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Conserved domains on  [gi|1871972815|ref|WP_179993307|]
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MULTISPECIES: NUDIX domain-containing protein [Acinetobacter]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
PRK08999 super family cl35755
Nudix family hydrolase;
6-297 1.97e-65

Nudix family hydrolase;


The actual alignment was detected with superfamily member PRK08999:

Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 207.42  E-value: 1.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFH-QTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLH 84
Cdd:PRK08999    5 IHVAAGVIRDaDGRILLARRPEGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIEVTAARPLITVRHDYPDKRVRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  85 IFHASV---QPEQLAGikQPWRWYSRDELSELNFPKANQAMIQKLQWPRKIKISED--------LSHLNN-LETD-QMLY 151
Cdd:PRK08999   85 VRRVTAwqgEPHGREG--QPLAWVAPDELAVYPFPPANQPIVRALRLPDTYLITPEgedgdaafLARLERaLAAGiRLIQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 152 WRVMA-SPEH----ISQLQQIPVDQLSRLIINqelwSQLNELQQQTIRTLHLKQSQLMQLQKGELAGGYRYLAACHDLEA 226
Cdd:PRK08999  163 LRAPQlPPAAyralARAALGLCRRAGAQLLLN----GDPELAEDLGADGVHLTSAQLAALAARPLPAGRWVAASCHDAEE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1871972815 227 LKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFALGGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:PRK08999  239 LARAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVPLPVYALGGLGPGDLEEAREHGAQGIAGIR 309
 
Name Accession Description Interval E-value
PRK08999 PRK08999
Nudix family hydrolase;
6-297 1.97e-65

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 207.42  E-value: 1.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFH-QTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLH 84
Cdd:PRK08999    5 IHVAAGVIRDaDGRILLARRPEGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIEVTAARPLITVRHDYPDKRVRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  85 IFHASV---QPEQLAGikQPWRWYSRDELSELNFPKANQAMIQKLQWPRKIKISED--------LSHLNN-LETD-QMLY 151
Cdd:PRK08999   85 VRRVTAwqgEPHGREG--QPLAWVAPDELAVYPFPPANQPIVRALRLPDTYLITPEgedgdaafLARLERaLAAGiRLIQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 152 WRVMA-SPEH----ISQLQQIPVDQLSRLIINqelwSQLNELQQQTIRTLHLKQSQLMQLQKGELAGGYRYLAACHDLEA 226
Cdd:PRK08999  163 LRAPQlPPAAyralARAALGLCRRAGAQLLLN----GDPELAEDLGADGVHLTSAQLAALAARPLPAGRWVAASCHDAEE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1871972815 227 LKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFALGGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:PRK08999  239 LARAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVPLPVYALGGLGPGDLEEAREHGAQGIAGIR 309
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
6-127 1.65e-36

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: 126.80  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLHI 85
Cdd:cd03425     1 IEVVAAIIVDDGRVLIAQRPEGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIEVEVGEPLGTVEHDYPDFHVRLHV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1871972815  86 FHASV---QPEQLAGikQPWRWYSRDELSELNFPKANQAMIQKLQ 127
Cdd:cd03425    81 YLCTLwsgEPQLLEH--QELRWVTPEELDDLDWLPADIPIVEALL 123
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
1-124 3.68e-24

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 94.66  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   1 MSKTTIHVAIAILFH-QTQVLVGWREAKQHQGnKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDV 79
Cdd:COG1051     1 MTKVPKVAVDAVIFRkDGRVLLVRRADEPGKG-LWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPDRGH 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  80 IVnLHIFHASVQPEQLAGIK--QPWRWYSRDELSELNFPKANQAMIQ 124
Cdd:COG1051    80 VV-SVAFLAEVLSGEPRADDeiDEARWFPLDELPELAFTPADHEILE 125
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
196-297 5.05e-20

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: 85.29  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 196 LHLKQSQLMQLQKGELAGGYRYL-AACHDLEALKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFAL 274
Cdd:pfam02581  76 VHLGQDDLPVAEARELLGPDLIIgVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVEIPVVAI 155
                          90       100
                  ....*....|....*....|...
gi 1871972815 275 GGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:pfam02581 156 GGITPENVPEVIEAGADGVAVVS 178
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
2-126 4.38e-13

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: 64.89  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   2 SKTTIHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIV 81
Cdd:TIGR00586   1 KKLQQIAVGIIRNENGEIIITRRADGHMFAKLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKLEYEFYPRHIT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1871972815  82 NLHIFHASVQPEQLAGIKQPWRWYSRDELSELNFPKANQAMIQKL 126
Cdd:TIGR00586  81 LWFWLLERWEGGPPGKEGQPEEWWVLVGLLADDFFPAANPVIIKL 125
 
Name Accession Description Interval E-value
PRK08999 PRK08999
Nudix family hydrolase;
6-297 1.97e-65

Nudix family hydrolase;


Pssm-ID: 236361 [Multi-domain]  Cd Length: 312  Bit Score: 207.42  E-value: 1.97e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFH-QTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLH 84
Cdd:PRK08999    5 IHVAAGVIRDaDGRILLARRPEGKHQGGLWEFPGGKVEPGETVEQALARELQEELGIEVTAARPLITVRHDYPDKRVRLD 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  85 IFHASV---QPEQLAGikQPWRWYSRDELSELNFPKANQAMIQKLQWPRKIKISED--------LSHLNN-LETD-QMLY 151
Cdd:PRK08999   85 VRRVTAwqgEPHGREG--QPLAWVAPDELAVYPFPPANQPIVRALRLPDTYLITPEgedgdaafLARLERaLAAGiRLIQ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 152 WRVMA-SPEH----ISQLQQIPVDQLSRLIINqelwSQLNELQQQTIRTLHLKQSQLMQLQKGELAGGYRYLAACHDLEA 226
Cdd:PRK08999  163 LRAPQlPPAAyralARAALGLCRRAGAQLLLN----GDPELAEDLGADGVHLTSAQLAALAARPLPAGRWVAASCHDAEE 238
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1871972815 227 LKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFALGGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:PRK08999  239 LARAQRLGVDFAVLSPVQPTASHPGAAPLGWEGFAALIAGVPLPVYALGGLGPGDLEEAREHGAQGIAGIR 309
NUDIX_MutT_NudA_like cd03425
MutT pyrophosphohydrolase; The MutT pyrophosphohydrolase is a prototypical NUDIX hydrolase ...
6-127 1.65e-36

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: 126.80  E-value: 1.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLHI 85
Cdd:cd03425     1 IEVVAAIIVDDGRVLIAQRPEGKHLAGLWEFPGGKVEPGETPEQALVRELREELGIEVEVGEPLGTVEHDYPDFHVRLHV 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1871972815  86 FHASV---QPEQLAGikQPWRWYSRDELSELNFPKANQAMIQKLQ 127
Cdd:cd03425    81 YLCTLwsgEPQLLEH--QELRWVTPEELDDLDWLPADIPIVEALL 123
PRK10776 PRK10776
8-oxo-dGTP diphosphatase MutT;
3-127 6.05e-25

8-oxo-dGTP diphosphatase MutT;


