NCBI Conserved Domain Search

isopentenyl-diphosphate Delta-isomerase;

Pssm-ID: 235156 [Multi-domain] Cd Length: 184 Bit Score: 326.54 E-value: 5.23e-116

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A         1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAV 80
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAHTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        81 IRRCRYELGVEITPPESIYPDFRFRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSP 160
Cdd:PRK03759  83 IRRCREELGVEITDLELVLPDFRYRATDPNGIVENEVCPVFAARVTSALQPNPDEVMDYQWVDPADLLRAVDATPWAFSP 162

                        170       180
                 ....*....|....*....|
2G74_A       161 WMVMQATNREARKRLSAFTQ 180
Cdd:PRK03759 163 WMVLQAANLEARELLLAFAQ 182

Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the NUDIX hydrolase superfamily, is a key enzyme in the isoprenoid biosynthetic pathway. Isoprenoids comprise a large family of natural products including sterols, carotenoids, dolichols and prenylated proteins. These compounds are synthesized from two precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IPP isomerase catalyzes the interconversion of IPP and DMAPP by a stereoselective antarafacial transposition of hydrogen. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains 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. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N-terminus), the core structure is highly conserved.

Pssm-ID: 467529 [Multi-domain] Cd Length: 162 Bit Score: 243.56 E-value: 1.56e-83

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        5 HVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRC 84
Cdd:cd02885   1 EVILVDEDDNPIGTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       85 RYELGVEITPPESIyPDFRFRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd02885  81 REELGIPVCDLEEL-PRFRYRATDDNGLVEHEIDHVFVGRADGDPVPNPEEVSDYRWVSLEELRELLAATPEAFTPWFRL 159


                ..
2G74_A      165 QA 166
Cdd:cd02885 160 IL 161

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: 225.85 E-value: 1.50e-76

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        3 TEHVILLNAQGVPTGTLEKYAAHtADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIR 82
Cdd:COG1443   1 EELVDLVDEDGRPIGTAERAEVH-RKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       83 RCRYELGVEITPPESIYPDFRFRATDPSGIVENEVCPVFAARTTSALQINDDEVMDYQWCDLADVLHGIDATPWAFSPWM 162
Cdd:COG1443  80 ELEEELGITVDDDLRPLGTFRYRAVDANGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAGPEAFTPWF 159


                ...
2G74_A      163 VMQ 165
Cdd:COG1443 160 RLY 162

isopentenyl-diphosphate delta-isomerase, type 1; This model represents type 1 of two non-homologous families of the enzyme isopentenyl-diphosphate delta-isomerase (IPP isomerase). IPP is an essential building block for many compounds, including enzyme cofactors, sterols, and prenyl groups. This inzyme interconverts isopentenyl diphosphate and dimethylallyl diphosphate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]

Pssm-ID: 273998 [Multi-domain] Cd Length: 158 Bit Score: 194.87 E-value: 2.49e-64

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A          6 VILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGEsnEDAVIRRCR 85
Cdd:TIGR02150   1 VILVDENDNPIGTASKAEVHLQETPLHRAFSVFLFNEEGELLLQRRASSKITWPGVWTNSCCSHPLPGE--LEAAIRRLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A         86 YELGVEITP-PESIYPDFRFRATD-PSGivENEVCPVFAARTTSALQINdDEVMDYQWCDLaDVLHGIDATPWA-FSPWM 162
Cdd:TIGR02150  79 HELGIPADDvPLTVLPRFSYRARDdAWG--EHELCPVFFARANVDLNPN-PEVAEYRWVSL-EELKEILAKPWAgFSPWF 154


                  ....
2G74_A        163 VMQA 166
Cdd:TIGR02150 155 RIQA 158

isopentenyl-diphosphate delta-isomerase

Pssm-ID: 215303 [Multi-domain] Cd Length: 247 Bit Score: 87.87 E-value: 1.63e-21

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A         1 MQTEHVILLNAQGVPTGTLEKYAAH-----TADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLG-E 74
Cdd:PLN02552  20 MFEDECILVDENDNVVGHDSKYNCHlfekiEPRGLLHRAFSVFLFNSKYELLLQQRAATKVTFPLVWTNTCCSHPLYGqD 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        75 SNE----------------DAVIRRCRYELGV--EITPPESIYPDFRFRATDPSGIV--------ENEVCPVFAARTTSA 128
Cdd:PLN02552 100 PNEvdreselidgnvlgvkNAAQRKLLHELGIpaEDVPVDQFTFLTRLHYKAADDVThgpdgkwgEHELDYLLFIRPVRD 179

