ID   NTPTH_PYRCJ             Reviewed;         175 AA.
AC   A3MX10;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=Nucleoside-triphosphatase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE            Short=NTPase THEP1 {ECO:0000255|HAMAP-Rule:MF_00796};
DE            EC=3.6.1.15 {ECO:0000255|HAMAP-Rule:MF_00796};
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000255|HAMAP-Rule:MF_00796};
GN   OrderedLocusNames=Pcal_1760;
OS   Pyrobaculum calidifontis (strain DSM 21063 / JCM 11548 / VA1).
OC   Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC   Pyrobaculum.
OX   NCBI_TaxID=410359;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21063 / JCM 11548 / VA1;
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Cozen A.E.,
RA   Fitz-Gibbon S.T., House C.H., Saltikov C., Lowe T.M., Richardson P.;
RT   "Complete sequence of Pyrobaculum calidifontis JCM 11548.";
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC       TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC       efficiency. {ECO:0000255|HAMAP-Rule:MF_00796}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a ribonucleoside 5'-triphosphate + H2O = a ribonucleoside 5'-
CC         diphosphate + H(+) + phosphate; Xref=Rhea:RHEA:23680,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:57930, ChEBI:CHEBI:61557; EC=3.6.1.15;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00796};
CC   -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000255|HAMAP-
CC       Rule:MF_00796}.
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DR   EMBL; CP000561; ABO09177.1; -; Genomic_DNA.
DR   AlphaFoldDB; A3MX10; -.
DR   SMR; A3MX10; -.
DR   STRING; 410359.Pcal_1760; -.
DR   EnsemblBacteria; ABO09177; ABO09177; Pcal_1760.
DR   KEGG; pcl:Pcal_1760; -.
DR   eggNOG; arCOG01034; Archaea.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   OMA; GAMEFKC; -.
DR   Proteomes; UP000001431; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0017111; F:nucleoside-triphosphatase activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.300; -; 1.
DR   HAMAP; MF_00796; NTPase_1; 1.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43146; PTHR43146; 1.
DR   Pfam; PF03266; NTPase_1; 1.
DR   SMART; SM00382; AAA; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding.
FT   CHAIN           1..175
FT                   /note="Nucleoside-triphosphatase THEP1"
FT                   /id="PRO_0000360026"
FT   BINDING         16..23
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT   BINDING         103..110
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ   SEQUENCE   175 AA;  19546 MW;  8CE79F221638A8DE CRC64;
     MTWRERAEKL LIGISGMPGV GKTTLVLRVL ELARSKYRCC GFVTVEVRER GVRIGFDTID
     VVSGARVPLA RVGTGSPSVG KYVVNLPSCE VISRALRQED CEVAFIDEIG AMEFKCPTFY
     TDLRVAVDRI PRIIATVHRN YIHTAEKLGF EIIWLTRENW NSTLSTVLKA LSLST