Pssm-ID: 182721 [Multi-domain]  Cd Length: 129  Bit Score: 96.98  E-value: 6.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   3 KTTIHVAIAILFH-QTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIV 81
Cdd:PRK10776    1 MKKLQIAVGIIRNpNNEIFITRRAADAHMAGKWEFPGGKIEAGETPEQALIRELQEEVGITVQHATLFEKLEYEFPDRHI 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  82 NLHIFHA-SVQPEQLAGIKQPWRWYSRDELSELNFPKANQAMIQKLQ 127
Cdd:PRK10776   81 TLWFWLVeSWEGEPWGKEGQPGRWVSQVALNADEFPPANEPIIAKLK 127
YjhB COG1051
ADP-ribose pyrophosphatase YjhB, NUDIX family [Nucleotide transport and metabolism];
1-124 3.68e-24

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


Pssm-ID: 440671 [Multi-domain]  Cd Length: 125  Bit Score: 94.66  E-value: 3.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   1 MSKTTIHVAIAILFH-QTQVLVGWREAKQHQGnKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDV 79
Cdd:COG1051     1 MTKVPKVAVDAVIFRkDGRVLLVRRADEPGKG-LWALPGGKVEPGETPEEAALRELREETGLEVEVLELLGVFDHPDRGH 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  80 IVnLHIFHASVQPEQLAGIK--QPWRWYSRDELSELNFPKANQAMIQ 124
Cdd:COG1051    80 VV-SVAFLAEVLSGEPRADDeiDEARWFPLDELPELAFTPADHEILE 125
ThiE COG0352
Thiamine monophosphate synthase [Coenzyme transport and metabolism]; Thiamine monophosphate ...
196-299 1.28e-22

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: 92.94  E-value: 1.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 196 LHLKQSQLMQLQKGELAGGYRYL-AACHDLEALKHAENIGCEAALLSPVLATETHPDT-AALGWEKFKQMAEQVQIPVFA 273
Cdd:COG0352    81 VHLGQEDLPVAEARALLGPDLIIgVSCHSLEEALRAEEAGADYVGFGPVFPTPTKPGApPPLGLEGLAWWAELVEIPVVA 160
                          90       100
                  ....*....|....*....|....*.
gi 1871972815 274 LGGIKAEDLDHAQNQHAYGIAGIRYV 299
Cdd:COG0352   161 IGGITPENAAEVLAAGADGVAVISAI 186
TMP-TENI pfam02581
Thiamine monophosphate synthase; Thiamine monophosphate synthase (TMP) (EC:2.5.1.3) catalyzes ...
196-297 5.05e-20

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: 85.29  E-value: 5.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 196 LHLKQSQLMQLQKGELAGGYRYL-AACHDLEALKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFAL 274
Cdd:pfam02581  76 VHLGQDDLPVAEARELLGPDLIIgVSTHTLEEALEAEALGADYIGFGPIFPTPTKPDAPPLGLEGLKAIAEAVEIPVVAI 155
                          90       100
                  ....*....|....*....|...
gi 1871972815 275 GGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:pfam02581 156 GGITPENVPEVIEAGADGVAVVS 178
NUDIX_4 pfam14815
NUDIX domain;
8-125 2.92e-19

NUDIX domain;


Pssm-ID: 464330 [Multi-domain]  Cd Length: 114  Bit Score: 81.21  E-value: 2.92e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRRevIEEVGIDIEQWQAFDfISHEYEDVIVNLHIFH 87
Cdd:pfam14815   1 AVLVIRNGDGRVLLRKRPEKGLLGGLWEFPGGKVEPGETLEEALAR--LEELGIEVEVLEPGT-VKHVFTHFRLTLHVYL 77
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1871972815  88 ASVQPEQlAGIKQPWRWYSRDELSELNFPKANQAMIQK 125
Cdd:pfam14815  78 VREVEGE-EEPQQELRWVTPEELDKYALPAAVRKILEA 114
MutT COG0494
8-oxo-dGTP pyrophosphatase MutT and related house-cleaning NTP pyrophosphohydrolases, NUDIX ...
8-127 3.63e-18

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: 79.31  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQ-AFDFISHEYEDVIVnlHIF 86
Cdd:COG0494    16 VVVVLLDDDGRVLLVRRYRYGVGPGLWEFPGGKIEPGESPEEAALRELREETGLTAEDLElLGELPSPGYTDEKV--HVF 93
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  87 HA-SVQPEQLAGIKQP-----WRWYSRDELSELNFPKANQAMIQKLQ 127
Cdd:COG0494    94 LArGLGPGEEVGLDDEdefieVRWVPLDEALALVTAGEIAKTLAALA 140
NUDIX pfam00293
NUDIX domain;
7-126 4.20e-17

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 75.98  E-value: 4.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   7 HVAIAILFH--QTQVLVGWReAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVN-- 82
Cdd:pfam00293   3 RVAVGVVLLneKGRVLLVRR-SKKPFPGWWSLPGGKVEPGETPEEAARRELEEETGLEPELLELLGSLHYLAPFDGRFpd 81
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1871972815  83 ----LHIFHASVQPEQLAGIK---QPWRWYSRDELSELNFPKANQAMIQKL 126
Cdd:pfam00293  82 eheiLYVFLAEVEGELEPDPDgevEEVRWVPLEELLLLKLAPGDRKLLPWL 132
NUDIX_Hydrolase cd02883
NUDIX hydrolase superfamily; NUDIX hydrolase is a superfamily of enzymes found in all three ...
7-106 3.52e-15

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: 70.13  E-value: 3.52e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   7 HVAIAILFH-QTQVLVGWReAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVN--L 83
Cdd:cd02883     1 VAVGAVVFDdEGRVLLVRR-SDGPGPGGWELPGGGVEPGETPEEAAVREVREETGLDVEVLRLLGVYEFPDPDEGRHvvV 79
                          90       100
                  ....*....|....*....|....*..
gi 1871972815  84 HIFHASVQPEQLAGIK----QPWRWYS 106
Cdd:cd02883    80 LVFLARVVGGEPPPLDdeeiSEVRWVP 106
mutt TIGR00586
mutator mutT protein; All proteins in this family for which functions are known are involved ...
2-126 4.38e-13

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: 64.89  E-value: 4.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   2 SKTTIHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIV 81
Cdd:TIGR00586   1 KKLQQIAVGIIRNENGEIIITRRADGHMFAKLLEFPGGKEEGGETPEQAVVRELEEEIGIPQHFSEFEKLEYEFYPRHIT 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1871972815  82 NLHIFHASVQPEQLAGIKQPWRWYSRDELSELNFPKANQAMIQKL 126
Cdd:TIGR00586  81 LWFWLLERWEGGPPGKEGQPEEWWVLVGLLADDFFPAANPVIIKL 125
TMP_TenI cd00564
Thiamine monophosphate synthase (TMP synthase)/TenI. TMP synthase catalyzes an important step ...
196-299 5.77e-13

