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The query sequence YP_001452322.1 may be preliminary or obsolete. For more information, check Entrez.
Conserved domains on  [gi|157145003|ref|YP_001452322.1|]
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hypothetical protein CKO_00734 [Citrobacter koseri ATCC BAA-895]

Protein Classification

GDP-mannose mannosyl hydrolase( domain architecture ID 10794161)

GDP-mannose mannosyl hydrolase catalyzes the hydrolysis of GDP-alpha-D-mannose or GDP-alpha-D-glucose to yield sugar and GDP in a Mg2+-dependent manner

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK15434 PRK15434
GDP-mannose mannosyl hydrolase;
1-159 2.60e-122

GDP-mannose mannosyl hydrolase;


:

Pssm-ID: 237966 [Multi-domain]  Cd Length: 159  Bit Score: 341.73  E-value: 2.60e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   1 MFLRQEDFATVVRSTPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGA 80
Cdd:PRK15434   1 MFLRQEDFATVVRSTPLISLDFIVENSRGEFLLGKRTNRPAQGYWFVPGGRVQKDETLEAAFERLTMAELGLRLPITAGQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157145003  81 FYGVWQHFYDDNFSGEDFTTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAYFLADRQSGVPGC 159
Cdd:PRK15434  81 FYGVWQHFYDDNFSGTDFTTHYVVLGFRLRVAEEDLLLPDEQHDDYRWLTPDALLASDNVHANSRAYFLAEKRAGVPGL 159
 
Name Accession Description Interval E-value
PRK15434 PRK15434
GDP-mannose mannosyl hydrolase;
1-159 2.60e-122

GDP-mannose mannosyl hydrolase;


Pssm-ID: 237966 [Multi-domain]  Cd Length: 159  Bit Score: 341.73  E-value: 2.60e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   1 MFLRQEDFATVVRSTPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGA 80
Cdd:PRK15434   1 MFLRQEDFATVVRSTPLISLDFIVENSRGEFLLGKRTNRPAQGYWFVPGGRVQKDETLEAAFERLTMAELGLRLPITAGQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157145003  81 FYGVWQHFYDDNFSGEDFTTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAYFLADRQSGVPGC 159
Cdd:PRK15434  81 FYGVWQHFYDDNFSGTDFTTHYVVLGFRLRVAEEDLLLPDEQHDDYRWLTPDALLASDNVHANSRAYFLAEKRAGVPGL 159
NUDIX_GDPMH_NudD cd03430
GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose ...
3-148 1.07e-89

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


Pssm-ID: 467536 [Multi-domain]  Cd Length: 146  Bit Score: 258.71  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   3 LRQEDFATVVRSTPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGAFY 82
Cdd:cd03430    1 LPEEDFKTVVENTPLVSIDLIIRNEDGEILLGKRNNRPAQGYWFVPGGRILKNETLDDAFKRIAREELGLEVTINAAEFL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157145003  83 GVWQHFYDDNFSGEDFTTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAYF 148
Cdd:cd03430   81 GVYEHFYDDNFSGEDFSTHYVVLAYRLKLDEGLLLLPDDQHDEYRWFTIDELLANDDVHPYTKAYF 146
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
14-136 8.95e-22

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 85.42  E-value: 8.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  14 STPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYddnf 93
Cdd:COG1051    3 KVPKVAVDAVIFRKDGRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRELREETGLE--VEVLELLGVFDHPD---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157145003  94 sgedfTTHYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERLLA 136
Cdd:COG1051   77 -----RGHVVSVAFLAEVLSGEPRADDE-IDEARWFPLDELPE 113
NUDIX pfam00293
NUDIX domain;
15-147 2.36e-20

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 82.15  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   15 TPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLsaGAFYGVWQHFYDDNFS 94
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPEL--LELLGSLHYLAPFDGR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157145003   95 GEDftTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAY 147
Cdd:pfam00293  79 FPD--EHEILYVFLAEVEGELEPDPDGEVEEVRWVPLEELLLLKLAPGDRKLL 129
 
Name Accession Description Interval E-value
PRK15434 PRK15434
GDP-mannose mannosyl hydrolase;
1-159 2.60e-122

GDP-mannose mannosyl hydrolase;


