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Conserved domains on  [gi|1043698614|gb|ANS19551|]
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NADH pyrophosphatase [Enterobacter hormaechei]

Protein Classification

NAD(+) diphosphatase( domain architecture ID 11478360)

NAD(+) diphosphatase catalyzes the cleavage of NADH into reduced nicotinamide mononucleotide (NMNH) and AMP

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
nudC PRK00241
NAD(+) diphosphatase;
1-252 9.36e-175

NAD(+) diphosphatase;


:

Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 481.27  E-value: 9.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614   1 MDRIIEKSDLGWWIVSHEQKLWLPGGEIPYGAADIFDLVGQPALRIGEWQGDPVWLIQQA--RRQDMGSVRQVLDRDVGL 78
Cdd:PRK00241    3 MRRDLEALDAGWWVVSHEQQLWLPDGELPFGAAANLDLPGLRALQIGEWQGEPVWLVRQDplRGHEMGSLRQLLDLDDGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  79 FQLAGRGVQLAEFYRSHKYCGYCGHTMHPSKTEWAMLCGHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGIHTVLA 158
Cdd:PRK00241   83 FQLLGRAVQLAEFYRSHRFCGYCGHPMHPSKTEWAMLCPHCRERYYPRIAPCIIVAVRRGDEILLARHPRHRNGVYTVLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLPLLPPPG 238
Cdd:PRK00241  163 GFVEVGETLEQCVAREVMEESGIKVKNLRYVGSQPWPFPHSLMLGFHADYDSGEIVFDPKEIADAQWFRYDELPLLPPSG 242
                         250
                  ....*....|....
gi 1043698614 239 TVARRLIEDTVAMC 252
Cdd:PRK00241  243 TIARRLIEDTVALC 256
 
Name Accession Description Interval E-value
nudC PRK00241
NAD(+) diphosphatase;
1-252 9.36e-175

NAD(+) diphosphatase;


Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 481.27  E-value: 9.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614   1 MDRIIEKSDLGWWIVSHEQKLWLPGGEIPYGAADIFDLVGQPALRIGEWQGDPVWLIQQA--RRQDMGSVRQVLDRDVGL 78
Cdd:PRK00241    3 MRRDLEALDAGWWVVSHEQQLWLPDGELPFGAAANLDLPGLRALQIGEWQGEPVWLVRQDplRGHEMGSLRQLLDLDDGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  79 FQLAGRGVQLAEFYRSHKYCGYCGHTMHPSKTEWAMLCGHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGIHTVLA 158
Cdd:PRK00241   83 FQLLGRAVQLAEFYRSHRFCGYCGHPMHPSKTEWAMLCPHCRERYYPRIAPCIIVAVRRGDEILLARHPRHRNGVYTVLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLPLLPPPG 238
Cdd:PRK00241  163 GFVEVGETLEQCVAREVMEESGIKVKNLRYVGSQPWPFPHSLMLGFHADYDSGEIVFDPKEIADAQWFRYDELPLLPPSG 242
                         250
                  ....*....|....
gi 1043698614 239 TVARRLIEDTVAMC 252
Cdd:PRK00241  243 TIARRLIEDTVALC 256
NPY1 COG2816
NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];
11-252 6.68e-111

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


Pssm-ID: 442065 [Multi-domain]  Cd Length: 288  Bit Score: 320.71  E-value: 6.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  11 GWWIVSHEQKLWL-PGGEIPYGAADIFDLVGQPALRI--GEWQGDPVWLI------QQARRQDMGSVRQVLDR-DVGLFQ 80
Cdd:COG2816    31 PRVLVVDGGRLLLlEDGGELLLPAGEAADLGPPAEAVflGLDDGRPVFAVdlpaelELPEGAEFVDLRELGGLlDPRDAG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  81 LAGRGVQLAEFYRSHKYCGYCGHTMHPSKTEWAMLCGHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGIHTVLAGF 160
Cdd:COG2816   111 LAARAVALLNWHRTHRFCGRCGAPTVVAAAGWARRCPACGAEHYPRTDPAVIVLVTDGDRILLARQARWPPGRYSLLAGF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 161 VEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLP------LL 234
Cdd:COG2816   191 VEPGETLEQAVRREVFEEVGVRVKNVRYVGSQPWPFPSSLMLGFTAEADSGEITVDGDEIEDARWFSRDELPaalaglLL 270
                         250
                  ....*....|....*...
gi 1043698614 235 PPPGTVARRLIEDTVAMC 252
Cdd:COG2816   271 PPPGSIARRLIEAWLAGP 288
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
128-247 2.07e-62

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: 191.93  E-value: 2.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 128 APCIIVAIRRD-DSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMA 206
Cdd:cd03429     1 DPAVIVLVTNGeDKILLARQPRWPPGRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKNVRYVGSQPWPFPSSLMLGFTA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1043698614 207 EYDSGEIVIDQKELLEANWYRYDDLP---LLPPPGTVARRLIED 247
Cdd:cd03429    81 EADSGEITVDDDELEDARWFSRDELPealFLPPPGSIARRLIRA 124
NUDIX pfam00293
NUDIX domain;
131-235 3.01e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 70.20  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVAIRRDDSILLAQHT-RHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPM--------SLM 201
Cdd:pfam00293   7 GVVLLNEKGRVLLVRRSkKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFdgrfpdehEIL 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1043698614 202 TAFMAEYDSGEIVIDQKELLEANWYRYDDLPLLP 235
Cdd:pfam00293  87 YVFLAEVEGELEPDPDGEVEEVRWVPLEELLLLK 120
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
136-210 1.15e-04

nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins of about 200 amino acids, including the recently characterized nudix hydrolase YffH, shows to be highly active as a GDP-mannose pyrophosphatase. It also includes the C-terminal half of a 361-amino acid protein, TrgB from Rhodobacter sphaeroides, shown experimentally to help confer tellurite resistance. This model also hits a region near the C-terminus of a 1092-amino acid protein of C. elegans. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129162 [Multi-domain]  Cd Length: 185  Bit Score: 41.73  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 136 RRDDSILLAQ------HTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTsQPWPFP---MSLMTAFMA 206
Cdd:TIGR00052  55 KKDTVVLIEQfriaayVNGEEPWLLELSAGMVEKGESPEDVARREAIEEAGYQVKNLRKLL-SFYMSPggvTELIHLFIA 133

                  ....
gi 1043698614 207 EYDS 210
Cdd:TIGR00052 134 EVDD 137
 
Name Accession Description Interval E-value
nudC PRK00241
NAD(+) diphosphatase;
1-252 9.36e-175

