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Database: UniProt
Entry: K8E0R1_9FIRM
LinkDB: K8E0R1_9FIRM
Original site: K8E0R1_9FIRM 
ID   K8E0R1_9FIRM            Unreviewed;       333 AA.
AC   K8E0R1;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 45.
DE   RecName: Full=Deoxyguanosinetriphosphate triphosphohydrolase-like protein {ECO:0000256|HAMAP-Rule:MF_01212};
GN   ORFNames=DESHY_60287 {ECO:0000313|EMBL:CCO09115.1};
OS   Desulforamulus hydrothermalis Lam5 = DSM 18033.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptococcaceae;
OC   Desulforamulus.
OX   NCBI_TaxID=1121428 {ECO:0000313|EMBL:CCO09115.1, ECO:0000313|Proteomes:UP000009315};
RN   [1] {ECO:0000313|EMBL:CCO09115.1, ECO:0000313|Proteomes:UP000009315}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lam5 / DSM 18033 {ECO:0000313|Proteomes:UP000009315};
RX   PubMed=23405336; DOI=10.1128/genomeA.00114-12;
RA   Amin O., Fardeau M.L., Valette O., Hirschler-Rea A., Barbe V., Medigue C.,
RA   Vacherie B., Ollivier B., Bertin P.N., Dolla A.;
RT   "Genome Sequence of the Sulfate-Reducing Bacterium Desulfotomaculum
RT   hydrothermale Lam5(T).";
RL   Genome Announc. 1:e00114-e00112(2013).
CC   -!- SIMILARITY: Belongs to the dGTPase family. Type 2 subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01212}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:CCO09115.1}.
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DR   EMBL; CAOS01000013; CCO09115.1; -; Genomic_DNA.
DR   RefSeq; WP_008412934.1; NZ_FQXF01000012.1.
DR   AlphaFoldDB; K8E0R1; -.
DR   STRING; 1121428.DESHY_60287; -.
DR   eggNOG; COG0232; Bacteria.
DR   OrthoDB; 9803619at2; -.
DR   Proteomes; UP000009315; Unassembled WGS sequence.
DR   GO; GO:0016793; F:triphosphoric monoester hydrolase activity; IEA:InterPro.
DR   CDD; cd00077; HDc; 1.
DR   Gene3D; 1.10.3210.10; Hypothetical protein af1432; 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   NCBIfam; TIGR01353; dGTP_triPase; 1.
DR   PANTHER; PTHR35795:SF1; BIS(5'-NUCLEOSYL)-TETRAPHOSPHATASE, SYMMETRICAL; 1.
DR   PANTHER; PTHR35795; SLR1885 PROTEIN; 1.
DR   Pfam; PF01966; HD; 1.
DR   Pfam; PF13286; HD_assoc; 1.
DR   SMART; SM00471; HDc; 1.
DR   SUPFAM; SSF109604; HD-domain/PDEase-like; 1.
DR   PROSITE; PS51831; HD; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|HAMAP-Rule:MF_01212, ECO:0000313|EMBL:CCO09115.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009315}.
FT   DOMAIN          75..185
FT                   /note="HD"
FT                   /evidence="ECO:0000259|PROSITE:PS51831"
SQ   SEQUENCE   333 AA;  38149 MW;  0157B72228918D8B CRC64;
     MEIRLRTEEL ENKHLSPFAC RSSMSRGRER PEEPCPVRTV FQRDRDRIIH SKAFRRLKLK
     TQVFIIPEGD HYRTRLTHTL EVAQIARTCA KALGLNEDLT EAIALGHDLG HTPFGHAGEQ
     VLNRLYEGGF KHNEQSLRVV DLLEGQRGLN LTYEVRDGIL NHTGPRIPFT LEGQIVRIAD
     RIAYINHDID DALRAGVLLQ QDLPRDCLQV LGATHSRRIN TMVLDLVQSS MGKPFIAMSP
     AVQEAMDRLR TFMFDHVYIG SEAKKEEDKA RHVVEGLYLH YIRHPRLLPE YLLQRLEQEG
     VARAVLDYIA GMTDRFAVAQ YKKMFIPKGF PLG
//
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