NCBI Conserved Domain Search

Nudix family hydrolase;

Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 502.10 E-value: 0e+00

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596    1 MKRVHVAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHV 80
Cdd:PRK08999   2 MKRIHVAAGVIRDADGRILLARRPEGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIEVTAARPLITVRHDYPDKRV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   81 LLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQAARLPAHYLITPDGLEPG-ELISGVRKAVEAGIRLI 159
Cdd:PRK08999  82 RLDVRRVTAWQGEPHGREGQPLAWVAPDELAVYPFPPANQPIVRALRLPDTYLITPEGEDGDaAFLARLERALAAGIRLI 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  160 QLRAPNMFSPEYRDLAIDIQGLCAG-KAQLMLKGPLEWLGDFPAAGWHLTSAQLRKYASagRPFPEGRLLAASCHDAEEL 238
Cdd:PRK08999 162 QLRAPQLPPAAYRALARAALGLCRRaGAQLLLNGDPELAEDLGADGVHLTSAQLAALAA--RPLPAGRWVAASCHDAEEL 239

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599596  239 ALAASMGVEFVTLSPVQPTESHPGEPALGWDKAAELIAGFNQPVYLLGGLGPQQAEQAWEHGAQGVAGIRAFW 311
Cdd:PRK08999 240 ARAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVPLPVYALGGLGPGDLEEAREHGAQGIAGIRGLW 312

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: 176.49 E-value: 1.17e-55

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   4 VHVAAAVIRgSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLLD 83
Cdd:cd03425   1 IEVVAAIIV-DDGRVLIAQRPEGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIEVEVGEPLGTVEHDYPDFHVRLH 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|..
gi 15599596  84 VWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQA 125
Cdd:cd03425  80 VYLCTLWSGEPQLLEHQELRWVTPEELDDLDWLPADIPIVEA 121

Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl)thiazole phosphate to yield thiamine phosphate. This Pfam family also includes the regulatory protein TENI, a protein from Bacillus subtilis that regulates the production of several extracellular enzymes by reducing alkaline protease production. While TenI shows high sequence similarity with thiamin phosphate synthase, the purified protein has no thiamin phosphate synthase activity. Instead, it is a thiazole tautomerase.

Pssm-ID: 426849 [Multi-domain] Cd Length: 180 Bit Score: 149.62 E-value: 1.80e-44

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   132 YLITPDGLEPGELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLC-AGKAQLMLKGPLEWLGDFPAAGWHLTSA 210
Cdd:pfam02581   2 YLVTDPGLDGEDLLEVVEEALKGGVTIVQLREKELDDREFLELAKELRALCrKYGVPLIINDRVDLALAVGADGVHLGQD 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   211 QLrKYASAGRPFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPGEPALGWDKAAELIAGFNQPVYLLGGLGP 290
Cdd:pfam02581  82 DL-PVAEARELLGPDLIIGVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVEIPVVAIGGITP 160

                         170       180
                  ....*....|....*....|
gi 15599596   291 QQAEQAWEHGAQGVAGIRAF 310
Cdd:pfam02581 161 ENVPEVIEAGADGVAVVSAI 180

Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate synthase is part of the Pathway/BioSystem: Thiamine biosynthesis

Pssm-ID: 440121 [Multi-domain] Cd Length: 206 Bit Score: 141.48 E-value: 5.83e-41

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596 127 RLPAHYLITPDGLEPGELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLCAG-KAQLMLKGPLEWLGDFPAAGW 205
Cdd:COG0352   2 TLPRLYLITDPDLCGRDLLEVLEAALAGGVDLVQLREKDLDERELLALARALRALCRAyGVPLIINDRVDLALALGADGV 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596 206 HLTSAQLRKyASAGRPFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPG-EPALGWDKAAELIAGFNQPVYL 284
Cdd:COG0352  82 HLGQEDLPV-AEARALLGPDLIIGVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGaPPPLGLEGLAWWAELVEIPVVA 160

                       170       180
                ....*....|....*....|....*..
gi 15599596 285 LGGLGPQQAEQAWEHGAQGVAGIRAFW 311
Cdd:COG0352 161 IGGITPENAAEVLAAGADGVAVISAIW 187

8-oxo-dGTP diphosphatase MutT;

Pssm-ID: 182721 [Multi-domain] Cd Length: 129 Bit Score: 137.42 E-value: 2.08e-40

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596    1 MKRVHVAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHV 80
Cdd:PRK10776   1 MKKLQIAVGIIRNPNNEIFITRRAADAHMAGKWEFPGGKIEAGETPEQALIRELQEEVGITVQHATLFEKLEYEFPDRHI 80

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 15599596   81 LLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQ 124
Cdd:PRK10776  81 TLWFWLVESWEGEPWGKEGQPGRWVSQVALNADEFPPANEPIIA 124

NUDIX domain;

Pssm-ID: 464330 [Multi-domain] Cd Length: 114 Bit Score: 116.64 E-value: 1.83e-32

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596     7 AAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARelEEELGIRVERARPlIQVRHDYADKHVLLDVWE 86
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALAR--LEELGIEVEVLEP-GTVKHVFTHFRLTLHVYL 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 15599596    87 VDGFSGEAhgAEGQPLAWVEPRELADYEFPAANAPIVQA 125
Cdd:pfam14815  78 VREVEGEE--EPQQELRWVTPEELDKYALPAAVRKILEA 114

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;

Pssm-ID: 182536 [Multi-domain] Cd Length: 135 Bit Score: 109.83 E-value: 1.02e-29

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596    1 MKRVHVAAAVIRgSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHV 80
Cdd:PRK10546   1 MKMIDVVAAIIE-RDGKILLAQRPAHSDQAGLWEFAGGKVEPGESQPQALIRELREELGIEATVGEYVASHQREVSGRRI 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 15599596   81 LLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQA 125
Cdd:PRK10546  80 HLHAWHVPDFHGELQAHEHQALVWCTPEEALRYPLAPADIPLLEA 124

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

Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 105.45 E-value: 4.31e-28

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   1 MKRV--HVAAAVIRGSDGRVLIARRPeDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYaDK 78
Cdd:COG1051   1 MTKVpkVAVDAVIFRKDGRVLLVRRA-DEPGKGLWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPD-RG 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599596  79 HVLLDVWEVDGFSGEAH-GAEGQPLAWVEPRELADYEFPAANAPIVQ 124
Cdd:COG1051  79 HVVSVAFLAEVLSGEPRaDDEIDEARWFPLDELPELAFTPADHEILE 125

mutator mutT protein; All proteins in this family for which functions are known are involved in repairing oxidative damage to dGTP (they are 8-oxo-dGTPases). This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Lowering the threshold picks up members of MutT superfamily well. [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 200031 [Multi-domain] Cd Length: 128 Bit Score: 100.72 E-value: 2.95e-26

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596     1 MKRVHVAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYaDKHV 80
Cdd:TIGR00586   1 KKLQQIAVGIIRNENGEIIITRRADGHMFAKLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKLEYEFY-PRHI 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 15599596    81 LLDVWEVDGFSGEAHGAEGQP-LAWVEPRELADYEFPAANAPIVQAARL 128
Cdd:TIGR00586  80 TLWFWLLERWEGGPPGKEGQPeEWWVLVGLLADDFFPAANPVIIKLLRL 128

Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step in the thiamine biosynthesis pathway, the substitution of the pyrophosphate of 2-methyl-4-amino-5- hydroxymethylpyrimidine pyrophosphate by 4-methyl-5- (beta-hydroxyethyl) thiazole phosphate to yield thiamine phosphate. TenI is a enzymatically inactive regulatory protein involved in the regulation of several extracellular enzymes. This superfamily also contains other enzymatically inactive proteins with unknown functions.

