ID   DGTL1_CORGB             Reviewed;         424 AA.
AC   A4QFY0;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 83.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=cgR_2144;
OS   Corynebacterium glutamicum (strain R).
OC   Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC   Corynebacterium.
OX   NCBI_TaxID=340322;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=R;
RX   PubMed=17379713; DOI=10.1099/mic.0.2006/003657-0;
RA   Yukawa H., Omumasaba C.A., Nonaka H., Kos P., Okai N., Suzuki N., Suda M.,
RA   Tsuge Y., Watanabe J., Ikeda Y., Vertes A.A., Inui M.;
RT   "Comparative analysis of the Corynebacterium glutamicum group and complete
RT   genome sequence of strain R.";
RL   Microbiology 153:1042-1058(2007).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AP009044; BAF55146.1; -; Genomic_DNA.
DR   RefSeq; WP_011897627.1; NC_009342.1.
DR   AlphaFoldDB; A4QFY0; -.
DR   SMR; A4QFY0; -.
DR   EnsemblBacteria; BAF55146; BAF55146; cgR_2144.
DR   KEGG; cgt:cgR_2144; -.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   PhylomeDB; A4QFY0; -.
DR   Proteomes; UP000006698; 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   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..424
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138917"
FT   DOMAIN          67..217
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  46171 MW;  F09615AA9C11F9A7 CRC64;
     MYPYSDADAF RRHPERAKSS QLRTSAVDTR SAFARDRARV LHSAALRRLA DKTQVVGPND
     GDTPRTRLTH SLEVAQIARG IGAGLDLDPD LCDLAGLCHD IGHPPYGHNG ENALNEVAAA
     CGGFEGNAQT LRILTRLEPK IVSDEGASFG LNLSRAALDA ACKYPWAKTN ADGSVNKKYS
     AYDEDAEILD WIRQGHEDLR PPIEAQVMDF SDDIAYSVHD VEDGIVSGRI DLKVLWDLVE
     LAALADKGAA AFGGSPAELI EGAASLRELP VVAAAADFDF SLRSYAALKA MTSELVGRYV
     GSTIESTKKT HAGIDVGRMY GDLIIPETAA SEVKLLKTLA VLYVMDDPGH LARQNRQRDR
     IFRVFDYLVL GAPGSLDPMY RQWFIEANSE SEQIRVIVDQ IASMTESRLE RLARNAADIS
     GFLG