ID   DGTL1_MYCSJ             Reviewed;         423 AA.
AC   A3Q255;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 81.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=Mjls_3454;
OS   Mycobacterium sp. (strain JLS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164757;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JLS;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Miller C.D., Anderson A.J.,
RA   Sims R.C., Richardson P.;
RT   "Complete sequence of Mycobacterium sp. JLS.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000580; ABN99232.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3Q255; -.
DR   SMR; A3Q255; -.
DR   STRING; 164757.Mjls_3454; -.
DR   KEGG; mjl:Mjls_3454; -.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   BioCyc; MSP164757:G1G8C-3484-MON; -.
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..423
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000066423"
FT   DOMAIN          72..217
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..21
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   423 AA;  45944 MW;  1D1A1117989EECA5 CRC64;
     MNPRLQDSYD EFDRQRRVDE PAKSAVLPGT GTEHRTDFAR DRARVLHCAA LRRLADKTQV
     VGPREGDTPR TRLTHSLEVA QIGRGMAVGL GCDPDLVDLA GLAHDIGHPP YGHNGERALN
     EIAKAFGGFE GNAQNFRILT RLEPKVLDAT GRSAGLNLTR AALDAVTKYP WQRGDRTKFG
     FYGDDMAAAR WVRDGAPAER PCLEAQVMDW ADDVAYSVHD VEDGVVSGRI DLRVLADDDA
     AASLARLGAE AFPTLAPDDL LAAAERLSQM PVVSQVGKYD GTLGASVALK RMTSELVGRF
     ANAAITETRS VAGGGALHRF DTELAVPTLV RAEVAVLKML ALQFIMSDHG HLGIQADQRT
     RIHEVALILW GQAPSSLDPL FAPEFVAAED DGARLRVVID QIASYTEGRL ERVHEARSPR
     PLD