ID   DGTL1_ALISL             Reviewed;         448 AA.
AC   B6EJ48;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   25-NOV-2008, sequence version 1.
DT   25-MAY-2022, entry version 69.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=VSAL_I1091;
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238;
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; FM178379; CAQ78776.1; -; Genomic_DNA.
DR   RefSeq; WP_012549845.1; NC_011312.1.
DR   AlphaFoldDB; B6EJ48; -.
DR   SMR; B6EJ48; -.
DR   STRING; 316275.VSAL_I1091; -.
DR   EnsemblBacteria; CAQ78776; CAQ78776; VSAL_I1091.
DR   KEGG; vsa:VSAL_I1091; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000001730; Chromosome 1.
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_1000138913"
FT   DOMAIN          67..260
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
SQ   SEQUENCE   448 AA;  51693 MW;  6787D8BB048FD764 CRC64;
     MNKTIDITLS PHWEDRISNE QKLRRNDQRS VFQRDRARIL HSAAFRRLQA KTQVHGPGSA
     NDFYRTRLTH SLEVSQIGTG IVAQLKLRQP EFRHLLTSTS LMESICLAHD IGHPPFGHGG
     EIALNYMMRN HGGFEGNGQT LRILSKLEPY TEHFGMNLAR RTLMGVLKYP AFLDQVHSKY
     RPDDVTNLRH LKSIEWHPPK GIYRDDESIL HWITAPLSEA DKTLFSTFRF QKENDKVHKK
     TRFKSIDCSI MELADDIAYG IHDLEDAIVM GIVTRNQWQE SVASKLAECG DEWFEAHINN
     IGDKLFSGLQ YQRKDGIGGM VNALLTSITI QKSTFEEEQS FESELLKWNA YLSPSMSYAL
     NILKKFVGQY VIHNSEMQRI EYKGQQIVME IFDALNSDPE RLLPENDKRE WREAKESGTN
     HHRIIADYIA GMTDGYAQRL YNQLFVPI