ID   DGTL1_SHESA             Reviewed;         446 AA.
AC   A0KX58;
DT   14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN   OrderedLocusNames=Shewana3_2147;
OS   Shewanella sp. (strain ANA-3).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC   Shewanellaceae; Shewanella.
OX   NCBI_TaxID=94122;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANA-3;
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   Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA   Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT   "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL   Submitted (SEP-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; CP000469; ABK48377.1; -; Genomic_DNA.
DR   RefSeq; WP_011717103.1; NC_008577.1.
DR   AlphaFoldDB; A0KX58; -.
DR   SMR; A0KX58; -.
DR   STRING; 94122.Shewana3_2147; -.
DR   EnsemblBacteria; ABK48377; ABK48377; Shewana3_2147.
DR   KEGG; shn:Shewana3_2147; -.
DR   eggNOG; COG0232; Bacteria.
DR   HOGENOM; CLU_028163_0_0_6; -.
DR   OMA; KLAECGD; -.
DR   OrthoDB; 370035at2; -.
DR   Proteomes; UP000002589; 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..446
FT                   /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT                   protein"
FT                   /id="PRO_1000138931"
FT   DOMAIN          59..252
FT                   /note="HD"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT   REGION          1..28
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        7..28
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   446 AA;  50705 MW;  F60528C1019EA6E1 CRC64;
     MSSSVWQERR HGEDKQRRND HRSPFQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
     THSLEVSQIG TGIAAQLSRK YPEHKPLLGS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
     RHHGGFEGNG QTFRILSKLE PYTEAFGMNL CRRTMLGILK YPASQSLLFV AGSHPEITNH
     RQLKPSQWPP VKGIFDDDSD IFDWVLEPLS VADRARFTSV QPSLQPNYPH LRTQFKSFDC
     SIMELADDIA YAVHDLEDAI VMGIVTASQW QQDVAPTLKH SGDPWIRQEL ADIGTKLFSH
     EHHLRKDAIG TLVNGFVTAI IINDDPAFEE PLLRFNASLE PEFANALNVL KQLVFKYVIR
     KPEIQMLEYK GQQIVMGLFE AFASDPERLL PLNTQERWRT SEQQGQNSHR VLADYISGMT
     DEFAGRLYQQ LFSPKAGSNV ELSKEM