ID   DGTL1_HAES1             Reviewed;         448 AA.
AC   Q0I3A1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-OCT-2006, sequence version 1.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=HS_0964;
OS   Haemophilus somnus (strain 129Pt) (Histophilus somni).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Histophilus.
OX   NCBI_TaxID=205914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=129Pt;
RX   PubMed=17172329; DOI=10.1128/jb.01422-06;
RA   Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O.,
RA   Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N.,
RA   Xie G., Inzana T.J.;
RT   "Complete genome sequence of Haemophilus somnus (Histophilus somni) strain
RT   129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus
RT   influenzae Rd.";
RL   J. Bacteriol. 189:1890-1898(2007).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000436; ABI25239.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q0I3A1; -.
DR   SMR; Q0I3A1; -.
DR   STRING; 205914.HS_0964; -.
DR   EnsemblBacteria; ABI25239; ABI25239; HS_0964.
DR   KEGG; hso:HS_0964; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
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   CDD; cd00077; HDc; 1.
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..448
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138920"
FT   DOMAIN          59..272
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   448 AA;  52219 MW;  39ECC89B10B6D15E CRC64;
     MQINSSWQER FLADPPREKD HRPPFRRDRG RILHSAAFRC LQAKTQIHAI GENDFYRTRL
     THSLEVAQIG SSIVAQMKLI DSFIYLAQQL KEDRADLQKQ LKLILPSNDL IESLCFAHDI
     GHPPFGHGGE VALNYMMRHH GGFEGNAQTF RLLTKLEPYT PNAGMNLTRR TLLGVVKYPT
     ILDRSSPQYH QGVIVDNVDS KYVKISAWKP GKGIFRDDLK MFEWLLEPLS ENDRTLFGQY
     KKERTRPDEV LKTRYKSLDC SIMELADDIA YAVHDLEDAI VVGVVTFQQW QSAVEKLAEC
     RSEWIVQTIS SLSQKLFSEL HYERKNAIGA LVNYFITHVR WKINNGFSEP LLRYNAELPD
     EVIEVLNIFK RFVWEYVIKH VDTQRVEYKG QRMLTEMFQI FDSDPLRLLP RNTAMRWQKA
     TETDRKRIIC DYIAGMSDAY ALRVYQQL