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Conserved domains on  [gi|23956126|ref|NP_079675|]
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uridine diphosphate glucose pyrophosphatase NUDT14 isoform 1 [Mus musculus]

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 2.08e-92

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: 268.66  E-value: 2.08e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  25 YRQDGVQKSWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYAGEVERHFPGSLTAVNQdqpqelqqaLPGSAGVMVELC 104
Cdd:cd18887   1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNGGKDTEK---------YPPELGYTYELC 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 105 AGIVDQPgLSLEEAACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVIHL 184
Cdd:cd18887  72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                       170       180
                ....*....|....*....|....*...
gi 23956126 185 NLDDAQAFADNPDIPKTLGVIYAISWFF 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 2.08e-92

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: 268.66  E-value: 2.08e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  25 YRQDGVQKSWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYAGEVERHFPGSLTAVNQdqpqelqqaLPGSAGVMVELC 104
Cdd:cd18887   1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNGGKDTEK---------YPPELGYTYELC 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 105 AGIVDQPgLSLEEAACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVIHL 184
Cdd:cd18887  72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                       170       180
                ....*....|....*....|....*...
gi 23956126 185 NLDDAQAFADNPDIPKTLGVIYAISWFF 212
Cdd:cd18887 151 PVEEAKEFIFDEEIPKPPGLLFALLWFL 178
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
 17-210 3.75e-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: 115.30  E-value: 3.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    17 YLRPFT---------LHYRQDGVQKSWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYageverhfpgsltaVNQDQPQ 87
Cdd:TIGR00052  12 YSGFFSllhnifyhrLFKGGESIRVTREIYDRGNAAAVLLYDPKKDTVVLIEQFRIAAY--------------VNGEEPW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    88 ELqqalpgsagvmvELCAGIVDQpGLSLEEAACKEAWEECGYRLvpTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGG 167
Cdd:TIGR00052  78 LL------------ELSAGMVEK-GESPEDVARREAIEEAGYQV--KNLRKLLSFYMSPGGVTELIHLFIAEVDDNQAAG 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 23956126   168 PGGGlAEEGElIEVIHLNLDDAQAFADNPDIPKTLGVIYAISW 210
Cdd:TIGR00052 143 IGGG-ADEEE-IEVLHLVFSQALQWIKEGKIDNGKTVILLQWL 183
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 41-202 7.46e-16

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: 71.60  E-value: 7.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  41 DSVTILMFNSSRRsLVLVKQFRPAVYAGEVErhFPGsltavnqdqpqelqqalpgsagvmvelcaGIVDqPGLSLEEAAC 120
Cdd:COG0494  14 PAVVVVLLDDDGR-VLLVRRYRYGVGPGLWE--FPG-----------------------------GKIE-PGESPEEAAL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 121 KEAWEECGYRlvPTDLRRVATYMSGvGLTSSRQTMFYAEVTDAqrgGPGGGLAEEGELIEVIHLNLDDAQAFADNPDIPK 200
Cdd:COG0494  61 RELREETGLT--AEDLELLGELPSP-GYTDEKVHVFLARGLGP---GEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAK 134


                ..
gi 23956126 201 TL 202
Cdd:COG0494 135 TL 136
PRK15009 PRK15009
GDP-mannose pyrophosphatase NudK; Provisional
 44-189 1.98e-13

GDP-mannose pyrophosphatase NudK; Provisional


Pssm-ID: 184971  Cd Length: 191  Bit Score: 66.02  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126   44 TILMFNSSRRSLVLVKQFRPAvyageverhfpgslTAVNQDQpqelqqalpgsAGVMVELCAGIVDQPglslEEAAC--K 121
Cdd:PRK15009  49 TILLYNAKKKTVVLIRQFRVA--------------TWVNGNE-----------SGQLIETCAGLLDND----EPEVCirK 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956126  122 EAWEECGYRLvpTDLRRV-ATYMSGVGLTSSRQtMFYAEVTDAQRGGPGGGLaeEGELIEVIHLNLDDA 189
Cdd:PRK15009 100 EAIEETGYEV--GEVRKLfELYMSPGGVTELIH-FFIAEYSDSQRANAGGGV--EDEDIEVLELPFSQA 163
NUDIX pfam00293
NUDIX domain;
38-202 7.68e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 38.23  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    38 KTHDSVTILMFNSSRRsLVLVKQFRpavyageveRHFPGsltavnqdqpqelqqalpgsagvMVELCAGIVDqPGLSLEE 117
Cdd:pfam00293   1 KRRVAVGVVLLNEKGR-VLLVRRSK---------KPFPG-----------------------WWSLPGGKVE-PGETPEE 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126   118 AACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTM----FYAEVTDAQRGGPGgglaeeGELIEVIHLNLDDAQAFA 193
Cdd:pfam00293  47 AARRELEEETGLEPELLELLGSLHYLAPFDGRFPDEHEilyvFLAEVEGELEPDPD------GEVEEVRWVPLEELLLLK 120


