NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1235542952|gb|OZU33416|]
View 

NUDIX hydrolase [Salmonella enterica subsp. enterica serovar Tees]

Protein Classification

NUDIX hydrolase( domain architecture ID 10015101)

NUDIX hydrolase YfcD

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 2-181 1.12e-129

NUDIX hydrolase YfcD; Provisional


:

Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 361.04  E-value: 1.12e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952   2 VEQRRLASTEWVDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQ 81
Cdd:PRK15393    1 VEQRRLASTEWVDIVNENNEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  82 LLESARREAEEELGIAGVPFAEHGLFYFEDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDEFTPDSLKA 161
Cdd:PRK15393   81 LLESARREAEEELGIAGVPFAEHGQFYFEDENCRVWGALFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEFTPDSLKA 160

                         170       180
                  ....*....|....*....|
gi 1235542952 162 LALWMTRNAKNEAALQEKPE 181
Cdd:PRK15393  161 LALWLTRNAKNEAVETETAE 180
 
Name Accession Description Interval E-value
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 2-181 1.12e-129

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 361.04  E-value: 1.12e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952   2 VEQRRLASTEWVDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQ 81
Cdd:PRK15393    1 VEQRRLASTEWVDIVNENNEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  82 LLESARREAEEELGIAGVPFAEHGLFYFEDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDEFTPDSLKA 161
Cdd:PRK15393   81 LLESARREAEEELGIAGVPFAEHGQFYFEDENCRVWGALFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEFTPDSLKA 160

                         170       180
                  ....*....|....*....|
gi 1235542952 162 LALWMTRNAKNEAALQEKPE 181
Cdd:PRK15393  161 LALWLTRNAKNEAVETETAE 180
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 13-166 5.18e-70

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: 209.40  E-value: 5.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  13 VDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEE 92
Cdd:cd04697     1 VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1235542952  93 ELGIAGVPFAEHGLFYFEDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEIT--ARCDEFTPDSLKALALWM 166
Cdd:cd04697    81 ELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILqaARGEEFTPDGRVALERYL 156
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 10-161 5.05e-41

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: 135.71  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  10 TEWVDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARRE 89
Cdd:COG1443     1 EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  90 AEEELGIAGV-PFAEHGLFYF-----EDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDE----FTPDSL 159
Cdd:COG1443    81 LEEELGITVDdDLRPLGTFRYravdaNGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAgpeaFTPWFR 160


                  ..
gi 1235542952 160 KA 161
Cdd:COG1443   161 LY 162
NUDIX pfam00293
NUDIX domain;
36-147 5.07e-03

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 35.54  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  36 LRHRATYIVVHDGMGKILVQRRTetKDFLPGMLdATAGGVVQADEQLLESARREAEEELGIAG-----VPFAEHGLFY-F 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRS--KKPFPGWW-SLPGGKVEPGETPEEAARRELEEETGLEPellelLGSLHYLAPFdG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1235542952 110 EDQHCRVWGALFSCVSHGPFALQ-EDEVSEVCWLTPEEI 147
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDpDGEVEEVRWVPLEEL 116
 
Name Accession Description Interval E-value
PRK15393 PRK15393
NUDIX hydrolase YfcD; Provisional
 2-181 1.12e-129

NUDIX hydrolase YfcD; Provisional


Pssm-ID: 185291 [Multi-domain]  Cd Length: 180  Bit Score: 361.04  E-value: 1.12e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952   2 VEQRRLASTEWVDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQ 81
Cdd:PRK15393    1 VEQRRLASTEWVDIVNENNEVIAQASREQMRAQCLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQAGEQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  82 LLESARREAEEELGIAGVPFAEHGLFYFEDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDEFTPDSLKA 161
Cdd:PRK15393   81 LLESARREAEEELGIAGVPFAEHGQFYFEDENCRVWGALFSCVSHGPFALQEEEVSEVCWMTPEEITARCDEFTPDSLKA 160

                         170       180
                  ....*....|....*....|
gi 1235542952 162 LALWMTRNAKNEAALQEKPE 181
Cdd:PRK15393  161 LALWLTRNAKNEAVETETAE 180
NUDIX_Hydrolase cd04697
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 13-166 5.18e-70

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: 209.40  E-value: 5.18e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  13 VDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEE 92
Cdd:cd04697     1 VDIVDENNEVVGAATRAEMRRQKLIHRATYIVVRNAAGRLLVQKRTMDKDYCPGYLDPATGGVVGAGESYEENARRELEE 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1235542952  93 ELGIAGVPFAEHGLFYFEDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEIT--ARCDEFTPDSLKALALWM 166
Cdd:cd04697    81 ELGIDGVPLRPLFTFYYEDDRSRVWGALFECVYDGPLKLQPEEVAEVDWMSEDEILqaARGEEFTPDGRVALERYL 156
Idi COG1443
Isopentenyldiphosphate isomerase [Lipid transport and metabolism]; Isopentenyldiphosphate ...
 10-161 5.05e-41

