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Conserved domains on  [gi|18676710|dbj|BAB85007|]
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FLJ00254 protein, partial [Homo sapiens]

Protein Classification

trimeric_dUTPase domain-containing protein( domain architecture ID 10165877)

trimeric_dUTPase domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 92-166 3.45e-13

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


:

Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 62.90  E-value: 3.45e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18676710  92 EGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQAKKGVAVL-AGVIDLDYQDEISLLLHNRSKKEYAWNTGDPLG 166
Cdd:cd07557  12 EGIVLPPGETVlVPTGEAIELPEGYVGLVFPRSSLARKGITVHnAGVIDPGYRGEITLELYNLGPEPVVIKKGDRIA 88
 
Name Accession Description Interval E-value
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 92-166 3.45e-13

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 62.90  E-value: 3.45e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18676710  92 EGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQAKKGVAVL-AGVIDLDYQDEISLLLHNRSKKEYAWNTGDPLG 166
Cdd:cd07557  12 EGIVLPPGETVlVPTGEAIELPEGYVGLVFPRSSLARKGITVHnAGVIDPGYRGEITLELYNLGPEPVVIKKGDRIA 88
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 71-195 4.02e-13

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 63.85  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710    71 AKFLLPLPATLRSAGLEVLVPEGGMLPPGDTTI-SLNWKLRLPTGHFGLLLPLSQQAKKGVAVLAGVIDLDYQDEISLLL 149
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLvPTDISIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18676710   150 HNRSKKEYAWNTGDPLGRPLVLPCSVIkvnrklqQPNPGRTTNGSD 195
Cdd:pfam00692  81 FNLGKSDFTIKKGDRIAQLIFEPILHP-------ELEPVETLDNTD 119
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 72-163 2.33e-12

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 62.25  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710    72 KFLLPLPATLRSAGLEVLVPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQAKK-GVAVL--AGVIDLDYQDEISL 147
Cdd:TIGR00576  10 NAPLPTYATEGAAGYDLRAAEDVTIPPGERAlVPTGIAIELPDGYYGRVAPRSGLALKhGVTIDnsPGVIDADYRGEIKV 89

                          90
                  ....*....|....*.
gi 18676710   148 LLHNRSKKEYAWNTGD 163
Cdd:TIGR00576  90 ILINLGKEDFTVKKGD 105
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 75-163 1.02e-09

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 55.02  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710  75 LPLP--ATLRSAGLEV--LVPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLP---LSqqAKKGVAVL--AGVIDLDYQDE 144
Cdd:COG0756  11 APLPayATPGSAGLDLraALDEPVTLKPGERAlVPTGLAIALPPGYEAQVRPrsgLA--LKHGITLLnsPGTIDSDYRGE 88

                        90
                ....*....|....*....
gi 18676710 145 ISLLLHNRSKKEYAWNTGD 163
Cdd:COG0756  89 IKVILINLGDEPFTIERGD 107
dut PRK00601
dUTP diphosphatase;
75-163 4.21e-07

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 47.85  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710   75 LPLP--ATLRSAGLEVL--VPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQA-KKGVAVL--AGVIDLDYQDEIS 146
Cdd:PRK00601  17 FPLPayATEGSAGLDLRacLDEPVTLAPGERAlVPTGLAIHIPDGYEAQILPRSGLAhKHGIVLGnlPGTIDSDYRGELK 96

                         90
                 ....*....|....*..
gi 18676710  147 LLLHNRSKKEYAWNTGD 163
Cdd:PRK00601  97 VSLWNRGQEPFTIEPGE 113
 
Name Accession Description Interval E-value
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 92-166 3.45e-13

Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common family of dUTPase, found in bacteria, eukaryotes, and archaea. They catalyze the hydrolysis of the dUTP-Mg complex (dUTP-Mg) into dUMP and pyrophosphate. This reaction is crucial for the preservation of chromosomal integrity as it removes dUTP and therefore reduces the cellular dUTP/dTTP ratio, and prevents dUTP from being incorporated into DNA. It also provides dUMP as the precursor for dTTP synthesis via the thymidylate synthase pathway. dUTPases are homotrimeric, except some monomeric viral dUTPases, which have been shown to mimic a trimer. Active sites are located at the subunit interface.


