8ODP_MOUSE
ID 8ODP_MOUSE Reviewed; 156 AA.
AC P53368; P97795; Q542J4; Q8VDG0;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Oxidized purine nucleoside triphosphate hydrolase {ECO:0000305};
DE EC=3.6.1.56 {ECO:0000250|UniProtKB:P36639};
DE AltName: Full=2-hydroxy-dATP diphosphatase;
DE AltName: Full=7,8-dihydro-8-oxoguanine triphosphatase;
DE AltName: Full=8-oxo-dGTPase;
DE AltName: Full=Methylated purine nucleoside triphosphate hydrolase {ECO:0000250|UniProtKB:P36639};
DE EC=3.6.1.- {ECO:0000250|UniProtKB:P36639};
DE AltName: Full=Nucleoside diphosphate-linked moiety X motif 1;
DE Short=Nudix motif 1;
GN Name=Nudt1; Synonyms=Mth1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY, AND TISSUE
RP SPECIFICITY.
RC STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RX PubMed=7592783; DOI=10.1074/jbc.270.43.25942;
RA Kakuma T., Nishida J., Tsuzuki T., Sekiguchi M.;
RT "Mouse MTH1 protein with 8-oxo-7,8-dihydro-2'-deoxyguanosine 5'-
RT triphosphatase activity that prevents transversion mutation. cDNA cloning
RT and tissue distribution.";
RL J. Biol. Chem. 270:25942-25948(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=129/Sv; TISSUE=Embryonic stem cell;
RX PubMed=9013634; DOI=10.1074/jbc.272.6.3766;
RA Igarashi H., Tsuzuki T., Kakuma T., Tominaga Y., Sekiguchi M.;
RT "Organization and expression of the mouse MTH1 gene for preventing
RT transversion mutation.";
RL J. Biol. Chem. 272:3766-3772(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, DBA/2J, and NOD; TISSUE=Embryo, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary gland, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND DISRUPTION PHENOTYPE.
RX PubMed=11572992; DOI=10.1073/pnas.191086798;
RA Tsuzuki T., Egashira A., Igarashi H., Iwakuma T., Nakatsuru Y.,
RA Tominaga Y., Kawate H., Nakao K., Nakamura K., Ide F., Kura S.,
RA Nakabeppu Y., Katsuki M., Ishikawa T., Sekiguchi M.;
RT "Spontaneous tumorigenesis in mice defective in the MTH1 gene encoding 8-
RT oxo-dGTPase.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:11456-11461(2001).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=30304478; DOI=10.1093/nar/gky896;
RA Jemth A.S., Gustafsson R., Braeutigam L., Henriksson L., Vallin K.S.A.,
RA Sarno A., Almloef I., Homan E., Rasti A., Warpman Berglund U., Stenmark P.,
RA Helleday T.;
RT "MutT homologue 1 (MTH1) catalyzes the hydrolysis of mutagenic O6-methyl-
RT dGTP.";
RL Nucleic Acids Res. 46:10888-10904(2018).
RN [9]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=32144205; DOI=10.1074/jbc.ra120.012636;
RA Scaletti E.R., Vallin K.S., Braeutigam L., Sarno A., Warpman Berglund U.,
RA Helleday T., Stenmark P., Jemth A.S.;
RT "MutT homologue 1 (MTH1) removes N6-methyl-dATP from the dNTP pool.";
RL J. Biol. Chem. 295:4761-4772(2020).
RN [10] {ECO:0007744|PDB:5MZE, ECO:0007744|PDB:5MZG, ECO:0007744|PDB:6EHH}
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) IN COMPLEXES WITH 8-OXO-DGTP AND
RP SYNTHETIC INHIBITORS, CATALYTIC ACTIVITY, AND SUBUNIT.
RX PubMed=29281266; DOI=10.1021/acs.biochem.7b01163;
RA Narwal M., Jemth A.S., Gustafsson R., Almlof I., Warpman Berglund U.,
RA Helleday T., Stenmark P.;
RT "Crystal Structures and Inhibitor Interactions of Mouse and Dog MTH1 Reveal
RT Species-Specific Differences in Affinity.";
RL Biochemistry 57:593-603(2018).
