ID   DGTL1_MYCTO             Reviewed;         431 AA.
AC   P9WNY6; L0TC18; P0A540; P95240;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   25-MAY-2022, entry version 35.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   Name=dgt; OrderedLocusNames=MT2409;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AE000516; AAK46702.1; -; Genomic_DNA.
DR   PIR; A70662; A70662.
DR   RefSeq; WP_003917616.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WNY6; -.
DR   SMR; P9WNY6; -.
DR   EnsemblBacteria; AAK46702; AAK46702; MT2409.
DR   KEGG; mtc:MT2409; -.
DR   PATRIC; fig|83331.31.peg.2597; -.
DR   HOGENOM; CLU_028163_0_1_11; -.
DR   Proteomes; UP000001020; 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_0000427045"
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;  46926 MW;  7578114923038EA2 CRC64;
     MSASEHDPYD DFDRQRRVAE APKTAGLPGT EGQYRSDFAR DRARVLHSAA LRRLADKTQV
     VGPREGDTPR TRLTHSLEVA QIGRGMAIGL GCDLDLVELA GLAHDIGHPP YGHNGERALD
     EVAASHGGFE GNAQNFRILT SLEPKVVDAQ GLSAGLNLTR ASLDAVTKYP WMRADGLGSQ
     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