ID   DING_STAES              Reviewed;         902 AA.
AC   Q8CP71;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 125.
DE   RecName: Full=3'-5' exonuclease DinG {ECO:0000255|HAMAP-Rule:MF_02206};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_02206};
GN   Name=dinG {ECO:0000255|HAMAP-Rule:MF_02206}; OrderedLocusNames=SE_1143;
OS   Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=176280;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 12228 / FDA PCI 1200;
RX   PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA   Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA   Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA   Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT   "Genome-based analysis of virulence genes in a non-biofilm-forming
RT   Staphylococcus epidermidis strain (ATCC 12228).";
RL   Mol. Microbiol. 49:1577-1593(2003).
CC   -!- FUNCTION: 3'-5' exonuclease. {ECO:0000255|HAMAP-Rule:MF_02206}.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 2 sub-
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02206}.
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DR   EMBL; AE015929; AAO04740.1; -; Genomic_DNA.
DR   RefSeq; NP_764698.1; NC_004461.1.
DR   RefSeq; WP_001831318.1; NZ_WBME01000006.1.
DR   AlphaFoldDB; Q8CP71; -.
DR   SMR; Q8CP71; -.
DR   STRING; 176280.SE_1143; -.
DR   DNASU; 1055710; -.
DR   EnsemblBacteria; AAO04740; AAO04740; SE_1143.
DR   GeneID; 50018734; -.
DR   KEGG; sep:SE_1143; -.
DR   PATRIC; fig|176280.10.peg.1116; -.
DR   eggNOG; COG0847; Bacteria.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_1_1_9; -.
DR   OMA; VVTNHAM; -.
DR   Proteomes; UP000001411; Chromosome.
DR   GO; GO:0008408; F:3'-5' exonuclease activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR   GO; GO:0003887; F:DNA-directed DNA polymerase activity; IEA:InterPro.
DR   GO; GO:0004386; F:helicase activity; IEA:InterPro.
DR   GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IEA:InterPro.
DR   GO; GO:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 3.30.420.10; -; 1.
DR   Gene3D; 3.40.50.300; -; 2.
DR   HAMAP; MF_02206; DinG_exonucl; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR006310; DinG.
DR   InterPro; IPR045028; DinG/Rad3-like.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR006935; Helicase/UvrB_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
DR   PANTHER; PTHR11472; PTHR11472; 1.
DR   Pfam; PF13307; Helicase_C_2; 1.
DR   Pfam; PF04851; ResIII; 1.
DR   Pfam; PF00929; RNase_T; 1.
DR   SMART; SM00479; EXOIII; 1.
DR   SMART; SM00491; HELICc2; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF53098; SSF53098; 1.
DR   TIGRFAMs; TIGR01407; dinG_rel; 1.
DR   TIGRFAMs; TIGR00573; dnaq; 1.
DR   PROSITE; PS51193; HELICASE_ATP_BIND_2; 1.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Exonuclease; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..902
FT                   /note="3'-5' exonuclease DinG"
FT                   /id="PRO_0000277600"
FT   DOMAIN          8..161
FT                   /note="Exonuclease"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206"
FT   DOMAIN          241..496
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206"
FT   DOMAIN          714..883
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206"
FT   MOTIF           448..451
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206"
FT   BINDING         276..283
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206"
SQ   SEQUENCE   902 AA;  105327 MW;  294CCB8A8206A2A7 CRC64;
     MGIATFAVVD LETTGNQLDY DEIIQIGITF VRQNQVIDTY HSMIRTDLEI PPFIQALTSI
     EEEMLVQAPY FNEVADDIYQ LIKDCVFVAH NISFDLNFIK KAFEKCNIQF KPKRVMDTLE
     LFKIAFPTDK SYQLSALAES HHIPLNNAHR ADEDATTTAK LMIKAFEKFE QLHLDTQKQL
     YYLSKNLKYD LYHILFEMVR NYQTKPPNNQ FEQFEQIIYR KQIDLKKPAV NFDGTLKDLY
     KNVTQSLNLT YRPQQLYLAE IILDQLMHSD KAMIEAPLGS GKSLAYLLAA TMYNIETGRH
     VMISTNTKLL QSQLLEKDIP LLNDVLDFKI NASLIKSKND YISLGLISQI LKDDTNNYEV
     SILKMQLLIW ITETNTGDIQ ELNLKGGQKM YVDQKIETYV PVRHDIHYYN YIKRNAQNIQ
     IGITNHAHLI HSDSENTIYQ LFDDCIIDEA HRLPDYALNQ VTNDLNYSDV KYQLGLIGKN
     ENEKLLKAVD KLEQQRILEK LDIAPIDVFG LKININELHD LNEQLFTTIY NIIQTSDVYD
     DDIHKYHYVY DFETGEILKD LRAIIDKLNK TIEIFNGMNH KTIKSVRKQL LYLHDKFKLI
     EQSIKDHHTS FISIKNLAQK STIRLLVKDY DVKDILTKQV LEKFKSLTFI SGTLTFNHSF
     KAFQNWFNED IDFNTFEIST PLTSSNHTNV FVPNDVETYN YKNLDDYVAS IVDYIVEYIT
     VTQSKCLVLF TSYKMMHMVQ DLLNELPELE DYVILTQQQN QNYKIVQQFN NFDKSILLGT
     STFFEGFDFQ ANGLKCVMIA KLPFMNKHNI KYWLMDSEFT STFKDYVLPD AVTRFRQGLG
     RLIRHEDDKG LIVSFDDRLV NSTYKSFFAQ SLEHFKQRKG NIKQFNKLLN QIQRSIDNES
     KS