ID   DGTL1_ALIFM             Reviewed;         448 AA.
AC   B5FFM1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-OCT-2008, sequence version 1.
DT   25-MAY-2022, entry version 70.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=VFMJ11_1806;
OS   Aliivibrio fischeri (strain MJ11) (Vibrio fischeri).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=388396;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MJ11;
RA   Mandel M.J., Stabb E.V., Ruby E.G., Ferriera S., Johnson J., Kravitz S.,
RA   Beeson K., Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RT   "Complete sequence of Vibrio fischeri strain MJ11.";
RL   Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; CP001139; ACH66450.1; -; Genomic_DNA.
DR   RefSeq; WP_012533735.1; NC_011184.1.
DR   AlphaFoldDB; B5FFM1; -.
DR   SMR; B5FFM1; -.
DR   EnsemblBacteria; ACH66450; ACH66450; VFMJ11_1806.
DR   GeneID; 64243839; -.
DR   KEGG; vfm:VFMJ11_1806; -.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   Proteomes; UP000001857; Chromosome I.
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..448
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138939"
FT   DOMAIN          67..260
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   448 AA;  51400 MW;  DD7FE4B4F8A53087 CRC64;
     MNKPNEITLS PHWEDRISNE QKLRRNDQRS VFQRDRARIL HSAAFRRLQA KTQVHGPGSA
     NDFYRTRLTH SLEVSQIGTG VVAQLKLRQP EFRALLTSTS LMESICLAHD IGHPPFGHGG
     EIALNYMMRD HGGFEGNGQT LRILSKLEPY TEHFGMNLAR RTLLGVLKYP AFLDQVHSTE
     RPQEVSNVRH LKSIDWHPPK GVYRDDADIL NWILKPLSDV DKALFSTFRF QQESQHTHRK
     TRFKSIDCSI MELADDIAYG VHDLEDAIVM GIVTRNQWQE SVASKLAECG DEWFEANIET
     ISDKLFSGLQ YQRKDGIGSI VNALLTSITI KPTTFNDEPE FESELLRWNA FLSPSMSYAL
     EVLKKFVGQF VIHNSEMQRI EYKGQQIVME IFDALNSDPE RLLPENDKRE WREAKESGAN
     AHRVIADYIA GMTDGYAQRL YNQLFVPI