CC -!- FUNCTION: Oxidized purine nucleoside triphosphate hydrolase which is a
CC prominent sanitizer of the oxidized nucleotide pool (PubMed:11572992,
CC PubMed:29281266, PubMed:7592783, PubMed:30304478). Catalyzes the
CC hydrolysis of 2-oxo-dATP (2-hydroxy-dATP) into 2-oxo-dAMP (By
CC similarity). Has also a significant hydrolase activity toward 2-oxo-
CC ATP, 8-oxo-dGTP and 8-oxo-dATP (PubMed:11572992, PubMed:29281266,
CC PubMed:7592783, PubMed:30304478). Through the hydrolysis of oxidized
CC purine nucleoside triphosphates, prevents their incorporation into DNA
CC and the subsequent transversions A:T to C:G and G:C to T:A
CC (PubMed:11572992, PubMed:29281266, PubMed:7592783, PubMed:30304478).
CC Also catalyzes the hydrolysis of methylated purine nucleoside
CC triphosphate preventing their integration into DNA (PubMed:30304478,
CC PubMed:32144205). Through this antimutagenic activity protects cells
CC from oxidative stress (PubMed:11572992, PubMed:29281266,
CC PubMed:7592783, PubMed:30304478, PubMed:32144205).
CC {ECO:0000250|UniProtKB:P36639, ECO:0000269|PubMed:11572992,
CC ECO:0000269|PubMed:29281266, ECO:0000269|PubMed:30304478,
CC ECO:0000269|PubMed:32144205, ECO:0000269|PubMed:7592783}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-dATP + H2O = 2-oxo-dAMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31583, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63212, ChEBI:CHEBI:77897; EC=3.6.1.56;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31584;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-oxo-ATP + H2O = 2-oxo-AMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:67392, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:71395, ChEBI:CHEBI:172878;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67393;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dGTP + H2O = 8-oxo-dGMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:31575, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:63224, ChEBI:CHEBI:77896;
CC Evidence={ECO:0000269|PubMed:11572992, ECO:0000269|PubMed:29281266,
CC ECO:0000269|PubMed:30304478, ECO:0000269|PubMed:7592783};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:31576;
CC Evidence={ECO:0000269|PubMed:11572992};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8-oxo-dATP + H2O = 8-oxo-dAMP + diphosphate + H(+);
CC Xref=Rhea:RHEA:65396, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:71361, ChEBI:CHEBI:172871;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:65397;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + O(6)-methyl-dGTP = diphosphate + H(+) + O(6)-methyl-
CC dGMP; Xref=Rhea:RHEA:67600, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:169974, ChEBI:CHEBI:169975;
CC Evidence={ECO:0000269|PubMed:30304478};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67601;
CC Evidence={ECO:0000305|PubMed:30304478};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-methyl-dATP = diphosphate + H(+) + N(6)-methyl-
CC dAMP; Xref=Rhea:RHEA:67604, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:169976, ChEBI:CHEBI:172872;
CC Evidence={ECO:0000269|PubMed:32144205};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67605;
CC Evidence={ECO:0000305|PubMed:32144205};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + N(6)-methyl-ATP = diphosphate + H(+) + N(6)-methyl-AMP;
CC Xref=Rhea:RHEA:67608, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:144842, ChEBI:CHEBI:172873;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:67609;
CC Evidence={ECO:0000250|UniProtKB:P36639};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7ZWC3};
CC Note=Binds 2 Mg(2+) ion per subunit. {ECO:0000250|UniProtKB:Q7ZWC3};
CC -!- SUBUNIT: Monomer. {ECO:0000305|PubMed:29281266}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P53369}. Nucleus
CC {ECO:0000250|UniProtKB:P53369}. Nucleus membrane
CC {ECO:0000250|UniProtKB:P53369}. Cytoplasmic vesicle, secretory vesicle,
CC acrosome {ECO:0000250|UniProtKB:P53369}.
CC -!- TISSUE SPECIFICITY: High expression levels detected in thymus, liver,
CC spleen, kidney, testis and large intestine, with lower levels detected
CC in brain, heart, lung and stomach (at protein level). Expressed in
CC kidney, liver and small intestine. {ECO:0000269|PubMed:7592783}.
CC -!- DISRUPTION PHENOTYPE: Mutant mice appear normal, but have higher
CC incidence of tumors in lung, liver and stomach.
CC {ECO:0000269|PubMed:11572992}.
CC -!- SIMILARITY: Belongs to the Nudix hydrolase family. {ECO:0000305}.
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DR EMBL; D49956; BAA08711.1; -; mRNA.
