NCBI Conserved Domain Search

NUDIX hydrolase YfcD; Provisional

Pssm-ID: 185291 [Multi-domain] Cd Length: 180 Bit Score: 370.29 E-value: 2.99e-133

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976   2 VEQSHLASTEWVDIVSEENEVIAQASREQMRAERLRHRATYIVVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEV 81
Cdd:PRK15393   1 VEQRRLASTEWVDIVNENNEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQ 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  82 LLDSARREAEEELGIAGVPFAEHGQFYFEDENCRVWGGLFSCVSHGPFALQEEEVSEVSWMTPEEITARCDEFTPDSLKA 161
Cdd:PRK15393  81 LLESARREAEEELGIAGVPFAEHGQFYFEDENCRVWGALFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEFTPDSLKA 160

                        170
                 ....*....|.
gi 556429976 162 LALWMTRNAKN 172
Cdd:PRK15393 161 LALWLTRNAKN 171

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: 230.58 E-value: 1.76e-78

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  13 VDIVSEENEVIAQASREQMRAERLRHRATYIVVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAEE 92
Cdd:cd04697    1 VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEE 80

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556429976  93 ELGIAGVPFAEHGQFYFEDENCRVWGGLFSCVSHGPFALQEEEVSEVSWMTPEEIT--ARCDEFTPDSLKALALWM 166
Cdd:cd04697   81 ELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILqaARGEEFTPDGRVALERYL 156

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: 163.83 E-value: 4.92e-52

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  10 TEWVDIVSEENEVIAQASREQMRAERLRHRATYIVVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARRE 89
Cdd:COG1443    1 EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVRE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  90 AEEELGIAGV-PFAEHGQFYF-----EDENCRVWGGLFSCVSHGPFALQEEEVSEVSWMTPEEITARCDE----FTPDSL 159
Cdd:COG1443   81 LEEELGITVDdDLRPLGTFRYravdaNGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAgpeaFTPWFR 160


                 ..
gi 556429976 160 KA 161
Cdd:COG1443  161 LY 162

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: 96.86 E-value: 4.29e-26

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  13 VDIVSEENEVIAQASREQMRAERLRHRATYI-VVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAE 91
Cdd:cd04692    1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVwLVNPEEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELE 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556429976  92 EELGIAgVPFAE-----------HGQFYFEDENCRVwgglFSCVSHGP---FALQEEEVSEVSWMTP 144
Cdd:cd04692   81 EELGLT-VSPEDliflgvireevIGGDFIDNEFVHV----YLYETDRPleeFKLQPEEVAGVVFVDL 142

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: 75.26 E-value: 1.32e-17

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVH----DGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAEEELGIAgVPFAE-------HGQFYFED 111
Cdd:cd04693   30 LVVHvwifNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLEAAIRELKEELGID-LDADElrpiltiRFDNGFDD 108

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 556429976 112 encrVWggLFSC-VSHGPFALQEEEVSEVSWMTPEEITARCDE 153
Cdd:cd04693  109 ----IY--LFRKdVDIEDLTLQKEEVQDVKWVTLEEILEMIES 145

Nudix hydrolase homolog

Pssm-ID: 215425 [Multi-domain] Cd Length: 770 Bit Score: 67.54 E-value: 1.71e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  38 HRATYIVVH-DGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAEEELGIAGVPFAEHGQFYFEDEnCRV 116
Cdd:PLN02791  32 HRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLSAQRELEEELGIILPKDAFELLFVFLQE-CVI 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 556429976 117 WGG-----------LFSCVSHGP---FALQEEEVSEVSWMTPEE 146
Cdd:PLN02791 111 NDGkfinneyndvyLVTTLDPIPleaFTLQESEVSAVKYMSIEE 154

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: 62.81 E-value: 3.09e-13

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  39 RATYIVVHDGMGKILVQRRTDTKDflPGMLDaTAGGVVQADEVLLDSARREAEEELGIAGVPFAEHGQFYFEDENCRVWG 118
Cdd:cd02883    1 VAVGAVVFDDEGRVLLVRRSDGPG--PGGWE-LPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHV 77

