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Conserved domains on  [gi|490310870|ref|WP_004205577|]
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MULTISPECIES: nucleoside triphosphate pyrophosphohydrolase [Klebsiella]

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

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List of domain hits

 Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-262 2.83e-163

nucleoside triphosphate pyrophosphohydrolase; Reviewed


:

Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 452.70  E-value: 2.83e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   1 MTQIDRLLGIMRRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFN 80
Cdd:PRK09562   6 SEAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  81 FDDICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKsaeRAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDWT 160
Cdd:PRK09562  86 FADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIK---AEERAESSVLDGIPRGLPALMRAYKIQKKAARVGFDWE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 161 SLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGLE 240
Cdd:PRK09562 163 SLEPVLDKVEEEIDELKEALAQG--DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKT 240

                        250       260
                 ....*....|....*....|..
gi 490310870 241 MTGVDLDTMEEVWQQVKRQETD 262
Cdd:PRK09562 241 LEDASLEEMDALWQEAKRQEKA 262
 
Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-262 2.83e-163

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 452.70  E-value: 2.83e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   1 MTQIDRLLGIMRRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFN 80
Cdd:PRK09562   6 SEAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  81 FDDICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKsaeRAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDWT 160
Cdd:PRK09562  86 FADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIK---AEERAESSVLDGIPRGLPALMRAYKIQKKAARVGFDWE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 161 SLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGLE 240
Cdd:PRK09562 163 SLEPVLDKVEEEIDELKEALAQG--DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKT 240

                        250       260
                 ....*....|....*....|..
gi 490310870 241 MTGVDLDTMEEVWQQVKRQETD 262
Cdd:PRK09562 241 LEDASLEEMDALWQEAKRQEKA 262
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 1-260 2.01e-155

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: 2.01e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   1 MTQIDRLLGIMRRLRDPEnGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFN 80
Cdd:COG3956    8 LYAFERLLEIMARLRDPD-GCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  81 FDDICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKSAERAEKAQ--HSALDDIPHSLPALMRAHKIQRRCSAVGFD 158
Cdd:COG3956   87 FDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEKGEgrKSVLDGVPRSLPALMRAYKLQKKAARVGFD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 159 WTSLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARG 238
Cdd:COG3956  167 WPDVEGVLDKVEEELAELKEALASG--DQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQG 244

                        250       260
                 ....*....|....*....|..
gi 490310870 239 LEMTGVDLDTMEEVWQQVKRQE 260
Cdd:COG3956  245 KSLEDLSLEEMDALWQEAKKAE 266
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 10-257 7.60e-141

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: 395.34  E-value: 7.60e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   10 IMRRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDICAAIS 89
Cdd:TIGR00444   1 IIAQLRDPENGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   90 DKLERRHPHIFADATAGNSSEVLARWEQIKSAERAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDWTSLGPVLDKV 169
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAQTSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  170 HEEIDEVMHEAQQAVVDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGLEMTGVDLDTM 249
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEQNKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVDLEEM 240


                  ....*...
gi 490310870  250 EEVWQQVK 257
Cdd:TIGR00444 241 EELWQQVK 248
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 5-119 7.31e-59

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: 182.71  E-value: 7.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   5 DRLLGIMRRLRDPeNGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDI 84
Cdd:cd11528    1 ERLVEIVARLRGP-GGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDV 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490310870  85 CAAISDKLERRHPHIFADATAGNSSEVLARWEQIK 119
Cdd:cd11528   80 IDGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 27-100 1.36e-29

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: 106.14  E-value: 1.36e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490310870   27 QTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDICAAISDKLERRHPHIF 100
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
 
Name Accession Description Interval E-value
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 1-262 2.83e-163