NAD(+) diphosphatase;


Pssm-ID: 234699 [Multi-domain]  Cd Length: 256  Bit Score: 481.27  E-value: 9.36e-175
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614   1 MDRIIEKSDLGWWIVSHEQKLWLPGGEIPYGAADIFDLVGQPALRIGEWQGDPVWLIQQA--RRQDMGSVRQVLDRDVGL 78
Cdd:PRK00241    3 MRRDLEALDAGWWVVSHEQQLWLPDGELPFGAAANLDLPGLRALQIGEWQGEPVWLVRQDplRGHEMGSLRQLLDLDDGL 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  79 FQLAGRGVQLAEFYRSHKYCGYCGHTMHPSKTEWAMLCGHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGIHTVLA 158
Cdd:PRK00241   83 FQLLGRAVQLAEFYRSHRFCGYCGHPMHPSKTEWAMLCPHCRERYYPRIAPCIIVAVRRGDEILLARHPRHRNGVYTVLA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLPLLPPPG 238
Cdd:PRK00241  163 GFVEVGETLEQCVAREVMEESGIKVKNLRYVGSQPWPFPHSLMLGFHADYDSGEIVFDPKEIADAQWFRYDELPLLPPSG 242
                         250
                  ....*....|....
gi 1043698614 239 TVARRLIEDTVAMC 252
Cdd:PRK00241  243 TIARRLIEDTVALC 256
NPY1 COG2816
NADH pyrophosphatase NudC, Nudix superfamily [Nucleotide transport and metabolism];
11-252 6.68e-111

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


Pssm-ID: 442065 [Multi-domain]  Cd Length: 288  Bit Score: 320.71  E-value: 6.68e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  11 GWWIVSHEQKLWL-PGGEIPYGAADIFDLVGQPALRI--GEWQGDPVWLI------QQARRQDMGSVRQVLDR-DVGLFQ 80
Cdd:COG2816    31 PRVLVVDGGRLLLlEDGGELLLPAGEAADLGPPAEAVflGLDDGRPVFAVdlpaelELPEGAEFVDLRELGGLlDPRDAG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614  81 LAGRGVQLAEFYRSHKYCGYCGHTMHPSKTEWAMLCGHCRERYYPQIAPCIIVAIRRDDSILLAQHTRHRNGIHTVLAGF 160
Cdd:COG2816   111 LAARAVALLNWHRTHRFCGRCGAPTVVAAAGWARRCPACGAEHYPRTDPAVIVLVTDGDRILLARQARWPPGRYSLLAGF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 161 VEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLP------LL 234
Cdd:COG2816   191 VEPGETLEQAVRREVFEEVGVRVKNVRYVGSQPWPFPSSLMLGFTAEADSGEITVDGDEIEDARWFSRDELPaalaglLL 270
                         250
                  ....*....|....*...
gi 1043698614 235 PPPGTVARRLIEDTVAMC 252
Cdd:COG2816   271 PPPGSIARRLIEAWLAGP 288
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
128-247 2.07e-62

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: 191.93  E-value: 2.07e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 128 APCIIVAIRRD-DSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTAFMA 206
Cdd:cd03429     1 DPAVIVLVTNGeDKILLARQPRWPPGRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKNVRYVGSQPWPFPSSLMLGFTA 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1043698614 207 EYDSGEIVIDQKELLEANWYRYDDLP---LLPPPGTVARRLIED 247
Cdd:cd03429    81 EADSGEITVDDDELEDARWFSRDELPealFLPPPGSIARRLIRA 124
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
130-244 9.63e-20

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 81.95  E-value: 9.63e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 130 CIIVaiRRDDSILLAQHTR-HRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMS-LMTAFMAE 207
Cdd:COG1051    11 AVIF--RKDGRVLLVRRADePGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPDRGHvVSVAFLAE 88
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1043698614 208 YDSGEIVIDQkELLEANWYRYDDLPLLPPPGTVARRL 244
Cdd:COG1051    89 VLSGEPRADD-EIDEARWFPLDELPELAFTPADHEIL 124
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
137-231 4.13e-16

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: 72.33  E-value: 4.13e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 137 RDDSILLAQHTRHRN-GIHTVLAGFVEVGETLEQAVAREVMEESGI--KVKNLRYVTSQPWPFPMS-LMTAFMAEYDSGE 212
Cdd:cd04691    10 KEGKVLLVKRAYGPGkGRWTLPGGFVEEGETLDEAIVREVLEETGIdaKPVGIIGVRSGVIRDGKSdNYVVFLLEYVGGE 89
                          90
                  ....*....|....*....
gi 1043698614 213 IVIDQKELLEANWYRYDDL 231
Cdd:cd04691    90 PKPDERENSEAGFLTLEEA 108
NUDIX pfam00293
NUDIX domain;
131-235 3.01e-15

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 70.20  E-value: 3.01e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVAIRRDDSILLAQHT-RHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPM--------SLM 201
Cdd:pfam00293   7 GVVLLNEKGRVLLVRRSkKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFdgrfpdehEIL 86
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1043698614 202 TAFMAEYDSGEIVIDQKELLEANWYRYDDLPLLP 235
Cdd:pfam00293  87 YVFLAEVEGELEPDPDGEVEEVRWVPLEELLLLK 120
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
123-235 1.01e-14

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


Pssm-ID: 467564 [Multi-domain]  Cd Length: 135  Bit Score: 69.14  E-value: 1.01e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 123 YYPQIAPCIIVAIRRDDSILLAqhTRHRN---GIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMS 199
Cdd:cd04681     1 YFHNVAAAVGVIIRNEGEILFV--RRAKEpgkGKLDLPGGFVDPGESAEEALRRELREELGLKIPKLRYLCSLPNTYLYK 78
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1043698614 200 LMTA------FMAEYDS-GEIVIDQKELLEANWYRYDDLPLLP 235
Cdd:cd04681    79 GITYktcdlfFTAELDEkPKLKKAEDEVAELEWLDLEEIEPEK 121
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
130-225 2.46e-14

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


Pssm-ID: 467528 [Multi-domain]  Cd Length: 106  Bit Score: 67.04  E-value: 2.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 130 CIIVAIRRDDSILLAQHTRHRNGIH-TVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMS----LMTAF 204
Cdd:cd02883     3 VGAVVFDDEGRVLLVRRSDGPGPGGwELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEgrhvVVLVF 82
                          90       100
                  ....*....|....*....|..
gi 1043698614 205 MAEYDSGEIVIDQK-ELLEANW 225
Cdd:cd02883    83 LARVVGGEPPPLDDeEISEVRW 104
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
131-246 1.22e-12