                         90       100
                 ....*....|....*....|....*....
gi 556429976 119 GLF----SCVSHGPFALQEEEVSEVSWMT 143
Cdd:cd02883   78 VVLvflaRVVGGEPPPLDDEEISEVRWVP 106

NUDIX domain;

Pssm-ID: 395229 [Multi-domain] Cd Length: 132 Bit Score: 62.50 E-value: 7.08e-13

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976   36 LRHRATYIVVHDGMGKILVQRRTdtKDFLPGMLdATAGGVVQADEVLLDSARREAEEELGIAGV------PFAEHGQFYF 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRS--KKPFPGWW-SLPGGKVEPGETPEEAARRELEEETGLEPEllellgSLHYLAPFDG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 556429976  110 EDENCRVWGGLFSCVSHGPFALQ-EEEVSEVSWMTPEEI 147
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDpDGEVEEVRWVPLEEL 116

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: 60.20 E-value: 7.94e-12

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  13 VDIVSEENEVIAQASREQM-RAERLRHRATYIVVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAE 91
Cdd:cd02885    2 VILVDEDDNPIGTAEKLEAhRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRLR 81

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 556429976  92 EELGIAGVPFAEHGQF-Y--------FEDENCRVwgglFSCVSHGPFALQEEEVSEVSWMTPEEI----TARCDEFTP 156
Cdd:cd02885   82 EELGIPVCDLEELPRFrYratddnglVEHEIDHV----FVGRADGDPVPNPEEVSDYRWVSLEELrellAATPEAFTP 155

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

Pssm-ID: 467602 [Multi-domain] Cd Length: 121 Bit Score: 55.30 E-value: 2.29e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  50 GKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAEEELGIagvpfaehgqfYFEDENCRVWgGLFSCVSHGPF 129
Cdd:cd24154   14 GQLWIPRRTADKRIFPLALDMSVGGHVSSGETYEQAFVRELQEELNL-----------DLDQLSYRVL-GKLTPYEHGVS 81

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556429976 130 A------LQEEEV--------SEVSWMTPEEITAR 150
Cdd:cd24154   82 AfmkvyeIRSDETpdynpddfSEAFWLTPEELLKR 116

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: 55.81 E-value: 2.63e-10

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  27 SREQMRAERLRHRATYIVVHDGMGKILVQRRTDTKdFLPGMLDATAGGVvQADEVLLDSARREAEEELGIAGVPFAEHGQ 106
Cdd:COG0494    2 TEILSSEPEHYRPAVVVVLLDDDGRVLLVRRYRYG-VGPGLWEFPGGKI-EPGESPEEAALRELREETGLTAEDLELLGE 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556429976 107 FY---FEDENCRVWGGLFSCVSHGPFALQEEEVSEVSWMTPEEITARCDEFT-PDSLKALALWM 166
Cdd:COG0494   80 LPspgYTDEKVHVFLARGLGPGEEVGLDDEDEFIEVRWVPLDEALALVTAGEiAKTLAALARLL 143

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

Pssm-ID: 440671 [Multi-domain] Cd Length: 125 Bit Score: 53.44 E-value: 1.26e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  34 ERLRHRATYIVVHDGMGKILVQRRTDtkDFLPGMLdATAGGVVQADEVLLDSARREAEEELGIAGVPFAEHGQFYFEDEN 113
Cdd:COG1051    2 TKVPKVAVDAVIFRKDGRVLLVRRAD--EPGKGLW-ALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPDRG 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556429976 114 CRVwGGLFSCVSHGPFALQEEEVSEVSWMTPEEITArcDEFTPDSLKALA 163
Cdd:COG1051   79 HVV-SVAFLAEVLSGEPRADDEIDEARWFPLDELPE--LAFTPADHEILE 125

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: 54.04 E-value: 1.62e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  44 VVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSARREAEEELGIA------GVPFAEHGQFYFEDENcrvw 117
Cdd:cd03676   15 VRDGDGLRLWVARRSATKATYPGKLDNLVAGGVPAGESPLETLVREAEEEAGLPedlarqARPAAGRVSYFYRSDE---- 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 556429976 118 GGLFSCVSHgPFAL----------QEEEVSEVSWMTPEEITA--RCDEFTPDSlkALAL 164
Cdd:cd03676   91 GGLQPEVLY-VYDLelpedfvpkpQDGEVESFELMSVDEVLEalRAGEFKPNC--ALVM 146

