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Conserved domains on  [gi|71988561|ref|NP_001021553|]
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dUTP diphosphatase [Caenorhabditis elegans]

Protein Classification

dUTP diphosphatase( domain architecture ID 10794620)

dUTP diphosphatase is involved in nucleotide metabolism: it produces dUMP, the immediate precursor of thymidine nucleotides and it decreases the intracellular concentration of dUTP so that uracil cannot be incorporated into DNA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 186-324 8.01e-73

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: 226.73  E-value: 8.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHF--IDVGAGVID 263
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   264 SDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGH-CVYEAASELENTDRGAGGFGSTGQ 324
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 349-487 8.63e-70

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: 219.03  E-value: 8.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   349 TIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHF--IDVGAGVID 426
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   427 SDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIAL-CTYSKVESLEVTERGAGGFGSTGQ 487
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 30-168 1.63e-60

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: 194.76  E-value: 1.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    30 TIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHF--IDVGAGVID 107
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   108 SDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGT-YEEVKSLPSTNRGAGGFGSTGE 168
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
 
Name Accession Description Interval E-value
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 186-324 8.01e-73

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: 226.73  E-value: 8.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHF--IDVGAGVID 263
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   264 SDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGH-CVYEAASELENTDRGAGGFGSTGQ 324
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 349-487 8.63e-70

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: 219.03  E-value: 8.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   349 TIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHF--IDVGAGVID 426
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   427 SDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIAL-CTYSKVESLEVTERGAGGFGSTGQ 487
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
PLN02547 PLN02547
dUTP pyrophosphatase
 342-486 1.19e-63

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 203.87  E-value: 1.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  342 KTSATSVTIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVG 421
Cdd:PLN02547   9 KIQKPSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVG 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988561  422 AGVIDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:PLN02547  89 AGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 186-328 1.47e-61

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 198.67  E-value: 1.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGAGVIDSD 265
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDAD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71988561  266 YRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTGQNTME 328
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSGACE 155
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 30-168 1.63e-60

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: 194.76  E-value: 1.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    30 TIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHF--IDVGAGVID 107
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   108 SDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGT-YEEVKSLPSTNRGAGGFGSTGE 168
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 349-486 2.59e-56

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: 184.06  E-value: 2.59e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 349 TIQITKSNDNAQMPTYGSAEAAGADLYSA--EDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVG--AGV 424
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 425 IDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 186-323 2.08e-55

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: 181.75  E-value: 2.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 186 TVRFTQLNENAQTPTYGSEEAAGADLYSA--EDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVG--AGV 261
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 262 IDSDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 30-170 2.24e-55

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 182.49  E-value: 2.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   30 TIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGAGVIDSD 109
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDAD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988561  110 YRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTGEST 170
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSGA 153
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 357-486 3.89e-52

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.47  E-value: 3.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   357 DNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVL 436
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 71988561   437 LFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 194-323 7.19e-52

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.09  E-value: 7.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   194 ENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVL 273
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 71988561   274 LFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 30-167 4.24e-49

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: 165.19  E-value: 4.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  30 TIRFTEMVGDAQKPTYGSISSAGADLYSA--EDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVG--AGV 105
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 106 IDSDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 43-167 3.93e-47

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 159.38  E-value: 3.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    43 PTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVLLFNFN 122
Cdd:pfam00692   6 PTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVVLFNLG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 71988561   123 TTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:pfam00692  85 KSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 207-294 1.51e-30

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: 113.74  E-value: 1.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 207 AGADLYSAED---ITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFTDNAF 282
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 283 EVKKGDRIAQLI 294
Cdd:cd07557  80 VIKKGDRIAQLV 91
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 370-457 6.07e-30

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: 112.20  E-value: 6.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 370 AGADLYSAED---VTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFGENDF 445
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 446 EVKKGDRIAQLV 457
Cdd:cd07557  80 VIKKGDRIAQLV 91
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 51-138 1.73e-27

