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Conserved domains on  [gi|260605425|gb|EEX31720|]
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hypothetical protein VIC_004670 [Vibrio coralliilyticus ATCC BAA-450]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
4-134 4.36e-53

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: 164.24  E-value: 4.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEF 83
Cdd:cd18880    1 RIRAKAIIIEDGKLLLVKHRDEGGIFYILPGGGQEHGE-TLPEALKRECLEETGLDVEVGDLLFVREYIGPNKPVHQVEL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  84 FYRVSRYHGEPHIENLAGLNdeeyIQSVEWVPLTELNDKRMYPKELKDKVL 134
Cdd:cd18880   80 FFLCTLEGGELTLGSDPDLN----QVGVEWIPLEELDSIRLYPAILRELII 126
 
Name Accession Description Interval E-value
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
4-134 4.36e-53

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: 164.24  E-value: 4.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEF 83
Cdd:cd18880    1 RIRAKAIIIEDGKLLLVKHRDEGGIFYILPGGGQEHGE-TLPEALKRECLEETGLDVEVGDLLFVREYIGPNKPVHQVEL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  84 FYRVSRYHGEPHIENLAGLNdeeyIQSVEWVPLTELNDKRMYPKELKDKVL 134
Cdd:cd18880   80 FFLCTLEGGELTLGSDPDLN----QVGVEWIPLEELDSIRLYPAILRELII 126
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
4-126 1.11e-17

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 74.24  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLL--KVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREflesHKNRYHS 81
Cdd:COG1051    6 KVAVDAVIFRKDGRVLLvrRADEPGKGLWALPGGKVEPGE-TPEEAALRELREETGLEVEVLELLGVFD----HPDRGHV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 260605425  82 -EFFYRVSRYHGEPHIenlaglnDEEyIQSVEWVPLTELNDKRMYP 126
Cdd:COG1051   81 vSVAFLAEVLSGEPRA-------DDE-IDEARWFPLDELPELAFTP 118
NUDIX pfam00293
NUDIX domain;
4-126 6.29e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 67.12  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425    4 RIRAAGILIDNDAMLLLKVR---DFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYH 80
Cdd:pfam00293   2 RRVAVGVVLLNEKGRVLLVRrskKPFPGWWSLPGGKVEPGE-TPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 260605425   81 SEFFYRVsRYHGEPHIENLAGLNDEeyIQSVEWVPLTELNDKRMYP 126
Cdd:pfam00293  81 DEHEILY-VFLAEVEGELEPDPDGE--VEEVRWVPLEELLLLKLAP 123
PRK08999 PRK08999
Nudix family hydrolase;
1-126 2.65e-14

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 68.36  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   1 MEQRIR-AAGILIDNDAMLLLKVR---DFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGE-LICVReFLESH 75
Cdd:PRK08999   1 SMKRIHvAAGVIRDADGRILLARRpegKHQGGLWEFPGGKVEPGE-TVEQALARELQEELGIEVTAARpLITVR-HDYPD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260605425  76 KN-RYHsefFYRVSRYHGEPH-IENlaglndeeyiQSVEWVPLTELNDKRMYP 126
Cdd:PRK08999  79 KRvRLD---VRRVTAWQGEPHgREG----------QPLAWVAPDELAVYPFPP 118
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
1-94 6.76e-04

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


Pssm-ID: 200031 [Multi-domain]  Cd Length: 128  Bit Score: 37.55  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425    1 MEQRIRAAGILIDNDAMLLLKVR----DFtGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELIcvrEFLESHK 76
Cdd:TIGR00586   1 KKLQQIAVGIIRNENGEIIITRRadghMF-AKLLEFPGGKEEGGE-TPEQAVVRELEEEIGIPQHFSEFE---KLEYEFY 75
                          90
                  ....*....|....*...
gi 260605425   77 NRYHSEFFYRVSRYHGEP 94
Cdd:TIGR00586  76 PRHITLWFWLLERWEGGP 93
 
Name Accession Description Interval E-value
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
4-134 4.36e-53

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: 164.24  E-value: 4.36e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEF 83
Cdd:cd18880    1 RIRAKAIIIEDGKLLLVKHRDEGGIFYILPGGGQEHGE-TLPEALKRECLEETGLDVEVGDLLFVREYIGPNKPVHQVEL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  84 FYRVSRYHGEPHIENLAGLNdeeyIQSVEWVPLTELNDKRMYPKELKDKVL 134
Cdd:cd18880   80 FFLCTLEGGELTLGSDPDLN----QVGVEWIPLEELDSIRLYPAILRELII 126
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
3-133 2.56e-26

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: 96.46  E-value: 2.56e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   3 QRIRAAGILIDNDAMLLlkVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNR-YHS 81
Cdd:cd04688    1 FNIRVAAIIIRDGKVLL--ARGEDDDYYRLPGGRVEFGE-TSEDALVREFKEELGVEVEVVRLLFVVENFFTYDGKpFHE 77
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260605425  82 -EFFYRVSRYHGEPHIENLAGLNDEEYIQSVEWVPLTELNDKRMYPKELKDKV 133
Cdd:cd04688   78 iGFYYLVELSDEALYEQDIFFLEEDGEKLEFRWIPLEELDEIDLYPEFLKELL 130
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
4-126 1.11e-17

