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Conserved domains on  [gi|15228146|ref|NP_178525|]
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MutT/nudix family protein [Arabidopsis thaliana]

Protein Classification

NUDIX hydrolase( domain architecture ID 16061889)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg2+ or Mn2+ for its activity

CATH:  3.90.79.10
EC:  3.6.1.-
Gene Ontology:  GO:0016817|GO:0009132|GO:0046872
SCOP:  3000098

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
13-91 4.35e-34

Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside diphosphate-linked moiety (Nudix) hydrolases (pfam00293). Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates which are often toxic metabolic intermediates and signalling molecules.


:

Pssm-ID: 465697  Cd Length: 80  Bit Score: 116.48  E-value: 4.35e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228146    13 GKEDRYGRVEVNlMEVEPMNAEDFNAKLDVSFKAWKDQGKKGIWIKLPCELSSLVDIAMKKGFTYHHAENEYAVLSSWI 91
Cdd:pfam18290   3 GKEDRYGGVTVD-SKELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
NUDIX_Hydrolase super family cl00447
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
104-149 6.37e-11

NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


The actual alignment was detected with superfamily member cd04670:

Pssm-ID: 469772 [Multi-domain]  Cd Length: 131  Bit Score: 57.93  E-value: 6.37e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15228146 104 HRIGIGALVLNKNREVLAVQEIDGvfkDTGLWKLPTGVIqENRENF 149
Cdd:cd04670   1 HQVGVGGLVINENNEVLVVQEKYG---GPGGWKLPGGLV-DPGEDI 42
 
Name Accession Description Interval E-value
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
13-91 4.35e-34

Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside diphosphate-linked moiety (Nudix) hydrolases (pfam00293). Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates which are often toxic metabolic intermediates and signalling molecules.


Pssm-ID: 465697  Cd Length: 80  Bit Score: 116.48  E-value: 4.35e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228146    13 GKEDRYGRVEVNlMEVEPMNAEDFNAKLDVSFKAWKDQGKKGIWIKLPCELSSLVDIAMKKGFTYHHAENEYAVLSSWI 91
Cdd:pfam18290   3 GKEDRYGGVTVD-SKELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
104-149 6.37e-11

Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC 3.6.1.-), also known as nucleoside diphosphate-linked moiety X)) motif 6/Nudt6, and similar proteins including peroxisomal coenzyme A diphosphatase/Nudt7 and mitochondrial coenzyme A diphosphatase/Nudt8. The Nudt6 gene overlaps and lies on the opposite strand from FGF2 gene, and is thought to be the FGF2 antisense gene. The two genes are independently transcribed, and their expression shows an inverse relationship, suggesting that this antisense transcript may regulate FGF2 expression. This gene has also been shown to have hormone-regulatory and antiproliferative actions in the pituitary that are independent of FGF2 expression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467554 [Multi-domain]  Cd Length: 131  Bit Score: 57.93  E-value: 6.37e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15228146 104 HRIGIGALVLNKNREVLAVQEIDGvfkDTGLWKLPTGVIqENRENF 149
Cdd:cd04670   1 HQVGVGGLVINENNEVLVVQEKYG---GPGGWKLPGGLV-DPGEDI 42
 
Name Accession Description Interval E-value
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
13-91 4.35e-34

Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside diphosphate-linked moiety (Nudix) hydrolases (pfam00293). Nudix hydrolases catalyze the hydrolysis of nucleoside diphosphates which are often toxic metabolic intermediates and signalling molecules.


Pssm-ID: 465697  Cd Length: 80  Bit Score: 116.48  E-value: 4.35e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15228146    13 GKEDRYGRVEVNlMEVEPMNAEDFNAKLDVSFKAWKDQGKKGIWIKLPCELSSLVDIAMKKGFTYHHAENEYAVLSSWI 91
Cdd:pfam18290   3 GKEDRYGGVTVD-SKELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
104-149 6.37e-11

Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC 3.6.1.-), also known as nucleoside diphosphate-linked moiety X)) motif 6/Nudt6, and similar proteins including peroxisomal coenzyme A diphosphatase/Nudt7 and mitochondrial coenzyme A diphosphatase/Nudt8. The Nudt6 gene overlaps and lies on the opposite strand from FGF2 gene, and is thought to be the FGF2 antisense gene. The two genes are independently transcribed, and their expression shows an inverse relationship, suggesting that this antisense transcript may regulate FGF2 expression. This gene has also been shown to have hormone-regulatory and antiproliferative actions in the pituitary that are independent of FGF2 expression. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467554 [Multi-domain]  Cd Length: 131  Bit Score: 57.93  E-value: 6.37e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 15228146 104 HRIGIGALVLNKNREVLAVQEIDGvfkDTGLWKLPTGVIqENRENF 149
Cdd:cd04670   1 HQVGVGGLVINENNEVLVVQEKYG---GPGGWKLPGGLV-DPGEDI 42
NUDIX_DR1025_like cd04700
DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX ...
109-148 4.28e-03

DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX hydrolase superfamily, show nucleoside triphosphatase and dinucleoside polyphosphate pyrophosphatase activities. Like other enzymes belonging to this superfamily, it requires a divalent cation, in this case Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. In general, substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467580 [Multi-domain]  Cd Length: 147  Bit Score: 36.43  E-value: 4.28e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15228146 109 GALVLNKNREVLAVQE--IDGVFKDTGLWKLPTGVIqENREN 148
Cdd:cd04700  17 GVVLLNERGDILLVQEkgISGHPEKAGLWHIPSGAV-EDGEN 57
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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