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: 105.27  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  51 AGADLYSAED---VVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFNTTAF 126
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 127 EVKTGDRIAKLI 138
Cdd:cd07557  80 VIKKGDRIAQLV 91
 
Name Accession Description Interval E-value
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 186-324 8.01e-73

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: 226.73  E-value: 8.01e-73
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHF--IDVGAGVID 263
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   264 SDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGH-CVYEAASELENTDRGAGGFGSTGQ 324
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 349-487 8.63e-70

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: 219.03  E-value: 8.63e-70
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   349 TIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHF--IDVGAGVID 426
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   427 SDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIAL-CTYSKVESLEVTERGAGGFGSTGQ 487
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTeVEFEEVEELDETERGEGGFGSTGV 142
PLN02547 PLN02547
dUTP pyrophosphatase
 342-486 1.19e-63

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 203.87  E-value: 1.19e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  342 KTSATSVTIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVG 421
Cdd:PLN02547   9 KIQKPSPLLRVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVG 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988561  422 AGVIDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:PLN02547  89 AGVIDADYRGPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 186-328 1.47e-61

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 198.67  E-value: 1.47e-61
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGAGVIDSD 265
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDAD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71988561  266 YRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTGQNTME 328
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSGACE 155
dut TIGR00576
deoxyuridine 5'-triphosphate nucleotidohydrolase (dut); The main function of these proteins is ...
 30-168 1.63e-60

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: 194.76  E-value: 1.63e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    30 TIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHF--IDVGAGVID 107
Cdd:TIGR00576   1 KLKFVKLSPNAPLPTYATEGAAGYDLRAAEDVTIPPGERALVPTGIAIELPDGYYGRVAPRSGLALKHGvtIDNSPGVID 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561   108 SDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGT-YEEVKSLPSTNRGAGGFGSTGE 168
Cdd:TIGR00576  81 ADYRGEIKVILINLGKEDFTVKKGDRIAQLVVEKIVTEVeFEEVEELDETERGEGGFGSTGV 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 349-486 5.09e-58

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 189.42  E-value: 5.09e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  349 TIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVGAGVIDSD 428
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDAD 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 71988561  429 YRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTG 150
PLN02547 PLN02547
dUTP pyrophosphatase
 188-323 1.00e-56

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 185.77  E-value: 1.00e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  188 RFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGAGVIDSDYR 267
Cdd:PLN02547  18 RVKKLSEKATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDADYR 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71988561  268 GEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:PLN02547  98 GPVGVILFNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 349-486 2.59e-56

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: 184.06  E-value: 2.59e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 349 TIQITKSNDNAQMPTYGSAEAAGADLYSA--EDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVG--AGV 424
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 425 IDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 186-323 2.08e-55

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: 181.75  E-value: 2.08e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 186 TVRFTQLNENAQTPTYGSEEAAGADLYSA--EDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVG--AGV 261
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 262 IDSDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
PHA02703 PHA02703
ORF007 dUTPase; Provisional
 30-170 2.24e-55

ORF007 dUTPase; Provisional


Pssm-ID: 165079  Cd Length: 165  Bit Score: 182.49  E-value: 2.24e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   30 TIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGAGVIDSD 109
Cdd:PHA02703  13 ALRVVRLSPNATIPTRGSPGAAGLDLCSACDCIVPAGCRCVVFTDLLIKLPDGCYGRIAPRSGLAVKHFIDVGAGVIDAD 92

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988561  110 YRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTGEST 170
Cdd:PHA02703  93 YRGNVGVVLFNFGHNDFEVKKGDRIAQLICERAAFPAVEEVACLDDTDRGAGGFGSTGSGA 153
PLN02547 PLN02547
dUTP pyrophosphatase
 39-167 1.39e-54

dUTP pyrophosphatase


Pssm-ID: 215302  Cd Length: 157  Bit Score: 179.99  E-value: 1.39e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   39 DAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGAGVIDSDYRGEVKVLL 118
Cdd:PLN02547  25 KATLPSRGSALAAGYDLSSAYDTVVPARGKALVPTDLSIAIPEGTYARIAPRSGLAWKHSIDVGAGVIDADYRGPVGVIL 104

