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Conserved domains on  [gi|2026149035|ref|YP_010038043|]
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pyrophosphatase [Pseudomonas phage Persinger]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase family protein( domain architecture ID 10183984)

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
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 59-153 5.93e-41

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: 212149  Cd Length: 99  Bit Score: 132.83  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026149035  59 CHGLAKRAGWWHDLQTGEpkdRNDGEMIALMHSELSEALEGLRKDRQDDHLPHRRSVEVELADTLVRIFDYAGARGLDLA 138
Cdd:cd11542     8 AHENAVAHGWWDDPRTGN---NNFGELLMLIHSEVSEALEGLRKGLMDDKLPHRPMIEVELADAVIRIFDTAGGLGIDLE 84

                          90
                  ....*....|....*
gi 2026149035 139 GALVEKLAYNAKRAD 153
Cdd:cd11542    85 GAIAEKMAYNKNRPD 99
 
Name Accession Description Interval E-value
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 59-153 5.93e-41

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: 212149  Cd Length: 99  Bit Score: 132.83  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026149035  59 CHGLAKRAGWWHDLQTGEpkdRNDGEMIALMHSELSEALEGLRKDRQDDHLPHRRSVEVELADTLVRIFDYAGARGLDLA 138
Cdd:cd11542     8 AHENAVAHGWWDDPRTGN---NNFGELLMLIHSEVSEALEGLRKGLMDDKLPHRPMIEVELADAVIRIFDTAGGLGIDLE 84

                          90
                  ....*....|....*
gi 2026149035 139 GALVEKLAYNAKRAD 153
Cdd:cd11542    85 GAIAEKMAYNKNRPD 99
 
Name Accession Description Interval E-value
NTP-PPase_u5 cd11542
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in a group of ...
 59-153 5.93e-41

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: 212149  Cd Length: 99  Bit Score: 132.83  E-value: 5.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2026149035  59 CHGLAKRAGWWHDLQTGEpkdRNDGEMIALMHSELSEALEGLRKDRQDDHLPHRRSVEVELADTLVRIFDYAGARGLDLA 138
Cdd:cd11542     8 AHENAVAHGWWDDPRTGN---NNFGELLMLIHSEVSEALEGLRKGLMDDKLPHRPMIEVELADAVIRIFDTAGGLGIDLE 84

                          90
                  ....*....|....*
gi 2026149035 139 GALVEKLAYNAKRAD 153
Cdd:cd11542    85 GAIAEKMAYNKNRPD 99
 
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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