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: 63.51  E-value: 1.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVAIRRDDSILLAQHTRHRNGIHTVL--AGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWP-FPMSLMTAFMAE 207
Cdd:COG0494    17 VVVLLDDDGRVLLVRRYRYGVGPGLWEfpGGKIEPGESPEEAALRELREETGLTAEDLELLGELPSPgYTDEKVHVFLAR 96
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1043698614 208 Y---DSGEIVIDQKELLEANWYRYDDLPLLPPPGTVARRLIE 246
Cdd:COG0494    97 GlgpGEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAKTLAA 138
NUDIX_Hydrolase cd18879
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
130-247 1.52e-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: 467590 [Multi-domain]  Cd Length: 142  Bit Score: 63.37  E-value: 1.52e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 130 CIIVAIRRDDSILLAQhtRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYV---TSQPWPFP-------MS 199
Cdd:cd18879    21 VTAVVLRDAGRVLLVR--RADNGRWTPVTGIVEPGEQPADAAVREVLEETGVDVEVERLAsvgASPPVTYPngdqcqyLD 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1043698614 200 LmtAFMAEYDSGEIVIDQKELLEANWYRYDDlplLPPPGTVARRLIED 247
Cdd:cd18879    99 L--TFRCRPVGGEARVNDDESLEVGWFPVDA---LPPMLPRFRRRIAL 141
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
125-246 1.26e-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: 467560 [Multi-domain]  Cd Length: 137  Bit Score: 60.60  E-value: 1.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 125 PQIAPCIIVAIRRDDSILLAQHtRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLR----------YVTsqpw 194
Cdd:cd04677     9 PLILVGAAVIILNEQGRILLQK-RTDTGDWGLPGGAMELGESLEETARREVFEETGLTVEELEllgvysgkdlYYT---- 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1043698614 195 pFP-----MSLMTAFMAEYDSGEIVIDQKELLEANWYRYDDLP-LLPPPgtvARRLIE 246
Cdd:cd04677    84 -YPngdevYNVTAVYLVRDVSGELKVDDEESLELRFFSLDELPeNINPQ---HRDVIE 137
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
131-235 2.02e-11

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: 59.77  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVA---IRRDDSILLAQhtRHRNGihtVLAGF-------VEVGETLEQAVAREVMEESGIKVKNLRYVT--SQPWPFPM 198
Cdd:cd03425     1 IEVVaaiIVDDGRVLIAQ--RPEGK---HLAGLwefpggkVEPGETPEQALVRELREELGIEVEVGEPLGtvEHDYPDFH 75
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1043698614 199 SLMTAFMAEYDSGEIVidQKELLEANWYRYDDLPLLP 235
Cdd:cd03425    76 VRLHVYLCTLWSGEPQ--LLEHQELRWVTPEELDDLD 110
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
129-246 2.61e-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: 467586 [Multi-domain]  Cd Length: 125  Bit Score: 59.61  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 129 PCIIVAIRRDDSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMS-------LM 201
Cdd:cd18874     3 PTVGALIFNPDGKVLLVRSHKWNDLYGIPGGKVEWGETLEEALKREVKEETGLDITDIRFILVQESINSEEfhkpahfVF 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1043698614 202 TAFMAEYDSGEiVIDQKELLEANWYR---YDDLPLlpppGTVARRLIE 246
Cdd:cd18874    83 VDYLARTDSSE-VVLNEEAVEYLWVEpeeALKYPL----NSFTRLLLE 125
NUDIX_ADPRase cd18889
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
134-252 3.07e-10

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


Pssm-ID: 467599 [Multi-domain]  Cd Length: 127  Bit Score: 56.46  E-value: 3.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 134 AIRRDDSILLAQHtrhRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPW------PFPMSLMTAF-MA 206
Cdd:cd18889     8 AIFKDDKILLVQE---KDGRWSLPGGWVDVNQSIKENTIKEAKEEAGLDVEPKRIIAVLDRnkhnkpPYAYGIYKIFvLC 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1043698614 207 EYDSGEIViDQKELLEANWYRYDDLPLLPPPGTVARRliedtVAMC 252
Cdd:cd18889    85 ELLGGEFQ-PNIETIESGYFSLDELPPLSEEKNTKEQ-----IEMC 124
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
131-246 3.15e-10

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


Pssm-ID: 467557 [Multi-domain]  Cd Length: 128  Bit Score: 56.37  E-value: 3.15e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVAIRRDDSILLAQhtRHRN---GIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVT---------SQPWPFPM 198
Cdd:cd04673     4 VGAVVFRDGRVLLVR--RGNPpdaGLWSFPGGKVELGETLEDAALRELREETGLEAEVVGLLTvvdvierdeAGRVRFHY 81
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1043698614 199 sLMTAFMAEYDSGEIVIDQkELLEANWYRYDDLPLLP-PPGTvaRRLIE 246
Cdd:cd04673    82 -VILDFLAEWVSGEPVAGD-DALDARWFSLEELDGLPlTPGT--RDVLE 126
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
130-236 5.24e-10

MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 15/Nudt15, may catalyze the hydrolysis of nucleoside diphosphates, triphosphates including dGTP, dTTP, dCTP, their oxidized forms like 8-oxo-dGTP, and prodrug thiopurine derivatives 6-thio-dGTP and 6-thio-GTP. MTH2 may also play a role in DNA synthesis and cell cycle progression by stabilizing PCNA. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467561 [Multi-domain]  Cd Length: 128  Bit Score: 56.03  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 130 CIIVaiRRDDSILLAQHT-RHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVT---SQPWPFPMSLMTAFM 205
Cdd:cd04678     7 VIVL--NDDGKVLLGRRKgSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVRFLTvtnDVFEEEGKHYVTIFV 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1043698614 206 -AEYDSGEividQKELLEAN------WYRYDDLPLLPP 236
Cdd:cd04678    85 lAEVDDGE----PEENMEPDkcegweWFSWDELPPLRP 118
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
130-191 6.82e-10