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 71988561  119 FNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:PLN02547 105 FNHSDVDFEVKVGDRIAQLILEKIVTPEVVEVEDLDATVRGAGGFGSTG 153
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 357-486 3.89e-52

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.47  E-value: 3.89e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   357 DNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVL 436
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 71988561   437 LFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 194-323 7.19e-52

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 172.09  E-value: 7.19e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   194 ENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVL 273
Cdd:pfam00692   1 DEAEIPTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVV 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 71988561   274 LFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:pfam00692  80 LFNLGKSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
Dut COG0756
dUTP pyrophosphatase (dUTPase) [Nucleotide transport and metabolism, Defense mechanisms]; dUTP ...
 30-167 4.24e-49

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: 165.19  E-value: 4.24e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  30 TIRFTEMVGDAQKPTYGSISSAGADLYSA--EDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVG--AGV 105
Cdd:COG0756   1 KVKIKRLDEDAPLPAYATPGSAGLDLRAAldEPVTLKPGERALVPTGLAIALPPGYEAQVRPRSGLALKHGITLLnsPGT 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 71988561 106 IDSDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:COG0756  81 IDSDYRGEIKVILINLGDEPFTIERGDRIAQLVIAPVVQAEFEEVEELDETERGAGGFGSTG 142
dut PRK00601
dUTP diphosphatase;
347-486 3.68e-48

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 163.03  E-value: 3.68e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  347 SVTIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTV---PARGKLcVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVG-- 421
Cdd:PRK00601   5 DVKILDPRLGKEFPLPAYATEGSAGLDLRACLDEPVtlaPGERAL-VPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGnl 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988561  422 AGVIDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:PRK00601  84 PGTIDSDYRGELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTG 148
dUTPase pfam00692
dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.
 43-167 3.93e-47

dUTPase; dUTPase hydrolyses dUTP to dUMP and pyrophosphate.


Pssm-ID: 395562 [Multi-domain]  Cd Length: 129  Bit Score: 159.38  E-value: 3.93e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    43 PTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGaGVIDSDYRGEVKVLLFNFN 122
Cdd:pfam00692   6 PTPGSPGDAGYDLYAPYDLTVKPGGTVLVPTDISIPLPDGTYGRIFPRSGLAAKGLIVVP-GVIDSDYRGEVKVVLFNLG 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 71988561   123 TTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:pfam00692  85 KSDFTIKKGDRIAQLIFEPILHPELEPVETLDNTDRGDGGFGSSG 129
dut PRK00601
dUTP diphosphatase;
192-323 3.85e-45

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 154.94  E-value: 3.85e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  192 LNENAQTPTYGSEEAAGADLYSAED--ITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVG--AGVIDSDYR 267
Cdd:PRK00601  13 LGKEFPLPAYATEGSAGLDLRACLDepVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGnlPGTIDSDYR 92

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 71988561  268 GEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTG 323
Cdd:PRK00601  93 GELKVSLWNRGQEPFTIEPGERIAQLVIVPVVQAEFEEVEEFDETERGAGGFGSTG 148
PHA03094 PHA03094
dUTPase; Provisional
 186-325 6.09e-44

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 151.46  E-value: 6.09e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  186 TVRFTQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGAGVIDSD 265
Cdd:PHA03094   5 PVRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVIDED 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  266 YRGEVKVLLFNFTDNAFEVKKGDRIAQLICEKIGHCVYEAASELENTDRGAGGFGSTGQN 325
Cdd:PHA03094  85 YRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSGLR 144
PHA03094 PHA03094
dUTPase; Provisional
 346-486 2.14e-43

