ID A0A101WV50_9CREN Unreviewed; 181 AA.
AC A0A101WV50;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 08-NOV-2023, entry version 22.
DE RecName: Full=Nucleoside-triphosphatase AT714_05305 {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=AT714_05305 {ECO:0000313|EMBL:KUO79785.1};
OS Vulcanisaeta sp. OSP_8.
OC Archaea; Thermoproteota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Vulcanisaeta.
OX NCBI_TaxID=1714252 {ECO:0000313|EMBL:KUO79785.1, ECO:0000313|Proteomes:UP000054992};
RN [1] {ECO:0000313|EMBL:KUO79785.1, ECO:0000313|Proteomes:UP000054992}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Jay Z.J., Beam J.P., Kozubal M.A., Jennings R.D.E., Rusch D.B.,
RA Inskeep W.P.;
RT "The distribution, diversity and function of predominant Thermoproteales in
RT high-temperature environments of Yellowstone National Park.";
RL Submitted (NOV-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUO79785.1}.
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DR EMBL; LOCF01000110; KUO79785.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A101WV50; -.
DR Proteomes; UP000054992; Unassembled WGS sequence.
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 2..163
FT /note="AAA+ ATPase"
FT /evidence="ECO:0000259|SMART:SM00382"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
FT BINDING 102..109
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00796"
SQ SEQUENCE 181 AA; 20134 MW; 43E52FB618305A3D CRC64;
MGYLRVLVTG PPGVGKTTLV RKVADYARDL GLKVFGFVTV EVREGGSRVG FKIIDINGGK
ETWLAHVSLF RGNPMVGKYY VNTRAMEEVG IPAIRSAGQG SLLIVDEIGK MELLSRDFLR
VLEEVTPKVH FLGTVFTAYR FNPGVRGFVE RFGFRVVELS RVNRDLVYGE IIRELGRVLG
L
//
