ID   DGTL1_MYCUA             Reviewed;         425 AA.
AC   A0PNR5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=MUL_1458;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA   Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C., Jones L.M.,
RA   Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(2007).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP000325; ABL03984.1; -; Genomic_DNA.
DR   RefSeq; WP_011739604.1; NC_008611.1.
DR   AlphaFoldDB; A0PNR5; -.
DR   SMR; A0PNR5; -.
DR   STRING; 362242.MUL_1458; -.
DR   EnsemblBacteria; ABL03984; ABL03984; MUL_1458.
DR   KEGG; mul:MUL_1458; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   Proteomes; UP000000765; 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..425
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000066427"
FT   DOMAIN          72..218
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..35
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   425 AA;  46129 MW;  1F9157D744437FAA CRC64;
     MSTKQQEPYG DFDRQRRVVE APKTAGLPGT EGQHRTDFAR DRARVLHCAA LRRLADKTQV
     VGPREGDTPR TRLTHSLEVA QIGRGMAIGL GCDLDLVELA GLAHDIGHPP YGHNGERALD
     EVAIGCGGFE GNAQNFRILT SLEPKVLDEH GLSVGLNLTR AALDAVTKYP WPRGRARRKF
     GFYDQDLQPA LWVRQGAPQR RPCLEAQVMD WADDVAYSVH DVEDGVVSER IDLRVLADHD
     EAAALAKLGE SEFSRVSADE LMEAAGRLSG LPVVAAVGKY DATLAASVAL KQLTSELVGR
     FASAAIATTR AAAGPGPLVR YQADLHVPEL VRAEVAVLKI LALQFIMSDP RHLETQARQR
     ERIHRVAQLL YAGAPRTLDP IFAAAFNAAG DDGARMRVVV DQIASYTEGR LERIDAAQLG
     DGRVG