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Conserved domains on  [gi|600880732|gb|EYQ71872|]
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phage dUTPase [Staphylococcus aureus DAR2075]

Protein Classification

dUTPase( domain architecture ID 18109064)

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]; ...
 9-166 3.49e-29

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: 105.37  E-value: 3.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   9 QLQELLQIQKEFDDRIPT------LNLRDSKI-AYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEehglegEDLFDKKYlALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732  82 QADNMEEILgYLDDGDFNDYIErVEIDFNDsdVVDEFMSTIDEmyeSPYSSNLFLPFALANNY-YTIDQLIDAYKKKMKR 160
Cdd:COG4508   82 LGYDLLELA-APMEAELKSLTE-QFLDVYE--AITAFAKNLTK---KNYQELFALFLQLGYALgFTEEDIEKAYLGKNEL 154


                 ....*.
gi 600880732 161 NHERQD 166
Cdd:COG4508  155 NHFRQD 160
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 9-166 3.49e-29

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: 105.37  E-value: 3.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   9 QLQELLQIQKEFDDRIPT------LNLRDSKI-AYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEehglegEDLFDKKYlALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732  82 QADNMEEILgYLDDGDFNDYIErVEIDFNDsdVVDEFMSTIDEmyeSPYSSNLFLPFALANNY-YTIDQLIDAYKKKMKR 160
Cdd:COG4508   82 LGYDLLELA-APMEAELKSLTE-QFLDVYE--AITAFAKNLTK---KNYQELFALFLQLGYALgFTEEDIEKAYLGKNEL 154


                 ....*.
gi 600880732 161 NHERQD 166
Cdd:COG4508  155 NHFRQD 160
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 13-81 5.39e-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: 74.56  E-value: 5.39e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600880732  13 LLQIQKEFDDRIPTL--------NLRDSKIAYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:cd11527    1 LFELQKELDDKINKKwnlnnkkkLLKNKALALIVELAELANETESFKYWKKNKPNDKEKILEELVDILHFLLSIALE 77
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 10-166 2.44e-16

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: 71.99  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   10 LQELLQIQKEFDDRI--------PTLNLRDSKIAYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:pfam08761   2 LKKLFELQKELDERIhkkhnlsgDDLWLFKKLLALLVELAELANETRSFKYWKNKKPPDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   82 QADNMEEilgylddGDFNDYIERvEIDFNDSDVVDEFMSTIDEMYESPYSSNLFLPFALANNY-YTIDQLIDAYKKKMKR 160
Cdd:pfam08761  82 LNYNYEE-------FNIAKLISK-DISEQFLEIFASINDFIENPNKQRYEKLFSSFLGLGEMLgFSEEDIEKAYVAKNEL 153


                  ....*.
gi 600880732  161 NHERQD 166
Cdd:pfam08761 154 NHQRQD 159
 
Name Accession Description Interval E-value
Dut2 COG4508
Dimeric dUTPase, all-alpha-NTP-PPase (MazG) superfamily [Nucleotide transport and metabolism]; ...
 9-166 3.49e-29

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: 105.37  E-value: 3.49e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   9 QLQELLQIQKEFDDRIPT------LNLRDSKI-AYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:COG4508    2 NLKKLFEMQKELDDRIEEehglegEDLFDKKYlALLVELGELANETRCFKFWSKKPPSPKEVILEEYVDGLHFILSLGLE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732  82 QADNMEEILgYLDDGDFNDYIErVEIDFNDsdVVDEFMSTIDEmyeSPYSSNLFLPFALANNY-YTIDQLIDAYKKKMKR 160
Cdd:COG4508   82 LGYDLLELA-APMEAELKSLTE-QFLDVYE--AITAFAKNLTK---KNYQELFALFLQLGYALgFTEEDIEKAYLGKNEL 154


                 ....*.
gi 600880732 161 NHERQD 166
Cdd:COG4508  155 NHFRQD 160
NTP-PPase_dUTPase cd11527
Nucleoside Triphosphate Pyrophosphohydrolase (EC 3.6.1.8) MazG-like domain found in dimeric ...
 13-81 5.39e-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: 74.56  E-value: 5.39e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 600880732  13 LLQIQKEFDDRIPTL--------NLRDSKIAYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:cd11527    1 LFELQKELDDKINKKwnlnnkkkLLKNKALALIVELAELANETESFKYWKKNKPNDKEKILEELVDILHFLLSIALE 77
dUTPase_2 pfam08761
dUTPase; 2-Deoxyuridine 5-triphosphate nucleotidohydrolase (dUTPase) catalyzes the hydrolysis ...
 10-166 2.44e-16

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: 71.99  E-value: 2.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   10 LQELLQIQKEFDDRI--------PTLNLRDSKIAYVVEFFEWFNTLETFKNWKKKPGKPLDVQLDELADMLAFGLSIANQ 81
Cdd:pfam08761   2 LKKLFELQKELDERIhkkhnlsgDDLWLFKKLLALLVELAELANETRSFKYWKNKKPPDLEKVLEEYVDGLHFLLSLGIE 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 600880732   82 QADNMEEilgylddGDFNDYIERvEIDFNDSDVVDEFMSTIDEMYESPYSSNLFLPFALANNY-YTIDQLIDAYKKKMKR 160
Cdd:pfam08761  82 LNYNYEE-------FNIAKLISK-DISEQFLEIFASINDFIENPNKQRYEKLFSSFLGLGEMLgFSEEDIEKAYVAKNEL 153


                  ....*.
gi 600880732  161 NHERQD 166
Cdd:pfam08761 154 NHQRQD 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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