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Conserved domains on  [gi|157822975|ref|NP_001100230|]
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uridine diphosphate glucose pyrophosphatase NUDT14 [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
NUDIX_UGPPase_Nudt14 cd18887
UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as ...
 25-212 1.22e-93

UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as NUDIX (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: 467597 [Multi-domain]  Cd Length: 181  Bit Score: 271.74  E-value: 1.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  25 YRQDGVQKSWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYAGEVERHFPGSltsvdqdqpQELQQILPGSAGVMVELC 104
Cdd:cd18887    1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNG---------GKDTEKYPPELGYTYELC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 105 AGIVDQPeLSLEEVACKEAWEECGYHLVPADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVVHL 184
Cdd:cd18887   72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                        170       180
                 ....*....|....*....|....*...
gi 157822975 185 NVDDAQAFADNPDIPKTLGVIFAISWFF 212
Cdd:cd18887  151 PVEEAKEFIFDEEIPKPPGLLFALLWFL 178
 
Name Accession Description Interval E-value
NUDIX_UGPPase_Nudt14 cd18887
UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as ...
 25-212 1.22e-93

UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as NUDIX (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: 467597 [Multi-domain]  Cd Length: 181  Bit Score: 271.74  E-value: 1.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  25 YRQDGVQKSWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYAGEVERHFPGSltsvdqdqpQELQQILPGSAGVMVELC 104
Cdd:cd18887    1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNG---------GKDTEKYPPELGYTYELC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 105 AGIVDQPeLSLEEVACKEAWEECGYHLVPADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVVHL 184
Cdd:cd18887   72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                        170       180
                 ....*....|....*....|....*...
gi 157822975 185 NVDDAQAFADNPDIPKTLGVIFAISWFF 212
Cdd:cd18887  151 PVEEAKEFIFDEEIPKPPGLLFALLWFL 178
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
 23-210 4.69e-32

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: 114.92  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975   23 LHYRQDGVQKSWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYageverhfpgsltsVDQDQPQELqqilpgsagvmvE 102
Cdd:TIGR00052  27 LFKGGESIRVTREIYDRGNAAAVLLYDPKKDTVVLIEQFRIAAY--------------VNGEEPWLL------------E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  103 LCAGIVDQPElSLEEVACKEAWEECGYHLvpADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGelIEVV 182
Cdd:TIGR00052  81 LSAGMVEKGE-SPEDVARREAIEEAGYQV--KNLRKLLSFYMSPGGVTELIHLFIAEVDDNQAAGIGGGADEEE--IEVL 155

                         170       180
                  ....*....|....*....|....*...
gi 157822975  183 HLNVDDAQAFADNPDIPKTLGVIFAISW 210
Cdd:TIGR00052 156 HLVFSQALQWIKEGKIDNGKTVILLQWL 183
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 41-202 1.47e-13

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: 65.44  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  41 DSVTILMFNSSQRsLVLVKQFRPAVYAGEVErhFPGsltsvdqdqpqelqqilpgsagvmvelcaGIVDqPELSLEEVAC 120
Cdd:COG0494   14 PAVVVVLLDDDGR-VLLVRRYRYGVGPGLWE--FPG-----------------------------GKIE-PGESPEEAAL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 121 KEAWEECGYHlvPADLRRVATYMSGvGLTGSRQTMFYAEVTDAqrgGPGGGLAEEGELIEVVHLNVDDAQAFADNPDIPK 200
Cdd:COG0494   61 RELREETGLT--AEDLELLGELPSP-GYTDEKVHVFLARGLGP---GEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAK 134


                 ..
gi 157822975 201 TL 202
Cdd:COG0494  135 TL 136
PRK15009 PRK15009
GDP-mannose pyrophosphatase NudK; Provisional
 44-184 4.70e-12

GDP-mannose pyrophosphatase NudK; Provisional


Pssm-ID: 184971  Cd Length: 191  Bit Score: 62.55  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  44 TILMFNSSQRSLVLVKQFRPAvyageverhfpgslTSVDQDQpqelqqilpgsAGVMVELCAGIVD--QPELSLEevacK 121
Cdd:PRK15009  49 TILLYNAKKKTVVLIRQFRVA--------------TWVNGNE-----------SGQLIETCAGLLDndEPEVCIR----K 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822975 122 EAWEECGYHLvpADLRRV-ATYMSGVGLTgSRQTMFYAEVTDAQRGGPGGGLaeEGELIEVVHL 184
Cdd:PRK15009 100 EAIEETGYEV--GEVRKLfELYMSPGGVT-ELIHFFIAEYSDSQRANAGGGV--EDEDIEVLEL 158
 
