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Conserved domains on  [gi|1972242785|ref|NP_001380056|]
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Nudix hydrolase 3 [Caenorhabditis elegans]

Protein Classification

NUDIX hydrolase( domain architecture ID 10130767)

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

CATH:  3.90.79.10
EC:  3.6.-.-
Gene Ontology:  GO:0016817|GO:0009132|GO:0046872
PubMed:  15581572|16378245
SCOP:  3000098

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
54-221 2.28e-52

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


:

Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 166.90  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  54 SVLIPLVTVDGRDSVLLTKRSIHLRSHRGEVCFPGGRMDPG-ETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqADF 132
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGdESPVETALRETEEEIGLPPESVEVLGRLDPLYTP-SGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785 133 NVTPIVGYISDErvlENLVVNSDEVQAVFTIPIDELIKKagltkfQSKRMKYTLPSFDSTEFKVHhnapnEYLHSTQRVW 212
Cdd:cd03426    83 VVTPFVGLLDDP---PPLRPNPDEVAEVFTVPLSFLLDP------EPRRYETFLRSGPRGTYRVP-----FYPYEGYVIW 148

                  ....*....
gi 1972242785 213 GLSGVMLHQ 221
Cdd:cd03426   149 GLTARILSE 157
 
Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
54-221 2.28e-52

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 166.90  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  54 SVLIPLVTVDGRDSVLLTKRSIHLRSHRGEVCFPGGRMDPG-ETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqADF 132
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGdESPVETALRETEEEIGLPPESVEVLGRLDPLYTP-SGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785 133 NVTPIVGYISDErvlENLVVNSDEVQAVFTIPIDELIKKagltkfQSKRMKYTLPSFDSTEFKVHhnapnEYLHSTQRVW 212
Cdd:cd03426    83 VVTPFVGLLDDP---PPLRPNPDEVAEVFTVPLSFLLDP------EPRRYETFLRSGPRGTYRVP-----FYPYEGYVIW 148

                  ....*....
gi 1972242785 213 GLSGVMLHQ 221
Cdd:cd03426   149 GLTARILSE 157
PRK10707 PRK10707
putative NUDIX hydrolase; Provisional
41-221 6.51e-29

putative NUDIX hydrolase; Provisional


Pssm-ID: 182663  Cd Length: 190  Bit Score: 107.38  E-value: 6.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  41 PRLVSDSDANSAMSVLIPLVTvDGRDSVLLTKRSIHLRSHRGEVCFPGGRMDPGETT-TETALRETFEEIGVNAESVEIW 119
Cdd:PRK10707   20 PQPNRETLNQRQAAVLIPIVR-RPQPTLLLTQRSIHLRKHAGQVAFPGGAVDPTDASlIATALREAQEEVAIPPSAVEVI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785 120 GHLKSViRRQADFNVTPIVGYISDERVLENlvvNSDEVQAVFTIPIDELIkkagltkfqskrmkyTLPSFDSTEFKVHHN 199
Cdd:PRK10707   99 GVLPPV-DSSTGYQVTPVVGIIPPDLPYRA---NEDEVAAVFEMPLAEAL---------------HLGRYHPLDIYRRGQ 159
                         170       180
                  ....*....|....*....|....
gi 1972242785 200 APNEYL--HSTQRVWGLSGVMLHQ 221
Cdd:PRK10707  160 SHRVWLswYEQYFVWGMTAGIIRE 183
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
62-172 6.81e-21

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: 85.08  E-value: 6.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  62 VDGRDSVLLTKRSIHlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqaDFNVTPIVGYI 141
Cdd:COG0494    21 LDDDGRVLLVRRYRY-GVGPGLWEFPGGKIEPGESPEEAALRELREETGLTAEDLELLGELPSPGYT--DEKVHVFLARG 97
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1972242785 142 SDERVLENLVVNsDEVQAVFTIPIDELIKKA 172
Cdd:COG0494    98 LGPGEEVGLDDE-DEFIEVRWVPLDEALALV 127
NUDIX pfam00293
NUDIX domain;
54-173 3.08e-18

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 77.91  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  54 SVLIPLVtvDGRDSVLLTKRSihLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRQADFN 133
Cdd:pfam00293   5 AVGVVLL--NEKGRVLLVRRS--KKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1972242785 134 VTPIVGYISDERVLENLVVNSD-EVQAVFTIPIDELIKKAG 173
Cdd:pfam00293  81 DEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKL 121
 
Name Accession Description Interval E-value
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
54-221 2.28e-52

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.


Pssm-ID: 467532 [Multi-domain]  Cd Length: 158  Bit Score: 166.90  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  54 SVLIPLVTVDGRDSVLLTKRSIHLRSHRGEVCFPGGRMDPG-ETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqADF 132
Cdd:cd03426     4 AVLIPLVEGDGELHVLLTKRASHLRSHPGQIAFPGGKREPGdESPVETALRETEEEIGLPPESVEVLGRLDPLYTP-SGF 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785 133 NVTPIVGYISDErvlENLVVNSDEVQAVFTIPIDELIKKagltkfQSKRMKYTLPSFDSTEFKVHhnapnEYLHSTQRVW 212
Cdd:cd03426    83 VVTPFVGLLDDP---PPLRPNPDEVAEVFTVPLSFLLDP------EPRRYETFLRSGPRGTYRVP-----FYPYEGYVIW 148