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 150.30  E-value: 2.14e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  346 TSVTIQITKSNDNAQMPTYGSAEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVGAGVI 425
Cdd:PHA03094   2 SNSPVRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988561  426 DSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQIALCTYSKVESLEVTERGAGGFGSTG 486
Cdd:PHA03094  82 DEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
dut PRK00601
dUTP diphosphatase;
43-167 4.76e-42

dUTP diphosphatase;


Pssm-ID: 234802 [Multi-domain]  Cd Length: 150  Bit Score: 146.85  E-value: 4.76e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   43 PTYGSISSAGADLYSAED--VVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVG--AGVIDSDYRGEVKVLL 118
Cdd:PRK00601  20 PAYATEGSAGLDLRACLDepVTLAPGERALVPTGLAIHIPDGYEAQILPRSGLAHKHGIVLGnlPGTIDSDYRGELKVSL 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71988561  119 FNFNTTAFEVKTGDRIAKLI---CEQIgngTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:PRK00601 100 WNRGQEPFTIEPGERIAQLVivpVVQA---EFEEVEEFDETERGAGGFGSTG 148
PHA03094 PHA03094
dUTPase; Provisional
 27-167 1.18e-40

dUTPase; Provisional


Pssm-ID: 165376 [Multi-domain]  Cd Length: 144  Bit Score: 142.98  E-value: 1.18e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   27 SHITIRFTEMVGDAQKPTYGSISSAGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGAGVI 106
Cdd:PHA03094   2 SNSPVRCVKLSNFAKIPTRSSPKSAGYDLYSAYDYTVPPKERILVKTDISLSIPKFCYGRIAPRSGLSLNYGIDIGGGVI 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 71988561  107 DSDYRGEVKVLLFNFNTTAFEVKTGDRIAKLICEQIGNGTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:PHA03094  82 DEDYRGNIGVIFINNGKCTFNIKTGDRIAQIIFERIEYPELKEVQSLDSTDRGDQGFGSSG 142
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 207-294 1.51e-30

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: 113.74  E-value: 1.51e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 207 AGADLYSAED---ITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFTDNAF 282
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 283 EVKKGDRIAQLI 294
Cdd:cd07557  80 VIKKGDRIAQLV 91
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 370-457 6.07e-30

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: 112.20  E-value: 6.07e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561 370 AGADLYSAED---VTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFGENDF 445
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 446 EVKKGDRIAQLV 457
Cdd:cd07557  80 VIKKGDRIAQLV 91
trimeric_dUTPase cd07557
Trimeric dUTP diphosphatases; Trimeric dUTP diphosphatases, or dUTPases, are the most common ...
 51-138 1.73e-27

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: 105.27  E-value: 1.73e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  51 AGADLYSAED---VVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAaKHFIDVG-AGVIDSDYRGEVKVLLFNFNTTAF 126
Cdd:cd07557   1 AGYDLRLGEDfegIVLPPGETVLVPTGEAIELPEGYVGLVFPRSSLA-RKGITVHnAGVIDPGYRGEITLELYNLGPEPV 79

                        90
                ....*....|..
gi 71988561 127 EVKTGDRIAKLI 138
Cdd:cd07557  80 VIKKGDRIAQLV 91
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 371-486 1.69e-15

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 73.61  E-value: 1.69e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  371 GADLYSAEDVTVPARGKLCVSTGIQMA-----------LPIGYYgrVAPRSGLAAKHF-IDVGAGVIDSDYRGEVKVLLF 438
Cdd:PTZ00143  28 GLDLFIVKDQTIKPGETAFIKLGIKAAafqkdedgsdgKNVSWL--LFPRSSISKTPLrLANSIGLIDAGYRGELIAAVD 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71988561  439 NFGENDFEVKKGDRIAQLVC---EQIalcTYSKVESLEVTERGAGGFGSTG 486
Cdd:PTZ00143 106 NIKDEPYTIKKGDRLVQLVSfdgEPI---TFELVDELDETTRGEGGFGSTG 153
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 208-325 5.09e-15

