DING_STAAC
ID DING_STAAC Reviewed; 897 AA.
AC Q5HFW8;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 125.
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=SACOL1495;
OS Staphylococcus aureus (strain COL).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93062;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=COL;
RX PubMed=15774886; DOI=10.1128/jb.187.7.2426-2438.2005;
RA Gill S.R., Fouts D.E., Archer G.L., Mongodin E.F., DeBoy R.T., Ravel J.,
RA Paulsen I.T., Kolonay J.F., Brinkac L.M., Beanan M.J., Dodson R.J.,
RA Daugherty S.C., Madupu R., Angiuoli S.V., Durkin A.S., Haft D.H.,
RA Vamathevan J.J., Khouri H., Utterback T.R., Lee C., Dimitrov G., Jiang L.,
RA Qin H., Weidman J., Tran K., Kang K.H., Hance I.R., Nelson K.E.,
RA Fraser C.M.;
RT "Insights on evolution of virulence and resistance from the complete genome
RT analysis of an early methicillin-resistant Staphylococcus aureus strain and
RT a biofilm-producing methicillin-resistant Staphylococcus epidermidis
RT strain.";
RL J. Bacteriol. 187:2426-2438(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; CP000046; AAW36690.1; -; Genomic_DNA.
DR RefSeq; WP_000525078.1; NC_002951.2.
DR AlphaFoldDB; Q5HFW8; -.
DR SMR; Q5HFW8; -.
DR EnsemblBacteria; AAW36690; AAW36690; SACOL1495.
DR KEGG; sac:SACOL1495; -.
DR HOGENOM; CLU_012117_1_1_9; -.
DR OMA; VVTNHAM; -.
DR Proteomes; UP000000530; 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; 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 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_0000277593"
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; 104218 MW; 13D81550EDCB683D 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
RLIRNENDRG IIVSFDDRLI NSNYKNFFEQ TLENYRQKKG DIQQFGKLLR QIQKKKK