DING_STAAR
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 03-AUG-2022, entry version 120.
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}.
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DR EMBL; BX571856; CAG40464.1; -; Genomic_DNA.
DR RefSeq; WP_000525060.1; NC_002952.2.
DR AlphaFoldDB; Q6GGV4; -.
DR SMR; Q6GGV4; -.
DR KEGG; sar:SAR1466; -.
DR HOGENOM; CLU_012117_1_1_9; -.
DR OMA; VVTNHAM; -.
DR OrthoDB; 679382at2; -.
DR Proteomes; UP000000596; 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 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 MOTIF 448..451
FT /note="DEAH box"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02206,
FT ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 276..283
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
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