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 72.46  E-value: 5.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  208 GADLYSAEDITVPAHGKCCVSTGIQM-----------ELPFGYYgrVAPRSGLAAKHF-IDVGAGVIDSDYRGEVKVLLF 275
Cdd:PTZ00143  28 GLDLFIVKDQTIKPGETAFIKLGIKAaafqkdedgsdGKNVSWL--LFPRSSISKTPLrLANSIGLIDAGYRGELIAAVD 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71988561  276 NFTDNAFEVKKGDRIAQLIC---EKIghcVYEAASELENTDRGAGGFGSTGQN 325
Cdd:PTZ00143 106 NIKDEPYTIKKGDRLVQLVSfdgEPI---TFELVDELDETTRGEGGFGSTGRL 155
PTZ00143 PTZ00143
deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional
 52-167 1.63e-12

deoxyuridine 5'-triphosphate nucleotidohydrolase; Provisional


Pssm-ID: 240288 [Multi-domain]  Cd Length: 155  Bit Score: 65.14  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   52 GADLYSAEDVVVPANGKLCVSTGLQI-----------ELPIGYYgrVAPRSGLAAKHF-IDVGAGVIDSDYRGEVKVLLF 119
Cdd:PTZ00143  28 GLDLFIVKDQTIKPGETAFIKLGIKAaafqkdedgsdGKNVSWL--LFPRSSISKTPLrLANSIGLIDAGYRGELIAAVD 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 71988561  120 NFNTTAFEVKTGDRIAKLIC---EQIgngTYEEVKSLPSTNRGAGGFGSTG 167
Cdd:PTZ00143 106 NIKDEPYTIKKGDRLVQLVSfdgEPI---TFELVDELDETTRGEGGFGSTG 153
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 398-468 2.26e-06

dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440481  Cd Length: 180  Bit Score: 47.90  E-value: 2.26e-06
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71988561 398 LPIGYYGRVAPRS-----GLaakhFIDVGAGVIDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLV---CEQIALCTYSK 468
Cdd:COG0717  88 LPDDLVAFLEGRSslarlGL----FVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLVffrLSGPAERPYGR 162
dut PRK13956
dUTP diphosphatase;
352-487 6.65e-06

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 45.94  E-value: 6.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  352 ITKSNDNAQMPTYGSAEAAGADLYSAEDVTV-PARGKLcVSTGIQMALPIG----YYGRVA-PR-SGLAakhFIDvGAGV 424
Cdd:PRK13956   9 VSSFTNENLLPKRETAHAAGYDLKVAERTVIaPGEIKL-VPTGVKAYMQPGevlyLYDRSSnPRkKGLV---LIN-SVGV 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71988561  425 IDSDY------RGEVKVLLFNFGENDFEVKKGDRIAQLVceqiaLCTYSKVESLEVTERGAGGFGSTGQ 487
Cdd:PRK13956  84 IDGDYygnpanEGHIFAQMKNITDQEVVLEVGERIVQGV-----FMPFLIADGDQADGERTGGFGSTGK 147
PHA03124 PHA03124
dUTPase; Provisional
 367-486 3.29e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 46.09  E-value: 3.29e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  367 AEAAGADLYSAEDVTVPARGKLCVSTGIQMALPIGYYGRVAPRSGLAAKHFIDVGAGVIDSDYrgeVKVLLFNFGENDFE 446
Cdd:PHA03124 288 AEDAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQDDDW---ISFNITNIRDAAAF 364