                  ....*....
gi 1972242785 213 GLSGVMLHQ 221
Cdd:cd03426   149 GLTARILSE 157
PRK10707 PRK10707
putative NUDIX hydrolase; Provisional
41-221 6.51e-29

putative NUDIX hydrolase; Provisional


Pssm-ID: 182663  Cd Length: 190  Bit Score: 107.38  E-value: 6.51e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  41 PRLVSDSDANSAMSVLIPLVTvDGRDSVLLTKRSIHLRSHRGEVCFPGGRMDPGETT-TETALRETFEEIGVNAESVEIW 119
Cdd:PRK10707   20 PQPNRETLNQRQAAVLIPIVR-RPQPTLLLTQRSIHLRKHAGQVAFPGGAVDPTDASlIATALREAQEEVAIPPSAVEVI 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785 120 GHLKSViRRQADFNVTPIVGYISDERVLENlvvNSDEVQAVFTIPIDELIkkagltkfqskrmkyTLPSFDSTEFKVHHN 199
Cdd:PRK10707   99 GVLPPV-DSSTGYQVTPVVGIIPPDLPYRA---NEDEVAAVFEMPLAEAL---------------HLGRYHPLDIYRRGQ 159
                         170       180
                  ....*....|....*....|....
gi 1972242785 200 APNEYL--HSTQRVWGLSGVMLHQ 221
Cdd:PRK10707  160 SHRVWLswYEQYFVWGMTAGIIRE 183
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
62-172 6.81e-21

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: 85.08  E-value: 6.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  62 VDGRDSVLLTKRSIHlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqaDFNVTPIVGYI 141
Cdd:COG0494    21 LDDDGRVLLVRRYRY-GVGPGLWEFPGGKIEPGESPEEAALRELREETGLTAEDLELLGELPSPGYT--DEKVHVFLARG 97
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1972242785 142 SDERVLENLVVNsDEVQAVFTIPIDELIKKA 172
Cdd:COG0494    98 LGPGEEVGLDDE-DEFIEVRWVPLDEALALV 127
NUDIX pfam00293
NUDIX domain;
54-173 3.08e-18

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 77.91  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  54 SVLIPLVtvDGRDSVLLTKRSihLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRQADFN 133
Cdd:pfam00293   5 AVGVVLL--NEKGRVLLVRRS--KKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1972242785 134 VTPIVGYISDERVLENLVVNSD-EVQAVFTIPIDELIKKAG 173
Cdd:pfam00293  81 DEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLLLKL 121
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
57-168 5.11e-17

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 74.63  E-value: 5.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  57 IPLVTVDG-----RDSVLLTKRSIhlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGhlksVIRRQAD 131
Cdd:COG1051     4 VPKVAVDAvifrkDGRVLLVRRAD--EPGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLG----VFDHPDR 77
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1972242785 132 FNVTpIVGYISdeRVLENLVVNSDEVQAVFTIPIDEL 168
Cdd:COG1051    78 GHVV-SVAFLA--EVLSGEPRADDEIDEARWFPLDEL 111
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
60-164 1.34e-14

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: 67.43  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  60 VTVDGRDSVLLTKRSIHlrSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLkSVIRRQADFNVTPIVg 139
Cdd:cd02883     6 VVFDDEGRVLLVRRSDG--PGPGGWELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVY-EFPDPDEGRHVVVLV- 81
                          90       100
                  ....*....|....*....|....*
gi 1972242785 140 YISDERVLENLVVNSDEVQAVFTIP 164
Cdd:cd02883    82 FLARVVGGEPPPLDDEEISEVRWVP 106
PLN02709 PLN02709
nudix hydrolase
68-170 1.85e-14

nudix hydrolase


Pssm-ID: 178311  Cd Length: 222  Bit Score: 70.14  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  68 VLLTKRSIHLRSHRGEVCFPGGRMDPGET-TTETALRETFEEIGVNAESVEIWGHLKSVIRRQAdFNVTPIVGYISDERV 146
Cdd:PLN02709   53 VILTKRSSTLSSHPGEVALPGGKRDEEDKdDIATALREAREEIGLDPSLVTIISVLEPFVNKKG-MSVAPVIGFLHDKKA 131
                          90       100
                  ....*....|....*....|....
gi 1972242785 147 LENLvVNSDEVQAVFTIPIDELIK 170
Cdd:PLN02709  132 FKPL-PNPAEVEEIFDVPLEMFLK 154
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
53-170 3.71e-13

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: 64.62  E-value: 3.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  53 MSVLIPLVTVDGRdsVLLTKRSIHLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHL---KSVIRRQ 129
Cdd:cd04694     3 VGVVVLIEDSDDR--VLLTRRAKHMRTFPGVWVPPGGHVELGESLLEAGLRELQEETGLEVSDIQSLSLLglwESVYPTL 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972242785 130 ADFNvTP----IVGYI-----SDERVLENLVVNSDEVQAVFTIPIDELIK 170
Cdd:cd04694    81 LSIG-LPkrhhIVVYYlvklsESHENQEQLKLQEDEVDAAVWLPKSLLAK 129
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
62-117 1.25e-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: 467560 [Multi-domain]  Cd Length: 137  Bit Score: 57.52  E-value: 1.25e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  62 VDGRDSVLLTKRSihlrsHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVE 117
Cdd:cd04677    20 LNEQGRILLQKRT-----DTGDWGLPGGAMELGESLEETARREVFEETGLTVEELE 70
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
59-131 3.56e-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: 467557 [Multi-domain]  Cd Length: 128  Bit Score: 55.98  E-value: 3.56e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972242785  59 LVTVDGRDSVLLTKRSihlRS-HRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRQAD 131
Cdd:cd04673     5 GAVVFRDGRVLLVRRG---NPpDAGLWSFPGGKVELGETLEDAALRELREETGLEAEVVGLLTVVDVIERDEAG 75
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
62-120 9.43e-10