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: 135.71  E-value: 5.05e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  10 TEWVDIVNEDNEVIAQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARRE 89
Cdd:COG1443     1 EELVDLVDEDGRPIGTAERAEVHRKGLLHRAFSVFVFNSDGRLLLQRRALTKDHWPGLWDNTVCGHPRAGETYEEAAVRE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  90 AEEELGIAGV-PFAEHGLFYF-----EDQHCRVWGALFSCVSHGPFALQEDEVSEVCWLTPEEITARCDE----FTPDSL 159
Cdd:COG1443    81 LEEELGITVDdDLRPLGTFRYravdaNGLVENEFCHVFVARLDGPLTPQPEEVAEVRWVTLEELLALLEAgpeaFTPWFR 160


                  ..
gi 1235542952 160 KA 161
Cdd:COG1443   161 LY 162
NUDIX_Hydrolase cd04692
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 13-144 6.56e-18

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: 75.67  E-value: 6.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  13 VDIVNEDNEVIAQSSREQMRAQRLRHRATYI-VVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAE 91
Cdd:cd04692     1 LDIVDEDGRPIGVATRSEVHRQGLWHRTVHVwLVNPEEGRLLLQKRSANKDDFPGLWDISAAGHIDAGETYEEAAVRELE 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1235542952  92 EELGIAGVPFAEHGLF----------YFEDQHCRVwgalFSCVSHGP---FALQEDEVSEVCWLTP 144
Cdd:cd04692    81 EELGLTVSPEDLIFLGvireeviggdFIDNEFVHV----YLYETDRPleeFKLQPEEVAGVVFVDL 142
NUDIX_Hydrolase cd04693
uncharacterized NUDIX hydrolase subfamily; NUDIX hydrolase is a superfamily of enzymes found ...
 11-153 6.55e-09

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: 52.14  E-value: 6.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  11 EWVDIVNEDNEVIAQSSReqmRAQRLRHRATYIVVH----DGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESA 86
Cdd:cd04693     1 ELWDLYDENRNKTGRTHR---RGEPLPEGEYHLVVHvwifNSDGEILIQQRSPDKKGFPGMWEASTGGSVLAGETSLEAA 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1235542952  87 RREAEEELGIAgVPFAE-------HGLFYFEDqhcrVWgaLFSC-VSHGPFALQEDEVSEVCWLTPEEITARCDE 153
Cdd:cd04693    78 IRELKEELGID-LDADElrpiltiRFDNGFDD----IY--LFRKdVDIEDLTLQKEEVQDVKWVTLEEILEMIES 145
PLN02791 PLN02791
Nudix hydrolase homolog
 38-146 3.08e-05

Nudix hydrolase homolog


Pssm-ID: 215425 [Multi-domain]  Cd Length: 770  Bit Score: 43.65  E-value: 3.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  38 HRATYIVVH-DGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEEELGIAGVPFAEHGLFYFEdQHCRV 116
Cdd:PLN02791   32 HRAVHVWIYsESTQELLLQRRADCKDSWPGQWDISSAGHISAGDTSLLSAQRELEEELGIILPKDAFELLFVFL-QECVI 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1235542952 117 WGA-----------LFSCVSHGP---FALQEDEVSEVCWLTPEE 146
Cdd:PLN02791  111 NDGkfinneyndvyLVTTLDPIPleaFTLQESEVSAVKYMSIEE 154
NUDIX_IPP_Isomerase cd02885
Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the ...
 13-156 2.99e-04

Isopentenyl diphosphate isomerase; Isopentenyl diphosphate (IPP) isomerase, a member of the NUDIX hydrolase superfamily, is a key enzyme in the isoprenoid biosynthetic pathway. Isoprenoids comprise a large family of natural products including sterols, carotenoids, dolichols and prenylated proteins. These compounds are synthesized from two precursors: isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). IPP isomerase catalyzes the interconversion of IPP and DMAPP by a stereoselective antarafacial transposition of hydrogen. The enzyme requires one Mn2+ or Mg2+ ion in its active site to fold into an active conformation and also contains the NUDIX motif, a highly conserved 23-residue block (GX5EX7REUXEEXGU, where U = I, L or V), that functions as a metal binding and catalytic site. The metal binding site is present within the active site and plays structural and catalytical roles. IPP isomerase is well represented in several bacteria, archaebacteria and eukaryotes, including fungi, mammals and plants. Despite sequence variations (mainly at the N-terminus), the core structure is highly conserved.


