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Conserved domains on  [gi|334186460|ref|NP_001190707|]
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MutT/nudix family protein [Arabidopsis thaliana]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
102-278 4.76e-50

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: 162.71  E-value: 4.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 102 HVVGAGALVINKNtKEVLVVQERSGFfkdKNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetk 181
Cdd:cd04670    1 HQVGVGGLVINEN-NEVLVVQEKYGG---PGGWKLPGGLVDP-------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 182 rmGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAiLKKKTDMFFLCVLSPRSY-DITEQKSEILQAKWMPIQEYVDQP 260
Cdd:cd04670   39 --GEDIGEAAVREVFEETGIDTEFVSILGFRHQHPG-RFGKSDLYFVCRLRPLSDeEIKICPEEIAEAKWMPLEEYLKQP 115
                        170
                 ....*....|....*...
gi 334186460 261 WNkkNEMFKFMANICQKK 278
Cdd:cd04670  116 NV--SQINKLVAKLLLEC 131
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
11-89 1.84e-42

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: 141.52  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460   11 LEGETDNYDGVTVTM-VEPMDSEVFTESLRASLSHWREEGKKGIWIKLPLGLANLVEAAVSEGFRYHHAEPEYLMLVSWI 89
Cdd:pfam18290   1 LPGKEDRYGGVTVDSkELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
 
Name Accession Description Interval E-value
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
102-278 4.76e-50

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: 162.71  E-value: 4.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 102 HVVGAGALVINKNtKEVLVVQERSGFfkdKNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetk 181
Cdd:cd04670    1 HQVGVGGLVINEN-NEVLVVQEKYGG---PGGWKLPGGLVDP-------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 182 rmGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAiLKKKTDMFFLCVLSPRSY-DITEQKSEILQAKWMPIQEYVDQP 260
Cdd:cd04670   39 --GEDIGEAAVREVFEETGIDTEFVSILGFRHQHPG-RFGKSDLYFVCRLRPLSDeEIKICPEEIAEAKWMPLEEYLKQP 115
                        170
                 ....*....|....*...
gi 334186460 261 WNkkNEMFKFMANICQKK 278
Cdd:cd04670  116 NV--SQINKLVAKLLLEC 131
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
11-89 1.84e-42

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: 141.52  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460   11 LEGETDNYDGVTVTM-VEPMDSEVFTESLRASLSHWREEGKKGIWIKLPLGLANLVEAAVSEGFRYHHAEPEYLMLVSWI 89
Cdd:pfam18290   1 LPGKEDRYGGVTVDSkELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
NUDIX pfam00293
NUDIX domain;
102-274 1.85e-11

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 60.57  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460  102 HVVGAGALVINKNTkEVLVVQERSGFFKdkNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetk 181
Cdd:pfam00293   2 RRVAVGVVLLNEKG-RVLLVRRSKKPFP--GWWSLPGGKVEP-------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460  182 rmGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILKKKTD-----MFFLCVLSPRsyDITEQKSEILQAKWMPIQEY 256
Cdd:pfam00293  41 --GETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFPDeheilYVFLAEVEGE--LEPDPDGEVEEVRWVPLEEL 116
                         170
                  ....*....|....*...
gi 334186460  257 vdQPWNKKNEMFKFMANI 274
Cdd:pfam00293 117 --LLLKLAPGDRKLLPWL 132
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
104-255 9.88e-08

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 49.98  E-value: 9.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 104 VGAGALVINKNTKeVLVVQERSGFFKDKnvWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetkrm 183
Cdd:COG1051    7 VAVDAVIFRKDGR-VLLVRRADEPGKGL--WALPGGKVEP---------------------------------------- 43
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAIlkKKTDMFFLCVLSPRSydiTEQKSEILQAKWMPIQE 255
Cdd:COG1051   44 GETPEEAALRELREETGLEVEVLELLGVFDHPDRG--HVVSVAFLAEVLSGE---PRADDEIDEARWFPLDE 110
 
Name Accession Description Interval E-value
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
102-278 4.76e-50