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: 54.88  E-value: 9.43e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  62 VDGRDSVLLTKRsihLRSH-RGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWG 120
Cdd:cd04678    10 LNDDGKVLLGRR---KGSHgAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVRFLT 66
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
63-114 1.27e-08

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: 51.79  E-value: 1.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  63 DGRDSVLLtkrsIHlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAE 114
Cdd:cd03673    13 GGGGEVLL----IH-RPRYDDWSLPKGKLEPGETPEEAAVREVEEETGLRVR 59
NUDIX_Hydrolase cd18877
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
50-120 1.51e-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: 467589 [Multi-domain]  Cd Length: 141  Bit Score: 51.97  E-value: 1.51e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  50 NSAMSVLIPLVTVDGRDSVLLTKRSIHlrSHRGEV-CFPGGRMDPGETTTETALRETFEEIGVNAESVEIWG 120
Cdd:cd18877    16 HGAAGLLLFAPAEDGGPHVLLQHRAWW--THQGGTwALPGGARDSGETPEAAALRETEEETGLDADTLRVVG 85
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
59-126 1.67e-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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 51.42  E-value: 1.67e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972242785  59 LVTVDGRdsVLLTKRSIHLRshRGEVCFPGGRMDPGETTTETALRETFEEIGVnaeSVEIwGHLKSVI 126
Cdd:cd04511     8 LPEWEGK--VLLCRRAIEPR--KGYWTLPAGFMELGETTEQGAARETREEAGA---RVEI-GSLYAVY 67
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
58-117 2.14e-08

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: 51.39  E-value: 2.14e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972242785  58 PLVTVD--------GRDSVLLTKRSIHlrSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVE 117
Cdd:cd18873     1 PSVTVDcvifgfddGELKVLLIKRKNE--PFKGGWALPGGFVREDETLEDAARRELREETGLKDIYLE 66
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
86-118 2.30e-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: 51.41  E-value: 2.30e-08
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd03671    31 FPQGGIDEGEDPEEAALRELYEETGLSPEDVEI 63
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
59-145 3.72e-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: 50.65  E-value: 3.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  59 LVTVDGRDSVLLtkrsihLRSH------RGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGhlkSVIRRQADF 132
Cdd:cd04685     5 VLLLDPDGRVLL------FRFHdpddpgRSWWFTPGGGVEPGESPEQAAVRELREETGLRLEPDDLGG---PVWRRRAVF 75
                          90
                  ....*....|...
gi 1972242785 133 NVTPIVgYISDER 145
Cdd:cd04685    76 DFSGET-VRQDER 87
NUDIX_Hydrolase cd04674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
55-118 8.41e-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: 467558 [Multi-domain]  Cd Length: 118  Bit Score: 49.38  E-value: 8.41e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1972242785  55 VLIPLVTVdgRDSVLLTKRSIHLRshRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04674     6 VVVALLPV--RDGLLVIRRGIEPG--HGELALPGGYIEYGETWQEAAVRELREETGVEADAAEV 65
nudE PRK11762
adenosine nucleotide hydrolase NudE; Provisional
54-125 1.23e-07

adenosine nucleotide hydrolase NudE; Provisional


Pssm-ID: 183303  Cd Length: 185  Bit Score: 50.19  E-value: 1.23e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  54 SVLIplVTVDGRDSVLLTkRSIHLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEiwgHLKSV 125
Cdd:PRK11762   49 AVMI--VPILDDDTLLLI-REYAAGTERYELGFPKGLIDPGETPLEAANRELKEEVGFGARQLT---FLKEL 114
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
86-118 1.36e-07

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: 49.07  E-value: 1.36e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04670    31 LPGGLVDPGEDIGEAAVREVFEETGIDTEFVSI 63
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
66-118 1.47e-07

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: 48.68  E-value: 1.47e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972242785  66 DSVLLTKrsihLRSHRGEV-CFPGGRMDPGETTTETALRETFEEIGVNaesVEI 118
Cdd:cd18880    12 GKLLLVK----HRDEGGIFyILPGGGQEHGETLPEALKRECLEETGLD---VEV 58
NUDIX_Hydrolase cd18875
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
63-178 2.39e-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: 467587 [Multi-domain]  Cd Length: 144  Bit Score: 48.72  E-value: 2.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  63 DGRDSVLLTKRSihlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEiwghLKSVIRRQADFNVTPIV-GYI 141
Cdd:cd18875    11 DGEDRVLVLDRV---KKDWGGYTFPGGHVEPGESFVDSVIREVKEETGLTIKNPE----LCGIKQWINPDGERYIVfLYK 83
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1972242785 142 SDERVLEnlVVNSDEVQaVFTIPIDELIKKAGLTKFQ 178
Cdd:cd18875    84 TDHFSGE--LLSSEEGE-LFWIPIEELKKLPLATDFD 117
NUDIX_ADPRase_NudE cd24156
NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine ...
54-125 2.43e-07

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: 48.40  E-value: 2.43e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  54 SVLIplVTVDGRDSVLLTkRSIHLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEiwgHLKSV 125
Cdd:cd24156     4 AVMI--VPILDDDHLLLI-REYAAGTERYELGFPKGLIDPGETPEEAANRELKEEIGFGARQLT---LLREL 69
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
63-121 3.61e-07