                        170       180       190
                 ....*....|....*....|....*....|....*.
2G74_A       129 LQI--NDDEVMDYQWCDLADVLHGIDATP-WAFSPW 161
Cdd:PLN02552 180 VKVnpNPDEVADVKYVNREELKEMMRKESgLKLSPW 215

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

Pssm-ID: 467574 [Multi-domain] Cd Length: 142 Bit Score: 82.99 E-value: 1.05e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        9 LNAQGVPTGTLEKYAAHtADTRLHLAFSSWLFNAK-GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04692   4 VDEDGRPIGVATRSEVH-RQGLWHRTVHVWLVNPEeGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELEEE 82

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
2G74_A       88 LGVEItPPESIYPDFRFRATDPSG-IVENEVCPVFAARTT---SALQINDDEV 136
Cdd:cd04692  83 LGLTV-SPEDLIFLGVIREEVIGGdFIDNEFVHVYLYETDrplEEFKLQPEEV 134

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: 82.96 E-value: 1.73e-20

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        8 LLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYE 87
Cdd:cd04693   5 LYDENRNKTGRTHRRGEPLPEGEYHLVVHVWIFNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLEAAIRELKEE 84

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
2G74_A       88 LGVEITpPESIYPDFRFRatDPSGIVEnevcpVFAARTT---SALQINDDEVMDYQWCDLADVLHGIDA 153
Cdd:cd04693  85 LGIDLD-ADELRPILTIR--FDNGFDD-----IYLFRKDvdiEDLTLQKEEVQDVKWVTLEEILEMIES 145

NUDIX domain;

Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 79.45 E-value: 2.36e-19

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A         30 RLHLAFSSWLFNAKGQLLVTRRalSKKAWPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRFRATDP 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRR--SKKPFPGWWS-LPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDG 77

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
2G74_A        110 SGIVENEVCPVFAARTTSALQINDD-EVMDYQWCDLADVL-HGIDATPWAFSPWM 162
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDPDgEVEEVRWVPLEELLlLKLAPGDRKLLPWL 132

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: 55.68 E-value: 1.86e-10

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
2G74_A       39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITP 94
Cdd:cd24154   9 LINSQGQLWIPRRTADKRIFPLALDMSVGGHVSSGETYEQAFVRELQEELNLDLDQ 64

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: 54.46 E-value: 5.51e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       38 WLFNAKGQLLVTRRAlSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITpPESIYPDFRFRAT---DPSGI 112
Cdd:cd04690   6 VIIIKDGRLLLVRKR-GTDAFylPG-------GKREPGETPLQALVRELKEELGLDLD-PDSLRFLGTFEAPaanEPGTT 76

                        90       100       110
                ....*....|....*....|....*....|....
2G74_A      113 VENEvcpVFAARTTSALQInDDEVMDYQWCDLAD 146
Cdd:cd04690  77 VRMT---CFTADYDGEPQP-AAEIEELRWLDPAD 106

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: 53.56 E-value: 7.43e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRalSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfrFRATDPSGIVENEVC 118
Cdd:cd02883   7 VFDDEGRVLLVRR--SDGPGPGGW-ELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLG----VYEFPDPDEGRHVVV 79

                        90       100
                ....*....|....*....|....*..
2G74_A      119 PVFAARTTS--ALQINDDEVMDYQWCD 143
Cdd:cd02883  80 LVFLARVVGgePPPLDDEEISEVRWVP 106

Nudix hydrolase homolog

Pssm-ID: 215425 [Multi-domain] Cd Length: 770 Bit Score: 55.98 E-value: 1.70e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A         1 MQTEHVILLNAQGVPTGTLEKYAAHTADTRLHLAFSSWLF-NAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDA 79
Cdd:PLN02791   1 MMEEHLDVLTAAGEKTGVSKPRGEVHRDGDYHRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLS 80