Pssm-ID: 238317 [Multi-domain] Cd Length: 196 Bit Score: 96.05 E-value: 9.63e-24

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596 132 YLITPDGLEPGELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLCAG-KAQLMLKGPLEWLGDFPAAGWHLTS- 209
Cdd:cd00564   2 YLITDRRLDGEDLLEVVEAALKGGVTLVQLREKDLSARELLELARALRELCRKyGVPLIINDRVDLALAVGADGVHLGQd 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596 210 ----AQLRKYasagrpFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPG-EPALGWDKAAELIAGFNQPVYL 284
Cdd:cd00564  82 dlpvAEARAL------LGPDLIIGVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGaGPPLGLELLREIAELVEIPVVA 155

                       170       180
                ....*....|....*....|....*..
gi 15599596 285 LGGLGPQQAEQAWEHGAQGVAGIRAFW 311
Cdd:cd00564 156 IGGITPENAAEVLAAGADGVAVISAIT 182

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: 93.56 E-value: 1.93e-23

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   5 HVAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRH-DYADKHV--- 80
Cdd:COG0494  14 PAVVVVLLDDDGRVLLVRRYRYGVGPGLWEFPGGKIEPGESPEEAALRELREETGLTAEDLELLGELPSpGYTDEKVhvf 93

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 15599596  81 LLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQAARL 128
Cdd:COG0494  94 LARGLGPGEEVGLDDEDEFIEVRWVPLDEALALVTAGEIAKTLAALAR 141

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: 79.76 E-value: 9.54e-19

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   5 HVAAAVIRGSDGRVLIARRPeDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL--IQVRHDYADKHVLL 82
Cdd:cd02883   1 VAVGAVVFDDEGRVLLVRRS-DGPGPGGWELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLgvYEFPDPDEGRHVVV 79

                        90       100
                ....*....|....*....|....*.
gi 15599596  83 DVWEVDGFSGEAH---GAEGQPLAWV 105
Cdd:cd02883  80 LVFLARVVGGEPPpldDEEISEVRWV 105

Adenine-specific DNA glycosylase, acts on AG and A-oxoG pairs [Replication, recombination and repair];

Pssm-ID: 440807 [Multi-domain] Cd Length: 350 Bit Score: 81.72 E-value: 1.72e-17

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   2 KRVHVAAAVIRgSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVrAALARELEEELGIRVERARPLIQVRHDYADKHVL 81
Cdd:COG1194 228 PERYGAALVIR-DDGRVLLEKRPPKGLWGGLWEFPEFEWEEAEDP-EALERWLREELGLEVEWLEPLGTVRHVFTHFRLH 305

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 15599596  82 LDVWEVDGfsGEAHGAEGQPLAWVEPRELADYEFPAANAPIVQAAR 127
Cdd:COG1194 306 LTVYLARV--PAGPPAEPDGGRWVPLEELAALPLPAPMRKLLKALL 349

NUDIX domain;

Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 75.60 E-value: 8.36e-17

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596     6 VAAAVIRGSDGRVLIARRPeDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADK------- 78
Cdd:pfam00293   5 AVGVVLLNEKGRVLLVRRS-KKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDgrfpdeh 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 15599596    79 ---HVLLDVWEVDGFSGEahGAEGQPLAWVEPRELADYEFPAANAPIVQA 125
Cdd:pfam00293  84 eilYVFLAEVEGELEPDP--DGEVEEVRWVPLEELLLLKLAPGDRKLLPW 131

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

Pssm-ID: 467579 [Multi-domain] Cd Length: 118 Bit Score: 71.50 E-value: 1.45e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   9 AVIRGsDGRVLIARRPEDKhqGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL--IQVRHDyADKHVLLDVW- 85
Cdd:cd04699   7 GVIFD-NGRVLLLRRSRAG--AGEWELPGGRLEPGESPEEALKREVKEETGLDVSVGELLdtWTFELD-PDKGVFIVTYl 82

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 15599596  86 -EVDGF----SGEAHGAEgqplaWVEPRELADYEFP 116
Cdd:cd04699  83 cRLVGGevtlSDEHEEYE-----WVTPEELAELELP 113

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: 70.64 E-value: 3.83e-15

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRGSDGRVLIARrpedKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRV--ERARPLIQVR---HDYADKHV 80
Cdd:cd04690   2 VKAAVIIIKDGRLLLVR----KRGTDAFYLPGGKREPGETPLQALVRELKEELGLDLdpDSLRFLGTFEapaANEPGTTV 77

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599596  81 LLDVWEVDgFSGEAH-GAEGQPLAWVEPRELADYEFpaanAPIVQAARLPA 130
Cdd:cd04690  78 RMTCFTAD-YDGEPQpAAEIEELRWLDPADPDDDRL----APLLREIVLPL 123

thiamine phosphate synthase;

Pssm-ID: 234590 [Multi-domain] Cd Length: 212 Bit Score: 71.37 E-value: 1.19e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  132 YLITPDGLEPGE-LISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLCAGK---------AQLMLKgplewLGdfp 201
Cdd:PRK00043  10 YLITDSRDDSGRdLLEVVEAALEGGVTLVQLREKGLDTRERLELARALKELCRRYgvplivndrVDLALA-----VG--- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  202 AAGWHL-----TSAQLRKYasagrpFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPGEPALGW----DKAA 272
Cdd:PRK00043  82 ADGVHLgqddlPVADARAL------LGPDAIIGLSTHTLEEAAAALAAGADYVGVGPIFPTPTKKDAKAPQGleglREIR 155

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 15599596  273 ELIAGFnqPVYLLGGLGPQQAEQAWEHGAQGVAGIRA 309
Cdd:PRK00043 156 AAVGDI--PIVAIGGITPENAPEVLEAGADGVAVVSA 190

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

Pssm-ID: 467557 [Multi-domain] Cd Length: 128 Bit Score: 69.47 E-value: 1.22e-14

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   3 RVHVAAAVIRgsDGRVLIARR--PEDKhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVeRARPLIQVR----HDYA 76
Cdd:cd04673   1 IVAVGAVVFR--DGRVLLVRRgnPPDA---GLWSFPGGKVELGETLEDAALRELREETGLEA-EVVGLLTVVdvieRDEA 74

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599596  77 DK---H-VLLDVWevdgfsgeAHGAEGQPLA--------WVEPRELADYEFPAANAPIVQAA 126
Cdd:cd04673  75 GRvrfHyVILDFL--------AEWVSGEPVAgddaldarWFSLEELDGLPLTPGTRDVLERA 128

thiamine phosphate synthase;

Pssm-ID: 235054 [Multi-domain] Cd Length: 347 Bit Score: 71.07 E-value: 7.08e-14

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  122 IVQAARLpahYLITpDGLEpgELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLCAGKAQLMLkgplewLGDFP 201
Cdd:PRK02615 143 RLKDARL---YLIT-SPSE--NLLEVVEAALKGGVTLVQYRDKTADDRQRLEEAKKLKELCHRYGALFI------VNDRV 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  202 -------AAGWHLTSAQLrKYASAGRPFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPGEPALGWDKAAEL 274
Cdd:PRK02615 211 dialavdADGVHLGQEDL-PLAVARQLLGPEKIIGRSTTNPEEMAKAIAEGADYIGVGPVFPTPTKPGKAPAGLEYLKYA 289

