ID   DGTL1_MYCTA             Reviewed;         431 AA.
AC   A5U533;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   10-JUL-2007, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=MRA_2364;
OS   Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=419947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25177 / H37Ra;
RX   PubMed=18584054; DOI=10.1371/journal.pone.0002375;
RA   Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L.,
RA   Wang H., Wang S., Zhao G., Zhang Y.;
RT   "Genetic basis of virulence attenuation revealed by comparative genomic
RT   analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv.";
RL   PLoS ONE 3:E2375-E2375(2008).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000611; ABQ74133.1; -; Genomic_DNA.
DR   RefSeq; WP_003899281.1; NZ_CP016972.1.
DR   AlphaFoldDB; A5U533; -.
DR   SMR; A5U533; -.
DR   STRING; 419947.MRA_2364; -.
DR   EnsemblBacteria; ABQ74133; ABQ74133; MRA_2364.
DR   GeneID; 45426329; -.
DR   KEGG; mra:MRA_2364; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000001988; 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..431
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000066426"
FT   DOMAIN          72..222
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..36
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   431 AA;  46912 MW;  75796A692301B0A2 CRC64;
     MSASEHDPYD DFDRQRRVAE APKTAGLPGT EGQYRSDFAR DRARVLHSAA LRRLADKTQV
     VGPREGDTPR TRLTHSLEVA QIGRGMAIGL GCDLDLVELA GLAHDIGHPP YGHNGERALD
     EVAASHGGFE GNAQNFRILT SLEPKVVDAQ GLSAGLNLTR ASLDAVTKYP WMRGDGLGSQ
     RRKFGFYDDD RESAVWVRQG APPERACLEA QVMDWADDVA YSVHDVEDGV VSERIDLRVL
     AAEEDAAALA RLGEREFSRV SADELMAAAR RLSRLPVVAA VGKYDATLSA SVALKRLTSE
     LVGRFASAAI ATTRAAAGPG PLVRFRADLQ VPDLVRAEVA VLKILALQFI MSDPRHLETQ
     ARQRERIHRV AHRLYSGAPQ TLDPVYAAAF NTAADDAARL RVVVDQIASY TEGRLERIDA
     DQLGVSRNAL D