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 74.24  E-value: 1.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLL--KVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREflesHKNRYHS 81
Cdd:COG1051    6 KVAVDAVIFRKDGRVLLvrRADEPGKGLWALPGGKVEPGE-TPEEAALRELREETGLEVEVLELLGVFD----HPDRGHV 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 260605425  82 -EFFYRVSRYHGEPHIenlaglnDEEyIQSVEWVPLTELNDKRMYP 126
Cdd:COG1051   81 vSVAFLAEVLSGEPRA-------DDE-IDEARWFPLDELPELAFTP 118
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
6-115 5.53e-16

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: 69.36  E-value: 5.53e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   6 RAAGILI--DNDAMLLLKVRDFTGE-YWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSE 82
Cdd:cd02883    1 VAVGAVVfdDEGRVLLVRRSDGPGPgGWELPGGGVEPGE-TPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHVVV 79
                         90       100       110
                 ....*....|....*....|....*....|...
gi 260605425  83 FFYRVSRYHGEPHIEnlaglnDEEYIQSVEWVP 115
Cdd:cd02883   80 LVFLARVVGGEPPPL------DDEEISEVRWVP 106
NUDIX pfam00293
NUDIX domain;
4-126 6.29e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 67.12  E-value: 6.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425    4 RIRAAGILIDNDAMLLLKVR---DFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYH 80
Cdd:pfam00293   2 RRVAVGVVLLNEKGRVLLVRrskKPFPGWWSLPGGKVEPGE-TPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFP 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 260605425   81 SEFFYRVsRYHGEPHIENLAGLNDEeyIQSVEWVPLTELNDKRMYP 126
Cdd:pfam00293  81 DEHEILY-VFLAEVEGELEPDPDGE--VEEVRWVPLEELLLLKLAP 123
PRK08999 PRK08999
Nudix family hydrolase;
1-126 2.65e-14

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 68.36  E-value: 2.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   1 MEQRIR-AAGILIDNDAMLLLKVR---DFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGE-LICVReFLESH 75
Cdd:PRK08999   1 SMKRIHvAAGVIRDADGRILLARRpegKHQGGLWEFPGGKVEPGE-TVEQALARELQEELGIEVTAARpLITVR-HDYPD 78
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 260605425  76 KN-RYHsefFYRVSRYHGEPH-IENlaglndeeyiQSVEWVPLTELNDKRMYP 126
Cdd:PRK08999  79 KRvRLD---VRRVTAWQGEPHgREG----------QPLAWVAPDELAVYPFPP 118
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
9-131 1.81e-13

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: 63.03  E-value: 1.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   9 GILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREF-LESHKNRYHSEFFYRV 87
Cdd:cd04699    7 GVIFDNGRVLLLRRSRAGAGEWELPGGRLEPGE-SPEEALKREVKEETGLDVSVGELLDTWTFeLDPDKGVFIVTYLCRL 85
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 260605425  88 SryHGEPHienlagLNDE--EYiqsvEWVPLTELNDKRMyPKELKD 131
Cdd:cd04699   86 V--GGEVT------LSDEheEY----EWVTPEELAELEL-PEGYRR 118
NUDIX_Hydrolase cd04669
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-129 2.93e-12

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


Pssm-ID: 467553 [Multi-domain]  Cd Length: 120  Bit Score: 59.68  E-value: 2.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   6 RAAGILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDRSSKDCvVREFKEEAGLDIEAGELICvreFLESHKNRyhSEFFY 85
Cdd:cd04669    2 RAVLVIYDDDKLLLIRRTKPGEEYYVFPGGGIEPGETPEEAA-LREAVEELGLDVAVTLITL---ILRVLNDG--TQHYF 75
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 260605425  86 RVSRYHGEPhiENLAGlndEEYIQS------VEWVPLTELNDKRMYPKEL 129
Cdd:cd04669   76 LARVITGSF--GLGTG---PEFERPergtyePVWVPLTALPALNLRPPEL 120
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
10-131 2.45e-11