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: 66.39  E-value: 5.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 196 LHLKQSQLMQLQKGELAGGYRYL-AACHDLEALKHAENIGCEAALLSPVLATETHPDT-AALGWEKFKQMAEQVQIPVFA 273
Cdd:cd00564    76 VHLGQDDLPVAEARALLGPDLIIgVSTHSLEEALRAEELGADYVGFGPVFPTPTKPGAgPPLGLELLREIAELVEIPVVA 155
                          90       100
                  ....*....|....*....|....*.
gi 1871972815 274 LGGIKAEDLDHAQNQHAYGIAGIRYV 299
Cdd:cd00564   156 IGGITPENAAEVLAAGADGVAVISAI 181
NUDIX_MTH2_Nudt15 cd04678
MutT homolog 2; MutT Homolog 2 (MTH2; EC 3.6.1.9), also known as NUDIX (nucleoside ...
8-114 7.29e-13

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: 64.12  E-value: 7.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGWReAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISheyeDVIV--NLH- 84
Cdd:cd04678     5 VGVIVLNDDGKVLLGRR-KGSHGAGTWALPGGHLEFGESFEECAAREVLEETGLEIRNVRFLTVTN----DVFEeeGKHy 79
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1871972815  85 --IFH-ASVQPEQLAGIKQP-----WRWYSRDELSELN 114
Cdd:cd04678    80 vtIFVlAEVDDGEPEENMEPdkcegWEWFSWDELPPLR 117
NUDIX_Hydrolase cd18876
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
35-116 3.18e-12

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: 62.22  E-value: 3.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  35 EFPGGKVEQGELPIEACRREVIEEVGIDIE--QWQAFDFISHEYEDVIVNLHIFHASV-QPEQLAGIKQP------WRWY 105
Cdd:cd18876    26 ELPGGVVEAGESPLQAARREVREELGLDVPvgRLLAVDWVPPAGGGDDAVLFVFDGGVlTPEQAAAIRLQdeelsaYRFV 105
                          90
                  ....*....|.
gi 1871972815 106 SRDELSELNFP 116
Cdd:cd18876   106 TPEEAAELLPP 116
NUDIX_Hydrolase cd18882
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-110 1.60e-11

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: 60.73  E-value: 1.60e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILF-HQTQVLVGWREAKQH--QGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIeqwQAFDFIsHEYEDVIVN 82
Cdd:cd18882     1 HEVAIAILYdDRGKVLLQLRDDKPGipYPGYWGLFGGHLEPGETPEEAIRRELEEEIGYEP---GEFRFF-LLYTEDDGE 76
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1871972815  83 ---LHIFHAS--VQPEQLA-GIKQPWRWYSRDEL 110
Cdd:cd18882    77 driRHVFHAPldVDLSDLVlNEGQALRLFSPEEI 110
NUDIX_MutT_Nudt1 cd04699
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
6-118 7.03e-11

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: 58.40  E-value: 7.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAI-AILFHQTQVLVGWREAKQhqGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLH 84
Cdd:cd04699     1 FPVSVkGVIFDNGRVLLLRRSRAG--AGEWELPGGRLEPGESPEEALKREVKEETGLDVSVGELLDTWTFELDPDKGVFI 78
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1871972815  85 IFHASVQPEQLAGIKQP---WRWYSRDELSELNFPKA 118
Cdd:cd04699    79 VTYLCRLVGGEVTLSDEheeYEWVTPEELAELELPEG 115
NUDIX_Hydrolase cd04688
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
9-115 1.51e-10

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: 57.94  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   9 AIAILFHQTQVLVgwreAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE--------------QWQAFDFISH 74
Cdd:cd04688     5 VAAIIIRDGKVLL----ARGEDDDYYRLPGGRVEFGETSEDALVREFKEELGVEVEvvrllfvvenfftyDGKPFHEIGF 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1871972815  75 EYEDVIVNLHIFHASVQPEQLAGIKQPWRWYSRDELSELNF 115
Cdd:cd04688    81 YYLVELSDEALYEQDIFFLEEDGEKLEFRWIPLEELDEIDL 121
NUDIX_Hydrolase cd04686
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
11-114 5.51e-10

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: 56.15  E-value: 5.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  11 AILFHQTQVLVGWREAKQHQGnKYEFPGGKVEQGELPIEACRREVIEEVG---IDIEQWQAFDFISHEYEDVIVNLH--- 84
Cdd:cd04686     6 GIIIRNDKLLLIRKTRGPYQG-RYDLPGGSQEFGESLEDALKREFAEETGmtvTSYDNLGVYDFFVPWSDKELGDVHhig 84
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1871972815  85 -IFHASVQPEQLAGIKQP-------WRWYSRDELSELN 114
Cdd:cd04686    85 vFYDVELLDNNISELLQFegqdslgAVWIPLQDLTELN 122
NUDIX_ADPRase cd04673
ADP-ribose pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1.13) catalyzes the ...
9-64 4.62e-09

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: 53.67  E-value: 4.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1871972815   9 AIAILFHQTQV-LVgwREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04673     4 VGAVVFRDGRVlLV--RRGNPPDAGLWSFPGGKVELGETLEDAALRELREETGLEAE 58
NUDIX_RppH cd04665
RNA pyrophosphohydrolase; The initiation of mRNA degradation often requires deprotection of ...
7-127 6.35e-09

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: 53.02  E-value: 6.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   7 HVAIaILFHQTQVLVgwreAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAF-DFISHEYEDVIVNLhI 85
Cdd:cd04665     2 HVVV-IARYKGKWLF----TRHKERRGWEFPGGKREPGETIEEAARRELYEETGAVIFELKPLgQYSVHGKGQEFFGA-V 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  86 FHASV-----QPEQLAgIKQPwRWYSRDELSELNFPKANQAMIQKLQ 127
Cdd:cd04665    76 YYAEVksfepILPYFE-TAEV-RLFDELPEFSLTYPDIQPHLLEKLK 120
NUDIX_DHNTPase_like cd04664
dihydroneopterin hydrolase; DHNTP pyrophosphatase (DHNTPase) catalyzes the hydrolysis of ...
39-129 6.89e-09

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: 53.41  E-value: 6.89e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  39 GKVEQGELPIEACRREVIEEVGIDIEQWQAFD-FISHEYE-------DVIVNL-HIFHASVQPEQ---LAGIKQPWRWys 106
Cdd:cd04664    33 GGIEDGETPWQAALRELKEETGLDPLELQLIDlNVSNFYEifddwrpGVTVNTeHVFAVEVPEEQpirLSPEHTDYRW-- 110
                          90       100
                  ....*....|....*....|...
gi 1871972815 107 rdelseLNFPKAnqamIQKLQWP 129
Cdd:cd04664   111 ------LPYEEA----AELLFWP 123
PRK10546 PRK10546
pyrimidine (deoxy)nucleoside triphosphate diphosphatase;
5-87 1.96e-08

pyrimidine (deoxy)nucleoside triphosphate diphosphatase;


Pssm-ID: 182536 [Multi-domain]  Cd Length: 135  Bit Score: 52.05  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   5 TIHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGID--IEQWQAfdfiSHEYE--DVI 80
Cdd:PRK10546    3 MIDVVAAIIERDGKILLAQRPAHSDQAGLWEFAGGKVEPGESQPQALIRELREELGIEatVGEYVA----SHQREvsGRR 78