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: 162.71  E-value: 4.76e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 102 HVVGAGALVINKNtKEVLVVQERSGFfkdKNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetk 181
Cdd:cd04670    1 HQVGVGGLVINEN-NEVLVVQEKYGG---PGGWKLPGGLVDP-------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 182 rmGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAiLKKKTDMFFLCVLSPRSY-DITEQKSEILQAKWMPIQEYVDQP 260
Cdd:cd04670   39 --GEDIGEAAVREVFEETGIDTEFVSILGFRHQHPG-RFGKSDLYFVCRLRPLSDeEIKICPEEIAEAKWMPLEEYLKQP 115
                        170
                 ....*....|....*...
gi 334186460 261 WNkkNEMFKFMANICQKK 278
Cdd:cd04670  116 NV--SQINKLVAKLLLEC 131
Nudix_hydro pfam18290
Nudix hydrolase domain; This domain is found just before the N-terminal region of nucleoside ...
11-89 1.84e-42

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: 141.52  E-value: 1.84e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460   11 LEGETDNYDGVTVTM-VEPMDSEVFTESLRASLSHWREEGKKGIWIKLPLGLANLVEAAVSEGFRYHHAEPEYLMLVSWI 89
Cdd:pfam18290   1 LPGKEDRYGGVTVDSkELPMDPEAFASKLRASLSQWRSQGKRGVWLKVPIEQSNLVPIAVKEGFQFHHAEPDYVMLTRWL 80
NUDIX pfam00293
NUDIX domain;
102-274 1.85e-11

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 60.57  E-value: 1.85e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460  102 HVVGAGALVINKNTkEVLVVQERSGFFKdkNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetk 181
Cdd:pfam00293   2 RRVAVGVVLLNEKG-RVLLVRRSKKPFP--GWWSLPGGKVEP-------------------------------------- 40
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460  182 rmGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILKKKTD-----MFFLCVLSPRsyDITEQKSEILQAKWMPIQEY 256
Cdd:pfam00293  41 --GETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFPDeheilYVFLAEVEGE--LEPDPDGEVEEVRWVPLEEL 116
                         170
                  ....*....|....*...
gi 334186460  257 vdQPWNKKNEMFKFMANI 274
Cdd:pfam00293 117 --LLLKLAPGDRKLLPWL 132
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
104-252 6.43e-09

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.


Pssm-ID: 467528 [Multi-domain]  Cd Length: 106  Bit Score: 52.79  E-value: 6.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 104 VGAGALVINKNTKeVLVVQERSGffKDKNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetkrm 183
Cdd:cd02883    1 VAVGAVVFDDEGR-VLLVRRSDG--PGPGGWELPGGGVEP---------------------------------------- 37
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILKKKTDMFFLCVLSPRSYDITEQKSEILQAKWMP 252
Cdd:cd02883   38 GETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHVVVLVFLARVVGGEPPPLDDEEISEVRWVP 106
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
103-255 6.35e-08

ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. In humans, there are four distinct ADPRase activities, three putative cytosolic (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). ADPRase-m is also known as NUDT9. It can be distinugished from the cytosolic ADPRase by a N-terminal target sequence unique to mitochondrial ADPRase. NUDT9 functions as a monomer.


Pssm-ID: 467573 [Multi-domain]  Cd Length: 122  Bit Score: 50.38  E-value: 6.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 103 VVGAGALVINKNtkEVLVVQERSGFFKDKnvWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetkr 182
Cdd:cd04691    1 WLGVGGVVVKEG--KVLLVKRAYGPGKGR--WTLPGGFVEE--------------------------------------- 37
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186460 183 mGEDIWTGVAREVEEETGIIADFVEVLAFRQshKAILKKKTDMFFLCVLSPRSYDITEQKSEILQAKWMPIQE 255
Cdd:cd04691   38 -GETLDEAIVREVLEETGIDAKPVGIIGVRS--GVIRDGKSDNYVVFLLEYVGGEPKPDERENSEAGFLTLEE 107
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
104-255 9.88e-08

ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 49.98  E-value: 9.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 104 VGAGALVINKNTKeVLVVQERSGFFKDKnvWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetkrm 183
Cdd:COG1051    7 VAVDAVIFRKDGR-VLLVRRADEPGKGL--WALPGGKVEP---------------------------------------- 43
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAIlkKKTDMFFLCVLSPRSydiTEQKSEILQAKWMPIQE 255
Cdd:COG1051   44 GETPEEAALRELREETGLEVEVLELLGVFDHPDRG--HVVSVAFLAEVLSGE---PRADDEIDEARWFPLDE 110
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
183-255 2.06e-07

uncharacterized NUDIX hydrolase subfamily; 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.


