ID A0A0P0N5U9_9CREN Unreviewed; 176 AA.
AC A0A0P0N5U9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Nucleoside-triphosphatase Pdsh_05240 {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 ORFNames=Pdsh_05240 {ECO:0000313|EMBL:OWJ55091.1}, Pyrde_1635
GN {ECO:0000313|EMBL:ALL01678.1};
OS Pyrodictium delaneyi.
OC Archaea; Thermoproteota; Thermoprotei; Desulfurococcales; Pyrodictiaceae;
OC Pyrodictium.
OX NCBI_TaxID=1273541 {ECO:0000313|EMBL:ALL01678.1, ECO:0000313|Proteomes:UP000058613};
RN [1] {ECO:0000313|EMBL:ALL01678.1, ECO:0000313|Proteomes:UP000058613}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Su06 {ECO:0000313|EMBL:ALL01678.1,
RC ECO:0000313|Proteomes:UP000058613};
RA Jung J.-H., Lin J., Holden J.F., Park C.-S.;
RT "Complete genome sequence of hyperthermophilic archaeon Pyrodictium
RT delaneyi Su06.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:OWJ55091.1, ECO:0000313|Proteomes:UP000196694}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hulk {ECO:0000313|EMBL:OWJ55091.1,
RC ECO:0000313|Proteomes:UP000196694};
RA Demey L.M., Miller C., Manzella M., Reguera G., Kashefi K.;
RT "The draft genome of the hyperthermophilic archaeon 'Pyrodictium delaneyi
RT strain Hulk', an iron and nitrate reducer, reveals the capacity for sulfate
RT reduction.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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; CP013011; ALL01678.1; -; Genomic_DNA.
DR EMBL; NCQP01000002; OWJ55091.1; -; Genomic_DNA.
DR RefSeq; WP_055409830.1; NZ_NCQP01000002.1.
DR AlphaFoldDB; A0A0P0N5U9; -.
DR STRING; 1273541.Pyrde_1635; -.
DR GeneID; 26099975; -.
DR KEGG; pdl:Pyrde_1635; -.
DR PATRIC; fig|1273541.4.peg.1744; -.
DR OrthoDB; 52698at2157; -.
DR Proteomes; UP000058613; Chromosome.
DR Proteomes; UP000196694; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0017111; F:ribonucleoside triphosphate phosphatase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Hydrolase {ECO:0000256|HAMAP-Rule:MF_00796};
KW Kinase {ECO:0000313|EMBL:ALL01678.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Transferase {ECO:0000313|EMBL:ALL01678.1}.
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
FT BINDING 99..106
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
SQ SEQUENCE 176 AA; 20082 MW; DFB5C749F94D7C99 CRC64;
MLRYVIVTGR PGVGKTTLVR RVVDKLHEDG YNIVGFFCPE VRRGGRRIGF KIVSLDGKLE
AWLAKTENCD GPRVGRYNTC REAEDVARSV LERLDEASLV VIDEIGPMEL KLMGVREAIL
RVLRSEKPGL FVVHERLSDR EILPLLQRYG NWYRVTVENR DALVDEVYSR VIALLS
//