                  ....*..
gi 1871972815  81 VNLHIFH 87
Cdd:PRK10546   79 IHLHAWH 85
NUDIX_Hydrolase cd04667
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
31-126 2.12e-08

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: 51.52  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  31 GNKYEFPGGKVEQGELPIEACRREVIEEVGID-IEQWQAFDFISHEyedvivNLH-IFHASVQPEqlaGIKQP------W 102
Cdd:cd04667    20 GGRWLLPGGKIEPGESPLEAAIRELKEETGLAaLSLLYLFEHEGPH------KLHhVFLAEAPDG---GRPRPgneiarC 90
                          90       100
                  ....*....|....*....|....
gi 1871972815 103 RWYSRDELSELNFPKANQAMIQKL 126
Cdd:cd04667    91 RWVSADQLRDLNLSRATRLIVRRY 114
NUDIX_Dcp2p_Nudt20 cd03672
mRNA decapping enzyme 2; mRNA decapping enzyme 2 (Dcp2p; EC 3.6.1.62), nucleoside diphosphate ...
11-76 3.06e-08

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: 51.78  E-value: 3.06e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  11 AILFHQ--TQVLV--GWREakqhqGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEY 76
Cdd:cd03672     6 AILLNEdlDKVLLvkGWKS-----NSSWGFPKGKINKDESDADCAIREVYEETGFDISDLINDKDYIELT 70
NUDIX_MutT_Nudt1 cd18886
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
10-114 3.37e-08

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: 51.85  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  10 IAILFHQTQVLVGWREAKQHQGnKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQ---AFDFISHEYEDVIVnLHIF 86
Cdd:cd18886     4 LCFIIRDDEVLLLNRNKKPNMG-KWNGVGGKLEPGESPEECAIREVFEETGLELEDLQlrgIVTFPSFDGGEDWL-MYVF 81
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1871972815  87 HASV-----QPEQLAGIKQpwrWYSRDELSELN 114
Cdd:cd18886    82 LAEAfsgelVESDREGILA---WVPIDWLLNLP 111
NUDIX_MTH1_Nudt1 cd03427
MutT homolog-1 (MTH1); MutT homolog-1 (MTH1; EC 3.6.1.- ), also called nucleoside ...
32-89 3.69e-08

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: 51.38  E-value: 3.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1871972815  32 NKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQA-----FDFISHEYEDVIvnlHIFHAS 89
Cdd:cd03427    27 GKWNGFGGKVEPGETIEEAAVRELEEEAGLTATELEKvgrlkFEFPDDPEAMDV---HVFRAD 86
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
8-113 4.63e-08

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: 51.37  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFH-QTQVLVGWR-EAKQHQGNKYEF-PGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDVIVNLH 84
Cdd:cd04693    31 VVHVWIFNsDGEILIQQRsPDKKGFPGMWEAsTGGSVLAGETSLEAAIRELKEELGIDLDADELRPILTIRFDNGFDDIY 110
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1871972815  85 IFHASV-------QPEQLAGIKqpwrWYSRDELSEL 113
Cdd:cd04693   111 LFRKDVdiedltlQKEEVQDVK----WVTLEEILEM 142
NUDIX_Hydrolase cd04681
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
11-124 7.97e-08

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: 50.26  E-value: 7.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  11 AILFHQTQVLVGWReAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFI--SHEYEDVIVN-LHIFH 87
Cdd:cd04681    11 VIIRNEGEILFVRR-AKEPGKGKLDLPGGFVDPGESAEEALRRELREELGLKIPKLRYLCSLpnTYLYKGITYKtCDLFF 89
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1871972815  88 ASVQPEQLAGIKQP-----WRWYSRDEL--SELNFPKANQAMIQ 124
Cdd:cd04681    90 TAELDEKPKLKKAEdevaeLEWLDLEEIepEKLAFPSIRKAVER 133
PRK02615 PRK02615
thiamine phosphate synthase;
221-297 9.65e-08

thiamine phosphate synthase;


Pssm-ID: 235054 [Multi-domain]  Cd Length: 347  Bit Score: 52.58  E-value: 9.65e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1871972815 221 CHDLEALKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFALGGIKAEDLDHAQNQHAYGIAGIR 297
Cdd:PRK02615  247 TTNPEEMAKAIAEGADYIGVGPVFPTPTKPGKAPAGLEYLKYAAKEAPIPWFAIGGIDKSNIPEVLQAGAKRVAVVR 323
NUDIX_ADPRase_Nudt5_UGPPase_Nudt14 cd03424
ADP-ribose pyrophosphatase, UDP-glucose pyrophosphatase, and similar proteins; ADP-ribose ...
34-67 1.23e-07

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: 49.81  E-value: 1.23e-07
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1871972815  34 YEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQ 67
Cdd:cd03424    31 LELPAGKIDPGEDPEEAARRELEEETGYTAGDLE 64
NUDIX_Hydrolase cd04690
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-88 1.52e-07

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: 49.07  E-value: 1.52e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFHQTQVLVgwreAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQwQAFDFI------SHEYEDV 79
Cdd:cd04690     1 IVKAAVIIIKDGRLLL----VRKRGTDAFYLPGGKREPGETPLQALVRELKEELGLDLDP-DSLRFLgtfeapAANEPGT 75

                  ....*....
gi 1871972815  80 IVNLHIFHA 88
Cdd:cd04690    76 TVRMTCFTA 84
NUDIX_Hydrolase cd03674
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
37-123 1.67e-07

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: 49.18  E-value: 1.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  37 PGGKVEQGELPIEACRREVIEEVGIDIE--QWQAFDFISHEYEDVIVN------LHI-----FHAS--VQPEQLAGIKqP 101
Cdd:cd03674    30 PGGHVEPDEDPLEAALREAREETGLDVEllSPLSPDPLDIDVHPIPANpgepahLHLdvrylAVADgdEALRKSDESS-D 108
                          90       100
                  ....*....|....*....|..
gi 1871972815 102 WRWYSRDELSELNFPKANQAMI 123
Cdd:cd03674   109 VRWFPLDELEELSMDPNLRKLL 130
NUDIX_DNA_Glycosylase_C-MutY cd03431
C-terminal domain of DNA glycosylase; DNA glycosylase (MutY in bacteria and hMYH in humans) is ...
3-124 2.09e-07

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: 48.84  E-value: 2.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   3 KTTIHVAIAILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFD--FiSHeyedVI 80
Cdd:cd03431     1 VPERYFTVLVLRDGGRVLLEKRPEKGLLAGLWEFPLVETEEEEEEAEALLGLLAEELLLILEPLGEVKhvF-SH----FR 75
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1871972815  81 VNLHIFHASVqPEQLAGIKQPWRWYSRDELSELNFPKANQAMIQ 124
Cdd:cd03431    76 LHITVYLVEL-PEAPPAAPDEGRWVDLEELDEYALPAPMRKLLE 118
NUDIX_Hydrolase cd18875
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
15-65 2.30e-07

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: 49.11  E-value: 2.30e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1871972815  15 HQTQVLVgwrEAKQHQG-NKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQ 65
Cdd:cd18875    12 GEDRVLV---LDRVKKDwGGYTFPGGHVEPGESFVDSVIREVKEETGLTIKN 60
nudix_YtkD TIGR02705
nucleoside triphosphatase YtkD; The functional assignment to the proteins of this family is ...
29-60 3.81e-07

