ID   DGTL1_MYCSS             Reviewed;         423 AA.
AC   Q1B6D4;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   11-JUL-2006, 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=Mmcs_3443;
OS   Mycobacterium sp. (strain MCS).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; unclassified Mycobacterium.
OX   NCBI_TaxID=164756;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS;
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   Martinez M., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Kim E., Miller C.D., Hughes J.E., Anderson A.J., Sims R.C., Richardson P.;
RT   "Complete sequence of chromosome of Mycobacterium sp. MCS.";
RL   Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP000384; ABG09550.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q1B6D4; -.
DR   SMR; Q1B6D4; -.
DR   KEGG; mmc:Mmcs_3443; -.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   BioCyc; MSP164756:G1G6O-3513-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_1000066425"
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;  45958 MW;  1D1B01568B2D12C5 CRC64;
     MNPRLQDSYD EFDRQRRVDE PAKSAVLPGT GTEHRTDFAR DRARVLHCAA LRRLADKTQV
     VGPREGDTPR TRLTHSLEVA QIGRGMAVGL GCDPDLVDLA GLAHDIGHPP YGHNGERALN
     EIAKAFGGFE GNAQNFRILT RLEPKVLDAT GRSAGLNLTR AALDAVTKYP WQRGDRTKFG
     FYGDDMAAAW WVRDGAPAER PCLEAQVMDW ADDVAYSVHD VEDGVVSGRI DLRVLADDDA
     AASLARLGAE AFPTLAPDDL LAAAERLSQM PVVSQVGKYD GTLGASVALK RMTSELVGRF
     ANAAITETRS VAGGGALHRF VTELAVPTLV RAEVAVLKML ALQFIMSDHG HLGIQADQRT
     RIHEVALILW GQAPSSLDPL FAPEFVAAED DGARLRVVID QIASYTEGRL ERVHEARSPR
     PLD