                         90
                 ....*....|.
2G74_A        80 VIRRCRYELGV 90
Cdd:PLN02791  81 AQRELEEELGI 91

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: 53.39 E-value: 2.36e-09

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIypdFRFRAtdpsgivENEVC 118
Cdd:cd04697  33 VRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEEELGIDGVPLRPL---FTFYY-------EDDRS 102

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
2G74_A      119 PV----FAARTTSALQINDDEVMDYQWCDLADVLhgIDATPWAFSP 160
Cdd:cd04697 103 RVwgalFECVYDGPLKLQPEEVAEVDWMSEDEIL--QAARGEEFTP 146

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: 50.03 E-value: 3.38e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       38 WLFNAKGQLLVTRRAlSKKAWPGVWtNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESIypdfrFRATDPSGIVENEV 117
Cdd:COG0494  19 VLLDDDGRVLLVRRY-RYGVGPGLW-EFPGGKIEPGESPEEAALRELREETGLTAEDLELL-----GELPSPGYTDEKVH 91

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
2G74_A      118 cpVFAARTTSALQI----NDDEVMDYQWCDLADVLHGIDA 153
Cdd:COG0494  92 --VFLARGLGPGEEvgldDEDEFIEVRWVPLDEALALVTA 129

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

Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 48.82 E-value: 7.75e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRAlsKKAWPGVWTNsVCGHPQLGESNEDAVIRRCRYELGVEITPPESIYpdfRFRATDPSGIVEnevc 118
Cdd:COG1051  13 IFRKDGRVLLVRRA--DEPGKGLWAL-PGGKVEPGETPEEAALRELREETGLEVEVLELLG---VFDHPDRGHVVS---- 82

                        90       100
                ....*....|....*....|....*....
2G74_A      119 PVFAARTTSALQINDDEVMDYQWCDLADV 147
Cdd:COG1051  83 VAFLAEVLSGEPRADDEIDEARWFPLDEL 111

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: 46.41 E-value: 6.79e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRRAL--SKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEItppesiyPDFRFRATDP-----SGIVE 114
Cdd:cd04681  17 GEILFVRRAKepGKGKLdlPG-------GFVDPGESAEEALRRELREELGLKI-------PKLRYLCSLPntylyKGITY 82

                        90       100       110
                ....*....|....*....|....*....|....*
2G74_A      115 NEVCPVFAAR--TTSALQINDDEVMDYQWCDLADV 147
Cdd:cd04681  83 KTCDLFFTAEldEKPKLKKAEDEVAELEWLDLEEI 117

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: 45.70 E-value: 1.04e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       41 NAKGQLLVTRRALSkkawPGVWTnSVCGHPQLGESNEDAVIRRCRYELGVEITP-------PESIYPDFRFRATDPSGIV 113
Cdd:cd04664  11 DEEGEVLLLKRTDD----GGFWQ-SVTGGIEDGETPWQAALRELKEETGLDPLElqlidlnVSNFYEIFDDWRPGVTVNT 85

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
2G74_A      114 EnevcPVFAARTTSALQIN-DDEVMDYQWCDLADVLhgidatpwAFSPWmvmqATNREA 171
Cdd:cd04664  86 E----HVFAVEVPEEQPIRlSPEHTDYRWLPYEEAA--------ELLFW----PSNREA 128

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: 45.75 E-value: 1.19e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRRALSKKAWPGVWtnsVC--GHPQLGESNEDAVIRRCRYELGVEITPPESIYPDFRFRATDPSGIVENE----- 116
Cdd:cd04694  14 DRVLLTRRAKHMRTFPGVW---VPpgGHVELGESLLEAGLRELQEETGLEVSDIQSLSLLGLWESVYPTLLSIGLpkrhh 90

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
2G74_A      117 VCPVFAAR------TTSALQINDDEVMDYQWCDLADVLHGIDAT 154
Cdd:cd04694  91 IVVYYLVKlsesheNQEQLKLQEDEVDAAVWLPKSLLAKLLEAE 134