Pssm-ID: 143638 [Multi-domain]  Cd Length: 92  Bit Score: 62.90  E-value: 3.45e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18676710  92 EGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQAKKGVAVL-AGVIDLDYQDEISLLLHNRSKKEYAWNTGDPLG 166
Cdd:cd07557  12 EGIVLPPGETVlVPTGEAIELPEGYVGLVFPRSSLARKGITVHnAGVIDPGYRGEITLELYNLGPEPVVIKKGDRIA 88
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 71-195 4.02e-13

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 63.85  E-value: 4.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710    71 AKFLLPLPATLRSAGLEVLVPEGGMLPPGDTTI-SLNWKLRLPTGHFGLLLPLSQQAKKGVAVLAGVIDLDYQDEISLLL 149
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLvPTDISIPLPDGTYGRIFPRSGLAAKGLIVVPGVIDSDYRGEVKVVL 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 18676710   150 HNRSKKEYAWNTGDPLGRPLVLPCSVIkvnrklqQPNPGRTTNGSD 195
Cdd:pfam00692  81 FNLGKSDFTIKKGDRIAQLIFEPILHP-------ELEPVETLDNTD 119
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 72-163 2.33e-12

deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is in maintaining the levels of dUTP in the cell to prevent dUTP incorporation into DNA during DNA replication. Pol proteins in viruses are very similar to this protein family. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). Changed role from 132 to 123. RTD [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 273149 [Multi-domain]  Cd Length: 142  Bit Score: 62.25  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710    72 KFLLPLPATLRSAGLEVLVPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQAKK-GVAVL--AGVIDLDYQDEISL 147
Cdd:TIGR00576  10 NAPLPTYATEGAAGYDLRAAEDVTIPPGERAlVPTGIAIELPDGYYGRVAPRSGLALKhGVTIDnsPGVIDADYRGEIKV 89

                          90
                  ....*....|....*.
gi 18676710   148 LLHNRSKKEYAWNTGD 163
Cdd:TIGR00576  90 ILINLGKEDFTVKKGD 105
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 75-163 1.02e-09

dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP pyrophosphatase (dUTPase) is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440519 [Multi-domain]  Cd Length: 143  Bit Score: 55.02  E-value: 1.02e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710  75 LPLP--ATLRSAGLEV--LVPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLP---LSqqAKKGVAVL--AGVIDLDYQDE 144
Cdd:COG0756  11 APLPayATPGSAGLDLraALDEPVTLKPGERAlVPTGLAIALPPGYEAQVRPrsgLA--LKHGITLLnsPGTIDSDYRGE 88

                        90
                ....*....|....*....
gi 18676710 145 ISLLLHNRSKKEYAWNTGD 163
Cdd:COG0756  89 IKVILINLGDEPFTIERGD 107
dut PRK00601
dUTP diphosphatase;
75-163 4.21e-07

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 47.85  E-value: 4.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710   75 LPLP--ATLRSAGLEVL--VPEGGMLPPGDTT-ISLNWKLRLPTGHFGLLLPLSQQA-KKGVAVL--AGVIDLDYQDEIS 146
Cdd:PRK00601  17 FPLPayATEGSAGLDLRacLDEPVTLAPGERAlVPTGLAIHIPDGYEAQILPRSGLAhKHGIVLGnlPGTIDSDYRGELK 96

                         90
                 ....*....|....*..
gi 18676710  147 LLLHNRSKKEYAWNTGD 163
Cdd:PRK00601  97 VSLWNRGQEPFTIEPGE 113
PLN02547 PLN02547
dUTP pyrophosphatase
 83-163 1.03e-05

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 44.01  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710   83 SAGLEVLVPEGG-MLPPGDTTIslnwklRLPTGHFGLLLPLSQQA-KKGVAVLAGVIDLDYQDEISLLLHNRSKKEYAWN 160
Cdd:PLN02547  42 SSAYDTVVPARGkALVPTDLSI------AIPEGTYARIAPRSGLAwKHSIDVGAGVIDADYRGPVGVILFNHSDVDFEVK 115


                 ...
gi 18676710  161 TGD 163
Cdd:PLN02547 116 VGD 118
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 75-202 2.02e-05

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 43.43  E-value: 2.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710   75 LPLPATLRSAGLEVLVPEGGMLPPGDTTISL-NWKLRLPTGHFGLLLPLSQQA-KKGVAVLAGVIDLDYQDEISLLLHNR 152
Cdd:PHA02703  25 IPTRGSPGAAGLDLCSACDCIVPAGCRCVVFtDLLIKLPDGCYGRIAPRSGLAvKHFIDVGAGVIDADYRGNVGVVLFNF 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18676710  153 SKKEYAWNTGDPLGRplvLPC------SVIKVNRkLQQPNPGRTTNGS------DPSGMTVW 202
Cdd:PHA02703 105 GHNDFEVKKGDRIAQ---LICeraafpAVEEVAC-LDDTDRGAGGFGStgsgacEGCGDTVW 162
PHA03094 PHA03094
dUTPase; Provisional
 75-163 1.62e-03

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 37.44  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18676710   75 LPLPATLRSAGLEVLVPEGGMLPPGD-----TTISLNwklrLPTGHFGLLLPLSQQA-KKGVAVLAGVIDLDYQDEISLL 148
Cdd:PHA03094  17 IPTRSSPKSAGYDLYSAYDYTVPPKErilvkTDISLS----IPKFCYGRIAPRSGLSlNYGIDIGGGVIDEDYRGNIGVI 92

                         90
                 ....*....|....*
gi 18676710  149 LHNRSKKEYAWNTGD 163
Cdd:PHA03094  93 FINNGKCTFNIKTGD 107
 
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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