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: 47.83  E-value: 3.61e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972242785  63 DGRdsVLLTKRSIHlRSHRG--EvcFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGH 121
Cdd:cd03425    11 DGR--VLIAQRPEG-KHLAGlwE--FPGGKVEPGETPEQALVRELREELGIEVEVGEPLGT 66
PRK00714 PRK00714
RNA pyrophosphohydrolase; Reviewed
86-118 6.37e-07

RNA pyrophosphohydrolase; Reviewed


Pssm-ID: 234820 [Multi-domain]  Cd Length: 156  Bit Score: 47.84  E-value: 6.37e-07
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:PRK00714   36 FPQGGIDPGETPEQAMYRELYEEVGLRPEDVEI 68
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
52-170 6.96e-07

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: 47.50  E-value: 6.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  52 AMSVLIplvtVDGRDSVLLTKRSIHlRSHrgevcFPG-------GRMDPGETTTETALRETFEEIGVNAESVEIwgHLKS 124
Cdd:COG1443    31 AFSVFV----FNSDGRLLLQRRALT-KDH-----WPGlwdntvcGHPRAGETYEEAAVRELEEELGITVDDDLR--PLGT 98
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972242785 125 VIRRQADFNvtpivGYISDE-------RVLENLVVNSDEVQAVFTIPIDELIK 170
Cdd:COG1443    99 FRYRAVDAN-----GLVENEfchvfvaRLDGPLTPQPEEVAEVRWVTLEELLA 146
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
86-172 9.39e-07

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: 46.73  E-value: 9.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHlksvirrqadFNVTPivgYISDERV----LENLVVNS------D 155
Cdd:cd03424    33 LPAGKIDPGEDPEEAARRELEEETGYTAGDLELLGS----------FYPSP---GFSDERIhlflAEDLTPVSeqaldeD 99
                          90
                  ....*....|....*..
gi 1972242785 156 EVQAVFTIPIDELIKKA 172
Cdd:cd03424   100 EFIEVVLVPLEEALEMI 116
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
59-120 1.23e-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: 467593 [Multi-domain]  Cd Length: 130  Bit Score: 46.48  E-value: 1.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  59 LVTVDGRDSVLLTKR----SIHlrsHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWG 120
Cdd:cd18882     6 AILYDDRGKVLLQLRddkpGIP---YPGYWGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFRFFL 68
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
50-120 1.33e-06

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: 46.33  E-value: 1.33e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1972242785  50 NSAMSVLIplvtVDGRDSVLLTkrsihlRSHRgevcFPGGR-------MDPGETTTETALRETFEEIGVNAESVEIWG 120
Cdd:cd03429     1 DPAVIVLV----TNGEDKILLA------RQPR----WPPGRysllagfVEPGETLEEAVRREVKEEVGLRVKNVRYVG 64
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
87-123 1.39e-06

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: 46.37  E-value: 1.39e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1972242785  87 PGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLK 123
Cdd:cd03427    32 FGGKVEPGETIEEAAVRELEEEAGLTATELEKVGRLK 68
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
59-168 1.69e-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: 467588 [Multi-domain]  Cd Length: 121  Bit Score: 45.66  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  59 LVTvDGRDSVLLTKRSIHLRSHrgevcFPGGRMDPGETTTETALRETFEEIGVnaeSVEIwGHLKSVIRRQADFNVTPIV 138
Cdd:cd18876     6 LFT-DAAGRVLLVKPTYKDGWE-----LPGGVVEAGESPLQAARREVREELGL---DVPV-GRLLAVDWVPPAGGGDDAV 75
                          90       100       110
                  ....*....|....*....|....*....|
gi 1972242785 139 GYISDERVLenlvvnSDEVQAVFTIPIDEL 168
Cdd:cd18876    76 LFVFDGGVL------TPEQAAAIRLQDEEL 99
NUDIX_MutT_Nudt1 cd18886
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
66-122 1.79e-06

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: 46.07  E-value: 1.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972242785  66 DSVLLTKRSIhlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHL 122
Cdd:cd18886    11 DEVLLLNRNK--KPNMGKWNGVGGKLEPGESPEECAIREVFEETGLELEDLQLRGIV 65
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
86-114 2.67e-06

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: 45.62  E-value: 2.67e-06
                          10        20
                  ....*....|....*....|....*....
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAE 114
Cdd:cd03428    32 FPKGHVEPGESELETALRETKEETGLTVD 60
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
59-120 2.68e-06

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: 45.37  E-value: 2.68e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  59 LVTVDGRdsVLLTKRSIHlrSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWG 120
Cdd:cd04691     7 VVVKEGK--VLLVKRAYG--PGKGRWTLPGGFVEEGETLDEAIVREVLEETGIDAKPVGIIG 64
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
86-122 2.93e-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: 467570 [Multi-domain]  Cd Length: 130  Bit Score: 45.23  E-value: 2.93e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHL 122
Cdd:cd04688    28 LPGGRVEFGETSEDALVREFKEELGVEVEVVRLLFVV 64
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
54-118 3.69e-06

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: 44.93  E-value: 3.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  54 SVLIPLVTVDGRDSVLLTKRSihlrsHRGEV-CFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04664     2 SVLVVIYRKDEEGEVLLLKRT-----DDGGFwQSVTGGIEDGETPWQAALRELKEETGLDPLELQL 62
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
60-118 3.85e-06

