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Conserved domains on  [gi|378975818|ref|YP_005220935|]
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hypothetical protein (plasmid) [Klebsiella pneumoniae subsp. pneumoniae HS11286]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase family protein( domain architecture ID 10183930)

nucleoside triphosphate pyrophosphohydrolase (NTP-PPase) family protein may hydrolyze the alpha-beta phosphodiester bond of canonical NTPs into monophosphate derivatives and pyrophosphate (PPi)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MazG2 super family cl44111
NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];
39-280 1.12e-14

NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];


The actual alignment was detected with superfamily member COG4696:

Pssm-ID: 443731  Cd Length: 130  Bit Score: 69.10  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPT---PELLRLRAKLIHEEaVEEGLPAAKKGDMQGLLDAMADFLYVGVGTMvaikgglstgm 115
Cdd:COG4696    7 FNLVKEFHRTFDLPILETPTapsEERAKLRASLLAEE-LVELLEAAEEGDLVEVADALGDLLYVLYGTI----------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 116 syytqeqsvdrfihtimvpgntvfddmaipfneaeeaalmlaaladkLEHnkvgdaeliqdlrrvmnkiyvacmmvyrla 195
Cdd:COG4696   75 -----------------------------------------------LEH------------------------------ 77

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 196 eflGVDVVELVAEIHRSNMTKLWPaDAEARrlavesckydkndlgfrhadgtdmmigYRlSDGKILKSPTYSDVDLSRFL 275
Cdd:COG4696   78 ---GIDLEAVFDEVHRSNMSKLGP-DGKPI---------------------------YR-EDGKVLKGPNYFPPDIKAEL 125


                 ....*
gi 378975818 276 EQAQA 280
Cdd:COG4696  126 ERQKQ 130
 
Name Accession Description Interval E-value
MazG2 COG4696
NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];
39-280 1.12e-14

NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];


Pssm-ID: 443731  Cd Length: 130  Bit Score: 69.10  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPT---PELLRLRAKLIHEEaVEEGLPAAKKGDMQGLLDAMADFLYVGVGTMvaikgglstgm 115
Cdd:COG4696    7 FNLVKEFHRTFDLPILETPTapsEERAKLRASLLAEE-LVELLEAAEEGDLVEVADALGDLLYVLYGTI----------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 116 syytqeqsvdrfihtimvpgntvfddmaipfneaeeaalmlaaladkLEHnkvgdaeliqdlrrvmnkiyvacmmvyrla 195
Cdd:COG4696   75 -----------------------------------------------LEH------------------------------ 77

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 196 eflGVDVVELVAEIHRSNMTKLWPaDAEARrlavesckydkndlgfrhadgtdmmigYRlSDGKILKSPTYSDVDLSRFL 275
Cdd:COG4696   78 ---GIDLEAVFDEVHRSNMSKLGP-DGKPI---------------------------YR-EDGKVLKGPNYFPPDIKAEL 125


                 ....*
gi 378975818 276 EQAQA 280
Cdd:COG4696  126 ERQKQ 130
NTP-PPase_DR2231_like cd11530
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 39-106 2.49e-12

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.


Pssm-ID: 212137  Cd Length: 88  Bit Score: 61.52  E-value: 2.49e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPTP--ELLRLRAKLIHEEaVEEGLPAAKKGDMQGLLDAMADFLYVGVGTMVA 106
Cdd:cd11530    1 LADVREFHRAFGLPVAEQPTLsdEDLALRQALLAEE-LAELAEALKKGDMVELADALADLLYVAYGTAVE 69
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 42-106 2.70e-12

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 61.48  E-value: 2.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378975818   42 VDQFHELFQHPRRVMP---TPELLRLRAKLIHEEAVEEgLPAAKKGDMQGLLDAMADFLYVGVGTMVA 106
Cdd:pfam01503   1 VREFHRTIGDRKPETPegsTAELAALRAAKIGEEAVEL-LEAAKAGDLAELADELADLLYHTYGLLVL 67
 
Name Accession Description Interval E-value
MazG2 COG4696
NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];
39-280 1.12e-14

NTP pyrophosphatase, MazG superfamily [Nucleotide transport and metabolism];


Pssm-ID: 443731  Cd Length: 130  Bit Score: 69.10  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPT---PELLRLRAKLIHEEaVEEGLPAAKKGDMQGLLDAMADFLYVGVGTMvaikgglstgm 115
Cdd:COG4696    7 FNLVKEFHRTFDLPILETPTapsEERAKLRASLLAEE-LVELLEAAEEGDLVEVADALGDLLYVLYGTI----------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 116 syytqeqsvdrfihtimvpgntvfddmaipfneaeeaalmlaaladkLEHnkvgdaeliqdlrrvmnkiyvacmmvyrla 195
Cdd:COG4696   75 -----------------------------------------------LEH------------------------------ 77

