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Conserved domains on  [gi|501464149|ref|WP_012487594|]
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dUTP diphosphatase [Cellvibrio japonicus]

Protein Classification

nucleoside triphosphate pyrophosphohydrolase family protein( domain architecture ID 96940)

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
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 6-160 1.37e-49

Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily is part of the Pathway/BioSystem: Thymidylate biosynthesis


:

Pssm-ID: 443588  Cd Length: 163  Bit Score: 158.53  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149   6 QQIRIMLELQDGMNTRVNAD----WHQQGYEWYRAIWVECAELMDHYG-WKWWKKQSPD-TDQVALELIDIWHFGLSILL 79
Cdd:COG4508    1 MNLKKLFEMQKELDDRIEEEhgleGEDLFDKKYLALLVELGELANETRcFKFWSKKPPSpKEVILEEYVDGLHFILSLGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149  80 QSGASLDEIIARIERELVIRTD-EQDFRLDLEQFAAaTLADKQFH--IGLFARLMAGVSLSFDQLYRGYVGKNVLNFFRQ 156
Cdd:COG4508   81 ELGYDLLELAAPMEAELKSLTEqFLDVYEAITAFAK-NLTKKNYQelFALFLQLGYALGFTEEDIEKAYLGKNELNHFRQ 159


                 ....
gi 501464149 157 DHGY 160
Cdd:COG4508  160 DNGY 163
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 6-160 1.37e-49

Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 443588  Cd Length: 163  Bit Score: 158.53  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149   6 QQIRIMLELQDGMNTRVNAD----WHQQGYEWYRAIWVECAELMDHYG-WKWWKKQSPD-TDQVALELIDIWHFGLSILL 79
Cdd:COG4508    1 MNLKKLFEMQKELDDRIEEEhgleGEDLFDKKYLALLVELGELANETRcFKFWSKKPPSpKEVILEEYVDGLHFILSLGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149  80 QSGASLDEIIARIERELVIRTD-EQDFRLDLEQFAAaTLADKQFH--IGLFARLMAGVSLSFDQLYRGYVGKNVLNFFRQ 156
Cdd:COG4508   81 ELGYDLLELAAPMEAELKSLTEqFLDVYEAITAFAK-NLTKKNYQelFALFLQLGYALGFTEEDIEKAYLGKNELNHFRQ 159


                 ....
gi 501464149 157 DHGY 160
Cdd:COG4508  160 DNGY 163
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 8-160 1.02e-32

dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate (EC:3.6.1.23). Members of this family have a novel all-alpha fold and are unrelated to the all-beta fold found in dUTPases of the majority of organizms. This family contains both dUTPase homologs of dUTPase including dCTPase of phage T4.


Pssm-ID: 430199  Cd Length: 162  Bit Score: 115.52  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149    8 IRIMLELQDGMNTRVNADWHQQGYE-WY----RAIWVECAELMDHY-GWKWWKKQSP-DTDQVALELIDIWHFGLSILLQ 80
Cdd:pfam08761   2 LKKLFELQKELDERIHKKHNLSGDDlWLfkklLALLVELAELANETrSFKYWKNKKPpDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149   81 SGasLDEIIARIERELVIRTDEQDFRLdLEQFAA----ATLADKQFHIGLFARLMAGVSLSFDQLYRGYVGKNVLNFFRQ 156
Cdd:pfam08761  82 LN--YNYEEFNIAKLISKDISEQFLEI-FASINDfienPNKQRYEKLFSSFLGLGEMLGFSEEDIEKAYVAKNELNHQRQ 158


                  ....
gi 501464149  157 DHGY 160
Cdd:pfam08761 159 DNGY 162
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 11-80 3.98e-18

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric 2-Deoxyuridine 5'-triphosphate nucleotidohydrolase and similar proteins; dUTPase (dUTP pyrophosphatase; EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. It acts to ensure chromosomal integrity by reducing the effective ratio of dUTP/dTTP. Members in this family are dimeric dUTPases, such as those from Leishmania major, Trypanosoma cruzi, and Campylobacter jejuni, which differ from the monomeric and trimeric forms and adopt an all-alpha topology. A central four-helix bundle, consisting of two alpha-helices from the rigid domain and two helices from the mobile domain and connecting loops, form the active site in dimeric dUTPase-like proteins, requiring the presence of metal ion cofactors to hydrolyze both dUTP and dUDP.


