ID   NTPTH_METS5             Reviewed;         180 AA.
AC   A4YEP4;
DT   20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-MAY-2007, sequence version 1.
DT   03-AUG-2022, entry version 74.
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=Msed_0721;
OS   Metallosphaera sedula (strain ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509
OS   / TH2).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Metallosphaera.
OX   NCBI_TaxID=399549;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51363 / DSM 5348 / JCM 9185 / NBRC 15509 / TH2;
RX   PubMed=18083856; DOI=10.1128/aem.02019-07;
RA   Auernik K.S., Maezato Y., Blum P.H., Kelly R.M.;
RT   "The genome sequence of the metal-mobilizing, extremely thermoacidophilic
RT   archaeon Metallosphaera sedula provides insights into bioleaching-
RT   associated metabolism.";
RL   Appl. Environ. Microbiol. 74:682-692(2008).
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; CP000682; ABP94896.1; -; Genomic_DNA.
DR   RefSeq; WP_012020683.1; NC_009440.1.
DR   AlphaFoldDB; A4YEP4; -.
DR   SMR; A4YEP4; -.
DR   STRING; 399549.Msed_0721; -.
DR   EnsemblBacteria; ABP94896; ABP94896; Msed_0721.
DR   GeneID; 5103759; -.
DR   GeneID; 59455825; -.
DR   KEGG; mse:Msed_0721; -.
DR   eggNOG; arCOG01034; Archaea.
DR   HOGENOM; CLU_103145_1_1_2; -.
DR   OMA; GAMEFKC; -.
DR   Proteomes; UP000000242; 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_0000360024"
FT   BINDING         18..25
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   180 AA;  20480 MW;  118B18EAA8318B76 CRC64;
     MQNSPWFKEN PLRLFITGRP GVGKTTLIKG LVSELRELKI AGFYTEEVRE RGERTGFLFV
     VIGDGSCPLA STKPIGKERV GRYFVVDSLT LLPQVKQRLE VADLVIMDEI GPMEKKIGDL
     WKLIQGVLSS NKPVVASVHR SMNIEGKRYE LTPVNRDRVR EDILNEIRRY FGTKQDTFSL