NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|780464027|gb|AJZ67461|]
View 

MazG family protein [Xanthomonas citri pv. citri]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase( domain architecture ID 11484350)

nucleoside triphosphate pyrophosphohydrolase hydrolyzes NTPs into their corresponding nucleoside monophosphates and pyrophosphate

CATH:  1.10.287.1080
EC:  3.6.1.-
Gene Ontology:  GO:0047429|GO:0046872|GO:0009117
PubMed:  18353782|19523960

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-272 1.11e-154

nucleoside triphosphate pyrophosphohydrolase; Reviewed


:

Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 434.21  E-value: 1.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   1 MPQTPSiGDIQQLLHVMARLRDREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAA 80
Cdd:PRK09562   1 SRMETS-EAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  81 EQGAFTFADVVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAAgnqddSALAGIARGLPEWQRSTKLQSRA 160
Cdd:PRK09562  80 EQGAFDFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAES-----SVLDGIPRGLPALMRAYKIQKKA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 161 ARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAM 240
Cdd:PRK09562 155 ARVGFDWESLEPVLDKVEEEIDELKEALAQG----DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAV 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 780464027 241 EAQARTAGTSLNALSLGEQEALWQQAKREERS 272
Cdd:PRK09562 231 EQLAAAQGKTLEDASLEEMDALWQEAKRQEKA 262
 
Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-272 1.11e-154

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 434.21  E-value: 1.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   1 MPQTPSiGDIQQLLHVMARLRDREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAA 80
Cdd:PRK09562   1 SRMETS-EAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  81 EQGAFTFADVVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAAgnqddSALAGIARGLPEWQRSTKLQSRA 160
Cdd:PRK09562  80 EQGAFDFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAES-----SVLDGIPRGLPALMRAYKIQKKA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 161 ARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAM 240
Cdd:PRK09562 155 ARVGFDWESLEPVLDKVEEEIDELKEALAQG----DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAV 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 780464027 241 EAQARTAGTSLNALSLGEQEALWQQAKREERS 272
Cdd:PRK09562 231 EQLAAAQGKTLEDASLEEMDALWQEAKRQEKA 262
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 1-272 3.84e-154

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 433.00  E-value: 3.84e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   1 MPQTPSIG-DIQQLLHVMARLRDREhGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMA 79
Cdd:COG3956    1 MENREKPLyAFERLLEIMARLRDPD-GCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  80 AEQGAFTFADVVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAAGNQDDSALAGIARGLPEWQRSTKLQSR 159
Cdd:COG3956   80 EEEGAFDFDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEKGEGRKSVLDGVPRSLPALMRAYKLQKK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 160 AARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRA 239
Cdd:COG3956  160 AARVGFDWPDVEGVLDKVEEELAELKEALASG----DQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRY 235

                        250       260       270
                 ....*....|....*....|....*....|...
gi 780464027 240 MEAQARTAGTSLNALSLGEQEALWQQAKREERS 272
Cdd:COG3956  236 IEAAAAEQGKSLEDLSLEEMDALWQEAKKAEKE 268
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 16-267 4.60e-95

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 282.48  E-value: 4.60e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   16 VMARLRDREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADVVATLR 95
Cdd:TIGR00444   1 IIAQLRDPENGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   96 DKLIRRHPHVFAAQPAADAQAVSANWEQIKREERraAGNQDDSALAGIARGLPEWQRSTKLQSRAARVGFDWPGPAPVLE 175
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEK--AQKAQTSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  176 KLQEEIEELRVEFARGPVadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAMEAQARTAGTSLNALS 255
Cdd:TIGR00444 159 KVYEELDEVMYEARQAVV--EQNKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVD 236

                         250
                  ....*....|..
gi 780464027  256 LGEQEALWQQAK 267
Cdd:TIGR00444 237 LEEMEELWQQVK 248
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 11-125 1.07e-58

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 184.64  E-value: 1.07e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  11 QQLLHVMARLRdREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADV 90
Cdd:cd11528    1 ERLVEIVARLR-GPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDV 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 780464027  91 VATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIK 125
Cdd:cd11528   80 IDGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 33-106 6.15e-34

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 119.62  E-value: 6.15e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780464027   33 QTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADVVATLRDKLIRRHPHVF 106
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
 
Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-272 1.11e-154

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 434.21  E-value: 1.11e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   1 MPQTPSiGDIQQLLHVMARLRDREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAA 80
Cdd:PRK09562   1 SRMETS-EAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  81 EQGAFTFADVVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAAgnqddSALAGIARGLPEWQRSTKLQSRA 160
Cdd:PRK09562  80 EQGAFDFADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIKAEERAES-----SVLDGIPRGLPALMRAYKIQKKA 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 161 ARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAM 240
Cdd:PRK09562 155 ARVGFDWESLEPVLDKVEEEIDELKEALAQG----DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAV 230

                        250       260       270
                 ....*....|....*....|....*....|..
gi 780464027 241 EAQARTAGTSLNALSLGEQEALWQQAKREERS 272
Cdd:PRK09562 231 EQLAAAQGKTLEDASLEEMDALWQEAKRQEKA 262
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 1-272 3.84e-154

Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like pyrophosphatase domain [General function prediction only];


Pssm-ID: 443156 [Multi-domain]  Cd Length: 268  Bit Score: 433.00  E-value: 3.84e-154
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   1 MPQTPSIG-DIQQLLHVMARLRDREhGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMA 79
Cdd:COG3956    1 MENREKPLyAFERLLEIMARLRDPD-GCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  80 AEQGAFTFADVVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAAGNQDDSALAGIARGLPEWQRSTKLQSR 159
Cdd:COG3956   80 EEEGAFDFDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEKGEGRKSVLDGVPRSLPALMRAYKLQKK 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 160 AARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRA 239
Cdd:COG3956  160 AARVGFDWPDVEGVLDKVEEELAELKEALASG----DQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRY 235

                        250       260       270
                 ....*....|....*....|....*....|...
gi 780464027 240 MEAQARTAGTSLNALSLGEQEALWQQAKREERS 272
Cdd:COG3956  236 IEAAAAEQGKSLEDLSLEEMDALWQEAKKAEKE 268
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 16-267 4.60e-95

MazG family protein; This family of prokaryotic proteins has no known function. It includes the uncharacterized protein MazG in E. coli. [Unknown function, General]


Pssm-ID: 273082 [Multi-domain]  Cd Length: 248  Bit Score: 282.48  E-value: 4.60e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   16 VMARLRDREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADVVATLR 95
Cdd:TIGR00444   1 IIAQLRDPENGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027   96 DKLIRRHPHVFAAQPAADAQAVSANWEQIKREERraAGNQDDSALAGIARGLPEWQRSTKLQSRAARVGFDWPGPAPVLE 175
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEK--AQKAQTSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWD 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  176 KLQEEIEELRVEFARGPVadNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAMEAQARTAGTSLNALS 255
Cdd:TIGR00444 159 KVYEELDEVMYEARQAVV--EQNKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVD 236

                         250
                  ....*....|..
gi 780464027  256 LGEQEALWQQAK 267
Cdd:TIGR00444 237 LEEMEELWQQVK 248
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 11-125 1.07e-58

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the N-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer; each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active site and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity; however, this domain does not exhibit an NTPase activity despite containing structural features such as the EEXX(E/D) motif and key basic catalytic residues responsible for nucleotide pyrophosphohydrolysis activity. It is suggested that the N-terminal domain of EcMazG might have a house-cleaning function by hydrolyzing noncanonical NTPs whose incorporation into the nascent DNA leads to increased mutagenesis and DNA damage.


Pssm-ID: 212135  Cd Length: 114  Bit Score: 184.64  E-value: 1.07e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  11 QQLLHVMARLRdREHGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADV 90
Cdd:cd11528    1 ERLVEIVARLR-GPGGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDV 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 780464027  91 VATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIK 125
Cdd:cd11528   80 IDGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 148-267 4.08e-53

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG proteins from Escherichia coli and bacterial homologs'; MazG is a NTP-PPase that hydrolyzes all canonical NTPs into their corresponding nucleoside monophosphates and pyrophosphate. The prototype of this family is MazG proteins from Escherichia coli (EcMazG) that represents the most abundant form consisting two sequence-related domains in tandem, this family corresponding to the C-terminal MazG-like domain. EcMazG functions as a regulator of cellular response to starvation by lowering the cellular concentration of guanosine 3',5'-bispyrophosphate (ppGpp). EcMazG exists as a dimer. Each monomer contains two tandem MazG-like domains with similarly folded globular structures. However, only the C-terminal domain has well-ordered active sites and exhibits an NTPase activity responsible for the regulation of bacterial cell survival under nutritional stress. Divalent ions, such as Mg2+ or Mn2+, are required for activity, along with structural features such as EEXX(E/D) motifs and key basic catalytic residues. It has been shown that the C-terminus NTPase activity is responsible for regulation of bacterial cell survival under nutritional stress.