Pssm-ID: 237966 [Multi-domain]  Cd Length: 159  Bit Score: 341.73  E-value: 2.60e-122
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   1 MFLRQEDFATVVRSTPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGA 80
Cdd:PRK15434   1 MFLRQEDFATVVRSTPLISLDFIVENSRGEFLLGKRTNRPAQGYWFVPGGRVQKDETLEAAFERLTMAELGLRLPITAGQ 80
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 157145003  81 FYGVWQHFYDDNFSGEDFTTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAYFLADRQSGVPGC 159
Cdd:PRK15434  81 FYGVWQHFYDDNFSGTDFTTHYVVLGFRLRVAEEDLLLPDEQHDDYRWLTPDALLASDNVHANSRAYFLAEKRAGVPGL 159
NUDIX_GDPMH_NudD cd03430
GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose ...
3-148 1.07e-89

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


Pssm-ID: 467536 [Multi-domain]  Cd Length: 146  Bit Score: 258.71  E-value: 1.07e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   3 LRQEDFATVVRSTPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGAFY 82
Cdd:cd03430    1 LPEEDFKTVVENTPLVSIDLIIRNEDGEILLGKRNNRPAQGYWFVPGGRILKNETLDDAFKRIAREELGLEVTINAAEFL 80
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 157145003  83 GVWQHFYDDNFSGEDFTTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAYF 148
Cdd:cd03430   81 GVYEHFYDDNFSGEDFSTHYVVLAYRLKLDEGLLLLPDDQHDEYRWFTIDELLANDDVHPYTKAYF 146
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
14-136 8.95e-22

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 85.42  E-value: 8.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  14 STPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYddnf 93
Cdd:COG1051    3 KVPKVAVDAVIFRKDGRVLLVRRADEPGKGLWALPGGKVEPGETPEEAALRELREETGLE--VEVLELLGVFDHPD---- 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157145003  94 sgedfTTHYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERLLA 136
Cdd:COG1051   77 -----RGHVVSVAFLAEVLSGEPRADDE-IDEARWFPLDELPE 113
NUDIX pfam00293
NUDIX domain;
15-147 2.36e-20

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 82.15  E-value: 2.36e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   15 TPLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLsaGAFYGVWQHFYDDNFS 94
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRSKKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPEL--LELLGSLHYLAPFDGR 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157145003   95 GEDftTHYVVLGFRLKVNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRAY 147
Cdd:pfam00293  79 FPD--EHEILYVFLAEVEGELEPDPDGEVEEVRWVPLEELLLLKLAPGDRKLL 129
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
23-128 9.07e-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: 9.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDNfsgedfTTHY 102
Cdd:cd02883    6 VVFDDEGRVLLVRRSDGPGPGGWELPGGGVEPGETPEEAAVREVREETGLD--VEVLRLLGVYEFPDPDE------GRHV 77
                         90       100
                 ....*....|....*....|....*..
gi 157145003 103 VVLGFRLKVNQADL-HLPDEQHEDYRW 128
Cdd:cd02883   78 VVLVFLARVVGGEPpPLDDEEISEVRW 104
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
29-138 4.56e-11

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: 57.52  E-value: 4.56e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  29 GEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDNFSGEDFttHYVVLGFR 108
Cdd:cd04673   12 GRVLLVRRGNPPDAGLWSFPGGKVELGETLEDAALRELREETGLE--AEVVGLLTVVDVIERDEAGRVRF--HYVILDFL 87
                         90       100       110
                 ....*....|....*....|....*....|
gi 157145003 109 LKVNQADLHLPDEQhEDYRWQTPERLLASA 138
Cdd:cd04673   88 AEWVSGEPVAGDDA-LDARWFSLEELDGLP 116
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
22-146 5.14e-10

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: 55.04  E-value: 5.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLLGKRTNRPAQ-GYWFVPGGRVQKDETLENAFERLTQAELGLRLplsagafyGVWQHFYD-DNFSGEDFT 99
Cdd:COG0494   18 VVLLDDDGRVLLVRRYRYGVGpGLWEFPGGKIEPGESPEEAALRELREETGLTA--------EDLELLGElPSPGYTDEK 89
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157145003 100 THYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERLLASASVHDNSRA 146
Cdd:COG0494   90 VHVFLARGLGPGEEVGLDDEDE-FIEVRWVPLDEALALVTAGEIAKT 135
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
18-134 8.68e-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: 467579 [Multi-domain]  Cd Length: 118  Bit Score: 53.78  E-value: 8.68e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  18 ISIDLIVENErGEFLLGKRtNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDnfsged 97
Cdd:cd04699    3 VSVKGVIFDN-GRVLLLRR-SRAGAGEWELPGGRLEPGESPEEALKREVKEETGLD--VSVGELLDTWTFELDP------ 72
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157145003  98 fTTHYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERL 134
Cdd:cd04699   73 -DKGVFIVTYLCRLVGGEVTLSDE-HEEYEWVTPEEL 107
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
23-75 2.22e-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: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 52.96  E-value: 2.22e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157145003  23 IVENErGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLP 75
Cdd:cd04681   12 IIRNE-GEILFVRRAKEPGKGKLDLPGGFVDPGESAEEALRRELREELGLKIP 63
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
16-134 3.03e-09

