ID A0A0W7YXB2_9BURK Unreviewed; 1181 AA.
AC A0A0W7YXB2;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
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:KUF39572.1};
GN ORFNames=AS359_05760 {ECO:0000313|EMBL:KUF39572.1};
OS Comamonas kerstersii.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Comamonas.
OX NCBI_TaxID=225992 {ECO:0000313|EMBL:KUF39572.1, ECO:0000313|Proteomes:UP000053300};
RN [1] {ECO:0000313|EMBL:KUF39572.1, ECO:0000313|Proteomes:UP000053300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=12322-1 {ECO:0000313|EMBL:KUF39572.1,
RC ECO:0000313|Proteomes:UP000053300};
RA Ming D., Wang M., Hu S., Zhou Y., Jiang T.;
RT "Complete genome sequence of a multi-drug resistant strain Acidovorax sp.
RT 12322-1.";
RL Submitted (DEC-2015) 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:KUF39572.1}.
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DR EMBL; LPXH01000035; KUF39572.1; -; Genomic_DNA.
DR RefSeq; WP_058880173.1; NZ_LPXH01000035.1.
DR AlphaFoldDB; A0A0W7YXB2; -.
DR STRING; 225992.B5M06_15355; -.
DR Proteomes; UP000053300; Unassembled WGS sequence.
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: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; 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 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:UP000053300};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 3..70
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1181 AA; 131789 MW; 14AD5B2E1FBA247F CRC64;
MFVHLRLHTE FSVIDGTCRI NDVISAAAAD GQPALALTDL NNMFGALKFY KAGRGKGVKP
LLGAELNMEA WGGDVASRVL LLVQSHQGFL NLSEILARGW TSNVPKGQAQ PLFKWEWLRE
LGEGLLLLSG ANAGPIGQLL LRGDSQGAAD AALQLASTFP HRFYLELQRA GRPDDERLVI
QTVQLAARMN LPVVATHPIQ FVKPGDFEAH ETRVCIAEGE VLANPKRVRR FTQEQYFKSS
AQMEALFADI PSAIENTLEI ARRCSVQLKL GTYYLPEFPI PEGMTEQQYF RHASYEGLEH
RLALLFPDVA ERNRKRPEYV ERLEFELGII LKMGFPGYFL IVADFINWAK NNGCPVGPGR
GSGAGSLVAY VLKITDLDPL YYNLLFERFL NPERVSMPDF DVDFCQANRD RVIDYVKERY
GRNAVSQIAT FGTMAARAVI RDVGRVLDLS YNFCDGISKL IPNKPGLHVT LKYPPNPKKE
GDKYTYAIEA EPILAQRIEQ EEDVKLLIEM AQKLEGLTRN IGMHAGGVVI APGKITDFCP
MYQQPGSESA VAMFDKDDVE QIGLVKFDFL GLATLTILEI AREFIMKRHK GQENFRFEEI
PLDDYPTYKL FQEGKTEAVF QFESRGMQGM LRDAKPSRLE DLIALNALYR PGPMDLIPSF
VARKHGREEI EYPHPLVEKV LAETYGIMVY QEQVMQTAQV LGGYSLGGAD LLRRAMGKKK
VEEMVKHRAI FREGAAKQGI SQEKADEVFD LMEKFAGYGF NKSHAAAYSL LAYHTAWLKV
HYTAEFYCGN MTVEMDNTDK LKVLFEDAIK MGMSFELPDV NRGVYRFEPV TDKVIRYGLG
AVKGTGQQAI EAIIAAREGQ GVGPDGHVKG PFKSLFDFCS RVDRSKINKR TVEALIKAGA
FDSIHLDRAA LAASIDTAFE YGNAQIVNAN QGGLFDMMGD DAQGSSSQEP PLANVLPWTV
KERLTQEKQA IGFYISGHLF DEVEHEVRQF IRTPLSELGD SREPQLVAGI VSDLRVINGQ
RGKLCLFKLD DKSTVLEASI DEATLLANSD LLKDDEFVVL SARAQHDHFS GGLRLKAQKV
FSLADARCLF ARYLQIDAKQ QLPNVQRILR EFPAKVVSDA EGDVVRGLRV RMEVRCQSGE
DAALVELDLG EHNRFYPSDA ALAAWRAEAG STACQLVWRN S
//
