ID   DING_STAS1              Reviewed;         900 AA.
AC   Q49XR1;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 119.
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=SSP1289;
OS   Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS   20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=342451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX   PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA   Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA   Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT   "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT   pathogenesis of uncomplicated urinary tract infection.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(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; AP008934; BAE18434.1; -; Genomic_DNA.
DR   RefSeq; WP_011303079.1; NZ_MTGA01000038.1.
DR   AlphaFoldDB; Q49XR1; -.
DR   SMR; Q49XR1; -.
DR   STRING; 342451.SSP1289; -.
DR   EnsemblBacteria; BAE18434; BAE18434; SSP1289.
DR   KEGG; ssp:SSP1289; -.
DR   PATRIC; fig|342451.11.peg.1291; -.
DR   eggNOG; COG0847; Bacteria.
DR   eggNOG; COG1199; Bacteria.
DR   HOGENOM; CLU_012117_1_1_9; -.
DR   OMA; VVTNHAM; -.
DR   OrthoDB; 679382at2; -.
DR   Proteomes; UP000006371; 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;
KW   Reference proteome.
FT   CHAIN           1..900
FT                   /note="3'-5' exonuclease DinG"
FT                   /id="PRO_0000277603"
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   900 AA;  105013 MW;  2E91AE7009FB6DF0 CRC64;
     MAKPCYAVVD LETTGNQLDY DEIIQIGITF VRENKIIGTY HSMIKTDLEI PPFIQALTSI
     EEDMLNQAPY FHEIAEDIYK QIDGCIFVAH NVAFDLNFIK KSFKQCHINY RPKKVMDTLE
     LFKVAFPTDK SYQLSELAEA HGIILNNAHR ADEDAATTAQ LMIIAFEKFE SLPLDTLKQL
     YYLSKNLKYD LHDIIFEMVR NYDEQTLSDR FDQFEQIIYK KQIDFKAPTV QFGGNLKALY
     TLVTKELGLT YRPQQLYLSE IILEQLMHSE KAMIEAPLGS GKSFAYLLAS LMYNIETGKH
     VMISTNTKLL QNQLLEKDIP AIKKALDFKI NATLIKSKRD YIALGLISQI LEEESSNYEV
     CILKMQLLIW ITETDTGDIQ ELDLKGGQKM YFEQKLETYV PVRNDIHYFN FIKRNAQNIQ
     IGITNHAHLI HAAHDNSIYQ LFDDCIIDEA HRLPDYALNQ VTNELSYADI KYQLGLIGKT
     ENEKLLKSID LLEQQRILEK LDIPPIDVFG LKTTVNEIHD LNEQLFTTMY DIIQSSEIQD
     DEVHKLHFVY HFDVTPILND LHAIIHKLNM TLEFFNGMSH KSIKSVRKQF LYINDRFKDI
     EQSLKNKHTC YLSIKNLNQK STIRLNVKDY DVKEILTKQV LDKFKSLTFI SGTLTFNHSF
     ENFKQWFNKD IEFNTYEIDT TVTSPNQTTV FIPNDVSSYN YKNINDYVSS IVNYVIEYVS
     VVESKCLILF TSYKMMHMVQ ELINELPEFE DYVVLTQQQN QNYKIVQQFN SFNKAILLGT
     GTFFEGFDFQ SNGIKCVMIA KLPFMNQNNT KYWLMESEFT STFKEYVLPD AVTRFRQGLG
     RLIRSENDKG IIVSFDDRLI RSNYKQFFEQ SLERYRQKKG DIKQFSTLLK KLKKENAKKP