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: 55.59  E-value: 6.82e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1043698614 130 CIIVAIRRDDSILLAQHTRHrnGIHTVL----AGFVEVGETLEQAVAREVMEESGIKVKNLRYVTS 191
Cdd:cd03424     5 VAVLAITDDGKVVLVRQYRH--PVGRVLlelpAGKIDPGEDPEEAARRELEEETGYTAGDLELLGS 68
NUDIX_MutT_Nudt1 cd18886
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
135-235 8.92e-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: 467596 [Multi-domain]  Cd Length: 147  Bit Score: 55.70  E-value: 8.92e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 135 IRRDDSILLAQHTRHRN-GIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRY----VTSQPWPFPMSLMTAFMAEYD 209
Cdd:cd18886     7 IIRDDEVLLLNRNKKPNmGKWNGVGGKLEPGESPEECAIREVFEETGLELEDLQLrgivTFPSFDGGEDWLMYVFLAEAF 86
                          90       100
                  ....*....|....*....|....*..
gi 1043698614 210 SGEIVIDQKE-LLEanWYRYDDLPLLP 235
Cdd:cd18886    87 SGELVESDREgILA--WVPIDWLLNLP 111
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
135-184 1.43e-09

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: 54.46  E-value: 1.43e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1043698614 135 IRRDDSILLAQHtRHRNGIHTVL-AGFVEVGETLEQAVAREVMEESGIKVK 184
Cdd:cd18880     8 IIEDGKLLLVKH-RDEGGIFYILpGGGQEHGETLPEALKRECLEETGLDVE 57
zf-NADH-PPase pfam09297
NADH pyrophosphatase zinc ribbon domain; This domain is found in between two duplicated NUDIX ...
93-124 2.94e-09

NADH pyrophosphatase zinc ribbon domain; This domain is found in between two duplicated NUDIX domains. It has a zinc ribbon structure.


Pssm-ID: 430510 [Multi-domain]  Cd Length: 32  Bit Score: 51.06  E-value: 2.94e-09
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1043698614  93 RSHKYCGYCGHTMHPSKTEWAMLCGHCRERYY 124
Cdd:pfam09297   1 RTHRFCGRCGAPTVPAEGGWARVCPSCGHEHY 32
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
133-246 4.38e-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: 467563 [Multi-domain]  Cd Length: 121  Bit Score: 53.02  E-value: 4.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLAQHTrHRNGIHtVLAGFVEVGETLEQAVAREVMEESGIKvknlryVTSQPWPFPMSLMTAFMA------ 206
Cdd:cd04680     6 IVLDDAGRVLLVRHT-YVPGWY-LPGGGVDKGETAEEAARRELREEAGVV------LTGPPRLFGVYFNRRVSPrdhval 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1043698614 207 ----EYDSGEIVIDQKELLEANWYRYDDLPLLPPPGTvARRLIE 246
Cdd:cd04680    78 yrvrEFEQTEPPEPNGEIAEAGFFALDALPEDTTPAT-RRRLAE 120
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
135-189 9.39e-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: 467570 [Multi-domain]  Cd Length: 130  Bit Score: 52.55  E-value: 9.39e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1043698614 135 IRRDDSILLAQHtrHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYV 189
Cdd:cd04688     9 IIRDGKVLLARG--EDDDYYRLPGGRVEFGETSEDALVREFKEELGVEVEVVRLL 61
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
159-231 1.15e-08

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: 52.15  E-value: 1.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVK-----NLRyvTSQPWPFPMS------LMTAfmaeYDSGEIVIDQKELLEANWYR 227
Cdd:cd04670    34 GLVDPGEDIGEAAVREVFEETGIDTEfvsilGFR--HQHPGRFGKSdlyfvcRLRP----LSDEEIKICPEEIAEAKWMP 107

                  ....
gi 1043698614 228 YDDL 231
Cdd:cd04670   108 LEEY 111
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
133-247 1.82e-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: 467552 [Multi-domain]  Cd Length: 117  Bit Score: 51.52  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLaqhTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVtsqpwpfpMSLMTA------FMA 206
Cdd:cd04667     5 VICRRGDRILL---VARRGGRWLLPGGKIEPGESPLEAAIRELKEETGLAALSLLYL--------FEHEGPhklhhvFLA 73
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1043698614 207 EYDSGEIVIDQKELLEANWYRYDDLPLLPPPGTvARRLIED 247
Cdd:cd04667    74 EAPDGGRPRPGNEIARCRWVSADQLRDLNLSRA-TRLIVRR 113
NUDIX_RppH cd04665
RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of ...
131-234 6.35e-08

RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of its 5' end. In eukaryotes, the 5'-methylguanosine (cap) structure is principally removed by the NUDIX family decapping enzyme Dcp2, yielding a 5'-monophosphorylated RNA that is a substrate for 5' exoribonucleases. In bacteria, the 5'-triphosphate group of primary transcripts is also converted to a 5' monophosphate by a NUDIX protein called RNA pyrophosphohydrolase (RppH), allowing access to both endo- and 5' exoribonucleases. NUDIX hydrolase is a superfamily of enzymes found in all three kingdoms of life, and it catalyzes the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+ for their activity. Members of this family are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site. Substrates of NUDIX hydrolase include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance and "house-cleaning" enzymes. Substrate specificity is used to define child families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required. This superfamily consists of at least nine families: IPP (isopentenyl diphosphate) isomerase, ADP ribose pyrophosphatase, mutT pyrophosphohydrolase, coenzyme-A pyrophosphatase, MTH1-7,8-dihydro-8-oxoguanine-triphosphatase, diadenosine tetraphosphate hydrolase, NADH pyrophosphatase, GDP-mannose hydrolase and the c-terminal portion of the mutY adenine glycosylase.


Pssm-ID: 467550 [Multi-domain]  Cd Length: 121  Bit Score: 49.94  E-value: 6.35e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 131 IIVAIRRDDSILLAQHtRHRNGIHTVlAGFVEVGETLEQAVAREVMEESGIKVKNLRY-----VTSQPWPFPMSLMTA-- 203
Cdd:cd04665     3 VVVIARYKGKWLFTRH-KERRGWEFP-GGKREPGETIEEAARRELYEETGAVIFELKPlgqysVHGKGQEFFGAVYYAev 80
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1043698614 204 --FMAEYDSGEI--VIDQKELLEANWYRYDDLPLL 234
Cdd:cd04665    81 ksFEPILPYFETaeVRLFDELPEFSLTYPDIQPHL 115
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
132-194 9.29e-08