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: 52.57 E-value: 4.03e-09

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  50 GKILVQRRTdtKDFLPGMLDaTAGGVVQADEVLLDSARREAEEELGIAgvpfAEHGQFYFEDENCRVWGGL--------F 121
Cdd:cd04681   17 GEILFVRRA--KEPGKGKLD-LPGGFVDPGESAEEALRRELREELGLK----IPKLRYLCSLPNTYLYKGItyktcdlfF 89

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556429976 122 SCVSHGPFAL--QEEEVSEVSWMTPEEItaRCDEFTPDSL-KALALWM 166
Cdd:cd04681   90 TAELDEKPKLkkAEDEVAELEWLDLEEI--EPEKLAFPSIrKAVERYI 135

isopentenyl-diphosphate Delta-isomerase;

Pssm-ID: 235156 [Multi-domain] Cd Length: 184 Bit Score: 52.28 E-value: 1.12e-08

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976   8 ASTEWVDIVSEENEVIAQASREQM-RAERLRHRATYIVVHDGMGKILVQRRTDTKDFLPGMLDATAGGVVQADEVLLDSA 86
Cdd:PRK03759   3 METELVVLLDEQGVPTGTAEKAAAhTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  87 RREAEEELGIAGVPFA-EHGQFYF---------EDENCRVWGGLFScvshGPFALQEEEVSEVSWMTPEEITARCD---- 152
Cdd:PRK03759  83 IRRCREELGVEITDLElVLPDFRYratdpngivENEVCPVFAARVT----SALQPNPDEVMDYQWVDPADLLRAVDatpw 158


                 ....
gi 556429976 153 EFTP 156
Cdd:PRK03759 159 AFSP 162

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

Pssm-ID: 467588 [Multi-domain] Cd Length: 121 Bit Score: 47.20 E-value: 2.48e-07

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  40 ATYIVVHDGMGKILVQRRTDTKDF-LPGmldatagGVVQADEVLLDSARREAEEELGI--------------AGVPFAEH 104
Cdd:cd18876    2 AAGALFTDAAGRVLLVKPTYKDGWeLPG-------GVVEAGESPLQAARREVREELGLdvpvgrllavdwvpPAGGGDDA 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 556429976 105 GQFYFEdencrvwGGLFSCVSHGPFALQEEEVSEVSWMTPEEITAR 150
Cdd:cd18876   75 VLFVFD-------GGVLTPEQAAAIRLQDEELSAYRFVTPEEAAEL 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: 467560 [Multi-domain] Cd Length: 137 Bit Score: 43.66 E-value: 7.43e-06

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 556429976  43 IVVHDGMGKILVQRRTDTKDF-LPgmldataGGVVQADEVLLDSARREAEEELGI 96
Cdd:cd04677   17 VIILNEQGRILLQKRTDTGDWgLP-------GGAMELGESLEETARREVFEETGL 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: 467593 [Multi-domain] Cd Length: 130 Bit Score: 43.40 E-value: 7.90e-06

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  38 HRATYIVVHDGMGKILVQRRTDTKDFL-PGMLdATAGGVVQADEVLLDSARREAEEELG--IAGVPFAEHGQFYFEDENC 114
Cdd:cd18882    1 HEVAIAILYDDRGKVLLQLRDDKPGIPyPGYW-GLFGGHLEPGETPEEAIRRELEEEIGyePGEFRFFLLYTEDDGEDRI 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 556429976 115 RVwgglfscVSHGPFALQEEEVS-----EVSWMTPEEITARcdEFTPDSLKALALWM 166
Cdd:cd18882   80 RH-------VFHAPLDVDLSDLVlnegqALRLFSPEEILQG--PLYSNLAGILRPLL 127

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: 42.27 E-value: 1.57e-05

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 556429976  38 HRATYIVVHDGmgKILVQRRTDTKDFLPGmldatagGVVQADEVLLDSARREAEEELGIAG 98
Cdd:cd04667    1 RRATVICRRGD--RILLVARRGGRWLLPG-------GKIEPGESPLEAAIRELKEETGLAA 52

