};
OS Rubrivivax gelatinosus (strain NBRC 100245 / IL144).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Sphaerotilaceae; Rubrivivax.
OX NCBI_TaxID=983917 {ECO:0000313|EMBL:BAL94709.1, ECO:0000313|Proteomes:UP000007883};
RN [1] {ECO:0000313|EMBL:BAL94709.1, ECO:0000313|Proteomes:UP000007883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100245 / IL144 {ECO:0000313|Proteomes:UP000007883};
RX PubMed=22689232; DOI=10.1128/JB.00511-12;
RA Nagashima S., Kamimura A., Shimizu T., Nakamura-isaki S., Aono E.,
RA Sakamoto K., Ichikawa N., Nakazawa H., Sekine M., Yamazaki S., Fujita N.,
RA Shimada K., Hanada S., Nagashima K.V.P.;
RT "Complete genome sequence of phototrophic betaproteobacterium Rubrivivax
RT gelatinosus IL144.";
RL J. Bacteriol. 194:3541-3542(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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AP012320; BAL94709.1; -; Genomic_DNA.
DR RefSeq; WP_014427578.1; NC_017075.1.
DR AlphaFoldDB; I0HNX2; -.
DR STRING; 983917.RGE_13680; -.
DR KEGG; rge:RGE_13680; -.
DR PATRIC; fig|983917.3.peg.1335; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_0_4; -.
DR Proteomes; UP000007883; 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 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 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; 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:BAL94709.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000007883};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:BAL94709.1}.
FT DOMAIN 4..71
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1169 AA; 128998 MW; 144FD03FF9A89C09 CRC64;
MPFVHLRTHT EYSVVDGTLR IDDAADAAKA DGQPALAITD LSNLFGAIKF YKACRGAGVK
PVVGVDVWMD PLPDAAERQP TRLALLVQDR GGYLNLCELL ARAWTQNVQR NQAWLKWEWL
RELSGGLIAM SGADMGAVGQ ALLAGDEERA AAAARELADI FPGRFYLELQ RAGLPTNEAQ
VRAAVPLAAR LGLPVVATHP IQFLGPDDFE AHEARVCIAE GETLANPKRI KRFTREQHFK
TAEQMQALFA DVPSAIANTV EIARRCSLTL VLGKPRLPDF PTPDGSPIEV YFRKASHEGL
EKRLAALFPK EEERDKRRPE YVERLEFELD TILKMGFPGY FLIVSDFIVW AKANGCPVGP
GRGSGAGSLV AYALFITDLD PLQYKLLFER FLNPERVSMP DFDIDFCQGN RDRVIRYVKE
KYGRDAVGQI ATFGTMAAKA ALRDVGRVLG MGYGHVDSIA KLIPAPPGKT VTLAKVPEKP
DPGIIYARQE EPEIDRREAA EEEVAELLSL ATRVEGMVRN IGMHAGGVLI APGKITDFCP
LYQQPGSDSA VSQYDKDDVE AIGLVKFDFL GLATLTILEL ARQYIVARRP NMKDFSYETL
PLDDQRVYKL FSDGLTEAVF QFESRGMQGM LREAKPSRLE DLIALNALYR PGPMDLIPTF
VARKHGKETV EYPHPLLETV LGETYGVMVY QEQVMQTAQV LGGYSLGGAD LLRRAMGKKK
AEEMAKHRAI FREGAAKKDI PEAKADEVFD LMEKFAGYGF NKSHAAAYSL LAYHTAWIKV
HCTAEFFAAN MTIEADNTDK LKVLLADAKL FGIRFDPPDV NTGTLRFEPI EDKRIRYGLG
AVKGTGAGAI EAIVAAREGR SGDGGGPFRS LFDFCARVDR QRVNKRVVEA LIKAGAFDSL
HADRAATLAS VGLAFEWADT QAANKDQGGL FDFGDAHGSS TQEPALVAVE PWSVRERLMQ
EKIAIGFYLS GHLFDACRDE VRKFVRRDIV ELVDSREPQS VAGIVSELRV INGQRGRVAI
FKLDDGSEAI EAVANEELLD ASRELLREDE LVIVVGKLQP DRFSGGLRLN AQQVWDLATA
RARFGRYLSV EVNGGLPPVA DVLKLWPARR VETEEGETQQ GLAVRLKLKR ATAVGELDLG
SDARFWPCDE ALARWKTIAE QGRASIVYE
//
