DING_STAEQ
ID DING_STAEQ Reviewed; 902 AA.
AC Q5HP88;
DT 06-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=SERP1025;
OS Staphylococcus epidermidis (strain ATCC 35984 / RP62A).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176279;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35984 / RP62A;
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; CP000029; AAW54401.1; -; Genomic_DNA.
DR RefSeq; WP_001831318.1; NC_002976.3.
DR AlphaFoldDB; Q5HP88; -.
DR SMR; Q5HP88; -.
DR STRING; 176279.SERP1025; -.
DR EnsemblBacteria; AAW54401; AAW54401; SERP1025.
DR GeneID; 50018734; -.
DR KEGG; ser:SERP1025; -.
DR eggNOG; COG0847; Bacteria.
DR eggNOG; COG1199; Bacteria.
DR HOGENOM; CLU_012117_1_1_9; -.
DR OMA; VVTNHAM; -.
DR OrthoDB; 679382at2; -.
DR Proteomes; UP000000531; 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..902
FT /note="3'-5' exonuclease DinG"
FT /id="PRO_0000277601"
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 902 AA; 105327 MW; 294CCB8A8206A2A7 CRC64;
MGIATFAVVD LETTGNQLDY DEIIQIGITF VRQNQVIDTY HSMIRTDLEI PPFIQALTSI
EEEMLVQAPY FNEVADDIYQ LIKDCVFVAH NISFDLNFIK KAFEKCNIQF KPKRVMDTLE
LFKIAFPTDK SYQLSALAES HHIPLNNAHR ADEDATTTAK LMIKAFEKFE QLHLDTQKQL
YYLSKNLKYD LYHILFEMVR NYQTKPPNNQ FEQFEQIIYR KQIDLKKPAV NFDGTLKDLY
KNVTQSLNLT YRPQQLYLAE IILDQLMHSD KAMIEAPLGS GKSLAYLLAA TMYNIETGRH
VMISTNTKLL QSQLLEKDIP LLNDVLDFKI NASLIKSKND YISLGLISQI LKDDTNNYEV
SILKMQLLIW ITETNTGDIQ ELNLKGGQKM YVDQKIETYV PVRHDIHYYN YIKRNAQNIQ
IGITNHAHLI HSDSENTIYQ LFDDCIIDEA HRLPDYALNQ VTNDLNYSDV KYQLGLIGKN
ENEKLLKAVD KLEQQRILEK LDIAPIDVFG LKININELHD LNEQLFTTIY NIIQTSDVYD
DDIHKYHYVY DFETGEILKD LRAIIDKLNK TIEIFNGMNH KTIKSVRKQL LYLHDKFKLI
EQSIKDHHTS FISIKNLAQK STIRLLVKDY DVKDILTKQV LEKFKSLTFI SGTLTFNHSF
KAFQNWFNED IDFNTFEIST PLTSSNHTNV FVPNDVETYN YKNLDDYVAS IVDYIVEYIT
VTQSKCLVLF TSYKMMHMVQ DLLNELPELE DYVILTQQQN QNYKIVQQFN NFDKSILLGT
STFFEGFDFQ ANGLKCVMIA KLPFMNKHNI KYWLMDSEFT STFKDYVLPD AVTRFRQGLG
RLIRHEDDKG LIVSFDDRLV NSTYKSFFAQ SLEHFKQRKG NIKQFNKLLN QIQRSIDNES
KS