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: 52.57  E-value: 3.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  16 PLISIDLIVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPlsAGAFYGVWQ-HFYDDNFs 94
Cdd:cd04678    1 PRVGVGVIVLNDDGKVLLGRRKGSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIR--NVRFLTVTNdVFEEEGK- 77
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157145003  95 gedfttHYVVLGFRLKVN--QADLHLPDEQHEDYRWQTPERL 134
Cdd:cd04678   78 ------HYVTIFVLAEVDdgEPEENMEPDKCEGWEWFSWDEL 113
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
26-137 7.69e-09

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


Pssm-ID: 467593 [Multi-domain]  Cd Length: 130  Bit Score: 51.49  E-value: 7.69e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  26 NERGEFLLGKRTNRPA---QGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAgafygvWQHFYDDNFsGEDFTTHY 102
Cdd:cd18882   10 DDRGKVLLQLRDDKPGipyPGYWGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFR------FFLLYTEDD-GEDRIRHV 82
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157145003 103 VVlgFRLKVNQADLHLpdeqHE--DYRWQTPERLLAS 137
Cdd:cd18882   83 FH--APLDVDLSDLVL----NEgqALRLFSPEEILQG 113
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
23-136 8.49e-09

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: 51.30  E-value: 8.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENErGEFLLGKRT-NRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDNfsgedfttH 101
Cdd:cd03425    7 IIVDD-GRVLIAQRPeGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIE--VEVGEPLGTVEHDYPDF--------H 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157145003 102 YVVLGFRLKVNQADLHLPDeqHEDYRWQTPERLLA 136
Cdd:cd03425   76 VRLHVYLCTLWSGEPQLLE--HQELRWVTPEELDD 108
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
16-75 1.05e-08

bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; Bacterial NadM-Nudix is a bifunctional enzyme containing a nicotinamide mononucleotide (NMN) adenylyltransferase (NMNAT) and an ADP-ribose pyrophosphatase (ADPRase) domain. NMNAT was initially identified as an NAD+ synthase that catalyzes the reversible conversion of NMN to NAD+ in the final step of both the de novo biosynthesis and salvage pathways in most organisms across all three kingdoms of life ADPRase is a member of the NUDIX family proteins, catalyzes the metal-induced and concerted general acid-base hydrolysis of ADP ribose (ADPR) into AMP and ribose-5'-phosphate (R5P). Additional members in this cd include bacterial transcriptional regulator, NrtR, which represses the transcription of NAD biosynthetic genes in vitro and adenosine diphosphate ribose (ADPR), as well as NadQ, a NUDIX-like ATP-responsive regulator of NAD biosynthesis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, U=I, L or V) which functions as metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467585 [Multi-domain]  Cd Length: 132  Bit Score: 51.39  E-value: 1.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157145003  16 PLISIDLIV---ENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLP 75
Cdd:cd18873    1 PSVTVDCVIfgfDDGELKVLLIKRKNEPFKGGWALPGGFVREDETLEDAARRELREETGLKDI 63
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
23-142 1.12e-08

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: 51.14  E-value: 1.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNRPAQ--GYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAG-AFYGVWQHFYDDNFSGEDFT 99
Cdd:cd04694    8 LIEDSDDRVLLTRRAKHMRTfpGVWVPPGGHVELGESLLEAGLRELQEETGLEVSDIQSlSLLGLWESVYPTLLSIGLPK 87
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157145003 100 THYVVLGFRLKV-----NQADLHL-PDEQHEdYRWQTPERLLASASVHD 142
Cdd:cd04694   88 RHHIVVYYLVKLsesheNQEQLKLqEDEVDA-AVWLPKSLLAKLLEAED 135
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
28-138 5.41e-08