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 15599596  275 IAGFNQPVYLLGGLGPQQAEQAWEHGAQGVAGIRA 309
Cdd:PRK02615 290 AKEAPIPWFAIGGIDKSNIPEVLQAGAKRVAVVRA 324

thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate pyrophosphorylase, ThiE, of a number of bacteria, and N-terminal domains of bifunctional thiamine proteins of Saccharomyces cerevisiae and Schizosaccharomyces pombe, in which the C-terminal domain corresponds to the bacterial hydroxyethylthiazole kinase (EC 2.7.1.50), ThiM. This model includes ThiE from Bacillus subtilis but excludes its paralog, the regulatory protein TenI (SP:P25053), and neighbors of TenI. [Biosynthesis of cofactors, prosthetic groups, and carriers, Thiamine]

Pssm-ID: 273222 [Multi-domain] Cd Length: 196 Bit Score: 68.04 E-value: 1.70e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   132 YLITPDGLEPGELISGVRKAVEAGIRLIQLRAPNMFSPEYRDLAIDIQGLC-AGKAQLMLKGPLEWLGDFPAAGWHLTSA 210
Cdd:TIGR00693   3 YLITDPQDGPADLLNRVEAALKGGVTLVQLRDKGSNTRERLALAEKLQELCrRYGVPFIVNDRVDLALALGADGVHLGQD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   211 QLrKYASAGRPFPEGRLLAASCHDAEELALAASMGVEFVTLSPVQPTESHPGE-PALGWDKAAELIA-GFNQPVYLLGGL 288
Cdd:TIGR00693  83 DL-PASEARALLGPDKIIGVSTHNLEELAEAEAEGADYIGFGPIFPTPTKKDPaPPAGVELLREIAAtLIDIPIVAIGGI 161

                         170       180
                  ....*....|....*....|...
gi 15599596   289 GPQQAEQAWEHGAQGVAGIRAFW 311
Cdd:TIGR00693 162 TLENAAEVLAAGADGVAVVSAIM 184

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: 64.47 E-value: 1.21e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   4 VHVaaaVIRGSDGRVLIARR-PEDKHQGGLWEF-PGGKVEDGEPVRAALARELEEELGIRV--ERARPLIQVRHDyadkH 79
Cdd:cd04693  32 VHV---WIFNSDGEILIQQRsPDKKGFPGMWEAsTGGSVLAGETSLEAAIRELKEELGIDLdaDELRPILTIRFD----N 104


                ....*...
gi 15599596  80 VLLDVWEV 87
Cdd:cd04693 105 GFDDIYLF 112

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

Pssm-ID: 467562 [Multi-domain] Cd Length: 126 Bit Score: 63.10 E-value: 1.92e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   3 RVHVAAAVIRgsDGRVLIARR---PEDKHqgglWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADK- 78
Cdd:cd04679   2 RVGCGAAILD--DGRLLLVLRlraPEAGH----WGLPGGKVDWLETVEDAVRREILEELGLEIELTRLLCVVDQIDAADg 75

                        90
                ....*....|....*..
gi 15599596  79 -HVLLDVWEVDGFSGEA 94
Cdd:cd04679  76 eHWVAPVYLAEIFSGEP 92

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: 62.99 E-value: 1.99e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   7 AAAVIRGSDGRVLIARRPEDKHqgglWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL----IQVRHDYADKHVLL 82
Cdd:cd18876   3 AGALFTDAAGRVLLVKPTYKDG----WELPGGVVEAGESPLQAARREVREELGLDVPVGRLLavdwVPPAGGGDDAVLFV 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599596  83 dvwevdgFSGEAHGAEGQPLAWVEPRELADYEF-PAANAPIVQAARL 128
Cdd:cd18876  79 -------FDGGVLTPEQAAAIRLQDEELSAYRFvTPEEAAELLPPRL 118

C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is responsible for repairing misread A*oxoG residues to C*G by removing the inappropriately paired adenine base from the DNA backbone. It belongs to the NUDIX hydrolase superfamily and is important for the repair of various genotoxic lesions. Enzymes belonging to this superfamily requires a divalent cation, such as Mg2+ or Mn2+ for their activity. They are also recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V). However, DNA glycosylase does not seem to contain this signature motif. DNA glycosylase consists of 2 domains: the N-terminal domain contains the catalytic properties of the enzyme and the C-terminal domain affects substrate (oxoG) binding and enzymatic turnover. The C-terminal domain is highly similar to MutT, based on secondary structure and topology, despite low sequence identity. MutT sanitizes the nucleotide precursor pool by hydrolyzing oxo-dGTP to oxo-dGMO and inorganic pyrophosphate. The similarity strongly suggests that the two proteins share a common evolutionary origin.

Pssm-ID: 467537 [Multi-domain] Cd Length: 118 Bit Score: 62.71 E-value: 2.42e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   2 KRVHVAAAVIRgSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVErarPLIQVRHDYADKHVL 81
Cdd:cd03431   2 PERYFTVLVLR-DGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILE---PLGEVKHVFSHFRLH 77

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15599596  82 LDVWEVDGfsGEAHGAEGQPLAWVEPRELADYEFPAA 118
Cdd:cd03431  78 ITVYLVEL--PEAPPAAPDEGRWVDLEELDEYALPAP 112

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

Pssm-ID: 467593 [Multi-domain] Cd Length: 130 Bit Score: 63.04 E-value: 2.61e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   4 VHVAAAVIRGSDGRVLIARRPEDKH--QGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIqVRHDYADKHVL 81
Cdd:cd18882   1 HEVAIAILYDDRGKVLLQLRDDKPGipYPGYWGLFGGHLEPGETPEEAIRRELEEEIGYEPGEFRFFL-LYTEDDGEDRI 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15599596  82 LDVWEV--DGFSGEAHGAEGQPLAWVEPRELADYEFPAANAPIV 123
Cdd:cd18882  80 RHVFHAplDVDLSDLVLNEGQALRLFSPEEILQGPLYSNLAGIL 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: 467586 [Multi-domain] Cd Length: 125 Bit Score: 62.69 E-value: 3.04e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   8 AAVIRGSDGRVLIARRPEdkhQGGLWEFPGGKVEDGEPVRAALARELEEELG-----IRVERARPLIQVRHDYADKH-VL 81
Cdd:cd18874   6 GALIFNPDGKVLLVRSHK---WNDLYGIPGGKVEWGETLEEALKREVKEETGlditdIRFILVQESINSEEFHKPAHfVF 82

                        90       100       110
                ....*....|....*....|....*....|...
gi 15599596  82 LDVWeVDGFSGEAH-GAEGQPLAWVEPRELADY 113
Cdd:cd18874  83 VDYL-ARTDSSEVVlNEEAVEYLWVEPEEALKY 114

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: 62.70 E-value: 4.11e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   7 AAAVIRGSDGRVLIARRPED-KHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVerarpliqvrhDYADKHVLLDVW 85
Cdd:cd04694   5 VVVLIEDSDDRVLLTRRAKHmRTFPGVWVPPGGHVELGESLLEAGLRELQEETGLEV-----------SDIQSLSLLGLW 73


                .
gi 15599596  86 E 86
Cdd:cd04694  74 E 74

MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside diphosphate-linked moiety X)) motif 1 (Nudt1), is a member of the NUDIX hydrolase superfamily. MTH1, the mammalian counterpart of MutT, hydrolyzes oxidized purine nucleoside triphosphates, such as 8-oxo-dGTP and 2-hydroxy-ATP, to monophosphates, thereby preventing the incorporation of such oxygen radicals during replication. This is an important step in the repair mechanism in genomic and mitochondrial DNA. Like other members of the NUDIX family, it requires a divalent cation, such as Mg2+ or Mn2+, for activity, and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. MTH1 is predominantly localized in the cytoplasm and mitochondria. Structurally, this enzyme adopts a similar fold to MutT despite low sequence similarity outside the conserved NUDIX motif. The most distinctive structural difference between MutT and MTH1 is the presence of a beta-hairpin, which is absent in MutT. This results in a much deeper and narrower substrate binding pocket. Mechanistically, MTH1 contains dual specificity for nucleotides that contain 2-OH-adenine bases and those that contain 8-oxo-guanine bases.

