DGTL1_CERS1
ID DGTL1_CERS1 Reviewed; 378 AA.
AC A3PJB1;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, 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=Rsph17029_1317;
OS Cereibacter sphaeroides (strain ATCC 17029 / ATH 2.4.9) (Rhodobacter
OS sphaeroides).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC Rhodobacteraceae; Cereibacter.
OX NCBI_TaxID=349101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17029 / ATH 2.4.9;
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., Richardson P.,
RA Mackenzie C., Choudhary M., Donohue T.J., Kaplan S.;
RT "Complete sequence of chromosome 1 of Rhodobacter sphaeroides ATCC 17029.";
RL Submitted (FEB-2007) 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; CP000577; ABN76427.1; -; Genomic_DNA.
DR RefSeq; WP_011840939.1; NC_009049.1.
DR AlphaFoldDB; A3PJB1; -.
DR SMR; A3PJB1; -.
DR EnsemblBacteria; ABN76427; ABN76427; Rsph17029_1317.
DR GeneID; 57469995; -.
DR KEGG; rsh:Rsph17029_1317; -.
DR HOGENOM; CLU_028163_1_0_5; -.
DR OMA; HCKAFRR; -.
DR GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IEA:InterPro.
DR CDD; cd00077; HDc; 1.
DR HAMAP; MF_01212; dGTPase_type2; 1.
DR InterPro; IPR006261; dNTPase.
DR InterPro; IPR023023; dNTPase_2.
DR InterPro; IPR003607; HD/PDEase_dom.
DR InterPro; IPR006674; HD_domain.
DR InterPro; IPR026875; PHydrolase_assoc_dom.
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..378
FT /note="Deoxyguanosinetriphosphate triphosphohydrolase-like
FT protein"
FT /id="PRO_1000164737"
FT DOMAIN 62..198
FT /note="HD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01175"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 42641 MW; 2848B1450A38A01A CRC64;
MLAPFACQPG ESRGRQKPES MSTFRSPFQR DRDRIIHSSA FRRLKHKTQV FVEHEGDYYR
TRLTHSIEVA QVARTISGVL GLNTDLAECI ALAHDLGHTP FGHTGEDALA RLMEPYGGFD
HNAQAMRIVT RLERHYAEFD GLNLTWESLE GIAKHNGPVE GPLPYALAEA NAQWDLELHT
YASAEAQVAA IADDVAYSHH DLHDGLRSGL FTEADLMELP VTAPAFDEVD ALYPGLEPMR
RRHEALRRVF GRMVEDVIAV AQGRLEAAQP KSVEEIRQMG ATVIRFSKPL YQELKVIRSF
LFHRMYRAPS VMKERAKVTA VVNDLFPLFM ARPELLPQEW RRDVEAAADE TTLARIVADY
VAGMTDRFAL QEHARLCG