ID A0A069II51_9BURK Unreviewed; 1170 AA.
AC A0A069II51;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 46.
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:KDP89203.1};
GN ORFNames=CF70_008620 {ECO:0000313|EMBL:KDP89203.1};
OS Cupriavidus sp. SK-3.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=1470558 {ECO:0000313|EMBL:KDP89203.1, ECO:0000313|Proteomes:UP000023560};
RN [1] {ECO:0000313|EMBL:KDP89203.1, ECO:0000313|Proteomes:UP000023560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK-3 {ECO:0000313|EMBL:KDP89203.1,
RC ECO:0000313|Proteomes:UP000023560};
RA Vilo C., Benedik M.J., Ilori M., Dong Q.;
RT "Cupriavidus sp. strain SK-3.";
RL Submitted (MAY-2014) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDP89203.1}.
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DR EMBL; JFJV02000018; KDP89203.1; -; Genomic_DNA.
DR RefSeq; WP_035859397.1; NZ_JFJV02000018.1.
DR AlphaFoldDB; A0A069II51; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000023560; Unassembled WGS sequence.
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; 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; 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 Aminoacyl-tRNA synthetase {ECO:0000256|ARBA:ARBA00023146};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW DNA replication {ECO:0000256|ARBA:ARBA00022705};
KW DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00022932};
KW Ligase {ECO:0000256|ARBA:ARBA00023146};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022840};
KW Nucleotidyltransferase {ECO:0000256|ARBA:ARBA00022695,
KW ECO:0000313|EMBL:KDP89203.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDP89203.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1170 AA; 129199 MW; 4B7376AEC8CA11B8 CRC64;
MSAPRFVHLR LHSEYSVVDG IVRLEDAVEA AAADGMGALA LTDLANAFGL IRFYKEARGG
GVKPVVGADV WLTNADDRDK PTRLLLLVQD RRGYLNLCVL LSRAWLSNQY RGRAEIDPAW
FDEAGEEGLP LATGMIALSG AMGGDIGVAL ANGNEAVAAQ AAAHWAKVFP QRFYIELQRA
GQPGTDAYVQ QAVQLASKMR LPVVATHPVQ FMTADDFTAH EARTCIAEGE LLANPRRTRR
FTTDQYFKSQ DEMCALFADI PSALENAVQI ARRCNLTLEL GKPRLPLFPT PDGMSLDDYL
VHLAKEGLEK RMAVLFPDEA VREAKRPEYY ARLEFETGTI IKMGFPGYFL IVADFINWAK
NNGVPVGPGR GSGAGSLVAY ALGITDLDPL KYALLFERFL NPERVSMPDF DIDFCQHGRD
RVITYVKEKY GHAAVSQIAT FGTMAAKAAV RDVGRVLDLG YGFVDGIAKL IPFKPGKLVT
IEEAKKEEPL LTEREKNEEE VRQLLELAQR VEGMTRNVGM HAGGVLIAPG KLTDFCPLYT
QGAQNDGMSG VVSQYDKDDV EAAGLVKFDF LGLTTLTILD WAERYIRRLD PTRADWNCSH
IPLDDGPAFD ILKTANTVAV FQLESRGMQG MLKDAKPDRF EDIIALVALY RPGPMDLIPS
FCARKHGREK VEYPDPRVEP VLKETYGIMV YQEQVMQMAQ IIGGYSLGGA DLLRRAMGKK
KAEEMAQHRE LFRAGAAKNG LTAEKADDTF DLMEKFAGYG FNKSHAAAYA LLAYYTAWLK
AHHPAEFMAA NMSLAMDDTD KVKILHEDCK LNHLKVLPPD VNASEYRFAP TDARTIRYGL
GGIKGSGQGA IEDILRAREE KPFTDLFDFC ERVDRRQVNR RTIEALIRAG AFDSLNDNRG
QLLASVSLAM EAAEQKAESA NQVSLFDLMA DAGESHRPEL VDEPRWPPKR TLQEEKQALG
YYFSGHLFDA YRDEVGRFLK GTLAGLEKEV QGNGGGYGRD VRGKVIAGVI TGMRTQMTQR
GKMLIVLLDD GTGQVEMTVF NELFDANRHM FREDEMVIVQ GNARHDTFTG GVRFTAESVM
DLVAARAKYA EAVGLAFNGN ASTELLRELL TPYLATVANS PGLPVRISYA TTGARCEAEL
GRQWLVTPSE DALASFRSAL SGENVRMLYG
//
