ID NTPTH_THEVO Reviewed; 178 AA.
AC Q97AR1;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 101.
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=TV0748; ORFNames=TVG0753265;
OS Thermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC
OS 15438 / GSS1).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1;
RX PubMed=11121031; DOI=10.1073/pnas.97.26.14257;
RA Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y.,
RA Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T.,
RA Yamamoto Y., Aramaki H., Makino K., Suzuki M.;
RT "Archaeal adaptation to higher temperatures revealed by genomic sequence of
RT Thermoplasma volcanium.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(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; BA000011; BAB59890.1; -; Genomic_DNA.
DR RefSeq; WP_048054101.1; NC_002689.2.
DR AlphaFoldDB; Q97AR1; -.
DR SMR; Q97AR1; -.
DR STRING; 273116.gene:9381538; -.
DR PaxDb; 273116-14324964; -.
DR GeneID; 1441843; -.
DR KEGG; tvo:TVG0753265; -.
DR eggNOG; arCOG01034; Archaea.
DR HOGENOM; CLU_103145_1_1_2; -.
DR PhylomeDB; Q97AR1; -.
DR Proteomes; UP000001017; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR CDD; cd19482; RecA-like_Thep1; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; CANCER-RELATED NUCLEOSIDE-TRIPHOSPHATASE; 1.
DR PANTHER; PTHR43146:SF1; CANCER-RELATED NUCLEOSIDE-TRIPHOSPHATASE; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding; Hydrolase; Nucleotide-binding.
FT CHAIN 1..178
FT /note="Nucleoside-triphosphatase THEP1"
FT /id="PRO_0000146708"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
FT BINDING 101..108
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00796"
SQ SEQUENCE 178 AA; 19779 MW; 958AB3B7946C14F4 CRC64;
MAIKIGITGP VGSIKAEALQ KIIGMLQNDG LNVQGVLISK VSDDGKLTGY TIEDILTKKK
VQFCDEKFVS RVKIDKLGVD TRLLEEILIP SLQKARESAD VIIIDEVGKL ENTTKKIHSE
IEETLKCGKP LIVTLHKRSR NPVLQEIKSL EGVRVFDITP INKNILPFKV MHVLKGEE
//
