ID K8WE94_9GAMM Unreviewed; 1160 AA.
AC K8WE94;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 27-MAR-2024, entry version 49.
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:EKT58251.1};
GN ORFNames=OOA_14032 {ECO:0000313|EMBL:EKT58251.1};
OS Providencia burhodogranariea DSM 19968.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Providencia.
OX NCBI_TaxID=1141662 {ECO:0000313|EMBL:EKT58251.1, ECO:0000313|Proteomes:UP000009336};
RN [1] {ECO:0000313|EMBL:EKT58251.1, ECO:0000313|Proteomes:UP000009336}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19968 {ECO:0000313|EMBL:EKT58251.1,
RC ECO:0000313|Proteomes:UP000009336};
RX PubMed=23145767; DOI=10.1186/1471-2164-13-612;
RA Galac M.R., Lazzaro B.P.;
RT "Comparative genomics of bacteria in the genus Providencia isolated from
RT wild Drosophila melanogaster.";
RL BMC Genomics 13:612-612(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 -!- 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:EKT58251.1}.
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DR EMBL; AKKL01000037; EKT58251.1; -; Genomic_DNA.
DR RefSeq; WP_008912797.1; NZ_KB233223.1.
DR AlphaFoldDB; K8WE94; -.
DR STRING; 1141662.OOA_14032; -.
DR PATRIC; fig|1141662.3.peg.2850; -.
DR eggNOG; COG0587; Bacteria.
DR HOGENOM; CLU_001600_0_2_6; -.
DR OrthoDB; 9803237at2; -.
DR Proteomes; UP000009336; 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; 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 Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:EKT58251.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EKT58251.1}.
FT DOMAIN 7..74
FT /note="Polymerase/histidinol phosphatase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00481"
SQ SEQUENCE 1160 AA; 130038 MW; B8D714755E4F1CB8 CRC64;
MAEPRFIHLR VHSDYSMIDG LAKTGPLVKK VAAMGMPAFA ITDFTNLCGL VKFYGAAHGA
GIKPIIGADF FVESEQLGDE IAHLTVLARN NEGYQNLTLL ISEAYQKGYG AIGPTIQRDW
LIKHKEGLIL LSGGRQGDVG QFLLRGNQAL VDECLRFYET HFPGCYYLEL IRTGRPDEES
YLHAAIELAT LRGLPVVATN EVCFLETGDF DAHEIRVAIH DGFTLSDPKR PKKYSPQQYL
RTEEEMCELF ADIPEALENS VEIAKRCNVT IRLGEYFLPQ FPTGDMKTED FLVLRSKEGL
EERLEFLFPD EKVRAEKRPE YDERLEIELN VINQMGFPGY FLIVMEFIQW SKDNGVPVGP
GRGSGAGSLV AYALKITDLD PLEFDLLFER FLNPERVSMP DFDVDFCMEK RDQVIDHVAQ
MYGRDAVSQI ITFGTMAAKA VIRDVGRVLG HPYGFVDRIS KLVPPDPGMT LDKAFEAEPQ
LPEVYEADEE VKALIDMARK LEGVTRNAGK HAGGVVIAPT KITDFAPLYC DAEGKNPVTQ
FDKNDVEYAG LVKFDFLGLR TLTIINWALE MINARRSKKN LEPIDIATIP LQDTKSFDML
QRSETTAVFQ LESRGMKDLI KRLRPDCFED MIALVALFRP GPLQSGMVDN FIDRKHGREE
LSYPDVQWQH ESLKPVLEPT YGIILYQEQV MQIAQVLAGY TLGGADMLRR AMGKKKPEEM
AKQRSVFEEG SINNGVDGEL SMKIFDLVEK FAGYGFNKSH SAAYALVSYQ TLWLKAHYPA
EFMAAVMTAD MDNTEKVVGL VDECWRMGLK VLPPDINSGL YHFHVNDEGE IVYGIGAIKG
VGEGPIEAII EARQKGGIFK EIFDLCARVD IKKINRRVME KLIMAGAFDH LGPHRAALMS
SLEDALKAAD QHAKAEAIGQ SDMFGVLADA PEQVESSYAS VPKWPEQVVL DGERETLGLY
LTGHPITRYL SEIERYTNGL RLKDVNPTPR GQMTTVVGLV LSSKVITTKR GNRIGICTLD
DRSGRLDIML FSDALDKYQH LLEKDSILIA TGQVSFDDFN GGNKMTVREL MDISEAREKY
ARGLAISLSD RQINDQLLNR LRSTLEPHRS GTIPVHLYYQ KEDARAKLKF GVVWRVTPVD
ALLNSLRALL GNEQVELEFD
//