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: 42.88 E-value: 1.31e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLvtrraLSKKAWPGVWtnsvcGHP----QLGESNEDAVIRRCRYELGVEITPPE--SIY--PDFRFRAtdPS 110
Cdd:cd04677  19 ILNEQGRIL-----LQKRTDTGDW-----GLPggamELGESLEETARREVFEETGLTVEELEllGVYsgKDLYYTY--PN 86

                        90       100       110
                ....*....|....*....|....*....|....*..
2G74_A      111 GIVENEVCPVFAARTTS-ALQINDDEVMDYQWCDLAD 146
Cdd:cd04677  87 GDEVYNVTAVYLVRDVSgELKVDDEESLELRFFSLDE 123

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: 42.78 E-value: 1.52e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLvtrraLSKKAWPGVWTNSVcGHPQLGESNEDAVIRRCRYELGVEITPPESI----YPDFRFraTDPSGIVE 114
Cdd:cd04676  24 ILNEDGRIL-----LQRKGGLGLWSLPA-GAIEPGEHPAEAVIREVREETGLLVKPTRLLgvfgGKEFRY--TYPNGDQV 95

                        90       100       110
                ....*....|....*....|....*....|...
2G74_A      115 NEVCPVFAARTTS-ALQINDDEVMDYQWCDLAD 146
Cdd:cd04676  96 EYTVIAFKCVVTGgTLNAIDGETSELRYFSRTQ 128

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: 40.90 E-value: 4.74e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRRAlSKKAWPGVWtnsvcghpQL-------GESNEDAVIRRCRYELGVEITPPESI------YPDFR-----FR 105
Cdd:cd03425  12 GRVLIAQRP-EGKHLAGLW--------EFpggkvepGETPEQALVRELREELGIEVEVGEPLgtvehdYPDFHvrlhvYL 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
2G74_A      106 ATDPSGIVENEVCpvfaarttSALQ-INDDEVMDYQWCDlADV 147
Cdd:cd03425  83 CTLWSGEPQLLEH--------QELRwVTPEELDDLDWLP-ADI 116

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: 40.86 E-value: 5.69e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       56 KAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESI--YPDFRFratdpsgiveNEVCPVFAARTTSALQINd 133
Cdd:cd18884  28 KAWPEGWYGLVTGFLEAGESPEEAVLREVKEELGLDGHEAKFIghYAFPER----------NQLIIAYHVRARGNVKLN- 96

                        90       100
                ....*....|....*....|....*
2G74_A      134 DEVMDYQWCDLADVlhgidaTPWAF 158
Cdd:cd18884  97 EELDDYKIVPIDKL------RPWPF 115

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: 40.70 E-value: 8.24e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       32 HLAFSSWLFNAKGQ--LLVTRRALSKKAWPGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITP--PESIYPdfrfRAT 107
Cdd:cd03674   1 HFTASAFVVNPDRGkvLLVHHRKLGRWLQPG-------GHVEPDEDPLEAALREAREETGLDVELlsPLSPDP----LDI 69

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
2G74_A      108 DPSGIVENEVCP-------VFAART-TSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03674  70 DVHPIPANPGEPahlhldvRYLAVAdGDEALRKSDESSDVRWFPLDELEE 119

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: 40.60 E-value: 9.01e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       41 NAKGQLLVTR-RALSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEiTPPESI-----YPDFRFRATDpsgi 112
Cdd:cd04670  11 NENNEVLVVQeKYGGPGGWklPG-------GLVDPGEDIGEAAVREVFEETGID-TEFVSIlgfrhQHPGRFGKSD---- 78

                        90       100       110
                ....*....|....*....|....*....|....*.
2G74_A      113 veneVCPVFAAR--TTSALQINDDEVMDYQWCDLAD 146
Cdd:cd04670  79 ----LYFVCRLRplSDEEIKICPEEIAEAKWMPLEE 110

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: 40.23 E-value: 1.18e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       68 GHPQLGESNEDAVIRRCRYELGVEItppESIYPDFRFRAT-DPSGIVENEVcpV-FAARTTSALQIN-DDEVMDYQWCDL 144
Cdd:cd03428  35 GHVEPGESELETALRETKEETGLTV---DDLPPGFRETLTySFKEGVEKTV--VyFLAELTPDVEVKlSEEHQDYKWLPY 109


