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Database: UniProt
Entry: A0A0D6TGB2_9RHOB
LinkDB: A0A0D6TGB2_9RHOB
Original site: A0A0D6TGB2_9RHOB 
ID   A0A0D6TGB2_9RHOB        Unreviewed;       624 AA.
AC   A0A0D6TGB2;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=DNA polymerase III subunit epsilon {ECO:0000313|EMBL:KIX19245.1};
GN   ORFNames=SY26_03990 {ECO:0000313|EMBL:KIX19245.1};
OS   Paracoccus sp. 228.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Paracoccaceae; Paracoccus.
OX   NCBI_TaxID=1192054 {ECO:0000313|EMBL:KIX19245.1, ECO:0000313|Proteomes:UP000032743};
RN   [1] {ECO:0000313|EMBL:KIX19245.1, ECO:0000313|Proteomes:UP000032743}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=361 {ECO:0000313|EMBL:KIX19245.1,
RC   ECO:0000313|Proteomes:UP000032743};
RA   Karczewska-Golec J., Kochanowska-Lyzen M., Balut M., Golec P.,
RA   Madanecki P., Markert S., Piotrowski A., Schweder T., Szalewska-Palasz A.;
RT   "Three Bacterial Inhabitants of the Baltic Sea under Osmotic Stress: a
RT   Genomic and a Proteomic Perspective.";
RL   Submitted (FEB-2015) 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}.
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:KIX19245.1}.
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DR   EMBL; JYGY01000001; KIX19245.1; -; Genomic_DNA.
DR   RefSeq; WP_045999328.1; NZ_JYGY01000001.1.
DR   STRING; 1192054.SY26_03990; -.
DR   PATRIC; fig|1603292.4.peg.819; -.
DR   OrthoDB; 9804290at2; -.
DR   Proteomes; UP000032743; 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:InterPro.
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:UP000032743};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        34..57
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          432..599
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000259|SMART:SM00479"
SQ   SEQUENCE   624 AA;  65957 MW;  D7B0784D250FC1C4 CRC64;
     MRRRILMLFL AALVAALVLA GLALWRVVQG GQDAVIQAAM IAGLGLLGLM TALWFLFDRH
     LARPLESLAG ALRTGRVPDL AQTRHLADLG PAARDAALAR ERSDHALAQA LQDHAAETLR
     EKASLEAILA DFGAGAVMAD ARGRVVFYNA SAARLLPGLA LDRALDTLLT SGALRAAQMR
     LSAGAAATDL TCLTVGGVRL SGRLRAIDDG LLLILRDGVV QRPAPRDTLE ALRRHASTLV
     PMLDALDGPI PPALAQAIRA EGQGLANATR SLSRIMASDA PGTVAALTEL AAGLEAADLP
     PXAFRAEAAS LNALLLLLDA RLRAVGHTPV LSVRPDPDDQ MRLVLDWRGS PVPIDLLEGW
     LTAAPDPGQP DVTGAEILAR HGTGIWPETD GARARLVMPL ALAQGVADGS GVTYDFALAT
     RGAASSRLAD LTCVVFDTET TGLTDRDRIV QIAGLRLARG RLTGERFETL VNPGCPIPPS
     STAIHHITDA MVADAPDLTA ALTAFRHFCD DSVLIAHNAP FDMGFLRRAE AQTGTRFDNR
     VLDTVLLSAM VWGQSEVHTL DALTERLGIA IPPEARHTAM GDTIATAQAY LALIPALEAK
     GITRFEEVVA KARDHRALIA DANR
//
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