ID   DGTL1_ROSDO             Reviewed;         387 AA.
AC   Q164B9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-JUL-2006, sequence version 1.
DT   25-MAY-2022, entry version 89.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=RD1_3167;
OS   Roseobacter denitrificans (strain ATCC 33942 / OCh 114) (Erythrobacter sp.
OS   (strain OCh 114)) (Roseobacter denitrificans).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Roseobacter.
OX   NCBI_TaxID=375451;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33942 / OCh 114;
RX   PubMed=17098896; DOI=10.1128/jb.01390-06;
RA   Swingley W.D., Sadekar S., Mastrian S.D., Matthies H.J., Hao J., Ramos H.,
RA   Acharya C.R., Conrad A.L., Taylor H.L., Dejesa L.C., Shah M.K.,
RA   O'Huallachain M.E., Lince M.T., Blankenship R.E., Beatty J.T.,
RA   Touchman J.W.;
RT   "The complete genome sequence of Roseobacter denitrificans reveals a
RT   mixotrophic rather than photosynthetic metabolism.";
RL   J. Bacteriol. 189:683-690(2007).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000362; ABG32674.1; -; Genomic_DNA.
DR   RefSeq; WP_011569290.1; NZ_FOOO01000004.1.
DR   AlphaFoldDB; Q164B9; -.
DR   SMR; Q164B9; -.
DR   STRING; 375451.RD1_3167; -.
DR   EnsemblBacteria; ABG32674; ABG32674; RD1_3167.
DR   KEGG; rde:RD1_3167; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_1_0_5; -.
DR   OMA; HCKAFRR; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000007029; 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; Reference proteome.
FT   CHAIN           1..387
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000164739"
FT   DOMAIN          62..198
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        11..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   387 AA;  44206 MW;  F498D661800758DE CRC64;
     MTAPYASDPQ RARGRRVKEE ESTFRSSFQR DRDRIIHASA FRRLKHKTQV FIEHEGDYYR
     TRLTHSIEVA QVARTIAGAL NLNQELTEAV ALAHDLGHTP FGHTGEDALS DMMAPYGGFD
     HNAQAIRIVT HLERHYADFD GLNLTWETLE GLAKHNGPVT GDIPWALKAY NDTHDLELGT
     FASAEAQVAA IADDVAYNHH DLHDGLRAEL FSTDELAELP ILNMCFAEVD RLYPGLNYYR
     RRHEALRRFF GVLVEDVIQL AQARLMTLQP KTVTDIRAAD RAIIRFSDDV FDDLKVIRSF
     LFDRMYRAPS VVVMRAQVTR VVEELFPHFM AHPDQLPKQW RKDVEAISSE TELARIVSDY
     ISGMTDRFAL QEHARLIHGT TPTETER