Pssm-ID: 467533 [Multi-domain] Cd Length: 136 Bit Score: 62.16 E-value: 6.59e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  10 VIRGSDgRVLIARrpedKHQG---GLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLLD--V 84
Cdd:cd03427   8 VLRGDD-RVLLGL----KKRGfgaGKWNGFGGKVEPGETIEEAAVRELEEEAGLTATELEKVGRLKFEFPDDPEAMDvhV 82

                        90
                ....*....|
gi 15599596  85 WEVDGFSGEA 94
Cdd:cd03427  83 FRADSWTGEP 92

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: 62.64 E-value: 6.64e-12

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  10 VIRGSDGRVLIARRPEDKH-QGGLWE-FPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLLDVWEV 87
Cdd:cd04697  32 VVRNAAGRLLVQKRTMDKDyCPGYLDpATGGVVGAGESYEENARRELEEELGIDGVPLRPLFTFYYEDDRSRVWGALFEC 111

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15599596  88 DgFSGEAHGAEGQpLAWVEPRELADyefpaanapIVQAARlpaHYLITPDGLE 140
Cdd:cd04697 112 V-YDGPLKLQPEE-VAEVDWMSEDE---------ILQAAR---GEEFTPDGRV 150

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: 61.43 E-value: 1.38e-11

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   7 AAAVIRGSDGRVLIARRpedKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYA 76
Cdd:cd03671   6 VGIVLFNRDGQVLVGRR---IDVPGAWQFPQGGIDEGEDPEEAALRELYEETGLSPEDVEIIAETPDWLT 72

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: 61.03 E-value: 1.41e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   7 AAAVIRgSDGRVLIARRPEDKHqgglWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL--IQVRHDYADK--HVLL 82
Cdd:cd04688   5 VAAIII-RDGKVLLARGEDDDY----YRLPGGRVEFGETSEDALVREFKEELGVEVEVVRLLfvVENFFTYDGKpfHEIG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599596  83 DVWEVDgFSGEAH----------GAEGQPLAWVEPRELADYEF 115
Cdd:cd04688  80 FYYLVE-LSDEALyeqdiffleeDGEKLEFRWIPLEELDEIDL 121

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: 60.60 E-value: 3.36e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   4 VHVaaaVIRGSDGRVLIARRPEDK-HQGGLWEFP-GGKVEDGEPVRAALARELEEELGIRVERA-RPLIQVRHDYADKHV 80
Cdd:COG1443  32 FSV---FVFNSDGRLLLQRRALTKdHWPGLWDNTvCGHPRAGETYEEAAVRELEEELGITVDDDlRPLGTFRYRAVDANG 108

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599596  81 LLDvWEVDG-FSGEAHGA-EGQP-----LAWVEPRELAD 112
Cdd:COG1443 109 LVE-NEFCHvFVARLDGPlTPQPeevaeVRWVTLEELLA 146

diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a member of the NUDIX hydrolase superfamily. Ap6A hydrolase specifically hydrolyzes diadenosine polyphosphates, but not ATP or diadenosine triphosphate, and it generates ATP as the product. Ap6A, the most preferred substrate, hydrolyzes to produce two ATP molecules, which is a novel hydrolysis mode for Ap6A. These results indicate that Ap6A hydrolase is a diadenosine polyphosphate hydrolase. It requires the presence of a divalent cation, such as Mn2+, Mg2+, Zn2+, and Co2+, for activity. Members of the NUDIX hydrolase superfamily are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which forms a structural motif that functions as a metal binding and catalytic site.

Pssm-ID: 467541 [Multi-domain] Cd Length: 131 Bit Score: 59.87 E-value: 3.48e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  10 VIRGSDG--RVLIARRPedkhQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLldVW-E 86
Cdd:cd03673   8 VWRGRGGggEVLLIHRP----RYDDWSLPKGKLEPGETPEEAAVREVEEETGLRVRLGRPLGTTRYTYTRKGKG--ILkK 81

                        90       100       110
                ....*....|....*....|....*....|....
gi 15599596  87 VDGFSGEAHGAEGQP--------LAWVEPRELAD 112
Cdd:cd03673  82 VHYWLMRALGGEFLPqpeeeideVRWLPPDEARR 115

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

Pssm-ID: 467561 [Multi-domain] Cd Length: 128 Bit Score: 59.50 E-value: 4.09e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   8 AAVIRGSDGRVLIARRpEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQVRHDY---ADKHVlLDV 84
Cdd:cd04678   6 GVIVLNDDGKVLLGRR-KGSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVR-FLTVTNDVfeeEGKHY-VTI 82

                        90       100       110
                ....*....|....*....|....*....|.
gi 15599596  85 WEVdgfsgeAHGAEGQPLAWVEPRELADYEF 115
Cdd:cd04678  83 FVL------AEVDDGEPEENMEPDKCEGWEW 107

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: 59.15 E-value: 7.78e-11

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599596   6 VAAAVIRGSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVE 63
Cdd:cd04683   1 VDVHLLLVRGDEVLLLRRANTGYDDGWWHLPAGHVEAGETVRAAAVREAKEELGVEID 58

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

Pssm-ID: 467596 [Multi-domain] Cd Length: 147 Bit Score: 59.17 E-value: 8.42e-11

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  15 DGRVLIARRPEDKHQGgLWEFPGGKVEDGEPVRAALARELEEELGIRVE--RARPLIQVRHDYADKHVLLDVWEVDGFSG 92
Cdd:cd18886  10 DDEVLLLNRNKKPNMG-KWNGVGGKLEPGESPEECAIREVFEETGLELEdlQLRGIVTFPSFDGGEDWLMYVFLAEAFSG 88

                        90       100
                ....*....|....*....|....
gi 15599596  93 EAH--GAEGqPLAWVEPRELADYE 114
Cdd:cd18886  89 ELVesDREG-ILAWVPIDWLLNLP 111

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

Pssm-ID: 467591 [Multi-domain] Cd Length: 126 Bit Score: 57.92 E-value: 1.39e-10

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   3 RVHVAAAVIRgsDGRVLIARRpeDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVErARPLIQVR---HDYADKH 79
Cdd:cd18880   1 RIRAKAIIIE--DGKLLLVKH--RDEGGIFYILPGGGQEHGETLPEALKRECLEETGLDVE-VGDLLFVReyiGPNKPVH 75

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599596  80 VLLDVWEVDGFSGEAH-GAEGQP----LAWVEPRELADYE-FPAANAPIVQ 124
Cdd:cd18880  76 QVELFFLCTLEGGELTlGSDPDLnqvgVEWIPLEELDSIRlYPAILRELII 126

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: 55.27 E-value: 1.43e-09

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599596   6 VAAAV---IRgSDGRVLIARRPED--KhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVERAR 66
Cdd:cd04681   5 VAAAVgviIR-NEGEILFVRRAKEpgK---GKLDLPGGFVDPGESAEEALRRELREELGLKIPKLR 66

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: 53.31 E-value: 6.77e-09

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599596   4 VHVAAAVIRgSDGRVLIARrpeDKHQG-GLWEFPGGKVEDGEPVRAALARELEEELGIRVErARPLIQVRH 73
Cdd:cd04670   3 VGVGGLVIN-ENNEVLVVQ---EKYGGpGGWKLPGGLVDPGEDIGEAAVREVFEETGIDTE-FVSILGFRH 68

