ID   DING_STAAW              Reviewed;         897 AA.
AC   Q8NWP2;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   03-AUG-2022, entry version 123.
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=MW1345;
OS   Staphylococcus aureus (strain MW2).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=196620;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MW2;
RX   PubMed=12044378; DOI=10.1016/s0140-6736(02)08713-5;
RA   Baba T., Takeuchi F., Kuroda M., Yuzawa H., Aoki K., Oguchi A., Nagai Y.,
RA   Iwama N., Asano K., Naimi T., Kuroda H., Cui L., Yamamoto K., Hiramatsu K.;
RT   "Genome and virulence determinants of high virulence community-acquired
RT   MRSA.";
RL   Lancet 359:1819-1827(2002).
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; BA000033; BAB95210.1; -; Genomic_DNA.
DR   RefSeq; WP_000525081.1; NC_003923.1.
DR   AlphaFoldDB; Q8NWP2; -.
DR   SMR; Q8NWP2; -.
DR   EnsemblBacteria; BAB95210; BAB95210; BAB95210.
DR   KEGG; sam:MW1345; -.
DR   HOGENOM; CLU_012117_1_1_9; -.
DR   OMA; VVTNHAM; -.
DR   Proteomes; UP000000418; 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; 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; 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..897
FT                   /note="3'-5' exonuclease DinG"
FT                   /id="PRO_0000277597"
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          703..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   897 AA;  104191 MW;  3ED81550F94DB344 CRC64;
     MGMATYAVVD LETTGNQLDF DDIIQIGITF VRNNQIIDTY HSMIRTNLEI PPFIQALTSI
     EENMLQQAPY FNQVAQEIYD KIKDCIFVAH NVDFDLNFIK KAFKDCNIQY RPKKVIDTLE
     IFKIAFPTDK SYQLSELAEA HGITLANAHR ADEDAATTAK LMILAFEKFE KLPLDTLKQL
     YYLSKQLKYD LYDIFFEMVR QYDAKPLDKS YEKFEQIIYR KQVDFKKPTT NYNGSLKSLY
     SKAVDQLGLT YRPQQLYLAE TILDQLMHSE KAMIEASLGS GKSLAYLLAA LMYNIETGKH
     VMISTNTKLL QSQLLEKDIP AMNEALNFKI NALLIKSKSD YISLGLISQI LKDDTSNYEV
     NILKMQLLIW ITETPSGDIQ ELNLKGGQKM YFDQKIETYV PARHDVHYYN FIKRNAQNIQ
     IGITNHAHLI HSDVENSIYQ LFDDCIVDEA HRLPDYALNQ VTNELSYADI KYQLGLIGKN
     ENEKLLKAID QLEKQRILEK LDIAPIDIFG LKASMNEIHE LNEQLFSTIF TIINDSDVYD
     DDIHRFHNVF TFETKDILKD LHAIIDKLNK TLEIFNGISH KTVKSLRKQL LYLKDKFKNI
     EQSLKAGHTS FISIKNLSQK STIRLYVKDY AVKDVLTKQV LEKFKSLIFI SGTLKFNHSF
     EAFKQLFNKD VHFNTFEVNT SLQSAKNTSV FIPSDVASYQ YKNIDEYVAS IVSYIIEYTT
     ITSSKCLVLF TSYKMMHMVQ DMLNELPEFE DYVVLTQQQN QNYKIVQQFN NFDKAILLGT
     STFFEGFDFQ ANGIKCVMIA KLPFMNKHNA KYWLMDSEFT STFKEYVLPD AVTRFRQGLG
     RLIRSENDRG IIVSFDDRLI NSNYKNFFEQ TLENYRQKKG DIQQFGKLLR QIQKKKK