ID   DING_STAHJ              Reviewed;         900 AA.
AC   Q4L6F9;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   02-AUG-2005, sequence version 1.
DT   03-AUG-2022, entry version 136.
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=SH1457;
OS   Staphylococcus haemolyticus (strain JCSC1435).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=279808;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCSC1435;
RX   PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA   Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA   Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA   Hiramatsu K.;
RT   "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT   extreme plasticity of its genome and the evolution of human-colonizing
RT   staphylococcal species.";
RL   J. Bacteriol. 187:7292-7308(2005).
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; AP006716; BAE04766.1; -; Genomic_DNA.
DR   RefSeq; WP_011275752.1; NC_007168.1.
DR   AlphaFoldDB; Q4L6F9; -.
DR   SMR; Q4L6F9; -.
DR   STRING; 279808.SH1457; -.
DR   EnsemblBacteria; BAE04766; BAE04766; SH1457.
DR   GeneID; 58062340; -.
DR   KEGG; sha:SH1457; -.
DR   eggNOG; COG0847; Bacteria.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_1_1_9; -.
DR   OMA; VVTNHAM; -.
DR   OrthoDB; 679382at2; -.
DR   Proteomes; UP000000543; 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..900
FT                   /note="3'-5' exonuclease DinG"
FT                   /id="PRO_0000277602"
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          713..893
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   900 AA;  105137 MW;  C33E28D4932586EA CRC64;
     MGHTSYAVVD LETTGNQLDY DEIIQIGITF VSNNKISGTY HSMIRTDLDI PPFIQALTSI
     EDTMLEQAPY FHEIAQEIYK QLKDRVFVAH NVDFDLNFIK KAFQNCNIDF KPKKVLDTLE
     LFKIAYPTDK SYQLSELAEA HDIPLDNAHR ADEDATTTAL LMIKAFQKFE QLPIDTLKQL
     YYLSKNLKYD LFNVLFEMVR QHENSPLDNQ YGQFEQIIYK KQIDLKAPKT SFNGSLKDLY
     SEVVKSLNLT YRPQQLYLSE IILEQLMHND KAMIEAPLGS GKSLAYLLAA LMYNIETGRH
     VMISTNTKLL QNQLLLKDIP SINQALNFKI NATLIKSKSE YISLGLISQI LKDETTNYEV
     NILKMQLLTW IIETETGDIQ DLNLKGGQKM YFDQKIETYV PVRHDMHYYN YIKRNAHHIQ
     IGITNHAHLI HSDQENSIYQ LFDDCIIDEA HRLPDYALNQ VTNDLDYSDL KYQLGLIGKN
     ENEKLLKAID KLEQQRILER LDIAPIDVFG LKMNISEIHD LNERLFNHIF EIIQNSDVYD
     DDIHRHHYVF EFDSTQILKD LHLIVDKINK TLEIFNGMTH KTIKTLRKQL LYINDTYRNI
     EQSLKDKHTA YLSIRNLTQK STIKLIVKDY AVRDILTTRV LDKFNSLTFI SGTLTFNHKF
     DAFKNWFKED VHFNTYQVPS TLSNHANTNV YIPSDVSSYN FKNIDDYVAS IVDYIQEYVT
     ITDSKCLVLF TSYRMMHMVQ ELLNELPTFE DYVVLTQQQN QNYKIVQQFN NFDKTILLGT
     STFFEGFDYQ AKGIKCVMIA KLPFMNKYNT KHWLMDSEFD STFKDYVLPD AVTRFRQGLG
     RLIRNEDDQG LIVSFDDRLV SSNYKNFFAQ TLENYKQKKG DIKQFSKLVN KIQHNIDANK