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Conserved domains on  [gi|515720468|ref|WP_017153068|]
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nucleoside triphosphate pyrophosphohydrolase [Bacillus bingmayongensis]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase( domain architecture ID 10183938)

MazG family nucleoside triphosphate (NTP) pyrophosphohydrolase catalyzes the hydrolysis of an NTP, such as ITP, GTP, CTP and UTP, to form the corresponding NMP and diphosphate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
COG4997 COG4997
Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) ...
 3-103 7.38e-40

Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) superfamily [General function prediction only];


:

Pssm-ID: 444021  Cd Length: 108  Bit Score: 128.04  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   3 THNKLIRDRIPEIIEHNGKTPITRILDGKEYIEEIGKKIGEELTEYLEAqSKDHKVEELADLLELINALARYEGITLEDV 82
Cdd:COG4997    4 EYNKLVRDRIPEIIESSGKTCVTRILSDEEYLQALRKKLIEEAQEYAEA-SDEDALEELADLLEVIDAIAEAHGISLEEL 82

                         90       100
                 ....*....|....*....|.
gi 515720468  83 EKIRKQKAEKRGGFQKRIFLV 103
Cdd:COG4997   83 EEIRKEKREERGGFEERIFLI 103
 
Name Accession Description Interval E-value
COG4997 COG4997
Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) ...
 3-103 7.38e-40

Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) superfamily [General function prediction only];


Pssm-ID: 444021  Cd Length: 108  Bit Score: 128.04  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   3 THNKLIRDRIPEIIEHNGKTPITRILDGKEYIEEIGKKIGEELTEYLEAqSKDHKVEELADLLELINALARYEGITLEDV 82
Cdd:COG4997    4 EYNKLVRDRIPEIIESSGKTCVTRILSDEEYLQALRKKLIEEAQEYAEA-SDEDALEELADLLEVIDAIAEAHGISLEEL 82

                         90       100
                 ....*....|....*....|.
gi 515720468  83 EKIRKQKAEKRGGFQKRIFLV 103
Cdd:COG4997   83 EEIRKEKREERGGFEERIFLI 103
NTP-PPase_COG4997 cd11532
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 4-99 2.10e-38

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria; The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show 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, the family contains a single MazG-like domain.


Pssm-ID: 212139  Cd Length: 95  Bit Score: 123.81  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   4 HNKLIRDRIPEIIEHNGKTPITRILDGKEYIEEIGKKIGEELTEYLEAQSKDhKVEELADLLELINALARYEGITLEDVE 83
Cdd:cd11532    1 YNKLVRDRIPEIIRASGKTCVTRILSDEEYLEALKKKLVEEAAEYAEAKTED-SLEELADLLEVIYAIAEAHGISLEELE 79

                         90
                 ....*....|....*.
gi 515720468  84 KIRKQKAEKRGGFQKR 99
Cdd:cd11532   80 KVREKKREERGGFEKR 95
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 36-85 3.59e-06

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 41.45  E-value: 3.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515720468   36 EIGKKIGEELTEYLEAQSKDHKVE---ELADLLELINALARYEGITLEDVEKI 85
Cdd:pfam01503  26 LRAAKIGEEAVELLEAAKAGDLAEladELADLLYHTYGLLVLQGVDLDAVFEE 78
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 34-84 3.93e-06

phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than pfam01503, as some paralogs that appear to be functionally distinct are excluded from this model. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 274477  Cd Length: 84  Bit Score: 41.32  E-value: 3.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515720468   34 IEEIGKKIGEELTEYLEA---QSKDHKVEELADLLELINALARYEGITLEDVEK 84
Cdd:TIGR03188  29 LDKILKKVGEEAVEVIIAaknGDKEELVYEAADLLYHLLVLLAAQGVSLEDVLA 82
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 8-87 1.95e-05

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 41.73  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   8 IRDRIPEIIEHNGKTPITRILDGKEyiEEIGKKIGEELTE----YLEAQSKDHKVEELADLLELINALARYEGITLEDV- 82
Cdd:PLN02346 171 IQQRKEEAVPQGGKPSWTKRLLQDP--ELLCSKIREEAGElcqtLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVl 248


                 ....*
gi 515720468  83 EKIRK 87
Cdd:PLN02346 249 EVLRK 253
 
Name Accession Description Interval E-value
COG4997 COG4997
Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) ...
 3-103 7.38e-40

Predicted house-cleaning noncanonical NTP pyrophosphatase, all-alpha NTP-PPase (MazG) superfamily [General function prediction only];