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: 44.99  E-value: 3.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1972242785  60 VTVDGRDSVLLTKRSihLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04671     6 VIINEQGEVLMIQEA--KRSCRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCEPSTL 62
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
50-114 3.99e-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: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 44.87  E-value: 3.99e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972242785  50 NSAMSVLIpLVTVDGRdsVLLTKRSIHLRshRGEVCFPGGRMDPGETTTETALRETFEEIGVNAE 114
Cdd:cd04681     4 NVAAAVGV-IIRNEGE--ILFVRRAKEPG--KGKLDLPGGFVDPGESAEEALRRELREELGLKIP 63
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
55-170 4.22e-06

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


Pssm-ID: 467575 [Multi-domain]  Cd Length: 157  Bit Score: 45.21  E-value: 4.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  55 VLIPLVTVDGRdsVLLTKRSIHLRSHRGE-VCFPGGRMDPGETTTETALRETFEEIGVNAESVEIwgHLKSVIRRQADFN 133
Cdd:cd04693    32 VHVWIFNSDGE--ILIQQRSPDKKGFPGMwEASTGGSVLAGETSLEAAIRELKEELGIDLDADEL--RPILTIRFDNGFD 107
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1972242785 134 VTPIVGYISDervLENLVVNSDEVQAVFTIPIDELIK 170
Cdd:cd04693   108 DIYLFRKDVD---IEDLTLQKEEVQDVKWVTLEEILE 141
NUDIX_DIPP2_like_Nudt4 cd04666
diadenosine 5',5'''-P1,P6-hexaphosphate hydrolase type 2 and similar proteins; Diadenosine 5', ...
57-111 5.44e-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: 44.44  E-value: 5.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972242785  57 IPLVTVDGRDSVLLtkrsIHLRSHRGEVcFPGGRMDPGETTTETALRETFEEIGV 111
Cdd:cd04666     6 LPYRITKGELEVLL----ITSRKTGRWI-LPKGGPEKGETPAEAAAREAWEEAGV 55
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
64-118 7.38e-06

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: 43.77  E-value: 7.38e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972242785  64 GRDSVLLTKRSihlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04699    11 DNGRVLLLRRS---RAGAGEWELPGGRLEPGESPEEALKREVKEETGLDVSVGEL 62
NUDIX_RppH cd04665
RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of ...
54-111 1.05e-05

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: 43.39  E-value: 1.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1972242785  54 SVLIpLVTVDGRdsVLLTKrsiHlrSHRGEVCFPGGRMDPGETTTETALRETFEEIGV 111
Cdd:cd04665     2 HVVV-IARYKGK--WLFTR---H--KERRGWEFPGGKREPGETIEEAARRELYEETGA 51
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
65-169 1.10e-05

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: 44.44  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  65 RDSVLLTKR---SIHLRSHRGEVC-FPGGRMDPGETTTETALRETFEEIGVNAESVEiwghlksvirRQADFNVTPivGY 140
Cdd:cd24155    55 RDEVVLIEQfriGALARDESPWLLeIVAGMIDAGETPEDVARREAEEEAGLTLDALE----------PIASYYPSP--GG 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1972242785 141 iSDERVLENL-VVNSDEVQA------------VFTIPIDELI 169
Cdd:cd24155   123 -STERVHLYLgLVDLSDLGGihglaeegedirVHVVPFDEAM 163
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
63-121 1.14e-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: 467572 [Multi-domain]  Cd Length: 123  Bit Score: 43.29  E-value: 1.14e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972242785  63 DGRdsvLLTKRSihlrshRGEVCF--PGGRMDPGETTTETALRETFEEIGVN--AESVEIWGH 121
Cdd:cd04690    11 DGR---LLLVRK------RGTDAFylPGGKREPGETPLQALVRELKEELGLDldPDSLRFLGT 64
NUDIX_ADPRase_NudF cd24159
Bdellovibrio Bacteriovorus nucleoside diphosphate sugar hydrolase, and similar proteins; ...
80-144 2.48e-05

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: 43.52  E-value: 2.48e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972242785  80 HRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESveiWGHLkSVIRrqadfnvtPIVGYiSDE 144
Cdd:cd24159    66 KRVFLEFPAGKIDPGEDTLETAKRELLEETGYEAQE---WAFL-TTIH--------PAIGY-SNE 117
NUDIX_Hydrolase cd04686
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
86-168 2.73e-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: 467569 [Multi-domain]  Cd Length: 130  Bit Score: 42.66  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRqADFNVTPI--VGYISDERVLENLVVN------SDEV 157
Cdd:cd04686    30 LPGGSQEFGESLEDALKREFAEETGMTVTSYDNLGVYDFFVPW-SDKELGDVhhIGVFYDVELLDNNISEllqfegQDSL 108
                          90
                  ....*....|.
gi 1972242785 158 QAVFtIPIDEL 168
Cdd:cd04686   109 GAVW-IPLQDL 118
NUDIX_AcylCoAdiphos_Nudt19 cd18870
Nucleoside diphosphate-linked moiety X)) motif 19; Acyl CoA diphosphohydrolase (also known as ...
68-111 4.25e-05

Nucleoside diphosphate-linked moiety X)) motif 19; Acyl CoA diphosphohydrolase (also known as NUDIX (nucleoside diphosphate linked moiety X))-type motif 10; Nudt19; testosterone-regulated protein rp2) has activity towards CoA, oxidized CoA and a wide range of CoA esters, including choloyl-CoA and branched-chain fatty-acyl-CoA esters. CoA is the major acyl carrier in mammals and a key cofactor in energy metabolism. Dynamic regulation of CoA in different tissues and organs supports metabolic flexibility. 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: 467582 [Multi-domain]  Cd Length: 159  Bit Score: 42.62  E-value: 4.25e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972242785  68 VLLTKRSIHLRSHRGEVCFPGGRMDPGETTTE---------------------------TALRETFEEIGV 111
Cdd:cd18870    17 VLLLRRSSTMSFMPGAYVFPGGRVDPADRDAPwagllppdvasasrpgksdpearalriAAIRETFEETGL 87
NUDIX_ADPRase_Nudt5 cd18888
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX ...
86-181 5.06e-05

