ID   DING_STAAB              Reviewed;         897 AA.
AC   Q2YY51;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   03-AUG-2022, entry version 110.
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=SAB1319c;
OS   Staphylococcus aureus (strain bovine RF122 / ET3-1).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=273036;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=bovine RF122 / ET3-1;
RX   PubMed=17971880; DOI=10.1371/journal.pone.0001120;
RA   Herron-Olson L., Fitzgerald J.R., Musser J.M., Kapur V.;
RT   "Molecular correlates of host specialization in Staphylococcus aureus.";
RL   PLoS ONE 2:E1120-E1120(2007).
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; AJ938182; CAI81008.1; -; Genomic_DNA.
DR   RefSeq; WP_000525055.1; NC_007622.1.
DR   AlphaFoldDB; Q2YY51; -.
DR   SMR; Q2YY51; -.
DR   KEGG; sab:SAB1319c; -.
DR   HOGENOM; CLU_012117_1_1_9; -.
DR   OMA; VVTNHAM; -.
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_0000277592"
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..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   897 AA;  104085 MW;  2C7AA5402DC330C8 CRC64;
     MGMATYAVVD LETTGNQLDF DDIIQIGITF VRNIQIIDTY HSMIRTNLEI PPFIQALTSI
     EENMLQQAPY FNQVAQGIYD NMKDCIFVAH NVDFDLNFIK KAFKDCNIQY RPKRVIDTLE
     IFKIAFPTDK SYQLSELAEA HGITLANAHR ADEDAATTAK LMILAFEKFE KLPLDTLKQL
     YYLSKQLKYD LYDIFFEMVR QYDAKPLAKS 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
     DAFKQLFNKD VHFNTFEVNT SLQSAKNTSV FIPSDVASYQ YKNIDEYVAS IVSYIIEYTT
     ITSSKCLVLF TSYKMMHMVQ DMLNELPEFE DYVVLTQQQN QNYKIVQQFN NFDKAILLGT
     STFFEGFDFQ ANGIKCVMIA KLPFMNKHNA KYWLMDSEFT STFKEYVLPD AVTRFRQGLG
     RLIRNENDRG IIVSFDDRLI NSNYKNIFEQ TLENYRQKKG DIQQFGKLLR QIQKKKK