ID   NTPTH_METJA             Reviewed;         170 AA.
AC   Q58954;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   11-OCT-2004, sequence version 2.
DT   03-AUG-2022, entry version 113.
DE   RecName: Full=Nucleoside-triphosphatase THEP1;
DE            Short=NTPase THEP1;
DE            EC=3.6.1.15;
DE   AltName: Full=Nucleoside triphosphate phosphohydrolase;
GN   OrderedLocusNames=MJ1559;
OS   Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS   10045 / NBRC 100440) (Methanococcus jannaschii).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanocaldococcaceae; Methanocaldococcus.
OX   NCBI_TaxID=243232;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX   PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA   Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA   Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA   Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA   Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA   Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA   Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA   Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA   Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT   "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT   jannaschii.";
RL   Science 273:1058-1073(1996).
CC   -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC       TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC       efficiency (By similarity). {ECO:0000250}.
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   -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAB99578.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; L77117; AAB99578.1; ALT_INIT; Genomic_DNA.
DR   PIR; F64494; F64494.
DR   AlphaFoldDB; Q58954; -.
DR   SMR; Q58954; -.
DR   STRING; 243232.MJ_1559; -.
DR   EnsemblBacteria; AAB99578; AAB99578; MJ_1559.
DR   KEGG; mja:MJ_1559; -.
DR   eggNOG; arCOG01034; Archaea.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   InParanoid; Q58954; -.
DR   OMA; GAMEFKC; -.
DR   PhylomeDB; Q58954; -.
DR   Proteomes; UP000000805; 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; Reference proteome.
FT   CHAIN           1..170
FT                   /note="Nucleoside-triphosphatase THEP1"
FT                   /id="PRO_0000146696"
FT   BINDING         7..14
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         98..105
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   170 AA;  19088 MW;  48DBF7DA574109F6 CRC64;
     MRIFITGMPG VGKTTLALKI AEKLKELGYK VGGFITKEIR DGGKRVGFKI ITLDTNEETI
     LAYVGDGKIK VGKYAVFIEN LDNVGVEAIK RALKDADIII IDELGAMEFK SRKFSEVVDE
     VIKSDKPLLA TLHRNWVNKF KDKGELYTLT IENREKLFEE ILNKILAGLK