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: 42.08  E-value: 5.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVeiwghlksvirrqadFNVTPIVGY---ISDERVleNLV---VNSD---- 155
Cdd:cd18888    37 FPAGLVDPGESPEQAALRELKEETGYTGEKV---------------LSVSPPLALdpgLSNANM--KLVtveVDGDdpen 99
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1972242785 156 ----------EVQAVFTIPIDELIKKagLTKFQSKR 181
Cdd:cd18888   100 qnpkqeledgEFIEVILVPLNELLER--LQELAKEE 133
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
52-170 5.19e-05

Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the NUDIX hydrolase superfamily, is a key enzyme in the isoprenoid biosynthetic pathway. Isoprenoids comprise a large family of natural products including sterols, carotenoids, dolichols and prenylated proteins. These compounds are synthesized from two precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IPP isomerase catalyzes the interconversion of IPP and DMAPP by a stereoselective antarafacial transposition of hydrogen. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains 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. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N-terminus), the core structure is highly conserved.


Pssm-ID: 467529 [Multi-domain]  Cd Length: 162  Bit Score: 42.48  E-value: 5.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  52 AMSVLIplvtVDGRDSVLLTKRSIHLR-----------SHrgevcfPGgrmdPGETTTETALRETFEEIGVNAESVEiwg 120
Cdd:cd02885    30 AFSVFL----FNSKGELLLQRRALSKYtwpglwtntccSH------PL----PGEGVEDAAQRRLREELGIPVCDLE--- 92
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972242785 121 HLKSVIRRQADFN------VTPI-VGYISDErvlenLVVNSDEVQAVFTIPIDELIK 170
Cdd:cd02885    93 ELPRFRYRATDDNglveheIDHVfVGRADGD-----PVPNPEEVSDYRWVSLEELRE 144
NUDIX_Hydrolase cd18879
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
60-114 6.41e-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: 467590 [Multi-domain]  Cd Length: 142  Bit Score: 41.80  E-value: 6.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1972242785  60 VTVDGRDSVLLTKRSihlrsHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAE 114
Cdd:cd18879    24 VVLRDAGRVLLVRRA-----DNGRWTPVTGIVEPGEQPADAAVREVLEETGVDVE 73
NUDIX_Hydrolase cd18884
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
89-168 6.64e-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: 467595 [Multi-domain]  Cd Length: 125  Bit Score: 41.24  E-value: 6.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  89 GRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRQAdfnvtpIVGYisDERVLENLVVNsDEVQAVFTIPIDEL 168
Cdd:cd18884    40 GFLEAGESPEEAVLREVKEELGLDGHEAKFIGHYAFPERNQL------IIAY--HVRARGNVKLN-EELDDYKIVPIDKL 110
NUDIX_Hydrolase cd04682
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
86-169 7.19e-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: 41.12  E-value: 7.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVN-AESVEIWGHLKSVIR---RQADFnvtpIVGYISDERVLEnlVVNSDEVQAVF 161
Cdd:cd04682    32 LPGGGREGDETPFACVLRELREELGLAlPEDRLVWERVYPSNHnpgRQSWF----FVARLPADEVDA--IRFGDEGQEWA 105

                  ....*...
gi 1972242785 162 TIPIDELI 169
Cdd:cd04682   106 LMPVDDFL 113
NUDIX_Hydrolase cd04669
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
60-111 8.49e-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: 467553 [Multi-domain]  Cd Length: 120  Bit Score: 40.80  E-value: 8.49e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972242785  60 VTVDGRDSVLLTKRSihlrSHRGEVC-FPGGRMDPGETTTETALRETFEEIGV 111
Cdd:cd04669     5 LVIYDDDKLLLIRRT----KPGEEYYvFPGGGIEPGETPEEAALREAVEELGL 53
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
59-177 1.59e-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: 467578 [Multi-domain]  Cd Length: 157  Bit Score: 40.68  E-value: 1.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  59 LVTVDGRDSVLLTKRSIHLRSHRGEV-CFPGGRMDPGETTTETALRETFEEIGVNA-------------ESVEIWGHLks 124
Cdd:cd04697    31 IVVRNAAGRLLVQKRTMDKDYCPGYLdPATGGVVGAGESYEENARRELEEELGIDGvplrplftfyyedDRSRVWGAL-- 108
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972242785 125 virrqadFNVTpivgyisderVLENLVVNSDEVQAVFTIPIDELIKKAGLTKF 177
Cdd:cd04697   109 -------FECV----------YDGPLKLQPEEVAEVDWMSEDEILQAARGEEF 144
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
66-121 1.64e-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: 467552 [Multi-domain]  Cd Length: 117  Bit Score: 39.96  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  66 DSVLLTKRSihlrshRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIWGH 121
Cdd:cd04667    11 DRILLVARR------GGRWLLPGGKIEPGESPLEAAIRELKEETGLAALSLLYLFE 60
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
86-168 1.80e-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: 467563 [Multi-domain]  Cd Length: 121  Bit Score: 39.93  E-value: 1.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEIwghLKSVIRRQADFNVTPIVGYISDERVLENLVVNSDEVQAVFTIPI 165
Cdd:cd04680    27 LPGGGVDKGETAEEAARRELREEAGVVLTGPPR---LFGVYFNRRVSPRDHVALYRVREFEQTEPPEPNGEIAEAGFFAL 103