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 49.74  E-value: 9.29e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1043698614 132 IVA--IRRDDSILLAQHTRHRN--GIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPW 194
Cdd:PRK10546    6 VVAaiIERDGKILLAQRPAHSDqaGLWEFAGGKVEPGESQPQALIRELREELGIEATVGEYVASHQR 72
PLN02325 PLN02325
nudix hydrolase
125-233 1.28e-07

nudix hydrolase


Pssm-ID: 215184 [Multi-domain]  Cd Length: 144  Bit Score: 49.47  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 125 PQIApcIIVAIRRDDSILLAQHtRHRNGIHT--VLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTS-----QPWPFP 197
Cdd:PLN02325    8 PRVA--VVVFLLKGNSVLLGRR-RSSIGDSTfaLPGGHLEFGESFEECAAREVKEETGLEIEKIELLTVtnnvfLEEPKP 84
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1043698614 198 MSLMTAFMAeydsgEIVIDQKEL---LEA------NWYRYDDLPL 233
Cdd:PLN02325   85 SHYVTVFMR-----AVLADPSQVpqnLEPekcygwDWYEWDNLPE 124
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
135-233 2.05e-07

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: 48.68  E-value: 2.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 135 IRRDDSILLAQHTR-----HRNGIhtvlAGFVEVGETLEQAVAREVMEESGIKVKNLRYV-------TSQPWPFPmslMT 202
Cdd:cd03427     9 LRGDDRVLLGLKKRgfgagKWNGF----GGKVEPGETIEEAAVRELEEEAGLTATELEKVgrlkfefPDDPEAMD---VH 81
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1043698614 203 AFMAEYDSGEIVidQKELLEANWYRYDDLPL 233
Cdd:cd03427    82 VFRADSWTGEPQ--ETEEMRPQWFDLDDIPY 110
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
133-232 3.43e-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: 467562 [Multi-domain]  Cd Length: 126  Bit Score: 48.07  E-value: 3.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLAQHTRHRNGIHTVL-AGFVEVGETLEQAVAREVMEESGIKVKNLRY--VTSQ-------PWPFPMSLMT 202
Cdd:cd04679     7 AAILDDGRLLLVLRLRAPEAGHWGLpGGKVDWLETVEDAVRREILEELGLEIELTRLlcVVDQidaadgeHWVAPVYLAE 86
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1043698614 203 AFmaeydSGEIVIDQKE-LLEANWYRYDDLP 232
Cdd:cd04679    87 IF-----SGEPRLMEPEkHGGIGWFALDALP 112
NUDIX_Hydrolase cd04683
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
133-254 3.78e-07

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


Pssm-ID: 467566 [Multi-domain]  Cd Length: 137  Bit Score: 47.98  E-value: 3.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLAQ--HTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVK--NLRYVTSqpwpfpMSLMTA----- 203
Cdd:cd04683     5 LLLVRGDEVLLLRraNTGYDDGWWHLPAGHVEAGETVRAAAVREAKEELGVEIDpeDLRLVHT------MHRRSDggrer 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043698614 204 ----FMAEYDSGEIVIDQKE-LLEANWYRYDDLPllpppgtvarrliEDTVAMCRA 254
Cdd:cd04683    79 idffFRATRWSGEPRNREPDkCAELRWFPLDALP-------------ENTVPYVRA 121
NUDIX_Hydrolase cd04511
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
127-183 3.95e-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: 467545 [Multi-domain]  Cd Length: 123  Bit Score: 47.57  E-value: 3.95e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 127 IAPCIIVAirrDDSILLAQhtRH---RNGIHTVLAGFVEVGETLEQAVAREVMEESGIKV 183
Cdd:cd04511     4 VVGCLPEW---EGKVLLCR--RAiepRKGYWTLPAGFMELGETTEQGAARETREEAGARV 58
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
159-243 5.88e-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: 467588 [Multi-domain]  Cd Length: 121  Bit Score: 47.20  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLR-----YVTSQPWPFPMSLMTAF---MAEYDSGEIVIDQKELLEANWYRYDD 230
Cdd:cd18876    30 GVVEAGESPLQAARREVREELGLDVPVGRllavdWVPPAGGGDDAVLFVFDggvLTPEQAAAIRLQDEELSAYRFVTPEE 109
                          90
                  ....*....|....
gi 1043698614 231 LP-LLPPPgtVARR 243
Cdd:cd18876   110 AAeLLPPR--LARR 121
NUDIX_CDP-Chase_like cd04672
CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ...
134-234 8.41e-07

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: 46.78  E-value: 8.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 134 AIRRDDSILLaqhTRHR-NGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVT------SQPWPFPMSLMTAFM- 205
Cdd:cd04672     8 AVFKDGKILL---VREKsDGRWTLPGGWADVGLSPAENAVKEVREESGYEVRARKLLAvfdrnkGGHPPSPFHVYKLFFl 84
                          90       100
                  ....*....|....*....|....*....
gi 1043698614 206 AEYDSGEiVIDQKELLEANWYRYDDLPLL 234
Cdd:cd04672    85 CELIGGE-AQTSIETSEVGFFALDDLPPL 112
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
159-244 2.42e-06

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


Pssm-ID: 467542 [Multi-domain]  Cd Length: 130  Bit Score: 45.71  E-value: 2.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPW-----PFPMSLMTA--------FMAEYDSGEIVIDQKELLEANW 225
Cdd:cd03674    32 GHVEPDEDPLEAALREAREETGLDVELLSPLSPDPLdidvhPIPANPGEPahlhldvrYLAVADGDEALRKSDESSDVRW 111
                          90
                  ....*....|....*....
gi 1043698614 226 YRYDDLPLLPPPGTVARRL 244
Cdd:cd03674   112 FPLDELEELSMDPNLRKLL 130
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
133-230 4.87e-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: 467572 [Multi-domain]  Cd Length: 123  Bit Score: 44.83  E-value: 4.87e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLAqhtRHRNGIHTVLA-GFVEVGETLEQAVAREVMEESGIKVKN--LRYVTS-------QPwPFPMsLMT 202
Cdd:cd04690     6 VIIIKDGRLLLV---RKRGTDAFYLPgGKREPGETPLQALVRELKEELGLDLDPdsLRFLGTfeapaanEP-GTTV-RMT 80
                          90       100
                  ....*....|....*....|....*...
gi 1043698614 203 AFMAEYDsGEIVIDQkELLEANWYRYDD 230
Cdd:cd04690    81 CFTADYD-GEPQPAA-EIEELRWLDPAD 106
PRK08999 PRK08999
Nudix family hydrolase;
133-194 6.87e-06

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 46.41  E-value: 6.87e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1043698614 133 VAIRRDDSILLAQHTRHRngihtVLAGF-------VEVGETLEQAVAREVMEESGIKVKNLRyvtsqPW 194
Cdd:PRK08999   11 VIRDADGRILLARRPEGK-----HQGGLwefpggkVEPGETVEQALARELQEELGIEVTAAR-----PL 69
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
159-230 9.37e-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: 44.08  E-value: 9.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYvtsqpwPFPMSLM-----------TAFMAEYDSGEIVIDQKELLEANWYR 227
Cdd:cd03428    35 GHVEPGESELETALRETKEETGLTVDDLPP------GFRETLTysfkegvektvVYFLAELTPDVEVKLSEEHQDYKWLP 108

