ID M9UHC5_SULIS Unreviewed; 175 AA.
AC M9UHC5;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE RecName: Full=Nucleoside-triphosphatase SiL_2629 {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=SiL_2629 {ECO:0000313|EMBL:AGJ64061.1};
OS Sulfolobus islandicus LAL14/1.
OC Archaea; Thermoproteota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Sulfolobus.
OX NCBI_TaxID=1241935;
RN [1] {ECO:0000313|EMBL:AGJ64061.1, ECO:0000313|Proteomes:UP000013006}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAL14/1 {ECO:0000313|EMBL:AGJ64061.1};
RX PubMed=23594878; DOI=10.1098/rsob.130010;
RA Jaubert C., Danioux C., Oberto J., Cortez D., Bize A., Krupovic M., She Q.,
RA Forterre P., Prangishvili D., Sezonov G.;
RT "Genomics and genetics of Sulfolobus islandicus LAL14/1, a model
RT hyperthermophilic archaeon.";
RL Open Biol. 3:130010-130010(2013).
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; CP003928; AGJ64061.1; -; Genomic_DNA.
DR RefSeq; WP_012719298.1; NC_021058.1.
DR AlphaFoldDB; M9UHC5; -.
DR GeneID; 84063046; -.
DR KEGG; sic:SiL_2629; -.
DR HOGENOM; CLU_103145_1_1_2; -.
DR Proteomes; UP000013006; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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; 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 Kinase {ECO:0000313|EMBL:AGJ64061.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00796}; Transferase {ECO:0000313|EMBL:AGJ64061.1}.
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; 19744 MW; 1A3ED2C7CFCEEBD8 CRC64;
MLEESKKALR VFITGNPGVG KTTILLFLIN KLSENNYKVA GFYCPEVREN GRRIGFRIVD
ITTNEGDWLA KENAPGRVKI GKYTVLEDSA KRITEITLSN INKADVLAID EIGPMELKIP
TIKKLIETIL NNQKPLIAVL HRTQKPMGGR IYVITVENRD SIKYEILNYI LSSLD
//