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: 49.23  E-value: 5.41e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  28 RGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDNfsgedfTTHYVVLGF 107
Cdd:cd04679   12 DGRLLLVLRLRAPEAGHWGLPGGKVDWLETVEDAVRREILEELGLE--IELTRLLCVVDQIDAAD------GEHWVAPVY 83
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 157145003 108 RLKVNQADLHL-PDEQHEDYRW----QTPERLLASA 138
Cdd:cd04679   84 LAEIFSGEPRLmEPEKHGGIGWfaldALPQPLTVAT 119
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
10-136 8.35e-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: 49.45  E-value: 8.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  10 TVVRSTPL------ISIDLIVENERGEFLLGKR--TNRPAQGYW-FVPGGRVQKDETLENAFERLTQAELGLRLPLSAGA 80
Cdd:cd04693   16 THRRGEPLpegeyhLVVHVWIFNSDGEILIQQRspDKKGFPGMWeASTGGSVLAGETSLEAAIRELKEELGIDLDADELR 95
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 157145003  81 FYGvwQHFYDDNFsgEDFtthYVvlgFRLKVNQADLHLPDEQHEDYRWQTPERLLA 136
Cdd:cd04693   96 PIL--TIRFDNGF--DDI---YL---FRKDVDIEDLTLQKEEVQDVKWVTLEEILE 141
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
23-73 1.60e-07

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


Pssm-ID: 467573 [Multi-domain]  Cd Length: 122  Bit Score: 47.68  E-value: 1.60e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157145003  23 IVENErGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLR 73
Cdd:cd04691    7 VVVKE-GKVLLVKRAYGPGKGRWTLPGGFVEEGETLDEAIVREVLEETGID 56
PRK08999 PRK08999
Nudix family hydrolase;
23-73 5.39e-07

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 48.33  E-value: 5.39e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 157145003  23 IVENERGEFLLGKRT-NRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLR 73
Cdd:PRK08999  11 VIRDADGRILLARRPeGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIE 62
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
16-132 3.49e-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: 44.20  E-value: 3.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  16 PLISIDLIVENERGEFLLGKRTNrpAQGYWFVPGGRVQKDETLENAFERLTQAELGL-----RLPLSAGAFYGvwQHFYD 90
Cdd:cd18874    1 PEPTVGALIFNPDGKVLLVRSHK--WNDLYGIPGGKVEWGETLEEALKREVKEETGLditdiRFILVQESINS--EEFHK 76
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157145003  91 DnfsgedftTHYVVLGFRLKVNQADLhLPDEQHEDYRWQTPE 132
Cdd:cd18874   77 P--------AHFVFVDYLARTDSSEV-VLNEEAVEYLWVEPE 109
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
22-147 3.70e-06

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


Pssm-ID: 467549 [Multi-domain]  Cd Length: 132  Bit Score: 44.16  E-value: 3.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLLGKRTNRPaqGYW-FVpGGRVQKDETLENAFERLTQAELGLRLplsAGAFYGVWQH--FYDDNFSGEDF 98
Cdd:cd04664    7 IYRKDEEGEVLLLKRTDDG--GFWqSV-TGGIEDGETPWQAALRELKEETGLDP---LELQLIDLNVsnFYEIFDDWRPG 80
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 157145003  99 TTHYVVLGFRLKVN-QADLHLPDEqHEDYRWQTPERLLASASVHDNSRAY 147
Cdd:cd04664   81 VTVNTEHVFAVEVPeEQPIRLSPE-HTDYRWLPYEEAAELLFWPSNREAL 129
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
22-138 4.25e-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: 467568 [Multi-domain]  Cd Length: 138  Bit Score: 44.10  E-value: 4.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLL--GKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYG-VWQHFYDDNFSGEDF 98
Cdd:cd04685    5 VLLLDPDGRVLLfrFHDPDDPGRSWWFTPGGGVEPGESPEQAAVRELREETGLR--LEPDDLGGpVWRRRAVFDFSGETV 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 157145003  99 TTH---YVVLGFRLKVNQAdlHLPDEQHE---DYRWQTPERLLASA 138
Cdd:cd04685   83 RQDerfFLVRVPAFEVDTA--GWTDLERAvidGHRWWSLAELAATG 126
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
22-135 1.25e-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: 467588 [Multi-domain]  Cd Length: 121  Bit Score: 42.57  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLLGKRTNRPAqgyWFVPGGRVQKDETLENAFERLTQAELGLRLPLSagafyGVWQHFYDDNFSGEDFTTH 101
Cdd:cd18876    5 ALFTDAAGRVLLVKPTYKDG---WELPGGVVEAGESPLQAARREVREELGLDVPVG-----RLLAVDWVPPAGGGDDAVL 76
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 157145003 102 YVVLGFRLKVNQAD-LHLPDEQHEDYRWQTPERLL 135
Cdd:cd18876   77 FVFDGGVLTPEQAAaIRLQDEELSAYRFVTPEEAA 111
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
23-102 4.43e-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: 467560 [Multi-domain]  Cd Length: 137  Bit Score: 41.34  E-value: 4.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNrpaQGYWFVPGGRVQKDETLENAFERLTQAELGLRL-PLSagaFYGVwqhfyddnFSGEDFTTH 101
Cdd:cd04677   18 IILNEQGRILLQKRTD---TGDWGLPGGAMELGESLEETARREVFEETGLTVeELE---LLGV--------YSGKDLYYT 83