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 71988561  447 VKKGDRIAQLVCEQIALCTYSKVESL-------------EVTERGAGGFGSTG 486
Cdd:PHA03124 365 FHAGDRIAQLIALEDKLEFLGEPDALpwkivnsvqdekkNLSSRGDGGFGSSG 417
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 234-294 4.48e-05

dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440481  Cd Length: 180  Bit Score: 44.04  E-value: 4.48e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 71988561 234 ELPFGYYGRVAPRS-----GLaakhFIDVGAGVIDSDYRGEVKVLLFNFTDNAFEVKKGDRIAQLI 294
Cdd:COG0717  87 RLPDDLVAFLEGRSslarlGL----FVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLV 148
PHA03124 PHA03124
dUTPase; Provisional
 200-323 5.09e-05

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 45.70  E-value: 5.09e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  200 TYGSEEA--AGADLYSAEDITVPAHGKCCVSTGIQMELPFGYYGRVAPRSGLAAKHFIDVGAGVIDSDYrgeVKVLLFNF 277
Cdd:PHA03124 282 IFAPKEAedAGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQDDDW---ISFNITNI 358

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 71988561  278 TDNAFEVKKGDRIAQLIC-----EKIGHC------VYEAASELENTD--RGAGGFGSTG 323
Cdd:PHA03124 359 RDAAAFFHAGDRIAQLIAledklEFLGEPdalpwkIVNSVQDEKKNLssRGDGGFGSSG 417
PHA03131 PHA03131
dUTPase; Provisional
 199-324 8.48e-05

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 44.21  E-value: 8.48e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  199 PTYgsEEAAGADLYSAEDITVPAHgkccVSTGIQMELP------------FGyygrvapRSGLAAKhfidvGAGVIDSDY 266
Cdd:PHA03131 127 PQY--PDDAGFDVSLPQDLVIFPT----TTFTFTLSLCcppisphfvpviFG-------RSGLASK-----GLTVKPTKW 188

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  267 RGE-VKVLLFNFTDNAFEVKKGDRIAQLI----------------CEKIGH--------CVYEAASELE----------- 310
Cdd:PHA03131 189 RRSgLQLKLYNYTDETIFLPAGSRICQVVfmhkdhlpsffnpllsARCLGPrilfrwarVSFEDIPKDPctssktlrqse 268

                        170
                 ....*....|....*...
gi 71988561  311 ----NTDRGAGGFGSTGQ 324
Cdd:PHA03131 269 dgdsDPSRGTKGFGSSGL 286
Dcd COG0717
dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway ...
 77-138 1.59e-04

dCTP deaminase [Nucleotide transport and metabolism]; dCTP deaminase is part of the Pathway/BioSystem: Thymidylate biosynthesis


Pssm-ID: 440481  Cd Length: 180  Bit Score: 42.50  E-value: 1.59e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71988561  77 IELPIGYYGRVAPRS-----GLaakhFIDVGAGVIDSDYRGEVKVLLFNFNTTAFEVKTGDRIAKLI 138
Cdd:COG0717  86 VRLPDDLVAFLEGRSslarlGL----FVHTTAGVIDPGFEGRITLELSNTGPLPIKLYPGMRIAQLV 148
PHA03131 PHA03131
dUTPase; Provisional
 362-457 2.02e-04

dUTPase; Provisional


Pssm-ID: 222996 [Multi-domain]  Cd Length: 286  Bit Score: 43.06  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  362 PTYgsAEAAGADLYSAEDVTVPARGK------LCVSTGIQMALPIgyygrVAPRSGLAAKhfidvGAGVIDSDYRGE-VK 434
Cdd:PHA03131 127 PQY--PDDAGFDVSLPQDLVIFPTTTftftlsLCCPPISPHFVPV-----IFGRSGLASK-----GLTVKPTKWRRSgLQ 194

                         90       100
                 ....*....|....*....|...
gi 71988561  435 VLLFNFGENDFEVKKGDRIAQLV 457
Cdd:PHA03131 195 LKLYNYTDETIFLPAGSRICQVV 217
dut PRK13956
dUTP diphosphatase;
190-324 2.30e-04

dUTP diphosphatase;


