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Conserved domains on  [gi|1519817542|gb|RPH74482|]
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NUDIX hydrolase [Hyphomicrobiales bacterium]

Protein Classification

NUDIX hydrolase( domain architecture ID 10632273)

NUDIX hydrolase catalyzes the hydrolysis of nucleoside diphosphates linked to other moieties (X); it requires a divalent cation, such as Mg(2+) or Mn(2+) for its activity

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-158 2.51e-71

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 211.28  E-value: 2.51e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQVQIMYL 115
Cdd:cd04511     1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519817542 116 ARLTSATISPGPESLEVVLAGWGEIPWAELAFPSVRWVLEQYQ 158
Cdd:cd04511    81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
11-32 5.73e-08

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


:

Pssm-ID: 464323  Cd Length: 32  Bit Score: 46.71  E-value: 5.73e-08
                          10        20
                  ....*....|....*....|..
gi 1519817542  11 RRKIPDGDTHQRDVCSTCGYVH 32
Cdd:pfam14803  11 ELRIPDGDNRPRLVCTACGTIH 32
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-158 2.51e-71

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 211.28  E-value: 2.51e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQVQIMYL 115
Cdd:cd04511     1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519817542 116 ARLTSATISPGPESLEVVLAGWGEIPWAELAFPSVRWVLEQYQ 158
Cdd:cd04511    81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
36-155 3.11e-30

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 106.99  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLH-DGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIP-RIAQVQIM 113
Cdd:COG1051     5 PKVAVDAVIFRkDGRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPdRGHVVSVA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519817542 114 YLARLTSATISPGPESLEVVLAGWGEIPwaELAF-PSVRWVLE 155
Cdd:COG1051    85 FLAEVLSGEPRADDEIDEARWFPLDELP--ELAFtPADHEILE 125
NUDIX pfam00293
NUDIX domain;
47-152 7.79e-14

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 64.81  E-value: 7.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  47 DGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV------YTIPRIAQVQIMYLARLTS 120
Cdd:pfam00293  14 KGRVLLVRRSKKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSlhylapFDGRFPDEHEILYVFLAEV 93
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1519817542 121 ATISPGPESLEVVLAGWgeIPWAELAFPSVRW 152
Cdd:pfam00293  94 EGELEPDPDGEVEEVRW--VPLEELLLLKLAP 123
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
38-99 3.27e-11

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 60.79  E-value: 3.27e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  38 IVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLL 99
Cdd:PRK05379  204 VTVDAVVVQSGHVLLVRRRAEPGKGLWALPGGFLEQDETLLDACLRELREETGLKLPEPVLR 265
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
11-32 5.73e-08

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


Pssm-ID: 464323  Cd Length: 32  Bit Score: 46.71  E-value: 5.73e-08
                          10        20
                  ....*....|....*....|..
gi 1519817542  11 RRKIPDGDTHQRDVCSTCGYVH 32
Cdd:pfam14803  11 ELRIPDGDNRPRLVCTACGTIH 32
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
37-172 7.75e-06

mutator mutT protein; All proteins in this family for which functions are known are involved in repairing oxidative damage to dGTP (they are 8-oxo-dGTPases). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Lowering the threshold picks up members of MutT superfamily well. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 200031 [Multi-domain]  Cd Length: 128  Bit Score: 43.32  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  37 KIVTGAIVLHD-GRILLCRRAIAPRIG-FWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV--YTIPRIAQVQI 112
Cdd:TIGR00586   4 QQIAVGIIRNEnGEIIITRRADGHMFAkLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKLeyEFYPRHITLWF 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542 113 MYLARLtsatispgpeslevvlagWGEiPWAELAFPSVRWVLeqyQTVQGrDDFAPFANP 172
Cdd:TIGR00586  84 WLLERW------------------EGG-PPGKEGQPEEWWVL---VGLLA-DDFFPAANP 120
 
Name Accession Description Interval E-value
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-158 2.51e-71

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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 211.28  E-value: 2.51e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQVQIMYL 115
Cdd:cd04511     1 PKIVVGCLPEWEGKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLYAVYSLPHISQVYIIFR 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519817542 116 ARLTSATISPGPESLEVVLAGWGEIPWAELAFPSVRWVLEQYQ 158
Cdd:cd04511    81 ARLLSPDFSPGPESLEVRLFDEEEIPWDELAFPSVRWALKHYF 123
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
36-155 3.11e-30

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 106.99  E-value: 3.11e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLH-DGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIP-RIAQVQIM 113
Cdd:COG1051     5 PKVAVDAVIFRkDGRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPdRGHVVSVA 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1519817542 114 YLARLTSATISPGPESLEVVLAGWGEIPwaELAF-PSVRWVLE 155
Cdd:COG1051    85 FLAEVLSGEPRADDEIDEARWFPLDELP--ELAFtPADHEILE 125
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
38-137 3.16e-22

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: 85.92  E-value: 3.16e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  38 IVTGAIVLHD-GRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIA----QVQI 112
Cdd:cd02883     1 VAVGAVVFDDeGRVLLVRRSDGPGPGGWELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDegrhVVVL 80
                          90       100
                  ....*....|....*....|....*
gi 1519817542 113 MYLARLTSATISPGPESlEVVLAGW 137
Cdd:cd02883    81 VFLARVVGGEPPPLDDE-EISEVRW 104
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
33-157 1.08e-21

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: 85.31  E-value: 1.08e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  33 YVNPKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEiaIERLLAVYTIPRIAQV-Q 111
Cdd:cd04681     2 FHNVAAAVGVIIRNEGEILFVRRAKEPGKGKLDLPGGFVDPGESAEEALRRELREELGLK--IPKLRYLCSLPNTYLYkG 79
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519817542 112 IMY-------LARLTSaTISPGPESLEVVLAGW---GEIPWAELAFPSVRWVLEQY 157
Cdd:cd04681    80 ITYktcdlffTAELDE-KPKLKKAEDEVAELEWldlEEIEPEKLAFPSIRKAVERY 134
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
40-157 1.85e-21

ADP-ribose pyrophosphatase; 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: 467557 [Multi-domain]  Cd Length: 128  Bit Score: 84.49  E-value: 1.85e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  40 TGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTI------PRIAQ--VQ 111
Cdd:cd04673     4 VGAVVFRDGRVLLVRRGNPPDAGLWSFPGGKVELGETLEDAALRELREETGLEAEVVGLLTVVDVierdeaGRVRFhyVI 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1519817542 112 IMYLARLTSATISPGPESLEvvlAGWgeIPWAELA----FPSVRWVLEQY 157
Cdd:cd04673    84 LDFLAEWVSGEPVAGDDALD---ARW--FSLEELDglplTPGTRDVLERA 128
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
41-137 2.24e-17

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: 73.87  E-value: 2.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIP---RIAQVQIMYLAR 117
Cdd:cd04691     5 GGVVVKEGKVLLVKRAYGPGKGRWTLPGGFVEEGETLDEAIVREVLEETGIDAKPVGIIGVRSGVirdGKSDNYVVFLLE 84
                          90       100
                  ....*....|....*....|
gi 1519817542 118 LTSATISPGPEslEVVLAGW 137
Cdd:cd04691    85 YVGGEPKPDER--ENSEAGF 102
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-132 3.56e-17

