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Database: UniProt
Entry: Q6GGV4
LinkDB: Q6GGV4
Original site: Q6GGV4 
ID   DING_STAAR              Reviewed;         897 AA.
AC   Q6GGV4;
DT   06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   19-JUL-2004, sequence version 1.
DT   11-DEC-2019, entry version 111.
DE   RecName: Full=3'-5' exonuclease DinG {ECO:0000255|HAMAP-Rule:MF_02206, ECO:0000305};
DE            EC=3.1.-.- {ECO:0000255|HAMAP-Rule:MF_02206, ECO:0000269|PubMed:22166102};
GN   Name=dinG {ECO:0000255|HAMAP-Rule:MF_02206, ECO:0000303|PubMed:22166102};
GN   OrderedLocusNames=SAR1466;
OS   Staphylococcus aureus (strain MRSA252).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=282458;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MRSA252;
RX   PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA   Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA   Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA   Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA   Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA   Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA   Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA   Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA   Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT   "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT   for the rapid evolution of virulence and drug resistance.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
RN   [2]
RP   FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT,
RP   DOMAIN, AND MUTAGENESIS OF ASP-10; GLU-12 AND LYS-282.
RC   STRAIN=MRSA252;
RX   PubMed=22166102; DOI=10.1042/bj20111903;
RA   McRobbie A.M., Meyer B., Rouillon C., Petrovic-Stojanovska B., Liu H.,
RA   White M.F.;
RT   "Staphylococcus aureus DinG, a helicase that has evolved into a nuclease.";
RL   Biochem. J. 442:77-84(2012).
CC   -!- FUNCTION: 3'-5' exonuclease acting on single-stranded DNA (ssDNA) and
CC       RNA (ssRNA) substrates. Displays ssDNA-stimulated ATPase activity, but
CC       lacks helicase activity. {ECO:0000269|PubMed:22166102}.
CC   -!- ACTIVITY REGULATION: The nuclease activity is inhibited by ATP or ADP.
CC       {ECO:0000269|PubMed:22166102}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         Note=kcat is 25 min(-1) for ATPase activity in the absence of DNA.
CC         kcat is 78 min(-1) for ATPase activity in the presence of ssDNA.
CC         {ECO:0000269|PubMed:22166102};
CC   -!- SUBUNIT: Monomer in solution. {ECO:0000269|PubMed:22166102}.
CC   -!- DOMAIN: Changes in the ATP-binding site of the helicase domain can
CC       affect the activity of the nuclease domain.
CC       {ECO:0000269|PubMed:22166102}.
CC   -!- SIMILARITY: Belongs to the helicase family. DinG subfamily. Type 2 sub-
CC       subfamily. {ECO:0000255|HAMAP-Rule:MF_02206, ECO:0000305}.
DR   EMBL; BX571856; CAG40464.1; -; Genomic_DNA.
DR   RefSeq; WP_000525060.1; NC_002952.2.
DR   SMR; Q6GGV4; -.
DR   EnsemblBacteria; CAG40464; CAG40464; SAR1466.
DR   KEGG; sar:SAR1466; -.
DR   HOGENOM; HOG000280037; -.
DR   KO; K03722; -.
DR   OMA; VVTNHAM; -.
DR   OrthoDB; 679382at2; -.
DR   BioCyc; SAUR282458:G1G3O-1552-MONOMER; -.
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:0006260; P:DNA replication; IEA:InterPro.
DR   Gene3D; 3.30.420.10; -; 1.
DR   HAMAP; MF_02206; DinG_exonucl; 1.
DR   InterPro; IPR006555; ATP-dep_Helicase_C.
DR   InterPro; IPR006310; DinG.
DR   InterPro; IPR006054; DnaQ.
DR   InterPro; IPR013520; Exonuclease_RNaseT/DNA_pol3.
DR   InterPro; IPR014013; Helic_SF1/SF2_ATP-bd_DinG/Rad3.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR012337; RNaseH-like_sf.
DR   InterPro; IPR036397; RNaseH_sf.
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   1: Evidence at protein level;
KW   ATP-binding; Exonuclease; Hydrolase; Nuclease; Nucleotide-binding.
FT   CHAIN           1..897
FT                   /note="3'-5' exonuclease DinG"
FT                   /id="PRO_0000277594"
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                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   DOMAIN          703..893
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206,
FT                   ECO:0000255|PROSITE-ProRule:PRU00542"
FT   NP_BIND         276..283
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206,
FT                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MOTIF           448..451
FT                   /note="DEAH box"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_02206,
FT                   ECO:0000255|PROSITE-ProRule:PRU00541"
FT   MUTAGEN         10
FT                   /note="D->A: Abolishes nuclease activity; when associated
FT                   with A-12."
FT                   /evidence="ECO:0000269|PubMed:22166102"
FT   MUTAGEN         12
FT                   /note="E->A: Abolishes nuclease activity; when associated
FT                   with A-10."
FT                   /evidence="ECO:0000269|PubMed:22166102"
FT   MUTAGEN         282
FT                   /note="K->A: Almost loss of ATPase activity."
FT                   /evidence="ECO:0000269|PubMed:22166102"
SQ   SEQUENCE   897 AA;  104205 MW;  154CA17030B763EE CRC64;
     MGMATYAVVD LETTGNQLDF DDIIQIGITF VRNNQIIDTY HSMIRTNLEI PPFIQALTSI
     EENMLQQAPY FNQVAEEIYD 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
     DAFKQLFNKD VHFNTFEVNT SLQSAKNTSV FIPSDVASYQ YKNIDEYVAS IVSYIIEYTT
     ITSSKCLVLF TSYKMMHMVQ DMLNELPEFE DYVVLTQQQN QNYKIVQQFN NFDKAILLGT
     STFFEGFDFQ ANGIKCVMIA KLPFMNKHNA KYWLMDSEFT STFKEYVLPD AVTRFRQGLG
     RLIRNENDRG IIVSFDDRLI NSNYKNFFEQ TLENYRQKKG DIQQFGKLLR QIQKKKK
//
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