                  ....*....
gi 23956126   194 DNPDIPKTL 202
Cdd:pfam00293 121 LAPGDRKLL 129
 
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 2.08e-92

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: 268.66  E-value: 2.08e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  25 YRQDGVQKSWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYAGEVERHFPGSLTAVNQdqpqelqqaLPGSAGVMVELC 104
Cdd:cd18887   1 YKQNGKKKTWDFVKSHDSVAILLYNKTRDAFVLVKQFRPAVYASQVRAAERNGGKDTEK---------YPPELGYTYELC 71

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 105 AGIVDQPgLSLEEAACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVIHL 184
Cdd:cd18887  72 AGLVDKD-KSLEEIAQEEILEECGYDVPLEDLEKITSFRSGVGTSGSRQTLFYAEVTDDMKVSEGGGVEEEGEMIEVVEL 150

                       170       180
                ....*....|....*....|....*...
gi 23956126 185 NLDDAQAFADNPDIPKTLGVIYAISWFF 212
Cdd:cd18887 151 PVEEAKEFIFDEEIPKPPGLLFALLWFL 178
NUDIX_GDPMK cd24157
GDP-mannose hydrolase (GDPMK), and similar proteins; GDP-mannose hydrolase (GDPMK) is a NUDIX ...
 41-189 3.02e-32

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: 114.19  E-value: 3.02e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  41 DSVTILMFNSSRRSLVLVKQFRPAVYAGeverhfpgsltavnqdqpqelqqalpGSAGVMVELCAGIVDqpGLSLEEAAC 120
Cdd:cd24157   5 DAAAVLLYDPKRKTVVLVRQFRAPAYLG--------------------------GGDGWLIEACAGLLD--GDDPEDCIR 56

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 121 KEAWEECGYRLvpTDLRRVAT-YMSGvGLTSSRQTMFYAEVTDAQRGGPGGGLAEEGELIEVIHLNLDDA 189
Cdd:cd24157  57 REAEEETGYRL--GDLEKVFTaYSSP-GIVTERIHLFIAEYSSADRVGAGGGLAEEGEDIEVLELPLDEA 123
TIGR00052 TIGR00052
nudix-type nucleoside diphosphatase, YffH/AdpP family; Members of this family include proteins ...
 17-210 3.75e-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: 115.30  E-value: 3.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    17 YLRPFT---------LHYRQDGVQKSWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYageverhfpgsltaVNQDQPQ 87
Cdd:TIGR00052  12 YSGFFSllhnifyhrLFKGGESIRVTREIYDRGNAAAVLLYDPKKDTVVLIEQFRIAAY--------------VNGEEPW 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    88 ELqqalpgsagvmvELCAGIVDQpGLSLEEAACKEAWEECGYRLvpTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGG 167
Cdd:TIGR00052  78 LL------------ELSAGMVEK-GESPEDVARREAIEEAGYQV--KNLRKLLSFYMSPGGVTELIHLFIAEVDDNQAAG 142

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 23956126   168 PGGGlAEEGElIEVIHLNLDDAQAFADNPDIPKTLGVIYAISW 210
Cdd:TIGR00052 143 IGGG-ADEEE-IEVLHLVFSQALQWIKEGKIDNGKTVILLQWL 183
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
 33-198 9.52e-23

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: 90.66  E-value: 9.52e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  33 SWDFMKTHDSVTILMFNSSRRSLVLVKQFRPAVYAGeverhfpgsltavnqdqpqelqqalpGSAGVMVELCAGIVDqPG 112
Cdd:cd24155  36 TREIFERGDAVAVLPYDPVRDEVVLIEQFRIGALAR--------------------------DESPWLLEIVAGMID-AG 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 113 LSLEEAACKEAWEECGyrLVPTDLRRVATYMSGVGLTSSRQTMFYAEVtDAQRGGPGGGLAEEGELIEVIHLNLDDAQAF 192
Cdd:cd24155  89 ETPEDVARREAEEEAG--LTLDALEPIASYYPSPGGSTERVHLYLGLV-DLSDLGGIHGLAEEGEDIRVHVVPFDEAMAL 165


                ....*.
gi 23956126 193 ADNPDI 198
Cdd:cd24155 166 LDDGEI 171
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
 39-211 6.44e-19

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: 79.47  E-value: 6.44e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  39 THDSVTILMFNSSRRsLVLVKQFRPAVyageverhfpgsltavnqdqpqelqqalpgsAGVMVELCAGIVDqPGLSLEEA 118
Cdd:cd03424   1 HPGAVAVLAITDDGK-VVLVRQYRHPV-------------------------------GRVLLELPAGKID-PGEDPEEA 47