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: 467560 [Multi-domain]  Cd Length: 137  Bit Score: 73.70  E-value: 3.56e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGA--IVLHD-GRILLCRRAIApriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY-------TIP 105
Cdd:cd04677     9 PLILVGAavIILNEqGRILLQKRTDT---GDWGLPGGAMELGESLEETARREVFEETGLTVEELELLGVYsgkdlyyTYP 85
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1519817542 106 ---RIAQVQIMYLARLTSATISP-GPESLEV 132
Cdd:cd04677    86 ngdEVYNVTAVYLVRDVSGELKVdDEESLEL 116
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
36-120 5.07e-17

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467562 [Multi-domain]  Cd Length: 126  Bit Score: 73.11  E-value: 5.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY-TIPRIAQ---VQ 111
Cdd:cd04679     1 PRVGCGAAILDDGRLLLVLRLRAPEAGHWGLPGGKVDWLETVEDAVRREILEELGLEIELTRLLCVVdQIDAADGehwVA 80

                  ....*....
gi 1519817542 112 IMYLARLTS 120
Cdd:cd04679    81 PVYLAEIFS 89
NUDIX_Hydrolase cd18879
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
42-137 8.47e-17

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: 467590 [Multi-domain]  Cd Length: 142  Bit Score: 73.00  E-value: 8.47e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  42 AIVLHD-GRILLCRRAIApriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIA-----QVQIM-- 113
Cdd:cd18879    23 AVVLRDaGRVLLVRRADN---GRWTPVTGIVEPGEQPADAAVREVLEETGVDVEVERLASVGASPPVTypngdQCQYLdl 99
                          90       100
                  ....*....|....*....|....*.
gi 1519817542 114 -YLARLTSATISPG-PESLEVvlaGW 137
Cdd:cd18879   100 tFRCRPVGGEARVNdDESLEV---GW 122
NUDIX_Hydrolase cd18884
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
29-114 1.52e-15

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: 467595 [Multi-domain]  Cd Length: 125  Bit Score: 69.36  E-value: 1.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  29 GYVHYVNPKIVTGAIVLHDGRILLCRRAIAPRiGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIA 108
Cdd:cd18884     1 GFVHWNNPIPVVAAIVEHDGHIVLARNKAWPE-GWYGLVTGFLEAGESPEEAVLREVKEELGLDGHEAKFIGHYAFPERN 79

                  ....*.
gi 1519817542 109 QVQIMY 114
Cdd:cd18884    80 QLIIAY 85
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
38-124 2.15e-15

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: 467591 [Multi-domain]  Cd Length: 126  Bit Score: 68.71  E-value: 2.15e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  38 IVTGAIVLHDGRILLCRrAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY-TIPRIA---QVQIM 113
Cdd:cd18880     2 IRAKAIIIEDGKLLLVK-HRDEGGIFYILPGGGQEHGETLPEALKRECLEETGLDVEVGDLLFVReYIGPNKpvhQVELF 80
                          90
                  ....*....|.
gi 1519817542 114 YLARLTSATIS 124
Cdd:cd18880    81 FLCTLEGGELT 91
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
43-161 2.93e-15

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: 68.91  E-value: 2.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  43 IVLHDGRILLCRRA-IAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPR-IAQVQIMYLARLTS 120
Cdd:COG0494    20 LLDDDGRVLLVRRYrYGVGPGLWEFPGGKIEPGESPEEAALRELREETGLTAEDLELLGELPSPGyTDEKVHVFLARGLG 99
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542 121 A----TISPGPESLEVVlagwgEIPWAELA----FPSVRWVLEQYQTVQ 161
Cdd:COG0494   100 PgeevGLDDEDEFIEVR-----WVPLDEALalvtAGEIAKTLAALARLL 143
NUDIX_CDP-Chase_like cd04672
CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ...
36-102 5.25e-15

CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ADP-ribose pyrophosphatase, and UDP-X diphosphatase. CDP-choline pyrophosphatase catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. ADP-ribose pyrophosphatase catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine. 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: 467556 [Multi-domain]  Cd Length: 128  Bit Score: 67.97  E-value: 5.25e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIApriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY 102
Cdd:cd04672     1 PKVDVRAAVFKDGKILLVREKSD---GRWTLPGGWADVGLSPAENAVKEVREESGYEVRARKLLAVF 64
NUDIX_Hydrolase cd04674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
35-148 5.45e-15

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: 467558 [Multi-domain]  Cd Length: 118  Bit Score: 67.49  E-value: 5.45e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  35 NPKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEI--AIERLLAVYTIPRIAQVQI 112
Cdd:cd04674     2 NPLPVVVALLPVRDGLLVIRRGIEPGHGELALPGGYIEYGETWQEAAVRELREETGVEAdaAEVRLFAVRSAPDGTLLIF 81
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1519817542 113 MYLARLTSATISPGPESLEVvlAGWGEIPW-AELAFP 148
Cdd:cd04674    82 GLLPERPVADLPPFAPTDEA--TEWVVLTEpVELAFP 116
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
39-137 8.29e-15

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: 67.13  E-value: 8.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  39 VTGAIVLHDGRILLCRRAIAPRiGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQVQIMYLARL 118
Cdd:cd03429     4 VIVLVTNGEDKILLARQPRWPP-GRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKNVRYVGSQPWPFPSSLMLGFTAEA 82
                          90
                  ....*....|....*....
gi 1519817542 119 TSATISPGPEslEVVLAGW 137
Cdd:cd03429    83 DSGEITVDDD--ELEDARW 99
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
40-101 1.08e-14

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: 467570 [Multi-domain]  Cd Length: 130  Bit Score: 67.19  E-value: 1.08e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  40 TGAIVLHDGRILLCRraiAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV 101
Cdd:cd04688     5 VAAIIIRDGKVLLAR---GEDDDYYRLPGGRVEFGETSEDALVREFKEELGVEVEVVRLLFV 63
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
42-146 3.54e-14

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467579 [Multi-domain]  Cd Length: 118  Bit Score: 65.34  E-value: 3.54e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  42 AIVLHDGRILLCRRAiAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT---IPRIAQVQIMYLARL 118
Cdd:cd04699     7 GVIFDNGRVLLLRRS-RAGAGEWELPGGRLEPGESPEEALKREVKEETGLDVSVGELLDTWTfelDPDKGVFIVTYLCRL 85
                          90       100
                  ....*....|....*....|....*...
gi 1519817542 119 TSATISPGPESLEVVLAGWGEIPWAELA 146
Cdd:cd04699    86 VGGEVTLSDEHEEYEWVTPEELAELELP 113
NPY1 COG2816
NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];
24-89 6.00e-14

NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];


Pssm-ID: 442065 [Multi-domain]  Cd Length: 288  Bit Score: 68.02  E-value: 6.00e-14
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519817542  24 VCSTCGYVHYvnPKIVTGAIVL--HDGRILLCRRAIAPRiGFWTLPAGFMELGETAEQAAVREAREEA 89
Cdd:COG2816   145 RCPACGAEHY--PRTDPAVIVLvtDGDRILLARQARWPP-GRYSLLAGFVEPGETLEQAVRREVFEEV 209
NUDIX pfam00293
NUDIX domain;
47-152 7.79e-14

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 64.81  E-value: 7.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  47 DGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV------YTIPRIAQVQIMYLARLTS 120
Cdd:pfam00293  14 KGRVLLVRRSKKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSlhylapFDGRFPDEHEILYVFLAEV 93
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1519817542 121 ATISPGPESLEVVLAGWgeIPWAELAFPSVRW 152
Cdd:pfam00293  94 EGELEPDPDGEVEEVRW--VPLEELLLLKLAP 123
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
38-154 1.29e-13

MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase that catalyzes the hydrolysis of nucleoside and deoxynucleoside triphosphates (NTPs and dNTPs) by substitution at a beta-phosphorus to yield a nucleotide monophosphate (NMP) and inorganic pyrophosphate (PPi). This enzyme requires two divalent cations for activity; one coordinates the phosphoryl groups of the NTP/dNTP substrate, and the other coordinates to the enzyme. It also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as metal binding and catalytic site. MutT pyrophosphohydrolase is important in preventing errors in DNA replication by hydrolyzing mutagenic nucleotides such as 8-oxo-dGTP (a product of oxidative damage), which can mispair with template adenine during DNA replication, to guanine nucleotides.