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: 48.91  E-value: 3.81e-07
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1871972815  29 HQGNKYEFPGGKVEQGELPIEACRREVIEEVG 60
Cdd:TIGR02705  42 HKRRGLEFPGGKVEPGETSKEAAIREVMEETG 73
NUDIX_8DGDPP_Nudt18 cd04671
8-oxo-DGDP phosphatase; 8-oxo-DGDP phosphatase (8DGDPP; EC 3.6.1.55), also known as NUDIX ...
8-64 3.90e-07

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: 48.08  E-value: 3.90e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1871972815   8 VAIAILFHQTQVLVgWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04671     3 VAAVIINEQGEVLM-IQEAKRSCRGKWYLPAGRVEPGESIVEAAKREVKEETGLKCE 58
NUDIX_Hydrolase cd04669
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
34-64 5.84e-07

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: 47.35  E-value: 5.84e-07
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1871972815  34 YEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04669    26 YVFPGGGIEPGETPEEAALREAVEELGLDVA 56
NUDIX_Hydrolase cd04663
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
8-112 6.78e-07

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: 47.67  E-value: 6.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVgwREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDiEQWQAFDFISHEYE-DVIVNLHIF 86
Cdd:cd04663     4 CAYVTRGRNRELLV--FEHPDFPEAGLQVPKGTVEPGESPEEAALRELAEETGLT-GARVVVDLGSHDEGfEELHQRWFF 80
                          90       100
                  ....*....|....*....|....*.
gi 1871972815  87 HASVQPEQlagiKQPWRWYSRDELSE 112
Cdd:cd04663    81 HLCLAGEP----PERWEHHETDDGEG 102
NUDIX_Ap4A_hydrolase_plant_like cd03671
plant diadenosine tetraphosphate (Ap4A) hydrolase and similar proteins; Diadenosine ...
8-116 7.17e-07

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: 47.95  E-value: 7.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGWReakQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQwqaFDFIShEYEDVI------- 80
Cdd:cd03671     6 VGIVLFNRDGQVLVGRR---IDVPGAWQFPQGGIDEGEDPEEAALRELYEETGLSPED---VEIIA-ETPDWLtydlped 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1871972815  81 VNLHIFHAsvqpeQLAGIKQPW---RWYSRDELSELNFP 116
Cdd:cd03671    79 LIRKGWGG-----KYRGQKQKWflfRFTGDDSEINLDTH 112
NUDIX_Hydrolase cd04684
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
9-64 1.04e-06

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: 47.23  E-value: 1.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1871972815   9 AIAILFHQT-QVLVgwreaKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04684    18 AYAVIFNDEgKVLL-----VQTPNGGYFLPGGGIEPGETPEEALHREVLEETGWEIE 69
PRK07695 PRK07695
thiazole tautomerase TenI;
222-294 1.64e-06

thiazole tautomerase TenI;


Pssm-ID: 181086 [Multi-domain]  Cd Length: 201  Bit Score: 47.71  E-value: 1.64e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1871972815 222 HDLEALKHAENIGCEAALLSPVLATETHPDTAALGWEKFKQMAEQVQIPVFALGGIKAEDLDHAQNQHAYGIA 294
Cdd:PRK07695  103 HSLEEAIQAEKNGADYVVYGHVFPTDCKKGVPARGLEELSDIARALSIPVIAIGGITPENTRDVLAAGVSGIA 175
NUDIX_ASFGF2_Nudt6 cd04670
Antisense Basic Fibroblast Growth Factor; Antisense Basic Fibroblast Growth Factor (ASFGF2; EC ...
4-64 1.66e-06

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: 46.38  E-value: 1.66e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1871972815   4 TTIHVAIAILFHQTQVLVGwREaKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04670     1 HQVGVGGLVINENNEVLVV-QE-KYGGPGGWKLPGGLVDPGEDIGEAAVREVFEETGIDTE 59
nudB PRK09438
dihydroneopterin triphosphate pyrophosphatase; Provisional
39-128 2.11e-06

dihydroneopterin triphosphate pyrophosphatase; Provisional


Pssm-ID: 236516 [Multi-domain]  Cd Length: 148  Bit Score: 46.43  E-value: 2.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  39 GKVEQGELPIEACRREVIEEVGIDI--EQWQAFDF-ISHEYE-----------DVIVNL-HIF----HASVQP---EQLA 96
Cdd:PRK09438   38 GSLEEGETPAQTAIREVKEETGIDVlaEQLTLIDCqRSIEYEifphwrhryapGVTRNTeHWFclalPHERPVvltEHLA 117
                          90       100       110
                  ....*....|....*....|....*....|..
gi 1871972815  97 gikqpWRWYSRDELSELNFPKANQAMIQKLQW 128
Cdd:PRK09438  118 -----YQWLDAREAAALTKSWSNAEAIEQLVI 144
NUDIX_ADPRase cd04691
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
33-64 3.60e-06

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: 45.37  E-value: 3.60e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1871972815  33 KYEFPGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04691    27 RWTLPGGFVEEGETLDEAIVREVLEETGIDAK 58
NUDIX_Hydrolase cd18874
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
31-63 7.82e-06

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: 44.58  E-value: 7.82e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1871972815  31 GNKYEFPGGKVEQGELPIEACRREVIEEVGIDI 63
Cdd:cd18874    25 NDLYGIPGGKVEWGETLEEALKREVKEETGLDI 57
thiE PRK00043
thiamine phosphate synthase;
221-283 8.49e-06

thiamine phosphate synthase;


Pssm-ID: 234590 [Multi-domain]  Cd Length: 212  Bit Score: 45.94  E-value: 8.49e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815 221 CHDLEALKHAEN-----IGceaalLSPVLATETHPDT-AALGWEKFKQMAEQVQ-IPVFALGGIKAEDLD 283
Cdd:PRK00043  111 THTLEEAAAALAagadyVG-----VGPIFPTPTKKDAkAPQGLEGLREIRAAVGdIPIVAIGGITPENAP 175
NUDIX_CoAse_Nudt7 cd03426
coenzyme A pyrophosphatase and similar proteins; Coenzyme A pyrophosphatase (CoAse; EC 3.6.1.1) ...
36-67 9.24e-06

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: 44.79  E-value: 9.24e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1871972815  36 FPGGKVEQG-ELPIEACRREVIEEVGIDIEQWQ 67
Cdd:cd03426    36 FPGGKREPGdESPVETALRETEEEIGLPPESVE 68
NUDIX_Ap4A_Nudt2 cd03428
diadenosine tetraphosphate; Diadenosine tetraphosphate (Ap4A; EC 3.6.1.17), also called NUDIX ...
27-65 1.00e-05

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: 44.08  E-value: 1.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1871972815  27 KQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQ 65
Cdd:cd03428    23 QHSYGGHWDFPKGHVEPGESELETALRETKEETGLTVDD 61
NUDIX_Hydrolase cd04682
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
12-118 1.41e-05

