ID   DGT1B_VIBCH             Reviewed;         402 AA.
AC   Q9KMM3;
DT   06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein 2 {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=VC_A0308;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AE003853; AAF96216.1; -; Genomic_DNA.
DR   PIR; F82473; F82473.
DR   RefSeq; NP_232704.1; NC_002506.1.
DR   RefSeq; WP_000272282.1; NZ_LT906615.1.
DR   AlphaFoldDB; Q9KMM3; -.
DR   SMR; Q9KMM3; -.
DR   STRING; 243277.VC_A0308; -.
DR   PRIDE; Q9KMM3; -.
DR   DNASU; 2611913; -.
DR   EnsemblBacteria; AAF96216; AAF96216; VC_A0308.
DR   KEGG; vch:VC_A0308; -.
DR   PATRIC; fig|243277.26.peg.2944; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; AQLMDLC; -.
DR   BioCyc; VCHO:VCA0308-MON; -.
DR   Proteomes; UP000000584; Chromosome 2.
DR   GO; GO:0008832; F:dGTPase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..402
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein 2"
FT                   /id="PRO_0000205327"
FT   DOMAIN          72..215
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   402 AA;  45908 MW;  881A9411457C1A18 CRC64;
     MYDSEVIEYA KEQENIISKL EYRVYKHDDG RSVNRQDLMR DYARVLYSSS FRRLQGKMQL
     LGVDASKFNR NRLTHSLEVA QIARSIAYDL ELNHTVVAET ASLAHDIGNP PFGHYGEVVL
     NDLSLACGGY EGNAQAFRIL RTLEKKHYAY PGLNLNVRTL MAITKYFFNK HQNNKKFLYD
     ADYEFLKTEL DSKGVTVTKS IDAEIMDLAD EIAYAAHDLE DALSFGMISL GEIVHEFSIS
     DKFKDAYPTM TDIAKEAQNV AMKASRSGTS EEYAIVLKKE LTSMIVNILC SDIGLVDGCL
     GYKRHAKLAE GLKKLLFKAI LRKKDIQLYE RRGEQIIRGL FEVYSDEKYN KDNMLLPPEL
     RAINDCKTRL VTDYISGMMD SYAAQEYEKY FGKGSADKLY FK