ID   DGTL1_BRUSU             Reviewed;         402 AA.
AC   P63934; G0K9A4; Q8YGR8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 1.
DT   25-MAY-2022, entry version 94.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   Name=dgt; OrderedLocusNames=BR0876, BS1330_I0872;
OS   Brucella suis biovar 1 (strain 1330).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=204722;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=12271122; DOI=10.1073/pnas.192319099;
RA   Paulsen I.T., Seshadri R., Nelson K.E., Eisen J.A., Heidelberg J.F.,
RA   Read T.D., Dodson R.J., Umayam L.A., Brinkac L.M., Beanan M.J.,
RA   Daugherty S.C., DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R.,
RA   Nelson W.C., Ayodeji B., Kraul M., Shetty J., Malek J.A., Van Aken S.E.,
RA   Riedmuller S., Tettelin H., Gill S.R., White O., Salzberg S.L.,
RA   Hoover D.L., Lindler L.E., Halling S.M., Boyle S.M., Fraser C.M.;
RT   "The Brucella suis genome reveals fundamental similarities between animal
RT   and plant pathogens and symbionts.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:13148-13153(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=1330;
RX   PubMed=22038969; DOI=10.1128/jb.06181-11;
RA   Tae H., Shallom S., Settlage R., Preston D., Adams L.G., Garner H.R.;
RT   "Revised genome sequence of Brucella suis 1330.";
RL   J. Bacteriol. 193:6410-6410(2011).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AE014291; AAN29804.1; -; Genomic_DNA.
DR   EMBL; CP002997; AEM18221.1; -; Genomic_DNA.
DR   RefSeq; WP_004683694.1; NZ_KN046804.1.
DR   AlphaFoldDB; P63934; -.
DR   SMR; P63934; -.
DR   EnsemblBacteria; AEM18221; AEM18221; BS1330_I0872.
DR   GeneID; 45051939; -.
DR   GeneID; 55590581; -.
DR   KEGG; bms:BR0876; -.
DR   KEGG; bsi:BS1330_I0872; -.
DR   PATRIC; fig|204722.21.peg.2569; -.
DR   HOGENOM; CLU_028163_1_0_5; -.
DR   OMA; HCKAFRR; -.
DR   PhylomeDB; P63934; -.
DR   Proteomes; UP000007104; Chromosome I.
DR   GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   HAMAP; MF_01212; dGTPase_type2; 1.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR023023; dNTPase_2.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR006675; HDIG_dom.
DR   InterPro; IPR026875; PHydrolase_assoc_dom.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF13286; HD_assoc; 1.
DR   SMART; SM00471; HDc; 1.
DR   TIGRFAMs; TIGR01353; dGTP_triPase; 1.
DR   TIGRFAMs; TIGR00277; HDIG; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..402
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_0000205297"
FT   DOMAIN          73..217
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          20..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   402 AA;  45727 MW;  283F7B5E0FE206D4 CRC64;
     MSLEGIGFGY RERAPYASNP AFSRGRLVPE PESPTRTPFQ RDRDRIIHST AFRRLKHKTQ
     VFIAHEGDHY RTRLTHTIEV AQIARALARA LRLDEDLAEA VALVHDFGHT PFGHTGEDAL
     NERMKNFGGF DHNAQSLRIV TKLEHRYADF DGLNLSWETL EGLVKHNGPL LGPYAAHPDI
     PVPQPILDFN ARYDLELSRF ASLEAQCAAI ADDIAYNAHD IDDGLRAGLL TLESLDEVPL
     AKRLLDIVRT RYPNLDPVRT GHELVRRQIT IMVEDVIEEA QRRLASARPG TMEDVHNQPR
     ALVGFSDAMR AEEKVLKRFL FKNLYFHESV VVRRHAADRI VQDLFDACFT DPSLMPDEWR
     LGCEALDKAA LARRVADYLA GMTDNYAVRE HRRLFDRTPD LA