ID   NTPTH_METKA             Reviewed;         180 AA.
AC   Q8TX49;
DT   11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 90.
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=MK0827;
OS   Methanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938).
OC   Archaea; Euryarchaeota; Methanopyri; Methanopyrales; Methanopyraceae;
OC   Methanopyrus.
OX   NCBI_TaxID=190192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AV19 / DSM 6324 / JCM 9639 / NBRC 100938;
RX   PubMed=11930014; DOI=10.1073/pnas.032671499;
RA   Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N.,
RA   Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A.,
RA   Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G.,
RA   Koonin E.V., Kozyavkin S.A.;
RT   "The complete genome of hyperthermophile Methanopyrus kandleri AV19 and
RT   monophyly of archaeal methanogens.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002).
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; AE009439; AAM02040.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q8TX49; -.
DR   SMR; Q8TX49; -.
DR   STRING; 190192.MK0827; -.
DR   EnsemblBacteria; AAM02040; AAM02040; MK0827.
DR   KEGG; mka:MK0827; -.
DR   PATRIC; fig|190192.8.peg.869; -.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   OMA; GAMEFKC; -.
DR   Proteomes; UP000001826; 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..180
FT                   /note="Nucleoside-triphosphatase THEP1"
FT                   /id="PRO_0000146697"
FT   BINDING         9..16
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT   BINDING         99..106
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ   SEQUENCE   180 AA;  20326 MW;  E41855768894B701 CRC64;
     MPHNVVLTGR PGIGKTTVCL KVRNVLEEEG YTVGGIYCPE IREGGRRIGF EIVDLTEGDR
     YLLAREGASG PRVGRYGVFV DNLERAAESI ERAVKRTDVV IVDEVGPMEL KSNAFVDAVR
     RAADAHTPAI FVVHERSRHP VVVDLREERP DVVRFRVTLS NRDELSDRIL EHVLEWLEER