Name Accession Description Interval E-value
NUDIX_UGPPase_Nudt14 cd18887
UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as ...
 25-212 1.22e-93

UDP-glucose pyrophosphatase; UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as NUDIX (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: 467597 [Multi-domain]  Cd Length: 181  Bit Score: 271.74  E-value: 1.22e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  25 YRQDGVQKSWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYAGEVERHFPGSltsvdqdqpQELQQILPGSAGVMVELC 104
Cdd:cd18887    1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNG---------GKDTEKYPPELGYTYELC 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 105 AGIVDQPeLSLEEVACKEAWEECGYHLVPADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVVHL 184
Cdd:cd18887   72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                        170       180
                 ....*....|....*....|....*...
gi 157822975 185 NVDDAQAFADNPDIPKTLGVIFAISWFF 212
Cdd:cd18887  151 PVEEAKEFIFDEEIPKPPGLLFALLWFL 178
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
 23-210 4.69e-32

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: 114.92  E-value: 4.69e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975   23 LHYRQDGVQKSWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYageverhfpgsltsVDQDQPQELqqilpgsagvmvE 102
Cdd:TIGR00052  27 LFKGGESIRVTREIYDRGNAAAVLLYDPKKDTVVLIEQFRIAAY--------------VNGEEPWLL------------E 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  103 LCAGIVDQPElSLEEVACKEAWEECGYHLvpADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGelIEVV 182
Cdd:TIGR00052  81 LSAGMVEKGE-SPEDVARREAIEEAGYQV--KNLRKLLSFYMSPGGVTELIHLFIAEVDDNQAAGIGGGADEEE--IEVL 155

                         170       180
                  ....*....|....*....|....*...
gi 157822975  183 HLNVDDAQAFADNPDIPKTLGVIFAISW 210
Cdd:TIGR00052 156 HLVFSQALQWIKEGKIDNGKTVILLQWL 183
NUDIX_GDPMK cd24157
GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX ...
 41-189 4.07e-28

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: 103.41  E-value: 4.07e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  41 DSVTILMFNSSQRSLVLVKQFRPAVYAGeverhfpgsltsvdqdqpqelqqilpGSAGVMVELCAGIVDqpELSLEEVAC 120
Cdd:cd24157    5 DAAAVLLYDPKRKTVVLVRQFRAPAYLG--------------------------GGDGWLIEACAGLLD--GDDPEDCIR 56

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 121 KEAWEECGYHLvpADLRRVAT-YMSGvGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVVHLNVDDA 189
Cdd:cd24157   57 REAEEETGYRL--GDLEKVFTaYSSP-GIVTERIHLFIAEYSSADRVGAGGGLAEEGEDIEVLELPLDEA 123
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
 33-212 2.66e-19

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: 81.80  E-value: 2.66e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  33 SWDFMKTHDSVTILMFNSSQRSLVLVKQFRPAVYAGeverhfpgsltsvdqdqpqelqqilpGSAGVMVELCAGIVDQPE 112
Cdd:cd24155   36 TREIFERGDAVAVLPYDPVRDEVVLIEQFRIGALAR--------------------------DESPWLLEIVAGMIDAGE 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 113 lSLEEVACKEAWEECGyhLVPADLRRVATYMSGVGLTGSRQTMFYAEVtDAQRGGPGGGLAEEGELIEVVHLNVDDAQAF 192
Cdd:cd24155   90 -TPEDVARREAEEEAG--LTLDALEPIASYYPSPGGSTERVHLYLGLV-DLSDLGGIHGLAEEGEDIRVHVVPFDEAMAL 165

                        170       180
                 ....*....|....*....|
gi 157822975 193 ADNPDIpKTLGVIFAISWFF 212
Cdd:cd24155  166 LDDGEI-DNAPLIIALQWLA 184
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
 39-206 4.39e-16

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: 71.77  E-value: 4.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  39 THDSVTILMFNSSQRsLVLVKQFRPAVyageverhfpgsltsvdqdqpqelqqilpgsAGVMVELCAGIVDQPElSLEEV 118
Cdd:cd03424    1 HPGAVAVLAITDDGK-VVLVRQYRHPV-------------------------------GRVLLELPAGKIDPGE-DPEEA 47

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 119 ACKEAWEECGYHlvPADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGgglaEEGELIEVVHLNVDDAQAFADNPDI 198
Cdd:cd03424   48 ARRELEEETGYT--AGDLELLGSFYPSPGFSDERIHLFLAEDLTPVSEQAL----DEDEFIEVVLVPLEEALEMIEDGEI 121

