ID   DGTL1_BORPA             Reviewed;         384 AA.
AC   Q7W2B5;
DT   16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 94.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=BPP0073;
OS   Bordetella parapertussis (strain 12822 / ATCC BAA-587 / NCTC 13253).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257311;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12822 / ATCC BAA-587 / NCTC 13253;
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX640423; CAE39814.1; -; Genomic_DNA.
DR   RefSeq; WP_010927275.1; NC_002928.3.
DR   AlphaFoldDB; Q7W2B5; -.
DR   SMR; Q7W2B5; -.
DR   EnsemblBacteria; CAE39814; CAE39814; BPP0073.
DR   KEGG; bpa:BPP0073; -.
DR   HOGENOM; CLU_028163_1_0_4; -.
DR   OMA; HCKAFRR; -.
DR   Proteomes; UP000001421; 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_0000205293"
FT   DOMAIN          73..208
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          12..39
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..39
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   384 AA;  43978 MW;  D6E39B01D89B5966 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 VRMTTKVQRI VRELFQAFLG DPRLLPPDYR REQPQDQARA
     ISDYIAGMTD RYAIREHRRL FEMG