                 .
gi 157145003 102 Y 102
Cdd:cd04677   84 Y 84
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
23-134 5.52e-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: 467563 [Multi-domain]  Cd Length: 121  Bit Score: 40.70  E-value: 5.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNRPAqgyWFVPGGRVQKDETLENAFERLTQAELGLRLpLSAGAFYGVWQHFYddnFSGEDFTTHY 102
Cdd:cd04680    6 IVLDDAGRVLLVRHTYVPG---WYLPGGGVDKGETAEEAARRELREEAGVVL-TGPPRLFGVYFNRR---VSPRDHVALY 78
                         90       100       110
                 ....*....|....*....|....*....|..
gi 157145003 103 VVLGFRlkvnQADLHLPDEQHEDYRWQTPERL 134
Cdd:cd04680   79 RVREFE----QTEPPEPNGEIAEAGFFALDAL 106
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
23-72 8.38e-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: 8.38e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGL 72
Cdd:cd04671    6 VIINEQGEVLMIQEAKRSCRGKWYLPAGRVEPGESIVEAAKREVKEETGL 55
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
29-91 1.55e-04

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 41.15  E-value: 1.55e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 157145003  29 GEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGAFYGVWQHFYDD 91
Cdd:PRK05379 214 GHVLLVRRRAEPGKGLWALPGGFLEQDETLLDACLRELREETGLKLPEPVLRGSIRDQQVFDH 276
NUDIX_NudI cd04696
NUDIX hydrolase subfamily; Nucleoside triphosphatase NudI catalyzes the hydrolysis of ...
23-134 2.18e-04

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


Pssm-ID: 467577 [Multi-domain]  Cd Length: 134  Bit Score: 39.53  E-value: 2.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENErGEFLLGKR-TNRPA-QGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGAfygVWQhFYDDNF-----SG 95
Cdd:cd04696    8 LIENE-GCYLLCKMaDDRGVfPGQWALSGGGVEPGERIEEALRREIREELGEQLILSDIT---PWT-FRDDIRiktypDG 82
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 157145003  96 EDFTTHYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERL 134
Cdd:cd04696   83 RQEEIYMIYLIFDCVSANRDVCINDE-FQDYAWVKPADL 120
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
22-146 2.39e-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: 39.16  E-value: 2.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLLgkrTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGL---RLPLSAGAFYGVWQHFYDDNFsGEDF 98
Cdd:cd03674    7 FVVNPDRGKVLL---VHHRKLGRWLQPGGHVEPDEDPLEAALREAREETGLdveLLSPLSPDPLDIDVHPIPANP-GEPA 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 157145003  99 TTHY-VVLGFRLKVNQAdLHLPDEqHEDYRWQTPERlLASASVHDNSRA 146
Cdd:cd03674   83 HLHLdVRYLAVADGDEA-LRKSDE-SSDVRWFPLDE-LEELSMDPNLRK 128
PRK15472 PRK15472
nucleoside triphosphatase NudI; Provisional
23-134 3.12e-04

nucleoside triphosphatase NudI; Provisional


Pssm-ID: 185369 [Multi-domain]  Cd Length: 141  Bit Score: 38.96  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENErGEFLLGKR-TNR---PAQgyWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAGAfygVWQhFYDD--NFSGE 96
Cdd:PRK15472  10 LIQND-GAYLLCKMaDDRgvfPGQ--WALSGGGVEPGERIEEALRREIREELGEQLLLTEIT---PWT-FRDDirTKTYA 82
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 157145003  97 DFTT---HYVVLGFRLKVNQADLHLPDEqHEDYRWQTPERL 134
Cdd:PRK15472  83 DGRKeeiYMIYLIFDCVSANRDVKINEE-FQDYAWVKPEDL 122
NUDIX_MutT_Nudt1 cd18883
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
44-134 4.61e-04

