ID   DGTL1_HAEIG             Reviewed;         461 AA.
AC   A5UF19;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=CGSHiGG_01465;
OS   Haemophilus influenzae (strain PittGG).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=374931;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PittGG;
RX   PubMed=17550610; DOI=10.1186/gb-2007-8-6-r103;
RA   Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C.,
RA   Ehrlich G.D.;
RT   "Characterization and modeling of the Haemophilus influenzae core and
RT   supragenomes based on the complete genomic sequences of Rd and 12 clinical
RT   nontypeable strains.";
RL   Genome Biol. 8:R103.1-R103.18(2007).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000672; ABQ99374.1; -; Genomic_DNA.
DR   RefSeq; WP_011962154.1; NC_009567.1.
DR   AlphaFoldDB; A5UF19; -.
DR   SMR; A5UF19; -.
DR   EnsemblBacteria; ABQ99374; ABQ99374; CGSHiGG_01465.
DR   KEGG; hiq:CGSHiGG_01465; -.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   Proteomes; UP000001990; Chromosome.
DR   GO; GO:0008832; F:dGTPase activity; IEA:InterPro.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IEA:InterPro.
DR   HAMAP; MF_01212; dGTPase_type2; 1.
DR   InterPro; IPR006261; dNTPase.
DR   InterPro; IPR020779; dNTPase_1.
DR   InterPro; IPR023023; dNTPase_2.
DR   InterPro; IPR003607; HD/PDEase_dom.
DR   InterPro; IPR006674; HD_domain.
DR   InterPro; IPR026875; PHydrolase_assoc_dom.
DR   PANTHER; PTHR11373:SF32; PTHR11373:SF32; 1.
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..461
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000073115"
FT   DOMAIN          72..285
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          22..41
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        24..41
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   461 AA;  53478 MW;  A18E6652135A12AB CRC64;
     MQKNEIKQID MKPLIIDSSW TERFLPDPPR EKDNRPPFRR DRGRILHSAA FRCLQAKTQI
     HSIGENDFYR TRLTHSLEVA QIGSSLVAQL KFLETFESLS QTLNIDKNEL QKQLKPLLPS
     NDLIESLCFA HDIGHPPFGH GGETALNYMM AEQGGFEGNA QTFRILTKLE PYTENAGMNL
     TRRTLLGVVK YPALLDVASP QYAELNFSRN IDARFVRIHD WIPGKGIFRD DLKMFNWLLE
     NLSENDRTLF CQFKKVRENP AESLHTRFKS LDCSIMELAD DIAYGVHDLE DAIVTGMVNP
     HQWQAAHSAL KQIPSAWLHE NIDSISQRLF SDKHFERKQA IGALVNFFIT NVRWKLTANF
     DEPLLRYNAE LSPEVIVALG VFKKFVWDYV IRNVDTQRIE YKGQRMLTEM FQIFESDPER
     LLPRNTANRW RNAPEERKKR IICDYIAGMS DAHALRVYQQ L