Pssm-ID: 212136  Cd Length: 116  Bit Score: 170.34  E-value: 4.08e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027 148 PEWQRSTKLQSRAARVGFDWPGPAPVLEKLQEEIEELRVEFARGpvadNQARLEDELGDVLFVCANLARHAKVDVGAALR 227
Cdd:cd11529    1 PALMRAQKLQKRAAKVGFDWPDAEGVLDKVEEELAELKEALASG----DKEEIEEELGDLLFSLVNLARFLGVDPEEALR 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 780464027 228 HANLKFERRFRAMEAQARTAGTSLNALSLGEQEALWQQAK 267
Cdd:cd11529   77 RANRKFERRFRYMEELAAEQGKDLEDLSLEELDALWEEAK 116
PRK12334 PRK12334
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 16-248 1.88e-50

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237065 [Multi-domain]  Cd Length: 277  Bit Score: 169.08  E-value: 1.88e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  16 VMARLRDRehgCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAE--QGAFTFADVVAT 93
Cdd:PRK12334  70 VMDRLRSP---GPWESEQTHRSLARYLLEETYELLDAIESGDRDELREELGDVLLQVLFHARIAEEapEDPFDIDDVAAT 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  94 LRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERRAagnqdDSALAGIARGLPEWQRSTKLQSRAARVGFDWPGPAPv 173
Cdd:PRK12334 147 LVAKLVRRHPHVFADGEAISLEEQLAQWEARKAAEKAR-----TSVLDGVPLGQPALALAAKVLSRARKAGLPVPLAPA- 220

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 780464027 174 leklqeeieelrvefargpvadnqARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRFRAMEAQARTAG 248
Cdd:PRK12334 221 ------------------------EDSEDELGALLLALVAVAVAAGVDAEAALRAAVRDFRDRIRAAERAAAADG 271
PRK12333 PRK12333
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 10-232 1.87e-40

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237064 [Multi-domain]  Cd Length: 204  Bit Score: 141.10  E-value: 1.87e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  10 IQQLLHVMARLRDREhGCPWDVQQTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFAD 89
Cdd:PRK12333   1 MERLLEVMRRLRGPD-GCPWDREQTHESLRPYLLEEAAEAVDALSEGDPQELAEELGDVLLQVAFHSVIAEEEGRFTYPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 780464027  90 VVATLRDKLIRRHPHVFAAQPAADAQAVSANWEQIKREERraaGNQDDSALAGIARGLPEWQRSTKLQSRAARvgfDWPG 169
Cdd:PRK12333  80 VERGIVEKLIRRHPHVFGDVQVSGPEEVVANWQAIKAAER---GGGPRSAAERVPASLGALARAAELQKKLGR---EAGS 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 780464027 170 PAPVLEKLQeeieelrvefargpvadnqarlEDELGDVLFVCANLARHAKVDVGAALRHANLK 232
Cdd:PRK12333 154 REGVIAALE----------------------EGGVAEALWAVVAWARAEGIDPEIALRERTEK 194
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 33-106 6.15e-34

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 119.62  E-value: 6.15e-34
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 780464027   33 QTFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLLLQVVFHSQMAAEQGAFTFADVVATLRDKLIRRHPHVF 106
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
176-237 2.25e-07

NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];


Pssm-ID: 441300  Cd Length: 95  Bit Score: 48.27  E-value: 2.25e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780464027 176 KLQEEIEELRVEFARG------PVADNQARLEDELGDVLFVCANLARHAKVDVGAALRHANLKFERRF 237
Cdd:COG1694   28 ALTEEVGELAEAFQWLtgeqskKDPEKKEELAEELADVLIYLLCLANQLGIDLEEAFEEKMEKNEKRY 95
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 159-215 1.97e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families.


Pssm-ID: 212133  Cd Length: 72  Bit Score: 39.29  E-value: 1.97e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 780464027 159 RAARVGFDWPGPAPVLEKLQEEIEEL-----RVEFARGPVADNQARLEDELGDVLFVCANLA 215
Cdd:cd11523    8 RRERGWDKEEGPETRALKLAEEVGELaeairKEEGYGRSSAEDKENLAEELADVLWNLLILA 69
NTP-PPase_BsYpjD cd11531
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative ...
 174-236 2.86e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain putative pyrophosphatase YpjD from Bacillus subtilis and its bacterial homologs; This family includes a putative pyrophosphatase Ypjd from Bacillus subtilis (BsYpjD) and its homologs. Although its biological role has not been described in detail, BsYpjD shows significant sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, BsYpjD contains a single MazG-like domain.


