ID   DGTL1_SHEB8             Reviewed;         449 AA.
AC   A6WN87;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   25-MAY-2022, entry version 74.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=Shew185_2134;
OS   Shewanella baltica (strain OS185).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=402882;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OS185;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Sims D., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N.,
RA   Brettar I., Rodrigues J., Konstantinidis K., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome of Shewanella baltica OS185.";
RL   Submitted (JUL-2007) 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; CP000753; ABS08276.1; -; Genomic_DNA.
DR   RefSeq; WP_012089188.1; NC_009665.1.
DR   AlphaFoldDB; A6WN87; -.
DR   SMR; A6WN87; -.
DR   KEGG; sbm:Shew185_2134; -.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
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_1000138926"
FT   DOMAIN          59..255
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..27
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..27
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   449 AA;  51317 MW;  E6B7E2A412BB221C CRC64;
     MTSSVWQERR HGEDKQRRND HRSPYQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
     THSLEVSQIG TGIAAQLRRK YPQHKQLLCS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
     RDHGGFEGNG QTFRILSKLE PYTLDFGMNL CRRTMLGILK YPAPHSKLFV AGKHSEITNH
     RQLKPSQWPP VKGIFDDDND IFAWVLEPLS EADRSRFTST QQGSHPALHH YPHLRTQFKS
     FDCSIMELAD DIAYAVHDLE DAIVMGIVTA SQWHQDVAPT LTNSGDAWIR QELADIGNKL
     FSHEHHLRKD AIGTLVNGFV TAIVISEDDV FEEPLLRFNA TLEPEFAIAL NVLKQLVYKY
     VIRKPEIQML EYKGQQIVMG LFEAFASDPE RLLPLNTQER WRESEQQGLN SHRVLADYIS
     GMTDEFAGRL YQQLFSPKAG SNVELSKEM