ID   NTPTH_THEAC             Reviewed;         181 AA.
AC   Q9HJH0;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 98.
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=Ta0998;
OS   Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS   15155 / AMRC-C165).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Thermoplasmataceae; Thermoplasma.
OX   NCBI_TaxID=273075;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX   PubMed=11029001; DOI=10.1038/35035069;
RA   Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA   Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT   "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT   acidophilum.";
RL   Nature 407:508-513(2000).
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; AL445066; CAC12127.1; -; Genomic_DNA.
DR   RefSeq; WP_010901409.1; NC_002578.1.
DR   AlphaFoldDB; Q9HJH0; -.
DR   SMR; Q9HJH0; -.
DR   STRING; 273075.Ta0998; -.
DR   EnsemblBacteria; CAC12127; CAC12127; CAC12127.
DR   GeneID; 1456522; -.
DR   KEGG; tac:Ta0998; -.
DR   eggNOG; arCOG01034; Archaea.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   OMA; GAMEFKC; -.
DR   OrthoDB; 90019at2157; -.
DR   Proteomes; UP000001024; 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; IPR004948; Nuc-triphosphatase_THEP1.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR43146; PTHR43146; 1.
DR   Pfam; PF03266; NTPase_1; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Hydrolase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..181
FT                   /note="Nucleoside-triphosphatase THEP1"
FT                   /id="PRO_0000146707"
FT   BINDING         12..19
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT   BINDING         104..111
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ   SEQUENCE   181 AA;  20194 MW;  C18742AB6FB99FAD CRC64;
     MIPLAIKIGI TGPVGSIKSE ALQKIIDMLK NDNLNVQGVL VSKVTNNGKL TGYTIEDIES
     KRKAQFCFDN FVSRVKIDKL GVDTKILEEI LIPSLQKARE TADVIVIDEI GKLENTTKKV
     HAEIEETLKC GKPLIVTLHK RSRNPVLQEI KSLEGVRVFD ITPINKNILP FKVMHVLKGE
     E