Pssm-ID: 212138  Cd Length: 93  Bit Score: 39.21  E-value: 2.86e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 780464027 174 LEKLQEEIEELRVEFARG----PVADNQAR-LEDELGDVLFVCANLARHAKVDVGAALRHANLKFERR 236
Cdd:cd11531   25 LARLTEEVGELAREINHRygekPKPGEDEGeLEEELADILFVLTCLANQLGIDLEEAFKRTMEKKETR 92
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 23-74 4.03e-04

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This superfamily contains enzymes that hydrolyze the alpha-beta phosphodiester bond of all canonical NTPs into monophosphate derivatives and pyrophosphate (PPi). Divalent ions, such as Mg2+ ion(s), are essential to activate a proposed water nucleophile and stabilize the charged intermediates to facilitate catalysis. These enzymes share a conserved divalent ion-binding motif EXX[E/D] in their active sites. They also share a highly conserved four-helix bundle, where one face forms the active site, while the other participates in oligomer assembly. The four-helix bundle consists of two central antiparallel alpha-helices that can be contained within a single protomer or form upon dimerization. The superfamily members include dimeric dUTP pyrophosphatases (dUTPases; EC 3.6.1.23), the nonspecific NTP-PPase MazG proteins, HisE-encoded phosphoribosyl ATP pyrophosphohydolase (PRA-PH), fungal histidine biosynthesis trifunctional proteins, and several uncharacterized protein families.


Pssm-ID: 212133  Cd Length: 72  Bit Score: 38.52  E-value: 4.03e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 780464027  23 REHGcpWDVQQTFASIAPYTIEEAYEVADAIDRN---------DLAGLRDELGDLLLQVVF 74
Cdd:cd11523    9 RERG--WDKEEGPETRALKLAEEVGELAEAIRKEegygrssaeDKENLAEELADVLWNLLI 67
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 174-236 2.46e-03

MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in length. It is found in the MazG protein from E. coli. It contains four conserved negatively charged residues that probably form an active site or metal binding site. This domain is found in isolation in some proteins as well as associated with pfam00590. This domain is clearly related to pfam01503 another pyrophosphohydrolase involved in histidine biosynthesis. This family may be structurally related to the NUDIX domain pfam00293 (Bateman A pers. obs.).


Pssm-ID: 427525  Cd Length: 74  Bit Score: 36.04  E-value: 2.46e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 780464027  174 LEKLQEEIEELRVEFARGPVADnqarLEDELGDVLFVCANLARHAK----VDVGAALRHANLKFERR 236
Cdd:pfam03819   7 LPYLIEEVYEVAEAIEKEDLDN----LEEELGDVLLQVLFHANIAEeeggFDLEDVFQRILEKLIRR 69
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 34-69 3.71e-03

Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the histidine biosynthetic pathway.


Pssm-ID: 426294  Cd Length: 83  Bit Score: 36.06  E-value: 3.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 780464027   34 TFASIAPYTIEEAYEVADAIDRNDLAGLRDELGDLL 69
Cdd:pfam01503  23 LAALRAAKIGEEAVELLEAAKAGDLAELADELADLL 58
NTP-PPase_u4 cd11541
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 191-237 5.17e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212148  Cd Length: 91  Bit Score: 35.66  E-value: 5.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 780464027 191 GPVADNQARLEDELGDVLFVCANLARHAKVDVGAALRHaNL-KFERRF 237
Cdd:cd11541   45 GHAPLDKEALAEELGDVLWYLAALANVLGISLEEIAEA-NIaKLRSRY 91
NTP-PPase_u3 cd11540
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 42-69 6.22e-03

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from bacteria and archaea; This family corresponds to a group of uncharacterized hypothetical proteins from bacteria and archaea, showing a high sequence similarity to the dimeric 2-deoxyuridine 5'-triphosphate nucleotidohydrolase (dUTP pyrophosphatase or dUTPase) and NTP-PPase MazG proteins. However, unlike typical tandem-domain MazG proteins, members in this family consist of a single MazG-like domain that contains a well conserved divalent ion-binding motif EXX[E/D].


Pssm-ID: 212147  Cd Length: 76  Bit Score: 35.30  E-value: 6.22e-03
                         10        20
                 ....*....|....*....|....*...
gi 780464027  42 TIEEAYEVADAIDRNDLAGLRDELGDLL 69
Cdd:cd11540   28 LVEEVGELSEAIAKNKQEEIKDSIGDVL 55
 
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