RNA pyrophosphohydrolase; Reviewed

Pssm-ID: 234820 [Multi-domain] Cd Length: 156 Bit Score: 53.62 E-value: 8.96e-09

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599596    8 AAVIRGSDGRVLIARRPEDKHqggLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRH 73
Cdd:PRK00714  12 GIILLNRQGQVFWGRRIGQGH---SWQFPQGGIDPGETPEQAMYRELYEEVGLRPEDVEILAETRD 74

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: 52.12 E-value: 2.30e-08

                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15599596  32 LWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL 68
Cdd:cd03424  30 LLELPAGKIDPGEDPEEAARRELEEETGYTAGDLELL 66

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

Pssm-ID: 467594 Cd Length: 136 Bit Score: 52.08 E-value: 2.40e-08

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15599596   5 HVAAAVIRgSDGRVLIARRPEDKHqgglWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVL 81
Cdd:cd18883   1 YTARGVII-SDEHLLLARVKGDDK----TFLPGGHIEIGESAEIALVRELREELGLSCKVGRYLGAVENQWQDKEVI 72

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

Pssm-ID: 467563 [Multi-domain] Cd Length: 121 Bit Score: 51.48 E-value: 2.42e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRGsDGRVLIARrpedkHQ-GGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQV---RHDYADKHVL 81
Cdd:cd04680   3 VRAIVLDD-AGRVLLVR-----HTyVPGWYLPGGGVDKGETAEEAARRELREEAGVVLTGPPRLFGVyfnRRVSPRDHVA 76

                        90
                ....*....|...
gi 15599596  82 LDVweVDGFSGEA 94
Cdd:cd04680  77 LYR--VREFEQTE 87

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: 51.80 E-value: 2.57e-08

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599596  14 SDGRVLIAR-RPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERAR---PLIQVR--HDYADKHVLLD 83
Cdd:cd04685  10 PDGRVLLFRfHDPDDPGRSWWFTPGGGVEPGESPEQAAVRELREETGLRLEPDDlggPVWRRRavFDFSGETVRQD 85

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: 51.53 E-value: 2.77e-08

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRgsDGRVLIARRpedKHQG--GLWEFPGGKVEDGEPVRAALARELEEELGIRVeRARPLIQVRH--DYADKHVL 81
Cdd:cd04691   4 VGGVVVK--EGKVLLVKR---AYGPgkGRWTLPGGFVEEGETLDEAIVREVLEETGIDA-KPVGIIGVRSgvIRDGKSDN 77

                        90       100       110
                ....*....|....*....|....*....|..
gi 15599596  82 LDVWEVDGFSGE--AHGAEGQPLAWVEPRELA 111
Cdd:cd04691  78 YVVFLLEYVGGEpkPDERENSEAGFLTLEEAL 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: 467587 [Multi-domain] Cd Length: 144 Bit Score: 49.88 E-value: 1.36e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  10 VIRGSDGRVLIARRPEDKHQGglWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQVRHDYADKH---VLLDVWe 86
Cdd:cd18875   8 MIYDGEDRVLVLDRVKKDWGG--YTFPGGHVEPGESFVDSVIREVKEETGLTIKNPE-LCGIKQWINPDGeryIVFLYK- 83

                        90       100
                ....*....|....*....|....*....
gi 15599596  87 VDGFSGEAHG-AEGQpLAWVEPRELADYE 114
Cdd:cd18875  84 TDHFSGELLSsEEGE-LFWIPIEELKKLP 111

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: 49.56 E-value: 1.70e-07

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRGSD-GRVLIARRPEDkhqGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERArPLIQVRHD 74
Cdd:cd04664   3 VLVVIYRKDEeGEVLLLKRTDD---GGFWQSVTGGIEDGETPWQAALRELKEETGLDPLEL-QLIDLNVS 68

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: 49.43 E-value: 2.13e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   7 AAAVIRGSDGRVLIARRPEdkhqGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQVrhdYADK-------- 78
Cdd:cd04677  15 AAVIILNEQGRILLQKRTD----TGDWGLPGGAMELGESLEETARREVFEETGLTVEELE-LLGV---YSGKdlyytypn 86

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 15599596  79 ----HVLLDVWEVDGFSGE--AHGAEGQPLAWVEPRELADYEFP 116
Cdd:cd04677  87 gdevYNVTAVYLVRDVSGElkVDDEESLELRFFSLDELPENINP 130

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: 48.01 E-value: 3.89e-07

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15599596  33 WEFPGGKVEDGEPVRAALARELEEELGIRVERARPL 68
Cdd:cd04665  24 WEFPGGKREPGETIEEAARRELYEETGAVIFELKPL 59

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: 48.64 E-value: 5.77e-07

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15599596   8 AAVI-----RGSDGRVLIARRPED-KHQGGLWEFPGGKVEDGE--PVRAALaRELEEELGIRVERARPL 68
Cdd:cd03426   3 AAVLiplveGDGELHVLLTKRASHlRSHPGQIAFPGGKREPGDesPVETAL-RETEEEIGLPPESVEVL 70

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

Pssm-ID: 467585 [Multi-domain] Cd Length: 132 Bit Score: 47.92 E-value: 6.56e-07

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599596   4 VHVAA-AVIRGSDG---RVLIARRPEDKHQGGlWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:cd18873   1 PSVTVdCVIFGFDDgelKVLLIKRKNEPFKGG-WALPGGFVREDETLEDAARRELREETGLKD 62

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: 47.78 E-value: 8.03e-07

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   8 AAVIRGSDGRVLIaRRPEDkhqGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQV------RHDYADKH-- 79
Cdd:cd04676  21 AAVILNEDGRILL-QRKGG---LGLWSLPAGAIEPGEHPAEAVIREVREETGLLVKPTR-LLGVfggkefRYTYPNGDqv 95

                        90       100       110
                ....*....|....*....|....*....|...
gi 15599596  80 ---VLLDVWEVDGFSGEAHGAEGQPLAWVEPRE 109
Cdd:cd04676  96 eytVIAFKCVVTGGTLNAIDGETSELRYFSRTQ 128

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: 46.89 E-value: 1.11e-06

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....
gi 15599596   8 AAVIRGSDGRVLIARRPedkhqGGLWEFPGGKVEDGEPVRAALARELEEELGIR 61
Cdd:cd04667   3 ATVICRRGDRILLVARR-----GGRWLLPGGKIEPGESPLEAAIRELKEETGLA 51

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

Pssm-ID: 467558 [Multi-domain] Cd Length: 118 Bit Score: 46.69 E-value: 1.21e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599596   6 VAAAVIRGSDGRVLIARRPEDKHqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVERAR 66
Cdd:cd04674   6 VVVALLPVRDGLLVIRRGIEPGH--GELALPGGYIEYGETWQEAAVRELREETGVEADAAE 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: 467569 [Multi-domain] Cd Length: 130 Bit Score: 46.90 E-value: 1.26e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  15 DGRVLIARRPEDKHQGgLWEFPGGKVEDGEPVRAALARELEEELGIRVE-----RARPLIQVRHDYADKHV--LLDVWEV 87
Cdd:cd04686  11 NDKLLLIRKTRGPYQG-RYDLPGGSQEFGESLEDALKREFAEETGMTVTsydnlGVYDFFVPWSDKELGDVhhIGVFYDV 89

                        90       100
                ....*....|....*....|....*....
gi 15599596  88 DGFSG---EAHGAEGQP---LAWVEPREL 110
Cdd:cd04686  90 ELLDNnisELLQFEGQDslgAVWIPLQDL 118

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

Pssm-ID: 467565 [Multi-domain] Cd Length: 123 Bit Score: 46.51 E-value: 1.56e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  31 GLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQ---VRHDYADKHVLLDV--WEVDGFSGEAHGAEGQPLAWV 105
Cdd:cd04682  28 NLWDLPGGGREGDETPFACVLRELREELGLALPEDRLVWErvyPSNHNPGRQSWFFVarLPADEVDAIRFGDEGQEWALM 107