Pssm-ID: 444021  Cd Length: 108  Bit Score: 128.04  E-value: 7.38e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   3 THNKLIRDRIPEIIEHNGKTPITRILDGKEYIEEIGKKIGEELTEYLEAqSKDHKVEELADLLELINALARYEGITLEDV 82
Cdd:COG4997    4 EYNKLVRDRIPEIIESSGKTCVTRILSDEEYLQALRKKLIEEAQEYAEA-SDEDALEELADLLEVIDAIAEAHGISLEEL 82

                         90       100
                 ....*....|....*....|.
gi 515720468  83 EKIRKQKAEKRGGFQKRIFLV 103
Cdd:COG4997   83 EEIRKEKREERGGFEERIFLI 103
NTP-PPase_COG4997 cd11532
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 4-99 2.10e-38

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of uncharacterized proteins from archaea and bacteria; The family includes some uncharacterized hypothetical proteins from archaea and bacteria. Although their biological roles remain unclear, the family members show 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, the family contains a single MazG-like domain.


Pssm-ID: 212139  Cd Length: 95  Bit Score: 123.81  E-value: 2.10e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   4 HNKLIRDRIPEIIEHNGKTPITRILDGKEYIEEIGKKIGEELTEYLEAQSKDhKVEELADLLELINALARYEGITLEDVE 83
Cdd:cd11532    1 YNKLVRDRIPEIIRASGKTCVTRILSDEEYLEALKKKLVEEAAEYAEAKTED-SLEELADLLEVIYAIAEAHGISLEELE 79

                         90
                 ....*....|....*.
gi 515720468  84 KIRKQKAEKRGGFQKR 99
Cdd:cd11532   80 KVREKKREERGGFEKR 95
NTP-PPase_HisIE_like cd11534
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 34-84 1.47e-06

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase (HisIE or PRATP-PH) and its homologs; This family includes Escherichia coli phosphoribosyl-ATP pyrophosphohydrolase, HisIE, and its homologs from all three kingdoms of life. E. coli HisIE is encoded by the hisIE gene, which is formed by hisE gene fused to hisl. HisIE is a bifunctional enzyme responsible for the second and third steps of the histidine-biosynthesis pathway. Its N-terminal and C-terminal domains have phosphoribosyl-AMP cyclohydrolase (HisI) and phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH) activity, respectively. This family corresponds to the C-terminal domain of HisIE and includes many hisE gene encoding proteins, all of which show significant sequence similarity to Mycobacterium tuberculosis phosphoribosyl-ATP pyrophosphohydrolase (HisE or PRATP-PH). These proteins may be responsible for only the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate.


Pssm-ID: 212141  Cd Length: 84  Bit Score: 42.45  E-value: 1.47e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515720468  34 IEEIGKKIGEELTEYLEA---QSKDHKVEELADLLELINALARYEGITLEDVEK 84
Cdd:cd11534   29 LDKILKKVGEEAVEVIIAaknGDKEELVYEAADLLYHLLVLLAYRGISLEDVLE 82
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 36-85 3.59e-06

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 41.45  E-value: 3.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 515720468   36 EIGKKIGEELTEYLEAQSKDHKVE---ELADLLELINALARYEGITLEDVEKI 85
Cdd:pfam01503  26 LRAAKIGEEAVELLEAAKAGDLAEladELADLLYHTYGLLVLQGVDLDAVFEE 78
histidine_hisI TIGR03188
phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, ...
 34-84 3.93e-06

phosphoribosyl-ATP pyrophosphohydrolase; This enzyme, phosphoribosyl-ATP pyrophosphohydrolase, catalyses the second step in the histidine biosynthesis pathway. It often occurs as a fusion protein. This model a somewhat narrower scope than pfam01503, as some paralogs that appear to be functionally distinct are excluded from this model. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 274477  Cd Length: 84  Bit Score: 41.32  E-value: 3.93e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 515720468   34 IEEIGKKIGEELTEYLEA---QSKDHKVEELADLLELINALARYEGITLEDVEK 84
Cdd:TIGR03188  29 LDKILKKVGEEAVEVIIAaknGDKEELVYEAADLLYHLLVLLAAQGVSLEDVLA 82
NTP-PPase_His4 cd11546
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like ...
 40-84 1.40e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in His4-like fungal histidine biosynthesis trifunctional proteins and their homologs; This family includes fungal histidine biosynthesis trifunctional proteins and their homologs from eukaryotes and bacteria. Some family members contain three domains responsible for phosphoribosyl-AMP cyclohydrolase (PRAMP-CH), phosphoribosyl-ATP pyrophosphohydrolase (PRATP-PH), and histidinol dehydrogenase (Histidinol-DH) activity, respectively. Some others do not have Histidinol-DH domain, but have an additional N-terminal TIM phosphate binding domain. This family corresponds to the domain for PRATP-PH activity, which shows significant sequence similarity to Mycobacterium tuberculosis PRATP-PH that catalyzes the second step in the histidine-biosynthetic pathway, irreversibly hydrolyzing phosphoribosyl-ATP (PRATP) to phosphoribosyl-AMP (PRAMP) and pyrophosphate.