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 119 ACKEAWEECGYRlvPTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPGgglaEEGELIEVIHLNLDDAQAFADNPDI 198
Cdd:cd03424  48 ARRELEEETGYT--AGDLELLGSFYPSPGFSDERIHLFLAEDLTPVSEQAL----DEDEFIEVVLVPLEEALEMIEDGEI 121

                       170
                ....*....|....*
gi 23956126 199 --PKTlgvIYAISWF 211
Cdd:cd03424 122 tdAKT---LAALLLA 133
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
 41-202 7.46e-16

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: 71.60  E-value: 7.46e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  41 DSVTILMFNSSRRsLVLVKQFRPAVYAGEVErhFPGsltavnqdqpqelqqalpgsagvmvelcaGIVDqPGLSLEEAAC 120
Cdd:COG0494  14 PAVVVVLLDDDGR-VLLVRRYRYGVGPGLWE--FPG-----------------------------GKIE-PGESPEEAAL 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 121 KEAWEECGYRlvPTDLRRVATYMSGvGLTSSRQTMFYAEVTDAqrgGPGGGLAEEGELIEVIHLNLDDAQAFADNPDIPK 200
Cdd:COG0494  61 RELREETGLT--AEDLELLGELPSP-GYTDEKVHVFLARGLGP---GEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAK 134


                ..
gi 23956126 201 TL 202
Cdd:COG0494 135 TL 136
PRK15009 PRK15009
GDP-mannose pyrophosphatase NudK; Provisional
 44-189 1.98e-13

GDP-mannose pyrophosphatase NudK; Provisional


Pssm-ID: 184971  Cd Length: 191  Bit Score: 66.02  E-value: 1.98e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126   44 TILMFNSSRRSLVLVKQFRPAvyageverhfpgslTAVNQDQpqelqqalpgsAGVMVELCAGIVDQPglslEEAAC--K 121
Cdd:PRK15009  49 TILLYNAKKKTVVLIRQFRVA--------------TWVNGNE-----------SGQLIETCAGLLDND----EPEVCirK 99

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956126  122 EAWEECGYRLvpTDLRRV-ATYMSGVGLTSSRQtMFYAEVTDAQRGGPGGGLaeEGELIEVIHLNLDDA 189
Cdd:PRK15009 100 EAIEETGYEV--GEVRKLfELYMSPGGVTELIH-FFIAEYSDSQRANAGGGV--EDEDIEVLELPFSQA 163
NUDIX_ADPRase_Nudt5 cd18888
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) (also known as NUDIX ...
 41-192 3.79e-11

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: 59.03  E-value: 3.79e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  41 DSVTILMF---NSSRRSLVLVKQFRPAVyageverhfpgsltavnqdqpqelqqalpgsAGVMVELCAGIVDqPGLSLEE 117
Cdd:cd18888   3 DAVAIIAIlkrKLKPPELVLVKQYRPPV-------------------------------NAYTIEFPAGLVD-PGESPEQ 50

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956126 118 AACKEAWEECGYrlVPTDLRRV--ATYMSgVGLTSSRQTMFYAEV--TDAQRGGPGGGLaEEGELIEVIHLNLDDAQAF 192
Cdd:cd18888  51 AALRELKEETGY--TGEKVLSVspPLALD-PGLSNANMKLVTVEVdgDDPENQNPKQEL-EDGEFIEVILVPLNELLER 125
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
 102-179 3.84e-06

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: 44.32  E-value: 3.84e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956126 102 ELCAGIVDqPGLSLEEAACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPGGGLAEEGELI 179
Cdd:cd02883  29 ELPGGGVE-PGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHVVVLVFLARVVGGEPPPLDDEEISEVRWV 105
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
102-202 1.97e-05

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 42.66  E-value: 1.97e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 102 ELCAGIVDqPGLSLEEAACKEAWEECGYRLVPTDLRRVATYMSGVGLTSsrqTMFYAEVTDaqrggpgGGLAEEGELIEV 181
Cdd:COG1051  35 ALPGGKVE-PGETPEEAALRELREETGLEVEVLELLGVFDHPDRGHVVS---VAFLAEVLS-------GEPRADDEIDEA 103

                        90       100
                ....*....|....*....|.
gi 23956126 182 IHLNLDDAQAFADNPDIPKTL 202
Cdd:COG1051 104 RWFPLDELPELAFTPADHEIL 124
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 110-169 4.28e-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: 39.09  E-value: 4.28e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 23956126 110 QPGLSLEEAACKEAWEECGYRLVPTDL-----RRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPG 169
Cdd:cd04685  38 EPGESPEQAAVRELREETGLRLEPDDLggpvwRRRAVFDFSGETVRQDERFFLVRVPAFEVDTAG 102
NUDIX_RppH cd04665
RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of ...
 102-162 5.34e-04