Pssm-ID: 467531 [Multi-domain]  Cd Length: 123  Bit Score: 64.01  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  38 IVTGAIVLHDGRILLCRR-AIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLA--VYTIPRIAQVQIMY 114
Cdd:cd03425     2 EVVAAIIVDDGRVLIAQRpEGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIEVEVGEPLGtvEHDYPDFHVRLHVY 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1519817542 115 LARLTSATispgPESLEVVLAGW------GEIPWAELAFPSVRWVL 154
Cdd:cd03425    82 LCTLWSGE----PQLLEHQELRWvtpeelDDLDWLPADIPIVEALL 123
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
41-157 1.55e-13

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: 64.11  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVLHD----GRILLCRRaiaPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV--YTIPRIAQV---Q 111
Cdd:cd03673     5 GGVVWRGrgggGEVLLIHR---PRYDDWSLPKGKLEPGETPEEAAVREVEEETGLRVRLGRPLGTtrYTYTRKGKGilkK 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542 112 IMY-LARLTSATISPGPESlEVVLAGWGEIPWAE--LAFPSVRWVLEQY 157
Cdd:cd03673    82 VHYwLMRALGGEFLPQPEE-EIDEVRWLPPDEARrlLTYPSDREVLDAA 129
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
36-101 2.80e-13

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: 63.35  E-value: 2.80e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  36 PKIVTGAIVLHD-GRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV 101
Cdd:cd04678     1 PRVGVGVIVLNDdGKVLLGRRKGSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVRFLTV 67
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
46-147 3.64e-13

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as 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 _ "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: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 62.94  E-value: 3.64e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  46 HDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT----IPRIAQVQIMYLA--RLT 119
Cdd:cd18873    15 GELKVLLIKRKNEPFKGGWALPGGFVREDETLEDAARRELREETGLKDIYLEQLGTFGdpdrDPRGRVISVAYLAlvPEE 94
                          90       100
                  ....*....|....*....|....*...
gi 1519817542 120 SATISPGPESLEVVLAGWGEIPwAELAF 147
Cdd:cd18873    95 DLAPKAGDDAAEARWFPVDELL-PPLAF 121
NUDIX_Hydrolase cd04676
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
39-149 6.06e-12

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: 467559 [Multi-domain]  Cd Length: 144  Bit Score: 60.11  E-value: 6.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  39 VTGAIVLHDGRILLCRRAiapRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV-------YTIPRIAQVQ 111
Cdd:cd04676    20 VAAVILNEDGRILLQRKG---GLGLWSLPAGAIEPGEHPAEAVIREVREETGLLVKPTRLLGVfggkefrYTYPNGDQVE 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1519817542 112 ---IMYLARLTSATISP-GPESLEvvLAGWGEIPWAELAFPS 149
Cdd:cd04676    97 ytvIAFKCVVTGGTLNAiDGETSE--LRYFSRTQMPTLALPY 136
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
38-99 3.27e-11

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 60.79  E-value: 3.27e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  38 IVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLL 99
Cdd:PRK05379  204 VTVDAVVVQSGHVLLVRRRAEPGKGLWALPGGFLEQDETLLDACLRELREETGLKLPEPVLR 265
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
38-102 4.56e-11

nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) motif 17 (EC 3.6.1.-) encoded by the NUDT17 gene on chromosome 1q21.1 and encodes an enzyme thought to hydrolyse some nucleoside diphosphate derivatives. 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: 467576 [Multi-domain]  Cd Length: 135  Bit Score: 57.69  E-value: 4.56e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519817542  38 IVTGAIVL---HDGRILLCRRAIAPRI--GFWTLPAGFMELGETAEQAAVREAREEANAEIAIE---RLLAVY 102
Cdd:cd04694     1 VDVGVVVLiedSDDRVLLTRRAKHMRTfpGVWVPPGGHVELGESLLEAGLRELQEETGLEVSDIqslSLLGLW 73
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
47-141 5.84e-11

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: 467588 [Multi-domain]  Cd Length: 121  Bit Score: 56.83  E-value: 5.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  47 DGRILLCRRAIAPRigfWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIP----RIAQVQIMYLA-RLTSA 121
Cdd:cd18876    11 AGRVLLVKPTYKDG---WELPGGVVEAGESPLQAARREVREELGLDVPVGRLLAVDWVPpaggGDDAVLFVFDGgVLTPE 87
                          90       100
                  ....*....|....*....|....
gi 1519817542 122 TIS----PGPESLEVVLAGWGEIP 141
Cdd:cd18876    88 QAAairlQDEELSAYRFVTPEEAA 111
NUDIX_Hydrolase cd04683
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
47-106 1.49e-10

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: 467566 [Multi-domain]  Cd Length: 137  Bit Score: 56.46  E-value: 1.49e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519817542  47 DGRILLCRRAIAPRIGF-WTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPR 106
Cdd:cd04683    10 GDEVLLLRRANTGYDDGwWHLPAGHVEAGETVRAAAVREAKEELGVEIDPEDLRLVHTMHR 70
nudC PRK00241
NAD(+) diphosphatase;
24-93 2.18e-10

NAD(+) diphosphatase;


Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 57.94  E-value: 2.18e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  24 VCSTCGYVHYvnPKIVTGAIVL-HDG-RILLCRRAIAPRiGFWTLPAGFMELGETAEQAAVREAREEANAEI 93
Cdd:PRK00241  119 LCPHCRERYY--PRIAPCIIVAvRRGdEILLARHPRHRN-GVYTVLAGFVEVGETLEQCVAREVMEESGIKV 187
NUDIX_ADPRase cd18889
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
36-102 2.53e-10

ADP-ribose pyrophosphatase; 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: 467599 [Multi-domain]  Cd Length: 127  Bit Score: 55.31  E-value: 2.53e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRaiapRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY 102
Cdd:cd18889     1 PKIDTRAAIFKDDKILLVQE----KDGRWSLPGGWVDVNQSIKENTIKEAKEEAGLDVEPKRIIAVL 63
NUDIX_UDP-X_diphosphatase cd18891
UDP-X diphosphatase; UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and ...
36-102 2.98e-10

UDP-X diphosphatase; UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine, the last step of the Mur pathway of peptidoglycan biosynthesis. 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: 467601 [Multi-domain]  Cd Length: 128  Bit Score: 55.48  E-value: 2.98e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAiapRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY 102
Cdd:cd18891     1 PKVDVRAFIQNENKVLLVQDK---HTKEWALPGGFAEVGLSPKENILKEVKEETGLHVEVERLLAVF 64
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
41-106 3.37e-10