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: 41.86 E-value: 2.55e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  73 GGVVQADEVLLDSARREAEEELGIAGVPFAEHGQFYF----EDENCRVWGG---------LFsCVSHGPFALQEEEVSEV 139
Cdd:cd03674   31 GGHVEPDEDPLEAALREAREETGLDVELLSPLSPDPLdidvHPIPANPGEPahlhldvryLA-VADGDEALRKSDESSDV 109

                         90
                 ....*....|
gi 556429976 140 SWMTPEEITA 149
Cdd:cd03674  110 RWFPLDELEE 119

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: 41.52 E-value: 3.46e-05

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDGmgKILVQRRT----DTKDFLPGmldatagGVVQADEVLLDSARREAEEELGIAGVPFAEHG-QFYFEDENCRVW 117
Cdd:cd04691    7 VVVKEG--KVLLVKRAygpgKGRWTLPG-------GFVEEGETLDEAIVREVLEETGIDAKPVGIIGvRSGVIRDGKSDN 77

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 556429976 118 GGLFSC--VSHGPFAlQEEEVSEVSWMTPEEITAR 150
Cdd:cd04691   78 YVVFLLeyVGGEPKP-DERENSEAGFLTLEEALAN 111

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

Pssm-ID: 467587 [Multi-domain] Cd Length: 144 Bit Score: 40.63 E-value: 1.08e-04

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 556429976  44 VVHDGMGKILVQRRTdtKDFLPGMldaTA-GGVVQADEVLLDSARREAEEELGI 96
Cdd:cd18875    8 MIYDGEDRVLVLDRV--KKDWGGY---TFpGGHVEPGESFVDSVIREVKEETGL 56

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: 40.15 E-value: 1.36e-04

                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  37 RHRATYIVVHDGMGKILVQRRTDtKDFLPGMLDATAGGVVQADEVLLDSARREAEEELGI 96
Cdd:cd04689    1 RHIARAIVVDDQNRFYFVVVVRD-DDFGKGTLIETAGGGVEENENLEEAIRRELKEELGV 59

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: 39.80 E-value: 1.51e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  73 GGVVQADEVLLDSARREAEEELGIAGVPFAEHGQFY----FEDENCRvwggLFS---CVSHGPFALQEEEVSEVSWMTPE 145
Cdd:cd03424   35 AGKIDPGEDPEEAARRELEEETGYTAGDLELLGSFYpspgFSDERIH----LFLaedLTPVSEQALDEDEFIEVVLVPLE 110

                         90       100
                 ....*....|....*....|.
gi 556429976 146 EITARCDEFTPDSLKALALWM 166
Cdd:cd03424  111 EALEMIEDGEITDAKTLAALL 131

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: 39.05 E-value: 3.49e-04

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 556429976  73 GGVVQADEVLLDSARREAEEELGIAGVPFAEHG--QFYFEDEN 113
Cdd:cd03427   33 GGKVEPGETIEEAAVRELEEEAGLTATELEKVGrlKFEFPDDP 75

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: 38.54 E-value: 4.55e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  25 QASREQMRAERLRHRATYIVVHDGMGKILVQRRTDTKDF-LPgmldataGGVVQADEVLLDSARREAEEELGIAGVPFAE 103
Cdd:cd04676    4 KNLRAKIGNELLFTPSVAAVILNEDGRILLQRKGGLGLWsLP-------AGAIEPGEHPAEAVIREVREETGLLVKPTRL 76

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 556429976 104 HGQFYFEDENCRVWGG--------LFSC-VSHGPFALQEEEVSEVSWMTPEE 146
Cdd:cd04676   77 LGVFGGKEFRYTYPNGdqveytviAFKCvVTGGTLNAIDGETSELRYFSRTQ 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: 467572 [Multi-domain] Cd Length: 123 Bit Score: 37.90 E-value: 7.56e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  37 RHRATYIVVHDGmgKILVQRRTDTKDFlpgMLdatAGGVVQADEVLLDSARREAEEELGIAGVPFAEH--GQF----YFE 110
Cdd:cd04690    1 IVKAAVIIIKDG--RLLLVRKRGTDAF---YL---PGGKREPGETPLQALVRELKEELGLDLDPDSLRflGTFeapaANE 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 556429976 111 DEnCRVWGGLFSCVSHGPFALQeEEVSEVSWMTPEEITAR 150
Cdd:cd04690   73 PG-TTVRMTCFTADYDGEPQPA-AEIEELRWLDPADPDDD 110

