ID   A0A1I6EJ92_9RHOB        Unreviewed;       477 AA.
AC   A0A1I6EJ92;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   27-MAR-2024, entry version 16.
DE   SubName: Full=DNA polymerase-3 subunit epsilon {ECO:0000313|EMBL:SFR17823.1};
GN   ORFNames=SAMN04515673_1133 {ECO:0000313|EMBL:SFR17823.1};
OS   Poseidonocella sedimentorum.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Poseidonocella.
OX   NCBI_TaxID=871652 {ECO:0000313|EMBL:SFR17823.1, ECO:0000313|Proteomes:UP000199302};
RN   [1] {ECO:0000313|EMBL:SFR17823.1, ECO:0000313|Proteomes:UP000199302}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KMM 9023,NRIC 0796,JCM 17311,KCTC 23692
RC   {ECO:0000313|Proteomes:UP000199302};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: DNA polymerase III is a complex, multichain enzyme
CC       responsible for most of the replicative synthesis in bacteria. The
CC       epsilon subunit contain the editing function and is a proofreading 3'-
CC       5' exonuclease. {ECO:0000256|ARBA:ARBA00025483}.
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DR   EMBL; FOYI01000013; SFR17823.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1I6EJ92; -.
DR   STRING; 871652.SAMN04515673_1133; -.
DR   OrthoDB; 9804290at2; -.
DR   Proteomes; UP000199302; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:UniProtKB-EC.
DR   GO; GO:0004527; F:exonuclease activity; IEA:UniProt.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   CDD; cd06127; DEDDh; 1.
DR   Gene3D; 3.30.420.10; Ribonuclease H-like superfamily/Ribonuclease H; 1.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   NCBIfam; TIGR00573; dnaq; 1.
DR   PANTHER; PTHR30231; DNA POLYMERASE III SUBUNIT EPSILON; 1.
DR   PANTHER; PTHR30231:SF4; PROTEIN NEN2; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SUPFAM; SSF53098; Ribonuclease H-like; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199302};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        15..38
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        50..72
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          283..452
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
SQ   SEQUENCE   477 AA;  51167 MW;  D5A2ED2A22E4088F CRC64;
     MGGRGLLGLG LRLRVFLFFV LLALGALALA GGALYLGWSR LDPPGPSAPF MTAFLIFAFA
     NTGLVLGVWL LFDENVARPI DRLAAALRLR AHADLEASVQ AGAAPYLGDL APAAEALARR
     IGGAKSASAD GAEDGGEAES LRSDREQLTA LLTEIPIATI LLNPAEQIIL YDAQAAEVLS
     RIAPPRLRAP VSDYFDMGSL RDAMRRLEQG AGETILTLFD TARSQGFQAR MKQLRRGGHM
     IFIEVQSEPD ADGLSARPLV FDFTLHDTAQ SREIEDTPLM DLCFVPFDTE TTGLSVARDA
     VVQLSALRVL KGRIVEGEVF DSYVNPGRPI PPASTRIHKI TDALVAGAPP MPDVARAFHH
     FARESVLVAH NAPFDIGLLR RDAAEAGLTW PHPVLDTVLL SAVVFGTTES HTLDALCARL
     SIDIPEGRRH TALGDADATA RALVKLLPLV AARGITTFGA LIAETRKHGR LLRDLND
//