NTPCR_BOVIN
ID NTPCR_BOVIN Reviewed; 190 AA.
AC Q1LZ78;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 03-AUG-2022, entry version 75.
DE RecName: Full=Cancer-related nucleoside-triphosphatase homolog;
DE Short=NTPase;
DE EC=3.6.1.15;
DE AltName: Full=Nucleoside triphosphate phosphohydrolase;
GN Name=NTPCR;
OS Bos taurus (Bovine).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Hereford; TISSUE=Fetal pons;
RG NIH - Mammalian Gene Collection (MGC) project;
RL Submitted (MAY-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Has nucleotide phosphatase activity towards ATP, GTP, CTP,
CC TTP and UTP. Hydrolyzes nucleoside diphosphates with lower efficiency.
CC {ECO:0000250|UniProtKB:Q9BSD7}.
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:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:23681;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + TTP = H(+) + phosphate + TDP; Xref=Rhea:RHEA:65580,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:61417, ChEBI:CHEBI:63527;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65581;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=CTP + H2O = CDP + H(+) + phosphate; Xref=Rhea:RHEA:29387,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37563,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58069;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:29388;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:13066;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58189;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:19670;
CC Evidence={ECO:0000250|UniProtKB:Q9BSD7};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:Q9BSD7}.
CC -!- SIMILARITY: Belongs to the THEP1 NTPase family. {ECO:0000305}.
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DR EMBL; BC116158; AAI16159.1; -; mRNA.
DR RefSeq; NP_001069284.1; NM_001075816.2.
DR AlphaFoldDB; Q1LZ78; -.
DR SMR; Q1LZ78; -.
DR STRING; 9913.ENSBTAP00000018514; -.
DR PaxDb; Q1LZ78; -.
DR PRIDE; Q1LZ78; -.
DR GeneID; 521103; -.
DR KEGG; bta:521103; -.
DR CTD; 84284; -.
DR eggNOG; ENOG502QVJ8; Eukaryota.
DR InParanoid; Q1LZ78; -.
DR OrthoDB; 1401569at2759; -.
DR Proteomes; UP000009136; Unplaced.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:RHEA.
DR GO; GO:0003924; F:GTPase activity; IEA:RHEA.
DR GO; GO:0017111; F:nucleoside-triphosphatase activity; ISS:UniProtKB.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00796; NTPase_1; 1.
DR InterPro; IPR004948; Nuc-triphosphatase_THEP1.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR43146; PTHR43146; 1.
DR Pfam; PF03266; NTPase_1; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 2: Evidence at transcript level;
KW Acetylation; ATP-binding; Hydrolase; Nucleotide-binding;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250|UniProtKB:Q9BSD7"
FT CHAIN 2..190
FT /note="Cancer-related nucleoside-triphosphatase homolog"
FT /id="PRO_0000278092"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 109..116
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSD7"
FT MOD_RES 165
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q9BSD7"
SQ SEQUENCE 190 AA; 20682 MW; 2FB76296808077DB CRC64;
MARHVFLTGP PGVGKTTLIQ KATEVLKSSG MPVDGFYTEE VRQGGRRIGF DVVTLSGIRG
PLSRIGSEPL PGKRECRVGQ YVVDLTSFEQ LALPVLRNAG ASGRPGQSIC VIDEVGKMEL
FSQPFIQAVR QVLSIPGTVV LGTIPVPKGK PLALVEEIRT RKDVKVFSVT KENRNHLLPE
IVTHMQSSRK