Pssm-ID: 212134 [Multi-domain]  Cd Length: 94  Bit Score: 75.72  E-value: 3.98e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501464149  11 MLELQDGMNTRVNADWHQQGYE-----WYRAIWVECAELMDHYG-WKWWKKQSPDTDQVAL-ELIDIWHFGLSILLQ 80
Cdd:cd11527    1 LFELQKELDDKINKKWNLNNKKkllknKALALIVELAELANETEsFKYWKKNKPNDKEKILeELVDILHFLLSIALE 77
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 6-160 1.37e-49

Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 443588  Cd Length: 163  Bit Score: 158.53  E-value: 1.37e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149   6 QQIRIMLELQDGMNTRVNAD----WHQQGYEWYRAIWVECAELMDHYG-WKWWKKQSPD-TDQVALELIDIWHFGLSILL 79
Cdd:COG4508    1 MNLKKLFEMQKELDDRIEEEhgleGEDLFDKKYLALLVELGELANETRcFKFWSKKPPSpKEVILEEYVDGLHFILSLGL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149  80 QSGASLDEIIARIERELVIRTD-EQDFRLDLEQFAAaTLADKQFH--IGLFARLMAGVSLSFDQLYRGYVGKNVLNFFRQ 156
Cdd:COG4508   81 ELGYDLLELAAPMEAELKSLTEqFLDVYEAITAFAK-NLTKKNYQelFALFLQLGYALGFTEEDIEKAYLGKNELNHFRQ 159


                 ....
gi 501464149 157 DHGY 160
Cdd:COG4508  160 DNGY 163
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 8-160 1.02e-32

dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate (EC:3.6.1.23). Members of this family have a novel all-alpha fold and are unrelated to the all-beta fold found in dUTPases of the majority of organizms. This family contains both dUTPase homologs of dUTPase including dCTPase of phage T4.


Pssm-ID: 430199  Cd Length: 162  Bit Score: 115.52  E-value: 1.02e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149    8 IRIMLELQDGMNTRVNADWHQQGYE-WY----RAIWVECAELMDHY-GWKWWKKQSP-DTDQVALELIDIWHFGLSILLQ 80
Cdd:pfam08761   2 LKKLFELQKELDERIHKKHNLSGDDlWLfkklLALLVELAELANETrSFKYWKNKKPpDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501464149   81 SGasLDEIIARIERELVIRTDEQDFRLdLEQFAA----ATLADKQFHIGLFARLMAGVSLSFDQLYRGYVGKNVLNFFRQ 156
Cdd:pfam08761  82 LN--YNYEEFNIAKLISKDISEQFLEI-FASINDfienPNKQRYEKLFSSFLGLGEMLGFSEEDIEKAYVAKNELNHQRQ 158


                  ....
gi 501464149  157 DHGY 160
Cdd:pfam08761 159 DNGY 162
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 11-80 3.98e-18

Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric 2-Deoxyuridine 5'-triphosphate nucleotidohydrolase and similar proteins; dUTPase (dUTP pyrophosphatase; EC 3.6.1.23) catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate. It acts to ensure chromosomal integrity by reducing the effective ratio of dUTP/dTTP. Members in this family are dimeric dUTPases, such as those from Leishmania major, Trypanosoma cruzi, and Campylobacter jejuni, which differ from the monomeric and trimeric forms and adopt an all-alpha topology. A central four-helix bundle, consisting of two alpha-helices from the rigid domain and two helices from the mobile domain and connecting loops, form the active site in dimeric dUTPase-like proteins, requiring the presence of metal ion cofactors to hydrolyze both dUTP and dUDP.


Pssm-ID: 212134 [Multi-domain]  Cd Length: 94  Bit Score: 75.72  E-value: 3.98e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 501464149  11 MLELQDGMNTRVNADWHQQGYE-----WYRAIWVECAELMDHYG-WKWWKKQSPDTDQVAL-ELIDIWHFGLSILLQ 80
Cdd:cd11527    1 LFELQKELDDKINKKWNLNNKKkllknKALALIVELAELANETEsFKYWKKNKPNDKEKILeELVDILHFLLSIALE 77
 
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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