ID C3MND7_SULIL Unreviewed; 175 AA.
AC C3MND7;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 27-MAR-2024, entry version 71.
DE RecName: Full=Nucleoside-triphosphatase LS215_2953 {ECO:0000256|HAMAP-Rule:MF_00796};
DE Short=NTPase {ECO:0000256|HAMAP-Rule:MF_00796};
DE EC=3.6.1.15 {ECO:0000256|HAMAP-Rule:MF_00796};
DE AltName: Full=Nucleoside triphosphate phosphohydrolase {ECO:0000256|HAMAP-Rule:MF_00796};
GN OrderedLocusNames=LS215_2953 {ECO:0000313|EMBL:ACP36880.1};
OS Sulfolobus islandicus (strain L.S.2.15 / Lassen #1).
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=429572 {ECO:0000313|EMBL:ACP36880.1, ECO:0000313|Proteomes:UP000001747};
RN [1] {ECO:0000313|EMBL:ACP36880.1, ECO:0000313|Proteomes:UP000001747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L.S.2.15 / Lassen #1 {ECO:0000313|Proteomes:UP000001747};
RX PubMed=19435847; DOI=10.1073/pnas.0808945106;
RA Reno M.L., Held N.L., Fields C.J., Burke P.V., Whitaker R.J.;
RT "Biogeography of the Sulfolobus islandicus pan-genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:8605-8610(2009).
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. May hydrolyze nucleoside diphosphates with lower
CC efficiency. {ECO:0000256|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:0000256|HAMAP-Rule:MF_00796};
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000256|HAMAP-
CC Rule:MF_00796}.
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DR EMBL; CP001399; ACP36880.1; -; Genomic_DNA.
DR RefSeq; WP_009992133.1; NC_012589.1.
DR AlphaFoldDB; C3MND7; -.
DR SMR; C3MND7; -.
DR GeneID; 7808726; -.
DR KEGG; sis:LS215_2953; -.
DR HOGENOM; CLU_103145_1_1_2; -.
DR OrthoDB; 52698at2157; -.
DR Proteomes; UP000001747; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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; IPR003593; AAA+_ATPase.
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 SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00796};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00796}.
FT DOMAIN 7..161
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 15..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
FT BINDING 106..113
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
SQ SEQUENCE 175 AA; 19730 MW; 6E2A814F2E8FEFCC CRC64;
MLEESKNALR VFITGNPGVG KTTILLFLIN KLSENNYKVA GFYCPEVREN GRRIGFRIVD
ITTNEGDWLA KENAPGRVKI GKYTVLEDSA KRITEITLSN INKADVLAID EIGPMELKIP
TIKKLIETIL NNQKPLIAVL HRTQKPMGGR IYVITVENRD SIKYEILNYI LSSLD
//