                  ...
gi 1972242785 166 DEL 168
Cdd:cd04680   104 DAL 106
NUDIX_Hydrolase cd04684
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
60-115 1.96e-04

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: 40.30  E-value: 1.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  60 VTVDGRDSVLLTKRSihlrshRGEVCFPGGRMDPGETTTETALRETFEEIGVNAES 115
Cdd:cd04684    21 VIFNDEGKVLLVQTP------NGGYFLPGGGIEPGETPEEALHREVLEETGWEIEI 70
nudB PRK09438
dihydroneopterin triphosphate pyrophosphatase; Provisional
54-113 2.71e-04

dihydroneopterin triphosphate pyrophosphatase; Provisional


Pssm-ID: 236516 [Multi-domain]  Cd Length: 148  Bit Score: 39.88  E-value: 2.71e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  54 SVLIPLVTVDGRdsVLLTKRSIHlrshrgevcfPG------GRMDPGETTTETALRETFEEIGVNA 113
Cdd:PRK09438    9 SVLVVIYTPDLG--VLMLQRADD----------PDfwqsvtGSLEEGETPAQTAIREVKEETGIDV 62
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
73-165 2.73e-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: 467574 [Multi-domain]  Cd Length: 142  Bit Score: 39.85  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  73 RSIH---LRSHRGEVC----------FPG-------GRMDPGETTTETALRETFEEIGVNAESVEIwgHLKSVIRRQADF 132
Cdd:cd04692    27 RTVHvwlVNPEEGRLLlqkrsankddFPGlwdisaaGHIDAGETYEEAAVRELEEELGLTVSPEDL--IFLGVIREEVIG 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1972242785 133 NvtpivGYISDERV----------LENLVVNSDEVQAVFTIPI 165
Cdd:cd04692   105 G-----DFIDNEFVhvylyetdrpLEEFKLQPEEVAGVVFVDL 142
PRK08999 PRK08999
Nudix family hydrolase;
60-111 3.33e-04

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 41.01  E-value: 3.33e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1972242785  60 VTVDGRDSVLLTKRSIHlRSHRGEVCFPGGRMDPGEtTTETAL-RETFEEIGV 111
Cdd:PRK08999   11 VIRDADGRILLARRPEG-KHQGGLWEFPGGKVEPGE-TVEQALaRELQEELGI 61
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
63-118 4.47e-04

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: 39.21  E-value: 4.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972242785  63 DGRdsVLLTKRsihLRS-HRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd04679    12 DGR--LLLVLR---LRApEAGHWGLPGGKVDWLETVEDAVRREILEELGLEIELTRL 63
PLN02325 PLN02325
nudix hydrolase
66-130 4.83e-04

nudix hydrolase


Pssm-ID: 215184 [Multi-domain]  Cd Length: 144  Bit Score: 39.46  E-value: 4.83e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1972242785  66 DSVLLTKRsihlRSHRGEVCF--PGGRMDPGETTTETALRETFEEIGVNAESVEIWGHLKSVIRRQA 130
Cdd:PLN02325   20 NSVLLGRR----RSSIGDSTFalPGGHLEFGESFEECAAREVKEETGLEIEKIELLTVTNNVFLEEP 82
NUDIX_Hydrolase cd04683
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
55-119 5.98e-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: 467566 [Multi-domain]  Cd Length: 137  Bit Score: 38.74  E-value: 5.98e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972242785  55 VLIPLVTVDGrDSVLLtkrsiHLRSH----RGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIW 119
Cdd:cd04683     1 VDVHLLLVRG-DEVLL-----LRRANtgydDGWWHLPAGHVEAGETVRAAAVREAKEELGVEIDPEDLR 63
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
87-116 7.30e-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: 467542 [Multi-domain]  Cd Length: 130  Bit Score: 38.39  E-value: 7.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972242785  87 PGGRMDPGETTTETALRETFEEIGVNAESV 116
Cdd:cd03674    30 PGGHVEPDEDPLEAALREAREETGLDVELL 59
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
86-135 9.30e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 38.04  E-value: 9.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVNAESVEiwgHLKSVIRRQADFNVT 135
Cdd:PRK10776   35 FPGGKIEAGETPEQALIRELQEEVGITVQHAT---LFEKLEYEFPDRHIT 81
NUDIX_eIF-2B cd18872
translation initiation factor IF-2B alpha subunit; Eukaryotic translation initiation factor 2B ...
54-119 1.39e-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: 37.62  E-value: 1.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  54 SVLIPLVTVDGRdsVLLTKRSIHLRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEIW 119
Cdd:cd18872     1 SVVTSFLFHDGK--VLLFRRSDKVGTYQGRWAGISGSIESDDPPLAAAWREIREETGLTPEDVELL 64
NUDIX_Hydrolase cd04663
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
87-116 1.40e-03

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: 37.66  E-value: 1.40e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1972242785  87 PGGRMDPGETTTETALRETFEEIGVNAESV 116
Cdd:cd04663    31 PKGTVEPGESPEEAALRELAEETGLTGARV 60
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
59-132 1.70e-03

