ID   NTPTH_PICTO             Reviewed;         180 AA.
AC   Q6L2J8;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 85.
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=PTO0219;
OS   Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS   100828).
OC   Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC   Picrophilaceae; Picrophilus.
OX   NCBI_TaxID=263820;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX   PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA   Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA   Schepers B., Dock C., Antranikian G., Liebl W.;
RT   "Genome sequence of Picrophilus torridus and its implications for life
RT   around pH 0.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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; AE017261; AAT42804.1; -; Genomic_DNA.
DR   RefSeq; WP_011177020.1; NC_005877.1.
DR   AlphaFoldDB; Q6L2J8; -.
DR   SMR; Q6L2J8; -.
DR   STRING; 263820.PTO0219; -.
DR   EnsemblBacteria; AAT42804; AAT42804; PTO0219.
DR   GeneID; 2843980; -.
DR   KEGG; pto:PTO0219; -.
DR   eggNOG; arCOG01034; Archaea.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   OMA; GAMEFKC; -.
DR   OrthoDB; 90019at2157; -.
DR   Proteomes; UP000000438; 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..180
FT                   /note="Nucleoside-triphosphatase THEP1"
FT                   /id="PRO_0000146699"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT   BINDING         100..107
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ   SEQUENCE   180 AA;  20202 MW;  C0CD3771CB0EBB39 CRC64;
     MVKVGITGPV GSIKAEALAK IMEMLANEGK IIEGFLVSEK VEHNKLISYS VMDILSKKKA
     EFARQDIVSR VKIDKLGVDT RLLEDIVIPS LERAKSEADV IIIDELGKIE NTTKNIKNII
     EDVLKLDKTI IVTLHKKSRN PVLQEFRSLE SVRVFDITPI NKNILPFKIL KVINGEEESI