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


Pssm-ID: 467568 [Multi-domain]  Cd Length: 138  Bit Score: 57.97  E-value: 2.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  10 ILIDND-AMLLLKVRDF---TGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELI-CV---REFLESHKNRYHS 81
Cdd:cd04685    6 LLLDPDgRVLLFRFHDPddpGRSWWFTPGGGVEPGE-SPEQAAVRELREETGLRLEPDDLGgPVwrrRAVFDFSGETVRQ 84
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 260605425  82 -EFFYRVSRYHGEPHIenlAGLNDEE--YIQSVEWVPLTELNDKRM--YPKELKD 131
Cdd:cd04685   85 dERFFLVRVPAFEVDT---AGWTDLEraVIDGHRWWSLAELAATGEtvYPRDLAE 136
NUDIX_Hydrolase cd18875
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
18-122 1.72e-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: 467587 [Multi-domain]  Cd Length: 144  Bit Score: 55.65  E-value: 1.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  18 LLLKVR-DFTGeyWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSeFFYRVSRYHGEPHi 96
Cdd:cd18875   18 VLDRVKkDWGG--YTFPGGHVEPGE-SFVDSVIREVKEETGLTIKNPELCGIKQWINPDGERYIV-FLYKTDHFSGELL- 92
                         90       100
                 ....*....|....*....|....*..
gi 260605425  97 enlagLNDE-EyiqsVEWVPLTELNDK 122
Cdd:cd18875   93 -----SSEEgE----LFWIPIEELKKL 110
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
8-119 1.85e-10

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: 55.39  E-value: 1.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   8 AGILIDNDAMLLLKVRDFTGEYWIPPGGGMEAGDRSsKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEFFYRV 87
Cdd:cd04679    7 AAILDDGRLLLVLRLRAPEAGHWGLPGGKVDWLETV-EDAVRREILEELGLEIELTRLLCVVDQIDAADGEHWVAPVYLA 85
                         90       100       110
                 ....*....|....*....|....*....|..
gi 260605425  88 SRYHGEPHIEnlaglnDEEYIQSVEWVPLTEL 119
Cdd:cd04679   86 EIFSGEPRLM------EPEKHGGIGWFALDAL 111
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
7-121 7.72e-10

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: 53.61  E-value: 7.72e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKvRDFT---GEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKnryHSEF 83
Cdd:cd03425    4 VAAIIVDDGRVLIAQ-RPEGkhlAGLWEFPGGKVEPGE-TPEQALVRELREELGIEVEVGEPLGTVEHDYPDF---HVRL 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 260605425  84 -FYRVSRYHGEPH-IENlaglndeeyiQSVEWVPLTELND 121
Cdd:cd03425   79 hVYLCTLWSGEPQlLEH----------QELRWVTPEELDD 108
NUDIX_MutT_Nudt1 cd18883
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
7-135 9.70e-10

MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 1/Nudt1, is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467594  Cd Length: 136  Bit Score: 53.63  E-value: 9.70e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLlkVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEF--F 84
Cdd:cd18883    3 ARGVIISDEHLLL--ARVKGDDKTFLPGGHIEIGE-SAEIALVRELREELGLSCKVGRYLGAVENQWQDKEVIHVELnhL 79
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 260605425  85 YRVsryhgephieNLAGLNDEEYIQSVE------WVPLTELNDKRMYPKELKDKVLE 135
Cdd:cd18883   80 FEV----------ELQDLHTSDTPESQEphlefyWIPYNDLELHNLQPMPLRNLLLN 126
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
2-119 1.39e-09

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: 53.50  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   2 EQRIRAAGILI--DNDAMLLLKVRD--FTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICvreflESHKN 77
Cdd:COG0494   10 EHYRPAVVVVLldDDGRVLLVRRYRygVGPGLWEFPGGKIEPGE-SPEEAALRELREETGLTAEDLELLG-----ELPSP 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 260605425  78 RYHSEffyRVSRYHGEPHI-ENLAGLNDEEYIQSVEWVPLTEL 119
Cdd:COG0494   84 GYTDE---KVHVFLARGLGpGEEVGLDDEDEFIEVRWVPLDEA 123
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
7-119 6.59e-09

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


Pssm-ID: 467588 [Multi-domain]  Cd Length: 121  Bit Score: 51.05  E-value: 6.59e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDA--MLLLKV--RDFtgeyWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVrEFLESHKNRY-HS 81
Cdd:cd18876    2 AAGALFTDAAgrVLLVKPtyKDG----WELPGGVVEAGE-SPLQAARREVREELGLDVPVGRLLAV-DWVPPAGGGDdAV 75
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 260605425  82 EFFYRVSRyHGEPHIENLAgLNDEEyIQSVEWVPLTEL 119
Cdd:cd18876   76 LFVFDGGV-LTPEQAAAIR-LQDEE-LSAYRFVTPEEA 110
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
33-119 7.82e-09

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: 51.73  E-value: 7.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  33 PGGGMEAGDRSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNryhseffYRVSRYHGEPHIENLAGLNDEEyIQSVE 112
Cdd:cd03426   37 PGGKREPGDESPVETALRETEEEIGLPPESVEVLGRLDPLYTPSG-------FVVTPFVGLLDDPPPLRPNPDE-VAEVF 108

                 ....*..
gi 260605425 113 WVPLTEL 119
Cdd:cd03426  109 TVPLSFL 115
NUDIX_Hydrolase cd04686
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-131 8.18e-09