                ....
2G74_A      145 ADVL 148
Cdd:cd03428 110 EEAL 113

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

Pssm-ID: 467573 [Multi-domain] Cd Length: 122 Bit Score: 39.21 E-value: 1.94e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       43 KGQLLVTRRALSKKAwpGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITPPESIypDFRFRatdPSGIVENEVCPVFA 122
Cdd:cd04691  11 EGKVLLVKRAYGPGK--GRWTLP-GGFVEEGETLDEAIVREVLEETGIDAKPVGII--GVRSG---VIRDGKSDNYVVFL 82

                        90       100
                ....*....|....*....|....*..
2G74_A      123 ARTTSA-LQINDDEVMDYQWCDLADVL 148
Cdd:cd04691  83 LEYVGGePKPDERENSEAGFLTLEEAL 109

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: 38.81 E-value: 3.17e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       40 FNAKGQLLVTRralSKKaWPGVWTNSvCGHPQLGESNEDAVIRRCRYELGVEITP------PESIYPDfRFRatDPSGIV 113
Cdd:cd18874  10 FNPDGKVLLVR---SHK-WNDLYGIP-GGKVEWGETLEEALKREVKEETGLDITDirfilvQESINSE-EFH--KPAHFV 81

                        90       100       110
                ....*....|....*....|....*....|....*
2G74_A      114 ENEvcpvFAARTTSALQINDDEVMDYQWCDLADVL 148
Cdd:cd18874  82 FVD----YLARTDSSEVVLNEEAVEYLWVEPEEAL 112

NUDIX hydrolase YfcD; Provisional

Pssm-ID: 185291 [Multi-domain] Cd Length: 180 Bit Score: 39.01 E-value: 5.20e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A        41 NAKGQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITPPESiYPDFRFratdpsgivENEVCPV 120
Cdd:PRK15393  46 DGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQLLESARREAEEELGIAGVPFAE-HGQFYF---------EDENCRV 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
2G74_A       121 ----FAARTTSALQINDDEVMDYQWCDLADVLHGIDA-TP---WAFSPWMVMQATNREARK 173
Cdd:PRK15393 116 wgalFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEfTPdslKALALWLTRNAKNEAVET 176

thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a bifunctional enzyme composed of a C-terminal thiamine pyrophosphokinase domain, which transfers pyrophosphate from ATP to thiamine and an N-terminal NUDIX hydrolase domain that converts oxidized derivatives of thiamine diphosphate (oxothiamine and oxythiamine) to their respective monophosphates. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belong to this superfamily requires a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.

Pssm-ID: 467544 Cd Length: 153 Bit Score: 37.86 E-value: 1.03e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRRALSKKAWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVE------ITPPESI--YPDFRfratdPSGIVEN 115
Cdd:cd03676  21 LRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLPedlarqARPAAGRvsYFYRS-----DEGGLQP 95

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
2G74_A      116 EVCPVFAARTTSAL--QINDDEVMDYQWCDLADVLHGIDATPWAFSPWMVM 164
Cdd:cd03676  96 EVLYVYDLELPEDFvpKPQDGEVESFELMSVDEVLEALRAGEFKPNCALVM 146

coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1), also called nucleoside diphosphate-linked moiety X)) motif 7, is a member of the NUDIX hydrolase superfamily, functions to catalyze the elimination of oxidized inactive CoA, which can inhibit CoA-utilizing enzymes. The need of CoAses mainly arises under conditions of oxidative stress. CoAse has a conserved NUDIX fold and requires a single divalent cation for catalysis. In addition to a signature NUDIX motif G[X5]E[X7]REUXEEXGU, where U is Ile, Leu, or Val, CoAse contains an additional motif upstream called the NuCoA motif (LLTXT(SA)X3RX3GX3FPGG) which is postulated to be involved in CoA recognition. CoA plays a central role in lipid metabolism. It is involved in the initial steps of fatty acid sythesis in the cytosol, in the oxidation of fatty acids and the citric acid cycle in the mitochondria, and in the oxidation of long-chain fatty acids in peroxisomes. CoA has the important role of activating fatty acids for further modification into key biological signalling molecules.