Pssm-ID: 184417 [Multi-domain]  Cd Length: 147  Bit Score: 41.32  E-value: 2.30e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561  190 TQLNENAQTPTYGSEEAAGADLYSAEDITVPAHGKCCVSTGIQMELPFG----YYGRVA-PR-SGLAakhFIDvGAGVID 263
Cdd:PRK13956  10 SSFTNENLLPKRETAHAAGYDLKVAERTVIAPGEIKLVPTGVKAYMQPGevlyLYDRSSnPRkKGLV---LIN-SVGVID 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 71988561  264 SDY------RGEVKVLLFNFTDNAFEVKKGDRIAQLIcekigHCVYEAASELENTDRGAGGFGSTGQ 324
Cdd:PRK13956  86 GDYygnpanEGHIFAQMKNITDQEVVLEVGERIVQGV-----FMPFLIADGDQADGERTGGFGSTGK 147
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 58-141 6.35e-04

deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274062  Cd Length: 179  Bit Score: 40.76  E-value: 6.35e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561    58 AEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKH-FIDVGAGVIDSDYRGEVKVLLFNFNTTAFEVKTGDRIAK 136
Cdd:TIGR02274  68 GEEFVIPPGEFALATTLEYVKLPDDVVGFLEGRSSLARLGlFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQ 147


                  ....*
gi 71988561   137 LICEQ 141
Cdd:TIGR02274 148 LVFER 152
PHA03124 PHA03124
dUTPase; Provisional
 51-167 1.44e-03

dUTPase; Provisional


Pssm-ID: 165396 [Multi-domain]  Cd Length: 418  Bit Score: 41.08  E-value: 1.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71988561   51 AGADLYSAEDVVVPANGKLCVSTGLQIELPIGYYGRVAPRSGLAAKHFIDVGAGVIDSDYrgeVKVLLFNFNTTAFEVKT 130
Cdd:PHA03124 291 AGYDIRAPEDCTILPGGSTRIILPQKLACGKFRAAFILGRSSMNLKGLLVDPEHVQDDDW---ISFNITNIRDAAAFFHA 367

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 71988561  131 GDRIAKLICEQ---------------IGNGTYEEVKSLPStnRGAGGFGSTG 167
Cdd:PHA03124 368 GDRIAQLIALEdkleflgepdalpwkIVNSVQDEKKNLSS--RGDGGFGSSG 417
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 234-297 1.59e-03

deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274062  Cd Length: 179  Bit Score: 39.61  E-value: 1.59e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 71988561   234 ELPFGYYGRVAPRSGLAAKH-FIDVGAGVIDSDYRGEVKVLLFNFTDNAFEVKKGDRIAQLICEK 297
Cdd:TIGR02274  88 KLPDDVVGFLEGRSSLARLGlFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFER 152
dCTP_deam TIGR02274
deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli ...
 404-460 1.93e-03

deoxycytidine triphosphate deaminase; Members of this family include the Escherichia coli monofunctional deoxycytidine triphosphate deaminase (dCTP deaminase) and a Methanocaldococcus jannaschii bifunctional dCTP deaminase (3.5.4.13)/dUTP diphosphatase (EC 3.6.1.23), which has the EC number 3.5.4.30 for the overall operation. [Purines, pyrimidines, nucleosides, and nucleotides, 2'-Deoxyribonucleotide metabolism]


Pssm-ID: 274062  Cd Length: 179  Bit Score: 39.22  E-value: 1.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 71988561   404 GRVAPRSGLAAKH-FIDVGAGVIDSDYRGEVKVLLFNFGENDFEVKKGDRIAQLVCEQ 460
Cdd:TIGR02274  95 GFLEGRSSLARLGlFIHVTAGRIDPGFEGNITLELFNAGKLPVKLRPGMRIAQLVFER 152
 
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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