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


Pssm-ID: 467569 [Multi-domain]  Cd Length: 130  Bit Score: 51.14  E-value: 8.18e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   9 GILIDNDAMLLlkVRDFTGEY---WIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFL--ESHKNR---YH 80
Cdd:cd04686    6 GIIIRNDKLLL--IRKTRGPYqgrYDLPGGSQEFGE-SLEDALKREFAEETGMTVTSYDNLGVYDFFvpWSDKELgdvHH 82
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  81 SEFFYRVSRYHGEPHIENLAGLNDEEYIqsvEWVPLTELNDKRMYPKELKD 131
Cdd:cd04686   83 IGVFYDVELLDNNISELLQFEGQDSLGA---VWIPLQDLTELNSSPLVLKA 130
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
4-126 2.81e-08

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


Pssm-ID: 467572 [Multi-domain]  Cd Length: 123  Bit Score: 49.46  E-value: 2.81e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   4 RIRAAGILIDNDAMLLLKVRDftGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELicvrEFLESHKNRYHSE- 82
Cdd:cd04690    1 IVKAAVIIIKDGRLLLVRKRG--TDAFYLPGGKREPGE-TPLQALVRELKEELGLDLDPDSL----RFLGTFEAPAANEp 73
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 260605425  83 ------FFYRVsRYHGEPHIENlaglndEeyIQSVEWVPLTELNDKRMYP 126
Cdd:cd04690   74 gttvrmTCFTA-DYDGEPQPAA------E--IEELRWLDPADPDDDRLAP 114
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-121 3.23e-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: 467575 [Multi-domain]  Cd Length: 157  Bit Score: 49.83  E-value: 3.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   9 GILIDNDAMLLLKVRDFTGEYW-----IPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFlesHKNRYHSEF 83
Cdd:cd04693   34 VWIFNSDGEILIQQRSPDKKGFpgmweASTGGSVLAGE-TSLEAAIRELKEELGIDLDADELRPILTI---RFDNGFDDI 109
                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 260605425  84 FyrvsRYHGEPHIENLAgLNDEEyIQSVEWVPLTELND 121
Cdd:cd04693  110 Y----LFRKDVDIEDLT-LQKEE-VQDVKWVTLEEILE 141
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
7-119 4.17e-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: 467560 [Multi-domain]  Cd Length: 137  Bit Score: 49.05  E-value: 4.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKVRDFTGEyWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVRefleSHKNRYHS----- 81
Cdd:cd04677   15 AAVIILNEQGRILLQKRTDTGD-WGLPGGAMELGE-SLEETARREVFEETGLTVEELELLGVY----SGKDLYYTypngd 88
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 260605425  82 EFF-----YRVSRYHGEPHIenlaglnDEEYIQSVEWVPLTEL 119
Cdd:cd04677   89 EVYnvtavYLVRDVSGELKV-------DDEESLELRFFSLDEL 124
NUDIX_Hydrolase cd04684
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
7-88 4.19e-08

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: 49.16  E-value: 4.19e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKVRDFTGEYWIPpGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICV--REFLESHKNRY--HSE 82
Cdd:cd04684   17 GAYAVIFNDEGKVLLVQTPNGGYFLP-GGGIEPGE-TPEEALHREVLEETGWEIEIGEFLGNasRYFYSPDYDRYylNIG 94

                 ....*.
gi 260605425  83 FFYRVS 88
Cdd:cd04684   95 YFYLAE 100
NUDIX_ADPRase cd18889
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
5-89 1.13e-07

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


Pssm-ID: 467599 [Multi-domain]  Cd Length: 127  Bit Score: 47.99  E-value: 1.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   5 IRAAgiLIDNDAMLLLKVRDftgEYWIPPGGGMEAgDRSSKDCVVREFKEEAGLDIEAGELICVrefLESHKNrYHSEFF 84
Cdd:cd18889    5 TRAA--IFKDDKILLVQEKD---GRWSLPGGWVDV-NQSIKENTIKEAKEEAGLDVEPKRIIAV---LDRNKH-NKPPYA 74

                 ....*
gi 260605425  85 YRVSR 89
Cdd:cd18889   75 YGIYK 79
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
7-80 1.18e-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: 467593 [Multi-domain]  Cd Length: 130  Bit Score: 48.02  E-value: 1.18e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKVRD------FTGeYWIPPGGGMEAGdRSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYH 80
Cdd:cd18882    4 AIAILYDDRGKVLLQLRDdkpgipYPG-YWGLFGGHLEPG-ETPEEAIRRELEEEIGYEPGEFRFFLLYTEDDGEDRIRH 81
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
33-80 2.95e-07

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: 46.74  E-value: 2.95e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  33 PGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFL---ESHKNRYH 80
Cdd:cd04673   31 PGGKVELGE-TLEDAALRELREETGLEAEVVGLLTVVDVIerdEAGRVRFH 80
NUDIX_MutT_Nudt1 cd18886
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
30-121 3.44e-07