                  ...
gi 1043698614 228 YDD 230
Cdd:cd03428   109 YEE 111
NUDIX_Hydrolase cd18875
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
130-187 1.09e-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: 467587 [Multi-domain]  Cd Length: 144  Bit Score: 44.10  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1043698614 130 CIIvaIRRDDSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLR 187
Cdd:cd18875     7 CMI--YDGEDRVLVLDRVKKDWGGYTFPGGHVEPGESFVDSVIREVKEETGLTIKNPE 62
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
133-231 1.12e-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: 43.84  E-value: 1.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 133 VAIRRDDSILLAQHTRHR-NGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKnLRYVTSQPWPFPMSLMTAFMAEYDSG 211
Cdd:cd04671     6 VIINEQGEVLMIQEAKRScRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCE-PSTLLSVEEAGGSWYRFVFTGNITGG 84
                          90       100
                  ....*....|....*....|.
gi 1043698614 212 EI-VIDQKELLEANWYRYDDL 231
Cdd:cd04671    85 KLkTPADADSESLQAFWIDDI 105
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
158-191 1.32e-05

Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site.


Pssm-ID: 467603 [Multi-domain]  Cd Length: 187  Bit Score: 44.44  E-value: 1.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1043698614 158 AGFVEVGETLEQAVAREVMEESGIKVKNLRYVTS 191
Cdd:cd24155    82 AGMIDAGETPEDVARREAEEEAGLTLDALEPIAS 115
NUDIX_GDPMK cd24157
GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX ...
156-210 3.38e-05

GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX enzyme that uses GDP-mannose as the preferred substrate. It is distinct from Nudix ADP-ribose hydrolases. GDPMK and ADP-ribose pyrophosphatase seem to use similar catalytic mechanism. However, GDPMK hydrolysis does not rely on a single glutamate as the catalytic base; rather, it is dependent on residues that coordinate the magnesium ions and residues that position the substrate properly for catalysis. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467605  Cd Length: 146  Bit Score: 42.55  E-value: 3.38e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1043698614 156 VLAGFVEvGETLEQAVAREVMEESGIKVKNLRYVtSQPWPFP---MSLMTAFMAEYDS 210
Cdd:cd24157    41 ACAGLLD-GDDPEDCIRREAEEETGYRLGDLEKV-FTAYSSPgivTERIHLFIAEYSS 96
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
135-184 4.07e-05

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: 41.84  E-value: 4.07e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1043698614 135 IRRDDSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVK 184
Cdd:cd04699     9 IFDNGRVLLLRRSRAGAGEWELPGGRLEPGESPEEALKREVKEETGLDVS 58
NUDIX_Hydrolase cd03675
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
158-231 5.12e-05

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


Pssm-ID: 467543 [Multi-domain]  Cd Length: 138  Bit Score: 42.13  E-value: 5.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 158 AGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMS----LMTAFMAEYDS--GEIVIDQkELLEANWYRYDDL 231
Cdd:cd03675    30 AGHLEPGESLLEAAIRETLEETGWEVEPTALLGIYQWTAPDNgvtyLRFAFAGELLEhlPDQPLDS-GIIRAHWLTLEEI 108
nudF PRK10729
ADP-ribose pyrophosphatase NudF; Provisional
156-191 5.51e-05

ADP-ribose pyrophosphatase NudF; Provisional


Pssm-ID: 182682 [Multi-domain]  Cd Length: 202  Bit Score: 42.80  E-value: 5.51e-05
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1043698614 156 VLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTS 191
Cdd:PRK10729   86 MVAGMIEEGESVEDVARREAIEEAGLIVGRTKPVLS 121
NUDIX_DR0079 cd24154
NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus ...
158-217 6.44e-05

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: 41.43  E-value: 6.44e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1043698614 158 AGFVEVGETLEQAVAREVMEESGIKVKNLRY-VTSQPWPFPMSLmTAFMAEYdsgEIVIDQ 217
Cdd:cd24154    37 GGHVSSGETYEQAFVRELQEELNLDLDQLSYrVLGKLTPYEHGV-SAFMKVY---EIRSDE 93
NUDIX_Hydrolase cd04663
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
130-197 6.79e-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: 467548 [Multi-domain]  Cd Length: 132  Bit Score: 41.51  E-value: 6.79e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 130 CIIVAIRRDDSILLAQHTRHRN-GIHtVLAGFVEVGETLEQAVAREVMEESGIK-VKNLRYVTSQPWPFP 197
Cdd:cd04663     4 CAYVTRGRNRELLVFEHPDFPEaGLQ-VPKGTVEPGESPEEAALRELAEETGLTgARVVVDLGSHDEGFE 72
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
161-231 8.11e-05

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: 41.39  E-value: 8.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1043698614 161 VEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTA------FMAEYDSGEIVIDQK-ELLEANWYRYDDL 231
Cdd:cd03673    36 LEPGETPEEAAVREVEEETGLRVRLGRPLGTTRYTYTRKGKGIlkkvhyWLMRALGGEFLPQPEeEIDEVRWLPPDEA 113
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
155-231 8.70e-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: 467578 [Multi-domain]  Cd Length: 157  Bit Score: 41.84  E-value: 8.70e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1043698614 155 TVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLM--TAFMAEYDsGEIVIDQKELLEANWYRYDDL 231
Cdd:cd04697    58 PATGGVVGAGESYEENARRELEEELGIDGVPLRPLFTFYYEDDRSRVwgALFECVYD-GPLKLQPEEVAEVDWMSEDEI 135
NUDIX_Hydrolase cd04674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
150-183 1.07e-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: 467558 [Multi-domain]  Cd Length: 118  Bit Score: 40.91  E-value: 1.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1043698614 150 RNGI---HTVLA---GFVEVGETLEQAVAREVMEESGIKV 183
Cdd:cd04674    21 RRGIepgHGELAlpgGYIEYGETWQEAAVRELREETGVEA 60
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
136-210 1.15e-04

nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins of about 200 amino acids, including the recently characterized nudix hydrolase YffH, shows to be highly active as a GDP-mannose pyrophosphatase. It also includes the C-terminal half of a 361-amino acid protein, TrgB from Rhodobacter sphaeroides, shown experimentally to help confer tellurite resistance. This model also hits a region near the C-terminus of a 1092-amino acid protein of C. elegans. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 129162 [Multi-domain]  Cd Length: 185  Bit Score: 41.73  E-value: 1.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 136 RRDDSILLAQ------HTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTsQPWPFP---MSLMTAFMA 206
Cdd:TIGR00052  55 KKDTVVLIEQfriaayVNGEEPWLLELSAGMVEKGESPEDVARREAIEEAGYQVKNLRKLL-SFYMSPggvTELIHLFIA 133