DR EMBL; D88356; BAA19866.1; -; Genomic_DNA.
DR EMBL; AK011695; BAB27785.1; -; mRNA.
DR EMBL; AK088309; BAC40274.1; -; mRNA.
DR EMBL; AK168312; BAE40252.1; -; mRNA.
DR EMBL; CH466529; EDL19122.1; -; Genomic_DNA.
DR EMBL; CH466529; EDL19123.1; -; Genomic_DNA.
DR EMBL; BC021940; AAH21940.1; -; mRNA.
DR EMBL; BC098239; AAH98239.1; -; mRNA.
DR CCDS; CCDS19818.1; -.
DR PIR; I49446; I49446.
DR RefSeq; NP_032663.1; NM_008637.1.
DR RefSeq; XP_006504718.1; XM_006504655.2.
DR RefSeq; XP_006504719.1; XM_006504656.2.
DR RefSeq; XP_006504720.1; XM_006504657.2.
DR PDB; 5MZE; X-ray; 2.10 A; A/B/C/D=1-156.
DR PDB; 5MZG; X-ray; 1.85 A; A/B=1-156.
DR PDB; 6EHH; X-ray; 2.40 A; A/B/C/D=1-156.
DR PDBsum; 5MZE; -.
DR PDBsum; 5MZG; -.
DR PDBsum; 6EHH; -.
DR AlphaFoldDB; P53368; -.
DR SMR; P53368; -.
DR STRING; 10090.ENSMUSP00000059983; -.
DR iPTMnet; P53368; -.
DR PhosphoSitePlus; P53368; -.
DR EPD; P53368; -.
DR PaxDb; P53368; -.
DR PRIDE; P53368; -.
DR ProteomicsDB; 296458; -.
DR Antibodypedia; 1866; 242 antibodies from 30 providers.
DR DNASU; 17766; -.
DR Ensembl; ENSMUST00000050205; ENSMUSP00000059983; ENSMUSG00000036639.
DR Ensembl; ENSMUST00000071881; ENSMUSP00000071778; ENSMUSG00000036639.
DR Ensembl; ENSMUST00000110826; ENSMUSP00000106450; ENSMUSG00000036639.
DR Ensembl; ENSMUST00000110827; ENSMUSP00000106451; ENSMUSG00000036639.
DR GeneID; 17766; -.
DR KEGG; mmu:17766; -.
DR UCSC; uc009ahn.1; mouse.
DR CTD; 4521; -.
DR MGI; MGI:109280; Nudt1.
DR VEuPathDB; HostDB:ENSMUSG00000036639; -.
DR eggNOG; ENOG502S254; Eukaryota.
DR GeneTree; ENSGT00390000000341; -.
DR InParanoid; P53368; -.
DR OMA; FRADSYN; -.
DR PhylomeDB; P53368; -.
DR TreeFam; TF106348; -.
DR BRENDA; 3.6.1.56; 3474.
DR Reactome; R-MMU-2393930; Phosphate bond hydrolysis by NUDT proteins.
DR BioGRID-ORCS; 17766; 3 hits in 111 CRISPR screens.
DR ChiTaRS; Nudt1; mouse.
DR PRO; PR:P53368; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; P53368; protein.
DR Bgee; ENSMUSG00000036639; Expressed in otic placode and 209 other tissues.
DR ExpressionAtlas; P53368; baseline and differential.
DR Genevisible; P53368; MM.
DR GO; GO:0001669; C:acrosomal vesicle; ISO:MGI.
DR GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0005615; C:extracellular space; ISO:MGI.
DR GO; GO:0005759; C:mitochondrial matrix; ISS:UniProtKB.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; ISO:MGI.
DR GO; GO:0106377; F:2-hydroxy-ATP hydrolase activity; ISS:UniProtKB.
DR GO; GO:0106378; F:2-hydroxy-dATP hydrolase activity; ISS:UniProtKB.
DR GO; GO:0035539; F:8-oxo-7,8-dihydrodeoxyguanosine triphosphate pyrophosphatase activity; ISS:UniProtKB.
DR GO; GO:0008413; F:8-oxo-7,8-dihydroguanosine triphosphate pyrophosphatase activity; IDA:MGI.
DR GO; GO:0047693; F:ATP diphosphatase activity; ISO:MGI.
DR GO; GO:0008828; F:dATP pyrophosphohydrolase activity; ISO:MGI.