                ....
gi 15599596 106 EPRE 109
Cdd:cd04682 108 PVDD 111

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: 47.10 E-value: 1.91e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  14 SDGRVLIARRPEDK-HQGGLWE-------FPGgkvedgEPVRAALARELEEELGIRVERARPLIQVRHDYADKHVLLDvW 85
Cdd:cd02885  38 SKGELLLQRRALSKyTWPGLWTntccshpLPG------EGVEDAAQRRLREELGIPVCDLEELPRFRYRATDDNGLVE-H 110

                        90       100       110
                ....*....|....*....|....*....|....
gi 15599596  86 EVDG-FSGEAHG------AEGQPLAWVEPRELAD 112
Cdd:cd02885 111 EIDHvFVGRADGdpvpnpEEVSDYRWVSLEELRE 144

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

Pssm-ID: 467590 [Multi-domain] Cd Length: 142 Bit Score: 46.42 E-value: 2.48e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15599596   9 AVIRGSDGRVLIARRPEDkhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQV 71
Cdd:cd18879  23 AVVLRDAGRVLLVRRADN----GRWTPVTGIVEPGEQPADAAVREVLEETGVDVEVER-LASV 80

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

Pssm-ID: 467548 [Multi-domain] Cd Length: 132 Bit Score: 44.98 E-value: 6.69e-06

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRGSDGRVLIARRPeDKHQGGLwEFPGGKVEDGEPVRAALARELEEELGIRVERA----------RPLIQVRHDY 75
Cdd:cd04663   3 VCAYVTRGRNRELLVFEHP-DFPEAGL-QVPKGTVEPGESPEEAALRELAEETGLTGARVvvdlgshdegFEELHQRWFF 80

                        90       100       110
                ....*....|....*....|....*....|....
gi 15599596  76 adkHVLL-----DVWEvdgfSGEAHGAEGQPLAW 104
Cdd:cd04663  81 ---HLCLageppERWE----HHETDDGEGGGLRF 107

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: 44.86 E-value: 8.09e-06

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599596   4 VHVAaaVIRGSDGRVLIARRPEDK-HQGGLWEFP-GGKVEDGEPVRAALARELEEELGIRVERAR 66
Cdd:cd04692  29 VHVW--LVNPEEGRLLLQKRSANKdDFPGLWDISaAGHIDAGETYEEAAVRELEEELGLTVSPED 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: 467542 [Multi-domain] Cd Length: 130 Bit Score: 44.17 E-value: 1.17e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   6 VAAAVIRGSDGRVLIArrpedKHQ-GGLWEFPGGKVEDGEPVRAALARELEEELGIRVE----RARPLIQVR------HD 74
Cdd:cd03674   4 ASAFVVNPDRGKVLLV-----HHRkLGRWLQPGGHVEPDEDPLEAALREAREETGLDVEllspLSPDPLDIDvhpipaNP 78

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 15599596  75 YADKHVLLDV---WEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAA 118
Cdd:cd03674  79 GEPAHLHLDVrylAVADGDEALRKSDESSDVRWFPLDELEELSMDPN 125

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

Pssm-ID: 467535 [Multi-domain] Cd Length: 126 Bit Score: 44.02 E-value: 1.22e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599596   6 VAAAVIRGSDgRVLIARRPedKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERAR 66
Cdd:cd03429   4 VIVLVTNGED-KILLARQP--RWPPGRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKNVR 61

8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 18/Nudt18; 2-hydroxy-DADP phosphatase; 7,8-dihydro-8-oxoguanine phosphatase, hydrolyzes 8-oxo-7,8-dihydroguanine (8-oxo-Gua)-containing deoxyribo- and ribonucleoside diphosphates to the monophosphates. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.

Pssm-ID: 467555 [Multi-domain] Cd Length: 130 Bit Score: 44.22 E-value: 1.24e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   5 HVAAAVIRGSDGRVLIARrpEDKHQ-GGLWEFPGGKVEDGEPVRAALARELEEELGIRVE 63
Cdd:cd04671   1 YVVAAVIINEQGEVLMIQ--EAKRScRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCE 58

thiazole tautomerase TenI;

Pssm-ID: 181086 [Multi-domain] Cd Length: 201 Bit Score: 44.63 E-value: 1.81e-05

                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599596  231 SCHDAEELALAASMGVEFVTLSPVQPTESHPGEPALGWDKAAELIAGFNQPVYLLGGLGPQQAEQAWEHGAQGVA 305
Cdd:PRK07695 101 SVHSLEEAIQAEKNGADYVVYGHVFPTDCKKGVPARGLEELSDIARALSIPVIAIGGITPENTRDVLAAGVSGIA 175

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;

Pssm-ID: 235436 [Multi-domain] Cd Length: 340 Bit Score: 45.77 E-value: 1.93e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596    3 RVHVAAAVIRgsDGRVLIARRPEDKHQGgLWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:PRK05379 203 FVTVDAVVVQ--SGHVLLVRRRAEPGKG-LWALPGGFLEQDETLLDACLRELREETGLKL 259

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: 467553 [Multi-domain] Cd Length: 120 Bit Score: 42.73 E-value: 2.63e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15599596   7 AAAVIRGSDGRVLIAR-RPEDKHqgglWEFPGGKVEDGEPVRAALARELEEELGIRVE 63
Cdd:cd04669   3 AVLVIYDDDKLLLIRRtKPGEEY----YVFPGGGIEPGETPEEAALREAVEELGLDVA 56

nucleoside triphosphatase YtkD; The functional assignment to the proteins of this family is contentious, with papers disagreeing in both interpretation and enzyme assay results. This protein belongs to the nudix family and shares some sequence identity with E. coli MutT but appears not to be functionally interchangeable with it. [DNA metabolism, DNA replication, recombination, and repair]

Pssm-ID: 131752 Cd Length: 156 Bit Score: 43.13 E-value: 3.63e-05

                          10        20        30
                  ....*....|....*....|....*....|....*
gi 15599596    25 EDKHQGglWEFPGGKVEDGEPVRAALARELEEELG 59
Cdd:TIGR02705  41 EHKRRG--LEFPGGKVEPGETSKEAAIREVMEETG 73

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

Pssm-ID: 467609 [Multi-domain] Cd Length: 137 Bit Score: 42.93 E-value: 3.89e-05

                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15599596  33 WEFPGGKVEDGEPVRAALARELEEELGIRVERARPL 68
Cdd:cd24161  32 WEIPAGGWPEGEDPEEAARRELREETGLRAERWTPL 67

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

Pssm-ID: 467545 [Multi-domain] Cd Length: 123 Bit Score: 42.56 E-value: 3.97e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 15599596  15 DGRVLIARRP-EDKHqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPL 68
Cdd:cd04511  12 EGKVLLCRRAiEPRK--GYWTLPAGFMELGETTEQGAARETREEAGARVEIGSLY 64

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

Pssm-ID: 467567 [Multi-domain] Cd Length: 140 Bit Score: 42.22 E-value: 5.84e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599596   7 AAAVIRGSDGRVLIARRPEDKHQgglweFPGGKVEDGEPVRAALARELEEELGIRVERARPL 68
Cdd:cd04684  18 AYAVIFNDEGKVLLVQTPNGGYF-----LPGGGIEPGETPEEALHREVLEETGWEIEIGEFL 74

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: 41.84 E-value: 7.41e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  14 SDGRVLIARRPEDKHQ-GGLWEFPGGKVEDGEPVRAALARELEEELG--IRVERARPLIqVRHD-----YADKH------ 79
Cdd:cd04696  11 NEGCYLLCKMADDRGVfPGQWALSGGGVEPGERIEEALRREIREELGeqLILSDITPWT-FRDDiriktYPDGRqeeiym 89