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: 43.82  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  12 ILFHQTQVLVGWREAKQH--QGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQ----WQAFdFISHEYEDVIVnlHI 85
Cdd:cd04682     6 ALFLGDKLLTILRDDKPGipFPNLWDLPGGGREGDETPFACVLRELREELGLALPEdrlvWERV-YPSNHNPGRQS--WF 82
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1871972815  86 FHASVQPEQLAGIK-----QPWRWYSRDELseLNFPKA 118
Cdd:cd04682    83 FVARLPADEVDAIRfgdegQEWALMPVDDF--LAHPDA 118
NUDIX_Hydrolase cd04685
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
37-110 1.47e-05

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: 43.72  E-value: 1.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  37 PGGKVEQGELPIEACRREVIEEVGIDIEQ--------WQAFDFishEYEDVIVNLH--IFHASVQPEQL----------A 96
Cdd:cd04685    33 PGGGVEPGESPEQAAVRELREETGLRLEPddlggpvwRRRAVF---DFSGETVRQDerFFLVRVPAFEVdtagwtdlerA 109
                          90
                  ....*....|....
gi 1871972815  97 GIKQpWRWYSRDEL 110
Cdd:cd04685   110 VIDG-HRWWSLAEL 122
NUDIX_ADPRase cd18880
ADP-ribose pyrophosphatase and similar proteins; ADP-ribose pyrophosphatase (ADPRase; EC 3.6.1. ...
11-64 1.48e-05

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: 43.67  E-value: 1.48e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1871972815  11 AILFHQTQVLVgwreaKQHQGNKYEF---PGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd18880     6 AIIIEDGKLLL-----VKHRDEGGIFyilPGGGQEHGETLPEALKRECLEETGLDVE 57
NUDIX_NADH_pyrophosphatase_Nudt13 cd03429
NADH pyrophosphatase; NADH pyrophosphatase, also known as NUDIX (nucleoside diphosphate linked ...
8-116 2.18e-05

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: 43.25  E-value: 2.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGwrEAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE-------QWQAFdfiSHeyedvi 80
Cdd:cd03429     4 VIVLVTNGEDKILLA--RQPRWPPGRYSLLAGFVEPGETLEEAVRREVKEEVGLRVKnvryvgsQPWPF---PS------ 72
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1871972815  81 vNLHI-FHASVQPEQLagIKQPW-----RWYSRDELSELNFP 116
Cdd:cd03429    73 -SLMLgFTAEADSGEI--TVDDDeledaRWFSRDELPEALFL 111
NUDIX_Hydrolase cd04683
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
12-112 2.32e-05

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: 43.36  E-value: 2.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  12 ILFHQTQVLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDI------------------EQWQAFDFIS 73
Cdd:cd04683     6 LLVRGDEVLLLRRANTGYDDGWWHLPAGHVEAGETVRAAAVREAKEELGVEIdpedlrlvhtmhrrsdggRERIDFFFRA 85
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1871972815  74 HEYEDVIVNLhifhasvQPEQLAGikqpWRWYSRDELSE 112
Cdd:cd04683    86 TRWSGEPRNR-------EPDKCAE----LRWFPLDALPE 113
NUDIX_Ap6A_hydrolase cd03673
diadenosine hexaphosphate (Ap6A) hydrolase; Diadenosine hexaphosphate (Ap6A) hydrolase is a ...
36-113 4.39e-05

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: 42.54  E-value: 4.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  36 FPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYED---VIVNL-HIFHA-----SVQPEQLAGIKQPwRWYS 106
Cdd:cd03673    31 LPKGKLEPGETPEEAAVREVEEETGLRVRLGRPLGTTRYTYTRkgkGILKKvHYWLMralggEFLPQPEEEIDEV-RWLP 109

                  ....*..
gi 1871972815 107 RDELSEL 113
Cdd:cd03673   110 PDEARRL 116
NUDIX_ADPRase_Ndx2 cd24161
NUDIX family Ndx2; NUDIX family protein Ndx2 found in Thermus thermophilus has ADP-ribose ...
34-67 4.98e-05

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: 42.54  E-value: 4.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1871972815  34 YEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQ 67
Cdd:cd24161    32 WEIPAGGWPEGEDPEEAARRELREETGLRAERWT 65
NUDIX_Nudt17 cd04694
nucleoside diphosphate-linked moiety X)) motif 17; Nucleoside diphosphate-linked moiety X)) ...
36-67 5.21e-05

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: 42.28  E-value: 5.21e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1871972815  36 FPGGKVEQGELPIEACRREVIEEVGIDIEQWQ 67
Cdd:cd04694    34 PPGGHVELGESLLEAGLRELQEETGLEVSDIQ 65
NUDIX_Hydrolase cd04676
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
8-116 6.62e-05

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


Pssm-ID: 467559 [Multi-domain]  Cd Length: 144  Bit Score: 42.01  E-value: 6.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVGWREAKQHqgnkYEFPGGKVEQGELPIEACRREVIEEVG--------IDIEQWQAFDFISHEYEDV 79
Cdd:cd04676    20 VAAVILNEDGRILLQRKGGLGL----WSLPAGAIEPGEHPAEAVIREVREETGllvkptrlLGVFGGKEFRYTYPNGDQV 95
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1871972815  80 IVNLHIFHASVQP---EQLAGIKQPWRWYSRDELSELNFP 116
Cdd:cd04676    96 EYTVIAFKCVVTGgtlNAIDGETSELRYFSRTQMPTLALP 135
thiE TIGR00693
thiamine-phosphate diphosphorylase; This model represents the thiamine-phosphate ...
221-296 7.54e-05

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: 42.62  E-value: 7.54e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1871972815 221 CHDLEALKHAENIGCEAALLSPVLATETHPDTAA-LGWEKFKQMAEQVQ-IPVFALGGIkaeDLDHAQNQHAYGIAGI 296
Cdd:TIGR00693 103 THNLEELAEAEAEGADYIGFGPIFPTPTKKDPAPpAGVELLREIAATLIdIPIVAIGGI---TLENAAEVLAAGADGV 177
NUDIX_Hydrolase cd18877
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
19-65 7.99e-05

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: 7.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1871972815  19 VLVGWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQ 65
Cdd:cd18877    34 VLLQHRAWWTHQGGTWALPGGARDSGETPEAAALRETEEETGLDADT 80
NUDIX_Hydrolase cd04677
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-79 7.99e-05

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: 41.73  E-value: 7.99e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1871972815  36 FPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDV 79
Cdd:cd04677    39 LPGGAMELGESLEETARREVFEETGLTVEELELLGVYSGKDLYY 82
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
3-113 9.79e-05

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: 42.11  E-value: 9.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   3 KTTIHVAIAILFH--QTQVLVGWREAkqhqgNKYEFPG-------GKVEQGELPIEACRREVIEEVGIDIEQW--QAFDF 71
Cdd:COG1443    25 KGLLHRAFSVFVFnsDGRLLLQRRAL-----TKDHWPGlwdntvcGHPRAGETYEEAAVRELEEELGITVDDDlrPLGTF 99
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1871972815  72 ISHEY--EDVIVN--LHIFHASV------QPEQLAGikqpWRWYSRDELSEL 113
Cdd:COG1443   100 RYRAVdaNGLVENefCHVFVARLdgpltpQPEEVAE----VRWVTLEELLAL 147
PRK00714 PRK00714
RNA pyrophosphohydrolase; Reviewed
8-62 1.62e-04