                  ....
gi 1043698614 207 EYDS 210
Cdd:TIGR00052 134 EVDD 137
NUDIX_Hydrolase cd18884
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
129-181 1.43e-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: 467595 [Multi-domain]  Cd Length: 125  Bit Score: 40.47  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1043698614 129 PCIIVAIRRDDSILLAQHTRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGI 181
Cdd:cd18884    10 PVVAAIVEHDGHIVLARNKAWPEGWYGLVTGFLEAGESPEEAVLREVKEELGL 62
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
159-212 1.88e-04

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 40.35  E-value: 1.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFPMSLMTA--FMAEYDSGE 212
Cdd:PRK10776   38 GKIEAGETPEQALIRELQEEVGITVQHATLFEKLEYEFPDRHITLwfWLVESWEGE 93
NUDIX_UDP-X_diphosphatase cd18891
UDP-X diphosphatase; UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and ...
135-244 2.30e-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: 40.07  E-value: 2.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 135 IRRDDSILLAQHTRHrnGIHTVLAGFVEVGETLEQAVAREVMEESGIKV--KNLR--YVTSQPWPFPMSLM---TAFMAE 207
Cdd:cd18891     9 IQNENKVLLVQDKHT--KEWALPGGFAEVGLSPKENILKEVKEETGLHVevERLLavFDTDLRQDIPQSFQyykFIFACK 86
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1043698614 208 YDSGEIViDQKELLEANWYRYDDLPLLPPPGTVARRL 244
Cdd:cd18891    87 ILDGEFQ-ENSETSDLQYFSLDQLPNLSLKRTTKEQL 122
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
159-187 2.73e-04

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: 39.83  E-value: 2.73e-04
                          10        20
                  ....*....|....*....|....*....
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLR 187
Cdd:cd18873    38 GFVREDETLEDAARRELREETGLKDIYLE 66
NUDIX_Hydrolase cd04676
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
129-184 3.45e-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: 467559 [Multi-domain]  Cd Length: 144  Bit Score: 39.69  E-value: 3.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1043698614 129 PCIIVAIRRDDSILLAQhtRHRNGIHTVL-AGFVEVGETLEQAVAREVMEESGIKVK 184
Cdd:cd04676    18 PSVAAVILNEDGRILLQ--RKGGLGLWSLpAGAIEPGEHPAEAVIREVREETGLLVK 72
NUDIX_Hydrolase cd04686
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
135-193 3.58e-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: 467569 [Multi-domain]  Cd Length: 130  Bit Score: 39.58  E-value: 3.58e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1043698614 135 IRRDDSILLAQHTRhrnGIHTVL----AGFVEVGETLEQAVAREVMEESGIKV---KNLRYVTSQP 193
Cdd:cd04686     8 IIRNDKLLLIRKTR---GPYQGRydlpGGSQEFGESLEDALKREFAEETGMTVtsyDNLGVYDFFV 70
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
132-189 6.15e-04

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: 38.77  E-value: 6.15e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 132 IVAIRRDDS--ILLAQHTrHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYV 189
Cdd:cd04664     5 VVIYRKDEEgeVLLLKRT-DDGGFWQSVTGGIEDGETPWQAALRELKEETGLDPLELQLI 63
NUDIX_CDP-Chase cd18890
CDP-choline pyrophosphatase; CDP-choline pyrophosphatase catalyzes the hydrolysis of ...
139-234 6.97e-04

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


Pssm-ID: 467600 [Multi-domain]  Cd Length: 129  Bit Score: 38.56  E-value: 6.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 139 DSILLAQHTRhrNGIHTVLAGFVEVGETLEQAVAREVMEESGIKV---KNLRYVTSQPWPFPMSLMTA----FMAEYDSG 211
Cdd:cd18890    14 EEILLVKEKE--DGKWTLPGGWADVGYTPTEVAAKEVEEETGLEVspkKLLAILDKRKHPHPPQPTYVyklfILCEIEGG 91
                          90       100
                  ....*....|....*....|...
gi 1043698614 212 EIViDQKELLEANWYRYDDLPLL 234
Cdd:cd18890    92 ELK-PSFETGEVRFFSENELPEL 113
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
132-183 8.82e-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: 467568 [Multi-domain]  Cd Length: 138  Bit Score: 38.32  E-value: 8.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1043698614 132 IVAIRRDDSILLaQHTRHR-NGIHTVLA---GFVEVGETLEQAVAREVMEESGIKV 183
Cdd:cd04685     5 VLLLDPDGRVLL-FRFHDPdDPGRSWWFtpgGGVEPGESPEQAAVRELREETGLRL 59
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
159-189 9.09e-04

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


Pssm-ID: 467539 [Multi-domain]  Cd Length: 147  Bit Score: 38.70  E-value: 9.09e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKVKNLRYV 189
Cdd:cd03671    34 GGIDEGEDPEEAALRELYEETGLSPEDVEII 64
NUDIX_ADPRase cd24160
Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ...
128-249 9.25e-04

Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ADP-ribose pyrophosphatase (ADPRase) such as found in extreme thermophile Thermus thermophilus (TtADPRase) catalyzes the hydrolysis of ADPR to AMP and ribose 5'-phosphate in the presence of Mg2+ and Zn2+ ions. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site.