Pssm-ID: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 49.10  E-value: 2.06e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 334186460 183 MGEDIWTGVAREVEEETGIIADFVEVLaFRQS----HKAILKKKTDMFFLCVLsPRSYDITEQKSEILQAKWMPIQE 255
Cdd:cd04681   42 PGESAEEALRRELREELGLKIPKLRYL-CSLPntylYKGITYKTCDLFFTAEL-DEKPKLKKAEDEVAELEWLDLEE 116
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
184-255 3.37e-06

uncharacterized NUDIX hydrolase subfamily; 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.


Pssm-ID: 467575 [Multi-domain]  Cd Length: 157  Bit Score: 46.37  E-value: 3.37e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVE-VLAFRQSHKAILkkktDMFFLCVLSPRSYDITEQKSEILQAKWMPIQE 255
Cdd:cd04693   70 GETSLEAAIRELKEELGIDLDADElRPILTIRFDNGF----DDIYLFRKDVDIEDLTLQKEEVQDVKWVTLEE 138
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
184-258 1.72e-05

8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX family [Defense mechanisms];


Pssm-ID: 440260 [Multi-domain]  Cd Length: 143  Bit Score: 43.87  E-value: 1.72e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEVLaFRQSHKAILKKKTDMFFLCVLSPRSYDITEQKSEILQAKWMPIQEYVD 258
Cdd:COG0494   52 GESPEEAALRELREETGLTAEDLELL-GELPSPGYTDEKVHVFLARGLGPGEEVGLDDEDEFIEVRWVPLDEALA 125
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
105-269 1.59e-04

plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine tetraphosphate (Ap4A) hydrolase is a member of the NUDIX hydrolase superfamily. Members of this family are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one group (represented by this subfamily) and fungi/animals/archaea enzymes fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for the inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU where U is Ile, Leu, or Val), Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variations. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.


Pssm-ID: 467539 [Multi-domain]  Cd Length: 147  Bit Score: 41.40  E-value: 1.59e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 105 GAGALVINKNtKEVLVVQeRSGffkDKNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknetkrmG 184
Cdd:cd03671    5 NVGIVLFNRD-GQVLVGR-RID---VPGAWQFPQGGIDE----------------------------------------G 39
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 185 EDIWTGVAREVEEETGIIADFVEVLA---------FRQSHKAILKK-----KTDMFFLCVLSPRSYDI---TEQKSEILQ 247
Cdd:cd03671   40 EDPEEAALRELYEETGLSPEDVEIIAetpdwltydLPEDLIRKGWGgkyrgQKQKWFLFRFTGDDSEInldTHEHPEFDA 119
                        170       180
                 ....*....|....*....|..
gi 334186460 248 AKWMPIQEYVDQPWNKKNEMFK 269
Cdd:cd03671  120 WRWVDLEELPDLVVPFKRDVYR 141
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
103-255 1.13e-03

diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily 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.


Pssm-ID: 467541 [Multi-domain]  Cd Length: 131  Bit Score: 38.30  E-value: 1.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 103 VVGAGALVINKNTK--EVLVVQERSGffkdkNVWKLPTGVINEelvvlrvvgelhkkvvltsyrsikclliicndtknet 180
Cdd:cd03673    1 VEAAGGVVWRGRGGggEVLLIHRPRY-----DDWSLPKGKLEP------------------------------------- 38
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 181 krmGEDIWTGVAREVEEETGIIADFVEVLA-----FRQSHKAILkKKTDmFFLcvLSPRSYDITEQK-SEILQAKWMPIQ 254
Cdd:cd03673   39 ---GETPEEAAVREVEEETGLRVRLGRPLGttrytYTRKGKGIL-KKVH-YWL--MRALGGEFLPQPeEEIDEVRWLPPD 111

