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Conserved domains on  [gi|447086824|ref|WP_001164080|]
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MazG nucleotide pyrophosphohydrolase domain-containing protein [Vibrio cholerae]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase family protein( domain architecture ID 10510847)

nucleoside triphosphate (NTP) pyrophosphohydrolase family protein may hydrolyze the alpha-beta phosphodiester bond of canonical NTPs into monophosphate derivatives and pyrophosphate, similar to Deinococcus radiodurans DR2231 with specific dUTPase activity

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 26-93 3.84e-19

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: 74.94  E-value: 3.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447086824   26 GSSTYLAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWDYLNTILSLEKEAGVKIESVVQRACRKYEER 93
Cdd:pfam03819   2 THETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRR 69
 
Name Accession Description Interval E-value
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 26-93 3.84e-19

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: 74.94  E-value: 3.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447086824   26 GSSTYLAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWDYLNTILSLEKEAGVKIESVVQRACRKYEER 93
Cdd:pfam03819   2 THETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRR 69
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 31-117 4.15e-08

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: 47.85  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824  31 LAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWdylnTILSLEKEAGVKIESVVQRACRKYEERVSAIE-----NGISWDE 105
Cdd:cd11529   27 LDKVEEELAELKEALASGDKEEIEEELGDLLF----SLVNLARFLGVDPEEALRRANRKFERRFRYMEelaaeQGKDLED 102

                         90
                 ....*....|..
gi 447086824 106 VKLKQKKELEQE 117
Cdd:cd11529  103 LSLEELDALWEE 114
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
9-93 3.04e-06

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 42.49  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824   9 EVAKRKSEFDKNNSW--YLGSSTYLAEIKQEVDEVVEEI----------PKNRLCYLEDELGDVLWdYLntiLSLEKEAG 76
Cdd:COG1694    2 ELQKRVRAFIKERGWgqYHSPKNLAAALTEEVGELAEAFqwltgeqskkDPEKKEELAEELADVLI-YL---LCLANQLG 77

                         90
                 ....*....|....*..
gi 447086824  77 VKIESVVQRACRKYEER 93
Cdd:COG1694   78 IDLEEAFEEKMEKNEKR 94
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 31-117 3.12e-06

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 44.38  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824  31 LAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWdylnTILSLEKEAGVKIESVVQRACRKYEERVSAIE-----NGISWDE 105
Cdd:PRK09562 168 LDKVEEEIDELKEALAQGDQAKIEEEFGDLLF----ALVNLARHLGIDPEAALRKANAKFERRFRAVEqlaaaQGKTLED 243

                         90
                 ....*....|..
gi 447086824 106 VKLKQKKELEQE 117
Cdd:PRK09562 244 ASLEEMDALWQE 255
 
Name Accession Description Interval E-value
MazG pfam03819
MazG nucleotide pyrophosphohydrolase domain; This domain is about 100 amino acid residues in ...
 26-93 3.84e-19

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: 74.94  E-value: 3.84e-19
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 447086824   26 GSSTYLAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWDYLNTILSLEKEAGVKIESVVQRACRKYEER 93
Cdd:pfam03819   2 THETLLPYLIEEVYEVAEAIEKEDLDNLEEELGDVLLQVLFHANIAEEEGGFDLEDVFQRILEKLIRR 69
NTP-PPase_MazG_Cterm cd11529
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) C-terminal tandem-domain of MazG ...
 31-117 4.15e-08

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: 47.85  E-value: 4.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824  31 LAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWdylnTILSLEKEAGVKIESVVQRACRKYEERVSAIE-----NGISWDE 105
Cdd:cd11529   27 LDKVEEELAELKEALASGDKEEIEEELGDLLF----SLVNLARFLGVDPEEALRRANRKFERRFRYMEelaaeQGKDLED 102

                         90
                 ....*....|..
gi 447086824 106 VKLKQKKELEQE 117
Cdd:cd11529  103 LSLEELDALWEE 114
MazG COG1694
NTP pyrophosphatase, house-cleaning of non-canonical NTPs [Defense mechanisms];
9-93 3.04e-06

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


Pssm-ID: 441300  Cd Length: 95  Bit Score: 42.49  E-value: 3.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824   9 EVAKRKSEFDKNNSW--YLGSSTYLAEIKQEVDEVVEEI----------PKNRLCYLEDELGDVLWdYLntiLSLEKEAG 76
Cdd:COG1694    2 ELQKRVRAFIKERGWgqYHSPKNLAAALTEEVGELAEAFqwltgeqskkDPEKKEELAEELADVLI-YL---LCLANQLG 77

                         90
                 ....*....|....*..
gi 447086824  77 VKIESVVQRACRKYEER 93
Cdd:COG1694   78 IDLEEAFEEKMEKNEKR 94
mazG PRK09562
nucleoside triphosphate pyrophosphohydrolase; Reviewed
 31-117 3.12e-06

nucleoside triphosphate pyrophosphohydrolase; Reviewed


Pssm-ID: 236569 [Multi-domain]  Cd Length: 262  Bit Score: 44.38  E-value: 3.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824  31 LAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWdylnTILSLEKEAGVKIESVVQRACRKYEERVSAIE-----NGISWDE 105
Cdd:PRK09562 168 LDKVEEEIDELKEALAQGDQAKIEEEFGDLLF----ALVNLARHLGIDPEAALRKANAKFERRFRAVEqlaaaQGKTLED 243

                         90
                 ....*....|..
gi 447086824 106 VKLKQKKELEQE 117
Cdd:PRK09562 244 ASLEEMDALWQE 255
NTP-PPase cd11523
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain superfamily; This ...
 12-66 4.64e-06

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: 41.60  E-value: 4.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 447086824  12 KRKSEFDKNNSW--YLGSSTYLAEIKQEVDEVVEEIPKNR---------LCYLEDELGDVLWDYLN 66
Cdd:cd11523    2 ERIKEFRRERGWdkEEGPETRALKLAEEVGELAEAIRKEEgygrssaedKENLAEELADVLWNLLI 67
YabN COG3956
Uncharacterized conserved protein YabN, contains tetrapyrrole methylase and MazG-like ...
 31-117 1.05e-05

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: 42.79  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 447086824  31 LAEIKQEVDEVVEEIPKNRLCYLEDELGDVLWdylnTILSLEKEAGVKIESVVQRACRKYEERVSAIE-----NGISWDE 105
Cdd:COG3956  174 LDKVEEELAELKEALASGDQEAIEEELGDLLF----ALVNLARHLGIDPEEALRRANRKFERRFRYIEaaaaeQGKSLED 249

                         90
                 ....*....|..
gi 447086824 106 VKLKQKKELEQE 117
Cdd:COG3956  250 LSLEEMDALWQE 261
 
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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