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Conserved domains on  [gi|259162010|gb|EEW46590|]
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hypothetical protein SAD30_0317 [Staphylococcus aureus D30]

Protein Classification

dUTPase( domain architecture ID 10183895)

dUTPase catalyzes the hydrolysis of dUTP to dUMP and pyrophosphate, ensuring chromosomal integrity by reducing the effective ratio of dUTP/dTTP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Dut2 super family cl44079
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 9-168 8.05e-36

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


The actual alignment was detected with superfamily member COG4508:

Pssm-ID: 443588  Cd Length: 163  Bit Score: 122.32  E-value: 8.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   9 QLQELLQIQKEFDDRIPTRN-------LNDTVASMIIEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLT 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEEHglegedlFDKKYLALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010  82 IVDEEDLeettevMVDLIENEVTlpKLHSVyFVHVMHTLTEqFVKGIDNSIVQVLIMPFLY--ANTYYSIDQLIDAYKKK 159
Cdd:COG4508   82 LGYDLLE------LAAPMEAELK--SLTEQ-FLDVYEAITA-FAKNLTKKNYQELFALFLQlgYALGFTEEDIEKAYLGK 151


                 ....*....
gi 259162010 160 MKRNHERQD 168
Cdd:COG4508  152 NELNHFRQD 160
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 9-168 8.05e-36

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: 122.32  E-value: 8.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   9 QLQELLQIQKEFDDRIPTRN-------LNDTVASMIIEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLT 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEEHglegedlFDKKYLALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010  82 IVDEEDLeettevMVDLIENEVTlpKLHSVyFVHVMHTLTEqFVKGIDNSIVQVLIMPFLY--ANTYYSIDQLIDAYKKK 159
Cdd:COG4508   82 LGYDLLE------LAAPMEAELK--SLTEQ-FLDVYEAITA-FAKNLTKKNYQELFALFLQlgYALGFTEEDIEKAYLGK 151


                 ....*....
gi 259162010 160 MKRNHERQD 168
Cdd:COG4508  152 NELNHFRQD 160
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 13-82 3.25e-14

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: 64.54  E-value: 3.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259162010  13 LLQIQKEFDDRI--------PTRNLNDTVASMIIEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLTI 82
Cdd:cd11527    1 LFELQKELDDKInkkwnlnnKKKLLKNKALALIVELAELANETESFKYWKKNKPNDKEKILEELVDILHFLLSIALEL 78
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 10-168 1.24e-08

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: 51.58  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   10 LQELLQIQKEFDDRI-------PTRNLNDTVASMI-IEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLT 81
Cdd:pfam08761   2 LKKLFELQKELDERIhkkhnlsGDDLWLFKKLLALlVELAELANETRSFKYWKNKKPPDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   82 IvdeeDLEETTEVMVDLIENEVtlpklhSVYFVHVMHTlTEQFVKGIDNSIVQVLIMPFLY-ANTY-YSIDQLIDAYKKK 159
Cdd:pfam08761  82 L----NYNYEEFNIAKLISKDI------SEQFLEIFAS-INDFIENPNKQRYEKLFSSFLGlGEMLgFSEEDIEKAYVAK 150


                  ....*....
gi 259162010  160 MKRNHERQD 168
Cdd:pfam08761 151 NELNHQRQD 159
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 9-168 8.05e-36

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: 122.32  E-value: 8.05e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   9 QLQELLQIQKEFDDRIPTRN-------LNDTVASMIIEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLT 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEEHglegedlFDKKYLALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010  82 IVDEEDLeettevMVDLIENEVTlpKLHSVyFVHVMHTLTEqFVKGIDNSIVQVLIMPFLY--ANTYYSIDQLIDAYKKK 159
Cdd:COG4508   82 LGYDLLE------LAAPMEAELK--SLTEQ-FLDVYEAITA-FAKNLTKKNYQELFALFLQlgYALGFTEEDIEKAYLGK 151


                 ....*....
gi 259162010 160 MKRNHERQD 168
Cdd:COG4508  152 NELNHFRQD 160
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 13-82 3.25e-14

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: 64.54  E-value: 3.25e-14
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 259162010  13 LLQIQKEFDDRI--------PTRNLNDTVASMIIEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLTI 82
Cdd:cd11527    1 LFELQKELDDKInkkwnlnnKKKLLKNKALALIVELAELANETESFKYWKKNKPNDKEKILEELVDILHFLLSIALEL 78
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 10-168 1.24e-08

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: 51.58  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   10 LQELLQIQKEFDDRI-------PTRNLNDTVASMI-IEFVEWINTLEFFKNWKKQPGKPLDTQLDEIADYLAFSLQLTLT 81
Cdd:pfam08761   2 LKKLFELQKELDERIhkkhnlsGDDLWLFKKLLALlVELAELANETRSFKYWKNKKPPDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 259162010   82 IvdeeDLEETTEVMVDLIENEVtlpklhSVYFVHVMHTlTEQFVKGIDNSIVQVLIMPFLY-ANTY-YSIDQLIDAYKKK 159
Cdd:pfam08761  82 L----NYNYEEFNIAKLISKDI------SEQFLEIFAS-INDFIENPNKQRYEKLFSSFLGlGEMLgFSEEDIEKAYVAK 150


                  ....*....
gi 259162010  160 MKRNHERQD 168
Cdd:pfam08761 151 NELNHQRQD 159
 
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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