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: 467593 [Multi-domain]  Cd Length: 130  Bit Score: 55.34  E-value: 3.37e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519817542  41 GAIVLHD--GRILLCRR-----AIAPriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPR 106
Cdd:cd18882     4 AIAILYDdrGKVLLQLRddkpgIPYP--GYWGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFRFFLLYTEDD 74
NUDIX_Hydrolase cd04669
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
41-128 8.36e-10

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: 467553 [Multi-domain]  Cd Length: 120  Bit Score: 53.90  E-value: 8.36e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVLHDGRILLCRRaIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIeRLLAVYTIPRIAQVQIMYLARLTS 120
Cdd:cd04669     4 VLVIYDDDKLLLIRR-TKPGEEYYVFPGGGIEPGETPEEAALREAVEELGLDVAV-TLITLILRVLNDGTQHYFLARVIT 81
                          90
                  ....*....|
gi 1519817542 121 ATIS--PGPE 128
Cdd:cd04669    82 GSFGlgTGPE 91
PLN02325 PLN02325
nudix hydrolase
36-169 9.11e-10

nudix hydrolase


Pssm-ID: 215184 [Multi-domain]  Cd Length: 144  Bit Score: 54.48  E-value: 9.11e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIA-IERLLAVYTIPRIAQVQIMY 114
Cdd:PLN02325    8 PRVAVVVFLLKGNSVLLGRRRSSIGDSTFALPGGHLEFGESFEECAAREVKEETGLEIEkIELLTVTNNVFLEEPKPSHY 87
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1519817542 115 LA---RLTSATISPGPESLEV-VLAGWGEIPWAELAFPsVRWVLEqyQTVQGrdDFAPF 169
Cdd:PLN02325   88 VTvfmRAVLADPSQVPQNLEPeKCYGWDWYEWDNLPEP-LFWPLE--KLVGS--GFNPF 141
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
39-137 9.39e-10

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: 467563 [Multi-domain]  Cd Length: 121  Bit Score: 53.79  E-value: 9.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  39 VTGAIVLHDGRILLCRRAIAPrigFWTLPAGFMELGETAEQAAVREAREEANAEIAIE-RLLAVYTIPRIA---QVqIMY 114
Cdd:cd04680     3 VRAIVLDDAGRVLLVRHTYVP---GWYLPGGGVDKGETAEEAARRELREEAGVVLTGPpRLFGVYFNRRVSprdHV-ALY 78
                          90       100
                  ....*....|....*....|...
gi 1519817542 115 LARLTSATISPGPeSLEVVLAGW 137
Cdd:cd04680    79 RVREFEQTEPPEP-NGEIAEAGF 100
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
41-156 1.13e-09

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: 53.71  E-value: 1.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVL--HDGRI---LLCRRAIapriGFWTLPAGFMELGETAEQAAVREAREEANaeIAIERLLAV------YTIPRIAQ 109
Cdd:cd03428     6 GAIIYrrDNGEIeflLLQHSYG----GHWDFPKGHVEPGESELETALRETKEETG--LTVDDLPPGfretltYSFKEGVE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542 110 VQ-IMYLARLTS-ATISPGPESLEVVLAGWGEiPWAELAFPSVRWVLEQ 156
Cdd:cd03428    80 KTvVYFLAELTPdVEVKLSEEHQDYKWLPYEE-ALQLLTYENIKELLKE 127
NUDIX_MutT_Nudt1 cd18886
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
38-106 1.93e-09

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467596 [Multi-domain]  Cd Length: 147  Bit Score: 53.39  E-value: 1.93e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519817542  38 IVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPR 106
Cdd:cd18886     1 KYTLCFIIRDDEVLLLNRNKKPNMGKWNGVGGKLEPGESPEECAIREVFEETGLELEDLQLRGIVTFPS 69
NUDIX_MutT_Nudt1 cd18883
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
42-157 2.84e-09

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467594  Cd Length: 136  Bit Score: 52.85  E-value: 2.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  42 AIVLHDGRILLCRRAIAPRigfWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV----YTIPRIAQVQIMYLAR 117
Cdd:cd18883     5 GVIISDEHLLLARVKGDDK---TFLPGGHIEIGESAEIALVRELREELGLSCKVGRYLGAvenqWQDKEVIHVELNHLFE 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542 118 LTSATISP--GPESLEVVLA-GWgeIPWAELA------FPSVRWVLEQY 157
Cdd:cd18883    82 VELQDLHTsdTPESQEPHLEfYW--IPYNDLElhnlqpMPLRNLLLNRK 128
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
44-145 3.20e-09

ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose pyrophosphatase (ADPRase) ( NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as 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 site/catalytic site.


Pssm-ID: 467530 [Multi-domain]  Cd Length: 134  Bit Score: 52.51  E-value: 3.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  44 VLHDGRILLCRRaiaPRIG----FWTLPAGFMELGETAEQAAVREAREEANAEIA-IERLLAVYTIP-RIAQVQIMYLAR 117
Cdd:cd03424    10 ITDDGKVVLVRQ---YRHPvgrvLLELPAGKIDPGEDPEEAARRELEEETGYTAGdLELLGSFYPSPgFSDERIHLFLAE 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1519817542 118 LTSATISPGP---ESLEVVLagwgeIPWAEL 145
Cdd:cd03424    87 DLTPVSEQALdedEFIEVVL-----VPLEEA 112
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
38-101 3.47e-09

8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 18/Nudt18; 2-hydroxy-DADP phosphatase; 7,8-dihydro-8-oxoguanine phosphatase, hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. 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: 467555 [Multi-domain]  Cd Length: 130  Bit Score: 52.70  E-value: 3.47e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519817542  38 IVTGAIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV 101
Cdd:cd04671     2 VVAAVIINEQGEVLMIQEAKRSCRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCEPSTLLSV 65
NUDIX_CDP-Chase cd18890
CDP-choline pyrophosphatase; CDP-choline pyrophosphatase catalyzes the hydrolysis of ...
36-141 3.99e-09

CDP-choline pyrophosphatase; CDP-choline pyrophosphatase catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. 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: 467600 [Multi-domain]  Cd Length: 129  Bit Score: 52.42  E-value: 3.99e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLHD-GRILLCRRAIApriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT------IPRIA 108
Cdd:cd18890     1 PKVDIRAVVFNDkEEILLVKEKED---GKWTLPGGWADVGYTPTEVAAKEVEEETGLEVSPKKLLAILDkrkhphPPQPT 77
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1519817542 109 QV-QIMYLARLTSATISPGPESLEVVLAGWGEIP 141
Cdd:cd18890    78 YVyKLFILCEIEGGELKPSFETGEVRFFSENELP 111
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-131 4.69e-09

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: 467586 [Multi-domain]  Cd Length: 125  Bit Score: 51.90  E-value: 4.69e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  36 PKIVTGAIVLH-DGRILLCRRAiaPRIGFWTLPAGFMELGETAEQAAVREAREEANaeiaierlLAVYTIpRIAQVQ--- 111
Cdd:cd18874     1 PEPTVGALIFNpDGKVLLVRSH--KWNDLYGIPGGKVEWGETLEEALKREVKEETG--------LDITDI-RFILVQesi 69
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519817542 112 -----------IM--YLARLTSATISPGPESLE 131
Cdd:cd18874    70 nseefhkpahfVFvdYLARTDSSEVVLNEEAVE 102
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
11-104 8.13e-09

