ID   DGTL1_BORBR             Reviewed;         384 AA.
AC   Q7WR83;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=BB0073;
OS   Bordetella bronchiseptica (strain ATCC BAA-588 / NCTC 13252 / RB50)
OS   (Alcaligenes bronchisepticus).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-588 / NCTC 13252 / RB50;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; BX640437; CAE30575.1; -; Genomic_DNA.
DR   RefSeq; WP_003806949.1; NC_002927.3.
DR   AlphaFoldDB; Q7WR83; -.
DR   SMR; Q7WR83; -.
DR   STRING; 257310.BB0073; -.
DR   EnsemblBacteria; CAE30575; CAE30575; BB0073.
DR   GeneID; 45390313; -.
DR   KEGG; bbr:BB0073; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_1_0_4; -.
DR   OMA; HCKAFRR; -.
DR   Proteomes; UP000001027; Chromosome.
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; 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   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase.
FT   CHAIN           1..384
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_0000205292"
FT   DOMAIN          73..208
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          13..42
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..42
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  43949 MW;  D6F48C01CF8C5966 CRC64;
     MNKDGTVVLM NELASYASDP SKTRGRRHSE PPPENRTEFQ RDRDRIIHSN AFRRLEYKTQ
     VFVNHEGDLF RTRLTHSLEV AQIARTLARS LRVSEDLTEA IALAHDLGHT PFGHAGQDEL
     NACMRELAPQ AGGFEHNLQS LRVVDELEER YAEFNGLNLC FETREGILKH CSATHARQLG
     AVGERFLDRT QPSLEAQLAN LADEVAYNNH DVDDGLRSGL ITLEQLQEVG IFARHYAEVA
     RRYPQLAPRR ATSETIRRMI NTLIVDLTAT SLARIRDHAP ASADDVRRAP PLAGFSAAVR
     READELKKFL FDNLYRHYRV VRMTTKAQRI VRELFQAFLG DPRLLPPDYR REQPQDQARA
     ISDYIAGMTD RYAIREHRRL FEMG