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: 46.84  E-value: 3.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  30 WIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEFFYRVSRYHGEPHIENLAGLndeeyiq 109
Cdd:cd18886   27 WNGVGGKLEPGE-SPEECAIREVFEETGLELEDLQLRGIVTFPSFDGGEDWLMYVFLAEAFSGELVESDREGI------- 98
                         90
                 ....*....|..
gi 260605425 110 sVEWVPLTELND 121
Cdd:cd18886   99 -LAWVPIDWLLN 109
NUDIX_Hydrolase cd04683
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
10-119 5.44e-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: 467566 [Multi-domain]  Cd Length: 137  Bit Score: 46.06  E-value: 5.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  10 ILIDNDAMLLLKvRDFTG---EYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELicvrEFL-----ESHKNRYHS 81
Cdd:cd04683    6 LLVRGDEVLLLR-RANTGyddGWWHLPAGHVEAGE-TVRAAAVREAKEELGVEIDPEDL----RLVhtmhrRSDGGRERI 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 260605425  82 EFFYRVSRYHGEPHI---ENLAGLndeeyiqsvEWVPLTEL 119
Cdd:cd04683   80 DFFFRATRWSGEPRNrepDKCAEL---------RWFPLDAL 111
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
5-137 1.40e-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: 44.85  E-value: 1.40e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   5 IRAAGILI---DNDAMLLLKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEagelICVREFLESHknRYHS 81
Cdd:cd03428    2 EKSAGAIIyrrDNGEIEFLLLQHSYGGHWDFPKGHVEPGE-SELETALRETKEETGLTVD----DLPPGFRETL--TYSF 74
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 260605425  82 EFF------YRVSRYHGEPHIEnlagLNDEeyIQSVEWVPLTELNDKRMYP--KELKDKVLELI 137
Cdd:cd03428   75 KEGvektvvYFLAELTPDVEVK----LSEE--HQDYKWLPYEEALQLLTYEniKELLKEANEYL 132
NUDIX_Hydrolase cd18877
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
7-126 1.72e-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: 467589 [Multi-domain]  Cd Length: 141  Bit Score: 45.04  E-value: 1.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILI-----DNDAMLLLKVR-DFT--GEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDieAGELICVREFLESHKN- 77
Cdd:cd18877   18 AAGLLLfapaeDGGPHVLLQHRaWWThqGGTWALPGGARDSGE-TPEAAALRETEEETGLD--ADTLRVVGTHVDDHGGw 94
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 260605425  78 RYHSeFFYRVsryhgePHIENLAGLNDEeyiqSVE--WVPLTELNDKRMYP 126
Cdd:cd18877   95 SYTT-VLASA------PEPLPVRPANEE----SVElrWVPLDEVESLPLHP 134
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
5-119 3.43e-06

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


Pssm-ID: 467554 [Multi-domain]  Cd Length: 131  Bit Score: 44.07  E-value: 3.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   5 IRAAGILI-DNDAMLLLKVRDFTGEYWIPPGGGMEAGDRSSkDCVVREFKEEAGLDIEAGELICVREFlesHKNRYHSEF 83
Cdd:cd04670    3 VGVGGLVInENNEVLVVQEKYGGPGGWKLPGGLVDPGEDIG-EAAVREVFEETGIDTEFVSILGFRHQ---HPGRFGKSD 78
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 260605425  84 FYRVSRYHGEPHIENLAglnDEEYIQSVEWVPLTEL 119
Cdd:cd04670   79 LYFVCRLRPLSDEEIKI---CPEEIAEAKWMPLEEY 111
NUDIX_CDP-Chase_like cd04672
CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ...
5-80 3.56e-06

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: 43.70  E-value: 3.56e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 260605425   5 IRAAgiLIDNDAMLLlkVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVReflesHKNRYH 80
Cdd:cd04672    5 VRAA--VFKDGKILL--VREKSDGRWTLPGGWADVGL-SPAENAVKEVREESGYEVRARKLLAVF-----DRNKGG 70
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-118 5.24e-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: 467586 [Multi-domain]  Cd Length: 125  Bit Score: 43.43  E-value: 5.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   9 GILIDNDAMLLLKVRDFTGEY-WIPPGGGMEAGDRSsKDCVVREFKEEAGLDIEAGELICVRE--FLESHKNRYHSEFFY 85
Cdd:cd18874    6 GALIFNPDGKVLLVRSHKWNDlYGIPGGKVEWGETL-EEALKREVKEETGLDITDIRFILVQEsiNSEEFHKPAHFVFVD 84
                         90       100       110
                 ....*....|....*....|....*....|...
gi 260605425  86 RVSRYHGEPHIenlagLNDEeyIQSVEWVPLTE 118
Cdd:cd18874   85 YLARTDSSEVV-----LNEE--AVEYLWVEPEE 110
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
7-121 9.81e-06

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: 42.67  E-value: 9.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKVRDFTGEY----WIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGE---LICVREFLESHK--- 76
Cdd:cd04694    5 VVVLIEDSDDRVLLTRRAKHMRTfpgvWVPPGGHVELGE-SLLEAGLRELQEETGLEVSDIQslsLLGLWESVYPTLlsi 83
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 260605425  77 ---NRYHSEFFYRVsRYHgEPHiENLAGLN-DEEYIQSVEWVPLTELND 121
Cdd:cd04694   84 glpKRHHIVVYYLV-KLS-ESH-ENQEQLKlQEDEVDAAVWLPKSLLAK 129
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
10-96 1.38e-05