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 452.70  E-value: 2.83e-163
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   1 MTQIDRLLGIMRRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFN 80
Cdd:PRK09562   6 SEAIDRLLEIMARLRDPEGGCPWDKEQTFASLAPYTIEEAYEVVDAIERGDLDDLREELGDLLLQVVFHAQMAEEQGAFD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  81 FDDICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKsaeRAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDWT 160
Cdd:PRK09562  86 FADVVEAISDKLIRRHPHVFGDVEAESSEEVLANWEQIK---AEERAESSVLDGIPRGLPALMRAYKIQKKAARVGFDWE 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 161 SLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGLE 240
Cdd:PRK09562 163 SLEPVLDKVEEEIDELKEALAQG--DQAKIEEEFGDLLFALVNLARHLGIDPEAALRKANAKFERRFRAVEQLAAAQGKT 240

                        250       260
                 ....*....|....*....|..
gi 490310870 241 MTGVDLDTMEEVWQQVKRQETD 262
Cdd:PRK09562 241 LEDASLEEMDALWQEAKRQEKA 262
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 1-260 2.01e-155

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: 2.01e-155
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   1 MTQIDRLLGIMRRLRDPEnGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFN 80
Cdd:COG3956    8 LYAFERLLEIMARLRDPD-GCPWDREQTHESLRPYTIEEAYEVADAIERGDLDELKEELGDLLLQVVFHAQIAEEEGAFD 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  81 FDDICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKSAERAEKAQ--HSALDDIPHSLPALMRAHKIQRRCSAVGFD 158
Cdd:COG3956   87 FDDVIDGISEKLIRRHPHVFGDVEVEDAEEVLANWEKIKAQEKAEKGEgrKSVLDGVPRSLPALMRAYKLQKKAARVGFD 166

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 159 WTSLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARG 238
Cdd:COG3956  167 WPDVEGVLDKVEEELAELKEALASG--DQEAIEEELGDLLFALVNLARHLGIDPEEALRRANRKFERRFRYIEAAAAEQG 244

                        250       260
                 ....*....|....*....|..
gi 490310870 239 LEMTGVDLDTMEEVWQQVKRQE 260
Cdd:COG3956  245 KSLEDLSLEEMDALWQEAKKAE 266
mazG TIGR00444
MazG family protein; This family of prokaryotic proteins has no known function. It includes ...
 10-257 7.60e-141

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: 395.34  E-value: 7.60e-141
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   10 IMRRLRDPENGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDICAAIS 89
Cdd:TIGR00444   1 IIAQLRDPENGCPWDKKQTFQSLIPYTLEETYEVLEAIAREDFDDLREELGDLLLQVVFYAQMAQEEGYFDFDDVCAGIS 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   90 DKLERRHPHIFADATAGNSSEVLARWEQIKSAERAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDWTSLGPVLDKV 169
Cdd:TIGR00444  81 EKLVRRHPHVFADVKAEDESEVLARWEQIKAEEKAQKAQTSALDDVPRTLPALMRAAKIQKRCAKVGFDWEDVSPVWDKV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  170 HEEIDEVMHEAQQAVVDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGLEMTGVDLDTM 249
Cdd:TIGR00444 161 YEELDEVMYEARQAVVEQNKLEEEMGDLLFATVNLARHLKTDAEIALQKANEKFERRFREVERIVAARGLELTGVDLEEM 240


                  ....*...
gi 490310870  250 EEVWQQVK 257
Cdd:TIGR00444 241 EELWQQVK 248
PRK12334 PRK12334
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 7-239 7.47e-61

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237065 [Multi-domain]  Cd Length: 277  Bit Score: 193.35  E-value: 7.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   7 LLGIMRRLRDPengCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGR--FNFDDI 84
Cdd:PRK12334  67 AVAVMDRLRSP---GPWESEQTHRSLARYLLEETYELLDAIESGDRDELREELGDVLLQVLFHARIAEEAPEdpFDIDDV 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  85 CAAISDKLERRHPHIFADATAGNSSEVLARWEQIKsaeRAEKAQHSALDDIPHSLPALMRAHKIQRRCSAVGFDwtslgp 164
Cdd:PRK12334 144 AATLVAKLVRRHPHVFADGEAISLEEQLAQWEARK---AAEKARTSVLDGVPLGQPALALAAKVLSRARKAGLP------ 214

