ID A0A2K8NXR2_9MOLU Unreviewed; 986 AA.
AC A0A2K8NXR2;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE RecName: Full=DNA-directed DNA polymerase {ECO:0000256|ARBA:ARBA00012417};
DE EC=2.7.7.7 {ECO:0000256|ARBA:ARBA00012417};
GN Name=dnaE {ECO:0000313|EMBL:ATZ18577.1};
GN ORFNames=ESOMN_v1c01920 {ECO:0000313|EMBL:ATZ18577.1};
OS Williamsoniiplasma somnilux.
OC Bacteria; Mycoplasmatota; Mollicutes; Entomoplasmatales;
OC Williamsoniiplasma.
OX NCBI_TaxID=215578 {ECO:0000313|EMBL:ATZ18577.1, ECO:0000313|Proteomes:UP000232230};
RN [1] {ECO:0000313|EMBL:ATZ18577.1, ECO:0000313|Proteomes:UP000232230}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PYAN-1 {ECO:0000313|EMBL:ATZ18577.1,
RC ECO:0000313|Proteomes:UP000232230};
RA Lo W.-S., Gasparich G.E., Kuo C.-H.;
RT "Genome sequence of Entomoplasma somnilux PYAN-1 (ATCC 49194).";
RL Submitted (NOV-2017) 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}.
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DR EMBL; CP024965; ATZ18577.1; -; Genomic_DNA.
DR RefSeq; WP_024863737.1; NZ_CP024965.1.
DR AlphaFoldDB; A0A2K8NXR2; -.
DR KEGG; esx:ESOMN_v1c01920; -.
DR Proteomes; UP000232230; 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; cd07431; PHP_PolIIIA; 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 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.
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:UP000232230};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 9..118
FT /note="PHP"
FT /evidence="ECO:0000259|Pfam:PF02811"
FT DOMAIN 235..495
FT /note="Bacterial DNA polymerase III alpha subunit NTPase"
FT /evidence="ECO:0000259|Pfam:PF07733"
FT DOMAIN 498..663
FT /note="DNA polymerase III alpha subunit finger"
FT /evidence="ECO:0000259|Pfam:PF17657"
FT DOMAIN 736..826
FT /note="DNA polymerase helix-hairpin-helix motif"
FT /evidence="ECO:0000259|Pfam:PF14579"
FT DOMAIN 908..982
FT /note="OB"
FT /evidence="ECO:0000259|Pfam:PF01336"
SQ SEQUENCE 986 AA; 114041 MW; 435E6841D707E647 CRC64;
MKFSPQINLR SCYNFQESLI KVPDYIDFAV RNNFKFAFYS ELNSMYGVAE FVNLAKKNNI
KPIIGLTLEF EHQIAILIAK NEQGYQNLTI LSSWLMNENN HFNFDFQWTK FISDNLIMVT
NSLTFKNSVK ELIKTNDIYF NVVDLRKISY LEDKNYETFV ILNAIKNNLT IAEVQNIGHE
HYLSDEELLK LNVNLDINNK SLLEIANKCS FELFSNRQWN FAKFKTPQNM PSGNFLRKLC
EESLNSYLLF AKNKKNPNVD YFERLNYELD VIYKTGFIDY FLVVWDYVKY ARENQIMVGP
GRGSAAGSLV SFLLKITTID PLQYDLLFER FLNPKRVSLP DIDLDFQDDK RDLIIEYLFE
KYGADKVATI VTFQSIGLKS AIRDVARVYE IDLKIVNEIA KLFPSFVVNQ SFAEIINKSS
KLRKYQEEYP EIFDHASALI GLPRQTGTHA AGVILSDVDI KNIVPIRIGY NGINQTQFDM
KYLEPLGLIK MDVLGLRNLT TLQEILSSVY KSEKKLINLD EINLQDNETF VNLQAGKTSG
IFQLESPGMT NVIMKIKTNS IEDISIASAL FRPGPQEMIP EYVKRKFSNV PVEKYLIDKD
LKSILEPTYG IIVYQEQVIQ ILRKVANFSL AQADLVRRAI GKKDFQKLHA AKNEFIEKAT
ENNYQIQKAK MIWEWIEKFA AYGFNKSHSI AYSYISYWLA YLKTHYPAEF YCSLLNGVTG
NVEKTSQYLK EINNYGIKII KPSIKNINFN YIGFKTALIM PLTLIKGVGI EFIRKLREQY
KSNPQIMDSV FSLVTLMFNH GLNKNVFEAL VWSGALDCFG YSRSTLVENY EEILKFANFN
KDIEIINNNL IPELTNYEDK EEILLNKEKE FIGFFISSHP IEKIRTEYSF LKAHKIINLL
NKKGNFIIIG YVSAIKEKND KHGDPMAFIE MSDETENIEI TVFSRTFKNF KNDILLGSVL
CVEINIDSFN DKPSFVLNKI IKIIKN
//