Pssm-ID: 212153  Cd Length: 84  Bit Score: 39.96  E-value: 1.40e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 515720468  40 KIGEELTEYLEAQSKDHKVEELADLLELINALARYEGITLEDVEK 84
Cdd:cd11546   35 KIMEEAEELCEAKTKDEVAWEAADLLYFALVRCVAAGVSLDDVER 79
PLN02346 PLN02346
histidine biosynthesis bifunctional protein hisIE
 8-87 1.95e-05

histidine biosynthesis bifunctional protein hisIE


Pssm-ID: 215196 [Multi-domain]  Cd Length: 271  Bit Score: 41.73  E-value: 1.95e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 515720468   8 IRDRIPEIIEHNGKTPITRILDGKEyiEEIGKKIGEELTE----YLEAQSKDHKVEELADLLELINALARYEGITLEDV- 82
Cdd:PLN02346 171 IQQRKEEAVPQGGKPSWTKRLLQDP--ELLCSKIREEAGElcqtLEENEGKERTASEMADVLYHAMVLLAKQGVKMEDVl 248


                 ....*
gi 515720468  83 EKIRK 87
Cdd:PLN02346 249 EVLRK 253
hisE PRK00400
phosphoribosyl-ATP diphosphatase;
34-84 2.44e-05

phosphoribosyl-ATP diphosphatase;


Pssm-ID: 179005  Cd Length: 105  Bit Score: 39.76  E-value: 2.44e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 515720468  34 IEEIGKKIGEELTEYL---EAQSKDHKVEELADLLELINALARYEGITLEDVEK 84
Cdd:PRK00400  33 LDKILKKVGEEATEVViaaKDGDREELVYEIADLLYHLLVLLAARGISLEDVLA 86
HisI2 COG0140
Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; ...
 34-99 2.88e-05

Phosphoribosyl-ATP pyrophosphohydrolase [Amino acid transport and metabolism]; Phosphoribosyl-ATP pyrophosphohydrolase is part of the Pathway/BioSystem: Histidine biosynthesis


Pssm-ID: 439910  Cd Length: 103  Bit Score: 39.73  E-value: 2.88e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 515720468  34 IEEIGKKIGEELTEYLEA---QSKDHKVEELADLLELINALARYEGITLEDVEKIRKQKAEKRGGFQKR 99
Cdd:COG0140   33 IDKILKKVGEEAVEVVIAaknGDKEELIYEAADLLYHLLVLLAARGISLDDVLAELARRHGLSGLEEKA 101
PRK02759 PRK02759
bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;
34-84 1.33e-03

bifunctional phosphoribosyl-AMP cyclohydrolase/phosphoribosyl-ATP diphosphatase HisIE;


Pssm-ID: 235067 [Multi-domain]  Cd Length: 203  Bit Score: 36.29  E-value: 1.33e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 515720468  34 IEEIGKKIGEELTEY-LEAQSKDHK--VEELADLL-ELINALArYEGITLEDVEK 84
Cdd:PRK02759 144 TKRIAQKVGEEAVEVvLAAKNNDKEelINEAADLLyHLLVLLA-DQGLSLSDVIA 197
Histone_HNS pfam00816
H-NS histone family;
43-99 2.26e-03

H-NS histone family;


Pssm-ID: 425884 [Multi-domain]  Cd Length: 91  Bit Score: 34.55  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 515720468   43 EELTEYLEAQSKDHKVEELADLLELINALARYEGITLEDVEKIRKQKAEKRGGFQKR 99
Cdd:pfam00816   2 EALIAELEKEIEALRKRERKEVLAQIRELAAEYGLTLEELGGAAKAARKAKAKAAKV 58
 
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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