DR GO; GO:0016818; F:hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; IBA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030515; F:snoRNA binding; IDA:UniProtKB.
DR GO; GO:0007568; P:aging; IEA:Ensembl.
DR GO; GO:0042262; P:DNA protection; ISS:UniProtKB.
DR GO; GO:0008584; P:male gonad development; IEA:Ensembl.
DR GO; GO:0006152; P:purine nucleoside catabolic process; ISS:UniProtKB.
DR GO; GO:0046686; P:response to cadmium ion; IEA:Ensembl.
DR InterPro; IPR003563; 8ODP.
DR InterPro; IPR020476; Nudix_hydrolase.
DR InterPro; IPR015797; NUDIX_hydrolase-like_dom_sf.
DR InterPro; IPR020084; NUDIX_hydrolase_CS.
DR InterPro; IPR000086; NUDIX_hydrolase_dom.
DR Pfam; PF00293; NUDIX; 1.
DR PRINTS; PR01403; 8OXTPHPHTASE.
DR PRINTS; PR00502; NUDIXFAMILY.
DR SUPFAM; SSF55811; SSF55811; 1.
DR PROSITE; PS51462; NUDIX; 1.
DR PROSITE; PS00893; NUDIX_BOX; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Cytoplasmic vesicle; Hydrolase; Magnesium;
KW Membrane; Metal-binding; Nucleus; Reference proteome; RNA-binding.
FT CHAIN 1..156
FT /note="Oxidized purine nucleoside triphosphate hydrolase"
FT /id="PRO_0000057100"
FT DOMAIN 3..132
FT /note="Nudix hydrolase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT MOTIF 37..58
FT /note="Nudix box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00794"
FT BINDING 8
FT /ligand="2-oxo-dATP"
FT /ligand_id="ChEBI:CHEBI:77897"
FT /evidence="ECO:0000250|UniProtKB:P36639"
FT BINDING 8
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 23
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 33
FT /ligand="2-oxo-dATP"
FT /ligand_id="ChEBI:CHEBI:77897"
FT /evidence="ECO:0000250|UniProtKB:P36639"
FT BINDING 33
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 35..38
FT /ligand="2-oxo-dATP"
FT /ligand_id="ChEBI:CHEBI:77897"
FT /evidence="ECO:0000250|UniProtKB:P36639"
FT BINDING 35..38
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7ZWC3"
FT BINDING 52
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 52
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7ZWC3"
FT BINDING 55
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:Q7ZWC3"
FT BINDING 56
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 56
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7ZWC3"
FT BINDING 100
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT BINDING 100
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q7ZWC3"
FT BINDING 117..120
FT /ligand="2-oxo-dATP"
FT /ligand_id="ChEBI:CHEBI:77897"
FT /evidence="ECO:0000250|UniProtKB:P36639"
FT BINDING 117..120
FT /ligand="8-oxo-dGTP"
FT /ligand_id="ChEBI:CHEBI:77896"
FT /evidence="ECO:0000269|PubMed:29281266,
FT ECO:0007744|PDB:5MZE"
FT CONFLICT 116
FT /note="L -> M (in Ref. 5; AAH21940)"
FT /evidence="ECO:0000305"
FT STRAND 4..13
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 15..23
FT /evidence="ECO:0007829|PDB:5MZG"
FT TURN 27..30
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 31..33
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 35..38
FT /evidence="ECO:0007829|PDB:5MZG"
FT HELIX 45..57
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 65..74
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 80..88
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 99..107
FT /evidence="ECO:0007829|PDB:5MZG"
FT HELIX 108..110
FT /evidence="ECO:0007829|PDB:5MZE"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5MZG"
FT HELIX 120..128
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 132..141
FT /evidence="ECO:0007829|PDB:5MZG"
FT STRAND 144..153
FT /evidence="ECO:0007829|PDB:5MZG"
SQ SEQUENCE 156 AA; 17908 MW; 9E6C12EC2A6DE4B7 CRC64;
MSTSRLYTLV LVLQPQRVLL GMKKRGFGAG RWNGFGGKVQ EGETIEDGAK RELLEESGLS
VDTLHKVGHI SFEFVGSPEL MDVHIFSADH VHGTPTESEE MRPQWFQLDQ IPFADLWPDD
SYWFPLLLQK KKFCGHFKFQ DQDTILSYSL REVDSF