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: 52.14  E-value: 8.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  11 RRKIpdGDTHQRDVCSTCGYVHyvnpkIVTGAIVLH-DGRILLCRRA----IAPriGFWTL-PAGFMELGETAEQAAVRE 84
Cdd:cd04693    10 RNKT--GRTHRRGEPLPEGEYH-----LVVHVWIFNsDGEILIQQRSpdkkGFP--GMWEAsTGGSVLAGETSLEAAIRE 80
                          90       100
                  ....*....|....*....|
gi 1519817542  85 AREEANAEIAIERLLAVYTI 104
Cdd:cd04693    81 LKEELGIDLDADELRPILTI 100
NUDIX_Hydrolase cd04686
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
42-103 5.13e-08

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: 467569 [Multi-domain]  Cd Length: 130  Bit Score: 49.21  E-value: 5.13e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  42 AIVLHDGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT 103
Cdd:cd04686     6 GIIIRNDKLLLIRKTRGPYQGRYDLPGGSQEFGESLEDALKREFAEETGMTVTSYDNLGVYD 67
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
47-146 5.29e-08

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: 467568 [Multi-domain]  Cd Length: 138  Bit Score: 49.49  E-value: 5.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  47 DGRILLCR--RAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLL-------AVYTI--PRIAQVQIMYL 115
Cdd:cd04685    11 DGRVLLFRfhDPDDPGRSWWFTPGGGVEPGESPEQAAVRELREETGLRLEPDDLGgpvwrrrAVFDFsgETVRQDERFFL 90
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519817542 116 ARLTSATISPGPES-LEV-VLAGWGEIPWAELA 146
Cdd:cd04685    91 VRVPAFEVDTAGWTdLERaVIDGHRWWSLAELA 123
Nudix_N_2 pfam14803
Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate ...
11-32 5.73e-08

Nudix N-terminal; Ths domain occurs at the N-terminus of several Nudix (Nucleoside Diphosphate linked to X) hydrolases.


Pssm-ID: 464323  Cd Length: 32  Bit Score: 46.71  E-value: 5.73e-08
                          10        20
                  ....*....|....*....|..
gi 1519817542  11 RRKIPDGDTHQRDVCSTCGYVH 32
Cdd:pfam14803  11 ELRIPDGDNRPRLVCTACGTIH 32
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
41-153 5.76e-08

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: 49.49  E-value: 5.76e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVLH-DGRILLCRRAIAPriGFWTLPAGFMELGETAEQAAVREAREE-----ANAEI--AIERLLAvYTIPR------ 106
Cdd:cd03671     7 GIVLFNrDGQVLVGRRIDVP--GAWQFPQGGIDEGEDPEEAALRELYEEtglspEDVEIiaETPDWLT-YDLPEdlirkg 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519817542 107 -----IAQVQIMYLARLTsatispGPESlEVVLAGWGEipwAElaFPSVRWV 153
Cdd:cd03671    84 wggkyRGQKQKWFLFRFT------GDDS-EINLDTHEH---PE--FDAWRWV 123
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
38-105 7.63e-08

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: 467572 [Multi-domain]  Cd Length: 123  Bit Score: 48.69  E-value: 7.63e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  38 IVTGAIVLHDGRILLCRRAIAPRigfWTLPAGFMELGETAEQAAVREAREEANAEIAIERL--LAVYTIP 105
Cdd:cd04690     2 VKAAVIIIKDGRLLLVRKRGTDA---FYLPGGKREPGETPLQALVRELKEELGLDLDPDSLrfLGTFEAP 68
NUDIX_Hydrolase cd03675
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
42-103 1.44e-07

uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase from Nitrosomonas europaea, which has an unknown function. 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: 467543 [Multi-domain]  Cd Length: 138  Bit Score: 48.29  E-value: 1.44e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  42 AIVLHDGRILLCRRAIAPRIGFwTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT 103
Cdd:cd03675     5 AVVERDGRFLLVEEETDGRLVL-NQPAGHLEPGESLLEAAIRETLEETGWEVEPTALLGIYQ 65
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
42-88 1.78e-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: 467552 [Multi-domain]  Cd Length: 117  Bit Score: 47.66  E-value: 1.78e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1519817542  42 AIVLHDGRILLCRRaiapRIGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd04667     5 VICRRGDRILLVAR----RGGRWLLPGGKIEPGESPLEAAIRELKEE 47
NUDIX_RppH cd04665
RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of ...
42-109 1.79e-07

RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of its 5' end. In eukaryotes, the 5'-methylguanosine (cap) structure is principally removed by the NUDIX family decapping enzyme Dcp2, yielding a 5'-monophosphorylated RNA that is a substrate for 5' exoribonucleases. In bacteria, the 5'-triphosphate group of primary transcripts is also converted to a 5' monophosphate by a NUDIX protein called RNA pyrophosphohydrolase (RppH), allowing access to both endo- and 5' exoribonucleases. 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: 467550 [Multi-domain]  Cd Length: 121  Bit Score: 47.63  E-value: 1.79e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519817542  42 AIVLHDGRILLCRRAiapRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQ 109
Cdd:cd04665     5 VIARYKGKWLFTRHK---ERRGWEFPGGKREPGETIEEAARRELYEETGAVIFELKPLGQYSVHGKGQ 69
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
48-98 2.04e-07

dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of dihydroneopterin triphosphate (DHNTP) to dihydroneopterin monophosphate (DHNMP) and pyrophosphate,the second step in the pterin branch of the folate synthesis pathway in bacteria. 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: 467549 [Multi-domain]  Cd Length: 132  Bit Score: 47.63  E-value: 2.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519817542  48 GRILLCRRAIAPriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERL 98
Cdd:cd04664    14 GEVLLLKRTDDG--GFWQSVTGGIEDGETPWQAALRELKEETGLDPLELQL 62
NUDIX_ADPRase cd24160
Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ...
43-133 2.63e-07

Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ADP-ribose pyrophosphatase (ADPRase) such as found in extreme thermophile Thermus thermophilus (TtADPRase) catalyzes the hydrolysis of ADPR to AMP and ribose 5'-phosphate in the presence of Mg2+ and Zn2+ ions. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as 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 site/catalytic site.


Pssm-ID: 467608 [Multi-domain]  Cd Length: 151  Bit Score: 47.88  E-value: 2.63e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  43 IVLHDGRiLLCRRAIAPRIGFWTL--PAGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIPRIAQvQIMYLARLTS 120
Cdd:cd24160    27 LALREGR-MLFVRQMRPAVGAATLeiPAGLIDPGETPEEAARRELAEETGLSGDLTYLTRFYVSPGFCD-EKLHVFLAEN 104
                          90
                  ....*....|....*..
gi 1519817542 121 ATISPGP----ESLEVV 133
Cdd:cd24160   105 LREVEAHpdedEAIEVV 121
PRK08999 PRK08999
Nudix family hydrolase;
37-88 2.67e-07

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 49.10  E-value: 2.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519817542  37 KIVTGAIVLHDGRILLCRRA-IAPRIGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:PRK08999    6 HVAAGVIRDADGRILLARRPeGKHQGGLWEFPGGKVEPGETVEQALARELQEE 58
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
64-105 2.69e-07

Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as 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 site/catalytic site.