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


Pssm-ID: 467594  Cd Length: 136  Bit Score: 38.60  E-value: 4.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  44 YWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQHFYDDNfsgedfTTHYVVLGFRLKVNQADLHLPD--- 120
Cdd:cd18883   23 KTFLPGGHIEIGESAEIALVRELREELGLS--CKVGRYLGAVENQWQDK------EVIHVELNHLFEVELQDLHTSDtpe 94
                         90
                 ....*....|....*.
gi 157145003 121 --EQHEDYRWQTPERL 134
Cdd:cd18883   95 sqEPHLEFYWIPYNDL 110
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
23-72 8.73e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 37.66  E-value: 8.73e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157145003  23 IVENERGEFLLgkrTNRPAQ----GYWFVPGGRVQKDETLENAFERLTQAELGL 72
Cdd:PRK10776  10 IIRNPNNEIFI---TRRAADahmaGKWEFPGGKIEAGETPEQALIRELQEEVGI 60
NUDIX_Hydrolase cd04682
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
43-140 8.96e-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: 467565 [Multi-domain]  Cd Length: 123  Bit Score: 37.65  E-value: 8.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  43 GYWFVPGGRVQKDETLENAFERLTQAELGLRLPLSAgafyGVWQHFYDDNFSGEdfTTHYVVLGfRLKVNQ-ADLHLPDE 121
Cdd:cd04682   28 NLWDLPGGGREGDETPFACVLRELREELGLALPEDR----LVWERVYPSNHNPG--RQSWFFVA-RLPADEvDAIRFGDE 100
                         90
                 ....*....|....*....
gi 157145003 122 QHEdYRWQTPERLLASASV 140
Cdd:cd04682  101 GQE-WALMPVDDFLAHPDA 118
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
25-132 1.42e-03

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


Pssm-ID: 467534 [Multi-domain]  Cd Length: 132  Bit Score: 37.15  E-value: 1.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  25 ENERGEFLLGKRtnrPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRlplsagafygvwQHFYDDNFSgedFTTHYVV 104
Cdd:cd03428   13 DNGEIEFLLLQH---SYGGHWDFPKGHVEPGESELETALRETKEETGLT------------VDDLPPGFR---ETLTYSF 74
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 157145003 105 LGFRLKV---------NQADLHLPDEqHEDYRWQTPE 132
Cdd:cd03428   75 KEGVEKTvvyflaeltPDVEVKLSEE-HQDYKWLPYE 110
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
23-146 2.77e-03

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: 36.36  E-value: 2.77e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVENERGEFLLGKRTNRPAQGYWFvPGGRVQKDETLENAFERLTQAELGLRLplsagAFYGV--WQHFYDDNFSGEDFtt 100
Cdd:cd04670    8 LVINENNEVLVVQEKYGGPGGWKL-PGGLVDPGEDIGEAAVREVFEETGIDT-----EFVSIlgFRHQHPGRFGKSDL-- 79
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 157145003 101 hYVVlgFRLK-VNQADLHLPDEQHEDYRWQTPERLLASASVHDNSRA 146
Cdd:cd04670   80 -YFV--CRLRpLSDEEIKICPEEIAEAKWMPLEEYLKQPNVSQINKL 123
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
42-134 3.37e-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: 467570 [Multi-domain]  Cd Length: 130  Bit Score: 35.99  E-value: 3.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  42 QGYWFVPGGRVQKDETLENAFERLTQAELGlrLPLSAGAFYGVWQHFYDDNfsGEDFttHYVVLGFRLK-VNQADLHLPD 120
Cdd:cd04688   23 DDYYRLPGGRVEFGETSEDALVREFKEELG--VEVEVVRLLFVVENFFTYD--GKPF--HEIGFYYLVElSDEALYEQDI 96
                         90       100
                 ....*....|....*....|
gi 157145003 121 EQHED------YRWQTPERL 134
Cdd:cd04688   97 FFLEEdgekleFRWIPLEEL 116
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
23-132 3.44e-03