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490310870 165 vLDKVHEEIDevmheaqqavvdeaklEEEVGDLLFATVNLSRHLGVKAEVALQKANRKFERRFREVERIVAARGL 239
Cdd:PRK12334 215 -VPLAPAEDS----------------EDELGALLLALVAVAVAAGVDAEAALRAAVRDFRDRIRAAERAAAADGL 272
NTP-PPase_MazG_Nterm cd11528
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) N-terminal tandem-domain of MazG ...
 5-119 7.31e-59

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: 182.71  E-value: 7.31e-59
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   5 DRLLGIMRRLRDPeNGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDI 84
Cdd:cd11528    1 ERLVEIVARLRGP-GGCPWDREQTHESLRPYLLEEAYELVEAIEEGDPDNLREELGDVLLQVLFHAQIAEEEGAFDLDDV 79

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 490310870  85 CAAISDKLERRHPHIFADATAGNSSEVLARWEQIK 119
Cdd:cd11528   80 IDGLTEKLIRRHPHVFGDEKAETAEEVLRNWEKIK 114
PRK12333 PRK12333
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 4-222 1.93e-55

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 237064 [Multi-domain]  Cd Length: 204  Bit Score: 176.92  E-value: 1.93e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870   4 IDRLLGIMRRLRDPeNGCPWDKEQTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDD 83
Cdd:PRK12333   1 MERLLEVMRRLRGP-DGCPWDREQTHESLRPYLLEEAAEAVDALSEGDPQELAEELGDVLLQVAFHSVIAEEEGRFTYPD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  84 ICAAISDKLERRHPHIFADATAGNSSEVLARWEQIKSAERaEKAQHSALDDIPHSLPALMRAHKIQRRcsaVGFDWTSlg 163
Cdd:PRK12333  80 VERGIVEKLIRRHPHVFGDVQVSGPEEVVANWQAIKAAER-GGGPRSAAERVPASLGALARAAELQKK---LGREAGS-- 153

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 490310870 164 pvldkvHEEIDEVMHEAqqavvdeakleeEVGDLLFATVNLSRHLGVKAEVALQKANRK 222
Cdd:PRK12333 154 ------REGVIAALEEG------------GVAEALWAVVAWARAEGIDPEIALRERTEK 194
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 140-257 1.00e-51

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: 164.57  E-value: 1.00e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870 140 PALMRAHKIQRRCSAVGFDWTSLGPVLDKVHEEIDEVMHEAQQAvvDEAKLEEEVGDLLFATVNLSRHLGVKAEVALQKA 219
Cdd:cd11529    1 PALMRAQKLQKRAAKVGFDWPDAEGVLDKVEEELAELKEALASG--DKEEIEEELGDLLFSLVNLARFLGVDPEEALRRA 78

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 490310870 220 NRKFERRFREVERIVAARGLEMTGVDLDTMEEVWQQVK 257
Cdd:cd11529   79 NRKFERRFRYMEELAAEQGKDLEDLSLEELDALWEEAK 116
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 27-100 1.36e-29

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: 106.14  E-value: 1.36e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490310870   27 QTFATIAPYTLEETYEVLDAISREDFDDLRGELGDLLFQVVFYAQMAQEEGRFNFDDICAAISDKLERRHPHIF 100
Cdd:pfam03819   1 QTHETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRRHPHVF 74
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 22-73 8.77e-05

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: 40.06  E-value: 8.77e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490310870  22 PWDKEQTFATIAPYTLEETYEVLDAI---------SREDFDDLRGELGDLLFQVVFYAQMA 73
Cdd:cd11523   12 GWDKEEGPETRALKLAEEVGELAEAIrkeegygrsSAEDKENLAEELADVLWNLLILANKL 72
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 171-226 6.86e-04

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: 37.58  E-value: 6.86e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 490310870  171 EEIDEVMHEAQQavVDEAKLEEEVGDLLFATVNLS----RHLGVKAEVALQKANRKFERR 226
Cdd:pfam03819  12 EEVYEVAEAIEK--EDLDNLEEELGDVLLQVLFHAniaeEEGGFDLEDVFQRILEKLIRR 69
 
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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