Pssm-ID: 467603 [Multi-domain]  Cd Length: 187  Bit Score: 48.29  E-value: 2.69e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1519817542  64 WTL--PAGFMELGETAEQAAVREAREEANAEI-AIERLLAVYTIP 105
Cdd:cd24155    76 WLLeiVAGMIDAGETPEDVARREAEEEAGLTLdALEPIASYYPSP 120
NUDIX_DR1025_like cd04700
DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX ...
41-102 3.87e-07

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: 47.21  E-value: 3.87e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  41 GAIVLHD-GRILLCRRAIAP----RIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY 102
Cdd:cd04700    17 GVVLLNErGDILLVQEKGISghpeKAGLWHIPSGAVEDGENPQDAAVREACEETGLRVRLVKFLGAY 83
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
39-103 5.54e-07

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 46.66  E-value: 5.54e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519817542  39 VTGAIVLHDGRILLCRR-AIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVYT 103
Cdd:PRK10546    6 VVAAIIERDGKILLAQRpAHSDQAGLWEFAGGKVEPGESQPQALIRELREELGIEATVGEYVASHQ 71
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
47-105 6.65e-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: 467574 [Multi-domain]  Cd Length: 142  Bit Score: 46.40  E-value: 6.65e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519817542  47 DGRILLCRRA----IAPriGFWTLP-AGFMELGETAEQAAVREAREEANAEIAIERLLAVYTIP 105
Cdd:cd04692    38 EGRLLLQKRSankdDFP--GLWDISaAGHIDAGETYEEAAVRELEEELGLTVSPEDLIFLGVIR 99
NUDIX_DIPP2_like_Nudt4 cd04666
diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 and similar proteins; Diadenosine 5', ...
64-106 1.03e-06

diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 and similar proteins; Diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 (DIPP2), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 4; Nudt4, and other proteins including DIPP1/Nudt3, DIPP3a;APS2/Nudt10 and DIPP3beta;APS1/Nudt11. DIPP regulates the turnover of diphosphoinositol polyphosphates. The turnover of these high-energy diphosphoinositol polyphosphates represents a molecular switching activity with important regulatory consequences. Molecular switching by diphosphoinositol polyphosphates may contribute to regulating intracellular trafficking. Several alternatively spliced transcript variants have been described, but the full-length nature of some variants has not been determined. Isoforms DIPP2alpha and DIPP2beta are distinguishable from each other solely by DIPP2beta possessing one additional amino acid due to intron boundary skidding in alternate splicing. 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: 467551 [Multi-domain]  Cd Length: 128  Bit Score: 45.60  E-value: 1.03e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1519817542  64 WTLPAGFMELGETAEQAAVREAREEANAE-IAIERLLAVYTIPR 106
Cdd:cd04666    28 WILPKGGPEKGETPAEAAAREAWEEAGVRgKVLKRPLGVYRYRK 71
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
41-88 1.28e-06

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: 45.61  E-value: 1.28e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542  41 GAIVLHD-GRILLCRRAIAPRiGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd04670     6 GGLVINEnNEVLVVQEKYGGP-GGWKLPGGLVDPGEDIGEAAVREVFEE 53
nudB PRK09438
dihydroneopterin triphosphate pyrophosphatase; Provisional
43-98 3.29e-06

dihydroneopterin triphosphate pyrophosphatase; Provisional


Pssm-ID: 236516 [Multi-domain]  Cd Length: 148  Bit Score: 44.88  E-value: 3.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519817542  43 IVLH--DGRILLCRRAIAPriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERL 98
Cdd:PRK09438   12 VVIYtpDLGVLMLQRADDP--DFWQSVTGSLEEGETPAQTAIREVKEETGIDVLAEQL 67
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
38-150 3.41e-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: 467542 [Multi-domain]  Cd Length: 130  Bit Score: 44.56  E-value: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  38 IVTGAIVLHD--GRILLCRRaiaPRIGFWTLPAGFMELGETAEQAAVREAREEAnaeiAIERLLAVYTIPRIAQVQIM-- 113
Cdd:cd03674     2 FTASAFVVNPdrGKVLLVHH---RKLGRWLQPGGHVEPDEDPLEAALREAREET----GLDVELLSPLSPDPLDIDVHpi 74
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519817542 114 ---------------YLARLTSATISPGP-ESLEVvlaGWgeIPWAELAFPSV 150
Cdd:cd03674    75 panpgepahlhldvrYLAVADGDEALRKSdESSDV---RW--FPLDELEELSM 122
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
37-172 7.75e-06

mutator mutT protein; All proteins in this family for which functions are known are involved in repairing oxidative damage to dGTP (they are 8-oxo-dGTPases). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Lowering the threshold picks up members of MutT superfamily well. [DNA metabolism, DNA replication, recombination, and repair]


Pssm-ID: 200031 [Multi-domain]  Cd Length: 128  Bit Score: 43.32  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  37 KIVTGAIVLHD-GRILLCRRAIAPRIG-FWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV--YTIPRIAQVQI 112
Cdd:TIGR00586   4 QQIAVGIIRNEnGEIIITRRADGHMFAkLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKLeyEFYPRHITLWF 83
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542 113 MYLARLtsatispgpeslevvlagWGEiPWAELAFPSVRWVLeqyQTVQGrDDFAPFANP 172
Cdd:TIGR00586  84 WLLERW------------------EGG-PPGKEGQPEEWWVL---VGLLA-DDFFPAANP 120
PRK15472 PRK15472
nucleoside triphosphatase NudI; Provisional
37-88 7.95e-06

nucleoside triphosphatase NudI; Provisional


Pssm-ID: 185369 [Multi-domain]  Cd Length: 141  Bit Score: 43.58  E-value: 7.95e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1519817542  37 KIVTGAIVLHDGRILLCR----RAIAPriGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:PRK15472    4 RTIVCPLIQNDGAYLLCKmaddRGVFP--GQWALSGGGVEPGERIEEALRREIREE 57
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
47-146 8.97e-06

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: 43.65  E-value: 8.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  47 DGRILLCRRA----IAPriGFWTLP-AGFMELGETAEQAAVREAREEANAEIAiERLLAVYTIPRIAQVQI--------- 112
Cdd:COG1443    40 DGRLLLQRRAltkdHWP--GLWDNTvCGHPRAGETYEEAAVRELEEELGITVD-DDLRPLGTFRYRAVDANglvenefch 116
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1519817542 113 MYLARLTsATISPGPEslEVvlAGWGEIPWAELA 146
Cdd:COG1443   117 VFVARLD-GPLTPQPE--EV--AEVRWVTLEELL 145
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
37-90 1.65e-05

MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside diphosphate-linked moiety X)) motif 1 (Nudt1), is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain 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. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467533 [Multi-domain]  Cd Length: 136  Bit Score: 42.52  E-value: 1.65e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519817542  37 KIVTGAIVLHD-GRILLCRRAiapR---IGFWTLPAGFMELGETAEQAAVREAREEAN 90
Cdd:cd03427     1 KLTTLVFVLRGdDRVLLGLKK---RgfgAGKWNGFGGKVEPGETIEEAAVRELEEEAG 55
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
53-89 4.07e-05

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 41.51  E-value: 4.07e-05
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1519817542  53 CRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEA 89
Cdd:PRK10776   22 RRAADAHMAGKWEFPGGKIEAGETPEQALIRELQEEV 58
NUDIX_NudI cd04696
NUDIX hydrolase subfamily; Nucleoside triphosphatase NudI catalyzes the hydrolysis of ...
37-96 6.20e-05

NUDIX hydrolase subfamily; Nucleoside triphosphatase NudI catalyzes the hydrolysis of nucleoside triphosphates, with a preference for pyrimidine deoxynucleoside triphosphates (dUTP, dTTP and dCTP). It is a members of the NUDIX hydrolase superfamily which 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: 467577 [Multi-domain]  Cd Length: 134  Bit Score: 41.07  E-value: 6.20e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519817542  37 KIVTGAIVLHDGRILLCR----RAIAPriGFWTLPAGFMELGETAEQAAVREAREEANAEIAIE 96
Cdd:cd04696     2 RTIVCPLIENEGCYLLCKmaddRGVFP--GQWALSGGGVEPGERIEEALRREIREELGEQLILS 63
NUDIX_Hydrolase cd18877
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
62-89 7.08e-05

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: 467589 [Multi-domain]  Cd Length: 141  Bit Score: 40.80  E-value: 7.08e-05
                          10        20
                  ....*....|....*....|....*...
gi 1519817542  62 GFWTLPAGFMELGETAEQAAVREAREEA 89
Cdd:cd18877    47 GTWALPGGARDSGETPEAAALRETEEET 74
NUDIX_GDPMH_NudD cd03430
GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose ...
43-102 7.27e-05

GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose mannosyl hydrolase/GDPMH, is a member of the NUDIX hydrolase superfamily. This class of enzymes is unique from other members of the superfamily in two aspects. First, it contains a modified NUDIX signature sequence. The slight changes to the conserved sequence motif, GX5EX7REUXEEXGU, where U = I, L or V), are believed to contribute to the removal of all magnesium binding sites but one, retaining only the metal site that coordinates the pyrophosphate of the substrate. Secondly, it is not a pyrophosphatase that substitutes at a phosphorus; instead, it hydrolyzes nucleotide sugars such as GDP-mannose to GDP and mannose, cleaving the phosphoglycosyl bond by substituting at a carbon position. GDP-mannose provides mannosyl components for cell wall synthesis and is required for the synthesis of other glycosyl donors (such as GDP-fucose and colitose) for the cell wall. The importance of GDP-sugar hydrolase activities is thus closely related to the regulation of cell wall biosynthesis. Enzymes in this family are believed to regulate the concentration of GDP-mannose and GDP-glucose in the bacterial cell wall.


Pssm-ID: 467536 [Multi-domain]  Cd Length: 146  Bit Score: 41.07  E-value: 7.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519817542  43 IVLH-DGRILLCRRAIAPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIE--RLLAVY 102
Cdd:cd03430    21 IIRNeDGEILLGKRNNRPAQGYWFVPGGRILKNETLDDAFKRIAREELGLEVTINaaEFLGVY 83
NUDIX_Hydrolase cd04682
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
43-88 8.94e-05

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: 467565 [Multi-domain]  Cd Length: 123  Bit Score: 40.35  E-value: 8.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1519817542  43 IVLHDGRILLCRRAIAPRI---GFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd04682     6 ALFLGDKLLTILRDDKPGIpfpNLWDLPGGGREGDETPFACVLRELREE 54
NUDIX_Hydrolase cd04663
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
46-89 1.00e-04

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: 467548 [Multi-domain]  Cd Length: 132  Bit Score: 40.35  E-value: 1.00e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1519817542  46 HDGRILLCRRAIAPRIGFwTLPAGFMELGETAEQAAVREAREEA 89
Cdd:cd04663    11 RNRELLVFEHPDFPEAGL-QVPKGTVEPGESPEEAALRELAEET 53
NUDIX_ADPRase_Nudt5 cd18888
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX ...
66-88 1.28e-04

ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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.


Pssm-ID: 467598 [Multi-domain]  Cd Length: 149  Bit Score: 40.16  E-value: 1.28e-04
                          10        20
                  ....*....|....*....|...
gi 1519817542  66 LPAGFMELGETAEQAAVREAREE 88
Cdd:cd18888    37 FPAGLVDPGESPEQAALRELKEE 59
PRK00714 PRK00714
RNA pyrophosphohydrolase; Reviewed
41-128 1.37e-04

RNA pyrophosphohydrolase; Reviewed


Pssm-ID: 234820 [Multi-domain]  Cd Length: 156  Bit Score: 40.14  E-value: 1.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  41 GAIVLH-DGRILLCRRAiaPRIGFWTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAV------YTIPR------- 106
Cdd:PRK00714   12 GIILLNrQGQVFWGRRI--GQGHSWQFPQGGIDPGETPEQAMYRELYEEVGLRPEDVEILAEtrdwlrYDLPKrlvrrsk 89
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1519817542 107 ---IAQVQIMYLARLTS--ATI----SPGPE 128
Cdd:PRK00714   90 gvyRGQKQKWFLLRLTGddSEInlntTSHPE 120
NUDIX_ADPRase_NudF cd24159
Bdellovibrio Bacteriovorus nucleoside diphosphate sugar hydrolase, and similar proteins; ...
13-88 3.04e-04

Bdellovibrio Bacteriovorus nucleoside diphosphate sugar hydrolase, and similar proteins; Bdellovibrio bacteriovorus nucleoside diphosphate sugar (NDPS) hydrolase Bd3179 has been shown to similarities to the Escherichia coli adenosine diphosphate ribose (ADPR) hydrolase and the guanosine diphosphate mannose (GDPM) hydrolase. It may have a role when Bdellovibrio degrades and metabolizes host cell. ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as 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 site/catalytic site.


Pssm-ID: 467607 [Multi-domain]  Cd Length: 173  Bit Score: 39.67  E-value: 3.04e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519817542  13 KIPDGDTHQRDvcstcgYVHYvnPKIVTGAIVLHDGRILLCRRAIAP-RIGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd24159    26 RLPDGSTSTRE------YITH--PGAVAVVPLLDDGRVVMERQYRYPlKRVFLEFPAGKIDPGEDTLETAKRELLEE 94
NUDIX_Hydrolase cd18875
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
43-93 3.30e-04

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: 467587 [Multi-domain]  Cd Length: 144  Bit Score: 39.09  E-value: 3.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1519817542  43 IVLHDGRILLCRRaiaPRIGF--WTLPAGFMELGETAEQAAVREAREEANAEI 93
Cdd:cd18875     9 IYDGEDRVLVLDR---VKKDWggYTFPGGHVEPGESFVDSVIREVKEETGLTI 58
NUDIX_ADPRase_Rv1700 cd24158
ADP-ribose pyrophosphatase from Mycobacterium tuberculosis (Mt-ADPRase), and similar proteins; ...
47-117 4.99e-04

ADP-ribose pyrophosphatase from Mycobacterium tuberculosis (Mt-ADPRase), and similar proteins; Mycobacterium tuberculosis ADP-ribose pyrophosphatase mt-ADPRase(also called Rv1700) is a NUDIX protein that catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 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. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as 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 site/catalytic site.