                 .
gi 334186460 255 E 255
Cdd:cd03673  112 E 112
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
182-255 1.14e-03

Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate isomerase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 441052 [Multi-domain]  Cd Length: 162  Bit Score: 39.03  E-value: 1.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 182 RMGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILkkKTDMF-------FLCVLSPrsyDITEQKSEILQAKWMPIQ 254
Cdd:COG1443   68 RAGETYEEAAVRELEEELGITVDDDLRPLGTFRYRAVD--ANGLVenefchvFVARLDG---PLTPQPEEVAEVRWVTLE 142

                 .
gi 334186460 255 E 255
Cdd:COG1443  143 E 143
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
184-255 1.59e-03

diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX (nucleoside diphosphate-linked moiety X)) motif 2/Nudt2, is a member of the NUDIX hydrolase superfamily. Ap4A hydrolases are well represented in a variety of prokaryotic and eukaryotic organisms. Phylogenetic analysis reveals two distinct subgroups where plant enzymes fall into one subfamily and fungi/animals/archaea enzymes, represented by this subfamily, fall into another. Bacterial enzymes are found in both subfamilies. Ap4A is a potential by-product of aminoacyl tRNA synthesis, and accumulation of Ap4A has been implicated in a range of biological events, such as DNA replication, cellular differentiation, heat shock, metabolic stress, and apoptosis. Ap4A hydrolase cleaves Ap4A asymmetrically into ATP and AMP. It is important in the invasive properties of bacteria and thus presents a potential target for inhibition of such invasive bacteria. Besides the signature NUDIX motif (G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val) that functions as a metal binding and catalytic site, and a required divalent cation, Ap4A hydrolase is structurally similar to the other members of the NUDIX hydrolase superfamily with some degree of variation. Several regions in the sequences are poorly defined and substrate and metal binding sites are only predicted based on kinetic studies.


Pssm-ID: 467534 [Multi-domain]  Cd Length: 132  Bit Score: 37.92  E-value: 1.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEvLAFRQSHK---AILKKKTDMFFL-CVLSPRSYDITEqksEILQAKWMPIQE 255
Cdd:cd03428   40 GESELETALRETKEETGLTVDDLP-PGFRETLTysfKEGVEKTVVYFLaELTPDVEVKLSE---EHQDYKWLPYEE 111
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
183-232 3.12e-03

MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 15/Nudt15, may catalyze the hydrolysis of nucleoside diphosphates, triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP, and prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. MTH2 may also play a role in DNA synthesis and cell cycle progression by stabilizing PCNA. 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: 467561 [Multi-domain]  Cd Length: 128  Bit Score: 37.16  E-value: 3.12e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 334186460 183 MGEDIWTGVAREVEEETGIIADFVEVLAFRQSHKAILKKKT-DMFFLCVLS 232
Cdd:cd04678   39 FGESFEECAAREVLEETGLEIRNVRFLTVTNDVFEEEGKHYvTIFVLAEVD 89
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
184-258 4.28e-03

NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked moiety X)) motif 13/Nudt13, is thought to have NADH pyrophosphatase activity, be involved in NADH metabolic process and NADP catabolic process, catalyzing the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP, and located in mitochondrion. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity. Members of this family are also recognized by the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. A block of 8 conserved amino acids downstream of the NUDIX motif is thought to give NADH pyrophosphatase its specificity for NADH. NADH pyrophosphatase forms a dimer.


Pssm-ID: 467535 [Multi-domain]  Cd Length: 126  Bit Score: 36.70  E-value: 4.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 334186460 184 GEDIWTGVAREVEEETGIIADFVEVLA-----FRQShkaiLkkktdMF-FLCVLSPRsyDITEQKSEILQAKWMPIQEYV 257
Cdd:cd03429   38 GETLEEAVRREVKEEVGLRVKNVRYVGsqpwpFPSS----L-----MLgFTAEADSG--EITVDDDELEDARWFSRDELP 106

                 .
gi 334186460 258 D 258
Cdd:cd03429  107 E 107
 
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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