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: 42.24  E-value: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  10 ILIDNDAMLLLKVRDfTGEYWIPPGGGMEAGDRSSKDCVvREFKEEAGLDIEAGELICvrefleshknrYHSEFFYRVsR 89
Cdd:cd04664    9 RKDEEGEVLLLKRTD-DGGFWQSVTGGIEDGETPWQAAL-RELKEETGLDPLELQLID-----------LNVSNFYEI-F 74

                 ....*..
gi 260605425  90 YHGEPHI 96
Cdd:cd04664   75 DDWRPGV 81
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
27-120 1.75e-05

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 41.89  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  27 GEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFleSHKNRYHSEFFYRVSRYHGEPHienlaglNDEE 106
Cdd:PRK10776  30 AGKWEFPGGKIEAGE-TPEQALIRELQEEVGITVQHATLFEKLEY--EFPDRHITLWFWLVESWEGEPW-------GKEG 99
                         90
                 ....*....|....
gi 260605425 107 yiQSVEWVPLTELN 120
Cdd:PRK10776 100 --QPGRWVSQVALN 111
NUDIX_Hydrolase cd04682
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
29-84 2.02e-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: 41.89  E-value: 2.02e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 260605425  29 YWIPPGGGMEaGDRSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEFF 84
Cdd:cd04682   29 LWDLPGGGRE-GDETPFACVLRELREELGLALPEDRLVWERVYPSNHNPGRQSWFF 83
NUDIX_Hydrolase cd18879
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
10-119 2.08e-05

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


Pssm-ID: 467590 [Multi-domain]  Cd Length: 142  Bit Score: 41.80  E-value: 2.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  10 ILIDNDAMLLLKVRDFTGEyWIPPGGGMEAGDRSSkDCVVREFKEEAGLDIEAGELICVreflESHKNRYHSE------- 82
Cdd:cd18879   24 VVLRDAGRVLLVRRADNGR-WTPVTGIVEPGEQPA-DAAVREVLEETGVDVEVERLASV----GASPPVTYPNgdqcqyl 97
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 260605425  83 ---FFYRVSRyhGEPHIenlaglNDEEYIQsVEWVPLTEL 119
Cdd:cd18879   98 dltFRCRPVG--GEARV------NDDESLE-VGWFPVDAL 128
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
10-94 2.20e-05

MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside diphosphate-linked moiety X)) motif 1 (Nudt1), is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.


Pssm-ID: 467533 [Multi-domain]  Cd Length: 136  Bit Score: 41.75  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  10 ILIDNDAMLL-LKVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNRYHSEFFYRVS 88
Cdd:cd03427    8 VLRGDDRVLLgLKKRGFGAGKWNGFGGKVEPGE-TIEEAAVRELEEEAGLTATELEKVGRLKFEFPDDPEAMDVHVFRAD 86

                 ....*.
gi 260605425  89 RYHGEP 94
Cdd:cd03427   87 SWTGEP 92
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
9-78 3.14e-05

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: 41.39  E-value: 3.14e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260605425   9 GILI--DNDAMLLLKVRDFTGE-YWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVRE--FLESHKNR 78
Cdd:cd04678    6 GVIVlnDDGKVLLGRRKGSHGAgTWALPGGHLEFGE-SFEECAAREVLEETGLEIRNVRFLTVTNdvFEEEGKHY 79
NUDIX_Hydrolase cd04676
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
8-68 3.97e-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: 467559 [Multi-domain]  Cd Length: 144  Bit Score: 41.24  E-value: 3.97e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260605425   8 AGILIDNDAMLLLKvRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICV 68
Cdd:cd04676   21 AAVILNEDGRILLQ-RKGGLGLWSLPAGAIEPGE-HPAEAVIREVREETGLLVKPTRLLGV 79
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
30-70 8.01e-05

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: 40.37  E-value: 8.01e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 260605425  30 WIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVRE 70
Cdd:cd04671   28 WYLPAGRVEPGE-SIVEAAKREVKEETGLKCEPSTLLSVEE 67
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
7-70 8.42e-05