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818 196 eflGVDVVELVAEIHRSNMTKLWPaDAEARrlavesckydkndlgfrhadgtdmmigYRlSDGKILKSPTYSDVDLSRFL 275
Cdd:COG4696   78 ---GIDLEAVFDEVHRSNMSKLGP-DGKPI---------------------------YR-EDGKVLKGPNYFPPDIKAEL 125


                 ....*
gi 378975818 276 EQAQA 280
Cdd:COG4696  126 ERQKQ 130
NTP-PPase_DR2231_like cd11530
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 39-106 2.49e-12

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family includes a MazG-like NTP-PPase from Deinococcus radiodurans (DR2231), a putative NTP-PPase YP_001813558.1 from Exiguobacterium sibiricum and their bacterial homologs. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It can hydrolyze dUTP into dUMP. DR2231-like proteins contain a well conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for the all-alpha-helical NTP-PPase superfamily. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer. It potentially prefers to hydrolyze dCTPs or its derivatives. YP_001813558.1-like proteins contain a variant divalent ion binding motif, EXXEX(12-28)AXXD.


Pssm-ID: 212137  Cd Length: 88  Bit Score: 61.52  E-value: 2.49e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPTP--ELLRLRAKLIHEEaVEEGLPAAKKGDMQGLLDAMADFLYVGVGTMVA 106
Cdd:cd11530    1 LADVREFHRAFGLPVAEQPTLsdEDLALRQALLAEE-LAELAEALKKGDMVELADALADLLYVAYGTAVE 69
PRA-PH pfam01503
Phosphoribosyl-ATP pyrophosphohydrolase; This enzyme catalyzes the second step in the ...
 42-106 2.70e-12

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


Pssm-ID: 426294  Cd Length: 83  Bit Score: 61.48  E-value: 2.70e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 378975818   42 VDQFHELFQHPRRVMP---TPELLRLRAKLIHEEAVEEgLPAAKKGDMQGLLDAMADFLYVGVGTMVA 106
Cdd:pfam01503   1 VREFHRTIGDRKPETPegsTAELAALRAAKIGEEAVEL-LEAAKAGDLAELADELADLLYHTYGLLVL 67
NTP-PPase_YP_001813558 cd11545
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 39-105 5.10e-06

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Exiguobacterium sibiricum YP_001813558.1 protein and its bacterial homologs; This family contains a putative NTP_PPase (YP_001813558.1) from Exiguobacterium sibiricum and its bacterial homologs. Unlike normal dimeric dUTPase-like proteins with a central four-helix bundle forming the active site, YP_001813558.1 displays a very unusual interlaced segment-swapped dimer that might be important for it to adapt to an extremely cold environment. Moreover, structural analysis and comparisons indicate that YP_001813558.1 potentially prefers to hydrolyze dCTPs or its derivatives.


Pssm-ID: 212152  Cd Length: 115  Bit Score: 44.63  E-value: 5.10e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 378975818  39 YKMVDQFHELFQHPRRVMPTP---ELLRLRAKLIHEEAVEEgLPAAKkgdmqglLDAMADFLYVGVGTMV 105
Cdd:cd11545    2 YEQVKEFHEKFGHPVSEQPTAlpeERAVARAGWMLEELVEF-LYASQ-------ADALIDLIYFAYGSFV 63
NTP-PPase_DR2231 cd11544
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in ...
 41-103 2.34e-05

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in Deinococcus radiodurans DR2231 protein and its bacterial homologs; This family corresponds to the DR2231 protein, a MazG-like NTP-PPase from Deinococcus radiodurans, and its bacterial homologs. All family members contain a well-conserved divalent ion binding motif, EXXEX(12-28)EXXD, which is the identity signature for all-alpha-helical NTP-PPase superfamily. DR2231 shows significant structural resemblance to MazG proteins, but is functionally related to the dimeric dUTPases. It might be an evolutionary precursor of dimeric dUTPases with very high specificity in hydrolyzing dUTP into dUMP, but an inability to hydrolyze dTTP, a typical feature of dUTPases. Moreover, unlike the dUPase monomer containing a single active site, the DR2231 protein dimer holds two putative active sites.


Pssm-ID: 212151  Cd Length: 116  Bit Score: 42.91  E-value: 2.34e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 378975818  41 MVDQFHELFQHPRRVMPT---PELLRLRAKLIHEEAVeEGLPAAKKGDMQGLLDAMADFLYVGVGT 103
Cdd:cd11544    4 RVREFHRAIGADLPETPTlppPALLRLRQTLLAEEAA-EVRAAIDHGDLVPLAHELADLLYVTYGT 68
 
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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