ID   DGTL1_MYCLE             Reviewed;         429 AA.
AC   Q9CCG3;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   25-MAY-2022, entry version 99.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=ML0831;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AL583919; CAC30341.1; -; Genomic_DNA.
DR   PIR; A87013; A87013.
DR   RefSeq; NP_301628.1; NC_002677.1.
DR   RefSeq; WP_010907952.1; NC_002677.1.
DR   AlphaFoldDB; Q9CCG3; -.
DR   SMR; Q9CCG3; -.
DR   STRING; 272631.ML0831; -.
DR   PRIDE; Q9CCG3; -.
DR   EnsemblBacteria; CAC30341; CAC30341; CAC30341.
DR   KEGG; mle:ML0831; -.
DR   PATRIC; fig|272631.5.peg.1533; -.
DR   Leproma; ML0831; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   OMA; FGVYEDD; -.
DR   Proteomes; UP000000806; 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; IPR006675; HDIG_dom.
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   TIGRFAMs; TIGR00277; HDIG; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase; Reference proteome.
FT   CHAIN           1..429
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_0000205308"
FT   DOMAIN          76..226
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   429 AA;  46964 MW;  A25CAFBD66AED816 CRC64;
     MTTKANTNQH DPYDDFDRQR RAHEAPKTAV LPGSEGQHRT EFARDRARVL HSAALRRLSD
     KTQVVGPHEG DTPRTRLTHS LEVAQIGRSM AVGLGCDLDL VELAGLAHDI GHPPYGHNGE
     RALDEVAVGY GGFEGNAQNF RILTSLEPKV IDEQGCSVGL NLTRASLDAV TKYPWTRVGG
     LGHGRSKYGF YEEDRDPADW VRVYAPANRA CLEAQVMDWA DDVAYSVHDV EDGVVSQRID
     LRVLADEYET AALAKLGEGE FSWVTADELM AAAHRLSELP VVAAVGKYDA TLASSVALKR
     LTSELVGRFA SVAIATTRAV AGPGPLVRYQ ADLQVPDLVR AEVAVLKILA LQFIMSDPRH
     LEGQARQRER IHRVANWLYS GAPSTLDPVF VTAFTTAVDD NARWRVIVDQ IASYTEGRLE
     RIDAGQASP