DGTL1_SHESM
ID DGTL1_SHESM Reviewed; 446 AA.
AC Q0HIK2;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000255|HAMAP-Rule:MF_01212};
GN OrderedLocusNames=Shewmr4_2042;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
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 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 Shewanella sp. MR-4.";
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000446; ABI39115.1; -; Genomic_DNA.
DR RefSeq; WP_011622805.1; NC_008321.1.
DR AlphaFoldDB; Q0HIK2; -.
DR SMR; Q0HIK2; -.
DR KEGG; she:Shewmr4_2042; -.
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..446
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT protein"
FT /id="PRO_1000138933"
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; 50726 MW; AD5A981E0148AE20 CRC64;
MSSSVWQERR HGEDKQRRND HRSPFQRDRA RILHSAAFRR LQAKTQVLGV GMNDFYRTRL
THSLEVSQIG TGIAAQLSRK YPEHKPLLGS MSLLESLCLA HDIGHPPFGH GGEVALNYMM
RHHGGFEGNG QTFRILSKLE PYTEAFGMNL CRRTMLGILK YPAPQSLLFV PGSHPEITNH
RQLKPSQWPP VKGIFDDDSD IFDWVLEPLS VADRARFTSV QPSLQPNYPH LRTQFKSFDC
SIMELADDIA YAVHDLEDAI VMGIVTASQW QQDVAPTLKH SGDPWIRQEL ADIGTKLFSH
EHHLRKDAIG TLVNGFVTAI IINDDPAFEE PLLRFNASLE PEFANALNVL KQLVFKYVIR
KPEIQMLEYK GQQIVMGLFE AFASDPERLL PLNTQERWRT SELQGQNSHR VLADYISGMT
DEFAGRLYQQ LFSPKAGSNV ELSKEM