DGTL1_SHESR
ID DGTL1_SHESR Reviewed; 446 AA.
AC Q0HVD3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-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=Shewmr7_1933;
OS Shewanella sp. (strain MR-7).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60481;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-7;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. MR-7.";
RL Submitted (AUG-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; CP000444; ABI42922.1; -; Genomic_DNA.
DR RefSeq; WP_011626136.1; NC_008322.1.
DR AlphaFoldDB; Q0HVD3; -.
DR SMR; Q0HVD3; -.
DR EnsemblBacteria; ABI42922; ABI42922; Shewmr7_1933.
DR KEGG; shm:Shewmr7_1933; -.
DR HOGENOM; CLU_028163_0_0_6; -.
DR OMA; KLAECGD; -.
DR OrthoDB; 370035at2; -.
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_1000138934"
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; 50715 MW; E6EA2802FDA1A72C CRC64;
MSSSVWQERR HGEDKQRRND HRSPFQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
THSLEVSQIG TGIAAQLSRK YPEHKPLLGS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
RHHGGFEGNG QTFRILSKLE PYTEAFGMNL CRRTMLGILK YPAPQSLLFV 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