Pssm-ID: 467532 [Multi-domain] Cd Length: 158 Bit Score: 37.09 E-value: 1.92e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       45 QLLVTRRALSKKAWPGvwtnSVC---GHPQLG-ESNEDAVIRRCRYELGVeitPPESI-----YPDFRfratDPSGIVen 115
Cdd:cd03426  17 HVLLTKRASHLRSHPG----QIAfpgGKREPGdESPVETALRETEEEIGL---PPESVevlgrLDPLY----TPSGFV-- 83

                        90       100       110
                ....*....|....*....|....*....|....*
2G74_A      116 eVCP-VFAARTTSALQINDDEVMDYQWCDLADVLH 149
Cdd:cd03426  84 -VTPfVGLLDDPPPLRPNPDEVAEVFTVPLSFLLD 117

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: 36.76 E-value: 2.06e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRrALSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITPPEsiypdfrfratdPSGIVEN------ 115
Cdd:cd04688  13 GKVLLAR-GEDDDYYrlPG-------GRVEFGETSEDALVREFKEELGVEVEVVR------------LLFVVENfftydg 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
2G74_A      116 ----EVCPVFAAR--TTSALQIN------DDEVMDYQWCDLADvLHGIDATP 155
Cdd:cd04688  73 kpfhEIGFYYLVElsDEALYEQDiffleeDGEKLEFRWIPLEE-LDEIDLYP 123

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: 36.04 E-value: 3.39e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       44 GQLLVTRRALSKkaWPGVWTNSVCGHPQLGESNEDAVIRRCRYELGVEITP--------------PESIYPDFRFRATDP 109
Cdd:cd04683  11 DEVLLLRRANTG--YDDGWWHLPAGHVEAGETVRAAAVREAKEELGVEIDPedlrlvhtmhrrsdGGRERIDFFFRATRW 88


                ....*.
2G74_A      110 SGIVEN 115
Cdd:cd04683  89 SGEPRN 94

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: 35.64 E-value: 4.22e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRAlSKKAW--PGvwtnsvcGHPQLGESNEDAVIRRCRYELGVEITPPesiypdfRFRATD---PSGIV 113
Cdd:cd18876   7 FTDAAGRVLLVKPT-YKDGWelPG-------GVVEAGESPLQAARREVREELGLDVPVG-------RLLAVDwvpPAGGG 71

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
2G74_A      114 ENEVCPVFAARTTSALQIN-----DDEVMDYQWCDLADVL 148
Cdd:cd18876  72 DDAVLFVFDGGVLTPEQAAairlqDEELSAYRFVTPEEAA 111

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

Pssm-ID: 467577 [Multi-domain] Cd Length: 134 Bit Score: 35.68 E-value: 5.44e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRALSKKAWPGVWTNSVCGHPQlGESNEDAVIRRCRYELGVEIT----PPESIYPDFRFRaTDPSGIVE 114
Cdd:cd04696   8 LIENEGCYLLCKMADDRGVFPGQWALSGGGVEP-GERIEEALRREIREELGEQLIlsdiTPWTFRDDIRIK-TYPDGRQE 85

                        90       100       110
                ....*....|....*....|....*....|....*
2G74_A      115 N--EVCPVFAARTTSALQINDDEVMDYQWCDLADV 147
Cdd:cd04696  86 EiyMIYLIFDCVSANRDVCINDEFQDYAWVKPADL 120

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: 35.62 E-value: 5.62e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
2G74_A       39 LFNAKGQLLVTRRALSKKAWpgvwtnsvcGHPQ----LGESNEDAVIRrcryELGVEI-TPPESI-----YPDFrFRATD 108
Cdd:cd03671  10 LFNRDGQVLVGRRIDVPGAW---------QFPQggidEGEDPEEAALR----ELYEETgLSPEDVeiiaeTPDW-LTYDL 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
2G74_A      109 PSGIVENEVCPV--------FAARTT---SALQINDD---EVMDYQWCDLADVL 148
Cdd:cd03671  76 PEDLIRKGWGGKyrgqkqkwFLFRFTgddSEINLDTHehpEFDAWRWVDLEELP 129