DING_STAAS
ID DING_STAAS Reviewed; 897 AA.
AC Q6G9A7;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 115.
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=SAS1398;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
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).
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; BX571857; CAG43174.1; -; Genomic_DNA.
DR RefSeq; WP_000525081.1; NC_002953.3.
DR AlphaFoldDB; Q6G9A7; -.
DR SMR; Q6G9A7; -.
DR KEGG; sas:SAS1398; -.
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_0000277595"
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