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 38.84  E-value: 1.70e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1972242785  59 LVTVDGRdsVLLTKRsihlRSH--RGEVCFPGGRMDPGETTTETALRETFEEIGVNAESveiwGHLKSVIRRQADF 132
Cdd:PRK05379  209 VVVQSGH--VLLVRR----RAEpgKGLWALPGGFLEQDETLLDACLRELREETGLKLPE----PVLRGSIRDQQVF 274
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
63-113 1.70e-03

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 37.41  E-value: 1.70e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1972242785  63 DGRdsVLLTKRSIHlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGVNA 113
Cdd:PRK10546   14 DGK--ILLAQRPAH-SDQAGLWEFAGGKVEPGESQPQALIRELREELGIEA 61
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
52-117 2.62e-03

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 37.64  E-value: 2.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972242785  52 AMSVLIplvtVDGRDSVLLTKRSIHLRShrgevcFPG-------GRMDPGETTTETALRETFEEIGVNAESVE 117
Cdd:PRK03759   36 AFSCYL----FDADGRLLVTRRALSKKT------WPGvwtnsccGHPQPGESLEDAVIRRCREELGVEITDLE 98
NUDIX_ADPRase_Rv1700 cd24158
ADP-ribose pyrophosphatase from Mycobacterium tuberculosis (Mt-ADPRase), and similar proteins; ...
60-146 2.76e-03

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: 37.59  E-value: 2.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  60 VTVDGRDSVLLTKRSIH-LRSHRGEVcfPGGRMD-PGETTTETALRETFEEIGVNAESveiWGHLksvirrqADFNVTPi 137
Cdd:cd24158    43 VALDDDGRVLLIRQYRHpVRRRLWEL--PAGLLDvAGEPPLEAAARELAEEADLEAAR---WEVL-------VDLFTSP- 109

                  ....*....
gi 1972242785 138 vGYiSDERV 146
Cdd:cd24158   110 -GF-SSEAV 116
NUDIX_CDP-Chase_like cd04672
CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ...
87-114 2.90e-03

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: 36.77  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|....*...
gi 1972242785  87 PGGRMDPGETTTETALRETFEEIGVNAE 114
Cdd:cd04672    29 PGGWADVGLSPAENAVKEVREESGYEVR 56
NUDIX_Hydrolase cd03675
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
82-110 3.10e-03

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: 36.73  E-value: 3.10e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1972242785  82 GEVCF--PGGRMDPGETTTETALRETFEEIG 110
Cdd:cd03675    22 GRLVLnqPAGHLEPGESLLEAAIRETLEETG 52
NUDIX_Tnr3_like cd03676
thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a ...
88-170 3.38e-03

thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a bifunctional enzyme composed of a C-terminal thiamine pyrophosphokinase domain, which transfers pyrophosphate from ATP to thiamine and an N-terminal NUDIX hydrolase domain that converts oxidized derivatives of thiamine diphosphate (oxothiamine and oxythiamine) to their respective monophosphates. 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, 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: 467544  Cd Length: 153  Bit Score: 37.09  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972242785  88 GGRMDPGETTTETALRETFEEIGVNAESVE----IWGHLkSVIRRQADFNVTPIVGYISDERVLENLV--VNSDEVQAVF 161
Cdd:cd03676    44 AGGVPAGESPLETLVREAEEEAGLPEDLARqarpAAGRV-SYFYRSDEGGLQPEVLYVYDLELPEDFVpkPQDGEVESFE 122

                  ....*....
gi 1972242785 162 TIPIDELIK 170
Cdd:cd03676   123 LMSVDEVLE 131
NUDIX_Dcp2p_Nudt20 cd03672
mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate ...
86-112 3.41e-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: 36.76  E-value: 3.41e-03
                          10        20
                  ....*....|....*....|....*..
gi 1972242785  86 FPGGRMDPGETTTETALRETFEEIGVN 112
Cdd:cd03672    30 FPKGKINKDESDADCAIREVYEETGFD 56
NUDIX_GDPMH_NudD cd03430
GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose ...
55-111 4.01e-03

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: 36.45  E-value: 4.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1972242785  55 VLIPLVTVDGRDSVLLTKRSIhlRSHRGEVCFPGGRMDPGETTTETALRETFEEIGV 111
Cdd:cd03430    16 VSIDLIIRNEDGEILLGKRNN--RPAQGYWFVPGGRILKNETLDDAFKRIAREELGL 70
NPY1 COG2816
NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];
57-111 7.87e-03

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


Pssm-ID: 442065 [Multi-domain]  Cd Length: 288  Bit Score: 36.82  E-value: 7.87e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1972242785  57 IPLVTvDGrDSVLLTkrsihlRSHRgevcFPGGR-------MDPGETTTETALRETFEEIGV 111
Cdd:COG2816   162 IVLVT-DG-DRILLA------RQAR----WPPGRysllagfVEPGETLEQAVRREVFEEVGV 211
NUDIX_U8_SnoRNA_DE_Nudt16 cd18869
nucleoside diphosphate-linked moiety X)) motif 16; U8 SnoRNA-decapping enzyme, also known as ...
65-118 9.10e-03

nucleoside diphosphate-linked moiety X)) motif 16; U8 SnoRNA-decapping enzyme, also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 16/Nudt16, is encoded by the human NUDT16 gene and a RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. 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: 467581  Cd Length: 175  Bit Score: 35.79  E-value: 9.10e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1972242785  65 RDSVLLTKRsihlrsHRGEVCFPGGRMDPGETTTETALRETFEEIGVNAESVEI 118
Cdd:cd18869    25 RATLLMQMR------FDGLLGFPGGFVDTGESLEEGLNRELREELGLAHAVFPV 72
 
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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