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: 37.51 E-value: 8.09e-04

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  37 RHRATYIVVHDGmgKIL-VQRRTDTKDF--LPGmldataGGVvQADEVLLDSARREAEEELGIAGVP--------FAEHG 105
Cdd:cd18880    1 RIRAKAIIIEDG--KLLlVKHRDEGGIFyiLPG------GGQ-EHGETLPEALKRECLEETGLDVEVgdllfvreYIGPN 71

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 556429976 106 Q------FYFEdenCRVWGGLFSCVShgpfaLQEEEVSEVSWMTPEEI 147
Cdd:cd18880   72 KpvhqveLFFL---CTLEGGELTLGS-----DPDLNQVGVEWIPLEEL 111

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: 37.52 E-value: 1.01e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDgMGKIL-VQRRTDTKDF--LPGmldatagGVVQADEVLLDSARREAEEELGIA-------GVPFAEHGQF----- 107
Cdd:cd04670    8 LVINE-NNEVLvVQEKYGGPGGwkLPG-------GLVDPGEDIGEAAVREVFEETGIDtefvsilGFRHQHPGRFgksdl 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 556429976 108 YFEdenCRVwgglfSCVSHGPFALQEEEVSEVSWMTPEEITA 149
Cdd:cd04670   80 YFV---CRL-----RPLSDEEIKICPEEIAEAKWMPLEEYLK 113

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: 37.53 E-value: 1.02e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  74 GVVQADEVLLDSARREAEEELGIAGVPFAEHGQ----FYFEDENC--RVWGGLFSCVSHGPFALQEEEVSEVSWMTPEEI 147
Cdd:cd03673   34 GKLEPGETPEEAAVREVEEETGLRVRLGRPLGTtrytYTRKGKGIlkKVHYWLMRALGGEFLPQPEEEIDEVRWLPPDEA 113


                 ...
gi 556429976 148 TAR 150
Cdd:cd03673  114 RRL 116

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: 36.83 E-value: 1.79e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  42 YIVVHDGMGKILVQRRTDTKDFLPGmldataGGvVQADEVLLDSARREAEEELGIAGVPFAEHGQF--YFEDENCRVW-- 117
Cdd:cd04684   19 YAVIFNDEGKVLLVQTPNGGYFLPG------GG-IEPGETPEEALHREVLEETGWEIEIGEFLGNAsrYFYSPDYDRYyl 91

                         90       100       110
                 ....*....|....*....|....*....|.
gi 556429976 118 --GGLFSCVSHGPFALQEEEVSEVSWMTPEE 146
Cdd:cd04684   92 niGYFYLAELVRKVSEPTEEDHELVWLPPEE 122

Nudix family hydrolase;

Pssm-ID: 236361 [Multi-domain] Cd Length: 312 Bit Score: 37.55 E-value: 2.83e-03

                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 556429976  44 VVHDGMGKILVQRRTDTKDF-----LPGmldatagGVVQADEVLLDSARREAEEELGI 96
Cdd:PRK08999  11 VIRDADGRILLARRPEGKHQgglweFPG-------GKVEPGETVEQALARELQEELGI 61

GDP-mannose mannosyl hydrolase;

Pssm-ID: 237966 [Multi-domain] Cd Length: 159 Bit Score: 36.66 E-value: 2.93e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDGMGKILVQRRTDTKD----FLPGmldatagGVVQADEVLLDSARREAEEELGIAgVPFAEhGQFY-----FEDEN 113
Cdd:PRK15434  22 FIVENSRGEFLLGKRTNRPAqgywFVPG-------GRVQKDETLEAAFERLTMAELGLR-LPITA-GQFYgvwqhFYDDN 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556429976 114 CRvwGGLFSC----------VSHGPFALQEEEVSEVSWMTPEEITArCDE 153
Cdd:PRK15434  93 FS--GTDFTThyvvlgfrlrVAEEDLLLPDEQHDDYRWLTPDALLA-SDN 139

