ID   DNS2_BURPS              Reviewed;         350 AA.
AC   Q63IT3;
DT   04-APR-2006, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2004, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Putative deoxyribonuclease-2;
DE            EC=3.1.-.-;
DE   AltName: Full=Deoxyribonuclease II;
GN   OrderedLocusNames=BPSS1983;
OS   Burkholderia pseudomallei (strain K96243).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia; pseudomallei group.
OX   NCBI_TaxID=272560;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=K96243;
RX   PubMed=15377794; DOI=10.1073/pnas.0403302101;
RA   Holden M.T.G., Titball R.W., Peacock S.J., Cerdeno-Tarraga A.-M.,
RA   Atkins T., Crossman L.C., Pitt T., Churcher C., Mungall K.L., Bentley S.D.,
RA   Sebaihia M., Thomson N.R., Bason N., Beacham I.R., Brooks K., Brown K.A.,
RA   Brown N.F., Challis G.L., Cherevach I., Chillingworth T., Cronin A.,
RA   Crossett B., Davis P., DeShazer D., Feltwell T., Fraser A., Hance Z.,
RA   Hauser H., Holroyd S., Jagels K., Keith K.E., Maddison M., Moule S.,
RA   Price C., Quail M.A., Rabbinowitsch E., Rutherford K., Sanders M.,
RA   Simmonds M., Songsivilai S., Stevens K., Tumapa S., Vesaratchavest M.,
RA   Whitehead S., Yeats C., Barrell B.G., Oyston P.C.F., Parkhill J.;
RT   "Genomic plasticity of the causative agent of melioidosis, Burkholderia
RT   pseudomallei.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:14240-14245(2004).
RN   [2]
RP   DISCUSSION OF SEQUENCE.
RX   PubMed=12594037; DOI=10.1016/s0378-1119(02)01233-7;
RA   MacLea K.S., Krieser R.J., Eastman A.;
RT   "A family history of deoxyribonuclease II: surprises from Trichinella
RT   spiralis and Burkholderia pseudomallei.";
RL   Gene 305:1-12(2003).
CC   -!- MISCELLANEOUS: Unlike their eukaryotic orthologs the putative
CC       Burkholderia deoxyribonuclease-2 are probably not secreted from the
CC       cell, as they do not have a signal sequence.
CC   -!- SIMILARITY: Belongs to the DNase II family. {ECO:0000305}.
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DR   EMBL; BX571966; CAH39461.1; -; Genomic_DNA.
DR   RefSeq; WP_004524950.1; NZ_CP009537.1.
DR   RefSeq; YP_111989.1; NC_006351.1.
DR   AlphaFoldDB; Q63IT3; -.
DR   SMR; Q63IT3; -.
DR   STRING; 272560.BPSS1983; -.
DR   EnsemblBacteria; CAH39461; CAH39461; BPSS1983.
DR   GeneID; 56531902; -.
DR   KEGG; bps:BPSS1983; -.
DR   PATRIC; fig|272560.51.peg.5488; -.
DR   OMA; ILYNDQK; -.
DR   Proteomes; UP000000605; Chromosome 2.
DR   GO; GO:0004531; F:deoxyribonuclease II activity; IEA:InterPro.
DR   InterPro; IPR004947; DNase_II.
DR   PANTHER; PTHR10858; PTHR10858; 1.
DR   Pfam; PF03265; DNase_II; 1.
PE   3: Inferred from homology;
KW   Endonuclease; Hydrolase; Nuclease; Reference proteome.
FT   CHAIN           1..350
FT                   /note="Putative deoxyribonuclease-2"
FT                   /id="PRO_0000230669"
SQ   SEQUENCE   350 AA;  38837 MW;  4B5B6D59757B1B53 CRC64;
     MTISPRDEQN RSVDLWFAYK VPKLTKDTDS DSATGYEYVY YDREIGSVQK SPNRMNNPKG
     ALFYTLDSIF GDPGSTTGWI LYNDEMPADA DRSNNATLGH TKGVIAFDIA SNSALWLLHS
     WPKYTSPSAP GVPTPLYGQT FLCVSLDLET AGKIAAQMAL HQQPQVYLPR TAGLDHASPL
     YTLTQPLNAS APGDSDSLDF KTRGGAPFKV IAKNRKWGKD FWNDLVGPTL KADMDVETWI
     RGKIPPILDS DGVHKTYDIK FIDLRKLGAP WAWPETQDHA KWGITTTDDW VCVGDINRMV
     TQEKRGGGTI AFQDPQLWKA LSQTDLIVPP PGKTEAQARA MIHRTHQPAD