                        170
                 ....*....|
gi 157822975 199 --PKTLGVIF 206
Cdd:cd03424  122 tdAKTLAALL 131
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 41-202 1.47e-13

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: 65.44  E-value: 1.47e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  41 DSVTILMFNSSQRsLVLVKQFRPAVYAGEVErhFPGsltsvdqdqpqelqqilpgsagvmvelcaGIVDqPELSLEEVAC 120
Cdd:COG0494   14 PAVVVVLLDDDGR-VLLVRRYRYGVGPGLWE--FPG-----------------------------GKIE-PGESPEEAAL 60

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 121 KEAWEECGYHlvPADLRRVATYMSGvGLTGSRQTMFYAEVTDAqrgGPGGGLAEEGELIEVVHLNVDDAQAFADNPDIPK 200
Cdd:COG0494   61 RELREETGLT--AEDLELLGELPSP-GYTDEKVHVFLARGLGP---GEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAK 134


                 ..
gi 157822975 201 TL 202
Cdd:COG0494  135 TL 136
PRK15009 PRK15009
GDP-mannose pyrophosphatase NudK; Provisional
 44-184 4.70e-12

GDP-mannose pyrophosphatase NudK; Provisional


Pssm-ID: 184971  Cd Length: 191  Bit Score: 62.55  E-value: 4.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  44 TILMFNSSQRSLVLVKQFRPAvyageverhfpgslTSVDQDQpqelqqilpgsAGVMVELCAGIVD--QPELSLEevacK 121
Cdd:PRK15009  49 TILLYNAKKKTVVLIRQFRVA--------------TWVNGNE-----------SGQLIETCAGLLDndEPEVCIR----K 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157822975 122 EAWEECGYHLvpADLRRV-ATYMSGVGLTgSRQTMFYAEVTDAQRGGPGGGLaeEGELIEVVHL 184
Cdd:PRK15009 100 EAIEETGYEV--GEVRKLfELYMSPGGVT-ELIHFFIAEYSDSQRANAGGGV--EDEDIEVLEL 158
NUDIX_ADPRase_Nudt5 cd18888
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX ...
 41-192 1.65e-08

ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX (Nucleoside diphosphate-linked moiety X)) motif 5; Nudt5) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity.


Pssm-ID: 467598 [Multi-domain]  Cd Length: 149  Bit Score: 51.71  E-value: 1.65e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975  41 DSVTILMF---NSSQRSLVLVKQFRPAVyageverhfpgsltsvdqdqpqelqqilpgsAGVMVELCAGIVDQPElSLEE 117
Cdd:cd18888    3 DAVAIIAIlkrKLKPPELVLVKQYRPPV-------------------------------NAYTIEFPAGLVDPGE-SPEQ 50

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 118 VACKEAWEECGYHLVpadlrrVATYMSGV-----GLTGSRQTMFYAEV--TDAQRGGPGGGLaEEGELIEVVHLNVDDAQ 190
Cdd:cd18888   51 AALRELKEETGYTGE------KVLSVSPPlaldpGLSNANMKLVTVEVdgDDPENQNPKQEL-EDGEFIEVILVPLNELL 123


                 ..
gi 157822975 191 AF 192
Cdd:cd18888  124 ER 125
nudF PRK10729
ADP-ribose pyrophosphatase NudF; Provisional
 100-210 8.69e-06

ADP-ribose pyrophosphatase NudF; Provisional


Pssm-ID: 182682 [Multi-domain]  Cd Length: 202  Bit Score: 44.73  E-value: 8.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157822975 100 MVELCAGIVDQPElSLEEVACKEAWEECGyhLVPADLRRVATYMSGVGLTGSRQTMFYAEVtDAQRGGPGGGLAEEGELI 179
Cdd:PRK10729  83 LLEMVAGMIEEGE-SVEDVARREAIEEAG--LIVGRTKPVLSYLASPGGTSERSSIMVGEV-DATTASGIHGLADENEDI 158

                         90       100       110
                 ....*....|....*....|....*....|.
gi 157822975 180 EVVHLNVDDAQAFADNPDIPKTLGVIfAISW 210
Cdd:PRK10729 159 RVHVVSREQAYQWVEEGKIDNAASVI-ALQW 188
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 102-179 1.45e-03

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: 37.00  E-value: 1.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157822975 102 ELCAGIVDQPElSLEEVACKEAWEECGYHLVPADLRRVATYMSGVGLTGSRQTMFYAEVTDAQRGGPGGGLAEEGELI 179
Cdd:cd02883   29 ELPGGGVEPGE-TPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHVVVLVFLARVVGGEPPPLDDEEISEVRWV 105
 
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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