Pssm-ID: 467606 [Multi-domain]  Cd Length: 174  Bit Score: 39.13  E-value: 4.99e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519817542  47 DGRILLCRRAIAP-RIGFWTLPAGFMEL-GETAEQAAVREAREEANAEIA-IERLLAVYTIPRI-AQVQIMYLAR 117
Cdd:cd24158    48 DGRVLLIRQYRHPvRRRLWELPAGLLDVaGEPPLEAAARELAEEADLEAArWEVLVDLFTSPGFsSEAVRVYLAR 122
NUDIX_4 pfam14815
NUDIX domain;
39-101 5.43e-04

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 38.06  E-value: 5.43e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519817542  39 VTGAIVLHDGRILLCRRAiAPRI--GFWTLPAGFMELGETAEQAAVReaREEANAEIAIERLLAV 101
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRP-EKGLlgGLWEFPGGKVEPGETLEEALAR--LEELGIEVEVLEPGTV 62
NUDIX_ADPRase_Ndx2 cd24161
NUDIX family Ndx2; NUDIX family protein Ndx2 found in Thermus thermophilus has ADP-ribose ...
63-145 5.51e-04

NUDIX family Ndx2; NUDIX family protein Ndx2 found in Thermus thermophilus has ADP-ribose pyrophosphatase (ADPRase) as well as flavin adenine dinucleotide (FAD) activity. 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.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: 467609 [Multi-domain]  Cd Length: 137  Bit Score: 38.31  E-value: 5.51e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  63 FWTLPAGFMELGETAEQAAVREAREEAN--AEiAIERLLAVYTIPRIA-QVQIMYLAR-LTSATISP-GPESLEVVLAgw 137
Cdd:cd24161    31 SWEIPAGGWPEGEDPEEAARRELREETGlrAE-RWTPLGRFYPSNGVSdERAHVFLATgLTPGEPAPeETEEDLEVRR-- 107

                  ....*...
gi 1519817542 138 geIPWAEL 145
Cdd:cd24161   108 --VPLAEA 113
NUDIX_ADPRase_NudE cd24156
NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine ...
65-167 9.35e-04

NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine nucleotide hydrolase NudE protein in Escherichia coli is a NUDIX hydrolase family member active against ADP ribose, NADH, AP2A and AP3A33, and is classified as a hydrolase (E.C. 3.6.1.-) based on gene annotations. It is an 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. 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: 467604 [Multi-domain]  Cd Length: 134  Bit Score: 37.61  E-value: 9.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  65 TLPAGFMELGETAEQAAVREAREEAN-AEIAIERLLAVYTIPRI--AQVQIMyLARLTSATISPG--PESLEVvlagwge 139
Cdd:cd24156    32 GFPKGLIDPGETPEEAANRELKEEIGfGARQLTLLRELSLAPSYmsHKMHIV-LARDLYPERLEGdePEPLEV------- 103
                          90       100
                  ....*....|....*....|....*...
gi 1519817542 140 ipwaelafpsVRWVLEQYQTVQGRDDFA 167
Cdd:cd24156   104 ----------VRWPLADLDELLADPDFT 121
NUDIX_eIF-2B cd18872
translation initiation factor IF-2B alpha subunit; Eukaryotic translation initiation factor 2B ...
39-88 1.23e-03

translation initiation factor IF-2B alpha subunit; Eukaryotic translation initiation factor 2B subunit alpha (EIF2B1) is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Mutations in this gene and the genes encoding other EIF2B subunits have been associated with leukoencephalopathy with vanishing white matter. 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: 467584 [Multi-domain]  Cd Length: 129  Bit Score: 37.23  E-value: 1.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519817542  39 VTGAIVLHDGRILLCRR--AIAPRIGFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd18872     2 VVTSFLFHDGKVLLFRRsdKVGTYQGRWAGISGSIESDDPPLAAAWREIREE 53
NUDIX_Hydrolase cd04684
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
42-102 1.36e-03

uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase from Enterococcus faecalis, which has an unknown function. 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: 467567 [Multi-domain]  Cd Length: 140  Bit Score: 37.22  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519817542  42 AIVLHDGRILLCRRAIAPRIgfwTLPAGFMELGETAEQAAVREAREEANAEIAIERLLAVY 102
Cdd:cd04684    20 AVIFNDEGKVLLVQTPNGGY---FLPGGGIEPGETPEEALHREVLEETGWEIEIGEFLGNA 77
nudE PRK11762
adenosine nucleotide hydrolase NudE; Provisional
65-166 1.78e-03

adenosine nucleotide hydrolase NudE; Provisional


Pssm-ID: 183303  Cd Length: 185  Bit Score: 37.48  E-value: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  65 TLPAGFMELGETAEQAAVREAREEAN--AEiAIERLLAVYTIPRI--AQVQIM-----YLARLtsatisPG--PESLEVv 133
Cdd:PRK11762   77 GFPKGLIDPGETPLEAANRELKEEVGfgAR-QLTFLKELSLAPSYfsSKMNIVlaedlYPERL------EGdePEPLEV- 148
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1519817542 134 lagwgeipwaelafpsVRWVLEQYQTVQGRDDF 166
Cdd:PRK11762  149 ----------------VRWPLADLDELLARPDF 165
COG4119 COG4119
Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General ...
62-88 2.13e-03

Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General function prediction only];


Pssm-ID: 443295 [Multi-domain]  Cd Length: 153  Bit Score: 36.73  E-value: 2.13e-03
                          10        20
                  ....*....|....*....|....*..
gi 1519817542  62 GFWTLPAGFMELGETAEQAAVREAREE 88
Cdd:COG4119    36 GAWSIPKGEYEPGEDPLAAARREFAEE 62
NUDIX_Dcp2p_Nudt20 cd03672
mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate ...
39-88 2.95e-03

mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate linked moiety X))-type motif 20/Nudt20, is required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). Its catalytic subunit, and Dcp1p are the two components of the decapping enzyme complex. Decapping is a key step in both general and nonsense-mediated 5'->3' mRNA-decay pathways. Dcp2p contains an all-alpha helical N-terminal domain and a C-terminal domain which has the NUDIX fold. While decapping is not dependent on the N-terminus of Dcp2p, it does affect its efficiency. Dcp1p binds the N-terminal domain of Dcp2p stimulating the decapping activity of Dcp2p. Decapping permits the degradation of the transcript and is a site of numerous control inputs. It is responsible for nonsense-mediated decay as well as AU-rich element (ARE)-mediated decay. In addition, it may also play a role in the levels of mRNA. Enzymes belonging to the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V).


Pssm-ID: 467540  Cd Length: 144  Bit Score: 36.38  E-value: 2.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1519817542  39 VTGAIVL---HDgRILLCRraiapriGF-----WTLPAGFMELGETAEQAAVREAREE 88
Cdd:cd03672     3 VRGAILLnedLD-KVLLVK-------GWksnssWGFPKGKINKDESDADCAIREVYEE 52
NUDIX_GDPMK cd24157
GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX ...
67-146 4.22e-03

GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX enzyme that uses GDP-mannose as the preferred substrate. It is distinct from Nudix ADP-ribose hydrolases. GDPMK and ADP-ribose pyrophosphatase seem to use similar catalytic mechanism. However, GDPMK hydrolysis does not rely on a single glutamate as the catalytic base; rather, it is dependent on residues that coordinate the magnesium ions and residues that position the substrate properly for catalysis. 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: 467605  Cd Length: 146  Bit Score: 36.00  E-value: 4.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519817542  67 PAGFMElGETAEQAAVREAREEANAEIA-IERLLAVYTIPRIAQVQI-MYLARLTSAT-ISPG------PESLEVVlagw 137
Cdd:cd24157    42 CAGLLD-GDDPEDCIRREAEEETGYRLGdLEKVFTAYSSPGIVTERIhLFIAEYSSADrVGAGgglaeeGEDIEVL---- 116

                  ....*....
gi 1519817542 138 gEIPWAELA 146
Cdd:cd24157   117 -ELPLDEAL 124
 
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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