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: 39.98  E-value: 8.42e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260605425   7 AAGILIDNDAMLLLKVRDFTGE-YWIPPGGGMEAGDRSSKdCVVREFKEEAGLDIEAGELICVRE 70
Cdd:cd04691    4 VGGVVVKEGKVLLVKRAYGPGKgRWTLPGGFVEEGETLDE-AIVREVLEETGIDAKPVGIIGVRS 67
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
7-124 1.09e-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: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 39.86  E-value: 1.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   7 AAGILIDNDAMLLLKVRDFTGE--YWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICvrefleSHKNRYH-SEF 83
Cdd:cd04681    8 AVGVIIRNEGEILFVRRAKEPGkgKLDLPGGFVDPGE-SAEEALRRELREELGLKIPKLRYLC------SLPNTYLyKGI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 260605425  84 FYRVSRYHGEPHIENLAGLN-DEEYIQSVEWVPLTELNDKRM 124
Cdd:cd04681   81 TYKTCDLFFTAELDEKPKLKkAEDEVAELEWLDLEEIEPEKL 122
PLN02325 PLN02325
nudix hydrolase
33-86 1.65e-04

nudix hydrolase


Pssm-ID: 215184 [Multi-domain]  Cd Length: 144  Bit Score: 39.46  E-value: 1.65e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 260605425  33 PGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVRE--FLESHKNRYHSEFFYR 86
Cdd:PLN02325  39 PGGHLEFGE-SFEECAAREVKEETGLEIEKIELLTVTNnvFLEEPKPSHYVTVFMR 93
NUDIX_UDP-X_diphosphatase cd18891
UDP-X diphosphatase; UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and ...
11-68 3.22e-04

UDP-X diphosphatase; UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine, the last step of the Mur pathway of peptidoglycan biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467601 [Multi-domain]  Cd Length: 128  Bit Score: 38.53  E-value: 3.22e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 260605425  11 LIDNDAMLLLkVRDFTGEYWIPPGGGMEAGdRSSKDCVVREFKEEAGLDIEAGELICV 68
Cdd:cd18891    8 FIQNENKVLL-VQDKHTKEWALPGGFAEVG-LSPKENILKEVKEETGLHVEVERLLAV 63
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
13-116 3.33e-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: 38.69  E-value: 3.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  13 DNDAMLLLKVR-----DFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICVREFLESHKNR------YHS 81
Cdd:cd04692   36 PEEGRLLLQKRsankdDFPGLWDISAAGHIDAGE-TYEEAAVRELEEELGLTVSPEDLIFLGVIREEVIGGdfidneFVH 114
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 260605425  82 EFFYRVSRYHGEPHienlagLNDEEyIQSVEWVPL 116
Cdd:cd04692  115 VYLYETDRPLEEFK------LQPEE-VAGVVFVDL 142
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-80 3.73e-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: 467552 [Multi-domain]  Cd Length: 117  Bit Score: 38.03  E-value: 3.73e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 260605425   6 RAAGILIDNDAMLLlkVRDfTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDieAGELICVREFlESHKNRYH 80
Cdd:cd04667    2 RATVICRRGDRILL--VAR-RGGRWLLPGGKIEPGE-SPLEAAIRELKEETGLA--ALSLLYLFEH-EGPHKLHH 69
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
30-126 4.14e-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: 4.14e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  30 WIPPGGGMEaGDRSSKDCVVREFKEEAGLDIE-----AGELICV-REFLESHKNR---YHSEFFYRVsRYHGEPHIENLA 100
Cdd:cd03674   27 WLQPGGHVE-PDEDPLEAALREAREETGLDVEllsplSPDPLDIdVHPIPANPGEpahLHLDVRYLA-VADGDEALRKSD 104
                         90       100
                 ....*....|....*....|....*.
gi 260605425 101 GLNDeeyiqsVEWVPLTELNDKRMYP 126
Cdd:cd03674  105 ESSD------VRWFPLDELEELSMDP 124
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-119 5.83e-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: 37.61  E-value: 5.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   9 GILIDNDAMLLLkVRDFTGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAG-ELICVreflesHKNRYHSE----F 83
Cdd:cd04680    5 AIVLDDAGRVLL-VRHTYVPGWYLPGGGVDKGE-TAEEAARRELREEAGVVLTGPpRLFGV------YFNRRVSPrdhvA 76
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 260605425  84 FYRVSRYHGEPHIENlaglNDEeyIQSVEWVPLTEL 119
Cdd:cd04680   77 LYRVREFEQTEPPEP----NGE--IAEAGFFALDAL 106
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
43-119 6.67e-04

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: 37.87  E-value: 6.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  43 SSKDCVVREFKEEAGLDI-----EAGELICVREFLESHKNRYHSEFFyrVSRYHGEPHienlagLNDEEyIQSVEWVPLT 117
Cdd:COG1443   72 TYEEAAVRELEEELGITVdddlrPLGTFRYRAVDANGLVENEFCHVF--VARLDGPLT------PQPEE-VAEVRWVTLE 142

                 ..
gi 260605425 118 EL 119
Cdd:COG1443  143 EL 144
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
1-94 6.76e-04

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


Pssm-ID: 200031 [Multi-domain]  Cd Length: 128  Bit Score: 37.55  E-value: 6.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425    1 MEQRIRAAGILIDNDAMLLLKVR----DFtGEYWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELIcvrEFLESHK 76
Cdd:TIGR00586   1 KKLQQIAVGIIRNENGEIIITRRadghMF-AKLLEFPGGKEEGGE-TPEQAVVRELEEEIGIPQHFSEFE---KLEYEFY 75
                          90
                  ....*....|....*...
gi 260605425   77 NRYHSEFFYRVSRYHGEP 94
Cdd:TIGR00586  76 PRHITLWFWLLERWEGGP 93
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
33-119 7.90e-04

