ID   DGTL1_SHEWM             Reviewed;         444 AA.
AC   B1KEG7;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   25-MAY-2022, entry version 72.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=Swoo_2264;
OS   Shewanella woodyi (strain ATCC 51908 / MS32).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=392500;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51908 / MS32;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA   Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Lykidis A., Zhao J.-S., Richardson P.;
RT   "Complete sequence of Shewanella woodyi ATCC 51908.";
RL   Submitted (FEB-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; CP000961; ACA86545.1; -; Genomic_DNA.
DR   RefSeq; WP_012324888.1; NC_010506.1.
DR   AlphaFoldDB; B1KEG7; -.
DR   SMR; B1KEG7; -.
DR   STRING; 392500.Swoo_2264; -.
DR   PRIDE; B1KEG7; -.
DR   EnsemblBacteria; ACA86545; ACA86545; Swoo_2264.
DR   KEGG; swd:Swoo_2264; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000002168; 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; Reference proteome.
FT   CHAIN           1..444
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138936"
FT   DOMAIN          59..250
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..26
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   444 AA;  51066 MW;  0C94694AE97C56E1 CRC64;
     MIASPWHERR LNEDKKRRND HRSPFQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
     THSLEVSQIG TGIRAQLKLK QPQHLPLFDS MSLIESLCLA HDIGHPPFGH GGEVALNYMM
     RNHGGFEGNG QTFRILTGLE PYTECFGMNL CRRTLLGVLK YPGLYSSLHH NSQQAEVNNI
     RQLKPADWPP VKGVFDDDKA ILDWVLAPLI DSDRERFLQT HTAATGKHKR TRYKSLDCSI
     MELADDIAYA VHDLEDAIVM GIVSSFQWHS DVTETLKNSK DSWIREEFAT IGDKLFSHHH
     HQRKDAIGTL VNGFVTAIDL KEDLAFTEPL LRFNAALDDE FDSALEVLKQ FVYKFVIRKP
     EIQMLEYKGQ QTVMELFEAF ESDPERLLPT HTQERWRESH NKGLNCHRVI ADYISGMTDE
     FAARLHQQLF SPKLGSMIEL SHEL