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 36.26  E-value: 3.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  23 IVEnERGEFLLGKRTNRPAQ-GYWFVPGGRVQKDETLENAFERLTQAELGLRlpLSAGAFYGVWQH-----------FYD 90
Cdd:PRK10546  10 IIE-RDGKILLAQRPAHSDQaGLWEFAGGKVEPGESQPQALIRELREELGIE--ATVGEYVASHQRevsgrrihlhaWHV 86
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 157145003  91 DNFSGEdFTTHYvvlgfrlkvnqadlhlpdeqHEDYRWQTPE 132
Cdd:PRK10546  87 PDFHGE-LQAHE--------------------HQALVWCTPE 107
NUDIX_DR0079 cd24154
NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus ...
20-99 3.75e-03

NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus radiodurans protein DR_0079 is one of 21 NUDIX hydrolases that it encodes, and it has been observed to have a marked preference for cytosine ribonucleoside 5'-diphosphate (CDP) and cytosine ribonucleoside 5'-triphosphate (CTP), and for their corresponding deoxyribose nucleotides, dCDP and dCTP, to a lesser degree. 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: 467602 [Multi-domain]  Cd Length: 121  Bit Score: 35.65  E-value: 3.75e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  20 IDLIVENERGEFLLGKRTNRPAQ---GYWFVPGGRVQKDETLENAFERLTQAELGLRL------------PLSAG--AFY 82
Cdd:cd24154    5 VNAFLINSQGQLWIPRRTADKRIfplALDMSVGGHVSSGETYEQAFVRELQEELNLDLdqlsyrvlgkltPYEHGvsAFM 84
                         90
                 ....*....|....*....
gi 157145003  83 GVWQHFYDD--NFSGEDFT 99
Cdd:cd24154   85 KVYEIRSDEtpDYNPDDFS 103
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
22-96 4.55e-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: 4.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  22 LIVENERGEFLLGKRTNR----PaqGYW-FVPGGRVQKDETLENAFERLTQAELGLR-LPL-------SAGAFYGVWQHF 88
Cdd:cd04697   31 IVVRNAAGRLLVQKRTMDkdycP--GYLdPATGGVVGAGESYEENARRELEEELGIDgVPLrplftfyYEDDRSRVWGAL 108

                 ....*...
gi 157145003  89 YDDNFSGE 96
Cdd:cd04697  109 FECVYDGP 116
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
23-73 6.68e-03

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


Pssm-ID: 467535 [Multi-domain]  Cd Length: 126  Bit Score: 35.16  E-value: 6.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157145003  23 IVENERGEFLLGKRTNRPaQGYWFVPGGRVQKDETLENAFERLTQAELGLR 73
Cdd:cd03429    7 LVTNGEDKILLARQPRWP-PGRYSLLAGFVEPGETLEEAVRREVKEEVGLR 56
NUDIX_4 pfam14815
NUDIX domain;
22-134 6.90e-03

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 34.98  E-value: 6.90e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003   22 LIVENERGEFLLGKRtnrPA----QGYWFVPGGRVQKDETLENAFERLtqAELGLRLPLSAGafyGVWQHFYddnfsged 97
Cdd:pfam14815   3 LVIRNGDGRVLLRKR---PEkgllGGLWEFPGGKVEPGETLEEALARL--EELGIEVEVLEP---GTVKHVF-------- 66
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 157145003   98 ftTHYVVLGFRLKVNQADlhLPDEQHEDYRWQTPERL 134
Cdd:pfam14815  67 --THFRLTLHVYLVREVE--GEEEPQQELRWVTPEEL 99
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
16-85 9.47e-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: 34.47  E-value: 9.47e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157145003  16 PLISIDLIVENErGEFLLGKRTNRPAQGYWFVPGGRVQKDETLENAFERLTQAELGLRLPLsaGAFYGVW 85
Cdd:cd04511    1 PKIVVGCLPEWE-GKVLLCRRAIEPRKGYWTLPAGFMELGETTEQGAARETREEAGARVEI--GSLYAVY 67
 
Blast search parameters
Data Source: Live blast search RID = SX26TA37013
User Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01   Maximum number of hits: 500

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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