Pssm-ID: 467608 [Multi-domain]  Cd Length: 151  Bit Score: 38.64  E-value: 9.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 128 APCIIVAIRRDDSILLAQHTRHRNGIHT--VLAGFVEVGETLEQAVAREVMEESGIKvKNLRYVT---SQPwPFPMSLMT 202
Cdd:cd24160    21 ADAVAVLALREGRMLFVRQMRPAVGAATleIPAGLIDPGETPEEAARRELAEETGLS-GDLTYLTrfyVSP-GFCDEKLH 98
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1043698614 203 AFMAEY-DSGEIVIDQKELLEANWYRyddlpllppPGTVARRLIEDTV 249
Cdd:cd24160    99 VFLAENlREVEAHPDEDEAIEVVWMR---------PEEVLERLRRGEV 137
NUDIX_Hydrolase cd04684
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
129-189 1.36e-03

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


Pssm-ID: 467567 [Multi-domain]  Cd Length: 140  Bit Score: 37.99  E-value: 1.36e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1043698614 129 PCIIVAIRRDDS-ILLAQHTRHRngiHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYV 189
Cdd:cd04684    16 PGAYAVIFNDEGkVLLVQTPNGG---YFLPGGGIEPGETPEEALHREVLEETGWEIEIGEFL 74
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
130-197 1.71e-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: 467593 [Multi-domain]  Cd Length: 130  Bit Score: 37.62  E-value: 1.71e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1043698614 130 CIIVAIRRDDSILLaQHtRHRN-GIH-----TVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFP 197
Cdd:cd18882     4 AIAILYDDRGKVLL-QL-RDDKpGIPypgywGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFRFFLLYTEDDG 75
nudE PRK11762
adenosine nucleotide hydrolase NudE; Provisional
121-207 1.93e-03

adenosine nucleotide hydrolase NudE; Provisional


Pssm-ID: 183303  Cd Length: 185  Bit Score: 38.25  E-value: 1.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 121 ERYYPQIAP-----CIIVAIRRDDSILLAQHtrHRNGIHTVLAGF----VEVGETLEQAVAREVMEESGI---KVKNLRY 188
Cdd:PRK11762   36 ERVYERMRPsgrgaVMIVPILDDDTLLLIRE--YAAGTERYELGFpkglIDPGETPLEAANRELKEEVGFgarQLTFLKE 113
                          90
                  ....*....|....*....
gi 1043698614 189 VTSQPWPFPmSLMTAFMAE 207
Cdd:PRK11762  114 LSLAPSYFS-SKMNIVLAE 131
NUDIX_MutT_Nudt1 cd18883
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
135-231 2.03e-03

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: 37.45  E-value: 2.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 135 IRRDDSILLAqhtRHRNGIHTVL-AGFVEVGETLEQAVAREVMEESGIKVKNLRY--VTSQPWPFP------MSLMTAFM 205
Cdd:cd18883     7 IISDEHLLLA---RVKGDDKTFLpGGHIEIGESAEIALVRELREELGLSCKVGRYlgAVENQWQDKevihveLNHLFEVE 83
                          90       100
                  ....*....|....*....|....*..
gi 1043698614 206 AEYDSGEIVIDQKEL-LEANWYRYDDL 231
Cdd:cd18883    84 LQDLHTSDTPESQEPhLEFYWIPYNDL 110
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
159-183 3.90e-03

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: 36.50  E-value: 3.90e-03
                          10        20
                  ....*....|....*....|....*
gi 1043698614 159 GFVEVGETLEQAVAREVMEESGIKV 183
Cdd:cd04694    37 GHVELGESLLEAGLRELQEETGLEV 61
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
135-191 5.55e-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: 467575 [Multi-domain]  Cd Length: 157  Bit Score: 36.35  E-value: 5.55e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1043698614 135 IRRDDSILLAQhtRHRNGIH------TVLAGFVEVGETLEQAVAREVMEESGIKV--KNLRYVTS 191
Cdd:cd04693    37 FNSDGEILIQQ--RSPDKKGfpgmweASTGGSVLAGETSLEAAIRELKEELGIDLdaDELRPILT 99
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
158-231 6.70e-03

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


Pssm-ID: 441052 [Multi-domain]  Cd Length: 162  Bit Score: 36.33  E-value: 6.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 158 AGFVEVGETLEQAVAREVMEESGIKVKN-LRYVTSQPWPFPMS-------LMTAFMAEYDsGEIVIDQKELLEANWYRYD 229
Cdd:COG1443    64 CGHPRAGETYEEAAVRELEEELGITVDDdLRPLGTFRYRAVDAnglveneFCHVFVARLD-GPLTPQPEEVAEVRWVTLE 142

                  ..
gi 1043698614 230 DL 231
Cdd:COG1443   143 EL 144
NUDIX_DR1025_like cd04700
DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX ...
132-214 7.42e-03

DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX hydrolase superfamily, show nucleoside triphosphatase and dinucleoside polyphosphate pyrophosphatase activities. Like other enzymes belonging to this superfamily, it requires a divalent cation, in this case Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. In general, substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467580 [Multi-domain]  Cd Length: 147  Bit Score: 36.04  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 132 IVAIRRDDSILLAQH-----TRHRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQPWPFP---MSLMTA 203
Cdd:cd04700    18 VVLLNERGDILLVQEkgisgHPEKAGLWHIPSGAVEDGENPQDAAVREACEETGLRVRLVKFLGAYLGRFPdgvLVLRHV 97
                          90
                  ....*....|.
gi 1043698614 204 FMAEYDSGEIV 214
Cdd:cd04700    98 WLAEPEPGQVL 108
NUDIX_ADPRase_Ndx2 cd24161
NUDIX family Ndx2; NUDIX family protein Ndx2 found in Thermus thermophilus has ADP-ribose ...
130-191 9.39e-03

NUDIX family Ndx2; NUDIX family protein Ndx2 found in Thermus thermophilus has ADP-ribose pyrophosphatase (ADPRase) as well as flavin adenine dinucleotide (FAD) activity. ADPRase (EC 3.6.1.13) catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. Like other members of the NUDIX hydrolase superfamily of enzymes, it is thought to require a divalent cation, such as Mg2+, for its activity. It also contains a 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity.Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.


Pssm-ID: 467609 [Multi-domain]  Cd Length: 137  Bit Score: 35.61  E-value: 9.39e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1043698614 130 CIIVAIRRDDSILLAQHTRHRNGIHT--VLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTS 191
Cdd:cd24161     6 VGVLPITDDGEVVLVEQYRYPLGGWSweIPAGGWPEGEDPEEAARRELREETGLRAERWTPLGR 69
NUDIX_Hydrolase cd18877
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
132-236 9.54e-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: 467589 [Multi-domain]  Cd Length: 141  Bit Score: 35.41  E-value: 9.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1043698614 132 IVAIRRDDSI-LLAQHtR----HRNGIHTVLAGFVEVGETLEQAVAREVMEESGIKVKNLRYVTSQP-----WPFpmslm 201
Cdd:cd18877    23 LFAPAEDGGPhVLLQH-RawwtHQGGTWALPGGARDSGETPEAAALRETEEETGLDADTLRVVGTHVddhggWSY----- 96
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1043698614 202 TAFMAEYDSG-EIVIDQKELLEANWYRYDD---LPLLPP 236
Cdd:cd18877    97 TTVLASAPEPlPVRPANEESVELRWVPLDEvesLPLHPG 135
 
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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