RNA pyrophosphohydrolase; Reviewed


Pssm-ID: 234820 [Multi-domain]  Cd Length: 156  Bit Score: 41.30  E-value: 1.62e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1871972815   8 VAIAILFHQTQVLVGWREAkqhQGNKYEFPGGKVEQGELPIEACRREVIEEVGID 62
Cdd:PRK00714   11 VGIILLNRQGQVFWGRRIG---QGHSWQFPQGGIDPGETPEQAMYRELYEEVGLR 62
NUDIX_Hydrolase cd04680
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
36-65 1.65e-04

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


Pssm-ID: 467563 [Multi-domain]  Cd Length: 121  Bit Score: 40.70  E-value: 1.65e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1871972815  36 FPGGKVEQGELPIEACRREVIEEVGIDIEQ 65
Cdd:cd04680    27 LPGGGVDKGETAEEAARRELREEAGVVLTG 56
NUDIX_ADPRase cd24155
Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ...
34-98 1.76e-04

Adp Ribose Pyrophosphatase; ADP-ribose pyrophosphatase (ADPRase) catalyzes the hydrolysis of ADP-ribose and a variety of additional ADP-sugar conjugates to AMP and ribose-5-phosphate. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site.


Pssm-ID: 467603 [Multi-domain]  Cd Length: 187  Bit Score: 41.74  E-value: 1.76e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1871972815  34 YEFPGGKVEQGELPIEACRREVIEEVGIDIEQ-WQAFDFI-----SHEYedvivnLHIFHASVQPEQLAGI 98
Cdd:cd24155    78 LEIVAGMIDAGETPEDVARREAEEEAGLTLDAlEPIASYYpspggSTER------VHLYLGLVDLSDLGGI 142
PLN02325 PLN02325
nudix hydrolase
8-112 1.78e-04

nudix hydrolase


Pssm-ID: 215184 [Multi-domain]  Cd Length: 144  Bit Score: 41.00  E-value: 1.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAI-LFHQTQVLVGWREAKQHQGNkYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYEDV-----IV 81
Cdd:PLN02325   10 VAVVVfLLKGNSVLLGRRRSSIGDST-FALPGGHLEFGESFEECAAREVKEETGLEIEKIELLTVTNNVFLEEpkpshYV 88
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1871972815  82 NLHIFHASVQPEQLAGIKQP-----WRWYSRDELSE 112
Cdd:PLN02325   89 TVFMRAVLADPSQVPQNLEPekcygWDWYEWDNLPE 124
NUDIX_MutT_Nudt1 cd04679
MutT homolog-1 and similar proteins; MutT homolog-1 (MTH1), also known as NUDIX (nucleoside ...
37-64 5.66e-04

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: 39.21  E-value: 5.66e-04
                          10        20
                  ....*....|....*....|....*...
gi 1871972815  37 PGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd04679    32 PGGKVDWLETVEDAVRREILEELGLEIE 59
NUDIX_MRP_L46 cd04661
Mitochondrial ribosomal protein L46; Mitochondrial ribosomal protein L46 (MRP L46) is a ...
27-112 7.95e-04

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: 39.13  E-value: 7.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  27 KQHQGnKYEFPGGKVEQGELPIEACRREVIEEVGIDIEQWqafdFIS------HEYED------VIVNLHIFHASVQPEQ 94
Cdd:cd04661    38 KKGKG-PWQFPQGDVEEGETLREAAERGLRELGGDNMNTW----FVGnapigvYKYKYpkktkeFGYKSFFLKGRFMPGQ 112
                          90
                  ....*....|....*...
gi 1871972815  95 LAGIKQpWRWYSRDELSE 112
Cdd:cd04661   113 KKGVSD-FAWLTKEELKE 129
NUDIX_Hydrolase cd03675
uncharacterized NUDIX hydrolase subfamily; Contains a crystal structure of the NUDIX hydrolase ...
25-113 8.68e-04

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


Pssm-ID: 467543 [Multi-domain]  Cd Length: 138  Bit Score: 38.66  E-value: 8.68e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  25 EAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGIDIE--------QWQAfdfisHEYEDVIVNlHIFHASV-----Q 91
Cdd:cd03675    17 EEETDGRLVLNQPAGHLEPGESLLEAAIRETLEETGWEVEptallgiyQWTA-----PDNGVTYLR-FAFAGELlehlpD 90
                          90       100
                  ....*....|....*....|..
gi 1871972815  92 PEQLAGIKQPwRWYSRDELSEL 113
Cdd:cd03675    91 QPLDSGIIRA-HWLTLEEILAL 111
NUDIX_GDPMH_NudD cd03430
GDP-mannose glycosyl hydrolase; GDP-mannose glycosyl hydrolase, also known as GDP-mannose ...
18-110 1.25e-03

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: 38.38  E-value: 1.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  18 QVLVGWREAKQHQGnkYEF-PGGKVEQGELPIEACRREVIEEVGIDIEQwQAFDFI---SHEYED----------VIVNL 83
Cdd:cd03430    28 EILLGKRNNRPAQG--YWFvPGGRILKNETLDDAFKRIAREELGLEVTI-NAAEFLgvyEHFYDDnfsgedfsthYVVLA 104
                          90       100
                  ....*....|....*....|....*....
gi 1871972815  84 HIFHASVQPEQLAgIKQ--PWRWYSRDEL 110
Cdd:cd03430   105 YRLKLDEGLLLLP-DDQhdEYRWFTIDEL 132
nudE PRK11762
adenosine nucleotide hydrolase NudE; Provisional
34-60 1.28e-03

adenosine nucleotide hydrolase NudE; Provisional


Pssm-ID: 183303  Cd Length: 185  Bit Score: 39.02  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*....
gi 1871972815  34 YE--FPGGKVEQGELPIEACRREVIEEVG 60
Cdd:PRK11762   74 YElgFPKGLIDPGETPLEAANRELKEEVG 102
NUDIX_NadM_like cd18873
bifunctional NMN adenylyltransferase/ADP-ribose pyrophosphatase and similar proteins; ...
8-115 1.35e-03

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: 38.29  E-value: 1.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   8 VAIAILFHQTQVLVgWREAKQHQGNKYEFPGGKVEQGELPIEACRREVIEEVGID---IEQWQAFD---------FISHE 75
Cdd:cd18873     8 VIFGFDDGELKVLL-IKRKNEPFKGGWALPGGFVREDETLEDAARRELREETGLKdiyLEQLGTFGdpdrdprgrVISVA 86
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1871972815  76 YedvivnlhifHASVQPEQLAGIKQPW----RWYSRDE-LSELNF 115
Cdd:cd18873    87 Y----------LALVPEEDLAPKAGDDaaeaRWFPVDElLPPLAF 121
PRK05379 PRK05379
bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;
11-63 1.89e-03

bifunctional nicotinamide-nucleotide adenylyltransferase/Nudix hydroxylase;