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: 37.49  E-value: 7.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  33 PGGGMEAGDrSSKDCVVREFKEEAGLdiEAGELICVREFLES---HKNRYHSeFFYRVSRYHGEPHienlagLNDEEYIQ 109
Cdd:cd03424   34 PAGKIDPGE-DPEEAARRELEEETGY--TAGDLELLGSFYPSpgfSDERIHL-FLAEDLTPVSEQA------LDEDEFIE 103
                         90
                 ....*....|
gi 260605425 110 sVEWVPLTEL 119
Cdd:cd03424  104 -VVLVPLEEA 112
PRK15472 PRK15472
nucleoside triphosphatase NudI; Provisional
1-57 1.63e-03

nucleoside triphosphatase NudI; Provisional


Pssm-ID: 185369 [Multi-domain]  Cd Length: 141  Bit Score: 36.65  E-value: 1.63e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 260605425   1 MEQRIRAAGILIDNDAMLLLKVRD----FTGEyWIPPGGGMEAGDRsSKDCVVREFKEEAG 57
Cdd:PRK15472   1 MRQRTIVCPLIQNDGAYLLCKMADdrgvFPGQ-WALSGGGVEPGER-IEEALRREIREELG 59
NUDIX_Dcp2p_Nudt20 cd03672
mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate ...
41-123 2.22e-03

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


Pssm-ID: 467540  Cd Length: 144  Bit Score: 36.38  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425  41 DRSSKDCVVREFKEEAGLDIeaGELICVREFLESHKNRYHSEFFYRvsryHGEPHIENLAGLNDEEyIQSVEWVPLTELN 120
Cdd:cd03672   38 DESDADCAIREVYEETGFDI--SDLINDKDYIELTINGQRVRLYII----PGVPEDTPFEPQTRKE-ISKIEWFDIDDLP 110

                 ...
gi 260605425 121 DKR 123
Cdd:cd03672  111 KNK 113
NUDIX_Tnr3_like cd03676
thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a ...
34-61 2.75e-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: 36.32  E-value: 2.75e-03
                         10        20
                 ....*....|....*....|....*...
gi 260605425  34 GGGMEAGDrSSKDCVVREFKEEAGLDIE 61
Cdd:cd03676   44 AGGVPAGE-SPLETLVREAEEEAGLPED 70
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-119 3.21e-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: 467578 [Multi-domain]  Cd Length: 157  Bit Score: 36.06  E-value: 3.21e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   6 RAAGILIDNDAMLLLKVR-----DFTGEYWIP-PGGGMEAGDrSSKDCVVREFKEEAGLDIeaGELICVREFL-ESHKNR 78
Cdd:cd04697   27 RATYIVVRNAAGRLLVQKrtmdkDYCPGYLDPaTGGVVGAGE-SYEENARRELEEELGIDG--VPLRPLFTFYyEDDRSR 103
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 260605425  79 YHSEFFYRVSRyhgephiENLAgLNDEEyIQSVEWVPLTEL 119
Cdd:cd04697  104 VWGALFECVYD-------GPLK-LQPEE-VAEVDWMSEDEI 135
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
29-68 3.62e-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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 35.63  E-value: 3.62e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 260605425  29 YWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAGELICV 68
Cdd:cd04511   28 YWTLPAGFMELGE-TTEQGAARETREEAGARVEIGSLYAV 66
NUDIX_Hydrolase cd04663
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
33-94 4.64e-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: 35.35  E-value: 4.64e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 260605425  33 PGGGMEAGDrSSKDCVVREFKEEAGLDiEAGELICVREFLESHKNRYHSEFFYrvSRYHGEP 94
Cdd:cd04663   31 PKGTVEPGE-SPEEAALRELAEETGLT-GARVVVDLGSHDEGFEELHQRWFFH--LCLAGEP 88
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
5-128 6.28e-03

diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site.


Pssm-ID: 467541 [Multi-domain]  Cd Length: 131  Bit Score: 34.84  E-value: 6.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 260605425   5 IRAAGILIDNDAMLLLKV----RDFTGEyWIPPGGGMEAGDrSSKDCVVREFKEEAGLDIEAG-ELICVREFLESHKNRY 79
Cdd:cd03673    1 VEAAGGVVWRGRGGGGEVllihRPRYDD-WSLPKGKLEPGE-TPEEAAVREVEEETGLRVRLGrPLGTTRYTYTRKGKGI 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 260605425  80 HSEFFYRVSRYHGEPHIEnlaglNDEEYIQSVEWVPLTELNDKRMYPKE 128
Cdd:cd03673   79 LKKVHYWLMRALGGEFLP-----QPEEEIDEVRWLPPDEARRLLTYPSD 122
 
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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