ID   DGTL1_SHESW             Reviewed;         449 AA.
AC   A1RJX1;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   06-FEB-2007, sequence version 1.
DT   25-MAY-2022, entry version 77.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=Sputw3181_2138;
OS   Shewanella sp. (strain W3-18-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=351745;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=W3-18-1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Lykidis A., Tiedje J., Richardson P.;
RT   "Complete sequence of Shewanella sp. W3-18-1.";
RL   Submitted (DEC-2006) 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; CP000503; ABM24966.1; -; Genomic_DNA.
DR   RefSeq; WP_011789436.1; NC_008750.1.
DR   AlphaFoldDB; A1RJX1; -.
DR   SMR; A1RJX1; -.
DR   PRIDE; A1RJX1; -.
DR   GeneID; 45042327; -.
DR   KEGG; shw:Sputw3181_2138; -.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   Proteomes; UP000002597; 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..449
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138935"
FT   DOMAIN          59..255
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..25
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..25
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  51405 MW;  16F8AFA4F3D11F35 CRC64;
     MTSSVWQERR HGEDKQRRFD HRSPYQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
     THSLEVSQIG TGIAAQLRRK YPQHKQLLCS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
     RDHGGFEGNG QTFRILSKLE PYTLDFGMNL CRRTMLGILK YPAPYSKLFV AGEHNEITNH
     RQLKPSQWPP VKGIFDDDND IFAWVLEPLS EADRSRFTST QEGSHPALHH YPHLRTQFKS
     FDCSIMELAD DIAYAVHDLE DAIVMGIVTA SQWHQDVAPT LTNSSDAWIK QELADIGNKL
     FSHEHHLRKD AIGTLVNGFV TAIVISEDDV FEEPLLRFNA TLEPEFAIAL NVLKQLVYKY
     VIRKPEIQML EYKGQQIVMG LFEAFASDPE RLLPLNTQVR WRESEQQGLN THRILADYIS
     GMTDEFAGRL YQQLFSPKAG SNVELSKEM