Pssm-ID: 235436 [Multi-domain]  Cd Length: 340  Bit Score: 39.22  E-value: 1.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1871972815  11 AILFHQTQVLVGWREAKQHQGnKYEFPGGKVEQGELPIEACRREVIEEVGIDI 63
Cdd:PRK05379  208 AVVVQSGHVLLVRRRAEPGKG-LWALPGGFLEQDETLLDACLRELREETGLKL 259
NUDIX_ADPRase_NudF cd24159
Bdellovibrio Bacteriovorus nucleoside diphosphate sugar hydrolase, and similar proteins; ...
35-66 1.92e-03

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: 38.52  E-value: 1.92e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1871972815  35 EFPGGKVEQGELPIEACRREVIEEVGIDIEQW 66
Cdd:cd24159    71 EFPAGKIDPGEDTLETAKRELLEETGYEAQEW 102
NUDIX_ADPRase cd24160
Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ...
9-62 2.30e-03

Adp-ribose pyrophosphatase (ADPRase) found in Thermus thermophilus, and similar proteins; ADP-ribose pyrophosphatase (ADPRase) such as found in extreme thermophile Thermus thermophilus (TtADPRase) catalyzes the hydrolysis of ADPR to AMP and ribose 5'-phosphate in the presence of Mg2+ and Zn2+ ions. In humans, there are four distinct ADPRase activities, three putative cytosolic enzymes (ADPRase-I, -II, and -Mn) and a single mitochondrial enzyme (ADPRase-m). Human ADPRase-II is also referred to as NUDT5. It lacks the N-terminal target sequence unique to mitochondrial ADPRase. The different cytosolic types are distinguished by their specificities for substrate and specific requirement for metal ions. NUDT5 forms a homodimer. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site. In addition to the NUDIX motif, there are additional conserved amino acid residues, distal from the signature sequence, that correlate with substrate specificity. UDP-glucose pyrophosphatase (UGPPase) (EC 3.6.1.45; also known as nucleoside diphosphate-linked moiety X)) motif 14; Nudt14) hydrolyzes the pyrophosphate of the nucleoside diphosphate sugar to generate glucose-1-P and UMP. In mammals, UDP-glucose is the glucosyl donor for the synthesis of the storage polysaccharide glycogen. UGPPase, as a regulator of UDP-glucose, could play a regulatory role, but it has been shown to prefer ADP-ribose over UDP-glucose. Like other members of the NUDIX hydrolase superfamily, it requires a divalent cation, such as Mg2+, for its activity. It also contains a highly conserved 23-residue NUDIX motif (GX5EX7REUXEEXGU, where U = I, L or V) which functions as a metal binding site/catalytic site.


Pssm-ID: 467608 [Multi-domain]  Cd Length: 151  Bit Score: 37.87  E-value: 2.30e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1871972815   9 AIAILFHQTQVLVGWREAKQHQG-NKYEFPGGKVEQGELPIEACRREVIEEVGID 62
Cdd:cd24160    23 AVAVLALREGRMLFVRQMRPAVGaATLEIPAGLIDPGETPEEAARRELAEETGLS 77
NUDIX_Hydrolase cd18884
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
6-85 2.93e-03

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


Pssm-ID: 467595 [Multi-domain]  Cd Length: 125  Bit Score: 37.01  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   6 IHVAIAILFHQTQVL----VGWREakqhqgNKYEFPGGKVEQGELPIEACRREVIEEVGIDIEqwqAFDFISH----EYE 77
Cdd:cd18884     9 IPVVAAIVEHDGHIVlarnKAWPE------GWYGLVTGFLEAGESPEEAVLREVKEELGLDGH---EAKFIGHyafpERN 79

                  ....*...
gi 1871972815  78 DVIVNLHI 85
Cdd:cd18884    80 QLIIAYHV 87
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
37-122 2.94e-03

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


Pssm-ID: 467578 [Multi-domain]  Cd Length: 157  Bit Score: 37.60  E-value: 2.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  37 PGGKVEQGELPIEACRREVIEEVGIDIEQWQA-FDFIsheYEDVIVN--LHIFHASV------QPEQLAGIKqpwrWYSR 107
Cdd:cd04697    60 TGGVVGAGESYEENARRELEEELGIDGVPLRPlFTFY---YEDDRSRvwGALFECVYdgplklQPEEVAEVD----WMSE 132
                          90       100
                  ....*....|....*....|
gi 1871972815 108 DELSEL----NF-PKANQAM 122
Cdd:cd04697   133 DEILQAargeEFtPDGRVAL 152
NUDIX_ADPRase_NudE cd24156
NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine ...
34-60 3.32e-03

NUDIX domain family NudE found in Escherichia coli, and similar proteins; The adenosine nucleotide hydrolase NudE protein in Escherichia coli is a NUDIX hydrolase family member active against ADP ribose, NADH, AP2A and AP3A33, and is classified as a hydrolase (E.C. 3.6.1.-) based on gene annotations. It is an 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: 467604 [Multi-domain]  Cd Length: 134  Bit Score: 37.22  E-value: 3.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 1871972815  34 YE--FPGGKVEQGELPIEACRREVIEEVG 60
Cdd:cd24156    29 YElgFPKGLIDPGETPEEAANRELKEEIG 57
NUDIX_Hydrolase cd18879
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
37-64 3.66e-03

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


Pssm-ID: 467590 [Multi-domain]  Cd Length: 142  Bit Score: 37.18  E-value: 3.66e-03
                          10        20
                  ....*....|....*....|....*...
gi 1871972815  37 PGGKVEQGELPIEACRREVIEEVGIDIE 64
Cdd:cd18879    46 VTGIVEPGEQPADAAVREVLEETGVDVE 73
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
32-99 4.30e-03

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


Pssm-ID: 467574 [Multi-domain]  Cd Length: 142  Bit Score: 36.77  E-value: 4.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815  32 NKYEFPG-------GKVEQGELPIEACRREVIEEVGIDI------------EQWQAFDFISHEYEDV-----IVNLHIFH 87
Cdd:cd04692    49 NKDDFPGlwdisaaGHIDAGETYEEAAVRELEEELGLTVspedliflgvirEEVIGGDFIDNEFVHVylyetDRPLEEFK 128
                          90
                  ....*....|..
gi 1871972815  88 asVQPEQLAGIK 99
Cdd:cd04692   129 --LQPEEVAGVV 138
NUDIX_DR1025_like cd04700
DR1025 and similar proteins; DR1025 from Deinococcus radiodurans, a member of the NUDIX ...
5-94 8.24e-03

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: 36.04  E-value: 8.24e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1871972815   5 TIHVAIAILFHQTQ--VLVGWREAKQHQGNK--YEFPGGKVEQGELPIEACRREVIEEVGIDIEQWQAFDFISHEYED-V 79
Cdd:cd04700    12 TLRAAGVVLLNERGdiLLVQEKGISGHPEKAglWHIPSGAVEDGENPQDAAVREACEETGLRVRLVKFLGAYLGRFPDgV 91
                          90
                  ....*....|....*
gi 1871972815  80 IVNLHIFHASVQPEQ 94
Cdd:cd04700    92 LVLRHVWLAEPEPGQ 106
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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