                        90       100       110
                ....*....|....*....|....*....|....*....
gi 15599596  80 VLLDVWEVDGFSGEAHGAEGQPLAWVEPRELADYEFPAA 118
Cdd:cd04696  90 IYLIFDCVSANRDVCINDEFQDYAWVKPADLANYDLNVA 128

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

Pssm-ID: 467580 [Multi-domain] Cd Length: 147 Bit Score: 42.20 E-value: 7.49e-05

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599596   7 AAAVIRGSDGRVLIARR---PEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:cd04700  16 AGVVLLNERGDILLVQEkgiSGHPEKAGLWHIPSGAVEDGENPQDAAVREACEETGLRV 74

nucleoside triphosphatase NudI; Provisional

Pssm-ID: 185369 [Multi-domain] Cd Length: 141 Bit Score: 42.04 E-value: 7.49e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   15 DGRVLIARRPEDKhqG---GLWEFPGGKVEDGEPVRAALARELEEELGIRVERA-------RPLIQVRhDYADKH---VL 81
Cdd:PRK15472  14 DGAYLLCKMADDR--GvfpGQWALSGGGVEPGERIEEALRREIREELGEQLLLTeitpwtfRDDIRTK-TYADGRkeeIY 90

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 15599596   82 LDVWEVDGFSGEAH---GAEGQPLAWVEPRELADYEFPAA 118
Cdd:PRK15472  91 MIYLIFDCVSANRDvkiNEEFQDYAWVKPEDLVHYDLNVA 130

CDP-Choline Pyrophosphatase and similar proteins; Members include: CDP-Choline Pyrophosphatase, ADP-ribose pyrophosphatase, and UDP-X diphosphatase. CDP-choline pyrophosphatase catalyzes the hydrolysis of CDP-choline to produce CMP and phosphocholine. ADP-ribose pyrophosphatase catalyzes the hydrolysis of ADP-ribose to AMP and ribose-5-P. UDP-X diphosphatase hydrolyzes UDP-N-acetylmuramic acid and UDP-N-acetylmuramoyl-L-alanine. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.

Pssm-ID: 467556 [Multi-domain] Cd Length: 128 Bit Score: 41.78 E-value: 7.92e-05

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   4 VHVAAAVIRgsDGRVLIARRPEDkhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVeRARPLIQVRH 73
Cdd:cd04672   3 VDVRAAVFK--DGKILLVREKSD----GRWTLPGGWADVGLSPAENAVKEVREESGYEV-RARKLLAVFD 65

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

Pssm-ID: 467589 [Multi-domain] Cd Length: 141 Bit Score: 41.96 E-value: 8.99e-05

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  18 VLIARRPEDKHQGGLWEFPGGKVEDGE-PVRAALaRELEEELGI--RVERARPLIQVRHD-------YADKHVLLDVWEV 87
Cdd:cd18877  34 VLLQHRAWWTHQGGTWALPGGARDSGEtPEAAAL-RETEEETGLdaDTLRVVGTHVDDHGgwsyttvLASAPEPLPVRPA 112

                        90       100
                ....*....|....*....|....*.
gi 15599596  88 DGFSGEahgaegqpLAWVEPRELADY 113
Cdd:cd18877 113 NEESVE--------LRWVPLDEVESL 130

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: 41.39 E-value: 9.20e-05

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15599596  28 HQGGLWEFPGGKVEDGE-PVRAALaRELEEELGIRVER 64
Cdd:cd03428  25 SYGGHWDFPKGHVEPGEsELETAL-RETKEETGLTVDD 61

NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus radiodurans protein DR_0079 is one of 21 NUDIX hydrolases that it encodes, and it has been observed to have a marked preference for cytosine ribonucleoside 5'-diphosphate (CDP) and cytosine ribonucleoside 5'-triphosphate (CTP), and for their corresponding deoxyribose nucleotides, dCDP and dCTP, to a lesser degree. Members of the NUDIX hydrolase superfamily catalyze the hydrolysis of NUcleoside DIphosphates linked to other moieties, X. Enzymes belonging to this superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and contain a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. Substrates of NUDIX hydrolases include intact and oxidatively damaged nucleoside triphosphates, dinucleoside polyphosphates, nucleotide-sugars and dinucleotide enzymes. These substrates are metabolites or cell signaling molecules that require regulation during different stages of the cell cycle or during periods of stress. In general, the role of the NUDIX hydrolase is to sanitize the nucleotide pools and to maintain cell viability, thereby serving as surveillance _ "house-cleaning" enzymes. Substrate specificity is used to define families within the superfamily. Differences in substrate specificity are determined by the N-terminal extension or by residues in variable loop regions. Mechanistically, substrate hydrolysis occurs by a nucleophilic substitution reaction, with variation in the numbers and roles of divalent cations required.

Pssm-ID: 467602 [Multi-domain] Cd Length: 121 Bit Score: 41.43 E-value: 9.53e-05

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15599596   9 AVIRGSDGRVLIARRPEDKHQgglweFP-------GGKVEDGEPVRAALARELEEELGIRVERAR 66
Cdd:cd24154   7 AFLINSQGQLWIPRRTADKRI-----FPlaldmsvGGHVSSGETYEQAFVRELQEELNLDLDQLS 66

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: 467571 Cd Length: 145 Bit Score: 40.54 E-value: 2.40e-04

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599596   5 HVAAAVIRGSDGRVLIARRPEDKH--QGGLWEFPGGKVEDGEPVRAALARELEEELGIRVE 63
Cdd:cd04689   2 HIARAIVVDDQNRFYFVVVVRDDDfgKGTLIETAGGGVEENENLEEAIRRELKEELGVEVD 62

nucleoside diphosphate-linked moiety X)) motif 16; U8 SnoRNA-decapping enzyme, also known as NUDIX (nucleoside diphosphate-linked moiety X)) motif 16/Nudt16, is encoded by the human NUDT16 gene and a RNA-binding and decapping enzyme that catalyzes the cleavage of the cap structure of snoRNAs and mRNAs in a metal-dependent manner. 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: 467581 Cd Length: 175 Bit Score: 40.80 E-value: 2.96e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 15599596  31 GLWEFPGGKVEDGEPVRAALARELEEELGIrverARPLIQVRH-DYADKHV 80
Cdd:cd18869  36 GLLGFPGGFVDTGESLEEGLNRELREELGL----AHAVFPVTEdDYRSSHV 82

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

Pssm-ID: 467536 [Multi-domain] Cd Length: 146 Bit Score: 40.30 E-value: 3.54e-04

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596  10 VIRGSDGRVLIARRpEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVerarpliqvrhdYADKHVLLDVWE--- 86
Cdd:cd03430  21 IIRNEDGEILLGKR-NNRPAQGYWFVPGGRILKNETLDDAFKRIAREELGLEV------------TINAAEFLGVYEhfy 87


                ....*..
gi 15599596  87 VDGFSGE 93
Cdd:cd03430  88 DDNFSGE 94

NUDIX hydrolase YfcD; Provisional

Pssm-ID: 185291 [Multi-domain] Cd Length: 180 Bit Score: 39.78 E-value: 6.97e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 15599596   16 GRVLIARRPEDK--HQGGLWEFPGGKVEDGEPVRAALARELEEELGIR 61
Cdd:PRK15393  49 GKILVQRRTETKdfLPGMLDATAGGVVQAGEQLLESARREAEEELGIA 96

Bdellovibrio Bacteriovorus nucleoside diphosphate sugar hydrolase, and similar proteins; Bdellovibrio bacteriovorus nucleoside diphosphate sugar (NDPS) hydrolase Bd3179 has been shown to similarities to the Escherichia coli adenosine diphosphate ribose (ADPR) hydrolase and the guanosine diphosphate mannose (GDPM) hydrolase. It may have a role when Bdellovibrio degrades and metabolizes host cell. 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: 467607 [Multi-domain] Cd Length: 173 Bit Score: 39.67 E-value: 7.22e-04

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15599596   7 AAAVIR-GSDGRVLIARRPEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVER 64
Cdd:cd24159  43 AVAVVPlLDDGRVVMERQYRYPLKRVFLEFPAGKIDPGEDTLETAKRELLEETGYEAQE 101

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: 467547 Cd Length: 147 Bit Score: 38.71 E-value: 1.16e-03

                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15599596  11 IRGSDGRVLIArrpedkHQGG---------LWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:cd04662  10 RRDGGLEVLLV------HPGGpfwarkdegAWSIPKGEVEPGEDPLAAARREFEEETGFPA 64

translation initiation factor IF-2B alpha subunit; Eukaryotic translation initiation factor 2B subunit alpha (EIF2B1) is one of five subunits of eukaryotic translation initiation factor 2B (EIF2B), a GTP exchange factor for eukaryotic initiation factor 2 and an essential regulator for protein synthesis. Mutations in this gene and the genes encoding other EIF2B subunits have been associated with leukoencephalopathy with vanishing white matter. 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: 467584 [Multi-domain] Cd Length: 129 Bit Score: 38.39 E-value: 1.28e-03

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   5 HVAAAVIRgSDGRVLIARRpEDK---HQGgLWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLIQ---VRHDYADK 78
Cdd:cd18872   1 SVVTSFLF-HDGKVLLFRR-SDKvgtYQG-RWAGISGSIESDDPPLAAAWREIREETGLTPEDVELLRQgkpFEFTDESL 77

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 15599596  79 HVLldvWEVDGFSGEAHGA-------EGQPLAWVEPRELADYE 114
Cdd:cd18872  78 GRE---WTVHPFLFRLKDDraikldwEHTEWEWVDPTDILDYE 117

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: 38.25 E-value: 1.64e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15599596   4 VHVAAAVIRGSDGRVLIARRPEDKHqgglwEFPG-------GKVEDGEPVRAALARELEEELGIRVERARPLIQVR 72
Cdd:cd03676   9 VHLNGYVRDGDGLRLWVARRSATKA-----TYPGkldnlvaGGVPAGESPLETLVREAEEEAGLPEDLARQARPAA 79

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

Pssm-ID: 467599 [Multi-domain] Cd Length: 127 Bit Score: 37.98 E-value: 1.70e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599596   8 AAVIRgsDGRVLIArrpedKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVERARpLIQVrHDYaDKH 79
Cdd:cd18889   7 AAIFK--DDKILLV-----QEKDGRWSLPGGWVDVNQSIKENTIKEAKEEAGLDVEPKR-IIAV-LDR-NKH 68

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: 38.23 E-value: 1.72e-03

                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   9 AVIRGSDGR---VLIA--RRPEDKHqggLWEFPGGKVEDGE-PVRAALaRELEEELG---IRVERARPLI 69
Cdd:cd18888   9 AILKRKLKPpelVLVKqyRPPVNAY---TIEFPAGLVDPGEsPEQAAL-RELKEETGytgEKVLSVSPPL 74

Mitochondrial ribosomal protein L46; Mitochondrial ribosomal protein L46 (MRP L46) is a component of the large subunit (39S) of the mammalian mitochondrial ribosome and a member of the NUDIX hydrolase superfamily. MRPs are thought to be involved in the maintenance of the mitochondrial DNA. In general, members of the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for activity and contain the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), which functions as a metal binding and catalytic site. MRP L46 appears to contain a modified NUDIX motif.

Pssm-ID: 467546 Cd Length: 142 Bit Score: 37.59 E-value: 2.28e-03

                        10        20        30
                ....*....|....*....|....*....|....*...
gi 15599596  26 DKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVE 63
Cdd:cd04661  37 QKKGKGPWQFPQGDVEEGETLREAAERGLRELGGDNMN 74

mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate linked moiety X))-type motif 20/Nudt20, is required for degradation of mRNAs, both in normal mRNA turnover, and in nonsense-mediated mRNA decay (NMD). Its catalytic subunit, and Dcp1p are the two components of the decapping enzyme complex. Decapping is a key step in both general and nonsense-mediated 5'->3' mRNA-decay pathways. Dcp2p contains an all-alpha helical N-terminal domain and a C-terminal domain which has the NUDIX fold. While decapping is not dependent on the N-terminus of Dcp2p, it does affect its efficiency. Dcp1p binds the N-terminal domain of Dcp2p stimulating the decapping activity of Dcp2p. Decapping permits the degradation of the transcript and is a site of numerous control inputs. It is responsible for nonsense-mediated decay as well as AU-rich element (ARE)-mediated decay. In addition, it may also play a role in the levels of mRNA. Enzymes belonging to the NUDIX hydrolase superfamily require a divalent cation, such as Mg2+ or Mn2+, for their activity and are recognized by a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V).

Pssm-ID: 467540 Cd Length: 144 Bit Score: 37.53 E-value: 3.00e-03

                        10        20
                ....*....|....*....|....*...
gi 15599596  33 WEFPGGKVEDGEPVRAALARELEEELGI 60
Cdd:cd03672  28 WGFPKGKINKDESDADCAIREVYEETGF 55

GDP-mannose mannosyl hydrolase;

Pssm-ID: 237966 [Multi-domain] Cd Length: 159 Bit Score: 37.04 E-value: 4.52e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 15599596   10 VIRGSDGRVLIARRPEDKHQGgLWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:PRK15434  23 IVENSRGEFLLGKRTNRPAQG-YWFVPGGRVQKDETLEAAFERLTMAELGLRL 74

dihydroneopterin triphosphate pyrophosphatase; Provisional

Pssm-ID: 236516 [Multi-domain] Cd Length: 148 Bit Score: 36.80 E-value: 5.22e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599596   10 VIRGSDGRVLIARRPEDKhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRVERAR-PLI------------QVRHDYA 76
Cdd:PRK09438  13 VIYTPDLGVLMLQRADDP---DFWQSVTGSLEEGETPAQTAIREVKEETGIDVLAEQlTLIdcqrsieyeifpHWRHRYA 89

Predicted NTP pyrophosphohydrolase, NUDIX family [Nucleotide transport and metabolism, General function prediction only];

Pssm-ID: 443295 [Multi-domain] Cd Length: 153 Bit Score: 36.34 E-value: 8.26e-03

                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 15599596  21 ARRPEdkhqgGLWEFPGGKVEDGEPVRAALARELEEELGIRV 62
Cdd:COG4119  31 ARKDE-----GAWSIPKGEYEPGEDPLAAARREFAEETGVPA 67

nudix hydrolase

Pssm-ID: 215184 [Multi-domain] Cd Length: 144 Bit Score: 35.99 E-value: 8.79e-03

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15599596    3 RVHVAAAVIRGSdgRVLIARRpEDKHQGGLWEFPGGKVEDGEPVRAALARELEEELGIRVER 64
Cdd:PLN02325   9 RVAVVVFLLKGN--SVLLGRR-RSSIGDSTFALPGGHLEFGESFEECAAREVKEETGLEIEK 67

ADP-ribose pyrophosphatase NudF; Provisional

Pssm-ID: 182682 [Multi-domain] Cd Length: 202 Bit Score: 36.64 E-value: 9.91e-03

                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 15599596   32 LWEFPGGKVEDGEPVRAALARELEEELGIRVERARPLI 69
Cdd:PRK10729  83 LLEMVAGMIEEGESVEDVARREAIEEAGLIVGRTKPVL 120