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: 36.06 E-value: 3.18e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDGmgKILVQRRTDTKdflPGMLDaTAGGVVQADEVLLDSARREAEEELGI---AGVPFaeHGQFYFEDENCRVWGG 119
Cdd:cd04699    8 VIFDNG--RVLLLRRSRAG---AGEWE-LPGGRLEPGESPEEALKREVKEETGLdvsVGELL--DTWTFELDPDKGVFIV 79

                         90       100
                 ....*....|....*....|....*....
gi 556429976 120 LFSC-VSHGPFALQEEEvSEVSWMTPEEI 147
Cdd:cd04699   80 TYLCrLVGGEVTLSDEH-EEYEWVTPEEL 107

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: 35.89 E-value: 3.66e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDGmgKILVQRRTDTKDF-----LPGmldatagGVVQADEVLLDSARREAEEELGIAgvpfAEHGQFYFEDE----- 112
Cdd:cd03425    7 IIVDDG--RVLIAQRPEGKHLaglweFPG-------GKVEPGETPEQALVRELREELGIE----VEVGEPLGTVEhdypd 73

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 556429976 113 --------NCRVWGGLFSCVSHgpfalqeeevSEVSWMTPEEI 147
Cdd:cd03425   74 fhvrlhvyLCTLWSGEPQLLEH----------QELRWVTPEEL 106

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: 36.02 E-value: 4.55e-03

                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 556429976  73 GGVVQADEVLLDSARREAEEELG-IAGVPFAEHGQF 107
Cdd:cd04662   39 KGEVEPGEDPLAAARREFEEETGfPAPGPFIPLGEV 74

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: 35.54 E-value: 4.56e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IV-VHDGMGKILVQRRtdtKDFLPGMLDATAGgVVQADEVLLDSARREAEEELGIagvpfaehgqfyfEDENCRVWG--- 118
Cdd:cd03429    5 IVlVTNGEDKILLARQ---PRWPPGRYSLLAG-FVEPGETLEEAVRREVKEEVGL-------------RVKNVRYVGsqp 67

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 556429976 119 ---------GLFSCVSHGPFALQEEEVSEVSWMTPEEITARCDEFTPDSL 159
Cdd:cd03429   68 wpfpsslmlGFTAEADSGEITVDDDELEDARWFSRDELPEALFLPPPGSI 117

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: 35.68 E-value: 4.80e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  43 IVVHDGMGKILVQRRTD--TKD--FLPGmldatagGVVQADEVLLDSARREAEEELGIA----GVPF---AEHgqFYfeD 111
Cdd:cd03430   20 LIIRNEDGEILLGKRNNrpAQGywFVPG-------GRILKNETLDDAFKRIAREELGLEvtinAAEFlgvYEH--FY--D 88

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 556429976 112 ENcrVWGGLFSC----------VSHGPFALQEEEVSEVSWMTPEEITAR 150
Cdd:cd03430   89 DN--FSGEDFSThyvvlayrlkLDEGLLLLPDDQHDEYRWFTIDELLAN 135

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: 35.69 E-value: 5.10e-03

                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556429976  42 YIVVHDGMGKILVQRRTDTKDFLpgmlDATAGGVvQADEVLLDSARREAEEELGIAGVPF---AEHGQFYFEDEnCRVWG 118
Cdd:cd04664    6 VIYRKDEEGEVLLLKRTDDGGFW----QSVTGGI-EDGETPWQAALRELKEETGLDPLELqliDLNVSNFYEIF-DDWRP 79

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 556429976 119 GLFSCVSHGpFALQEEEVSEV---------SWMTPEEITARC 151
Cdd:cd04664   80 GVTVNTEHV-FAVEVPEEQPIrlspehtdyRWLPYEEAAELL 120

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: 35.27 E-value: 6.91e-03

                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 556429976  50 GKILVQRRTDTkDFLPGMLDATAGGVvQADEVLLDSARREAEEELGI 96
Cdd:cd04683   11 DEVLLLRRANT-GYDDGWWHLPAGHV-EAGETVRAAAVREAKEELGV 55