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: 38.38  E-value: 5.34e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956126 102 ELCAGIVdQPGLSLEEAACKEAWEECGYrlVPTDLRRVATY-MSGVGLTSSRqTMFYAEVTD 162
Cdd:cd04665  25 EFPGGKR-EPGETIEEAARRELYEETGA--VIFELKPLGQYsVHGKGQEFFG-AVYYAEVKS 82
NUDIX pfam00293
NUDIX domain;
38-202 7.68e-04

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 38.23  E-value: 7.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126    38 KTHDSVTILMFNSSRRsLVLVKQFRpavyageveRHFPGsltavnqdqpqelqqalpgsagvMVELCAGIVDqPGLSLEE 117
Cdd:pfam00293   1 KRRVAVGVVLLNEKGR-VLLVRRSK---------KPFPG-----------------------WWSLPGGKVE-PGETPEE 46

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126   118 AACKEAWEECGYRLVPTDLRRVATYMSGVGLTSSRQTM----FYAEVTDAQRGGPGgglaeeGELIEVIHLNLDDAQAFA 193
Cdd:pfam00293  47 AARRELEEETGLEPELLELLGSLHYLAPFDGRFPDEHEilyvFLAEVEGELEPDPD------GEVEEVRWVPLEELLLLK 120


                  ....*....
gi 23956126   194 DNPDIPKTL 202
Cdd:pfam00293 121 LAPGDRKLL 129
nudE PRK11762
adenosine nucleotide hydrolase NudE; Provisional
 106-197 1.30e-03

adenosine nucleotide hydrolase NudE; Provisional


Pssm-ID: 183303  Cd Length: 185  Bit Score: 38.25  E-value: 1.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  106 GIVDqPGLSLEEAACKEAWEECGY---RLvpTDLRRV---ATYMsgvgltSSRQTMFYAEVTDAQRgGPGgglaEEGELI 179
Cdd:PRK11762  81 GLID-PGETPLEAANRELKEEVGFgarQL--TFLKELslaPSYF------SSKMNIVLAEDLYPER-LEG----DEPEPL 146

                         90
                 ....*....|....*...
gi 23956126  180 EVIHLNLDDAQAFADNPD 197
Cdd:PRK11762 147 EVVRWPLADLDELLARPD 164
NUDIX_ADPRase cd24160
Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ...
 34-208 2.49e-03

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: 37.10  E-value: 2.49e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126  34 WDFMKTHDSVTILMFNSSRrsLVLVKQFRPAVYAgeverhfpgsltavnqdqpqelqqalpgsagVMVELCAGIVDqPGL 113
Cdd:cd24160  15 YEIVEHADAVAVLALREGR--MLFVRQMRPAVGA-------------------------------ATLEIPAGLID-PGE 60

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956126 114 SLEEAACKEAWEECGYRlvpTDLRRVATYMSGVGLTSSRQTMFYAEVTDAQRGGPggglaEEGELIEVI----HLNLDDA 189
Cdd:cd24160  61 TPEEAARRELAEETGLS---GDLTYLTRFYVSPGFCDEKLHVFLAENLREVEAHP-----DEDEAIEVVwmrpEEVLERL 132

                       170
                ....*....|....*....
gi 23956126 190 QAFADNPDIPKTLGVIYAI 208
Cdd:cd24160 133 RRGEVEFSATTLVGVLYYH 151
NUDIX_Hydrolase cd03675
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
 105-162 7.69e-03

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


Pssm-ID: 467543 [Multi-domain]  Cd Length: 138  Bit Score: 35.58  E-value: 7.69e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956126 105 AGIVDqPGLSLEEAACKEAWEECGYRLVPTDLrrVATYM---SGVGLTSSRQTmFYAEVTD 162
Cdd:cd03675  30 AGHLE-PGESLLEAAIRETLEETGWEVEPTAL--LGIYQwtaPDNGVTYLRFA-FAGELLE 86
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 92-169 8.31e-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: 467552 [Multi-domain]  Cd Length: 117  Bit Score: 34.95  E-value: 8.31e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956126  92 ALPGsagvmvelcaGIVdQPGLSLEEAACKEAWEECGyrLVPTDLRRVATYMSGvgltSSRQTMFYAEVTDAQRGGPG 169
Cdd:cd04667  24 LLPG----------GKI-EPGESPLEAAIRELKEETG--LAALSLLYLFEHEGP----HKLHHVFLAEAPDGGRPRPG 84
 
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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