Pssm-ID: 467529 [Multi-domain]  Cd Length: 162  Bit Score: 39.40  E-value: 2.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  13 VDIVNEDNEVI-AQSSREQMRAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAE 91
Cdd:cd02885     2 VILVDEDDNPIgTAEKLEAHRKGTLLHRAFSVFLFNSKGELLLQRRALSKYTWPGLWTNTCCSHPLPGEGVEDAAQRRLR 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1235542952  92 EELGIAGVPFAEHGLF-Y--------FEDQHCRVwgalFSCVSHGPFALQEDEVSEVCWLTPEEI----TARCDEFTP 156
Cdd:cd02885    82 EELGIPVCDLEELPRFrYratddnglVEHEIDHV----FVGRADGDPVPNPEEVSDYRWVSLEELrellAATPEAFTP 155
PRK03759 PRK03759
isopentenyl-diphosphate Delta-isomerase;
8-177 1.06e-03

isopentenyl-diphosphate Delta-isomerase;


Pssm-ID: 235156 [Multi-domain]  Cd Length: 184  Bit Score: 38.03  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952   8 ASTEWVDIVNEDNEVIAQSSREQM-RAQRLRHRATYIVVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESA 86
Cdd:PRK03759    3 METELVVLLDEQGVPTGTAEKAAAhTADTPLHLAFSCYLFDADGRLLVTRRALSKKTWPGVWTNSCCGHPQPGESLEDAV 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  87 RREAEEELGIAGVPFA-EHGLFYF---------EDQHCRVWGALFScvshGPFALQEDEVSEVCWLTPEEITARCD---- 152
Cdd:PRK03759   83 IRRCREELGVEITDLElVLPDFRYratdpngivENEVCPVFAARVT----SALQPNPDEVMDYQWVDPADLLRAVDatpw 158

                         170       180
                  ....*....|....*....|....*
gi 1235542952 153 EFTPdslkalalWMTRNAKNEAALQ 177
Cdd:PRK03759  159 AFSP--------WMVLQAANLEARE 175
NUDIX_DR0079 cd24154
NUDIX domain family found in Deinococcus radiodurans, and similar proteins; Deinococcus ...
 50-150 2.77e-03

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


Pssm-ID: 467602 [Multi-domain]  Cd Length: 121  Bit Score: 36.04  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  50 GKILVQRRTETKDFLPGMLDATAGGVVQADEQLLESARREAEEELGIagvpfaehglfYFEDQHCRVWGaLFSCVSHGPF 129
Cdd:cd24154    14 GQLWIPRRTADKRIFPLALDMSVGGHVSSGETYEQAFVRELQEELNL-----------DLDQLSYRVLG-KLTPYEHGVS 81

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1235542952 130 A------LQEDEV--------SEVCWLTPEEITAR 150
Cdd:cd24154    82 AfmkvyeIRSDETpdynpddfSEAFWLTPEELLKR 116
NUDIX pfam00293
NUDIX domain;
36-147 5.07e-03

NUDIX domain;


Pssm-ID: 395229 [Multi-domain]  Cd Length: 132  Bit Score: 35.54  E-value: 5.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1235542952  36 LRHRATYIVVHDGMGKILVQRRTetKDFLPGMLdATAGGVVQADEQLLESARREAEEELGIAG-----VPFAEHGLFY-F 109
Cdd:pfam00293   1 KRRVAVGVVLLNEKGRVLLVRRS--KKPFPGWW-SLPGGKVEPGETPEEAARRELEEETGLEPellelLGSLHYLAPFdG 77

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1235542952 110 EDQHCRVWGALFSCVSHGPFALQ-EDEVSEVCWLTPEEI 147
Cdd:pfam00293  78 RFPDEHEILYVFLAEVEGELEPDpDGEVEEVRWVPLEEL 116
NUDIX_Tnr3_like cd03676
thiamine diphosphokinase Tnr3 from Schizosaccharomyces pombe and similar proteins; Tnr3 is a ...
 44-83 8.85e-03

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


Pssm-ID: 467544  Cd Length: 153  Bit Score: 35.16  E-value: 8.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1235542952  44 VVHDGMGKILVQRRTETKDFLPGMLDATAGGVVQADEQLL 83
Cdd:cd03676    15 VRDGDGLRLWVARRSATKATYPGKLDNLVAGGVPAGESPL 54
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH