ID   DGTL1_SHEON             Reviewed;         441 AA.
AC   Q8EEA2;
DT   20-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=SO_2485;
OS   Shewanella oneidensis (strain MR-1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=211586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MR-1;
RX   PubMed=12368813; DOI=10.1038/nbt749;
RA   Heidelberg J.F., Paulsen I.T., Nelson K.E., Gaidos E.J., Nelson W.C.,
RA   Read T.D., Eisen J.A., Seshadri R., Ward N.L., Methe B.A., Clayton R.A.,
RA   Meyer T., Tsapin A., Scott J., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Dodson R.J., Durkin A.S., Haft D.H., Kolonay J.F., Madupu R.,
RA   Peterson J.D., Umayam L.A., White O., Wolf A.M., Vamathevan J.J.,
RA   Weidman J.F., Impraim M., Lee K., Berry K.J., Lee C., Mueller J.,
RA   Khouri H.M., Gill J., Utterback T.R., McDonald L.A., Feldblyum T.V.,
RA   Smith H.O., Venter J.C., Nealson K.H., Fraser C.M.;
RT   "Genome sequence of the dissimilatory metal ion-reducing bacterium
RT   Shewanella oneidensis.";
RL   Nat. Biotechnol. 20:1118-1123(2002).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01212}.
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DR   EMBL; AE014299; AAN55516.1; -; Genomic_DNA.
DR   RefSeq; NP_718072.1; NC_004347.2.
DR   RefSeq; WP_011072450.1; NC_004347.2.
DR   AlphaFoldDB; Q8EEA2; -.
DR   SMR; Q8EEA2; -.
DR   STRING; 211586.SO_2485; -.
DR   PaxDb; Q8EEA2; -.
DR   KEGG; son:SO_2485; -.
DR   PATRIC; fig|211586.12.peg.2393; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   OrthoDB; 370035at2; -.
DR   PhylomeDB; Q8EEA2; -.
DR   BioCyc; SONE211586:G1GMP-2270-MON; -.
DR   Proteomes; UP000008186; Chromosome.
DR   GO; GO:0008832; F:dGTPase activity; IBA:GO_Central.
DR   GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR   GO; GO:0006203; P:dGTP catabolic process; IBA:GO_Central.
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..441
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_0000205319"
FT   DOMAIN          59..252
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   441 AA;  50619 MW;  C1DA17F434ED9514 CRC64;
     MTSSVWQERR HGEDKQRRND HRSPYQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
     THSLEVSQIG TGIAAQLSRK YPEHKPLLDS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
     RHHGGFEGNG QTFRILSKLE PYTLDFGMNL CRRTMLGILK YPAPQSSLFI AGNHHEITNH
     RQLKPSQWPP VKGIFDDDND IFDWVLEPLS AADRTRFTSA QPSIQPNYPH LRTQFKSFDC
     SIMELADDIA YAVHDLEDAI VMGIVTASQW QQDVAPTFEH SNDPWIRQEL ADIGTKLFSH
     EHHLRKDAIG TLVNGFVTAI IITDDGVFEE PLLRFNASLE VEFAHALNVL KQLVYKYVIR
     KPEIQMLEYK GQQIVMGLFE AFASDPERLL PLNTQERWRA SEQLGLNSHR ILADYISGMT
     DEFAGRLYQQ LFTLRLDRTW S